data_9KO5
# 
_entry.id   9KO5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KO5         pdb_00009ko5 10.2210/pdb9ko5/pdb 
WWPDB D_1300053958 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KO5 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yasunori@sci.kj.yamagata-u.ac.jp 
_pdbx_contact_author.name_first         Yasunori 
_pdbx_contact_author.name_last          Watanabe 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7846-680X 
# 
_audit_author.name               'Watanabe, Y.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-7846-680X 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of Agrobacterium tumefaciens PmtA' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Watanabe, Y.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-7846-680X 
# 
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 Methyltransferase                 19043.137 4   ? ? ? ? 
2 non-polymer syn "5'-DEOXY-5'-METHYLTHIOADENOSINE" 297.334   4   ? ? ? ? 
3 water       nat water                             18.015    499 ? ? ? ? 
# 
_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       
;GPQPKKVGAIVPTSSITAKKMASVINPHSGLPVLELGPGTGVITKAILARGIKPESLTAIEYSTDFYNQLLRSYPGVNFV
NGDAFDLDATLGEHKGQMFDSVISAVPMLNFPMAARIKLLDELLKRVPHGRPVVQISYGPISPIVAQPHLYHIRHFDFIV
RNIPPAQLWTYTRA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPQPKKVGAIVPTSSITAKKMASVINPHSGLPVLELGPGTGVITKAILARGIKPESLTAIEYSTDFYNQLLRSYPGVNFV
NGDAFDLDATLGEHKGQMFDSVISAVPMLNFPMAARIKLLDELLKRVPHGRPVVQISYGPISPIVAQPHLYHIRHFDFIV
RNIPPAQLWTYTRA
;
_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 "5'-DEOXY-5'-METHYLTHIOADENOSINE" MTA 
3 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLN n 
1 4   PRO n 
1 5   LYS n 
1 6   LYS n 
1 7   VAL n 
1 8   GLY n 
1 9   ALA n 
1 10  ILE n 
1 11  VAL n 
1 12  PRO n 
1 13  THR n 
1 14  SER n 
1 15  SER n 
1 16  ILE n 
1 17  THR n 
1 18  ALA n 
1 19  LYS n 
1 20  LYS n 
1 21  MET n 
1 22  ALA n 
1 23  SER n 
1 24  VAL n 
1 25  ILE n 
1 26  ASN n 
1 27  PRO n 
1 28  HIS n 
1 29  SER n 
1 30  GLY n 
1 31  LEU n 
1 32  PRO n 
1 33  VAL n 
1 34  LEU n 
1 35  GLU n 
1 36  LEU n 
1 37  GLY n 
1 38  PRO n 
1 39  GLY n 
1 40  THR n 
1 41  GLY n 
1 42  VAL n 
1 43  ILE n 
1 44  THR n 
1 45  LYS n 
1 46  ALA n 
1 47  ILE n 
1 48  LEU n 
1 49  ALA n 
1 50  ARG n 
1 51  GLY n 
1 52  ILE n 
1 53  LYS n 
1 54  PRO n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ALA n 
1 60  ILE n 
1 61  GLU n 
1 62  TYR n 
1 63  SER n 
1 64  THR n 
1 65  ASP n 
1 66  PHE n 
1 67  TYR n 
1 68  ASN n 
1 69  GLN n 
1 70  LEU n 
1 71  LEU n 
1 72  ARG n 
1 73  SER n 
1 74  TYR n 
1 75  PRO n 
1 76  GLY n 
1 77  VAL n 
1 78  ASN n 
1 79  PHE n 
1 80  VAL n 
1 81  ASN n 
1 82  GLY n 
1 83  ASP n 
1 84  ALA n 
1 85  PHE n 
1 86  ASP n 
1 87  LEU n 
1 88  ASP n 
1 89  ALA n 
1 90  THR n 
1 91  LEU n 
1 92  GLY n 
1 93  GLU n 
1 94  HIS n 
1 95  LYS n 
1 96  GLY n 
1 97  GLN n 
1 98  MET n 
1 99  PHE n 
1 100 ASP n 
1 101 SER n 
1 102 VAL n 
1 103 ILE n 
1 104 SER n 
1 105 ALA n 
1 106 VAL n 
1 107 PRO n 
1 108 MET n 
1 109 LEU n 
1 110 ASN n 
1 111 PHE n 
1 112 PRO n 
1 113 MET n 
1 114 ALA n 
1 115 ALA n 
1 116 ARG n 
1 117 ILE n 
1 118 LYS n 
1 119 LEU n 
1 120 LEU n 
1 121 ASP n 
1 122 GLU n 
1 123 LEU n 
1 124 LEU n 
1 125 LYS n 
1 126 ARG n 
1 127 VAL n 
1 128 PRO n 
1 129 HIS n 
1 130 GLY n 
1 131 ARG n 
1 132 PRO n 
1 133 VAL n 
1 134 VAL n 
1 135 GLN n 
1 136 ILE n 
1 137 SER n 
1 138 TYR n 
1 139 GLY n 
1 140 PRO n 
1 141 ILE n 
1 142 SER n 
1 143 PRO n 
1 144 ILE n 
1 145 VAL n 
1 146 ALA n 
1 147 GLN n 
1 148 PRO n 
1 149 HIS n 
1 150 LEU n 
1 151 TYR n 
1 152 HIS n 
1 153 ILE n 
1 154 ARG n 
1 155 HIS n 
1 156 PHE n 
1 157 ASP n 
1 158 PHE n 
1 159 ILE n 
1 160 VAL n 
1 161 ARG n 
1 162 ASN n 
1 163 ILE n 
1 164 PRO n 
1 165 PRO n 
1 166 ALA n 
1 167 GLN n 
1 168 LEU n 
1 169 TRP n 
1 170 THR n 
1 171 TYR n 
1 172 THR n 
1 173 ARG n 
1 174 ALA 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                   174 
_entity_src_gen.gene_src_common_name               'Agrobacterium fabrum (strain C58 / ATCC 33970)' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Atu0300 
_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      'Agrobacterium tumefaciens (strain C58)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     176299 
_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              C43 
_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 
GLN 'L-peptide linking' y GLUTAMINE                         ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                           ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                         ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                             ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                           ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                            ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                        ? 'C5 H11 N O2 S'   149.211 
MTA non-polymer         . "5'-DEOXY-5'-METHYLTHIOADENOSINE" ? 'C11 H15 N5 O3 S' 297.334 
PHE 'L-peptide linking' y PHENYLALANINE                     ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                           ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                            ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                         ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                          ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                            ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   24  ?   ?   ?   A . n 
A 1 2   PRO 2   25  25  PRO PRO A . n 
A 1 3   GLN 3   26  26  GLN GLN A . n 
A 1 4   PRO 4   27  27  PRO PRO A . n 
A 1 5   LYS 5   28  28  LYS LYS A . n 
A 1 6   LYS 6   29  29  LYS LYS A . n 
A 1 7   VAL 7   30  30  VAL VAL A . n 
A 1 8   GLY 8   31  31  GLY GLY A . n 
A 1 9   ALA 9   32  32  ALA ALA A . n 
A 1 10  ILE 10  33  33  ILE ILE A . n 
A 1 11  VAL 11  34  34  VAL VAL A . n 
A 1 12  PRO 12  35  35  PRO PRO A . n 
A 1 13  THR 13  36  36  THR THR A . n 
A 1 14  SER 14  37  37  SER SER A . n 
A 1 15  SER 15  38  38  SER SER A . n 
A 1 16  ILE 16  39  39  ILE ILE A . n 
A 1 17  THR 17  40  40  THR THR A . n 
A 1 18  ALA 18  41  41  ALA ALA A . n 
A 1 19  LYS 19  42  42  LYS LYS A . n 
A 1 20  LYS 20  43  43  LYS LYS A . n 
A 1 21  MET 21  44  44  MET MET A . n 
A 1 22  ALA 22  45  45  ALA ALA A . n 
A 1 23  SER 23  46  46  SER SER A . n 
A 1 24  VAL 24  47  47  VAL VAL A . n 
A 1 25  ILE 25  48  48  ILE ILE A . n 
A 1 26  ASN 26  49  49  ASN ASN A . n 
A 1 27  PRO 27  50  50  PRO PRO A . n 
A 1 28  HIS 28  51  51  HIS HIS A . n 
A 1 29  SER 29  52  52  SER SER A . n 
A 1 30  GLY 30  53  53  GLY GLY A . n 
A 1 31  LEU 31  54  54  LEU LEU A . n 
A 1 32  PRO 32  55  55  PRO PRO A . n 
A 1 33  VAL 33  56  56  VAL VAL A . n 
A 1 34  LEU 34  57  57  LEU LEU A . n 
A 1 35  GLU 35  58  58  GLU GLU A . n 
A 1 36  LEU 36  59  59  LEU LEU A . n 
A 1 37  GLY 37  60  60  GLY GLY A . n 
A 1 38  PRO 38  61  61  PRO PRO A . n 
A 1 39  GLY 39  62  62  GLY GLY A . n 
A 1 40  THR 40  63  63  THR THR A . n 
A 1 41  GLY 41  64  64  GLY GLY A . n 
A 1 42  VAL 42  65  65  VAL VAL A . n 
A 1 43  ILE 43  66  66  ILE ILE A . n 
A 1 44  THR 44  67  67  THR THR A . n 
A 1 45  LYS 45  68  68  LYS LYS A . n 
A 1 46  ALA 46  69  69  ALA ALA A . n 
A 1 47  ILE 47  70  70  ILE ILE A . n 
A 1 48  LEU 48  71  71  LEU LEU A . n 
A 1 49  ALA 49  72  72  ALA ALA A . n 
A 1 50  ARG 50  73  73  ARG ARG A . n 
A 1 51  GLY 51  74  74  GLY GLY A . n 
A 1 52  ILE 52  75  75  ILE ILE A . n 
A 1 53  LYS 53  76  76  LYS LYS A . n 
A 1 54  PRO 54  77  77  PRO PRO A . n 
A 1 55  GLU 55  78  78  GLU GLU A . n 
A 1 56  SER 56  79  79  SER SER A . n 
A 1 57  LEU 57  80  80  LEU LEU A . n 
A 1 58  THR 58  81  81  THR THR A . n 
A 1 59  ALA 59  82  82  ALA ALA A . n 
A 1 60  ILE 60  83  83  ILE ILE A . n 
A 1 61  GLU 61  84  84  GLU GLU A . n 
A 1 62  TYR 62  85  85  TYR TYR A . n 
A 1 63  SER 63  86  86  SER SER A . n 
A 1 64  THR 64  87  87  THR THR A . n 
A 1 65  ASP 65  88  88  ASP ASP A . n 
A 1 66  PHE 66  89  89  PHE PHE A . n 
A 1 67  TYR 67  90  90  TYR TYR A . n 
A 1 68  ASN 68  91  91  ASN ASN A . n 
A 1 69  GLN 69  92  92  GLN GLN A . n 
A 1 70  LEU 70  93  93  LEU LEU A . n 
A 1 71  LEU 71  94  94  LEU LEU A . n 
A 1 72  ARG 72  95  95  ARG ARG A . n 
A 1 73  SER 73  96  96  SER SER A . n 
A 1 74  TYR 74  97  97  TYR TYR A . n 
A 1 75  PRO 75  98  98  PRO PRO A . n 
A 1 76  GLY 76  99  99  GLY GLY A . n 
A 1 77  VAL 77  100 100 VAL VAL A . n 
A 1 78  ASN 78  101 101 ASN ASN A . n 
A 1 79  PHE 79  102 102 PHE PHE A . n 
A 1 80  VAL 80  103 103 VAL VAL A . n 
A 1 81  ASN 81  104 104 ASN ASN A . n 
A 1 82  GLY 82  105 105 GLY GLY A . n 
A 1 83  ASP 83  106 106 ASP ASP A . n 
A 1 84  ALA 84  107 107 ALA ALA A . n 
A 1 85  PHE 85  108 108 PHE PHE A . n 
A 1 86  ASP 86  109 109 ASP ASP A . n 
A 1 87  LEU 87  110 110 LEU LEU A . n 
A 1 88  ASP 88  111 111 ASP ASP A . n 
A 1 89  ALA 89  112 112 ALA ALA A . n 
A 1 90  THR 90  113 113 THR THR A . n 
A 1 91  LEU 91  114 114 LEU LEU A . n 
A 1 92  GLY 92  115 115 GLY GLY A . n 
A 1 93  GLU 93  116 116 GLU GLU A . n 
A 1 94  HIS 94  117 117 HIS HIS A . n 
A 1 95  LYS 95  118 118 LYS LYS A . n 
A 1 96  GLY 96  119 119 GLY GLY A . n 
A 1 97  GLN 97  120 120 GLN GLN A . n 
A 1 98  MET 98  121 121 MET MET A . n 
A 1 99  PHE 99  122 122 PHE PHE A . n 
A 1 100 ASP 100 123 123 ASP ASP A . n 
A 1 101 SER 101 124 124 SER SER A . n 
A 1 102 VAL 102 125 125 VAL VAL A . n 
A 1 103 ILE 103 126 126 ILE ILE A . n 
A 1 104 SER 104 127 127 SER SER A . n 
A 1 105 ALA 105 128 128 ALA ALA A . n 
A 1 106 VAL 106 129 129 VAL VAL A . n 
A 1 107 PRO 107 130 130 PRO PRO A . n 
A 1 108 MET 108 131 131 MET MET A . n 
A 1 109 LEU 109 132 132 LEU LEU A . n 
A 1 110 ASN 110 133 133 ASN ASN A . n 
A 1 111 PHE 111 134 134 PHE PHE A . n 
A 1 112 PRO 112 135 135 PRO PRO A . n 
A 1 113 MET 113 136 136 MET MET A . n 
A 1 114 ALA 114 137 137 ALA ALA A . n 
A 1 115 ALA 115 138 138 ALA ALA A . n 
A 1 116 ARG 116 139 139 ARG ARG A . n 
A 1 117 ILE 117 140 140 ILE ILE A . n 
A 1 118 LYS 118 141 141 LYS LYS A . n 
A 1 119 LEU 119 142 142 LEU LEU A . n 
A 1 120 LEU 120 143 143 LEU LEU A . n 
A 1 121 ASP 121 144 144 ASP ASP A . n 
A 1 122 GLU 122 145 145 GLU GLU A . n 
A 1 123 LEU 123 146 146 LEU LEU A . n 
A 1 124 LEU 124 147 147 LEU LEU A . n 
A 1 125 LYS 125 148 148 LYS LYS A . n 
A 1 126 ARG 126 149 149 ARG ARG A . n 
A 1 127 VAL 127 150 150 VAL VAL A . n 
A 1 128 PRO 128 151 151 PRO PRO A . n 
A 1 129 HIS 129 152 152 HIS HIS A . n 
A 1 130 GLY 130 153 153 GLY GLY A . n 
A 1 131 ARG 131 154 154 ARG ARG A . n 
A 1 132 PRO 132 155 155 PRO PRO A . n 
A 1 133 VAL 133 156 156 VAL VAL A . n 
A 1 134 VAL 134 157 157 VAL VAL A . n 
A 1 135 GLN 135 158 158 GLN GLN A . n 
A 1 136 ILE 136 159 159 ILE ILE A . n 
A 1 137 SER 137 160 160 SER SER A . n 
A 1 138 TYR 138 161 161 TYR TYR A . n 
A 1 139 GLY 139 162 162 GLY GLY A . n 
A 1 140 PRO 140 163 163 PRO PRO A . n 
A 1 141 ILE 141 164 164 ILE ILE A . n 
A 1 142 SER 142 165 165 SER SER A . n 
A 1 143 PRO 143 166 166 PRO PRO A . n 
A 1 144 ILE 144 167 167 ILE ILE A . n 
A 1 145 VAL 145 168 168 VAL VAL A . n 
A 1 146 ALA 146 169 169 ALA ALA A . n 
A 1 147 GLN 147 170 170 GLN GLN A . n 
A 1 148 PRO 148 171 171 PRO PRO A . n 
A 1 149 HIS 149 172 172 HIS HIS A . n 
A 1 150 LEU 150 173 173 LEU LEU A . n 
A 1 151 TYR 151 174 174 TYR TYR A . n 
A 1 152 HIS 152 175 175 HIS HIS A . n 
A 1 153 ILE 153 176 176 ILE ILE A . n 
A 1 154 ARG 154 177 177 ARG ARG A . n 
A 1 155 HIS 155 178 178 HIS HIS A . n 
A 1 156 PHE 156 179 179 PHE PHE A . n 
A 1 157 ASP 157 180 180 ASP ASP A . n 
A 1 158 PHE 158 181 181 PHE PHE A . n 
A 1 159 ILE 159 182 182 ILE ILE A . n 
A 1 160 VAL 160 183 183 VAL VAL A . n 
A 1 161 ARG 161 184 184 ARG ARG A . n 
A 1 162 ASN 162 185 185 ASN ASN A . n 
A 1 163 ILE 163 186 186 ILE ILE A . n 
A 1 164 PRO 164 187 187 PRO PRO A . n 
A 1 165 PRO 165 188 188 PRO PRO A . n 
A 1 166 ALA 166 189 189 ALA ALA A . n 
A 1 167 GLN 167 190 190 GLN GLN A . n 
A 1 168 LEU 168 191 191 LEU LEU A . n 
A 1 169 TRP 169 192 192 TRP TRP A . n 
A 1 170 THR 170 193 193 THR THR A . n 
A 1 171 TYR 171 194 194 TYR TYR A . n 
A 1 172 THR 172 195 195 THR THR A . n 
A 1 173 ARG 173 196 196 ARG ARG A . n 
A 1 174 ALA 174 197 197 ALA ALA A . n 
B 1 1   GLY 1   24  ?   ?   ?   B . n 
B 1 2   PRO 2   25  ?   ?   ?   B . n 
B 1 3   GLN 3   26  ?   ?   ?   B . n 
B 1 4   PRO 4   27  ?   ?   ?   B . n 
B 1 5   LYS 5   28  ?   ?   ?   B . n 
B 1 6   LYS 6   29  ?   ?   ?   B . n 
B 1 7   VAL 7   30  ?   ?   ?   B . n 
B 1 8   GLY 8   31  ?   ?   ?   B . n 
B 1 9   ALA 9   32  ?   ?   ?   B . n 
B 1 10  ILE 10  33  ?   ?   ?   B . n 
B 1 11  VAL 11  34  34  VAL VAL B . n 
B 1 12  PRO 12  35  35  PRO PRO B . n 
B 1 13  THR 13  36  36  THR THR B . n 
B 1 14  SER 14  37  37  SER SER B . n 
B 1 15  SER 15  38  38  SER SER B . n 
B 1 16  ILE 16  39  39  ILE ILE B . n 
B 1 17  THR 17  40  40  THR THR B . n 
B 1 18  ALA 18  41  41  ALA ALA B . n 
B 1 19  LYS 19  42  42  LYS LYS B . n 
B 1 20  LYS 20  43  43  LYS LYS B . n 
B 1 21  MET 21  44  44  MET MET B . n 
B 1 22  ALA 22  45  45  ALA ALA B . n 
B 1 23  SER 23  46  46  SER SER B . n 
B 1 24  VAL 24  47  47  VAL VAL B . n 
B 1 25  ILE 25  48  48  ILE ILE B . n 
B 1 26  ASN 26  49  49  ASN ASN B . n 
B 1 27  PRO 27  50  50  PRO PRO B . n 
B 1 28  HIS 28  51  51  HIS HIS B . n 
B 1 29  SER 29  52  52  SER SER B . n 
B 1 30  GLY 30  53  53  GLY GLY B . n 
B 1 31  LEU 31  54  54  LEU LEU B . n 
B 1 32  PRO 32  55  55  PRO PRO B . n 
B 1 33  VAL 33  56  56  VAL VAL B . n 
B 1 34  LEU 34  57  57  LEU LEU B . n 
B 1 35  GLU 35  58  58  GLU GLU B . n 
B 1 36  LEU 36  59  59  LEU LEU B . n 
B 1 37  GLY 37  60  60  GLY GLY B . n 
B 1 38  PRO 38  61  61  PRO PRO B . n 
B 1 39  GLY 39  62  62  GLY GLY B . n 
B 1 40  THR 40  63  63  THR THR B . n 
B 1 41  GLY 41  64  64  GLY GLY B . n 
B 1 42  VAL 42  65  65  VAL VAL B . n 
B 1 43  ILE 43  66  66  ILE ILE B . n 
B 1 44  THR 44  67  67  THR THR B . n 
B 1 45  LYS 45  68  68  LYS LYS B . n 
B 1 46  ALA 46  69  69  ALA ALA B . n 
B 1 47  ILE 47  70  70  ILE ILE B . n 
B 1 48  LEU 48  71  71  LEU LEU B . n 
B 1 49  ALA 49  72  72  ALA ALA B . n 
B 1 50  ARG 50  73  73  ARG ARG B . n 
B 1 51  GLY 51  74  74  GLY GLY B . n 
B 1 52  ILE 52  75  75  ILE ILE B . n 
B 1 53  LYS 53  76  76  LYS LYS B . n 
B 1 54  PRO 54  77  77  PRO PRO B . n 
B 1 55  GLU 55  78  78  GLU GLU B . n 
B 1 56  SER 56  79  79  SER SER B . n 
B 1 57  LEU 57  80  80  LEU LEU B . n 
B 1 58  THR 58  81  81  THR THR B . n 
B 1 59  ALA 59  82  82  ALA ALA B . n 
B 1 60  ILE 60  83  83  ILE ILE B . n 
B 1 61  GLU 61  84  84  GLU GLU B . n 
B 1 62  TYR 62  85  85  TYR TYR B . n 
B 1 63  SER 63  86  86  SER SER B . n 
B 1 64  THR 64  87  87  THR THR B . n 
B 1 65  ASP 65  88  88  ASP ASP B . n 
B 1 66  PHE 66  89  89  PHE PHE B . n 
B 1 67  TYR 67  90  90  TYR TYR B . n 
B 1 68  ASN 68  91  91  ASN ASN B . n 
B 1 69  GLN 69  92  92  GLN GLN B . n 
B 1 70  LEU 70  93  93  LEU LEU B . n 
B 1 71  LEU 71  94  94  LEU LEU B . n 
B 1 72  ARG 72  95  95  ARG ARG B . n 
B 1 73  SER 73  96  96  SER SER B . n 
B 1 74  TYR 74  97  97  TYR TYR B . n 
B 1 75  PRO 75  98  98  PRO PRO B . n 
B 1 76  GLY 76  99  99  GLY GLY B . n 
B 1 77  VAL 77  100 100 VAL VAL B . n 
B 1 78  ASN 78  101 101 ASN ASN B . n 
B 1 79  PHE 79  102 102 PHE PHE B . n 
B 1 80  VAL 80  103 103 VAL VAL B . n 
B 1 81  ASN 81  104 104 ASN ASN B . n 
B 1 82  GLY 82  105 105 GLY GLY B . n 
B 1 83  ASP 83  106 106 ASP ASP B . n 
B 1 84  ALA 84  107 107 ALA ALA B . n 
B 1 85  PHE 85  108 108 PHE PHE B . n 
B 1 86  ASP 86  109 109 ASP ASP B . n 
B 1 87  LEU 87  110 110 LEU LEU B . n 
B 1 88  ASP 88  111 111 ASP ASP B . n 
B 1 89  ALA 89  112 112 ALA ALA B . n 
B 1 90  THR 90  113 113 THR THR B . n 
B 1 91  LEU 91  114 114 LEU LEU B . n 
B 1 92  GLY 92  115 115 GLY GLY B . n 
B 1 93  GLU 93  116 116 GLU GLU B . n 
B 1 94  HIS 94  117 117 HIS HIS B . n 
B 1 95  LYS 95  118 118 LYS LYS B . n 
B 1 96  GLY 96  119 119 GLY GLY B . n 
B 1 97  GLN 97  120 120 GLN GLN B . n 
B 1 98  MET 98  121 121 MET MET B . n 
B 1 99  PHE 99  122 122 PHE PHE B . n 
B 1 100 ASP 100 123 123 ASP ASP B . n 
B 1 101 SER 101 124 124 SER SER B . n 
B 1 102 VAL 102 125 125 VAL VAL B . n 
B 1 103 ILE 103 126 126 ILE ILE B . n 
B 1 104 SER 104 127 127 SER SER B . n 
B 1 105 ALA 105 128 128 ALA ALA B . n 
B 1 106 VAL 106 129 129 VAL VAL B . n 
B 1 107 PRO 107 130 130 PRO PRO B . n 
B 1 108 MET 108 131 131 MET MET B . n 
B 1 109 LEU 109 132 132 LEU LEU B . n 
B 1 110 ASN 110 133 133 ASN ASN B . n 
B 1 111 PHE 111 134 134 PHE PHE B . n 
B 1 112 PRO 112 135 135 PRO PRO B . n 
B 1 113 MET 113 136 136 MET MET B . n 
B 1 114 ALA 114 137 137 ALA ALA B . n 
B 1 115 ALA 115 138 138 ALA ALA B . n 
B 1 116 ARG 116 139 139 ARG ARG B . n 
B 1 117 ILE 117 140 140 ILE ILE B . n 
B 1 118 LYS 118 141 141 LYS LYS B . n 
B 1 119 LEU 119 142 142 LEU LEU B . n 
B 1 120 LEU 120 143 143 LEU LEU B . n 
B 1 121 ASP 121 144 144 ASP ASP B . n 
B 1 122 GLU 122 145 145 GLU GLU B . n 
B 1 123 LEU 123 146 146 LEU LEU B . n 
B 1 124 LEU 124 147 147 LEU LEU B . n 
B 1 125 LYS 125 148 148 LYS LYS B . n 
B 1 126 ARG 126 149 149 ARG ARG B . n 
B 1 127 VAL 127 150 150 VAL VAL B . n 
B 1 128 PRO 128 151 151 PRO PRO B . n 
B 1 129 HIS 129 152 152 HIS HIS B . n 
B 1 130 GLY 130 153 153 GLY GLY B . n 
B 1 131 ARG 131 154 154 ARG ARG B . n 
B 1 132 PRO 132 155 155 PRO PRO B . n 
B 1 133 VAL 133 156 156 VAL VAL B . n 
B 1 134 VAL 134 157 157 VAL VAL B . n 
B 1 135 GLN 135 158 158 GLN GLN B . n 
B 1 136 ILE 136 159 159 ILE ILE B . n 
B 1 137 SER 137 160 160 SER SER B . n 
B 1 138 TYR 138 161 161 TYR TYR B . n 
B 1 139 GLY 139 162 162 GLY GLY B . n 
B 1 140 PRO 140 163 163 PRO PRO B . n 
B 1 141 ILE 141 164 164 ILE ILE B . n 
B 1 142 SER 142 165 165 SER SER B . n 
B 1 143 PRO 143 166 166 PRO PRO B . n 
B 1 144 ILE 144 167 167 ILE ILE B . n 
B 1 145 VAL 145 168 168 VAL VAL B . n 
B 1 146 ALA 146 169 169 ALA ALA B . n 
B 1 147 GLN 147 170 170 GLN GLN B . n 
B 1 148 PRO 148 171 171 PRO PRO B . n 
B 1 149 HIS 149 172 172 HIS HIS B . n 
B 1 150 LEU 150 173 173 LEU LEU B . n 
B 1 151 TYR 151 174 174 TYR TYR B . n 
B 1 152 HIS 152 175 175 HIS HIS B . n 
B 1 153 ILE 153 176 176 ILE ILE B . n 
B 1 154 ARG 154 177 177 ARG ARG B . n 
B 1 155 HIS 155 178 178 HIS HIS B . n 
B 1 156 PHE 156 179 179 PHE PHE B . n 
B 1 157 ASP 157 180 180 ASP ASP B . n 
B 1 158 PHE 158 181 181 PHE PHE B . n 
B 1 159 ILE 159 182 182 ILE ILE B . n 
B 1 160 VAL 160 183 183 VAL VAL B . n 
B 1 161 ARG 161 184 184 ARG ARG B . n 
B 1 162 ASN 162 185 185 ASN ASN B . n 
B 1 163 ILE 163 186 186 ILE ILE B . n 
B 1 164 PRO 164 187 187 PRO PRO B . n 
B 1 165 PRO 165 188 188 PRO PRO B . n 
B 1 166 ALA 166 189 189 ALA ALA B . n 
B 1 167 GLN 167 190 190 GLN GLN B . n 
B 1 168 LEU 168 191 191 LEU LEU B . n 
B 1 169 TRP 169 192 192 TRP TRP B . n 
B 1 170 THR 170 193 193 THR THR B . n 
B 1 171 TYR 171 194 194 TYR TYR B . n 
B 1 172 THR 172 195 195 THR THR B . n 
B 1 173 ARG 173 196 196 ARG ARG B . n 
B 1 174 ALA 174 197 197 ALA ALA B . n 
C 1 1   GLY 1   24  ?   ?   ?   C . n 
C 1 2   PRO 2   25  ?   ?   ?   C . n 
C 1 3   GLN 3   26  ?   ?   ?   C . n 
C 1 4   PRO 4   27  ?   ?   ?   C . n 
C 1 5   LYS 5   28  ?   ?   ?   C . n 
C 1 6   LYS 6   29  ?   ?   ?   C . n 
C 1 7   VAL 7   30  ?   ?   ?   C . n 
C 1 8   GLY 8   31  ?   ?   ?   C . n 
C 1 9   ALA 9   32  ?   ?   ?   C . n 
C 1 10  ILE 10  33  ?   ?   ?   C . n 
C 1 11  VAL 11  34  34  VAL VAL C . n 
C 1 12  PRO 12  35  35  PRO PRO C . n 
C 1 13  THR 13  36  36  THR THR C . n 
C 1 14  SER 14  37  37  SER SER C . n 
C 1 15  SER 15  38  38  SER SER C . n 
C 1 16  ILE 16  39  39  ILE ILE C . n 
C 1 17  THR 17  40  40  THR THR C . n 
C 1 18  ALA 18  41  41  ALA ALA C . n 
C 1 19  LYS 19  42  42  LYS LYS C . n 
C 1 20  LYS 20  43  43  LYS LYS C . n 
C 1 21  MET 21  44  44  MET MET C . n 
C 1 22  ALA 22  45  45  ALA ALA C . n 
C 1 23  SER 23  46  46  SER SER C . n 
C 1 24  VAL 24  47  47  VAL VAL C . n 
C 1 25  ILE 25  48  48  ILE ILE C . n 
C 1 26  ASN 26  49  49  ASN ASN C . n 
C 1 27  PRO 27  50  50  PRO PRO C . n 
C 1 28  HIS 28  51  51  HIS HIS C . n 
C 1 29  SER 29  52  52  SER SER C . n 
C 1 30  GLY 30  53  53  GLY GLY C . n 
C 1 31  LEU 31  54  54  LEU LEU C . n 
C 1 32  PRO 32  55  55  PRO PRO C . n 
C 1 33  VAL 33  56  56  VAL VAL C . n 
C 1 34  LEU 34  57  57  LEU LEU C . n 
C 1 35  GLU 35  58  58  GLU GLU C . n 
C 1 36  LEU 36  59  59  LEU LEU C . n 
C 1 37  GLY 37  60  60  GLY GLY C . n 
C 1 38  PRO 38  61  61  PRO PRO C . n 
C 1 39  GLY 39  62  62  GLY GLY C . n 
C 1 40  THR 40  63  63  THR THR C . n 
C 1 41  GLY 41  64  64  GLY GLY C . n 
C 1 42  VAL 42  65  65  VAL VAL C . n 
C 1 43  ILE 43  66  66  ILE ILE C . n 
C 1 44  THR 44  67  67  THR THR C . n 
C 1 45  LYS 45  68  68  LYS LYS C . n 
C 1 46  ALA 46  69  69  ALA ALA C . n 
C 1 47  ILE 47  70  70  ILE ILE C . n 
C 1 48  LEU 48  71  71  LEU LEU C . n 
C 1 49  ALA 49  72  72  ALA ALA C . n 
C 1 50  ARG 50  73  73  ARG ARG C . n 
C 1 51  GLY 51  74  74  GLY GLY C . n 
C 1 52  ILE 52  75  75  ILE ILE C . n 
C 1 53  LYS 53  76  76  LYS LYS C . n 
C 1 54  PRO 54  77  77  PRO PRO C . n 
C 1 55  GLU 55  78  78  GLU GLU C . n 
C 1 56  SER 56  79  79  SER SER C . n 
C 1 57  LEU 57  80  80  LEU LEU C . n 
C 1 58  THR 58  81  81  THR THR C . n 
C 1 59  ALA 59  82  82  ALA ALA C . n 
C 1 60  ILE 60  83  83  ILE ILE C . n 
C 1 61  GLU 61  84  84  GLU GLU C . n 
C 1 62  TYR 62  85  85  TYR TYR C . n 
C 1 63  SER 63  86  86  SER SER C . n 
C 1 64  THR 64  87  87  THR THR C . n 
C 1 65  ASP 65  88  88  ASP ASP C . n 
C 1 66  PHE 66  89  89  PHE PHE C . n 
C 1 67  TYR 67  90  90  TYR TYR C . n 
C 1 68  ASN 68  91  91  ASN ASN C . n 
C 1 69  GLN 69  92  92  GLN GLN C . n 
C 1 70  LEU 70  93  93  LEU LEU C . n 
C 1 71  LEU 71  94  94  LEU LEU C . n 
C 1 72  ARG 72  95  95  ARG ARG C . n 
C 1 73  SER 73  96  96  SER SER C . n 
C 1 74  TYR 74  97  97  TYR TYR C . n 
C 1 75  PRO 75  98  98  PRO PRO C . n 
C 1 76  GLY 76  99  99  GLY GLY C . n 
C 1 77  VAL 77  100 100 VAL VAL C . n 
C 1 78  ASN 78  101 101 ASN ASN C . n 
C 1 79  PHE 79  102 102 PHE PHE C . n 
C 1 80  VAL 80  103 103 VAL VAL C . n 
C 1 81  ASN 81  104 104 ASN ASN C . n 
C 1 82  GLY 82  105 105 GLY GLY C . n 
C 1 83  ASP 83  106 106 ASP ASP C . n 
C 1 84  ALA 84  107 107 ALA ALA C . n 
C 1 85  PHE 85  108 108 PHE PHE C . n 
C 1 86  ASP 86  109 109 ASP ASP C . n 
C 1 87  LEU 87  110 110 LEU LEU C . n 
C 1 88  ASP 88  111 111 ASP ASP C . n 
C 1 89  ALA 89  112 112 ALA ALA C . n 
C 1 90  THR 90  113 113 THR THR C . n 
C 1 91  LEU 91  114 114 LEU LEU C . n 
C 1 92  GLY 92  115 115 GLY GLY C . n 
C 1 93  GLU 93  116 116 GLU GLU C . n 
C 1 94  HIS 94  117 117 HIS HIS C . n 
C 1 95  LYS 95  118 118 LYS LYS C . n 
C 1 96  GLY 96  119 119 GLY GLY C . n 
C 1 97  GLN 97  120 120 GLN GLN C . n 
C 1 98  MET 98  121 121 MET MET C . n 
C 1 99  PHE 99  122 122 PHE PHE C . n 
C 1 100 ASP 100 123 123 ASP ASP C . n 
C 1 101 SER 101 124 124 SER SER C . n 
C 1 102 VAL 102 125 125 VAL VAL C . n 
C 1 103 ILE 103 126 126 ILE ILE C . n 
C 1 104 SER 104 127 127 SER SER C . n 
C 1 105 ALA 105 128 128 ALA ALA C . n 
C 1 106 VAL 106 129 129 VAL VAL C . n 
C 1 107 PRO 107 130 130 PRO PRO C . n 
C 1 108 MET 108 131 131 MET MET C . n 
C 1 109 LEU 109 132 132 LEU LEU C . n 
C 1 110 ASN 110 133 133 ASN ASN C . n 
C 1 111 PHE 111 134 134 PHE PHE C . n 
C 1 112 PRO 112 135 135 PRO PRO C . n 
C 1 113 MET 113 136 136 MET MET C . n 
C 1 114 ALA 114 137 137 ALA ALA C . n 
C 1 115 ALA 115 138 138 ALA ALA C . n 
C 1 116 ARG 116 139 139 ARG ARG C . n 
C 1 117 ILE 117 140 140 ILE ILE C . n 
C 1 118 LYS 118 141 141 LYS LYS C . n 
C 1 119 LEU 119 142 142 LEU LEU C . n 
C 1 120 LEU 120 143 143 LEU LEU C . n 
C 1 121 ASP 121 144 144 ASP ASP C . n 
C 1 122 GLU 122 145 145 GLU GLU C . n 
C 1 123 LEU 123 146 146 LEU LEU C . n 
C 1 124 LEU 124 147 147 LEU LEU C . n 
C 1 125 LYS 125 148 148 LYS LYS C . n 
C 1 126 ARG 126 149 149 ARG ARG C . n 
C 1 127 VAL 127 150 150 VAL VAL C . n 
C 1 128 PRO 128 151 151 PRO PRO C . n 
C 1 129 HIS 129 152 152 HIS HIS C . n 
C 1 130 GLY 130 153 153 GLY GLY C . n 
C 1 131 ARG 131 154 154 ARG ARG C . n 
C 1 132 PRO 132 155 155 PRO PRO C . n 
C 1 133 VAL 133 156 156 VAL VAL C . n 
C 1 134 VAL 134 157 157 VAL VAL C . n 
C 1 135 GLN 135 158 158 GLN GLN C . n 
C 1 136 ILE 136 159 159 ILE ILE C . n 
C 1 137 SER 137 160 160 SER SER C . n 
C 1 138 TYR 138 161 161 TYR TYR C . n 
C 1 139 GLY 139 162 162 GLY GLY C . n 
C 1 140 PRO 140 163 163 PRO PRO C . n 
C 1 141 ILE 141 164 164 ILE ILE C . n 
C 1 142 SER 142 165 165 SER SER C . n 
C 1 143 PRO 143 166 166 PRO PRO C . n 
C 1 144 ILE 144 167 167 ILE ILE C . n 
C 1 145 VAL 145 168 168 VAL VAL C . n 
C 1 146 ALA 146 169 169 ALA ALA C . n 
C 1 147 GLN 147 170 170 GLN GLN C . n 
C 1 148 PRO 148 171 171 PRO PRO C . n 
C 1 149 HIS 149 172 172 HIS HIS C . n 
C 1 150 LEU 150 173 173 LEU LEU C . n 
C 1 151 TYR 151 174 174 TYR TYR C . n 
C 1 152 HIS 152 175 175 HIS HIS C . n 
C 1 153 ILE 153 176 176 ILE ILE C . n 
C 1 154 ARG 154 177 177 ARG ARG C . n 
C 1 155 HIS 155 178 178 HIS HIS C . n 
C 1 156 PHE 156 179 179 PHE PHE C . n 
C 1 157 ASP 157 180 180 ASP ASP C . n 
C 1 158 PHE 158 181 181 PHE PHE C . n 
C 1 159 ILE 159 182 182 ILE ILE C . n 
C 1 160 VAL 160 183 183 VAL VAL C . n 
C 1 161 ARG 161 184 184 ARG ARG C . n 
C 1 162 ASN 162 185 185 ASN ASN C . n 
C 1 163 ILE 163 186 186 ILE ILE C . n 
C 1 164 PRO 164 187 187 PRO PRO C . n 
C 1 165 PRO 165 188 188 PRO PRO C . n 
C 1 166 ALA 166 189 189 ALA ALA C . n 
C 1 167 GLN 167 190 190 GLN GLN C . n 
C 1 168 LEU 168 191 191 LEU LEU C . n 
C 1 169 TRP 169 192 192 TRP TRP C . n 
C 1 170 THR 170 193 193 THR THR C . n 
C 1 171 TYR 171 194 194 TYR TYR C . n 
C 1 172 THR 172 195 195 THR THR C . n 
C 1 173 ARG 173 196 196 ARG ARG C . n 
C 1 174 ALA 174 197 197 ALA ALA C . n 
D 1 1   GLY 1   24  ?   ?   ?   D . n 
D 1 2   PRO 2   25  ?   ?   ?   D . n 
D 1 3   GLN 3   26  ?   ?   ?   D . n 
D 1 4   PRO 4   27  ?   ?   ?   D . n 
D 1 5   LYS 5   28  ?   ?   ?   D . n 
D 1 6   LYS 6   29  ?   ?   ?   D . n 
D 1 7   VAL 7   30  ?   ?   ?   D . n 
D 1 8   GLY 8   31  ?   ?   ?   D . n 
D 1 9   ALA 9   32  ?   ?   ?   D . n 
D 1 10  ILE 10  33  ?   ?   ?   D . n 
D 1 11  VAL 11  34  34  VAL VAL D . n 
D 1 12  PRO 12  35  35  PRO PRO D . n 
D 1 13  THR 13  36  36  THR THR D . n 
D 1 14  SER 14  37  37  SER SER D . n 
D 1 15  SER 15  38  38  SER SER D . n 
D 1 16  ILE 16  39  39  ILE ILE D . n 
D 1 17  THR 17  40  40  THR THR D . n 
D 1 18  ALA 18  41  41  ALA ALA D . n 
D 1 19  LYS 19  42  42  LYS LYS D . n 
D 1 20  LYS 20  43  43  LYS LYS D . n 
D 1 21  MET 21  44  44  MET MET D . n 
D 1 22  ALA 22  45  45  ALA ALA D . n 
D 1 23  SER 23  46  46  SER SER D . n 
D 1 24  VAL 24  47  47  VAL VAL D . n 
D 1 25  ILE 25  48  48  ILE ILE D . n 
D 1 26  ASN 26  49  49  ASN ASN D . n 
D 1 27  PRO 27  50  50  PRO PRO D . n 
D 1 28  HIS 28  51  51  HIS HIS D . n 
D 1 29  SER 29  52  52  SER SER D . n 
D 1 30  GLY 30  53  53  GLY GLY D . n 
D 1 31  LEU 31  54  54  LEU LEU D . n 
D 1 32  PRO 32  55  55  PRO PRO D . n 
D 1 33  VAL 33  56  56  VAL VAL D . n 
D 1 34  LEU 34  57  57  LEU LEU D . n 
D 1 35  GLU 35  58  58  GLU GLU D . n 
D 1 36  LEU 36  59  59  LEU LEU D . n 
D 1 37  GLY 37  60  60  GLY GLY D . n 
D 1 38  PRO 38  61  61  PRO PRO D . n 
D 1 39  GLY 39  62  62  GLY GLY D . n 
D 1 40  THR 40  63  63  THR THR D . n 
D 1 41  GLY 41  64  64  GLY GLY D . n 
D 1 42  VAL 42  65  65  VAL VAL D . n 
D 1 43  ILE 43  66  66  ILE ILE D . n 
D 1 44  THR 44  67  67  THR THR D . n 
D 1 45  LYS 45  68  68  LYS LYS D . n 
D 1 46  ALA 46  69  69  ALA ALA D . n 
D 1 47  ILE 47  70  70  ILE ILE D . n 
D 1 48  LEU 48  71  71  LEU LEU D . n 
D 1 49  ALA 49  72  72  ALA ALA D . n 
D 1 50  ARG 50  73  73  ARG ARG D . n 
D 1 51  GLY 51  74  74  GLY GLY D . n 
D 1 52  ILE 52  75  75  ILE ILE D . n 
D 1 53  LYS 53  76  76  LYS LYS D . n 
D 1 54  PRO 54  77  77  PRO PRO D . n 
D 1 55  GLU 55  78  78  GLU GLU D . n 
D 1 56  SER 56  79  79  SER SER D . n 
D 1 57  LEU 57  80  80  LEU LEU D . n 
D 1 58  THR 58  81  81  THR THR D . n 
D 1 59  ALA 59  82  82  ALA ALA D . n 
D 1 60  ILE 60  83  83  ILE ILE D . n 
D 1 61  GLU 61  84  84  GLU GLU D . n 
D 1 62  TYR 62  85  85  TYR TYR D . n 
D 1 63  SER 63  86  86  SER SER D . n 
D 1 64  THR 64  87  87  THR THR D . n 
D 1 65  ASP 65  88  88  ASP ASP D . n 
D 1 66  PHE 66  89  89  PHE PHE D . n 
D 1 67  TYR 67  90  90  TYR TYR D . n 
D 1 68  ASN 68  91  91  ASN ASN D . n 
D 1 69  GLN 69  92  92  GLN GLN D . n 
D 1 70  LEU 70  93  93  LEU LEU D . n 
D 1 71  LEU 71  94  94  LEU LEU D . n 
D 1 72  ARG 72  95  95  ARG ARG D . n 
D 1 73  SER 73  96  96  SER SER D . n 
D 1 74  TYR 74  97  97  TYR TYR D . n 
D 1 75  PRO 75  98  98  PRO PRO D . n 
D 1 76  GLY 76  99  99  GLY GLY D . n 
D 1 77  VAL 77  100 100 VAL VAL D . n 
D 1 78  ASN 78  101 101 ASN ASN D . n 
D 1 79  PHE 79  102 102 PHE PHE D . n 
D 1 80  VAL 80  103 103 VAL VAL D . n 
D 1 81  ASN 81  104 104 ASN ASN D . n 
D 1 82  GLY 82  105 105 GLY GLY D . n 
D 1 83  ASP 83  106 106 ASP ASP D . n 
D 1 84  ALA 84  107 107 ALA ALA D . n 
D 1 85  PHE 85  108 108 PHE PHE D . n 
D 1 86  ASP 86  109 109 ASP ASP D . n 
D 1 87  LEU 87  110 110 LEU LEU D . n 
D 1 88  ASP 88  111 111 ASP ASP D . n 
D 1 89  ALA 89  112 112 ALA ALA D . n 
D 1 90  THR 90  113 113 THR THR D . n 
D 1 91  LEU 91  114 114 LEU LEU D . n 
D 1 92  GLY 92  115 115 GLY GLY D . n 
D 1 93  GLU 93  116 116 GLU GLU D . n 
D 1 94  HIS 94  117 117 HIS HIS D . n 
D 1 95  LYS 95  118 118 LYS LYS D . n 
D 1 96  GLY 96  119 119 GLY GLY D . n 
D 1 97  GLN 97  120 120 GLN GLN D . n 
D 1 98  MET 98  121 121 MET MET D . n 
D 1 99  PHE 99  122 122 PHE PHE D . n 
D 1 100 ASP 100 123 123 ASP ASP D . n 
D 1 101 SER 101 124 124 SER SER D . n 
D 1 102 VAL 102 125 125 VAL VAL D . n 
D 1 103 ILE 103 126 126 ILE ILE D . n 
D 1 104 SER 104 127 127 SER SER D . n 
D 1 105 ALA 105 128 128 ALA ALA D . n 
D 1 106 VAL 106 129 129 VAL VAL D . n 
D 1 107 PRO 107 130 130 PRO PRO D . n 
D 1 108 MET 108 131 131 MET MET D . n 
D 1 109 LEU 109 132 132 LEU LEU D . n 
D 1 110 ASN 110 133 133 ASN ASN D . n 
D 1 111 PHE 111 134 134 PHE PHE D . n 
D 1 112 PRO 112 135 135 PRO PRO D . n 
D 1 113 MET 113 136 136 MET MET D . n 
D 1 114 ALA 114 137 137 ALA ALA D . n 
D 1 115 ALA 115 138 138 ALA ALA D . n 
D 1 116 ARG 116 139 139 ARG ARG D . n 
D 1 117 ILE 117 140 140 ILE ILE D . n 
D 1 118 LYS 118 141 141 LYS LYS D . n 
D 1 119 LEU 119 142 142 LEU LEU D . n 
D 1 120 LEU 120 143 143 LEU LEU D . n 
D 1 121 ASP 121 144 144 ASP ASP D . n 
D 1 122 GLU 122 145 145 GLU GLU D . n 
D 1 123 LEU 123 146 146 LEU LEU D . n 
D 1 124 LEU 124 147 147 LEU LEU D . n 
D 1 125 LYS 125 148 148 LYS LYS D . n 
D 1 126 ARG 126 149 149 ARG ARG D . n 
D 1 127 VAL 127 150 150 VAL VAL D . n 
D 1 128 PRO 128 151 151 PRO PRO D . n 
D 1 129 HIS 129 152 152 HIS HIS D . n 
D 1 130 GLY 130 153 153 GLY GLY D . n 
D 1 131 ARG 131 154 154 ARG ARG D . n 
D 1 132 PRO 132 155 155 PRO PRO D . n 
D 1 133 VAL 133 156 156 VAL VAL D . n 
D 1 134 VAL 134 157 157 VAL VAL D . n 
D 1 135 GLN 135 158 158 GLN GLN D . n 
D 1 136 ILE 136 159 159 ILE ILE D . n 
D 1 137 SER 137 160 160 SER SER D . n 
D 1 138 TYR 138 161 161 TYR TYR D . n 
D 1 139 GLY 139 162 162 GLY GLY D . n 
D 1 140 PRO 140 163 163 PRO PRO D . n 
D 1 141 ILE 141 164 164 ILE ILE D . n 
D 1 142 SER 142 165 165 SER SER D . n 
D 1 143 PRO 143 166 166 PRO PRO D . n 
D 1 144 ILE 144 167 167 ILE ILE D . n 
D 1 145 VAL 145 168 168 VAL VAL D . n 
D 1 146 ALA 146 169 169 ALA ALA D . n 
D 1 147 GLN 147 170 170 GLN GLN D . n 
D 1 148 PRO 148 171 171 PRO PRO D . n 
D 1 149 HIS 149 172 172 HIS HIS D . n 
D 1 150 LEU 150 173 173 LEU LEU D . n 
D 1 151 TYR 151 174 174 TYR TYR D . n 
D 1 152 HIS 152 175 175 HIS HIS D . n 
D 1 153 ILE 153 176 176 ILE ILE D . n 
D 1 154 ARG 154 177 177 ARG ARG D . n 
D 1 155 HIS 155 178 178 HIS HIS D . n 
D 1 156 PHE 156 179 179 PHE PHE D . n 
D 1 157 ASP 157 180 180 ASP ASP D . n 
D 1 158 PHE 158 181 181 PHE PHE D . n 
D 1 159 ILE 159 182 182 ILE ILE D . n 
D 1 160 VAL 160 183 183 VAL VAL D . n 
D 1 161 ARG 161 184 184 ARG ARG D . n 
D 1 162 ASN 162 185 185 ASN ASN D . n 
D 1 163 ILE 163 186 186 ILE ILE D . n 
D 1 164 PRO 164 187 187 PRO PRO D . n 
D 1 165 PRO 165 188 188 PRO PRO D . n 
D 1 166 ALA 166 189 189 ALA ALA D . n 
D 1 167 GLN 167 190 190 GLN GLN D . n 
D 1 168 LEU 168 191 191 LEU LEU D . n 
D 1 169 TRP 169 192 192 TRP TRP D . n 
D 1 170 THR 170 193 193 THR THR D . n 
D 1 171 TYR 171 194 194 TYR TYR D . n 
D 1 172 THR 172 195 195 THR THR D . n 
D 1 173 ARG 173 196 196 ARG ARG D . n 
D 1 174 ALA 174 197 197 ALA ALA D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MTA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MTA 
_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 MTA 1   201 201 MTA MTA A . 
F 2 MTA 1   201 201 MTA MTA B . 
G 2 MTA 1   201 201 MTA MTA C . 
H 2 MTA 1   201 201 MTA MTA D . 
I 3 HOH 1   301 257 HOH HOH A . 
I 3 HOH 2   302 411 HOH HOH A . 
I 3 HOH 3   303 77  HOH HOH A . 
I 3 HOH 4   304 26  HOH HOH A . 
I 3 HOH 5   305 18  HOH HOH A . 
I 3 HOH 6   306 387 HOH HOH A . 
I 3 HOH 7   307 147 HOH HOH A . 
I 3 HOH 8   308 367 HOH HOH A . 
I 3 HOH 9   309 207 HOH HOH A . 
I 3 HOH 10  310 386 HOH HOH A . 
I 3 HOH 11  311 12  HOH HOH A . 
I 3 HOH 12  312 73  HOH HOH A . 
I 3 HOH 13  313 193 HOH HOH A . 
I 3 HOH 14  314 196 HOH HOH A . 
I 3 HOH 15  315 273 HOH HOH A . 
I 3 HOH 16  316 159 HOH HOH A . 
I 3 HOH 17  317 266 HOH HOH A . 
I 3 HOH 18  318 429 HOH HOH A . 
I 3 HOH 19  319 69  HOH HOH A . 
I 3 HOH 20  320 456 HOH HOH A . 
I 3 HOH 21  321 322 HOH HOH A . 
I 3 HOH 22  322 56  HOH HOH A . 
I 3 HOH 23  323 480 HOH HOH A . 
I 3 HOH 24  324 102 HOH HOH A . 
I 3 HOH 25  325 238 HOH HOH A . 
I 3 HOH 26  326 360 HOH HOH A . 
I 3 HOH 27  327 46  HOH HOH A . 
I 3 HOH 28  328 58  HOH HOH A . 
I 3 HOH 29  329 264 HOH HOH A . 
I 3 HOH 30  330 365 HOH HOH A . 
I 3 HOH 31  331 38  HOH HOH A . 
I 3 HOH 32  332 17  HOH HOH A . 
I 3 HOH 33  333 424 HOH HOH A . 
I 3 HOH 34  334 4   HOH HOH A . 
I 3 HOH 35  335 210 HOH HOH A . 
I 3 HOH 36  336 433 HOH HOH A . 
I 3 HOH 37  337 155 HOH HOH A . 
I 3 HOH 38  338 169 HOH HOH A . 
I 3 HOH 39  339 133 HOH HOH A . 
I 3 HOH 40  340 119 HOH HOH A . 
I 3 HOH 41  341 57  HOH HOH A . 
I 3 HOH 42  342 151 HOH HOH A . 
I 3 HOH 43  343 62  HOH HOH A . 
I 3 HOH 44  344 132 HOH HOH A . 
I 3 HOH 45  345 153 HOH HOH A . 
I 3 HOH 46  346 85  HOH HOH A . 
I 3 HOH 47  347 80  HOH HOH A . 
I 3 HOH 48  348 275 HOH HOH A . 
I 3 HOH 49  349 83  HOH HOH A . 
I 3 HOH 50  350 128 HOH HOH A . 
I 3 HOH 51  351 233 HOH HOH A . 
I 3 HOH 52  352 338 HOH HOH A . 
I 3 HOH 53  353 240 HOH HOH A . 
I 3 HOH 54  354 350 HOH HOH A . 
I 3 HOH 55  355 287 HOH HOH A . 
I 3 HOH 56  356 166 HOH HOH A . 
I 3 HOH 57  357 34  HOH HOH A . 
I 3 HOH 58  358 74  HOH HOH A . 
I 3 HOH 59  359 19  HOH HOH A . 
I 3 HOH 60  360 189 HOH HOH A . 
I 3 HOH 61  361 45  HOH HOH A . 
I 3 HOH 62  362 198 HOH HOH A . 
I 3 HOH 63  363 8   HOH HOH A . 
I 3 HOH 64  364 5   HOH HOH A . 
I 3 HOH 65  365 66  HOH HOH A . 
I 3 HOH 66  366 293 HOH HOH A . 
I 3 HOH 67  367 300 HOH HOH A . 
I 3 HOH 68  368 164 HOH HOH A . 
I 3 HOH 69  369 105 HOH HOH A . 
I 3 HOH 70  370 242 HOH HOH A . 
I 3 HOH 71  371 337 HOH HOH A . 
I 3 HOH 72  372 468 HOH HOH A . 
I 3 HOH 73  373 176 HOH HOH A . 
I 3 HOH 74  374 343 HOH HOH A . 
I 3 HOH 75  375 445 HOH HOH A . 
I 3 HOH 76  376 336 HOH HOH A . 
I 3 HOH 77  377 362 HOH HOH A . 
I 3 HOH 78  378 127 HOH HOH A . 
I 3 HOH 79  379 171 HOH HOH A . 
I 3 HOH 80  380 190 HOH HOH A . 
I 3 HOH 81  381 235 HOH HOH A . 
I 3 HOH 82  382 341 HOH HOH A . 
I 3 HOH 83  383 13  HOH HOH A . 
I 3 HOH 84  384 33  HOH HOH A . 
I 3 HOH 85  385 11  HOH HOH A . 
I 3 HOH 86  386 377 HOH HOH A . 
I 3 HOH 87  387 122 HOH HOH A . 
I 3 HOH 88  388 199 HOH HOH A . 
I 3 HOH 89  389 451 HOH HOH A . 
I 3 HOH 90  390 40  HOH HOH A . 
I 3 HOH 91  391 255 HOH HOH A . 
I 3 HOH 92  392 470 HOH HOH A . 
I 3 HOH 93  393 298 HOH HOH A . 
I 3 HOH 94  394 137 HOH HOH A . 
I 3 HOH 95  395 29  HOH HOH A . 
I 3 HOH 96  396 431 HOH HOH A . 
I 3 HOH 97  397 103 HOH HOH A . 
I 3 HOH 98  398 154 HOH HOH A . 
I 3 HOH 99  399 435 HOH HOH A . 
I 3 HOH 100 400 250 HOH HOH A . 
I 3 HOH 101 401 41  HOH HOH A . 
I 3 HOH 102 402 359 HOH HOH A . 
I 3 HOH 103 403 444 HOH HOH A . 
I 3 HOH 104 404 476 HOH HOH A . 
I 3 HOH 105 405 308 HOH HOH A . 
I 3 HOH 106 406 447 HOH HOH A . 
I 3 HOH 107 407 463 HOH HOH A . 
I 3 HOH 108 408 349 HOH HOH A . 
I 3 HOH 109 409 179 HOH HOH A . 
I 3 HOH 110 410 94  HOH HOH A . 
I 3 HOH 111 411 311 HOH HOH A . 
I 3 HOH 112 412 234 HOH HOH A . 
I 3 HOH 113 413 306 HOH HOH A . 
I 3 HOH 114 414 156 HOH HOH A . 
I 3 HOH 115 415 113 HOH HOH A . 
I 3 HOH 116 416 454 HOH HOH A . 
I 3 HOH 117 417 104 HOH HOH A . 
I 3 HOH 118 418 277 HOH HOH A . 
I 3 HOH 119 419 200 HOH HOH A . 
I 3 HOH 120 420 449 HOH HOH A . 
I 3 HOH 121 421 369 HOH HOH A . 
I 3 HOH 122 422 373 HOH HOH A . 
I 3 HOH 123 423 321 HOH HOH A . 
I 3 HOH 124 424 382 HOH HOH A . 
I 3 HOH 125 425 458 HOH HOH A . 
I 3 HOH 126 426 452 HOH HOH A . 
I 3 HOH 127 427 175 HOH HOH A . 
I 3 HOH 128 428 432 HOH HOH A . 
I 3 HOH 129 429 284 HOH HOH A . 
I 3 HOH 130 430 214 HOH HOH A . 
I 3 HOH 131 431 314 HOH HOH A . 
I 3 HOH 132 432 374 HOH HOH A . 
I 3 HOH 133 433 467 HOH HOH A . 
I 3 HOH 134 434 227 HOH HOH A . 
I 3 HOH 135 435 460 HOH HOH A . 
I 3 HOH 136 436 400 HOH HOH A . 
I 3 HOH 137 437 201 HOH HOH A . 
I 3 HOH 138 438 378 HOH HOH A . 
I 3 HOH 139 439 180 HOH HOH A . 
I 3 HOH 140 440 239 HOH HOH A . 
I 3 HOH 141 441 184 HOH HOH A . 
I 3 HOH 142 442 352 HOH HOH A . 
I 3 HOH 143 443 330 HOH HOH A . 
I 3 HOH 144 444 478 HOH HOH A . 
I 3 HOH 145 445 304 HOH HOH A . 
I 3 HOH 146 446 425 HOH HOH A . 
I 3 HOH 147 447 465 HOH HOH A . 
I 3 HOH 148 448 187 HOH HOH A . 
I 3 HOH 149 449 262 HOH HOH A . 
I 3 HOH 150 450 462 HOH HOH A . 
I 3 HOH 151 451 101 HOH HOH A . 
I 3 HOH 152 452 439 HOH HOH A . 
I 3 HOH 153 453 443 HOH HOH A . 
I 3 HOH 154 454 437 HOH HOH A . 
I 3 HOH 155 455 397 HOH HOH A . 
I 3 HOH 156 456 229 HOH HOH A . 
I 3 HOH 157 457 475 HOH HOH A . 
I 3 HOH 158 458 249 HOH HOH A . 
I 3 HOH 159 459 488 HOH HOH A . 
I 3 HOH 160 460 182 HOH HOH A . 
I 3 HOH 161 461 486 HOH HOH A . 
I 3 HOH 162 462 268 HOH HOH A . 
I 3 HOH 163 463 120 HOH HOH A . 
I 3 HOH 164 464 297 HOH HOH A . 
I 3 HOH 165 465 388 HOH HOH A . 
J 3 HOH 1   301 123 HOH HOH B . 
J 3 HOH 2   302 389 HOH HOH B . 
J 3 HOH 3   303 282 HOH HOH B . 
J 3 HOH 4   304 342 HOH HOH B . 
J 3 HOH 5   305 385 HOH HOH B . 
J 3 HOH 6   306 168 HOH HOH B . 
J 3 HOH 7   307 15  HOH HOH B . 
J 3 HOH 8   308 43  HOH HOH B . 
J 3 HOH 9   309 63  HOH HOH B . 
J 3 HOH 10  310 109 HOH HOH B . 
J 3 HOH 11  311 219 HOH HOH B . 
J 3 HOH 12  312 47  HOH HOH B . 
J 3 HOH 13  313 114 HOH HOH B . 
J 3 HOH 14  314 136 HOH HOH B . 
J 3 HOH 15  315 395 HOH HOH B . 
J 3 HOH 16  316 61  HOH HOH B . 
J 3 HOH 17  317 118 HOH HOH B . 
J 3 HOH 18  318 79  HOH HOH B . 
J 3 HOH 19  319 329 HOH HOH B . 
J 3 HOH 20  320 286 HOH HOH B . 
J 3 HOH 21  321 345 HOH HOH B . 
J 3 HOH 22  322 223 HOH HOH B . 
J 3 HOH 23  323 319 HOH HOH B . 
J 3 HOH 24  324 6   HOH HOH B . 
J 3 HOH 25  325 89  HOH HOH B . 
J 3 HOH 26  326 108 HOH HOH B . 
J 3 HOH 27  327 143 HOH HOH B . 
J 3 HOH 28  328 279 HOH HOH B . 
J 3 HOH 29  329 357 HOH HOH B . 
J 3 HOH 30  330 355 HOH HOH B . 
J 3 HOH 31  331 161 HOH HOH B . 
J 3 HOH 32  332 192 HOH HOH B . 
J 3 HOH 33  333 25  HOH HOH B . 
J 3 HOH 34  334 332 HOH HOH B . 
J 3 HOH 35  335 473 HOH HOH B . 
J 3 HOH 36  336 16  HOH HOH B . 
J 3 HOH 37  337 76  HOH HOH B . 
J 3 HOH 38  338 9   HOH HOH B . 
J 3 HOH 39  339 7   HOH HOH B . 
J 3 HOH 40  340 39  HOH HOH B . 
J 3 HOH 41  341 44  HOH HOH B . 
J 3 HOH 42  342 493 HOH HOH B . 
J 3 HOH 43  343 174 HOH HOH B . 
J 3 HOH 44  344 464 HOH HOH B . 
J 3 HOH 45  345 52  HOH HOH B . 
J 3 HOH 46  346 295 HOH HOH B . 
J 3 HOH 47  347 353 HOH HOH B . 
J 3 HOH 48  348 347 HOH HOH B . 
J 3 HOH 49  349 20  HOH HOH B . 
J 3 HOH 50  350 88  HOH HOH B . 
J 3 HOH 51  351 356 HOH HOH B . 
J 3 HOH 52  352 2   HOH HOH B . 
J 3 HOH 53  353 138 HOH HOH B . 
J 3 HOH 54  354 218 HOH HOH B . 
J 3 HOH 55  355 32  HOH HOH B . 
J 3 HOH 56  356 93  HOH HOH B . 
J 3 HOH 57  357 283 HOH HOH B . 
J 3 HOH 58  358 165 HOH HOH B . 
J 3 HOH 59  359 248 HOH HOH B . 
J 3 HOH 60  360 71  HOH HOH B . 
J 3 HOH 61  361 197 HOH HOH B . 
J 3 HOH 62  362 173 HOH HOH B . 
J 3 HOH 63  363 60  HOH HOH B . 
J 3 HOH 64  364 188 HOH HOH B . 
J 3 HOH 65  365 177 HOH HOH B . 
J 3 HOH 66  366 483 HOH HOH B . 
J 3 HOH 67  367 142 HOH HOH B . 
J 3 HOH 68  368 340 HOH HOH B . 
J 3 HOH 69  369 150 HOH HOH B . 
J 3 HOH 70  370 126 HOH HOH B . 
J 3 HOH 71  371 328 HOH HOH B . 
J 3 HOH 72  372 181 HOH HOH B . 
J 3 HOH 73  373 317 HOH HOH B . 
J 3 HOH 74  374 152 HOH HOH B . 
J 3 HOH 75  375 420 HOH HOH B . 
J 3 HOH 76  376 140 HOH HOH B . 
J 3 HOH 77  377 72  HOH HOH B . 
J 3 HOH 78  378 221 HOH HOH B . 
J 3 HOH 79  379 299 HOH HOH B . 
J 3 HOH 80  380 23  HOH HOH B . 
J 3 HOH 81  381 48  HOH HOH B . 
J 3 HOH 82  382 461 HOH HOH B . 
J 3 HOH 83  383 78  HOH HOH B . 
J 3 HOH 84  384 28  HOH HOH B . 
J 3 HOH 85  385 237 HOH HOH B . 
J 3 HOH 86  386 265 HOH HOH B . 
J 3 HOH 87  387 402 HOH HOH B . 
J 3 HOH 88  388 241 HOH HOH B . 
J 3 HOH 89  389 477 HOH HOH B . 
J 3 HOH 90  390 203 HOH HOH B . 
J 3 HOH 91  391 98  HOH HOH B . 
J 3 HOH 92  392 217 HOH HOH B . 
J 3 HOH 93  393 426 HOH HOH B . 
J 3 HOH 94  394 86  HOH HOH B . 
J 3 HOH 95  395 281 HOH HOH B . 
J 3 HOH 96  396 490 HOH HOH B . 
J 3 HOH 97  397 225 HOH HOH B . 
J 3 HOH 98  398 499 HOH HOH B . 
J 3 HOH 99  399 291 HOH HOH B . 
J 3 HOH 100 400 170 HOH HOH B . 
J 3 HOH 101 401 414 HOH HOH B . 
J 3 HOH 102 402 296 HOH HOH B . 
J 3 HOH 103 403 364 HOH HOH B . 
J 3 HOH 104 404 208 HOH HOH B . 
J 3 HOH 105 405 206 HOH HOH B . 
J 3 HOH 106 406 112 HOH HOH B . 
J 3 HOH 107 407 440 HOH HOH B . 
J 3 HOH 108 408 495 HOH HOH B . 
J 3 HOH 109 409 339 HOH HOH B . 
J 3 HOH 110 410 346 HOH HOH B . 
J 3 HOH 111 411 185 HOH HOH B . 
J 3 HOH 112 412 408 HOH HOH B . 
J 3 HOH 113 413 204 HOH HOH B . 
J 3 HOH 114 414 417 HOH HOH B . 
J 3 HOH 115 415 271 HOH HOH B . 
J 3 HOH 116 416 421 HOH HOH B . 
J 3 HOH 117 417 167 HOH HOH B . 
J 3 HOH 118 418 68  HOH HOH B . 
J 3 HOH 119 419 162 HOH HOH B . 
J 3 HOH 120 420 267 HOH HOH B . 
J 3 HOH 121 421 384 HOH HOH B . 
J 3 HOH 122 422 100 HOH HOH B . 
J 3 HOH 123 423 419 HOH HOH B . 
J 3 HOH 124 424 484 HOH HOH B . 
J 3 HOH 125 425 471 HOH HOH B . 
J 3 HOH 126 426 459 HOH HOH B . 
K 3 HOH 1   301 134 HOH HOH C . 
K 3 HOH 2   302 370 HOH HOH C . 
K 3 HOH 3   303 251 HOH HOH C . 
K 3 HOH 4   304 215 HOH HOH C . 
K 3 HOH 5   305 131 HOH HOH C . 
K 3 HOH 6   306 313 HOH HOH C . 
K 3 HOH 7   307 30  HOH HOH C . 
K 3 HOH 8   308 436 HOH HOH C . 
K 3 HOH 9   309 247 HOH HOH C . 
K 3 HOH 10  310 14  HOH HOH C . 
K 3 HOH 11  311 278 HOH HOH C . 
K 3 HOH 12  312 361 HOH HOH C . 
K 3 HOH 13  313 245 HOH HOH C . 
K 3 HOH 14  314 466 HOH HOH C . 
K 3 HOH 15  315 149 HOH HOH C . 
K 3 HOH 16  316 301 HOH HOH C . 
K 3 HOH 17  317 481 HOH HOH C . 
K 3 HOH 18  318 53  HOH HOH C . 
K 3 HOH 19  319 246 HOH HOH C . 
K 3 HOH 20  320 157 HOH HOH C . 
K 3 HOH 21  321 178 HOH HOH C . 
K 3 HOH 22  322 84  HOH HOH C . 
K 3 HOH 23  323 97  HOH HOH C . 
K 3 HOH 24  324 274 HOH HOH C . 
K 3 HOH 25  325 91  HOH HOH C . 
K 3 HOH 26  326 405 HOH HOH C . 
K 3 HOH 27  327 81  HOH HOH C . 
K 3 HOH 28  328 194 HOH HOH C . 
K 3 HOH 29  329 244 HOH HOH C . 
K 3 HOH 30  330 50  HOH HOH C . 
K 3 HOH 31  331 392 HOH HOH C . 
K 3 HOH 32  332 10  HOH HOH C . 
K 3 HOH 33  333 315 HOH HOH C . 
K 3 HOH 34  334 141 HOH HOH C . 
K 3 HOH 35  335 59  HOH HOH C . 
K 3 HOH 36  336 213 HOH HOH C . 
K 3 HOH 37  337 253 HOH HOH C . 
K 3 HOH 38  338 316 HOH HOH C . 
K 3 HOH 39  339 31  HOH HOH C . 
K 3 HOH 40  340 450 HOH HOH C . 
K 3 HOH 41  341 95  HOH HOH C . 
K 3 HOH 42  342 110 HOH HOH C . 
K 3 HOH 43  343 1   HOH HOH C . 
K 3 HOH 44  344 396 HOH HOH C . 
K 3 HOH 45  345 121 HOH HOH C . 
K 3 HOH 46  346 430 HOH HOH C . 
K 3 HOH 47  347 290 HOH HOH C . 
K 3 HOH 48  348 3   HOH HOH C . 
K 3 HOH 49  349 82  HOH HOH C . 
K 3 HOH 50  350 422 HOH HOH C . 
K 3 HOH 51  351 36  HOH HOH C . 
K 3 HOH 52  352 252 HOH HOH C . 
K 3 HOH 53  353 391 HOH HOH C . 
K 3 HOH 54  354 67  HOH HOH C . 
K 3 HOH 55  355 211 HOH HOH C . 
K 3 HOH 56  356 307 HOH HOH C . 
K 3 HOH 57  357 65  HOH HOH C . 
K 3 HOH 58  358 446 HOH HOH C . 
K 3 HOH 59  359 144 HOH HOH C . 
K 3 HOH 60  360 302 HOH HOH C . 
K 3 HOH 61  361 236 HOH HOH C . 
K 3 HOH 62  362 96  HOH HOH C . 
K 3 HOH 63  363 292 HOH HOH C . 
K 3 HOH 64  364 438 HOH HOH C . 
K 3 HOH 65  365 90  HOH HOH C . 
K 3 HOH 66  366 399 HOH HOH C . 
K 3 HOH 67  367 49  HOH HOH C . 
K 3 HOH 68  368 135 HOH HOH C . 
K 3 HOH 69  369 54  HOH HOH C . 
K 3 HOH 70  370 35  HOH HOH C . 
K 3 HOH 71  371 55  HOH HOH C . 
K 3 HOH 72  372 288 HOH HOH C . 
K 3 HOH 73  373 163 HOH HOH C . 
K 3 HOH 74  374 261 HOH HOH C . 
K 3 HOH 75  375 24  HOH HOH C . 
K 3 HOH 76  376 280 HOH HOH C . 
K 3 HOH 77  377 70  HOH HOH C . 
K 3 HOH 78  378 276 HOH HOH C . 
K 3 HOH 79  379 270 HOH HOH C . 
K 3 HOH 80  380 407 HOH HOH C . 
K 3 HOH 81  381 496 HOH HOH C . 
K 3 HOH 82  382 383 HOH HOH C . 
K 3 HOH 83  383 413 HOH HOH C . 
K 3 HOH 84  384 380 HOH HOH C . 
K 3 HOH 85  385 160 HOH HOH C . 
K 3 HOH 86  386 372 HOH HOH C . 
K 3 HOH 87  387 381 HOH HOH C . 
K 3 HOH 88  388 325 HOH HOH C . 
K 3 HOH 89  389 375 HOH HOH C . 
K 3 HOH 90  390 474 HOH HOH C . 
K 3 HOH 91  391 376 HOH HOH C . 
K 3 HOH 92  392 441 HOH HOH C . 
K 3 HOH 93  393 331 HOH HOH C . 
K 3 HOH 94  394 401 HOH HOH C . 
K 3 HOH 95  395 492 HOH HOH C . 
K 3 HOH 96  396 410 HOH HOH C . 
K 3 HOH 97  397 363 HOH HOH C . 
K 3 HOH 98  398 106 HOH HOH C . 
K 3 HOH 99  399 442 HOH HOH C . 
K 3 HOH 100 400 212 HOH HOH C . 
K 3 HOH 101 401 418 HOH HOH C . 
K 3 HOH 102 402 230 HOH HOH C . 
K 3 HOH 103 403 259 HOH HOH C . 
K 3 HOH 104 404 318 HOH HOH C . 
K 3 HOH 105 405 494 HOH HOH C . 
K 3 HOH 106 406 243 HOH HOH C . 
K 3 HOH 107 407 409 HOH HOH C . 
K 3 HOH 108 408 335 HOH HOH C . 
K 3 HOH 109 409 487 HOH HOH C . 
K 3 HOH 110 410 42  HOH HOH C . 
K 3 HOH 111 411 379 HOH HOH C . 
K 3 HOH 112 412 406 HOH HOH C . 
K 3 HOH 113 413 202 HOH HOH C . 
K 3 HOH 114 414 416 HOH HOH C . 
K 3 HOH 115 415 457 HOH HOH C . 
K 3 HOH 116 416 398 HOH HOH C . 
K 3 HOH 117 417 403 HOH HOH C . 
K 3 HOH 118 418 497 HOH HOH C . 
L 3 HOH 1   301 231 HOH HOH D . 
L 3 HOH 2   302 228 HOH HOH D . 
L 3 HOH 3   303 222 HOH HOH D . 
L 3 HOH 4   304 320 HOH HOH D . 
L 3 HOH 5   305 183 HOH HOH D . 
L 3 HOH 6   306 146 HOH HOH D . 
L 3 HOH 7   307 415 HOH HOH D . 
L 3 HOH 8   308 344 HOH HOH D . 
L 3 HOH 9   309 158 HOH HOH D . 
L 3 HOH 10  310 115 HOH HOH D . 
L 3 HOH 11  311 129 HOH HOH D . 
L 3 HOH 12  312 269 HOH HOH D . 
L 3 HOH 13  313 285 HOH HOH D . 
L 3 HOH 14  314 145 HOH HOH D . 
L 3 HOH 15  315 434 HOH HOH D . 
L 3 HOH 16  316 27  HOH HOH D . 
L 3 HOH 17  317 75  HOH HOH D . 
L 3 HOH 18  318 368 HOH HOH D . 
L 3 HOH 19  319 87  HOH HOH D . 
L 3 HOH 20  320 116 HOH HOH D . 
L 3 HOH 21  321 427 HOH HOH D . 
L 3 HOH 22  322 394 HOH HOH D . 
L 3 HOH 23  323 205 HOH HOH D . 
L 3 HOH 24  324 371 HOH HOH D . 
L 3 HOH 25  325 289 HOH HOH D . 
L 3 HOH 26  326 51  HOH HOH D . 
L 3 HOH 27  327 148 HOH HOH D . 
L 3 HOH 28  328 186 HOH HOH D . 
L 3 HOH 29  329 172 HOH HOH D . 
L 3 HOH 30  330 117 HOH HOH D . 
L 3 HOH 31  331 21  HOH HOH D . 
L 3 HOH 32  332 254 HOH HOH D . 
L 3 HOH 33  333 312 HOH HOH D . 
L 3 HOH 34  334 216 HOH HOH D . 
L 3 HOH 35  335 64  HOH HOH D . 
L 3 HOH 36  336 323 HOH HOH D . 
L 3 HOH 37  337 272 HOH HOH D . 
L 3 HOH 38  338 195 HOH HOH D . 
L 3 HOH 39  339 220 HOH HOH D . 
L 3 HOH 40  340 209 HOH HOH D . 
L 3 HOH 41  341 455 HOH HOH D . 
L 3 HOH 42  342 22  HOH HOH D . 
L 3 HOH 43  343 130 HOH HOH D . 
L 3 HOH 44  344 99  HOH HOH D . 
L 3 HOH 45  345 263 HOH HOH D . 
L 3 HOH 46  346 453 HOH HOH D . 
L 3 HOH 47  347 354 HOH HOH D . 
L 3 HOH 48  348 366 HOH HOH D . 
L 3 HOH 49  349 491 HOH HOH D . 
L 3 HOH 50  350 324 HOH HOH D . 
L 3 HOH 51  351 124 HOH HOH D . 
L 3 HOH 52  352 393 HOH HOH D . 
L 3 HOH 53  353 305 HOH HOH D . 
L 3 HOH 54  354 191 HOH HOH D . 
L 3 HOH 55  355 139 HOH HOH D . 
L 3 HOH 56  356 485 HOH HOH D . 
L 3 HOH 57  357 498 HOH HOH D . 
L 3 HOH 58  358 334 HOH HOH D . 
L 3 HOH 59  359 327 HOH HOH D . 
L 3 HOH 60  360 303 HOH HOH D . 
L 3 HOH 61  361 232 HOH HOH D . 
L 3 HOH 62  362 428 HOH HOH D . 
L 3 HOH 63  363 326 HOH HOH D . 
L 3 HOH 64  364 256 HOH HOH D . 
L 3 HOH 65  365 258 HOH HOH D . 
L 3 HOH 66  366 224 HOH HOH D . 
L 3 HOH 67  367 37  HOH HOH D . 
L 3 HOH 68  368 333 HOH HOH D . 
L 3 HOH 69  369 310 HOH HOH D . 
L 3 HOH 70  370 125 HOH HOH D . 
L 3 HOH 71  371 294 HOH HOH D . 
L 3 HOH 72  372 390 HOH HOH D . 
L 3 HOH 73  373 348 HOH HOH D . 
L 3 HOH 74  374 448 HOH HOH D . 
L 3 HOH 75  375 92  HOH HOH D . 
L 3 HOH 76  376 111 HOH HOH D . 
L 3 HOH 77  377 412 HOH HOH D . 
L 3 HOH 78  378 423 HOH HOH D . 
L 3 HOH 79  379 309 HOH HOH D . 
L 3 HOH 80  380 226 HOH HOH D . 
L 3 HOH 81  381 482 HOH HOH D . 
L 3 HOH 82  382 107 HOH HOH D . 
L 3 HOH 83  383 479 HOH HOH D . 
L 3 HOH 84  384 472 HOH HOH D . 
L 3 HOH 85  385 469 HOH HOH D . 
L 3 HOH 86  386 358 HOH HOH D . 
L 3 HOH 87  387 404 HOH HOH D . 
L 3 HOH 88  388 260 HOH HOH D . 
L 3 HOH 89  389 489 HOH HOH D . 
L 3 HOH 90  390 351 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B ARG 177 ? CG  ? B ARG 154 CG  
2  1 Y 1 B ARG 177 ? CD  ? B ARG 154 CD  
3  1 Y 1 B ARG 177 ? NE  ? B ARG 154 NE  
4  1 Y 1 B ARG 177 ? CZ  ? B ARG 154 CZ  
5  1 Y 1 B ARG 177 ? NH1 ? B ARG 154 NH1 
6  1 Y 1 B ARG 177 ? NH2 ? B ARG 154 NH2 
7  1 Y 1 C ARG 184 ? CG  ? C ARG 161 CG  
8  1 Y 1 C ARG 184 ? CD  ? C ARG 161 CD  
9  1 Y 1 C ARG 184 ? NE  ? C ARG 161 NE  
10 1 Y 1 C ARG 184 ? CZ  ? C ARG 161 CZ  
11 1 Y 1 C ARG 184 ? NH1 ? C ARG 161 NH1 
12 1 Y 1 C ARG 184 ? NH2 ? C ARG 161 NH2 
13 1 Y 1 D GLU 116 ? CG  ? D GLU 93  CG  
14 1 Y 1 D GLU 116 ? CD  ? D GLU 93  CD  
15 1 Y 1 D GLU 116 ? OE1 ? D GLU 93  OE1 
16 1 Y 1 D GLU 116 ? OE2 ? D GLU 93  OE2 
17 1 Y 1 D LYS 118 ? CG  ? D LYS 95  CG  
18 1 Y 1 D LYS 118 ? CD  ? D LYS 95  CD  
19 1 Y 1 D LYS 118 ? CE  ? D LYS 95  CE  
20 1 Y 1 D LYS 118 ? NZ  ? D LYS 95  NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.14_3260)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .             2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .             3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .             4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.56 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KO5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.611 
_cell.length_a_esd                 ? 
_cell.length_b                     76.394 
_cell.length_b_esd                 ? 
_cell.length_c                     87.227 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KO5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KO5 
_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             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.07 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M lithium sulfate, 0.1M Tris-HCl pH 8.0, 25% polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 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         2021-07-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KO5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               50 
_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                                     64020 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.358 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.984 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.322 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.04 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8449 
_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                               2.275 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.409 
_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                                  2.055 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KO5 
_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                            2.04 
_refine.ls_d_res_low                             46.7 
_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                     55903 
_refine.ls_number_reflns_R_free                  2733 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.46 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1722 
_refine.ls_R_factor_R_free                       0.2091 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1703 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.77 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5145 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.number_atoms_solvent             499 
_refine_hist.number_atoms_total               5724 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        46.7 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 5375 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.828 ? 7347 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.337 ? 3192 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 846  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 932  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.0402 2.0754  . . 142 2555 96.00  . . . . 0.2689 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 2.0754 2.1131  . . 132 2653 99.00  . . . . 0.2486 . . . . . . . . . . . 0.2989 
'X-RAY DIFFRACTION' 2.1131 2.1538  . . 128 2614 99.00  . . . . 0.2257 . . . . . . . . . . . 0.2538 
'X-RAY DIFFRACTION' 2.1538 2.1978  . . 135 2643 99.00  . . . . 0.2178 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 2.1978 2.2455  . . 130 2652 99.00  . . . . 0.2130 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 2.2455 2.2978  . . 141 2645 100.00 . . . . 0.2128 . . . . . . . . . . . 0.2812 
'X-RAY DIFFRACTION' 2.2978 2.3552  . . 142 2637 99.00  . . . . 0.1839 . . . . . . . . . . . 0.2172 
'X-RAY DIFFRACTION' 2.3552 2.4189  . . 137 2635 99.00  . . . . 0.1828 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 2.4189 2.4901  . . 124 2653 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 2.4901 2.5705  . . 155 2655 100.00 . . . . 0.1837 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 2.5705 2.6623  . . 117 2674 100.00 . . . . 0.1807 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 2.6623 2.7689  . . 133 2639 100.00 . . . . 0.1845 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 2.7689 2.8949  . . 143 2675 100.00 . . . . 0.1810 . . . . . . . . . . . 0.2157 
'X-RAY DIFFRACTION' 2.8949 3.0475  . . 138 2677 100.00 . . . . 0.1818 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 3.0475 3.2384  . . 129 2674 100.00 . . . . 0.1833 . . . . . . . . . . . 0.2275 
'X-RAY DIFFRACTION' 3.2384 3.4884  . . 128 2686 100.00 . . . . 0.1705 . . . . . . . . . . . 0.2378 
'X-RAY DIFFRACTION' 3.4884 3.8393  . . 144 2682 100.00 . . . . 0.1510 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 3.8393 4.3944  . . 125 2693 100.00 . . . . 0.1339 . . . . . . . . . . . 0.1384 
'X-RAY DIFFRACTION' 4.3944 5.5351  . . 144 2694 100.00 . . . . 0.1293 . . . . . . . . . . . 0.1730 
'X-RAY DIFFRACTION' 5.5351 46.6760 . . 166 2734 100.00 . . . . 0.1516 . . . . . . . . . . . 0.1783 
# 
_struct.entry_id                     9KO5 
_struct.title                        
;Crystal structure of Agrobacterium tumefaciens PmtA with 5'-methylthioadenosine
;
_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        9KO5 
_struct_keywords.text            'Phospholipid N-mehyltransferase, Phosphatidylcholine, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A9CKE9_AGRFC 
_struct_ref.pdbx_db_accession          A9CKE9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QPKKVGAIVPTSSITAKKMASVINPHSGLPVLELGPGTGVITKAILARGIKPESLTAIEYSTDFYNQLLRSYPGVNFVNG
DAFDLDATLGEHKGQMFDSVISAVPMLNFPMAARIKLLDELLKRVPHGRPVVQISYGPISPIVAQPHLYHIRHFDFIVRN
IPPAQLWTYTRA
;
_struct_ref.pdbx_align_begin           26 
# 
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 9KO5 A 3 ? 174 ? A9CKE9 26 ? 197 ? 26 197 
2 1 9KO5 B 3 ? 174 ? A9CKE9 26 ? 197 ? 26 197 
3 1 9KO5 C 3 ? 174 ? A9CKE9 26 ? 197 ? 26 197 
4 1 9KO5 D 3 ? 174 ? A9CKE9 26 ? 197 ? 26 197 
# 
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 9KO5 GLY A 1 ? UNP A9CKE9 ? ? 'expression tag' 24 1 
1 9KO5 PRO A 2 ? UNP A9CKE9 ? ? 'expression tag' 25 2 
2 9KO5 GLY B 1 ? UNP A9CKE9 ? ? 'expression tag' 24 3 
2 9KO5 PRO B 2 ? UNP A9CKE9 ? ? 'expression tag' 25 4 
3 9KO5 GLY C 1 ? UNP A9CKE9 ? ? 'expression tag' 24 5 
3 9KO5 PRO C 2 ? UNP A9CKE9 ? ? 'expression tag' 25 6 
4 9KO5 GLY D 1 ? UNP A9CKE9 ? ? 'expression tag' 24 7 
4 9KO5 PRO D 2 ? UNP A9CKE9 ? ? 'expression tag' 25 8 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,I 
2 1 B,F,J 
3 1 C,G,K 
4 1 D,H,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 14  ? SER A 23  ? SER A 37  SER A 46  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 41  ? ARG A 50  ? GLY A 64  ARG A 73  1 ? 10 
HELX_P HELX_P3  AA3 LYS A 53  ? GLU A 55  ? LYS A 76  GLU A 78  5 ? 3  
HELX_P HELX_P4  AA4 SER A 63  ? TYR A 74  ? SER A 86  TYR A 97  1 ? 12 
HELX_P HELX_P5  AA5 ASP A 86  ? GLY A 92  ? ASP A 109 GLY A 115 1 ? 7  
HELX_P HELX_P6  AA6 PRO A 107 ? PHE A 111 ? PRO A 130 PHE A 134 5 ? 5  
HELX_P HELX_P7  AA7 PRO A 112 ? LEU A 124 ? PRO A 135 LEU A 147 1 ? 13 
HELX_P HELX_P8  AA8 LYS A 125 ? VAL A 127 ? LYS A 148 VAL A 150 5 ? 3  
HELX_P HELX_P9  AA9 SER B 14  ? SER B 23  ? SER B 37  SER B 46  1 ? 10 
HELX_P HELX_P10 AB1 GLY B 41  ? ALA B 49  ? GLY B 64  ALA B 72  1 ? 9  
HELX_P HELX_P11 AB2 LYS B 53  ? GLU B 55  ? LYS B 76  GLU B 78  5 ? 3  
HELX_P HELX_P12 AB3 SER B 63  ? TYR B 74  ? SER B 86  TYR B 97  1 ? 12 
HELX_P HELX_P13 AB4 ASP B 86  ? GLY B 92  ? ASP B 109 GLY B 115 1 ? 7  
HELX_P HELX_P14 AB5 PRO B 107 ? PHE B 111 ? PRO B 130 PHE B 134 5 ? 5  
HELX_P HELX_P15 AB6 PRO B 112 ? ARG B 126 ? PRO B 135 ARG B 149 1 ? 15 
HELX_P HELX_P16 AB7 SER C 14  ? SER C 23  ? SER C 37  SER C 46  1 ? 10 
HELX_P HELX_P17 AB8 GLY C 41  ? ARG C 50  ? GLY C 64  ARG C 73  1 ? 10 
HELX_P HELX_P18 AB9 LYS C 53  ? GLU C 55  ? LYS C 76  GLU C 78  5 ? 3  
HELX_P HELX_P19 AC1 SER C 63  ? TYR C 74  ? SER C 86  TYR C 97  1 ? 12 
HELX_P HELX_P20 AC2 ASP C 86  ? GLY C 92  ? ASP C 109 GLY C 115 1 ? 7  
HELX_P HELX_P21 AC3 PRO C 112 ? LEU C 124 ? PRO C 135 LEU C 147 1 ? 13 
HELX_P HELX_P22 AC4 LYS C 125 ? VAL C 127 ? LYS C 148 VAL C 150 5 ? 3  
HELX_P HELX_P23 AC5 SER D 14  ? SER D 23  ? SER D 37  SER D 46  1 ? 10 
HELX_P HELX_P24 AC6 GLY D 41  ? ALA D 49  ? GLY D 64  ALA D 72  1 ? 9  
HELX_P HELX_P25 AC7 LYS D 53  ? GLU D 55  ? LYS D 76  GLU D 78  5 ? 3  
HELX_P HELX_P26 AC8 SER D 63  ? TYR D 74  ? SER D 86  TYR D 97  1 ? 12 
HELX_P HELX_P27 AC9 ASP D 86  ? GLY D 92  ? ASP D 109 GLY D 115 1 ? 7  
HELX_P HELX_P28 AD1 PRO D 107 ? PHE D 111 ? PRO D 130 PHE D 134 5 ? 5  
HELX_P HELX_P29 AD2 PRO D 112 ? LYS D 125 ? PRO D 135 LYS D 148 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 ILE 163 A . ? ILE 186 A PRO 164 A ? PRO 187 A 1 -7.45 
2 ILE 163 B . ? ILE 186 B PRO 164 B ? PRO 187 B 1 -4.05 
3 ILE 163 C . ? ILE 186 C PRO 164 C ? PRO 187 C 1 -5.91 
4 ILE 163 D . ? ILE 186 D PRO 164 D ? PRO 187 D 1 -4.33 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? 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 ASN A 78  ? ASN A 81  ? ASN A 101 ASN A 104 
AA1 2 LEU A 57  ? GLU A 61  ? LEU A 80  GLU A 84  
AA1 3 VAL A 33  ? LEU A 36  ? VAL A 56  LEU A 59  
AA1 4 VAL A 102 ? SER A 104 ? VAL A 125 SER A 127 
AA1 5 VAL A 133 ? SER A 137 ? VAL A 156 SER A 160 
AA1 6 ALA A 166 ? ARG A 173 ? ALA A 189 ARG A 196 
AA1 7 TYR A 151 ? ILE A 159 ? TYR A 174 ILE A 182 
AA2 1 ASN B 78  ? ASN B 81  ? ASN B 101 ASN B 104 
AA2 2 LEU B 57  ? GLU B 61  ? LEU B 80  GLU B 84  
AA2 3 VAL B 33  ? LEU B 36  ? VAL B 56  LEU B 59  
AA2 4 VAL B 102 ? SER B 104 ? VAL B 125 SER B 127 
AA2 5 VAL B 133 ? SER B 137 ? VAL B 156 SER B 160 
AA2 6 ALA B 166 ? ARG B 173 ? ALA B 189 ARG B 196 
AA2 7 TYR B 151 ? ILE B 159 ? TYR B 174 ILE B 182 
AA3 1 ASN C 78  ? ASN C 81  ? ASN C 101 ASN C 104 
AA3 2 LEU C 57  ? GLU C 61  ? LEU C 80  GLU C 84  
AA3 3 VAL C 33  ? LEU C 36  ? VAL C 56  LEU C 59  
AA3 4 VAL C 102 ? SER C 104 ? VAL C 125 SER C 127 
AA3 5 VAL C 133 ? SER C 137 ? VAL C 156 SER C 160 
AA3 6 ALA C 166 ? ARG C 173 ? ALA C 189 ARG C 196 
AA3 7 TYR C 151 ? ILE C 159 ? TYR C 174 ILE C 182 
AA4 1 ASN D 78  ? ASN D 81  ? ASN D 101 ASN D 104 
AA4 2 LEU D 57  ? GLU D 61  ? LEU D 80  GLU D 84  
AA4 3 VAL D 33  ? LEU D 36  ? VAL D 56  LEU D 59  
AA4 4 VAL D 102 ? SER D 104 ? VAL D 125 SER D 127 
AA4 5 VAL D 133 ? SER D 137 ? VAL D 156 SER D 160 
AA4 6 ALA D 166 ? ARG D 173 ? ALA D 189 ARG D 196 
AA4 7 TYR D 151 ? ILE D 159 ? TYR D 174 ILE D 182 
# 
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 VAL A 80  ? O VAL A 103 N GLU A 61  ? N GLU A 84  
AA1 2 3 O THR A 58  ? O THR A 81  N GLU A 35  ? N GLU A 58  
AA1 3 4 N LEU A 34  ? N LEU A 57  O ILE A 103 ? O ILE A 126 
AA1 4 5 N SER A 104 ? N SER A 127 O VAL A 134 ? O VAL A 157 
AA1 5 6 N SER A 137 ? N SER A 160 O GLN A 167 ? O GLN A 190 
AA1 6 7 O THR A 170 ? O THR A 193 N ARG A 154 ? N ARG A 177 
AA2 1 2 O VAL B 80  ? O VAL B 103 N GLU B 61  ? N GLU B 84  
AA2 2 3 O THR B 58  ? O THR B 81  N GLU B 35  ? N GLU B 58  
AA2 3 4 N LEU B 34  ? N LEU B 57  O ILE B 103 ? O ILE B 126 
AA2 4 5 N SER B 104 ? N SER B 127 O VAL B 134 ? O VAL B 157 
AA2 5 6 N SER B 137 ? N SER B 160 O GLN B 167 ? O GLN B 190 
AA2 6 7 O ALA B 166 ? O ALA B 189 N ILE B 159 ? N ILE B 182 
AA3 1 2 O VAL C 80  ? O VAL C 103 N GLU C 61  ? N GLU C 84  
AA3 2 3 O THR C 58  ? O THR C 81  N GLU C 35  ? N GLU C 58  
AA3 3 4 N LEU C 36  ? N LEU C 59  O ILE C 103 ? O ILE C 126 
AA3 4 5 N SER C 104 ? N SER C 127 O VAL C 134 ? O VAL C 157 
AA3 5 6 N GLN C 135 ? N GLN C 158 O TRP C 169 ? O TRP C 192 
AA3 6 7 O ALA C 166 ? O ALA C 189 N ILE C 159 ? N ILE C 182 
AA4 1 2 O VAL D 80  ? O VAL D 103 N GLU D 61  ? N GLU D 84  
AA4 2 3 O THR D 58  ? O THR D 81  N GLU D 35  ? N GLU D 58  
AA4 3 4 N LEU D 36  ? N LEU D 59  O ILE D 103 ? O ILE D 126 
AA4 4 5 N VAL D 102 ? N VAL D 125 O VAL D 134 ? O VAL D 157 
AA4 5 6 N SER D 137 ? N SER D 160 O GLN D 167 ? O GLN D 190 
AA4 6 7 O ALA D 166 ? O ALA D 189 N ILE D 159 ? N ILE D 182 
# 
_pdbx_entry_details.entry_id                   9KO5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 HOH 374 ? ? O C HOH 383 ? ? 2.12 
2 1 O D HOH 371 ? ? O D HOH 387 ? ? 2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 109 ? ? -113.12 77.97 
2 1 ASP B 109 ? ? -104.24 76.03 
3 1 ARG B 184 ? ? -87.83  37.32 
4 1 ASP C 109 ? ? -113.37 78.45 
5 1 MET C 131 ? ? 75.29   -6.73 
6 1 ASP D 109 ? ? -108.96 73.67 
7 1 HIS D 117 ? ? -68.06  70.52 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   HIS 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    117 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    118 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            145.92 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 24 ? A GLY 1  
2  1 Y 1 B GLY 24 ? B GLY 1  
3  1 Y 1 B PRO 25 ? B PRO 2  
4  1 Y 1 B GLN 26 ? B GLN 3  
5  1 Y 1 B PRO 27 ? B PRO 4  
6  1 Y 1 B LYS 28 ? B LYS 5  
7  1 Y 1 B LYS 29 ? B LYS 6  
8  1 Y 1 B VAL 30 ? B VAL 7  
9  1 Y 1 B GLY 31 ? B GLY 8  
10 1 Y 1 B ALA 32 ? B ALA 9  
11 1 Y 1 B ILE 33 ? B ILE 10 
12 1 Y 1 C GLY 24 ? C GLY 1  
13 1 Y 1 C PRO 25 ? C PRO 2  
14 1 Y 1 C GLN 26 ? C GLN 3  
15 1 Y 1 C PRO 27 ? C PRO 4  
16 1 Y 1 C LYS 28 ? C LYS 5  
17 1 Y 1 C LYS 29 ? C LYS 6  
18 1 Y 1 C VAL 30 ? C VAL 7  
19 1 Y 1 C GLY 31 ? C GLY 8  
20 1 Y 1 C ALA 32 ? C ALA 9  
21 1 Y 1 C ILE 33 ? C ILE 10 
22 1 Y 1 D GLY 24 ? D GLY 1  
23 1 Y 1 D PRO 25 ? D PRO 2  
24 1 Y 1 D GLN 26 ? D GLN 3  
25 1 Y 1 D PRO 27 ? D PRO 4  
26 1 Y 1 D LYS 28 ? D LYS 5  
27 1 Y 1 D LYS 29 ? D LYS 6  
28 1 Y 1 D VAL 30 ? D VAL 7  
29 1 Y 1 D GLY 31 ? D GLY 8  
30 1 Y 1 D ALA 32 ? D ALA 9  
31 1 Y 1 D ILE 33 ? D ILE 10 
# 
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  
GLN N      N N N 74  
GLN CA     C N S 75  
GLN C      C N N 76  
GLN O      O N N 77  
GLN CB     C N N 78  
GLN CG     C N N 79  
GLN CD     C N N 80  
GLN OE1    O N N 81  
GLN NE2    N N N 82  
GLN OXT    O N N 83  
GLN H      H N N 84  
GLN H2     H N N 85  
GLN HA     H N N 86  
GLN HB2    H N N 87  
GLN HB3    H N N 88  
GLN HG2    H N N 89  
GLN HG3    H N N 90  
GLN HE21   H N N 91  
GLN HE22   H N N 92  
GLN HXT    H N N 93  
GLU N      N N N 94  
GLU CA     C N S 95  
GLU C      C N N 96  
GLU O      O N N 97  
GLU CB     C N N 98  
GLU CG     C N N 99  
GLU CD     C N N 100 
GLU OE1    O N N 101 
GLU OE2    O N N 102 
GLU OXT    O N N 103 
GLU H      H N N 104 
GLU H2     H N N 105 
GLU HA     H N N 106 
GLU HB2    H N N 107 
GLU HB3    H N N 108 
GLU HG2    H N N 109 
GLU HG3    H N N 110 
GLU HE2    H N N 111 
GLU HXT    H N N 112 
GLY N      N N N 113 
GLY CA     C N N 114 
GLY C      C N N 115 
GLY O      O N N 116 
GLY OXT    O N N 117 
GLY H      H N N 118 
GLY H2     H N N 119 
GLY HA2    H N N 120 
GLY HA3    H N N 121 
GLY HXT    H N N 122 
HIS N      N N N 123 
HIS CA     C N S 124 
HIS C      C N N 125 
HIS O      O N N 126 
HIS CB     C N N 127 
HIS CG     C Y N 128 
HIS ND1    N Y N 129 
HIS CD2    C Y N 130 
HIS CE1    C Y N 131 
HIS NE2    N Y N 132 
HIS OXT    O N N 133 
HIS H      H N N 134 
HIS H2     H N N 135 
HIS HA     H N N 136 
HIS HB2    H N N 137 
HIS HB3    H N N 138 
HIS HD1    H N N 139 
HIS HD2    H N N 140 
HIS HE1    H N N 141 
HIS HE2    H N N 142 
HIS HXT    H N N 143 
HOH O      O N N 144 
HOH H1     H N N 145 
HOH H2     H N N 146 
ILE N      N N N 147 
ILE CA     C N S 148 
ILE C      C N N 149 
ILE O      O N N 150 
ILE CB     C N S 151 
ILE CG1    C N N 152 
ILE CG2    C N N 153 
ILE CD1    C N N 154 
ILE OXT    O N N 155 
ILE H      H N N 156 
ILE H2     H N N 157 
ILE HA     H N N 158 
ILE HB     H N N 159 
ILE HG12   H N N 160 
ILE HG13   H N N 161 
ILE HG21   H N N 162 
ILE HG22   H N N 163 
ILE HG23   H N N 164 
ILE HD11   H N N 165 
ILE HD12   H N N 166 
ILE HD13   H N N 167 
ILE HXT    H N N 168 
LEU N      N N N 169 
LEU CA     C N S 170 
LEU C      C N N 171 
LEU O      O N N 172 
LEU CB     C N N 173 
LEU CG     C N N 174 
LEU CD1    C N N 175 
LEU CD2    C N N 176 
LEU OXT    O N N 177 
LEU H      H N N 178 
LEU H2     H N N 179 
LEU HA     H N N 180 
LEU HB2    H N N 181 
LEU HB3    H N N 182 
LEU HG     H N N 183 
LEU HD11   H N N 184 
LEU HD12   H N N 185 
LEU HD13   H N N 186 
LEU HD21   H N N 187 
LEU HD22   H N N 188 
LEU HD23   H N N 189 
LEU HXT    H N N 190 
LYS N      N N N 191 
LYS CA     C N S 192 
LYS C      C N N 193 
LYS O      O N N 194 
LYS CB     C N N 195 
LYS CG     C N N 196 
LYS CD     C N N 197 
LYS CE     C N N 198 
LYS NZ     N N N 199 
LYS OXT    O N N 200 
LYS H      H N N 201 
LYS H2     H N N 202 
LYS HA     H N N 203 
LYS HB2    H N N 204 
LYS HB3    H N N 205 
LYS HG2    H N N 206 
LYS HG3    H N N 207 
LYS HD2    H N N 208 
LYS HD3    H N N 209 
LYS HE2    H N N 210 
LYS HE3    H N N 211 
LYS HZ1    H N N 212 
LYS HZ2    H N N 213 
LYS HZ3    H N N 214 
LYS HXT    H N N 215 
MET N      N N N 216 
MET CA     C N S 217 
MET C      C N N 218 
MET O      O N N 219 
MET CB     C N N 220 
MET CG     C N N 221 
MET SD     S N N 222 
MET CE     C N N 223 
MET OXT    O N N 224 
MET H      H N N 225 
MET H2     H N N 226 
MET HA     H N N 227 
MET HB2    H N N 228 
MET HB3    H N N 229 
MET HG2    H N N 230 
MET HG3    H N N 231 
MET HE1    H N N 232 
MET HE2    H N N 233 
MET HE3    H N N 234 
MET HXT    H N N 235 
MTA CS     C N N 236 
MTA "S5'"  S N N 237 
MTA "C5'"  C N N 238 
MTA "C4'"  C N S 239 
MTA "O4'"  O N N 240 
MTA "C2'"  C N R 241 
MTA "O2'"  O N N 242 
MTA "C3'"  C N S 243 
MTA "O3'"  O N N 244 
MTA "C1'"  C N R 245 
MTA N9     N Y N 246 
MTA C8     C Y N 247 
MTA N7     N Y N 248 
MTA C5     C Y N 249 
MTA C6     C Y N 250 
MTA N6     N N N 251 
MTA N1     N Y N 252 
MTA C2     C Y N 253 
MTA N3     N Y N 254 
MTA C4     C Y N 255 
MTA HCS1   H N N 256 
MTA HCS2   H N N 257 
MTA HCS3   H N N 258 
MTA "H5'1" H N N 259 
MTA "H5'2" H N N 260 
MTA "H4'"  H N N 261 
MTA "H2'"  H N N 262 
MTA "HO2'" H N N 263 
MTA "H3'"  H N N 264 
MTA H3T    H N N 265 
MTA "H1'"  H N N 266 
MTA H8     H N N 267 
MTA H61    H N N 268 
MTA H62    H N N 269 
MTA H2     H N N 270 
PHE N      N N N 271 
PHE CA     C N S 272 
PHE C      C N N 273 
PHE O      O N N 274 
PHE CB     C N N 275 
PHE CG     C Y N 276 
PHE CD1    C Y N 277 
PHE CD2    C Y N 278 
PHE CE1    C Y N 279 
PHE CE2    C Y N 280 
PHE CZ     C Y N 281 
PHE OXT    O N N 282 
PHE H      H N N 283 
PHE H2     H N N 284 
PHE HA     H N N 285 
PHE HB2    H N N 286 
PHE HB3    H N N 287 
PHE HD1    H N N 288 
PHE HD2    H N N 289 
PHE HE1    H N N 290 
PHE HE2    H N N 291 
PHE HZ     H N N 292 
PHE HXT    H N N 293 
PRO N      N N N 294 
PRO CA     C N S 295 
PRO C      C N N 296 
PRO O      O N N 297 
PRO CB     C N N 298 
PRO CG     C N N 299 
PRO CD     C N N 300 
PRO OXT    O N N 301 
PRO H      H N N 302 
PRO HA     H N N 303 
PRO HB2    H N N 304 
PRO HB3    H N N 305 
PRO HG2    H N N 306 
PRO HG3    H N N 307 
PRO HD2    H N N 308 
PRO HD3    H N N 309 
PRO HXT    H N N 310 
SER N      N N N 311 
SER CA     C N S 312 
SER C      C N N 313 
SER O      O N N 314 
SER CB     C N N 315 
SER OG     O N N 316 
SER OXT    O N N 317 
SER H      H N N 318 
SER H2     H N N 319 
SER HA     H N N 320 
SER HB2    H N N 321 
SER HB3    H N N 322 
SER HG     H N N 323 
SER HXT    H N N 324 
THR N      N N N 325 
THR CA     C N S 326 
THR C      C N N 327 
THR O      O N N 328 
THR CB     C N R 329 
THR OG1    O N N 330 
THR CG2    C N N 331 
THR OXT    O N N 332 
THR H      H N N 333 
THR H2     H N N 334 
THR HA     H N N 335 
THR HB     H N N 336 
THR HG1    H N N 337 
THR HG21   H N N 338 
THR HG22   H N N 339 
THR HG23   H N N 340 
THR HXT    H N N 341 
TRP N      N N N 342 
TRP CA     C N S 343 
TRP C      C N N 344 
TRP O      O N N 345 
TRP CB     C N N 346 
TRP CG     C Y N 347 
TRP CD1    C Y N 348 
TRP CD2    C Y N 349 
TRP NE1    N Y N 350 
TRP CE2    C Y N 351 
TRP CE3    C Y N 352 
TRP CZ2    C Y N 353 
TRP CZ3    C Y N 354 
TRP CH2    C Y N 355 
TRP OXT    O N N 356 
TRP H      H N N 357 
TRP H2     H N N 358 
TRP HA     H N N 359 
TRP HB2    H N N 360 
TRP HB3    H N N 361 
TRP HD1    H N N 362 
TRP HE1    H N N 363 
TRP HE3    H N N 364 
TRP HZ2    H N N 365 
TRP HZ3    H N N 366 
TRP HH2    H N N 367 
TRP HXT    H N N 368 
TYR N      N N N 369 
TYR CA     C N S 370 
TYR C      C N N 371 
TYR O      O N N 372 
TYR CB     C N N 373 
TYR CG     C Y N 374 
TYR CD1    C Y N 375 
TYR CD2    C Y N 376 
TYR CE1    C Y N 377 
TYR CE2    C Y N 378 
TYR CZ     C Y N 379 
TYR OH     O N N 380 
TYR OXT    O N N 381 
TYR H      H N N 382 
TYR H2     H N N 383 
TYR HA     H N N 384 
TYR HB2    H N N 385 
TYR HB3    H N N 386 
TYR HD1    H N N 387 
TYR HD2    H N N 388 
TYR HE1    H N N 389 
TYR HE2    H N N 390 
TYR HH     H N N 391 
TYR HXT    H N N 392 
VAL N      N N N 393 
VAL CA     C N S 394 
VAL C      C N N 395 
VAL O      O N N 396 
VAL CB     C N N 397 
VAL CG1    C N N 398 
VAL CG2    C N N 399 
VAL OXT    O N N 400 
VAL H      H N N 401 
VAL H2     H N N 402 
VAL HA     H N N 403 
VAL HB     H N N 404 
VAL HG11   H N N 405 
VAL HG12   H N N 406 
VAL HG13   H N N 407 
VAL HG21   H N N 408 
VAL HG22   H N N 409 
VAL HG23   H N N 410 
VAL HXT    H N N 411 
# 
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  
GLN N     CA     sing N N 70  
GLN N     H      sing N N 71  
GLN N     H2     sing N N 72  
GLN CA    C      sing N N 73  
GLN CA    CB     sing N N 74  
GLN CA    HA     sing N N 75  
GLN C     O      doub N N 76  
GLN C     OXT    sing N N 77  
GLN CB    CG     sing N N 78  
GLN CB    HB2    sing N N 79  
GLN CB    HB3    sing N N 80  
GLN CG    CD     sing N N 81  
GLN CG    HG2    sing N N 82  
GLN CG    HG3    sing N N 83  
GLN CD    OE1    doub N N 84  
GLN CD    NE2    sing N N 85  
GLN NE2   HE21   sing N N 86  
GLN NE2   HE22   sing N N 87  
GLN OXT   HXT    sing N N 88  
GLU N     CA     sing N N 89  
GLU N     H      sing N N 90  
GLU N     H2     sing N N 91  
GLU CA    C      sing N N 92  
GLU CA    CB     sing N N 93  
GLU CA    HA     sing N N 94  
GLU C     O      doub N N 95  
GLU C     OXT    sing N N 96  
GLU CB    CG     sing N N 97  
GLU CB    HB2    sing N N 98  
GLU CB    HB3    sing N N 99  
GLU CG    CD     sing N N 100 
GLU CG    HG2    sing N N 101 
GLU CG    HG3    sing N N 102 
GLU CD    OE1    doub N N 103 
GLU CD    OE2    sing N N 104 
GLU OE2   HE2    sing N N 105 
GLU OXT   HXT    sing N N 106 
GLY N     CA     sing N N 107 
GLY N     H      sing N N 108 
GLY N     H2     sing N N 109 
GLY CA    C      sing N N 110 
GLY CA    HA2    sing N N 111 
GLY CA    HA3    sing N N 112 
GLY C     O      doub N N 113 
GLY C     OXT    sing N N 114 
GLY OXT   HXT    sing N N 115 
HIS N     CA     sing N N 116 
HIS N     H      sing N N 117 
HIS N     H2     sing N N 118 
HIS CA    C      sing N N 119 
HIS CA    CB     sing N N 120 
HIS CA    HA     sing N N 121 
HIS C     O      doub N N 122 
HIS C     OXT    sing N N 123 
HIS CB    CG     sing N N 124 
HIS CB    HB2    sing N N 125 
HIS CB    HB3    sing N N 126 
HIS CG    ND1    sing Y N 127 
HIS CG    CD2    doub Y N 128 
HIS ND1   CE1    doub Y N 129 
HIS ND1   HD1    sing N N 130 
HIS CD2   NE2    sing Y N 131 
HIS CD2   HD2    sing N N 132 
HIS CE1   NE2    sing Y N 133 
HIS CE1   HE1    sing N N 134 
HIS NE2   HE2    sing N N 135 
HIS OXT   HXT    sing N N 136 
HOH O     H1     sing N N 137 
HOH O     H2     sing N N 138 
ILE N     CA     sing N N 139 
ILE N     H      sing N N 140 
ILE N     H2     sing N N 141 
ILE CA    C      sing N N 142 
ILE CA    CB     sing N N 143 
ILE CA    HA     sing N N 144 
ILE C     O      doub N N 145 
ILE C     OXT    sing N N 146 
ILE CB    CG1    sing N N 147 
ILE CB    CG2    sing N N 148 
ILE CB    HB     sing N N 149 
ILE CG1   CD1    sing N N 150 
ILE CG1   HG12   sing N N 151 
ILE CG1   HG13   sing N N 152 
ILE CG2   HG21   sing N N 153 
ILE CG2   HG22   sing N N 154 
ILE CG2   HG23   sing N N 155 
ILE CD1   HD11   sing N N 156 
ILE CD1   HD12   sing N N 157 
ILE CD1   HD13   sing N N 158 
ILE OXT   HXT    sing N N 159 
LEU N     CA     sing N N 160 
LEU N     H      sing N N 161 
LEU N     H2     sing N N 162 
LEU CA    C      sing N N 163 
LEU CA    CB     sing N N 164 
LEU CA    HA     sing N N 165 
LEU C     O      doub N N 166 
LEU C     OXT    sing N N 167 
LEU CB    CG     sing N N 168 
LEU CB    HB2    sing N N 169 
LEU CB    HB3    sing N N 170 
LEU CG    CD1    sing N N 171 
LEU CG    CD2    sing N N 172 
LEU CG    HG     sing N N 173 
LEU CD1   HD11   sing N N 174 
LEU CD1   HD12   sing N N 175 
LEU CD1   HD13   sing N N 176 
LEU CD2   HD21   sing N N 177 
LEU CD2   HD22   sing N N 178 
LEU CD2   HD23   sing N N 179 
LEU OXT   HXT    sing N N 180 
LYS N     CA     sing N N 181 
LYS N     H      sing N N 182 
LYS N     H2     sing N N 183 
LYS CA    C      sing N N 184 
LYS CA    CB     sing N N 185 
LYS CA    HA     sing N N 186 
LYS C     O      doub N N 187 
LYS C     OXT    sing N N 188 
LYS CB    CG     sing N N 189 
LYS CB    HB2    sing N N 190 
LYS CB    HB3    sing N N 191 
LYS CG    CD     sing N N 192 
LYS CG    HG2    sing N N 193 
LYS CG    HG3    sing N N 194 
LYS CD    CE     sing N N 195 
LYS CD    HD2    sing N N 196 
LYS CD    HD3    sing N N 197 
LYS CE    NZ     sing N N 198 
LYS CE    HE2    sing N N 199 
LYS CE    HE3    sing N N 200 
LYS NZ    HZ1    sing N N 201 
LYS NZ    HZ2    sing N N 202 
LYS NZ    HZ3    sing N N 203 
LYS OXT   HXT    sing N N 204 
MET N     CA     sing N N 205 
MET N     H      sing N N 206 
MET N     H2     sing N N 207 
MET CA    C      sing N N 208 
MET CA    CB     sing N N 209 
MET CA    HA     sing N N 210 
MET C     O      doub N N 211 
MET C     OXT    sing N N 212 
MET CB    CG     sing N N 213 
MET CB    HB2    sing N N 214 
MET CB    HB3    sing N N 215 
MET CG    SD     sing N N 216 
MET CG    HG2    sing N N 217 
MET CG    HG3    sing N N 218 
MET SD    CE     sing N N 219 
MET CE    HE1    sing N N 220 
MET CE    HE2    sing N N 221 
MET CE    HE3    sing N N 222 
MET OXT   HXT    sing N N 223 
MTA CS    "S5'"  sing N N 224 
MTA CS    HCS1   sing N N 225 
MTA CS    HCS2   sing N N 226 
MTA CS    HCS3   sing N N 227 
MTA "S5'" "C5'"  sing N N 228 
MTA "C5'" "C4'"  sing N N 229 
MTA "C5'" "H5'1" sing N N 230 
MTA "C5'" "H5'2" sing N N 231 
MTA "C4'" "O4'"  sing N N 232 
MTA "C4'" "C3'"  sing N N 233 
MTA "C4'" "H4'"  sing N N 234 
MTA "O4'" "C1'"  sing N N 235 
MTA "C2'" "O2'"  sing N N 236 
MTA "C2'" "C3'"  sing N N 237 
MTA "C2'" "C1'"  sing N N 238 
MTA "C2'" "H2'"  sing N N 239 
MTA "O2'" "HO2'" sing N N 240 
MTA "C3'" "O3'"  sing N N 241 
MTA "C3'" "H3'"  sing N N 242 
MTA "O3'" H3T    sing N N 243 
MTA "C1'" N9     sing N N 244 
MTA "C1'" "H1'"  sing N N 245 
MTA N9    C8     sing Y N 246 
MTA N9    C4     sing Y N 247 
MTA C8    N7     doub Y N 248 
MTA C8    H8     sing N N 249 
MTA N7    C5     sing Y N 250 
MTA C5    C6     sing Y N 251 
MTA C5    C4     doub Y N 252 
MTA C6    N6     sing N N 253 
MTA C6    N1     doub Y N 254 
MTA N6    H61    sing N N 255 
MTA N6    H62    sing N N 256 
MTA N1    C2     sing Y N 257 
MTA C2    N3     doub Y N 258 
MTA C2    H2     sing N N 259 
MTA N3    C4     sing Y N 260 
PHE N     CA     sing N N 261 
PHE N     H      sing N N 262 
PHE N     H2     sing N N 263 
PHE CA    C      sing N N 264 
PHE CA    CB     sing N N 265 
PHE CA    HA     sing N N 266 
PHE C     O      doub N N 267 
PHE C     OXT    sing N N 268 
PHE CB    CG     sing N N 269 
PHE CB    HB2    sing N N 270 
PHE CB    HB3    sing N N 271 
PHE CG    CD1    doub Y N 272 
PHE CG    CD2    sing Y N 273 
PHE CD1   CE1    sing Y N 274 
PHE CD1   HD1    sing N N 275 
PHE CD2   CE2    doub Y N 276 
PHE CD2   HD2    sing N N 277 
PHE CE1   CZ     doub Y N 278 
PHE CE1   HE1    sing N N 279 
PHE CE2   CZ     sing Y N 280 
PHE CE2   HE2    sing N N 281 
PHE CZ    HZ     sing N N 282 
PHE OXT   HXT    sing N N 283 
PRO N     CA     sing N N 284 
PRO N     CD     sing N N 285 
PRO N     H      sing N N 286 
PRO CA    C      sing N N 287 
PRO CA    CB     sing N N 288 
PRO CA    HA     sing N N 289 
PRO C     O      doub N N 290 
PRO C     OXT    sing N N 291 
PRO CB    CG     sing N N 292 
PRO CB    HB2    sing N N 293 
PRO CB    HB3    sing N N 294 
PRO CG    CD     sing N N 295 
PRO CG    HG2    sing N N 296 
PRO CG    HG3    sing N N 297 
PRO CD    HD2    sing N N 298 
PRO CD    HD3    sing N N 299 
PRO OXT   HXT    sing N N 300 
SER N     CA     sing N N 301 
SER N     H      sing N N 302 
SER N     H2     sing N N 303 
SER CA    C      sing N N 304 
SER CA    CB     sing N N 305 
SER CA    HA     sing N N 306 
SER C     O      doub N N 307 
SER C     OXT    sing N N 308 
SER CB    OG     sing N N 309 
SER CB    HB2    sing N N 310 
SER CB    HB3    sing N N 311 
SER OG    HG     sing N N 312 
SER OXT   HXT    sing N N 313 
THR N     CA     sing N N 314 
THR N     H      sing N N 315 
THR N     H2     sing N N 316 
THR CA    C      sing N N 317 
THR CA    CB     sing N N 318 
THR CA    HA     sing N N 319 
THR C     O      doub N N 320 
THR C     OXT    sing N N 321 
THR CB    OG1    sing N N 322 
THR CB    CG2    sing N N 323 
THR CB    HB     sing N N 324 
THR OG1   HG1    sing N N 325 
THR CG2   HG21   sing N N 326 
THR CG2   HG22   sing N N 327 
THR CG2   HG23   sing N N 328 
THR OXT   HXT    sing N N 329 
TRP N     CA     sing N N 330 
TRP N     H      sing N N 331 
TRP N     H2     sing N N 332 
TRP CA    C      sing N N 333 
TRP CA    CB     sing N N 334 
TRP CA    HA     sing N N 335 
TRP C     O      doub N N 336 
TRP C     OXT    sing N N 337 
TRP CB    CG     sing N N 338 
TRP CB    HB2    sing N N 339 
TRP CB    HB3    sing N N 340 
TRP CG    CD1    doub Y N 341 
TRP CG    CD2    sing Y N 342 
TRP CD1   NE1    sing Y N 343 
TRP CD1   HD1    sing N N 344 
TRP CD2   CE2    doub Y N 345 
TRP CD2   CE3    sing Y N 346 
TRP NE1   CE2    sing Y N 347 
TRP NE1   HE1    sing N N 348 
TRP CE2   CZ2    sing Y N 349 
TRP CE3   CZ3    doub Y N 350 
TRP CE3   HE3    sing N N 351 
TRP CZ2   CH2    doub Y N 352 
TRP CZ2   HZ2    sing N N 353 
TRP CZ3   CH2    sing Y N 354 
TRP CZ3   HZ3    sing N N 355 
TRP CH2   HH2    sing N N 356 
TRP OXT   HXT    sing N N 357 
TYR N     CA     sing N N 358 
TYR N     H      sing N N 359 
TYR N     H2     sing N N 360 
TYR CA    C      sing N N 361 
TYR CA    CB     sing N N 362 
TYR CA    HA     sing N N 363 
TYR C     O      doub N N 364 
TYR C     OXT    sing N N 365 
TYR CB    CG     sing N N 366 
TYR CB    HB2    sing N N 367 
TYR CB    HB3    sing N N 368 
TYR CG    CD1    doub Y N 369 
TYR CG    CD2    sing Y N 370 
TYR CD1   CE1    sing Y N 371 
TYR CD1   HD1    sing N N 372 
TYR CD2   CE2    doub Y N 373 
TYR CD2   HD2    sing N N 374 
TYR CE1   CZ     doub Y N 375 
TYR CE1   HE1    sing N N 376 
TYR CE2   CZ     sing Y N 377 
TYR CE2   HE2    sing N N 378 
TYR CZ    OH     sing N N 379 
TYR OH    HH     sing N N 380 
TYR OXT   HXT    sing N N 381 
VAL N     CA     sing N N 382 
VAL N     H      sing N N 383 
VAL N     H2     sing N N 384 
VAL CA    C      sing N N 385 
VAL CA    CB     sing N N 386 
VAL CA    HA     sing N N 387 
VAL C     O      doub N N 388 
VAL C     OXT    sing N N 389 
VAL CB    CG1    sing N N 390 
VAL CB    CG2    sing N N 391 
VAL CB    HB     sing N N 392 
VAL CG1   HG11   sing N N 393 
VAL CG1   HG12   sing N N 394 
VAL CG1   HG13   sing N N 395 
VAL CG2   HG21   sing N N 396 
VAL CG2   HG22   sing N N 397 
VAL CG2   HG23   sing N N 398 
VAL OXT   HXT    sing N N 399 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan 22K06096 1 
'Japan Society for the Promotion of Science (JSPS)' Japan 20K15734 2 
# 
_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                    9KO5 
_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]   0.014366 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004001 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013090 
_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]   0.011901 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . PRO A 1 2   ? -1.478  -24.203 -8.396  1.00 54.45 ? 25  PRO A N     1 
ATOM   2    C CA    . PRO A 1 2   ? -2.328  -23.861 -7.248  1.00 53.38 ? 25  PRO A CA    1 
ATOM   3    C C     . PRO A 1 2   ? -1.865  -22.571 -6.553  1.00 57.18 ? 25  PRO A C     1 
ATOM   4    O O     . PRO A 1 2   ? -0.789  -22.065 -6.875  1.00 54.97 ? 25  PRO A O     1 
ATOM   5    C CB    . PRO A 1 2   ? -2.195  -25.089 -6.345  1.00 52.66 ? 25  PRO A CB    1 
ATOM   6    C CG    . PRO A 1 2   ? -2.021  -26.236 -7.335  1.00 43.02 ? 25  PRO A CG    1 
ATOM   7    C CD    . PRO A 1 2   ? -1.184  -25.647 -8.468  1.00 45.64 ? 25  PRO A CD    1 
ATOM   8    N N     . GLN A 1 3   ? -2.681  -22.049 -5.627  1.00 56.40 ? 26  GLN A N     1 
ATOM   9    C CA    . GLN A 1 3   ? -2.510  -20.692 -5.107  1.00 53.32 ? 26  GLN A CA    1 
ATOM   10   C C     . GLN A 1 3   ? -1.640  -20.703 -3.859  1.00 53.93 ? 26  GLN A C     1 
ATOM   11   O O     . GLN A 1 3   ? -1.997  -21.363 -2.869  1.00 50.44 ? 26  GLN A O     1 
ATOM   12   C CB    . GLN A 1 3   ? -3.871  -20.071 -4.794  1.00 55.49 ? 26  GLN A CB    1 
ATOM   13   C CG    . GLN A 1 3   ? -3.881  -18.726 -4.017  1.00 57.66 ? 26  GLN A CG    1 
ATOM   14   C CD    . GLN A 1 3   ? -3.136  -17.567 -4.670  1.00 57.35 ? 26  GLN A CD    1 
ATOM   15   O OE1   . GLN A 1 3   ? -2.484  -17.709 -5.707  1.00 62.56 ? 26  GLN A OE1   1 
ATOM   16   N NE2   . GLN A 1 3   ? -3.234  -16.392 -4.038  1.00 53.73 ? 26  GLN A NE2   1 
ATOM   17   N N     . PRO A 1 4   ? -0.496  -20.009 -3.865  1.00 47.08 ? 27  PRO A N     1 
ATOM   18   C CA    . PRO A 1 4   ? 0.357   -19.963 -2.671  1.00 48.14 ? 27  PRO A CA    1 
ATOM   19   C C     . PRO A 1 4   ? -0.204  -19.055 -1.582  1.00 49.27 ? 27  PRO A C     1 
ATOM   20   O O     . PRO A 1 4   ? -0.817  -18.017 -1.845  1.00 45.87 ? 27  PRO A O     1 
ATOM   21   C CB    . PRO A 1 4   ? 1.699   -19.429 -3.200  1.00 46.88 ? 27  PRO A CB    1 
ATOM   22   C CG    . PRO A 1 4   ? 1.600   -19.466 -4.707  1.00 50.81 ? 27  PRO A CG    1 
ATOM   23   C CD    . PRO A 1 4   ? 0.137   -19.398 -5.044  1.00 50.15 ? 27  PRO A CD    1 
ATOM   24   N N     . LYS A 1 5   ? 0.005   -19.480 -0.336  1.00 50.09 ? 28  LYS A N     1 
ATOM   25   C CA    . LYS A 1 5   ? -0.314  -18.692 0.847   1.00 45.27 ? 28  LYS A CA    1 
ATOM   26   C C     . LYS A 1 5   ? 0.915   -17.898 1.289   1.00 43.68 ? 28  LYS A C     1 
ATOM   27   O O     . LYS A 1 5   ? 2.032   -18.118 0.817   1.00 47.46 ? 28  LYS A O     1 
ATOM   28   C CB    . LYS A 1 5   ? -0.795  -19.586 2.000   1.00 39.45 ? 28  LYS A CB    1 
ATOM   29   C CG    . LYS A 1 5   ? -1.858  -20.618 1.648   1.00 40.66 ? 28  LYS A CG    1 
ATOM   30   C CD    . LYS A 1 5   ? -2.093  -21.562 2.836   1.00 37.09 ? 28  LYS A CD    1 
ATOM   31   C CE    . LYS A 1 5   ? -3.324  -22.434 2.641   1.00 37.62 ? 28  LYS A CE    1 
ATOM   32   N NZ    . LYS A 1 5   ? -3.274  -23.305 1.443   1.00 45.98 ? 28  LYS A NZ    1 
ATOM   33   N N     . LYS A 1 6   ? 0.693   -16.977 2.228   1.00 47.08 ? 29  LYS A N     1 
ATOM   34   C CA    . LYS A 1 6   ? 1.760   -16.155 2.805   1.00 44.41 ? 29  LYS A CA    1 
ATOM   35   C C     . LYS A 1 6   ? 2.563   -15.427 1.717   1.00 49.93 ? 29  LYS A C     1 
ATOM   36   O O     . LYS A 1 6   ? 3.796   -15.322 1.785   1.00 48.54 ? 29  LYS A O     1 
ATOM   37   C CB    . LYS A 1 6   ? 2.665   -17.006 3.707   1.00 44.24 ? 29  LYS A CB    1 
ATOM   38   C CG    . LYS A 1 6   ? 1.918   -17.741 4.844   1.00 43.01 ? 29  LYS A CG    1 
ATOM   39   C CD    . LYS A 1 6   ? 2.827   -18.015 6.058   1.00 47.84 ? 29  LYS A CD    1 
ATOM   40   C CE    . LYS A 1 6   ? 2.105   -17.748 7.398   1.00 52.39 ? 29  LYS A CE    1 
ATOM   41   N NZ    . LYS A 1 6   ? 2.766   -16.692 8.261   1.00 55.44 ? 29  LYS A NZ    1 
ATOM   42   N N     . VAL A 1 7   ? 1.843   -14.917 0.701   1.00 45.90 ? 30  VAL A N     1 
ATOM   43   C CA    . VAL A 1 7   ? 2.466   -14.133 -0.376  1.00 47.37 ? 30  VAL A CA    1 
ATOM   44   C C     . VAL A 1 7   ? 3.191   -12.918 0.212   1.00 44.20 ? 30  VAL A C     1 
ATOM   45   O O     . VAL A 1 7   ? 2.890   -12.450 1.320   1.00 40.40 ? 30  VAL A O     1 
ATOM   46   C CB    . VAL A 1 7   ? 1.419   -13.696 -1.417  1.00 45.10 ? 30  VAL A CB    1 
ATOM   47   C CG1   . VAL A 1 7   ? 0.525   -12.590 -0.855  1.00 39.98 ? 30  VAL A CG1   1 
ATOM   48   C CG2   . VAL A 1 7   ? 2.080   -13.240 -2.716  1.00 48.04 ? 30  VAL A CG2   1 
ATOM   49   N N     . GLY A 1 8   ? 4.172   -12.411 -0.546  1.00 44.93 ? 31  GLY A N     1 
ATOM   50   C CA    . GLY A 1 8   ? 4.941   -11.245 -0.137  1.00 39.74 ? 31  GLY A CA    1 
ATOM   51   C C     . GLY A 1 8   ? 5.932   -11.565 0.971   1.00 41.74 ? 31  GLY A C     1 
ATOM   52   O O     . GLY A 1 8   ? 6.433   -12.686 1.095   1.00 38.70 ? 31  GLY A O     1 
ATOM   53   N N     . ALA A 1 9   ? 6.214   -10.557 1.796   1.00 37.53 ? 32  ALA A N     1 
ATOM   54   C CA    . ALA A 1 9   ? 7.111   -10.676 2.949   1.00 40.99 ? 32  ALA A CA    1 
ATOM   55   C C     . ALA A 1 9   ? 6.274   -10.557 4.218   1.00 44.13 ? 32  ALA A C     1 
ATOM   56   O O     . ALA A 1 9   ? 6.137   -9.471  4.784   1.00 50.78 ? 32  ALA A O     1 
ATOM   57   C CB    . ALA A 1 9   ? 8.212   -9.600  2.915   1.00 40.98 ? 32  ALA A CB    1 
ATOM   58   N N     . ILE A 1 10  ? 5.707   -11.676 4.668   1.00 41.31 ? 33  ILE A N     1 
ATOM   59   C CA    . ILE A 1 10  ? 4.884   -11.642 5.870   1.00 47.67 ? 33  ILE A CA    1 
ATOM   60   C C     . ILE A 1 10  ? 5.353   -12.690 6.874   1.00 48.13 ? 33  ILE A C     1 
ATOM   61   O O     . ILE A 1 10  ? 4.700   -12.913 7.901   1.00 50.99 ? 33  ILE A O     1 
ATOM   62   C CB    . ILE A 1 10  ? 3.390   -11.817 5.529   1.00 48.99 ? 33  ILE A CB    1 
ATOM   63   C CG1   . ILE A 1 10  ? 3.078   -13.257 5.108   1.00 46.77 ? 33  ILE A CG1   1 
ATOM   64   C CG2   . ILE A 1 10  ? 2.960   -10.802 4.449   1.00 43.84 ? 33  ILE A CG2   1 
ATOM   65   C CD1   . ILE A 1 10  ? 1.614   -13.642 5.292   1.00 41.55 ? 33  ILE A CD1   1 
ATOM   66   N N     . VAL A 1 11  ? 6.488   -13.327 6.601   1.00 40.20 ? 34  VAL A N     1 
ATOM   67   C CA    . VAL A 1 11  ? 7.088   -14.233 7.581   1.00 42.50 ? 34  VAL A CA    1 
ATOM   68   C C     . VAL A 1 11  ? 8.376   -13.588 8.078   1.00 36.64 ? 34  VAL A C     1 
ATOM   69   O O     . VAL A 1 11  ? 8.949   -12.740 7.378   1.00 38.03 ? 34  VAL A O     1 
ATOM   70   C CB    . VAL A 1 11  ? 7.331   -15.635 6.997   1.00 41.62 ? 34  VAL A CB    1 
ATOM   71   C CG1   . VAL A 1 11  ? 6.012   -16.276 6.603   1.00 37.80 ? 34  VAL A CG1   1 
ATOM   72   C CG2   . VAL A 1 11  ? 8.280   -15.569 5.807   1.00 39.00 ? 34  VAL A CG2   1 
ATOM   73   N N     . PRO A 1 12  ? 8.854   -13.928 9.277   1.00 41.50 ? 35  PRO A N     1 
ATOM   74   C CA    . PRO A 1 12  ? 10.047  -13.255 9.806   1.00 40.39 ? 35  PRO A CA    1 
ATOM   75   C C     . PRO A 1 12  ? 11.275  -13.471 8.929   1.00 39.89 ? 35  PRO A C     1 
ATOM   76   O O     . PRO A 1 12  ? 11.422  -14.488 8.241   1.00 38.93 ? 35  PRO A O     1 
ATOM   77   C CB    . PRO A 1 12  ? 10.228  -13.889 11.192  1.00 41.82 ? 35  PRO A CB    1 
ATOM   78   C CG    . PRO A 1 12  ? 8.846   -14.335 11.576  1.00 42.77 ? 35  PRO A CG    1 
ATOM   79   C CD    . PRO A 1 12  ? 8.223   -14.800 10.287  1.00 44.10 ? 35  PRO A CD    1 
ATOM   80   N N     . THR A 1 13  ? 12.164  -12.484 8.976   1.00 35.06 ? 36  THR A N     1 
ATOM   81   C CA    . THR A 1 13  ? 13.408  -12.525 8.222   1.00 31.85 ? 36  THR A CA    1 
ATOM   82   C C     . THR A 1 13  ? 14.265  -13.709 8.652   1.00 31.46 ? 36  THR A C     1 
ATOM   83   O O     . THR A 1 13  ? 14.316  -14.060 9.831   1.00 32.22 ? 36  THR A O     1 
ATOM   84   C CB    . THR A 1 13  ? 14.147  -11.205 8.432   1.00 30.18 ? 36  THR A CB    1 
ATOM   85   O OG1   . THR A 1 13  ? 13.367  -10.157 7.842   1.00 34.51 ? 36  THR A OG1   1 
ATOM   86   C CG2   . THR A 1 13  ? 15.535  -11.225 7.814   1.00 25.95 ? 36  THR A CG2   1 
ATOM   87   N N     . SER A 1 14  ? 14.927  -14.337 7.679   1.00 28.89 ? 37  SER A N     1 
ATOM   88   C CA    . SER A 1 14  ? 15.754  -15.503 7.955   1.00 30.45 ? 37  SER A CA    1 
ATOM   89   C C     . SER A 1 14  ? 16.923  -15.142 8.866   1.00 31.66 ? 37  SER A C     1 
ATOM   90   O O     . SER A 1 14  ? 17.449  -14.026 8.823   1.00 31.34 ? 37  SER A O     1 
ATOM   91   C CB    . SER A 1 14  ? 16.284  -16.087 6.644   1.00 32.59 ? 37  SER A CB    1 
ATOM   92   O OG    . SER A 1 14  ? 17.467  -16.821 6.859   1.00 35.93 ? 37  SER A OG    1 
ATOM   93   N N     . SER A 1 15  ? 17.352  -16.116 9.677   1.00 32.28 ? 38  SER A N     1 
ATOM   94   C CA    . SER A 1 15  ? 18.482  -15.902 10.585  1.00 29.98 ? 38  SER A CA    1 
ATOM   95   C C     . SER A 1 15  ? 19.790  -15.693 9.826   1.00 32.08 ? 38  SER A C     1 
ATOM   96   O O     . SER A 1 15  ? 20.724  -15.070 10.351  1.00 28.16 ? 38  SER A O     1 
ATOM   97   C CB    . SER A 1 15  ? 18.604  -17.085 11.538  1.00 26.85 ? 38  SER A CB    1 
ATOM   98   O OG    . SER A 1 15  ? 19.100  -18.204 10.837  1.00 41.64 ? 38  SER A OG    1 
ATOM   99   N N     . ILE A 1 16  ? 19.875  -16.199 8.593   1.00 31.60 ? 39  ILE A N     1 
ATOM   100  C CA    . ILE A 1 16  ? 21.040  -15.938 7.755   1.00 31.03 ? 39  ILE A CA    1 
ATOM   101  C C     . ILE A 1 16  ? 21.068  -14.477 7.322   1.00 29.44 ? 39  ILE A C     1 
ATOM   102  O O     . ILE A 1 16  ? 22.108  -13.811 7.380   1.00 24.25 ? 39  ILE A O     1 
ATOM   103  C CB    . ILE A 1 16  ? 21.043  -16.887 6.542   1.00 34.38 ? 39  ILE A CB    1 
ATOM   104  C CG1   . ILE A 1 16  ? 21.222  -18.336 7.006   1.00 37.10 ? 39  ILE A CG1   1 
ATOM   105  C CG2   . ILE A 1 16  ? 22.141  -16.505 5.535   1.00 32.75 ? 39  ILE A CG2   1 
ATOM   106  C CD1   . ILE A 1 16  ? 20.642  -19.353 6.027   1.00 45.13 ? 39  ILE A CD1   1 
ATOM   107  N N     . THR A 1 17  ? 19.924  -13.959 6.873   1.00 26.25 ? 40  THR A N     1 
ATOM   108  C CA    . THR A 1 17  ? 19.838  -12.540 6.543   1.00 26.70 ? 40  THR A CA    1 
ATOM   109  C C     . THR A 1 17  ? 20.162  -11.676 7.756   1.00 26.21 ? 40  THR A C     1 
ATOM   110  O O     . THR A 1 17  ? 20.923  -10.704 7.653   1.00 23.24 ? 40  THR A O     1 
ATOM   111  C CB    . THR A 1 17  ? 18.441  -12.226 6.005   1.00 25.97 ? 40  THR A CB    1 
ATOM   112  O OG1   . THR A 1 17  ? 18.132  -13.147 4.947   1.00 28.55 ? 40  THR A OG1   1 
ATOM   113  C CG2   . THR A 1 17  ? 18.358  -10.798 5.464   1.00 20.90 ? 40  THR A CG2   1 
ATOM   114  N N     . ALA A 1 18  ? 19.607  -12.033 8.918   1.00 25.93 ? 41  ALA A N     1 
ATOM   115  C CA    . ALA A 1 18  ? 19.791  -11.226 10.116  1.00 26.66 ? 41  ALA A CA    1 
ATOM   116  C C     . ALA A 1 18  ? 21.264  -11.144 10.484  1.00 24.83 ? 41  ALA A C     1 
ATOM   117  O O     . ALA A 1 18  ? 21.779  -10.064 10.799  1.00 23.23 ? 41  ALA A O     1 
ATOM   118  C CB    . ALA A 1 18  ? 18.965  -11.815 11.265  1.00 23.95 ? 41  ALA A CB    1 
ATOM   119  N N     . LYS A 1 19  ? 21.971  -12.270 10.393  1.00 25.76 ? 42  LYS A N     1 
ATOM   120  C CA    . LYS A 1 19  ? 23.393  -12.287 10.727  1.00 26.20 ? 42  LYS A CA    1 
ATOM   121  C C     . LYS A 1 19  ? 24.195  -11.389 9.794   1.00 25.34 ? 42  LYS A C     1 
ATOM   122  O O     . LYS A 1 19  ? 25.087  -10.660 10.242  1.00 23.09 ? 42  LYS A O     1 
ATOM   123  C CB    . LYS A 1 19  ? 23.923  -13.721 10.682  1.00 27.31 ? 42  LYS A CB    1 
ATOM   124  C CG    . LYS A 1 19  ? 25.375  -13.888 11.125  1.00 29.01 ? 42  LYS A CG    1 
ATOM   125  C CD    . LYS A 1 19  ? 25.741  -15.365 11.258  1.00 39.04 ? 42  LYS A CD    1 
ATOM   126  C CE    . LYS A 1 19  ? 27.106  -15.550 11.914  1.00 51.61 ? 42  LYS A CE    1 
ATOM   127  N NZ    . LYS A 1 19  ? 27.538  -16.988 11.973  1.00 55.82 ? 42  LYS A NZ    1 
ATOM   128  N N     . LYS A 1 20  ? 23.899  -11.419 8.494   1.00 23.80 ? 43  LYS A N     1 
ATOM   129  C CA    . LYS A 1 20  ? 24.642  -10.539 7.595   1.00 24.32 ? 43  LYS A CA    1 
ATOM   130  C C     . LYS A 1 20  ? 24.350  -9.058  7.874   1.00 24.25 ? 43  LYS A C     1 
ATOM   131  O O     . LYS A 1 20  ? 25.259  -8.218  7.808   1.00 26.16 ? 43  LYS A O     1 
ATOM   132  C CB    . LYS A 1 20  ? 24.331  -10.881 6.142   1.00 24.76 ? 43  LYS A CB    1 
ATOM   133  C CG    . LYS A 1 20  ? 25.175  -10.059 5.143   1.00 40.80 ? 43  LYS A CG    1 
ATOM   134  C CD    . LYS A 1 20  ? 26.672  -10.466 5.074   1.00 39.74 ? 43  LYS A CD    1 
ATOM   135  C CE    . LYS A 1 20  ? 27.302  -10.008 3.750   1.00 39.24 ? 43  LYS A CE    1 
ATOM   136  N NZ    . LYS A 1 20  ? 28.791  -9.950  3.759   1.00 42.86 ? 43  LYS A NZ    1 
ATOM   137  N N     . MET A 1 21  ? 23.089  -8.707  8.145   1.00 22.23 ? 44  MET A N     1 
ATOM   138  C CA    . MET A 1 21  ? 22.780  -7.318  8.483   1.00 21.88 ? 44  MET A CA    1 
ATOM   139  C C     . MET A 1 21  ? 23.566  -6.866  9.704   1.00 23.92 ? 44  MET A C     1 
ATOM   140  O O     . MET A 1 21  ? 24.083  -5.744  9.732   1.00 24.46 ? 44  MET A O     1 
ATOM   141  C CB    . MET A 1 21  ? 21.281  -7.144  8.721   1.00 21.73 ? 44  MET A CB    1 
ATOM   142  C CG    . MET A 1 21  ? 20.441  -7.374  7.477   1.00 23.40 ? 44  MET A CG    1 
ATOM   143  S SD    . MET A 1 21  ? 18.677  -7.154  7.797   1.00 26.61 ? 44  MET A SD    1 
ATOM   144  C CE    . MET A 1 21  ? 18.634  -5.358  7.716   1.00 23.44 ? 44  MET A CE    1 
ATOM   145  N N     . ALA A 1 22  ? 23.678  -7.727  10.722  1.00 23.18 ? 45  ALA A N     1 
ATOM   146  C CA    . ALA A 1 22  ? 24.368  -7.343  11.951  1.00 24.03 ? 45  ALA A CA    1 
ATOM   147  C C     . ALA A 1 22  ? 25.879  -7.400  11.816  1.00 27.16 ? 45  ALA A C     1 
ATOM   148  O O     . ALA A 1 22  ? 26.590  -6.933  12.716  1.00 24.45 ? 45  ALA A O     1 
ATOM   149  C CB    . ALA A 1 22  ? 23.918  -8.232  13.122  1.00 24.96 ? 45  ALA A CB    1 
ATOM   150  N N     . SER A 1 23  ? 26.394  -7.945  10.711  1.00 24.32 ? 46  SER A N     1 
ATOM   151  C CA    . SER A 1 23  ? 27.836  -8.025  10.550  1.00 24.72 ? 46  SER A CA    1 
ATOM   152  C C     . SER A 1 23  ? 28.463  -6.663  10.274  1.00 27.19 ? 46  SER A C     1 
ATOM   153  O O     . SER A 1 23  ? 29.676  -6.525  10.431  1.00 26.86 ? 46  SER A O     1 
ATOM   154  C CB    . SER A 1 23  ? 28.192  -9.000  9.416   1.00 26.67 ? 46  SER A CB    1 
ATOM   155  O OG    . SER A 1 23  ? 27.880  -8.409  8.170   1.00 26.33 ? 46  SER A OG    1 
ATOM   156  N N     . VAL A 1 24  ? 27.679  -5.658  9.863   1.00 22.83 ? 47  VAL A N     1 
ATOM   157  C CA    . VAL A 1 24  ? 28.258  -4.335  9.651   1.00 21.94 ? 47  VAL A CA    1 
ATOM   158  C C     . VAL A 1 24  ? 28.695  -3.689  10.953  1.00 23.21 ? 47  VAL A C     1 
ATOM   159  O O     . VAL A 1 24  ? 29.449  -2.715  10.917  1.00 22.68 ? 47  VAL A O     1 
ATOM   160  C CB    . VAL A 1 24  ? 27.282  -3.373  8.934   1.00 24.87 ? 47  VAL A CB    1 
ATOM   161  C CG1   . VAL A 1 24  ? 26.780  -3.979  7.647   1.00 27.05 ? 47  VAL A CG1   1 
ATOM   162  C CG2   . VAL A 1 24  ? 26.104  -2.996  9.858   1.00 20.03 ? 47  VAL A CG2   1 
ATOM   163  N N     . ILE A 1 25  ? 28.215  -4.177  12.105  1.00 20.88 ? 48  ILE A N     1 
ATOM   164  C CA    . ILE A 1 25  ? 28.461  -3.497  13.375  1.00 23.64 ? 48  ILE A CA    1 
ATOM   165  C C     . ILE A 1 25  ? 29.919  -3.658  13.794  1.00 26.15 ? 48  ILE A C     1 
ATOM   166  O O     . ILE A 1 25  ? 30.529  -4.722  13.600  1.00 22.37 ? 48  ILE A O     1 
ATOM   167  C CB    . ILE A 1 25  ? 27.521  -4.052  14.460  1.00 21.18 ? 48  ILE A CB    1 
ATOM   168  C CG1   . ILE A 1 25  ? 26.055  -3.706  14.147  1.00 22.27 ? 48  ILE A CG1   1 
ATOM   169  C CG2   . ILE A 1 25  ? 27.894  -3.518  15.833  1.00 24.76 ? 48  ILE A CG2   1 
ATOM   170  C CD1   . ILE A 1 25  ? 25.053  -4.563  14.956  1.00 22.57 ? 48  ILE A CD1   1 
ATOM   171  N N     . ASN A 1 26  ? 30.482  -2.602  14.397  1.00 22.23 ? 49  ASN A N     1 
ATOM   172  C CA    . ASN A 1 26  ? 31.748  -2.688  15.118  1.00 26.02 ? 49  ASN A CA    1 
ATOM   173  C C     . ASN A 1 26  ? 31.460  -2.720  16.609  1.00 25.97 ? 49  ASN A C     1 
ATOM   174  O O     . ASN A 1 26  ? 31.254  -1.660  17.216  1.00 26.10 ? 49  ASN A O     1 
ATOM   175  C CB    . ASN A 1 26  ? 32.670  -1.508  14.778  1.00 24.63 ? 49  ASN A CB    1 
ATOM   176  C CG    . ASN A 1 26  ? 34.037  -1.604  15.480  1.00 30.52 ? 49  ASN A CG    1 
ATOM   177  O OD1   . ASN A 1 26  ? 34.245  -2.435  16.378  1.00 27.29 ? 49  ASN A OD1   1 
ATOM   178  N ND2   . ASN A 1 26  ? 34.966  -0.747  15.072  1.00 28.14 ? 49  ASN A ND2   1 
ATOM   179  N N     . PRO A 1 27  ? 31.476  -3.889  17.256  1.00 29.37 ? 50  PRO A N     1 
ATOM   180  C CA    . PRO A 1 27  ? 31.173  -3.943  18.696  1.00 30.31 ? 50  PRO A CA    1 
ATOM   181  C C     . PRO A 1 27  ? 32.263  -3.366  19.577  1.00 33.79 ? 50  PRO A C     1 
ATOM   182  O O     . PRO A 1 27  ? 32.100  -3.354  20.803  1.00 36.20 ? 50  PRO A O     1 
ATOM   183  C CB    . PRO A 1 27  ? 30.984  -5.452  18.962  1.00 31.85 ? 50  PRO A CB    1 
ATOM   184  C CG    . PRO A 1 27  ? 31.739  -6.136  17.885  1.00 27.31 ? 50  PRO A CG    1 
ATOM   185  C CD    . PRO A 1 27  ? 31.732  -5.222  16.679  1.00 29.59 ? 50  PRO A CD    1 
ATOM   186  N N     . HIS A 1 28  ? 33.362  -2.881  19.002  1.00 30.97 ? 51  HIS A N     1 
ATOM   187  C CA    . HIS A 1 28  ? 34.466  -2.336  19.780  1.00 34.45 ? 51  HIS A CA    1 
ATOM   188  C C     . HIS A 1 28  ? 34.596  -0.826  19.635  1.00 31.85 ? 51  HIS A C     1 
ATOM   189  O O     . HIS A 1 28  ? 35.600  -0.260  20.081  1.00 30.80 ? 51  HIS A O     1 
ATOM   190  C CB    . HIS A 1 28  ? 35.779  -3.019  19.383  1.00 37.01 ? 51  HIS A CB    1 
ATOM   191  C CG    . HIS A 1 28  ? 35.730  -4.517  19.466  1.00 37.87 ? 51  HIS A CG    1 
ATOM   192  N ND1   . HIS A 1 28  ? 35.402  -5.192  20.626  1.00 43.66 ? 51  HIS A ND1   1 
ATOM   193  C CD2   . HIS A 1 28  ? 35.955  -5.469  18.529  1.00 40.10 ? 51  HIS A CD2   1 
ATOM   194  C CE1   . HIS A 1 28  ? 35.428  -6.494  20.399  1.00 43.70 ? 51  HIS A CE1   1 
ATOM   195  N NE2   . HIS A 1 28  ? 35.761  -6.689  19.134  1.00 42.57 ? 51  HIS A NE2   1 
ATOM   196  N N     . SER A 1 29  ? 33.605  -0.156  19.032  1.00 27.02 ? 52  SER A N     1 
ATOM   197  C CA    . SER A 1 29  ? 33.670  1.292   18.857  1.00 26.16 ? 52  SER A CA    1 
ATOM   198  C C     . SER A 1 29  ? 33.236  2.056   20.098  1.00 26.17 ? 52  SER A C     1 
ATOM   199  O O     . SER A 1 29  ? 33.438  3.274   20.160  1.00 23.92 ? 52  SER A O     1 
ATOM   200  C CB    . SER A 1 29  ? 32.806  1.725   17.665  1.00 26.98 ? 52  SER A CB    1 
ATOM   201  O OG    . SER A 1 29  ? 31.421  1.539   17.931  1.00 26.55 ? 52  SER A OG    1 
ATOM   202  N N     . GLY A 1 30  ? 32.640  1.386   21.080  1.00 25.53 ? 53  GLY A N     1 
ATOM   203  C CA    . GLY A 1 30  ? 32.116  2.106   22.225  1.00 26.80 ? 53  GLY A CA    1 
ATOM   204  C C     . GLY A 1 30  ? 30.842  2.885   21.963  1.00 23.29 ? 53  GLY A C     1 
ATOM   205  O O     . GLY A 1 30  ? 30.346  3.549   22.878  1.00 28.50 ? 53  GLY A O     1 
ATOM   206  N N     . LEU A 1 31  ? 30.267  2.816   20.707  1.00 20.33 ? 54  LEU A N     1 
ATOM   207  C CA    . LEU A 1 31  ? 29.042  3.529   20.367  1.00 23.55 ? 54  LEU A CA    1 
ATOM   208  C C     . LEU A 1 31  ? 27.856  2.571   20.333  1.00 20.91 ? 54  LEU A C     1 
ATOM   209  O O     . LEU A 1 31  ? 28.011  1.391   19.980  1.00 23.44 ? 54  LEU A O     1 
ATOM   210  C CB    . LEU A 1 31  ? 29.176  4.224   19.005  1.00 20.63 ? 54  LEU A CB    1 
ATOM   211  C CG    . LEU A 1 31  ? 30.327  5.221   18.840  1.00 26.04 ? 54  LEU A CG    1 
ATOM   212  C CD1   . LEU A 1 31  ? 30.425  5.728   17.389  1.00 21.45 ? 54  LEU A CD1   1 
ATOM   213  C CD2   . LEU A 1 31  ? 30.172  6.391   19.807  1.00 22.54 ? 54  LEU A CD2   1 
ATOM   214  N N     . PRO A 1 32  ? 26.670  3.051   20.708  1.00 23.70 ? 55  PRO A N     1 
ATOM   215  C CA    . PRO A 1 32  ? 25.477  2.188   20.695  1.00 21.79 ? 55  PRO A CA    1 
ATOM   216  C C     . PRO A 1 32  ? 25.016  1.900   19.273  1.00 24.52 ? 55  PRO A C     1 
ATOM   217  O O     . PRO A 1 32  ? 25.452  2.530   18.306  1.00 20.82 ? 55  PRO A O     1 
ATOM   218  C CB    . PRO A 1 32  ? 24.438  3.014   21.457  1.00 26.14 ? 55  PRO A CB    1 
ATOM   219  C CG    . PRO A 1 32  ? 24.833  4.446   21.189  1.00 22.13 ? 55  PRO A CG    1 
ATOM   220  C CD    . PRO A 1 32  ? 26.359  4.417   21.177  1.00 22.90 ? 55  PRO A CD    1 
ATOM   221  N N     . VAL A 1 33  ? 24.101  0.935   19.153  1.00 21.08 ? 56  VAL A N     1 
ATOM   222  C CA    . VAL A 1 33  ? 23.534  0.541   17.866  1.00 21.27 ? 56  VAL A CA    1 
ATOM   223  C C     . VAL A 1 33  ? 22.061  0.940   17.835  1.00 23.92 ? 56  VAL A C     1 
ATOM   224  O O     . VAL A 1 33  ? 21.374  0.895   18.867  1.00 21.88 ? 56  VAL A O     1 
ATOM   225  C CB    . VAL A 1 33  ? 23.699  -0.972  17.612  1.00 21.63 ? 56  VAL A CB    1 
ATOM   226  C CG1   . VAL A 1 33  ? 22.936  -1.397  16.360  1.00 17.72 ? 56  VAL A CG1   1 
ATOM   227  C CG2   . VAL A 1 33  ? 25.181  -1.360  17.506  1.00 25.20 ? 56  VAL A CG2   1 
ATOM   228  N N     . LEU A 1 34  ? 21.582  1.341   16.651  1.00 18.28 ? 57  LEU A N     1 
ATOM   229  C CA    . LEU A 1 34  ? 20.187  1.706   16.413  1.00 18.66 ? 57  LEU A CA    1 
ATOM   230  C C     . LEU A 1 34  ? 19.546  0.683   15.478  1.00 21.00 ? 57  LEU A C     1 
ATOM   231  O O     . LEU A 1 34  ? 20.032  0.479   14.362  1.00 20.48 ? 57  LEU A O     1 
ATOM   232  C CB    . LEU A 1 34  ? 20.099  3.107   15.795  1.00 19.53 ? 57  LEU A CB    1 
ATOM   233  C CG    . LEU A 1 34  ? 18.698  3.639   15.474  1.00 21.06 ? 57  LEU A CG    1 
ATOM   234  C CD1   . LEU A 1 34  ? 17.810  3.631   16.746  1.00 19.34 ? 57  LEU A CD1   1 
ATOM   235  C CD2   . LEU A 1 34  ? 18.785  5.052   14.851  1.00 14.39 ? 57  LEU A CD2   1 
ATOM   236  N N     . GLU A 1 35  ? 18.443  0.064   15.918  1.00 20.95 ? 58  GLU A N     1 
ATOM   237  C CA    . GLU A 1 35  ? 17.676  -0.869  15.097  1.00 22.73 ? 58  GLU A CA    1 
ATOM   238  C C     . GLU A 1 35  ? 16.296  -0.270  14.830  1.00 22.39 ? 58  GLU A C     1 
ATOM   239  O O     . GLU A 1 35  ? 15.686  0.305   15.728  1.00 21.83 ? 58  GLU A O     1 
ATOM   240  C CB    . GLU A 1 35  ? 17.547  -2.258  15.781  1.00 20.95 ? 58  GLU A CB    1 
ATOM   241  C CG    . GLU A 1 35  ? 16.886  -3.319  14.878  1.00 25.33 ? 58  GLU A CG    1 
ATOM   242  C CD    . GLU A 1 35  ? 16.445  -4.600  15.600  1.00 31.68 ? 58  GLU A CD    1 
ATOM   243  O OE1   . GLU A 1 35  ? 15.704  -5.408  14.983  1.00 31.74 ? 58  GLU A OE1   1 
ATOM   244  O OE2   . GLU A 1 35  ? 16.834  -4.818  16.770  1.00 29.60 ? 58  GLU A OE2   1 
ATOM   245  N N     . LEU A 1 36  ? 15.819  -0.377  13.592  1.00 20.73 ? 59  LEU A N     1 
ATOM   246  C CA    . LEU A 1 36  ? 14.494  0.104   13.199  1.00 20.85 ? 59  LEU A CA    1 
ATOM   247  C C     . LEU A 1 36  ? 13.625  -1.092  12.823  1.00 24.28 ? 59  LEU A C     1 
ATOM   248  O O     . LEU A 1 36  ? 14.037  -1.925  12.009  1.00 21.04 ? 59  LEU A O     1 
ATOM   249  C CB    . LEU A 1 36  ? 14.587  1.088   12.016  1.00 17.28 ? 59  LEU A CB    1 
ATOM   250  C CG    . LEU A 1 36  ? 15.631  2.206   12.154  1.00 20.89 ? 59  LEU A CG    1 
ATOM   251  C CD1   . LEU A 1 36  ? 15.642  3.122   10.932  1.00 20.60 ? 59  LEU A CD1   1 
ATOM   252  C CD2   . LEU A 1 36  ? 15.345  3.033   13.436  1.00 17.69 ? 59  LEU A CD2   1 
ATOM   253  N N     . GLY A 1 37  ? 12.442  -1.178  13.431  1.00 20.38 ? 60  GLY A N     1 
ATOM   254  C CA    . GLY A 1 37  ? 11.469  -2.206  13.134  1.00 23.70 ? 60  GLY A CA    1 
ATOM   255  C C     . GLY A 1 37  ? 11.825  -3.607  13.618  1.00 23.00 ? 60  GLY A C     1 
ATOM   256  O O     . GLY A 1 37  ? 11.863  -4.552  12.835  1.00 24.79 ? 60  GLY A O     1 
ATOM   257  N N     . PRO A 1 38  ? 12.074  -3.777  14.916  1.00 20.99 ? 61  PRO A N     1 
ATOM   258  C CA    . PRO A 1 38  ? 12.537  -5.100  15.405  1.00 23.65 ? 61  PRO A CA    1 
ATOM   259  C C     . PRO A 1 38  ? 11.508  -6.228  15.301  1.00 24.70 ? 61  PRO A C     1 
ATOM   260  O O     . PRO A 1 38  ? 11.911  -7.394  15.210  1.00 28.18 ? 61  PRO A O     1 
ATOM   261  C CB    . PRO A 1 38  ? 12.908  -4.816  16.865  1.00 21.57 ? 61  PRO A CB    1 
ATOM   262  C CG    . PRO A 1 38  ? 12.042  -3.621  17.235  1.00 22.38 ? 61  PRO A CG    1 
ATOM   263  C CD    . PRO A 1 38  ? 12.029  -2.777  15.994  1.00 21.53 ? 61  PRO A CD    1 
ATOM   264  N N     . GLY A 1 39  ? 10.212  -5.943  15.322  1.00 24.47 ? 62  GLY A N     1 
ATOM   265  C CA    . GLY A 1 39  ? 9.234   -6.995  15.049  1.00 26.99 ? 62  GLY A CA    1 
ATOM   266  C C     . GLY A 1 39  ? 9.309   -8.132  16.066  1.00 24.54 ? 62  GLY A C     1 
ATOM   267  O O     . GLY A 1 39  ? 9.168   -7.922  17.271  1.00 27.06 ? 62  GLY A O     1 
ATOM   268  N N     . THR A 1 40  ? 9.557   -9.357  15.596  1.00 23.21 ? 63  THR A N     1 
ATOM   269  C CA    . THR A 1 40  ? 9.668   -10.500 16.501  1.00 29.47 ? 63  THR A CA    1 
ATOM   270  C C     . THR A 1 40  ? 11.035  -10.617 17.166  1.00 28.72 ? 63  THR A C     1 
ATOM   271  O O     . THR A 1 40  ? 11.189  -11.434 18.076  1.00 26.76 ? 63  THR A O     1 
ATOM   272  C CB    . THR A 1 40  ? 9.372   -11.809 15.762  1.00 30.78 ? 63  THR A CB    1 
ATOM   273  O OG1   . THR A 1 40  ? 10.363  -12.031 14.745  1.00 31.28 ? 63  THR A OG1   1 
ATOM   274  C CG2   . THR A 1 40  ? 7.990   -11.761 15.135  1.00 35.92 ? 63  THR A CG2   1 
ATOM   275  N N     . GLY A 1 41  ? 12.033  -9.854  16.728  1.00 24.49 ? 64  GLY A N     1 
ATOM   276  C CA    . GLY A 1 41  ? 13.310  -9.841  17.407  1.00 20.71 ? 64  GLY A CA    1 
ATOM   277  C C     . GLY A 1 41  ? 14.414  -10.649 16.766  1.00 25.19 ? 64  GLY A C     1 
ATOM   278  O O     . GLY A 1 41  ? 15.464  -10.832 17.396  1.00 24.43 ? 64  GLY A O     1 
ATOM   279  N N     . VAL A 1 42  ? 14.221  -11.130 15.537  1.00 22.17 ? 65  VAL A N     1 
ATOM   280  C CA    . VAL A 1 42  ? 15.230  -11.975 14.910  1.00 23.23 ? 65  VAL A CA    1 
ATOM   281  C C     . VAL A 1 42  ? 16.512  -11.182 14.624  1.00 26.11 ? 65  VAL A C     1 
ATOM   282  O O     . VAL A 1 42  ? 17.624  -11.699 14.783  1.00 23.07 ? 65  VAL A O     1 
ATOM   283  C CB    . VAL A 1 42  ? 14.649  -12.637 13.642  1.00 29.49 ? 65  VAL A CB    1 
ATOM   284  C CG1   . VAL A 1 42  ? 14.072  -11.602 12.702  1.00 31.31 ? 65  VAL A CG1   1 
ATOM   285  C CG2   . VAL A 1 42  ? 15.717  -13.463 12.930  1.00 34.23 ? 65  VAL A CG2   1 
ATOM   286  N N     . ILE A 1 43  ? 16.386  -9.912  14.222  1.00 24.31 ? 66  ILE A N     1 
ATOM   287  C CA    . ILE A 1 43  ? 17.579  -9.095  14.018  1.00 23.88 ? 66  ILE A CA    1 
ATOM   288  C C     . ILE A 1 43  ? 18.144  -8.643  15.357  1.00 24.72 ? 66  ILE A C     1 
ATOM   289  O O     . ILE A 1 43  ? 19.364  -8.648  15.558  1.00 25.72 ? 66  ILE A O     1 
ATOM   290  C CB    . ILE A 1 43  ? 17.261  -7.910  13.082  1.00 26.41 ? 66  ILE A CB    1 
ATOM   291  C CG1   . ILE A 1 43  ? 16.733  -8.437  11.744  1.00 27.95 ? 66  ILE A CG1   1 
ATOM   292  C CG2   . ILE A 1 43  ? 18.504  -7.054  12.810  1.00 24.77 ? 66  ILE A CG2   1 
ATOM   293  C CD1   . ILE A 1 43  ? 16.382  -7.353  10.751  1.00 28.75 ? 66  ILE A CD1   1 
ATOM   294  N N     . THR A 1 44  ? 17.265  -8.283  16.299  1.00 24.90 ? 67  THR A N     1 
ATOM   295  C CA    . THR A 1 44  ? 17.688  -7.963  17.661  1.00 24.85 ? 67  THR A CA    1 
ATOM   296  C C     . THR A 1 44  ? 18.627  -9.028  18.208  1.00 23.10 ? 67  THR A C     1 
ATOM   297  O O     . THR A 1 44  ? 19.695  -8.726  18.755  1.00 22.59 ? 67  THR A O     1 
ATOM   298  C CB    . THR A 1 44  ? 16.470  -7.854  18.587  1.00 21.42 ? 67  THR A CB    1 
ATOM   299  O OG1   . THR A 1 44  ? 15.516  -6.926  18.059  1.00 24.58 ? 67  THR A OG1   1 
ATOM   300  C CG2   . THR A 1 44  ? 16.913  -7.411  19.958  1.00 20.92 ? 67  THR A CG2   1 
ATOM   301  N N     . LYS A 1 45  ? 18.215  -10.289 18.085  1.00 23.48 ? 68  LYS A N     1 
ATOM   302  C CA    . LYS A 1 45  ? 19.034  -11.413 18.536  1.00 23.39 ? 68  LYS A CA    1 
ATOM   303  C C     . LYS A 1 45  ? 20.410  -11.408 17.876  1.00 23.24 ? 68  LYS A C     1 
ATOM   304  O O     . LYS A 1 45  ? 21.438  -11.570 18.548  1.00 23.15 ? 68  LYS A O     1 
ATOM   305  C CB    . LYS A 1 45  ? 18.297  -12.722 18.234  1.00 24.63 ? 68  LYS A CB    1 
ATOM   306  C CG    . LYS A 1 45  ? 18.812  -13.902 19.010  1.00 30.99 ? 68  LYS A CG    1 
ATOM   307  C CD    . LYS A 1 45  ? 18.740  -15.191 18.205  1.00 36.53 ? 68  LYS A CD    1 
ATOM   308  C CE    . LYS A 1 45  ? 17.331  -15.685 18.054  1.00 42.32 ? 68  LYS A CE    1 
ATOM   309  N NZ    . LYS A 1 45  ? 17.287  -17.183 17.952  1.00 48.37 ? 68  LYS A NZ    1 
ATOM   310  N N     . ALA A 1 46  ? 20.448  -11.230 16.549  1.00 24.14 ? 69  ALA A N     1 
ATOM   311  C CA    . ALA A 1 46  ? 21.724  -11.208 15.830  1.00 24.07 ? 69  ALA A CA    1 
ATOM   312  C C     . ALA A 1 46  ? 22.600  -10.042 16.279  1.00 24.44 ? 69  ALA A C     1 
ATOM   313  O O     . ALA A 1 46  ? 23.834  -10.157 16.335  1.00 25.55 ? 69  ALA A O     1 
ATOM   314  C CB    . ALA A 1 46  ? 21.474  -11.128 14.324  1.00 20.41 ? 69  ALA A CB    1 
ATOM   315  N N     . ILE A 1 47  ? 21.985  -8.900  16.585  1.00 23.03 ? 70  ILE A N     1 
ATOM   316  C CA    . ILE A 1 47  ? 22.758  -7.760  17.075  1.00 20.60 ? 70  ILE A CA    1 
ATOM   317  C C     . ILE A 1 47  ? 23.394  -8.097  18.422  1.00 23.76 ? 70  ILE A C     1 
ATOM   318  O O     . ILE A 1 47  ? 24.590  -7.875  18.648  1.00 24.82 ? 70  ILE A O     1 
ATOM   319  C CB    . ILE A 1 47  ? 21.865  -6.512  17.175  1.00 19.69 ? 70  ILE A CB    1 
ATOM   320  C CG1   . ILE A 1 47  ? 21.469  -6.020  15.788  1.00 23.25 ? 70  ILE A CG1   1 
ATOM   321  C CG2   . ILE A 1 47  ? 22.581  -5.406  17.953  1.00 22.09 ? 70  ILE A CG2   1 
ATOM   322  C CD1   . ILE A 1 47  ? 20.387  -4.930  15.808  1.00 23.53 ? 70  ILE A CD1   1 
ATOM   323  N N     . LEU A 1 48  ? 22.596  -8.627  19.345  1.00 23.90 ? 71  LEU A N     1 
ATOM   324  C CA    . LEU A 1 48  ? 23.133  -9.019  20.645  1.00 23.83 ? 71  LEU A CA    1 
ATOM   325  C C     . LEU A 1 48  ? 24.197  -10.112 20.520  1.00 28.19 ? 71  LEU A C     1 
ATOM   326  O O     . LEU A 1 48  ? 25.130  -10.160 21.327  1.00 28.40 ? 71  LEU A O     1 
ATOM   327  C CB    . LEU A 1 48  ? 21.990  -9.476  21.554  1.00 28.70 ? 71  LEU A CB    1 
ATOM   328  C CG    . LEU A 1 48  ? 20.924  -8.419  21.856  1.00 28.04 ? 71  LEU A CG    1 
ATOM   329  C CD1   . LEU A 1 48  ? 19.817  -9.013  22.720  1.00 28.62 ? 71  LEU A CD1   1 
ATOM   330  C CD2   . LEU A 1 48  ? 21.545  -7.193  22.523  1.00 27.85 ? 71  LEU A CD2   1 
ATOM   331  N N     . ALA A 1 49  ? 24.093  -10.985 19.512  1.00 26.83 ? 72  ALA A N     1 
ATOM   332  C CA    . ALA A 1 49  ? 25.112  -12.019 19.332  1.00 27.72 ? 72  ALA A CA    1 
ATOM   333  C C     . ALA A 1 49  ? 26.476  -11.435 18.960  1.00 28.52 ? 72  ALA A C     1 
ATOM   334  O O     . ALA A 1 49  ? 27.486  -12.128 19.081  1.00 25.08 ? 72  ALA A O     1 
ATOM   335  C CB    . ALA A 1 49  ? 24.663  -13.033 18.273  1.00 22.56 ? 72  ALA A CB    1 
ATOM   336  N N     . ARG A 1 50  ? 26.541  -10.180 18.516  1.00 27.81 ? 73  ARG A N     1 
ATOM   337  C CA    . ARG A 1 50  ? 27.837  -9.547  18.280  1.00 26.23 ? 73  ARG A CA    1 
ATOM   338  C C     . ARG A 1 50  ? 28.532  -9.120  19.570  1.00 31.30 ? 73  ARG A C     1 
ATOM   339  O O     . ARG A 1 50  ? 29.687  -8.674  19.521  1.00 28.71 ? 73  ARG A O     1 
ATOM   340  C CB    . ARG A 1 50  ? 27.690  -8.318  17.363  1.00 27.01 ? 73  ARG A CB    1 
ATOM   341  C CG    . ARG A 1 50  ? 27.049  -8.583  15.998  1.00 22.86 ? 73  ARG A CG    1 
ATOM   342  C CD    . ARG A 1 50  ? 27.968  -9.394  15.056  1.00 24.58 ? 73  ARG A CD    1 
ATOM   343  N NE    . ARG A 1 50  ? 29.394  -9.081  15.198  1.00 29.04 ? 73  ARG A NE    1 
ATOM   344  C CZ    . ARG A 1 50  ? 30.026  -8.108  14.546  1.00 27.72 ? 73  ARG A CZ    1 
ATOM   345  N NH1   . ARG A 1 50  ? 29.363  -7.330  13.697  1.00 26.04 ? 73  ARG A NH1   1 
ATOM   346  N NH2   . ARG A 1 50  ? 31.320  -7.900  14.751  1.00 24.90 ? 73  ARG A NH2   1 
ATOM   347  N N     . GLY A 1 51  ? 27.874  -9.239  20.720  1.00 29.07 ? 74  GLY A N     1 
ATOM   348  C CA    . GLY A 1 51  ? 28.455  -8.756  21.960  1.00 29.65 ? 74  GLY A CA    1 
ATOM   349  C C     . GLY A 1 51  ? 28.104  -7.327  22.312  1.00 34.22 ? 74  GLY A C     1 
ATOM   350  O O     . GLY A 1 51  ? 28.762  -6.738  23.177  1.00 35.64 ? 74  GLY A O     1 
ATOM   351  N N     . ILE A 1 52  ? 27.106  -6.743  21.650  1.00 32.14 ? 75  ILE A N     1 
ATOM   352  C CA    . ILE A 1 52  ? 26.587  -5.438  22.043  1.00 34.49 ? 75  ILE A CA    1 
ATOM   353  C C     . ILE A 1 52  ? 25.864  -5.574  23.378  1.00 34.98 ? 75  ILE A C     1 
ATOM   354  O O     . ILE A 1 52  ? 24.959  -6.411  23.523  1.00 32.89 ? 75  ILE A O     1 
ATOM   355  C CB    . ILE A 1 52  ? 25.645  -4.898  20.953  1.00 30.19 ? 75  ILE A CB    1 
ATOM   356  C CG1   . ILE A 1 52  ? 26.410  -4.598  19.646  1.00 35.37 ? 75  ILE A CG1   1 
ATOM   357  C CG2   . ILE A 1 52  ? 24.868  -3.692  21.447  1.00 29.39 ? 75  ILE A CG2   1 
ATOM   358  C CD1   . ILE A 1 52  ? 27.563  -3.621  19.772  1.00 28.95 ? 75  ILE A CD1   1 
ATOM   359  N N     . LYS A 1 53  ? 26.257  -4.761  24.361  1.00 32.32 ? 76  LYS A N     1 
ATOM   360  C CA    . LYS A 1 53  ? 25.533  -4.740  25.631  1.00 31.34 ? 76  LYS A CA    1 
ATOM   361  C C     . LYS A 1 53  ? 24.064  -4.410  25.372  1.00 27.84 ? 76  LYS A C     1 
ATOM   362  O O     . LYS A 1 53  ? 23.763  -3.556  24.535  1.00 30.09 ? 76  LYS A O     1 
ATOM   363  C CB    . LYS A 1 53  ? 26.124  -3.710  26.603  1.00 36.81 ? 76  LYS A CB    1 
ATOM   364  C CG    . LYS A 1 53  ? 27.622  -3.860  26.879  1.00 40.87 ? 76  LYS A CG    1 
ATOM   365  C CD    . LYS A 1 53  ? 28.250  -2.517  27.297  1.00 53.64 ? 76  LYS A CD    1 
ATOM   366  C CE    . LYS A 1 53  ? 29.316  -2.020  26.306  1.00 50.77 ? 76  LYS A CE    1 
ATOM   367  N NZ    . LYS A 1 53  ? 30.682  -2.543  26.591  1.00 52.95 ? 76  LYS A NZ    1 
ATOM   368  N N     . PRO A 1 54  ? 23.128  -5.069  26.055  1.00 28.74 ? 77  PRO A N     1 
ATOM   369  C CA    . PRO A 1 54  ? 21.708  -4.814  25.746  1.00 29.60 ? 77  PRO A CA    1 
ATOM   370  C C     . PRO A 1 54  ? 21.325  -3.358  25.915  1.00 27.57 ? 77  PRO A C     1 
ATOM   371  O O     . PRO A 1 54  ? 20.556  -2.829  25.109  1.00 26.74 ? 77  PRO A O     1 
ATOM   372  C CB    . PRO A 1 54  ? 20.962  -5.729  26.732  1.00 24.87 ? 77  PRO A CB    1 
ATOM   373  C CG    . PRO A 1 54  ? 21.921  -6.799  27.042  1.00 27.69 ? 77  PRO A CG    1 
ATOM   374  C CD    . PRO A 1 54  ? 23.300  -6.188  26.997  1.00 29.99 ? 77  PRO A CD    1 
ATOM   375  N N     . GLU A 1 55  ? 21.899  -2.675  26.905  1.00 28.04 ? 78  GLU A N     1 
ATOM   376  C CA    . GLU A 1 55  ? 21.557  -1.279  27.149  1.00 34.34 ? 78  GLU A CA    1 
ATOM   377  C C     . GLU A 1 55  ? 22.096  -0.350  26.065  1.00 30.10 ? 78  GLU A C     1 
ATOM   378  O O     . GLU A 1 55  ? 21.644  0.796   25.971  1.00 27.67 ? 78  GLU A O     1 
ATOM   379  C CB    . GLU A 1 55  ? 22.086  -0.842  28.520  1.00 31.21 ? 78  GLU A CB    1 
ATOM   380  C CG    . GLU A 1 55  ? 21.396  -1.511  29.711  1.00 37.41 ? 78  GLU A CG    1 
ATOM   381  C CD    . GLU A 1 55  ? 21.909  -2.926  30.009  1.00 44.17 ? 78  GLU A CD    1 
ATOM   382  O OE1   . GLU A 1 55  ? 22.924  -3.362  29.407  1.00 38.27 ? 78  GLU A OE1   1 
ATOM   383  O OE2   . GLU A 1 55  ? 21.296  -3.601  30.871  1.00 47.70 ? 78  GLU A OE2   1 
ATOM   384  N N     . SER A 1 56  ? 23.045  -0.814  25.254  1.00 25.34 ? 79  SER A N     1 
ATOM   385  C CA    . SER A 1 56  ? 23.577  -0.044  24.139  1.00 28.03 ? 79  SER A CA    1 
ATOM   386  C C     . SER A 1 56  ? 22.876  -0.353  22.820  1.00 27.70 ? 79  SER A C     1 
ATOM   387  O O     . SER A 1 56  ? 23.377  0.039   21.756  1.00 28.40 ? 79  SER A O     1 
ATOM   388  C CB    . SER A 1 56  ? 25.083  -0.295  23.993  1.00 28.88 ? 79  SER A CB    1 
ATOM   389  O OG    . SER A 1 56  ? 25.760  0.067   25.183  1.00 32.45 ? 79  SER A OG    1 
ATOM   390  N N     . LEU A 1 57  ? 21.752  -1.057  22.858  1.00 24.32 ? 80  LEU A N     1 
ATOM   391  C CA    . LEU A 1 57  ? 20.913  -1.248  21.683  1.00 23.26 ? 80  LEU A CA    1 
ATOM   392  C C     . LEU A 1 57  ? 19.622  -0.475  21.886  1.00 23.29 ? 80  LEU A C     1 
ATOM   393  O O     . LEU A 1 57  ? 18.881  -0.744  22.841  1.00 25.49 ? 80  LEU A O     1 
ATOM   394  C CB    . LEU A 1 57  ? 20.613  -2.729  21.438  1.00 22.99 ? 80  LEU A CB    1 
ATOM   395  C CG    . LEU A 1 57  ? 19.625  -3.008  20.295  1.00 21.10 ? 80  LEU A CG    1 
ATOM   396  C CD1   . LEU A 1 57  ? 20.110  -2.387  18.981  1.00 20.86 ? 80  LEU A CD1   1 
ATOM   397  C CD2   . LEU A 1 57  ? 19.397  -4.517  20.121  1.00 21.43 ? 80  LEU A CD2   1 
ATOM   398  N N     . THR A 1 58  ? 19.358  0.480   20.997  1.00 23.01 ? 81  THR A N     1 
ATOM   399  C CA    . THR A 1 58  ? 18.071  1.164   20.921  1.00 21.69 ? 81  THR A CA    1 
ATOM   400  C C     . THR A 1 58  ? 17.326  0.655   19.695  1.00 19.84 ? 81  THR A C     1 
ATOM   401  O O     . THR A 1 58  ? 17.891  0.623   18.594  1.00 21.25 ? 81  THR A O     1 
ATOM   402  C CB    . THR A 1 58  ? 18.261  2.686   20.832  1.00 22.30 ? 81  THR A CB    1 
ATOM   403  O OG1   . THR A 1 58  ? 18.894  3.168   22.022  1.00 21.83 ? 81  THR A OG1   1 
ATOM   404  C CG2   . THR A 1 58  ? 16.925  3.383   20.651  1.00 23.37 ? 81  THR A CG2   1 
ATOM   405  N N     . ALA A 1 59  ? 16.067  0.255   19.879  1.00 22.51 ? 82  ALA A N     1 
ATOM   406  C CA    . ALA A 1 59  ? 15.267  -0.339  18.810  1.00 21.04 ? 82  ALA A CA    1 
ATOM   407  C C     . ALA A 1 59  ? 13.881  0.282   18.808  1.00 23.20 ? 82  ALA A C     1 
ATOM   408  O O     . ALA A 1 59  ? 13.173  0.227   19.823  1.00 22.11 ? 82  ALA A O     1 
ATOM   409  C CB    . ALA A 1 59  ? 15.164  -1.862  18.967  1.00 18.75 ? 82  ALA A CB    1 
ATOM   410  N N     . ILE A 1 60  ? 13.481  0.830   17.660  1.00 22.24 ? 83  ILE A N     1 
ATOM   411  C CA    . ILE A 1 60  ? 12.264  1.632   17.538  1.00 21.13 ? 83  ILE A CA    1 
ATOM   412  C C     . ILE A 1 60  ? 11.210  0.796   16.827  1.00 21.82 ? 83  ILE A C     1 
ATOM   413  O O     . ILE A 1 60  ? 11.406  0.398   15.671  1.00 22.67 ? 83  ILE A O     1 
ATOM   414  C CB    . ILE A 1 60  ? 12.519  2.939   16.767  1.00 23.87 ? 83  ILE A CB    1 
ATOM   415  C CG1   . ILE A 1 60  ? 13.648  3.748   17.422  1.00 18.26 ? 83  ILE A CG1   1 
ATOM   416  C CG2   . ILE A 1 60  ? 11.215  3.748   16.659  1.00 25.18 ? 83  ILE A CG2   1 
ATOM   417  C CD1   . ILE A 1 60  ? 13.929  5.128   16.758  1.00 19.82 ? 83  ILE A CD1   1 
ATOM   418  N N     . GLU A 1 61  ? 10.082  0.558   17.501  1.00 23.10 ? 84  GLU A N     1 
ATOM   419  C CA    . GLU A 1 61  ? 9.039   -0.340  17.011  1.00 21.95 ? 84  GLU A CA    1 
ATOM   420  C C     . GLU A 1 61  ? 7.687   0.354   17.091  1.00 24.55 ? 84  GLU A C     1 
ATOM   421  O O     . GLU A 1 61  ? 7.262   0.770   18.178  1.00 22.10 ? 84  GLU A O     1 
ATOM   422  C CB    . GLU A 1 61  ? 9.010   -1.633  17.830  1.00 24.08 ? 84  GLU A CB    1 
ATOM   423  C CG    . GLU A 1 61  ? 7.812   -2.524  17.503  1.00 24.65 ? 84  GLU A CG    1 
ATOM   424  C CD    . GLU A 1 61  ? 7.727   -2.837  16.011  1.00 25.13 ? 84  GLU A CD    1 
ATOM   425  O OE1   . GLU A 1 61  ? 6.667   -2.572  15.390  1.00 24.03 ? 84  GLU A OE1   1 
ATOM   426  O OE2   . GLU A 1 61  ? 8.735   -3.335  15.461  1.00 23.10 ? 84  GLU A OE2   1 
ATOM   427  N N     . TYR A 1 62  ? 6.995   0.457   15.954  1.00 20.51 ? 85  TYR A N     1 
ATOM   428  C CA    . TYR A 1 62  ? 5.716   1.166   15.965  1.00 24.40 ? 85  TYR A CA    1 
ATOM   429  C C     . TYR A 1 62  ? 4.614   0.333   16.625  1.00 29.88 ? 85  TYR A C     1 
ATOM   430  O O     . TYR A 1 62  ? 3.764   0.883   17.338  1.00 26.01 ? 85  TYR A O     1 
ATOM   431  C CB    . TYR A 1 62  ? 5.308   1.578   14.551  1.00 24.83 ? 85  TYR A CB    1 
ATOM   432  C CG    . TYR A 1 62  ? 4.115   2.514   14.539  1.00 26.32 ? 85  TYR A CG    1 
ATOM   433  C CD1   . TYR A 1 62  ? 4.281   3.887   14.664  1.00 27.45 ? 85  TYR A CD1   1 
ATOM   434  C CD2   . TYR A 1 62  ? 2.818   2.017   14.427  1.00 27.30 ? 85  TYR A CD2   1 
ATOM   435  C CE1   . TYR A 1 62  ? 3.180   4.752   14.673  1.00 28.25 ? 85  TYR A CE1   1 
ATOM   436  C CE2   . TYR A 1 62  ? 1.714   2.865   14.433  1.00 27.16 ? 85  TYR A CE2   1 
ATOM   437  C CZ    . TYR A 1 62  ? 1.900   4.230   14.553  1.00 31.98 ? 85  TYR A CZ    1 
ATOM   438  O OH    . TYR A 1 62  ? 0.804   5.069   14.557  1.00 27.18 ? 85  TYR A OH    1 
ATOM   439  N N     . SER A 1 63  ? 4.599   -0.986  16.400  1.00 25.33 ? 86  SER A N     1 
ATOM   440  C CA    . SER A 1 63  ? 3.514   -1.821  16.913  1.00 25.77 ? 86  SER A CA    1 
ATOM   441  C C     . SER A 1 63  ? 3.634   -1.951  18.422  1.00 29.21 ? 86  SER A C     1 
ATOM   442  O O     . SER A 1 63  ? 4.655   -2.429  18.930  1.00 29.15 ? 86  SER A O     1 
ATOM   443  C CB    . SER A 1 63  ? 3.526   -3.206  16.270  1.00 28.95 ? 86  SER A CB    1 
ATOM   444  O OG    . SER A 1 63  ? 2.787   -4.129  17.068  1.00 29.61 ? 86  SER A OG    1 
ATOM   445  N N     . THR A 1 64  ? 2.592   -1.520  19.138  1.00 31.16 ? 87  THR A N     1 
ATOM   446  C CA    . THR A 1 64  ? 2.589   -1.640  20.594  1.00 30.08 ? 87  THR A CA    1 
ATOM   447  C C     . THR A 1 64  ? 2.545   -3.095  21.045  1.00 27.81 ? 87  THR A C     1 
ATOM   448  O O     . THR A 1 64  ? 3.160   -3.443  22.059  1.00 30.82 ? 87  THR A O     1 
ATOM   449  C CB    . THR A 1 64  ? 1.411   -0.847  21.172  1.00 30.76 ? 87  THR A CB    1 
ATOM   450  O OG1   . THR A 1 64  ? 1.570   0.535   20.826  1.00 33.66 ? 87  THR A OG1   1 
ATOM   451  C CG2   . THR A 1 64  ? 1.381   -0.959  22.688  1.00 29.55 ? 87  THR A CG2   1 
ATOM   452  N N     . ASP A 1 65  ? 1.852   -3.960  20.303  1.00 31.50 ? 88  ASP A N     1 
ATOM   453  C CA    . ASP A 1 65  ? 1.848   -5.385  20.640  1.00 31.98 ? 88  ASP A CA    1 
ATOM   454  C C     . ASP A 1 65  ? 3.250   -5.980  20.520  1.00 33.07 ? 88  ASP A C     1 
ATOM   455  O O     . ASP A 1 65  ? 3.736   -6.647  21.440  1.00 29.54 ? 88  ASP A O     1 
ATOM   456  C CB    . ASP A 1 65  ? 0.867   -6.142  19.737  1.00 27.31 ? 88  ASP A CB    1 
ATOM   457  C CG    . ASP A 1 65  ? -0.593  -5.899  20.116  1.00 45.72 ? 88  ASP A CG    1 
ATOM   458  O OD1   . ASP A 1 65  ? -0.861  -5.628  21.312  1.00 48.76 ? 88  ASP A OD1   1 
ATOM   459  O OD2   . ASP A 1 65  ? -1.469  -5.981  19.219  1.00 45.63 ? 88  ASP A OD2   1 
ATOM   460  N N     . PHE A 1 66  ? 3.914   -5.765  19.379  1.00 28.79 ? 89  PHE A N     1 
ATOM   461  C CA    . PHE A 1 66  ? 5.295   -6.229  19.242  1.00 27.59 ? 89  PHE A CA    1 
ATOM   462  C C     . PHE A 1 66  ? 6.184   -5.649  20.331  1.00 24.51 ? 89  PHE A C     1 
ATOM   463  O O     . PHE A 1 66  ? 7.041   -6.348  20.886  1.00 26.84 ? 89  PHE A O     1 
ATOM   464  C CB    . PHE A 1 66  ? 5.850   -5.841  17.877  1.00 25.35 ? 89  PHE A CB    1 
ATOM   465  C CG    . PHE A 1 66  ? 5.384   -6.712  16.760  1.00 32.85 ? 89  PHE A CG    1 
ATOM   466  C CD1   . PHE A 1 66  ? 5.089   -8.051  16.981  1.00 39.07 ? 89  PHE A CD1   1 
ATOM   467  C CD2   . PHE A 1 66  ? 5.271   -6.201  15.468  1.00 32.06 ? 89  PHE A CD2   1 
ATOM   468  C CE1   . PHE A 1 66  ? 4.682   -8.868  15.929  1.00 38.26 ? 89  PHE A CE1   1 
ATOM   469  C CE2   . PHE A 1 66  ? 4.849   -6.996  14.425  1.00 36.19 ? 89  PHE A CE2   1 
ATOM   470  C CZ    . PHE A 1 66  ? 4.558   -8.336  14.651  1.00 42.32 ? 89  PHE A CZ    1 
ATOM   471  N N     . TYR A 1 67  ? 6.000   -4.358  20.634  1.00 26.56 ? 90  TYR A N     1 
ATOM   472  C CA    . TYR A 1 67  ? 6.829   -3.665  21.619  1.00 25.54 ? 90  TYR A CA    1 
ATOM   473  C C     . TYR A 1 67  ? 6.702   -4.296  23.001  1.00 28.33 ? 90  TYR A C     1 
ATOM   474  O O     . TYR A 1 67  ? 7.710   -4.499  23.691  1.00 27.06 ? 90  TYR A O     1 
ATOM   475  C CB    . TYR A 1 67  ? 6.430   -2.185  21.656  1.00 24.91 ? 90  TYR A CB    1 
ATOM   476  C CG    . TYR A 1 67  ? 6.949   -1.386  22.830  1.00 29.47 ? 90  TYR A CG    1 
ATOM   477  C CD1   . TYR A 1 67  ? 8.233   -0.847  22.818  1.00 25.38 ? 90  TYR A CD1   1 
ATOM   478  C CD2   . TYR A 1 67  ? 6.144   -1.144  23.945  1.00 29.71 ? 90  TYR A CD2   1 
ATOM   479  C CE1   . TYR A 1 67  ? 8.712   -0.100  23.882  1.00 23.18 ? 90  TYR A CE1   1 
ATOM   480  C CE2   . TYR A 1 67  ? 6.621   -0.400  25.026  1.00 29.14 ? 90  TYR A CE2   1 
ATOM   481  C CZ    . TYR A 1 67  ? 7.897   0.119   24.986  1.00 28.78 ? 90  TYR A CZ    1 
ATOM   482  O OH    . TYR A 1 67  ? 8.372   0.857   26.046  1.00 29.05 ? 90  TYR A OH    1 
ATOM   483  N N     . ASN A 1 68  ? 5.468   -4.599  23.422  1.00 27.04 ? 91  ASN A N     1 
ATOM   484  C CA    . ASN A 1 68  ? 5.240   -5.205  24.734  1.00 32.77 ? 91  ASN A CA    1 
ATOM   485  C C     . ASN A 1 68  ? 5.903   -6.573  24.825  1.00 30.47 ? 91  ASN A C     1 
ATOM   486  O O     . ASN A 1 68  ? 6.479   -6.920  25.861  1.00 30.78 ? 91  ASN A O     1 
ATOM   487  C CB    . ASN A 1 68  ? 3.732   -5.333  25.012  1.00 29.93 ? 91  ASN A CB    1 
ATOM   488  C CG    . ASN A 1 68  ? 3.061   -3.993  25.283  1.00 33.40 ? 91  ASN A CG    1 
ATOM   489  O OD1   . ASN A 1 68  ? 3.670   -3.081  25.841  1.00 33.59 ? 91  ASN A OD1   1 
ATOM   490  N ND2   . ASN A 1 68  ? 1.789   -3.874  24.892  1.00 34.10 ? 91  ASN A ND2   1 
ATOM   491  N N     . GLN A 1 69  ? 5.839   -7.358  23.745  1.00 26.92 ? 92  GLN A N     1 
ATOM   492  C CA    . GLN A 1 69  ? 6.477   -8.671  23.738  1.00 26.82 ? 92  GLN A CA    1 
ATOM   493  C C     . GLN A 1 69  ? 7.999   -8.550  23.763  1.00 31.31 ? 92  GLN A C     1 
ATOM   494  O O     . GLN A 1 69  ? 8.673   -9.302  24.481  1.00 27.77 ? 92  GLN A O     1 
ATOM   495  C CB    . GLN A 1 69  ? 6.009   -9.461  22.516  1.00 28.17 ? 92  GLN A CB    1 
ATOM   496  C CG    . GLN A 1 69  ? 6.468   -10.924 22.491  1.00 34.16 ? 92  GLN A CG    1 
ATOM   497  C CD    . GLN A 1 69  ? 6.079   -11.681 23.763  1.00 43.91 ? 92  GLN A CD    1 
ATOM   498  O OE1   . GLN A 1 69  ? 4.889   -11.850 24.059  1.00 45.62 ? 92  GLN A OE1   1 
ATOM   499  N NE2   . GLN A 1 69  ? 7.082   -12.130 24.525  1.00 36.27 ? 92  GLN A NE2   1 
ATOM   500  N N     . LEU A 1 70  ? 8.554   -7.592  23.003  1.00 28.50 ? 93  LEU A N     1 
ATOM   501  C CA    . LEU A 1 70  ? 10.003  -7.373  22.971  1.00 25.26 ? 93  LEU A CA    1 
ATOM   502  C C     . LEU A 1 70  ? 10.558  -7.030  24.348  1.00 27.13 ? 93  LEU A C     1 
ATOM   503  O O     . LEU A 1 70  ? 11.647  -7.491  24.720  1.00 24.06 ? 93  LEU A O     1 
ATOM   504  C CB    . LEU A 1 70  ? 10.341  -6.251  21.974  1.00 22.00 ? 93  LEU A CB    1 
ATOM   505  C CG    . LEU A 1 70  ? 10.174  -6.684  20.518  1.00 25.68 ? 93  LEU A CG    1 
ATOM   506  C CD1   . LEU A 1 70  ? 10.187  -5.489  19.578  1.00 23.22 ? 93  LEU A CD1   1 
ATOM   507  C CD2   . LEU A 1 70  ? 11.262  -7.675  20.165  1.00 26.65 ? 93  LEU A CD2   1 
ATOM   508  N N     . LEU A 1 71  ? 9.839   -6.203  25.114  1.00 24.91 ? 94  LEU A N     1 
ATOM   509  C CA    . LEU A 1 71  ? 10.313  -5.858  26.453  1.00 27.53 ? 94  LEU A CA    1 
ATOM   510  C C     . LEU A 1 71  ? 10.468  -7.103  27.314  1.00 27.66 ? 94  LEU A C     1 
ATOM   511  O O     . LEU A 1 71  ? 11.416  -7.206  28.101  1.00 26.81 ? 94  LEU A O     1 
ATOM   512  C CB    . LEU A 1 71  ? 9.353   -4.878  27.130  1.00 26.02 ? 94  LEU A CB    1 
ATOM   513  C CG    . LEU A 1 71  ? 9.223   -3.437  26.632  1.00 32.81 ? 94  LEU A CG    1 
ATOM   514  C CD1   . LEU A 1 71  ? 7.940   -2.830  27.193  1.00 29.66 ? 94  LEU A CD1   1 
ATOM   515  C CD2   . LEU A 1 71  ? 10.429  -2.612  27.041  1.00 26.56 ? 94  LEU A CD2   1 
ATOM   516  N N     . ARG A 1 72  ? 9.540   -8.056  27.175  1.00 24.89 ? 95  ARG A N     1 
ATOM   517  C CA    . ARG A 1 72  ? 9.571   -9.290  27.960  1.00 29.54 ? 95  ARG A CA    1 
ATOM   518  C C     . ARG A 1 72  ? 10.587  -10.294 27.427  1.00 32.16 ? 95  ARG A C     1 
ATOM   519  O O     . ARG A 1 72  ? 11.108  -11.105 28.201  1.00 28.89 ? 95  ARG A O     1 
ATOM   520  C CB    . ARG A 1 72  ? 8.183   -9.938  27.982  1.00 27.55 ? 95  ARG A CB    1 
ATOM   521  C CG    . ARG A 1 72  ? 7.077   -9.015  28.482  1.00 34.76 ? 95  ARG A CG    1 
ATOM   522  C CD    . ARG A 1 72  ? 5.809   -9.776  28.854  1.00 42.89 ? 95  ARG A CD    1 
ATOM   523  N NE    . ARG A 1 72  ? 5.105   -10.417 27.736  1.00 48.03 ? 95  ARG A NE    1 
ATOM   524  C CZ    . ARG A 1 72  ? 5.154   -11.723 27.470  1.00 50.99 ? 95  ARG A CZ    1 
ATOM   525  N NH1   . ARG A 1 72  ? 5.920   -12.508 28.206  1.00 53.66 ? 95  ARG A NH1   1 
ATOM   526  N NH2   . ARG A 1 72  ? 4.466   -12.248 26.455  1.00 50.50 ? 95  ARG A NH2   1 
ATOM   527  N N     . SER A 1 73  ? 10.871  -10.269 26.117  1.00 27.85 ? 96  SER A N     1 
ATOM   528  C CA    . SER A 1 73  ? 11.766  -11.251 25.509  1.00 27.56 ? 96  SER A CA    1 
ATOM   529  C C     . SER A 1 73  ? 13.231  -10.858 25.571  1.00 27.87 ? 96  SER A C     1 
ATOM   530  O O     . SER A 1 73  ? 14.096  -11.746 25.616  1.00 27.26 ? 96  SER A O     1 
ATOM   531  C CB    . SER A 1 73  ? 11.388  -11.488 24.044  1.00 27.70 ? 96  SER A CB    1 
ATOM   532  O OG    . SER A 1 73  ? 10.207  -12.263 23.950  1.00 29.29 ? 96  SER A OG    1 
ATOM   533  N N     . TYR A 1 74  ? 13.541  -9.557  25.579  1.00 25.15 ? 97  TYR A N     1 
ATOM   534  C CA    . TYR A 1 74  ? 14.924  -9.075  25.549  1.00 26.61 ? 97  TYR A CA    1 
ATOM   535  C C     . TYR A 1 74  ? 15.151  -8.074  26.679  1.00 31.17 ? 97  TYR A C     1 
ATOM   536  O O     . TYR A 1 74  ? 15.244  -6.862  26.449  1.00 25.72 ? 97  TYR A O     1 
ATOM   537  C CB    . TYR A 1 74  ? 15.261  -8.485  24.177  1.00 23.43 ? 97  TYR A CB    1 
ATOM   538  C CG    . TYR A 1 74  ? 15.210  -9.550  23.096  1.00 24.14 ? 97  TYR A CG    1 
ATOM   539  C CD1   . TYR A 1 74  ? 16.308  -10.361 22.849  1.00 25.59 ? 97  TYR A CD1   1 
ATOM   540  C CD2   . TYR A 1 74  ? 14.047  -9.780  22.373  1.00 22.10 ? 97  TYR A CD2   1 
ATOM   541  C CE1   . TYR A 1 74  ? 16.265  -11.358 21.886  1.00 22.49 ? 97  TYR A CE1   1 
ATOM   542  C CE2   . TYR A 1 74  ? 13.986  -10.788 21.412  1.00 24.50 ? 97  TYR A CE2   1 
ATOM   543  C CZ    . TYR A 1 74  ? 15.102  -11.571 21.174  1.00 27.43 ? 97  TYR A CZ    1 
ATOM   544  O OH    . TYR A 1 74  ? 15.064  -12.571 20.213  1.00 33.43 ? 97  TYR A OH    1 
ATOM   545  N N     . PRO A 1 75  ? 15.273  -8.558  27.915  1.00 32.85 ? 98  PRO A N     1 
ATOM   546  C CA    . PRO A 1 75  ? 15.527  -7.655  29.045  1.00 30.98 ? 98  PRO A CA    1 
ATOM   547  C C     . PRO A 1 75  ? 16.750  -6.773  28.821  1.00 29.91 ? 98  PRO A C     1 
ATOM   548  O O     . PRO A 1 75  ? 17.807  -7.229  28.369  1.00 33.77 ? 98  PRO A O     1 
ATOM   549  C CB    . PRO A 1 75  ? 15.748  -8.617  30.223  1.00 30.95 ? 98  PRO A CB    1 
ATOM   550  C CG    . PRO A 1 75  ? 15.113  -9.872  29.835  1.00 32.44 ? 98  PRO A CG    1 
ATOM   551  C CD    . PRO A 1 75  ? 15.199  -9.970  28.332  1.00 30.45 ? 98  PRO A CD    1 
ATOM   552  N N     . GLY A 1 76  ? 16.609  -5.497  29.170  1.00 28.09 ? 99  GLY A N     1 
ATOM   553  C CA    . GLY A 1 76  ? 17.721  -4.578  29.145  1.00 29.76 ? 99  GLY A CA    1 
ATOM   554  C C     . GLY A 1 76  ? 17.878  -3.787  27.861  1.00 29.59 ? 99  GLY A C     1 
ATOM   555  O O     . GLY A 1 76  ? 18.525  -2.736  27.883  1.00 25.83 ? 99  GLY A O     1 
ATOM   556  N N     . VAL A 1 77  ? 17.312  -4.265  26.746  1.00 25.49 ? 100 VAL A N     1 
ATOM   557  C CA    . VAL A 1 77  ? 17.378  -3.530  25.488  1.00 25.06 ? 100 VAL A CA    1 
ATOM   558  C C     . VAL A 1 77  ? 16.486  -2.296  25.571  1.00 24.80 ? 100 VAL A C     1 
ATOM   559  O O     . VAL A 1 77  ? 15.386  -2.332  26.140  1.00 23.58 ? 100 VAL A O     1 
ATOM   560  C CB    . VAL A 1 77  ? 16.964  -4.433  24.310  1.00 25.19 ? 100 VAL A CB    1 
ATOM   561  C CG1   . VAL A 1 77  ? 16.809  -3.611  23.005  1.00 21.93 ? 100 VAL A CG1   1 
ATOM   562  C CG2   . VAL A 1 77  ? 17.960  -5.571  24.121  1.00 23.54 ? 100 VAL A CG2   1 
ATOM   563  N N     . ASN A 1 78  ? 16.959  -1.192  24.995  1.00 25.06 ? 101 ASN A N     1 
ATOM   564  C CA    . ASN A 1 78  ? 16.244  0.084   25.036  1.00 23.83 ? 101 ASN A CA    1 
ATOM   565  C C     . ASN A 1 78  ? 15.260  0.149   23.867  1.00 24.86 ? 101 ASN A C     1 
ATOM   566  O O     . ASN A 1 78  ? 15.515  0.759   22.824  1.00 24.68 ? 101 ASN A O     1 
ATOM   567  C CB    . ASN A 1 78  ? 17.242  1.238   25.010  1.00 27.70 ? 101 ASN A CB    1 
ATOM   568  C CG    . ASN A 1 78  ? 16.569  2.597   25.068  1.00 32.87 ? 101 ASN A CG    1 
ATOM   569  O OD1   . ASN A 1 78  ? 15.602  2.785   25.799  1.00 29.28 ? 101 ASN A OD1   1 
ATOM   570  N ND2   . ASN A 1 78  ? 17.082  3.554   24.288  1.00 27.88 ? 101 ASN A ND2   1 
ATOM   571  N N     . PHE A 1 79  ? 14.107  -0.493  24.054  1.00 25.76 ? 102 PHE A N     1 
ATOM   572  C CA    . PHE A 1 79  ? 13.042  -0.449  23.058  1.00 21.63 ? 102 PHE A CA    1 
ATOM   573  C C     . PHE A 1 79  ? 12.263  0.855   23.191  1.00 27.81 ? 102 PHE A C     1 
ATOM   574  O O     . PHE A 1 79  ? 12.033  1.353   24.299  1.00 26.08 ? 102 PHE A O     1 
ATOM   575  C CB    . PHE A 1 79  ? 12.089  -1.638  23.217  1.00 23.69 ? 102 PHE A CB    1 
ATOM   576  C CG    . PHE A 1 79  ? 12.705  -2.979  22.870  1.00 22.58 ? 102 PHE A CG    1 
ATOM   577  C CD1   . PHE A 1 79  ? 12.941  -3.339  21.542  1.00 21.15 ? 102 PHE A CD1   1 
ATOM   578  C CD2   . PHE A 1 79  ? 13.036  -3.883  23.871  1.00 23.10 ? 102 PHE A CD2   1 
ATOM   579  C CE1   . PHE A 1 79  ? 13.506  -4.562  21.229  1.00 21.49 ? 102 PHE A CE1   1 
ATOM   580  C CE2   . PHE A 1 79  ? 13.586  -5.115  23.568  1.00 24.84 ? 102 PHE A CE2   1 
ATOM   581  C CZ    . PHE A 1 79  ? 13.826  -5.461  22.240  1.00 23.70 ? 102 PHE A CZ    1 
ATOM   582  N N     . VAL A 1 80  ? 11.862  1.412   22.051  1.00 24.44 ? 103 VAL A N     1 
ATOM   583  C CA    . VAL A 1 80  ? 11.078  2.638   21.999  1.00 25.55 ? 103 VAL A CA    1 
ATOM   584  C C     . VAL A 1 80  ? 9.859   2.344   21.146  1.00 26.53 ? 103 VAL A C     1 
ATOM   585  O O     . VAL A 1 80  ? 9.995   1.794   20.047  1.00 24.73 ? 103 VAL A O     1 
ATOM   586  C CB    . VAL A 1 80  ? 11.882  3.819   21.412  1.00 24.19 ? 103 VAL A CB    1 
ATOM   587  C CG1   . VAL A 1 80  ? 11.033  5.092   21.382  1.00 27.14 ? 103 VAL A CG1   1 
ATOM   588  C CG2   . VAL A 1 80  ? 13.151  4.058   22.205  1.00 24.01 ? 103 VAL A CG2   1 
ATOM   589  N N     . ASN A 1 81  ? 8.673   2.680   21.661  1.00 23.58 ? 104 ASN A N     1 
ATOM   590  C CA    . ASN A 1 81  ? 7.413   2.457   20.951  1.00 25.91 ? 104 ASN A CA    1 
ATOM   591  C C     . ASN A 1 81  ? 7.059   3.740   20.209  1.00 25.86 ? 104 ASN A C     1 
ATOM   592  O O     . ASN A 1 81  ? 6.640   4.725   20.821  1.00 27.46 ? 104 ASN A O     1 
ATOM   593  C CB    . ASN A 1 81  ? 6.318   2.046   21.933  1.00 26.63 ? 104 ASN A CB    1 
ATOM   594  C CG    . ASN A 1 81  ? 5.039   1.613   21.240  1.00 26.60 ? 104 ASN A CG    1 
ATOM   595  O OD1   . ASN A 1 81  ? 5.047   1.215   20.072  1.00 28.19 ? 104 ASN A OD1   1 
ATOM   596  N ND2   . ASN A 1 81  ? 3.933   1.702   21.948  1.00 25.93 ? 104 ASN A ND2   1 
ATOM   597  N N     . GLY A 1 82  ? 7.252   3.749   18.894  1.00 23.48 ? 105 GLY A N     1 
ATOM   598  C CA    . GLY A 1 82  ? 7.028   4.959   18.129  1.00 24.17 ? 105 GLY A CA    1 
ATOM   599  C C     . GLY A 1 82  ? 7.460   4.802   16.680  1.00 26.04 ? 105 GLY A C     1 
ATOM   600  O O     . GLY A 1 82  ? 7.827   3.715   16.225  1.00 22.57 ? 105 GLY A O     1 
ATOM   601  N N     . ASP A 1 83  ? 7.411   5.925   15.967  1.00 28.28 ? 106 ASP A N     1 
ATOM   602  C CA    . ASP A 1 83  ? 7.607   5.959   14.521  1.00 27.65 ? 106 ASP A CA    1 
ATOM   603  C C     . ASP A 1 83  ? 9.052   6.331   14.191  1.00 26.24 ? 106 ASP A C     1 
ATOM   604  O O     . ASP A 1 83  ? 9.503   7.429   14.529  1.00 24.85 ? 106 ASP A O     1 
ATOM   605  C CB    . ASP A 1 83  ? 6.635   6.954   13.886  1.00 24.81 ? 106 ASP A CB    1 
ATOM   606  C CG    . ASP A 1 83  ? 6.734   6.993   12.358  1.00 31.45 ? 106 ASP A CG    1 
ATOM   607  O OD1   . ASP A 1 83  ? 7.533   6.230   11.746  1.00 28.37 ? 106 ASP A OD1   1 
ATOM   608  O OD2   . ASP A 1 83  ? 5.994   7.803   11.769  1.00 33.05 ? 106 ASP A OD2   1 
ATOM   609  N N     . ALA A 1 84  ? 9.752   5.434   13.485  1.00 27.01 ? 107 ALA A N     1 
ATOM   610  C CA    . ALA A 1 84  ? 11.150  5.666   13.112  1.00 26.73 ? 107 ALA A CA    1 
ATOM   611  C C     . ALA A 1 84  ? 11.334  6.859   12.182  1.00 27.27 ? 107 ALA A C     1 
ATOM   612  O O     . ALA A 1 84  ? 12.431  7.428   12.140  1.00 27.24 ? 107 ALA A O     1 
ATOM   613  C CB    . ALA A 1 84  ? 11.738  4.427   12.433  1.00 25.39 ? 107 ALA A CB    1 
ATOM   614  N N     . PHE A 1 85  ? 10.310  7.234   11.413  1.00 26.75 ? 108 PHE A N     1 
ATOM   615  C CA    . PHE A 1 85  ? 10.413  8.428   10.583  1.00 26.57 ? 108 PHE A CA    1 
ATOM   616  C C     . PHE A 1 85  ? 10.362  9.719   11.393  1.00 31.44 ? 108 PHE A C     1 
ATOM   617  O O     . PHE A 1 85  ? 10.678  10.787  10.849  1.00 31.18 ? 108 PHE A O     1 
ATOM   618  C CB    . PHE A 1 85  ? 9.314   8.413   9.517   1.00 24.55 ? 108 PHE A CB    1 
ATOM   619  C CG    . PHE A 1 85  ? 9.575   7.428   8.415   1.00 25.59 ? 108 PHE A CG    1 
ATOM   620  C CD1   . PHE A 1 85  ? 9.349   6.060   8.621   1.00 24.96 ? 108 PHE A CD1   1 
ATOM   621  C CD2   . PHE A 1 85  ? 10.077  7.856   7.187   1.00 23.66 ? 108 PHE A CD2   1 
ATOM   622  C CE1   . PHE A 1 85  ? 9.606   5.139   7.619   1.00 25.22 ? 108 PHE A CE1   1 
ATOM   623  C CE2   . PHE A 1 85  ? 10.331  6.943   6.170   1.00 21.44 ? 108 PHE A CE2   1 
ATOM   624  C CZ    . PHE A 1 85  ? 10.096  5.582   6.381   1.00 25.40 ? 108 PHE A CZ    1 
ATOM   625  N N     . ASP A 1 86  ? 9.997   9.651   12.671  1.00 29.30 ? 109 ASP A N     1 
ATOM   626  C CA    . ASP A 1 86  ? 9.976   10.814  13.557  1.00 30.92 ? 109 ASP A CA    1 
ATOM   627  C C     . ASP A 1 86  ? 11.052  10.625  14.624  1.00 27.97 ? 109 ASP A C     1 
ATOM   628  O O     . ASP A 1 86  ? 10.761  10.285  15.770  1.00 29.84 ? 109 ASP A O     1 
ATOM   629  C CB    . ASP A 1 86  ? 8.588   10.994  14.190  1.00 32.35 ? 109 ASP A CB    1 
ATOM   630  C CG    . ASP A 1 86  ? 8.429   12.347  14.864  1.00 37.23 ? 109 ASP A CG    1 
ATOM   631  O OD1   . ASP A 1 86  ? 9.447   13.074  14.991  1.00 37.63 ? 109 ASP A OD1   1 
ATOM   632  O OD2   . ASP A 1 86  ? 7.291   12.690  15.251  1.00 40.45 ? 109 ASP A OD2   1 
ATOM   633  N N     . LEU A 1 87  ? 12.308  10.873  14.241  1.00 25.68 ? 110 LEU A N     1 
ATOM   634  C CA    . LEU A 1 87  ? 13.419  10.645  15.160  1.00 29.02 ? 110 LEU A CA    1 
ATOM   635  C C     . LEU A 1 87  ? 13.402  11.613  16.335  1.00 29.37 ? 110 LEU A C     1 
ATOM   636  O O     . LEU A 1 87  ? 13.812  11.245  17.447  1.00 30.45 ? 110 LEU A O     1 
ATOM   637  C CB    . LEU A 1 87  ? 14.748  10.753  14.416  1.00 29.49 ? 110 LEU A CB    1 
ATOM   638  C CG    . LEU A 1 87  ? 15.030  9.644   13.402  1.00 30.93 ? 110 LEU A CG    1 
ATOM   639  C CD1   . LEU A 1 87  ? 16.352  9.939   12.681  1.00 24.68 ? 110 LEU A CD1   1 
ATOM   640  C CD2   . LEU A 1 87  ? 15.024  8.260   14.082  1.00 24.86 ? 110 LEU A CD2   1 
ATOM   641  N N     . ASP A 1 88  ? 12.953  12.850  16.117  1.00 25.27 ? 111 ASP A N     1 
ATOM   642  C CA    . ASP A 1 88  ? 12.849  13.787  17.232  1.00 30.38 ? 111 ASP A CA    1 
ATOM   643  C C     . ASP A 1 88  ? 11.904  13.273  18.317  1.00 27.64 ? 111 ASP A C     1 
ATOM   644  O O     . ASP A 1 88  ? 12.182  13.434  19.505  1.00 27.32 ? 111 ASP A O     1 
ATOM   645  C CB    . ASP A 1 88  ? 12.403  15.158  16.730  1.00 31.59 ? 111 ASP A CB    1 
ATOM   646  C CG    . ASP A 1 88  ? 13.510  15.886  15.972  1.00 37.61 ? 111 ASP A CG    1 
ATOM   647  O OD1   . ASP A 1 88  ? 14.681  15.453  16.066  1.00 36.63 ? 111 ASP A OD1   1 
ATOM   648  O OD2   . ASP A 1 88  ? 13.214  16.888  15.283  1.00 47.75 ? 111 ASP A OD2   1 
ATOM   649  N N     . ALA A 1 89  ? 10.800  12.628  17.935  1.00 26.16 ? 112 ALA A N     1 
ATOM   650  C CA    . ALA A 1 89  ? 9.864   12.139  18.944  1.00 29.99 ? 112 ALA A CA    1 
ATOM   651  C C     . ALA A 1 89  ? 10.343  10.851  19.600  1.00 31.61 ? 112 ALA A C     1 
ATOM   652  O O     . ALA A 1 89  ? 10.052  10.617  20.778  1.00 32.39 ? 112 ALA A O     1 
ATOM   653  C CB    . ALA A 1 89  ? 8.477   11.915  18.330  1.00 34.58 ? 112 ALA A CB    1 
ATOM   654  N N     . THR A 1 90  ? 11.059  10.002  18.869  1.00 26.88 ? 113 THR A N     1 
ATOM   655  C CA    . THR A 1 90  ? 11.464  8.727   19.440  1.00 27.86 ? 113 THR A CA    1 
ATOM   656  C C     . THR A 1 90  ? 12.835  8.793   20.099  1.00 29.99 ? 113 THR A C     1 
ATOM   657  O O     . THR A 1 90  ? 13.023  8.210   21.170  1.00 33.44 ? 113 THR A O     1 
ATOM   658  C CB    . THR A 1 90  ? 11.441  7.643   18.359  1.00 29.91 ? 113 THR A CB    1 
ATOM   659  O OG1   . THR A 1 90  ? 12.259  8.050   17.262  1.00 26.01 ? 113 THR A OG1   1 
ATOM   660  C CG2   . THR A 1 90  ? 10.014  7.446   17.843  1.00 28.17 ? 113 THR A CG2   1 
ATOM   661  N N     . LEU A 1 91  ? 13.797  9.496   19.496  1.00 27.04 ? 114 LEU A N     1 
ATOM   662  C CA    . LEU A 1 91  ? 15.143  9.599   20.045  1.00 27.99 ? 114 LEU A CA    1 
ATOM   663  C C     . LEU A 1 91  ? 15.387  10.910  20.779  1.00 31.00 ? 114 LEU A C     1 
ATOM   664  O O     . LEU A 1 91  ? 16.379  11.014  21.503  1.00 32.54 ? 114 LEU A O     1 
ATOM   665  C CB    . LEU A 1 91  ? 16.200  9.455   18.930  1.00 24.28 ? 114 LEU A CB    1 
ATOM   666  C CG    . LEU A 1 91  ? 16.230  8.112   18.183  1.00 28.01 ? 114 LEU A CG    1 
ATOM   667  C CD1   . LEU A 1 91  ? 17.417  8.012   17.239  1.00 26.42 ? 114 LEU A CD1   1 
ATOM   668  C CD2   . LEU A 1 91  ? 16.230  6.954   19.184  1.00 24.85 ? 114 LEU A CD2   1 
ATOM   669  N N     . GLY A 1 92  ? 14.520  11.897  20.612  1.00 29.04 ? 115 GLY A N     1 
ATOM   670  C CA    . GLY A 1 92  ? 14.806  13.239  21.067  1.00 31.63 ? 115 GLY A CA    1 
ATOM   671  C C     . GLY A 1 92  ? 15.522  14.047  19.997  1.00 32.07 ? 115 GLY A C     1 
ATOM   672  O O     . GLY A 1 92  ? 16.134  13.509  19.071  1.00 27.38 ? 115 GLY A O     1 
ATOM   673  N N     . GLU A 1 93  ? 15.406  15.371  20.119  1.00 26.50 ? 116 GLU A N     1 
ATOM   674  C CA    . GLU A 1 93  ? 16.163  16.279  19.262  1.00 33.27 ? 116 GLU A CA    1 
ATOM   675  C C     . GLU A 1 93  ? 17.646  15.919  19.305  1.00 31.82 ? 116 GLU A C     1 
ATOM   676  O O     . GLU A 1 93  ? 18.172  15.537  20.353  1.00 28.37 ? 116 GLU A O     1 
ATOM   677  C CB    . GLU A 1 93  ? 15.943  17.727  19.725  1.00 36.31 ? 116 GLU A CB    1 
ATOM   678  C CG    . GLU A 1 93  ? 16.739  18.772  18.964  1.00 44.11 ? 116 GLU A CG    1 
ATOM   679  C CD    . GLU A 1 93  ? 16.451  20.198  19.435  1.00 55.79 ? 116 GLU A CD    1 
ATOM   680  O OE1   . GLU A 1 93  ? 16.329  20.416  20.664  1.00 56.05 ? 116 GLU A OE1   1 
ATOM   681  O OE2   . GLU A 1 93  ? 16.350  21.098  18.571  1.00 56.27 ? 116 GLU A OE2   1 
ATOM   682  N N     . HIS A 1 94  ? 18.319  16.002  18.158  1.00 27.03 ? 117 HIS A N     1 
ATOM   683  C CA    . HIS A 1 94  ? 19.712  15.559  18.116  1.00 31.89 ? 117 HIS A CA    1 
ATOM   684  C C     . HIS A 1 94  ? 20.582  16.534  18.899  1.00 29.88 ? 117 HIS A C     1 
ATOM   685  O O     . HIS A 1 94  ? 20.585  17.738  18.624  1.00 29.56 ? 117 HIS A O     1 
ATOM   686  C CB    . HIS A 1 94  ? 20.219  15.420  16.680  1.00 27.85 ? 117 HIS A CB    1 
ATOM   687  C CG    . HIS A 1 94  ? 21.494  14.632  16.565  1.00 28.12 ? 117 HIS A CG    1 
ATOM   688  N ND1   . HIS A 1 94  ? 22.387  14.798  15.527  1.00 25.44 ? 117 HIS A ND1   1 
ATOM   689  C CD2   . HIS A 1 94  ? 22.025  13.674  17.364  1.00 27.90 ? 117 HIS A CD2   1 
ATOM   690  C CE1   . HIS A 1 94  ? 23.414  13.983  15.690  1.00 26.28 ? 117 HIS A CE1   1 
ATOM   691  N NE2   . HIS A 1 94  ? 23.216  13.283  16.795  1.00 29.78 ? 117 HIS A NE2   1 
ATOM   692  N N     . LYS A 1 95  ? 21.310  16.015  19.886  1.00 26.42 ? 118 LYS A N     1 
ATOM   693  C CA    . LYS A 1 95  ? 22.202  16.841  20.689  1.00 31.77 ? 118 LYS A CA    1 
ATOM   694  C C     . LYS A 1 95  ? 23.598  16.242  20.793  1.00 29.11 ? 118 LYS A C     1 
ATOM   695  O O     . LYS A 1 95  ? 24.352  16.606  21.698  1.00 30.76 ? 118 LYS A O     1 
ATOM   696  C CB    . LYS A 1 95  ? 21.620  17.068  22.086  1.00 31.87 ? 118 LYS A CB    1 
ATOM   697  C CG    . LYS A 1 95  ? 20.376  17.939  22.098  1.00 36.67 ? 118 LYS A CG    1 
ATOM   698  C CD    . LYS A 1 95  ? 19.686  17.904  23.475  1.00 46.09 ? 118 LYS A CD    1 
ATOM   699  C CE    . LYS A 1 95  ? 18.413  18.754  23.488  1.00 51.12 ? 118 LYS A CE    1 
ATOM   700  N NZ    . LYS A 1 95  ? 17.330  18.151  24.332  1.00 56.73 ? 118 LYS A NZ    1 
ATOM   701  N N     . GLY A 1 96  ? 23.953  15.319  19.900  1.00 25.68 ? 119 GLY A N     1 
ATOM   702  C CA    . GLY A 1 96  ? 25.290  14.769  19.910  1.00 25.94 ? 119 GLY A CA    1 
ATOM   703  C C     . GLY A 1 96  ? 25.382  13.254  19.947  1.00 29.78 ? 119 GLY A C     1 
ATOM   704  O O     . GLY A 1 96  ? 26.461  12.708  19.689  1.00 23.62 ? 119 GLY A O     1 
ATOM   705  N N     . GLN A 1 97  ? 24.282  12.566  20.264  1.00 26.29 ? 120 GLN A N     1 
ATOM   706  C CA    . GLN A 1 97  ? 24.306  11.108  20.324  1.00 26.39 ? 120 GLN A CA    1 
ATOM   707  C C     . GLN A 1 97  ? 24.689  10.515  18.976  1.00 26.69 ? 120 GLN A C     1 
ATOM   708  O O     . GLN A 1 97  ? 24.074  10.827  17.948  1.00 24.50 ? 120 GLN A O     1 
ATOM   709  C CB    . GLN A 1 97  ? 22.946  10.563  20.754  1.00 28.88 ? 120 GLN A CB    1 
ATOM   710  C CG    . GLN A 1 97  ? 22.927  9.037   20.824  1.00 30.92 ? 120 GLN A CG    1 
ATOM   711  C CD    . GLN A 1 97  ? 21.553  8.483   21.144  1.00 36.21 ? 120 GLN A CD    1 
ATOM   712  O OE1   . GLN A 1 97  ? 20.532  8.973   20.640  1.00 38.41 ? 120 GLN A OE1   1 
ATOM   713  N NE2   . GLN A 1 97  ? 21.515  7.461   21.991  1.00 33.73 ? 120 GLN A NE2   1 
ATOM   714  N N     . MET A 1 98  ? 25.718  9.666   18.983  1.00 21.80 ? 121 MET A N     1 
ATOM   715  C CA    . MET A 1 98  ? 26.210  9.005   17.781  1.00 23.27 ? 121 MET A CA    1 
ATOM   716  C C     . MET A 1 98  ? 26.064  7.494   17.930  1.00 24.90 ? 121 MET A C     1 
ATOM   717  O O     . MET A 1 98  ? 26.455  6.923   18.957  1.00 22.65 ? 121 MET A O     1 
ATOM   718  C CB    . MET A 1 98  ? 27.674  9.364   17.515  1.00 20.38 ? 121 MET A CB    1 
ATOM   719  C CG    . MET A 1 98  ? 27.892  10.823  17.229  1.00 25.02 ? 121 MET A CG    1 
ATOM   720  S SD    . MET A 1 98  ? 27.175  11.340  15.653  1.00 32.51 ? 121 MET A SD    1 
ATOM   721  C CE    . MET A 1 98  ? 28.720  11.832  14.867  1.00 24.36 ? 121 MET A CE    1 
ATOM   722  N N     . PHE A 1 99  ? 25.507  6.860   16.909  1.00 18.70 ? 122 PHE A N     1 
ATOM   723  C CA    . PHE A 1 99  ? 25.364  5.416   16.861  1.00 20.07 ? 122 PHE A CA    1 
ATOM   724  C C     . PHE A 1 99  ? 26.446  4.821   15.973  1.00 20.75 ? 122 PHE A C     1 
ATOM   725  O O     . PHE A 1 99  ? 26.881  5.434   14.998  1.00 19.12 ? 122 PHE A O     1 
ATOM   726  C CB    . PHE A 1 99  ? 23.984  5.009   16.331  1.00 22.46 ? 122 PHE A CB    1 
ATOM   727  C CG    . PHE A 1 99  ? 22.840  5.368   17.255  1.00 21.61 ? 122 PHE A CG    1 
ATOM   728  C CD1   . PHE A 1 99  ? 22.463  4.510   18.279  1.00 21.35 ? 122 PHE A CD1   1 
ATOM   729  C CD2   . PHE A 1 99  ? 22.143  6.559   17.095  1.00 23.29 ? 122 PHE A CD2   1 
ATOM   730  C CE1   . PHE A 1 99  ? 21.392  4.827   19.126  1.00 26.47 ? 122 PHE A CE1   1 
ATOM   731  C CE2   . PHE A 1 99  ? 21.073  6.883   17.941  1.00 27.00 ? 122 PHE A CE2   1 
ATOM   732  C CZ    . PHE A 1 99  ? 20.704  6.020   18.956  1.00 26.56 ? 122 PHE A CZ    1 
ATOM   733  N N     . ASP A 1 100 ? 26.887  3.621   16.339  1.00 19.69 ? 123 ASP A N     1 
ATOM   734  C CA    . ASP A 1 100 ? 27.855  2.895   15.528  1.00 22.30 ? 123 ASP A CA    1 
ATOM   735  C C     . ASP A 1 100 ? 27.358  2.675   14.103  1.00 20.58 ? 123 ASP A C     1 
ATOM   736  O O     . ASP A 1 100 ? 28.116  2.815   13.140  1.00 20.68 ? 123 ASP A O     1 
ATOM   737  C CB    . ASP A 1 100 ? 28.139  1.544   16.164  1.00 23.13 ? 123 ASP A CB    1 
ATOM   738  C CG    . ASP A 1 100 ? 29.149  0.771   15.379  1.00 25.74 ? 123 ASP A CG    1 
ATOM   739  O OD1   . ASP A 1 100 ? 30.349  1.102   15.527  1.00 25.67 ? 123 ASP A OD1   1 
ATOM   740  O OD2   . ASP A 1 100 ? 28.738  -0.120  14.594  1.00 22.89 ? 123 ASP A OD2   1 
ATOM   741  N N     . SER A 1 101 ? 26.098  2.285   13.962  1.00 19.03 ? 124 SER A N     1 
ATOM   742  C CA    . SER A 1 101 ? 25.491  1.922   12.694  1.00 19.17 ? 124 SER A CA    1 
ATOM   743  C C     . SER A 1 101 ? 23.999  1.829   12.947  1.00 19.94 ? 124 SER A C     1 
ATOM   744  O O     . SER A 1 101 ? 23.559  1.794   14.095  1.00 20.16 ? 124 SER A O     1 
ATOM   745  C CB    . SER A 1 101 ? 26.058  0.599   12.149  1.00 19.93 ? 124 SER A CB    1 
ATOM   746  O OG    . SER A 1 101 ? 26.186  -0.384  13.173  1.00 23.06 ? 124 SER A OG    1 
ATOM   747  N N     . VAL A 1 102 ? 23.226  1.827   11.868  1.00 20.22 ? 125 VAL A N     1 
ATOM   748  C CA    . VAL A 1 102 ? 21.776  1.702   11.912  1.00 18.67 ? 125 VAL A CA    1 
ATOM   749  C C     . VAL A 1 102 ? 21.403  0.447   11.138  1.00 21.44 ? 125 VAL A C     1 
ATOM   750  O O     . VAL A 1 102 ? 21.859  0.263   10.003  1.00 19.25 ? 125 VAL A O     1 
ATOM   751  C CB    . VAL A 1 102 ? 21.076  2.926   11.297  1.00 18.58 ? 125 VAL A CB    1 
ATOM   752  C CG1   . VAL A 1 102 ? 19.551  2.745   11.349  1.00 18.62 ? 125 VAL A CG1   1 
ATOM   753  C CG2   . VAL A 1 102 ? 21.526  4.231   11.993  1.00 18.21 ? 125 VAL A CG2   1 
ATOM   754  N N     . ILE A 1 103 ? 20.587  -0.411  11.752  1.00 18.61 ? 126 ILE A N     1 
ATOM   755  C CA    . ILE A 1 103 ? 20.125  -1.662  11.149  1.00 19.02 ? 126 ILE A CA    1 
ATOM   756  C C     . ILE A 1 103 ? 18.632  -1.503  10.904  1.00 20.41 ? 126 ILE A C     1 
ATOM   757  O O     . ILE A 1 103 ? 17.858  -1.407  11.863  1.00 20.68 ? 126 ILE A O     1 
ATOM   758  C CB    . ILE A 1 103 ? 20.397  -2.864  12.064  1.00 18.70 ? 126 ILE A CB    1 
ATOM   759  C CG1   . ILE A 1 103 ? 21.759  -2.745  12.768  1.00 23.36 ? 126 ILE A CG1   1 
ATOM   760  C CG2   . ILE A 1 103 ? 20.231  -4.166  11.306  1.00 19.35 ? 126 ILE A CG2   1 
ATOM   761  C CD1   . ILE A 1 103 ? 22.961  -2.762  11.854  1.00 21.52 ? 126 ILE A CD1   1 
ATOM   762  N N     . SER A 1 104 ? 18.204  -1.479  9.638   1.00 19.47 ? 127 SER A N     1 
ATOM   763  C CA    . SER A 1 104 ? 16.833  -1.084  9.308   1.00 20.06 ? 127 SER A CA    1 
ATOM   764  C C     . SER A 1 104 ? 16.092  -2.199  8.584   1.00 23.09 ? 127 SER A C     1 
ATOM   765  O O     . SER A 1 104 ? 16.492  -2.616  7.490   1.00 23.22 ? 127 SER A O     1 
ATOM   766  C CB    . SER A 1 104 ? 16.800  0.178   8.447   1.00 20.48 ? 127 SER A CB    1 
ATOM   767  O OG    . SER A 1 104 ? 15.450  0.492   8.091   1.00 23.76 ? 127 SER A OG    1 
ATOM   768  N N     . ALA A 1 105 ? 14.986  -2.639  9.177   1.00 24.11 ? 128 ALA A N     1 
ATOM   769  C CA    . ALA A 1 105 ? 14.029  -3.512  8.513   1.00 24.60 ? 128 ALA A CA    1 
ATOM   770  C C     . ALA A 1 105 ? 12.644  -2.870  8.393   1.00 25.98 ? 128 ALA A C     1 
ATOM   771  O O     . ALA A 1 105 ? 11.656  -3.581  8.199   1.00 25.22 ? 128 ALA A O     1 
ATOM   772  C CB    . ALA A 1 105 ? 13.943  -4.849  9.251   1.00 23.72 ? 128 ALA A CB    1 
ATOM   773  N N     . VAL A 1 106 ? 12.536  -1.544  8.485   1.00 22.68 ? 129 VAL A N     1 
ATOM   774  C CA    . VAL A 1 106 ? 11.223  -0.939  8.257   1.00 25.63 ? 129 VAL A CA    1 
ATOM   775  C C     . VAL A 1 106 ? 10.849  -1.147  6.794   1.00 26.96 ? 129 VAL A C     1 
ATOM   776  O O     . VAL A 1 106 ? 11.728  -1.158  5.916   1.00 24.27 ? 129 VAL A O     1 
ATOM   777  C CB    . VAL A 1 106 ? 11.168  0.549   8.653   1.00 29.49 ? 129 VAL A CB    1 
ATOM   778  C CG1   . VAL A 1 106 ? 11.371  0.701   10.162  1.00 28.47 ? 129 VAL A CG1   1 
ATOM   779  C CG2   . VAL A 1 106 ? 12.163  1.363   7.872   1.00 28.61 ? 129 VAL A CG2   1 
ATOM   780  N N     . PRO A 1 107 ? 9.561   -1.362  6.498   1.00 28.84 ? 130 PRO A N     1 
ATOM   781  C CA    . PRO A 1 107 ? 9.143   -1.622  5.112   1.00 28.62 ? 130 PRO A CA    1 
ATOM   782  C C     . PRO A 1 107 ? 9.125   -0.352  4.277   1.00 26.00 ? 130 PRO A C     1 
ATOM   783  O O     . PRO A 1 107 ? 8.091   0.315   4.162   1.00 24.57 ? 130 PRO A O     1 
ATOM   784  C CB    . PRO A 1 107 ? 7.738   -2.229  5.272   1.00 27.47 ? 130 PRO A CB    1 
ATOM   785  C CG    . PRO A 1 107 ? 7.231   -1.698  6.589   1.00 26.51 ? 130 PRO A CG    1 
ATOM   786  C CD    . PRO A 1 107 ? 8.454   -1.507  7.467   1.00 26.61 ? 130 PRO A CD    1 
ATOM   787  N N     . MET A 1 108 ? 10.272  -0.047  3.660   1.00 25.17 ? 131 MET A N     1 
ATOM   788  C CA    . MET A 1 108 ? 10.461  1.235   2.985   1.00 28.66 ? 131 MET A CA    1 
ATOM   789  C C     . MET A 1 108 ? 9.380   1.486   1.948   1.00 27.53 ? 131 MET A C     1 
ATOM   790  O O     . MET A 1 108 ? 8.937   2.626   1.758   1.00 23.17 ? 131 MET A O     1 
ATOM   791  C CB    . MET A 1 108 ? 11.838  1.272   2.322   1.00 29.83 ? 131 MET A CB    1 
ATOM   792  C CG    . MET A 1 108 ? 12.941  1.675   3.260   1.00 34.75 ? 131 MET A CG    1 
ATOM   793  S SD    . MET A 1 108 ? 12.730  3.357   3.838   1.00 89.31 ? 131 MET A SD    1 
ATOM   794  C CE    . MET A 1 108 ? 13.943  3.394   5.129   1.00 34.81 ? 131 MET A CE    1 
ATOM   795  N N     . LEU A 1 109 ? 8.938   0.434   1.267   1.00 25.86 ? 132 LEU A N     1 
ATOM   796  C CA    . LEU A 1 109 ? 8.010   0.646   0.165   1.00 28.37 ? 132 LEU A CA    1 
ATOM   797  C C     . LEU A 1 109 ? 6.601   1.020   0.630   1.00 27.79 ? 132 LEU A C     1 
ATOM   798  O O     . LEU A 1 109 ? 5.802   1.479   -0.197  1.00 24.84 ? 132 LEU A O     1 
ATOM   799  C CB    . LEU A 1 109 ? 8.003   -0.595  -0.734  1.00 31.96 ? 132 LEU A CB    1 
ATOM   800  C CG    . LEU A 1 109 ? 9.094   -0.601  -1.825  1.00 38.76 ? 132 LEU A CG    1 
ATOM   801  C CD1   . LEU A 1 109 ? 8.666   0.284   -2.981  1.00 42.10 ? 132 LEU A CD1   1 
ATOM   802  C CD2   . LEU A 1 109 ? 10.485  -0.159  -1.345  1.00 30.60 ? 132 LEU A CD2   1 
ATOM   803  N N     . ASN A 1 110 ? 6.292   0.894   1.928   1.00 22.20 ? 133 ASN A N     1 
ATOM   804  C CA    . ASN A 1 110 ? 5.035   1.424   2.469   1.00 23.32 ? 133 ASN A CA    1 
ATOM   805  C C     . ASN A 1 110 ? 5.015   2.946   2.571   1.00 24.07 ? 133 ASN A C     1 
ATOM   806  O O     . ASN A 1 110 ? 3.992   3.497   2.994   1.00 23.78 ? 133 ASN A O     1 
ATOM   807  C CB    . ASN A 1 110 ? 4.761   0.856   3.871   1.00 21.71 ? 133 ASN A CB    1 
ATOM   808  C CG    . ASN A 1 110 ? 4.409   -0.623  3.844   1.00 26.95 ? 133 ASN A CG    1 
ATOM   809  O OD1   . ASN A 1 110 ? 4.437   -1.259  2.791   1.00 26.61 ? 133 ASN A OD1   1 
ATOM   810  N ND2   . ASN A 1 110 ? 4.082   -1.172  5.005   1.00 27.26 ? 133 ASN A ND2   1 
ATOM   811  N N     . PHE A 1 111 ? 6.104   3.634   2.240   1.00 23.00 ? 134 PHE A N     1 
ATOM   812  C CA    . PHE A 1 111 ? 6.210   5.074   2.435   1.00 23.17 ? 134 PHE A CA    1 
ATOM   813  C C     . PHE A 1 111 ? 6.617   5.741   1.125   1.00 21.15 ? 134 PHE A C     1 
ATOM   814  O O     . PHE A 1 111 ? 7.268   5.112   0.292   1.00 24.50 ? 134 PHE A O     1 
ATOM   815  C CB    . PHE A 1 111 ? 7.235   5.394   3.539   1.00 21.54 ? 134 PHE A CB    1 
ATOM   816  C CG    . PHE A 1 111 ? 6.941   4.703   4.862   1.00 23.82 ? 134 PHE A CG    1 
ATOM   817  C CD1   . PHE A 1 111 ? 7.453   3.435   5.124   1.00 21.60 ? 134 PHE A CD1   1 
ATOM   818  C CD2   . PHE A 1 111 ? 6.141   5.314   5.822   1.00 21.97 ? 134 PHE A CD2   1 
ATOM   819  C CE1   . PHE A 1 111 ? 7.172   2.791   6.328   1.00 25.21 ? 134 PHE A CE1   1 
ATOM   820  C CE2   . PHE A 1 111 ? 5.851   4.678   7.040   1.00 22.74 ? 134 PHE A CE2   1 
ATOM   821  C CZ    . PHE A 1 111 ? 6.361   3.420   7.288   1.00 24.18 ? 134 PHE A CZ    1 
ATOM   822  N N     . PRO A 1 112 ? 6.224   7.000   0.905   1.00 20.90 ? 135 PRO A N     1 
ATOM   823  C CA    . PRO A 1 112 ? 6.638   7.690   -0.323  1.00 24.83 ? 135 PRO A CA    1 
ATOM   824  C C     . PRO A 1 112 ? 8.150   7.835   -0.376  1.00 24.89 ? 135 PRO A C     1 
ATOM   825  O O     . PRO A 1 112 ? 8.820   7.960   0.654   1.00 21.65 ? 135 PRO A O     1 
ATOM   826  C CB    . PRO A 1 112 ? 5.967   9.066   -0.214  1.00 25.74 ? 135 PRO A CB    1 
ATOM   827  C CG    . PRO A 1 112 ? 5.042   8.988   0.948   1.00 30.78 ? 135 PRO A CG    1 
ATOM   828  C CD    . PRO A 1 112 ? 5.566   7.917   1.849   1.00 24.76 ? 135 PRO A CD    1 
ATOM   829  N N     . MET A 1 113 ? 8.675   7.831   -1.604  1.00 25.08 ? 136 MET A N     1 
ATOM   830  C CA    . MET A 1 113 ? 10.113  7.967   -1.816  1.00 23.91 ? 136 MET A CA    1 
ATOM   831  C C     . MET A 1 113 ? 10.682  9.167   -1.067  1.00 26.82 ? 136 MET A C     1 
ATOM   832  O O     . MET A 1 113 ? 11.747  9.067   -0.449  1.00 25.38 ? 136 MET A O     1 
ATOM   833  C CB    . MET A 1 113 ? 10.411  8.080   -3.318  1.00 26.49 ? 136 MET A CB    1 
ATOM   834  C CG    . MET A 1 113 ? 11.901  8.144   -3.644  1.00 25.81 ? 136 MET A CG    1 
ATOM   835  S SD    . MET A 1 113 ? 12.812  6.694   -3.061  1.00 28.78 ? 136 MET A SD    1 
ATOM   836  C CE    . MET A 1 113 ? 12.420  5.476   -4.334  1.00 27.07 ? 136 MET A CE    1 
ATOM   837  N N     . ALA A 1 114 ? 9.969   10.305  -1.089  1.00 26.23 ? 137 ALA A N     1 
ATOM   838  C CA    . ALA A 1 114 ? 10.470  11.514  -0.438  1.00 25.35 ? 137 ALA A CA    1 
ATOM   839  C C     . ALA A 1 114 ? 10.704  11.301  1.057   1.00 25.66 ? 137 ALA A C     1 
ATOM   840  O O     . ALA A 1 114 ? 11.695  11.786  1.612   1.00 24.91 ? 137 ALA A O     1 
ATOM   841  C CB    . ALA A 1 114 ? 9.499   12.673  -0.663  1.00 28.29 ? 137 ALA A CB    1 
ATOM   842  N N     . ALA A 1 115 ? 9.792   10.596  1.727   1.00 23.17 ? 138 ALA A N     1 
ATOM   843  C CA    . ALA A 1 115 ? 9.982   10.274  3.139   1.00 23.98 ? 138 ALA A CA    1 
ATOM   844  C C     . ALA A 1 115 ? 11.203  9.380   3.366   1.00 22.34 ? 138 ALA A C     1 
ATOM   845  O O     . ALA A 1 115 ? 11.933  9.548   4.354   1.00 20.14 ? 138 ALA A O     1 
ATOM   846  C CB    . ALA A 1 115 ? 8.720   9.593   3.684   1.00 19.94 ? 138 ALA A CB    1 
ATOM   847  N N     . ARG A 1 116 ? 11.426  8.403   2.483   1.00 19.05 ? 139 ARG A N     1 
ATOM   848  C CA    . ARG A 1 116 ? 12.579  7.517   2.645   1.00 21.87 ? 139 ARG A CA    1 
ATOM   849  C C     . ARG A 1 116 ? 13.884  8.294   2.539   1.00 21.37 ? 139 ARG A C     1 
ATOM   850  O O     . ARG A 1 116 ? 14.822  8.077   3.319   1.00 19.70 ? 139 ARG A O     1 
ATOM   851  C CB    . ARG A 1 116 ? 12.555  6.407   1.587   1.00 22.66 ? 139 ARG A CB    1 
ATOM   852  C CG    . ARG A 1 116 ? 11.187  5.803   1.296   1.00 22.63 ? 139 ARG A CG    1 
ATOM   853  C CD    . ARG A 1 116 ? 11.279  4.714   0.219   1.00 22.24 ? 139 ARG A CD    1 
ATOM   854  N NE    . ARG A 1 116 ? 9.964   4.465   -0.365  1.00 21.36 ? 139 ARG A NE    1 
ATOM   855  C CZ    . ARG A 1 116 ? 9.749   3.886   -1.540  1.00 28.35 ? 139 ARG A CZ    1 
ATOM   856  N NH1   . ARG A 1 116 ? 10.770  3.468   -2.284  1.00 22.59 ? 139 ARG A NH1   1 
ATOM   857  N NH2   . ARG A 1 116 ? 8.500   3.724   -1.969  1.00 24.15 ? 139 ARG A NH2   1 
ATOM   858  N N     . ILE A 1 117 ? 13.973  9.175   1.539   1.00 18.73 ? 140 ILE A N     1 
ATOM   859  C CA    . ILE A 1 117 ? 15.161  10.001  1.355   1.00 19.15 ? 140 ILE A CA    1 
ATOM   860  C C     . ILE A 1 117 ? 15.407  10.850  2.591   1.00 20.65 ? 140 ILE A C     1 
ATOM   861  O O     . ILE A 1 117 ? 16.524  10.912  3.114   1.00 22.15 ? 140 ILE A O     1 
ATOM   862  C CB    . ILE A 1 117 ? 15.000  10.881  0.104   1.00 19.93 ? 140 ILE A CB    1 
ATOM   863  C CG1   . ILE A 1 117 ? 14.993  10.048  -1.179  1.00 19.22 ? 140 ILE A CG1   1 
ATOM   864  C CG2   . ILE A 1 117 ? 16.085  11.958  0.055   1.00 21.65 ? 140 ILE A CG2   1 
ATOM   865  C CD1   . ILE A 1 117 ? 14.571  10.896  -2.406  1.00 22.98 ? 140 ILE A CD1   1 
ATOM   866  N N     . LYS A 1 118 ? 14.364  11.534  3.063   1.00 21.97 ? 141 LYS A N     1 
ATOM   867  C CA    . LYS A 1 118 ? 14.493  12.386  4.243   1.00 19.54 ? 141 LYS A CA    1 
ATOM   868  C C     . LYS A 1 118 ? 14.934  11.588  5.468   1.00 20.54 ? 141 LYS A C     1 
ATOM   869  O O     . LYS A 1 118 ? 15.833  12.013  6.204   1.00 23.48 ? 141 LYS A O     1 
ATOM   870  C CB    . LYS A 1 118 ? 13.166  13.100  4.511   1.00 23.00 ? 141 LYS A CB    1 
ATOM   871  C CG    . LYS A 1 118 ? 13.244  14.102  5.657   1.00 23.27 ? 141 LYS A CG    1 
ATOM   872  C CD    . LYS A 1 118 ? 11.898  14.759  5.888   1.00 29.52 ? 141 LYS A CD    1 
ATOM   873  C CE    . LYS A 1 118 ? 12.009  15.852  6.934   1.00 41.31 ? 141 LYS A CE    1 
ATOM   874  N NZ    . LYS A 1 118 ? 10.844  16.771  6.879   1.00 46.49 ? 141 LYS A NZ    1 
ATOM   875  N N     . LEU A 1 119 ? 14.328  10.413  5.698   1.00 19.82 ? 142 LEU A N     1 
ATOM   876  C CA    . LEU A 1 119 ? 14.732  9.602   6.847   1.00 20.13 ? 142 LEU A CA    1 
ATOM   877  C C     . LEU A 1 119 ? 16.204  9.228   6.761   1.00 17.86 ? 142 LEU A C     1 
ATOM   878  O O     . LEU A 1 119 ? 16.945  9.339   7.744   1.00 19.62 ? 142 LEU A O     1 
ATOM   879  C CB    . LEU A 1 119 ? 13.868  8.338   6.956   1.00 17.21 ? 142 LEU A CB    1 
ATOM   880  C CG    . LEU A 1 119 ? 14.295  7.459   8.133   1.00 20.54 ? 142 LEU A CG    1 
ATOM   881  C CD1   . LEU A 1 119 ? 14.271  8.257   9.449   1.00 22.60 ? 142 LEU A CD1   1 
ATOM   882  C CD2   . LEU A 1 119 ? 13.447  6.199   8.249   1.00 21.30 ? 142 LEU A CD2   1 
ATOM   883  N N     . LEU A 1 120 ? 16.649  8.780   5.580   1.00 19.77 ? 143 LEU A N     1 
ATOM   884  C CA    . LEU A 1 120 ? 18.040  8.365   5.422   1.00 19.66 ? 143 LEU A CA    1 
ATOM   885  C C     . LEU A 1 120 ? 18.994  9.524   5.686   1.00 21.04 ? 143 LEU A C     1 
ATOM   886  O O     . LEU A 1 120 ? 20.016  9.358   6.364   1.00 19.76 ? 143 LEU A O     1 
ATOM   887  C CB    . LEU A 1 120 ? 18.254  7.800   4.012   1.00 20.75 ? 143 LEU A CB    1 
ATOM   888  C CG    . LEU A 1 120 ? 19.684  7.421   3.635   1.00 26.81 ? 143 LEU A CG    1 
ATOM   889  C CD1   . LEU A 1 120 ? 20.240  6.414   4.655   1.00 21.93 ? 143 LEU A CD1   1 
ATOM   890  C CD2   . LEU A 1 120 ? 19.732  6.870   2.191   1.00 21.46 ? 143 LEU A CD2   1 
ATOM   891  N N     . ASP A 1 121 ? 18.647  10.717  5.186   1.00 21.43 ? 144 ASP A N     1 
ATOM   892  C CA    . ASP A 1 121 ? 19.457  11.906  5.417   1.00 22.91 ? 144 ASP A CA    1 
ATOM   893  C C     . ASP A 1 121 ? 19.542  12.247  6.906   1.00 28.16 ? 144 ASP A C     1 
ATOM   894  O O     . ASP A 1 121 ? 20.601  12.672  7.386   1.00 20.60 ? 144 ASP A O     1 
ATOM   895  C CB    . ASP A 1 121 ? 18.878  13.075  4.617   1.00 24.82 ? 144 ASP A CB    1 
ATOM   896  C CG    . ASP A 1 121 ? 19.675  14.372  4.794   1.00 32.30 ? 144 ASP A CG    1 
ATOM   897  O OD1   . ASP A 1 121 ? 20.882  14.418  4.431   1.00 27.60 ? 144 ASP A OD1   1 
ATOM   898  O OD2   . ASP A 1 121 ? 19.081  15.350  5.302   1.00 31.59 ? 144 ASP A OD2   1 
ATOM   899  N N     . GLU A 1 122 ? 18.444  12.048  7.652   1.00 19.88 ? 145 GLU A N     1 
ATOM   900  C CA    . GLU A 1 122 ? 18.452  12.290  9.100   1.00 25.75 ? 145 GLU A CA    1 
ATOM   901  C C     . GLU A 1 122 ? 19.224  11.217  9.864   1.00 23.11 ? 145 GLU A C     1 
ATOM   902  O O     . GLU A 1 122 ? 19.923  11.534  10.837  1.00 25.51 ? 145 GLU A O     1 
ATOM   903  C CB    . GLU A 1 122 ? 17.021  12.371  9.653   1.00 24.87 ? 145 GLU A CB    1 
ATOM   904  C CG    . GLU A 1 122 ? 16.306  13.684  9.340   1.00 33.07 ? 145 GLU A CG    1 
ATOM   905  C CD    . GLU A 1 122 ? 17.058  14.890  9.906   1.00 43.77 ? 145 GLU A CD    1 
ATOM   906  O OE1   . GLU A 1 122 ? 17.435  14.849  11.102  1.00 46.84 ? 145 GLU A OE1   1 
ATOM   907  O OE2   . GLU A 1 122 ? 17.283  15.872  9.158   1.00 49.88 ? 145 GLU A OE2   1 
ATOM   908  N N     . LEU A 1 123 ? 19.067  9.939   9.495   1.00 18.35 ? 146 LEU A N     1 
ATOM   909  C CA    . LEU A 1 123 ? 19.828  8.891   10.182  1.00 18.46 ? 146 LEU A CA    1 
ATOM   910  C C     . LEU A 1 123 ? 21.326  9.111   10.027  1.00 22.52 ? 146 LEU A C     1 
ATOM   911  O O     . LEU A 1 123 ? 22.093  8.946   10.984  1.00 20.70 ? 146 LEU A O     1 
ATOM   912  C CB    . LEU A 1 123 ? 19.444  7.505   9.645   1.00 19.57 ? 146 LEU A CB    1 
ATOM   913  C CG    . LEU A 1 123 ? 18.032  7.007   9.932   1.00 20.80 ? 146 LEU A CG    1 
ATOM   914  C CD1   . LEU A 1 123 ? 17.659  5.876   8.989   1.00 18.02 ? 146 LEU A CD1   1 
ATOM   915  C CD2   . LEU A 1 123 ? 17.878  6.583   11.408  1.00 18.65 ? 146 LEU A CD2   1 
ATOM   916  N N     . LEU A 1 124 ? 21.760  9.494   8.826   1.00 19.62 ? 147 LEU A N     1 
ATOM   917  C CA    . LEU A 1 124 ? 23.181  9.677   8.579   1.00 20.46 ? 147 LEU A CA    1 
ATOM   918  C C     . LEU A 1 124 ? 23.758  10.858  9.357   1.00 22.61 ? 147 LEU A C     1 
ATOM   919  O O     . LEU A 1 124 ? 24.979  10.947  9.505   1.00 21.79 ? 147 LEU A O     1 
ATOM   920  C CB    . LEU A 1 124 ? 23.426  9.838   7.075   1.00 20.77 ? 147 LEU A CB    1 
ATOM   921  C CG    . LEU A 1 124 ? 23.298  8.521   6.286   1.00 22.72 ? 147 LEU A CG    1 
ATOM   922  C CD1   . LEU A 1 124 ? 23.445  8.766   4.780   1.00 22.20 ? 147 LEU A CD1   1 
ATOM   923  C CD2   . LEU A 1 124 ? 24.324  7.489   6.731   1.00 20.17 ? 147 LEU A CD2   1 
ATOM   924  N N     . LYS A 1 125 ? 22.915  11.757  9.869   1.00 24.19 ? 148 LYS A N     1 
ATOM   925  C CA    . LYS A 1 125 ? 23.399  12.776  10.794  1.00 21.59 ? 148 LYS A CA    1 
ATOM   926  C C     . LYS A 1 125 ? 23.800  12.200  12.146  1.00 21.91 ? 148 LYS A C     1 
ATOM   927  O O     . LYS A 1 125 ? 24.579  12.834  12.871  1.00 20.27 ? 148 LYS A O     1 
ATOM   928  C CB    . LYS A 1 125 ? 22.337  13.843  10.996  1.00 20.07 ? 148 LYS A CB    1 
ATOM   929  C CG    . LYS A 1 125 ? 22.132  14.695  9.763   1.00 27.99 ? 148 LYS A CG    1 
ATOM   930  C CD    . LYS A 1 125 ? 21.107  15.791  10.010  1.00 32.29 ? 148 LYS A CD    1 
ATOM   931  C CE    . LYS A 1 125 ? 20.694  16.441  8.695   1.00 30.40 ? 148 LYS A CE    1 
ATOM   932  N NZ    . LYS A 1 125 ? 19.520  17.332  8.909   1.00 39.03 ? 148 LYS A NZ    1 
ATOM   933  N N     . ARG A 1 126 ? 23.293  11.018  12.498  1.00 17.88 ? 149 ARG A N     1 
ATOM   934  C CA    . ARG A 1 126 ? 23.459  10.458  13.834  1.00 23.26 ? 149 ARG A CA    1 
ATOM   935  C C     . ARG A 1 126 ? 24.418  9.274   13.868  1.00 19.96 ? 149 ARG A C     1 
ATOM   936  O O     . ARG A 1 126 ? 24.420  8.504   14.842  1.00 19.50 ? 149 ARG A O     1 
ATOM   937  C CB    . ARG A 1 126 ? 22.092  10.063  14.389  1.00 22.75 ? 149 ARG A CB    1 
ATOM   938  C CG    . ARG A 1 126 ? 21.234  11.271  14.619  1.00 24.61 ? 149 ARG A CG    1 
ATOM   939  C CD    . ARG A 1 126 ? 19.775  10.932  14.660  1.00 30.80 ? 149 ARG A CD    1 
ATOM   940  N NE    . ARG A 1 126 ? 19.215  11.393  15.907  1.00 38.78 ? 149 ARG A NE    1 
ATOM   941  C CZ    . ARG A 1 126 ? 18.260  12.301  16.029  1.00 33.27 ? 149 ARG A CZ    1 
ATOM   942  N NH1   . ARG A 1 126 ? 17.717  12.875  14.971  1.00 43.39 ? 149 ARG A NH1   1 
ATOM   943  N NH2   . ARG A 1 126 ? 17.846  12.617  17.232  1.00 34.03 ? 149 ARG A NH2   1 
ATOM   944  N N     . VAL A 1 127 ? 25.216  9.097   12.818  1.00 19.58 ? 150 VAL A N     1 
ATOM   945  C CA    . VAL A 1 127 ? 26.312  8.138   12.852  1.00 18.06 ? 150 VAL A CA    1 
ATOM   946  C C     . VAL A 1 127 ? 27.546  8.901   12.397  1.00 21.88 ? 150 VAL A C     1 
ATOM   947  O O     . VAL A 1 127 ? 27.427  9.871   11.630  1.00 20.86 ? 150 VAL A O     1 
ATOM   948  C CB    . VAL A 1 127 ? 26.056  6.898   11.969  1.00 21.55 ? 150 VAL A CB    1 
ATOM   949  C CG1   . VAL A 1 127 ? 24.765  6.171   12.379  1.00 19.04 ? 150 VAL A CG1   1 
ATOM   950  C CG2   . VAL A 1 127 ? 26.050  7.282   10.484  1.00 15.27 ? 150 VAL A CG2   1 
ATOM   951  N N     . PRO A 1 128 ? 28.743  8.487   12.821  1.00 21.65 ? 151 PRO A N     1 
ATOM   952  C CA    . PRO A 1 128 ? 29.955  9.173   12.373  1.00 19.30 ? 151 PRO A CA    1 
ATOM   953  C C     . PRO A 1 128 ? 30.082  9.107   10.861  1.00 22.90 ? 151 PRO A C     1 
ATOM   954  O O     . PRO A 1 128 ? 29.651  8.141   10.221  1.00 19.68 ? 151 PRO A O     1 
ATOM   955  C CB    . PRO A 1 128 ? 31.085  8.395   13.064  1.00 17.19 ? 151 PRO A CB    1 
ATOM   956  C CG    . PRO A 1 128 ? 30.416  7.743   14.263  1.00 21.54 ? 151 PRO A CG    1 
ATOM   957  C CD    . PRO A 1 128 ? 29.032  7.403   13.772  1.00 19.89 ? 151 PRO A CD    1 
ATOM   958  N N     . HIS A 1 129 ? 30.675  10.163  10.297  1.00 20.59 ? 152 HIS A N     1 
ATOM   959  C CA    . HIS A 1 129 ? 30.905  10.236  8.864   1.00 22.77 ? 152 HIS A CA    1 
ATOM   960  C C     . HIS A 1 129 ? 31.622  8.985   8.369   1.00 24.45 ? 152 HIS A C     1 
ATOM   961  O O     . HIS A 1 129 ? 32.703  8.642   8.862   1.00 27.63 ? 152 HIS A O     1 
ATOM   962  C CB    . HIS A 1 129 ? 31.717  11.492  8.543   1.00 21.84 ? 152 HIS A CB    1 
ATOM   963  C CG    . HIS A 1 129 ? 31.683  11.869  7.099   1.00 23.75 ? 152 HIS A CG    1 
ATOM   964  N ND1   . HIS A 1 129 ? 32.667  11.497  6.210   1.00 31.34 ? 152 HIS A ND1   1 
ATOM   965  C CD2   . HIS A 1 129 ? 30.770  12.560  6.380   1.00 24.88 ? 152 HIS A CD2   1 
ATOM   966  C CE1   . HIS A 1 129 ? 32.365  11.949  5.006   1.00 26.51 ? 152 HIS A CE1   1 
ATOM   967  N NE2   . HIS A 1 129 ? 31.220  12.601  5.082   1.00 29.51 ? 152 HIS A NE2   1 
ATOM   968  N N     . GLY A 1 130 ? 30.993  8.272   7.424   1.00 26.27 ? 153 GLY A N     1 
ATOM   969  C CA    . GLY A 1 130 ? 31.544  7.054   6.857   1.00 21.87 ? 153 GLY A CA    1 
ATOM   970  C C     . GLY A 1 130 ? 30.946  5.759   7.383   1.00 24.11 ? 153 GLY A C     1 
ATOM   971  O O     . GLY A 1 130 ? 31.183  4.703   6.788   1.00 21.45 ? 153 GLY A O     1 
ATOM   972  N N     . ARG A 1 131 ? 30.188  5.803   8.470   1.00 22.22 ? 154 ARG A N     1 
ATOM   973  C CA    . ARG A 1 131 ? 29.527  4.623   9.011   1.00 21.07 ? 154 ARG A CA    1 
ATOM   974  C C     . ARG A 1 131 ? 28.186  4.401   8.317   1.00 22.61 ? 154 ARG A C     1 
ATOM   975  O O     . ARG A 1 131 ? 27.617  5.335   7.739   1.00 19.64 ? 154 ARG A O     1 
ATOM   976  C CB    . ARG A 1 131 ? 29.331  4.781   10.517  1.00 19.65 ? 154 ARG A CB    1 
ATOM   977  C CG    . ARG A 1 131 ? 30.643  4.676   11.331  1.00 20.03 ? 154 ARG A CG    1 
ATOM   978  C CD    . ARG A 1 131 ? 31.348  3.319   11.115  1.00 20.92 ? 154 ARG A CD    1 
ATOM   979  N NE    . ARG A 1 131 ? 30.600  2.206   11.704  1.00 24.98 ? 154 ARG A NE    1 
ATOM   980  C CZ    . ARG A 1 131 ? 30.690  0.947   11.281  1.00 25.97 ? 154 ARG A CZ    1 
ATOM   981  N NH1   . ARG A 1 131 ? 31.500  0.654   10.269  1.00 27.34 ? 154 ARG A NH1   1 
ATOM   982  N NH2   . ARG A 1 131 ? 29.973  -0.017  11.866  1.00 23.20 ? 154 ARG A NH2   1 
ATOM   983  N N     . PRO A 1 132 ? 27.636  3.160   8.364   1.00 22.99 ? 155 PRO A N     1 
ATOM   984  C CA    . PRO A 1 132 ? 26.511  2.825   7.478   1.00 19.55 ? 155 PRO A CA    1 
ATOM   985  C C     . PRO A 1 132 ? 25.122  2.750   8.100   1.00 22.87 ? 155 PRO A C     1 
ATOM   986  O O     . PRO A 1 132 ? 24.930  2.481   9.296   1.00 19.23 ? 155 PRO A O     1 
ATOM   987  C CB    . PRO A 1 132 ? 26.918  1.438   6.957   1.00 19.19 ? 155 PRO A CB    1 
ATOM   988  C CG    . PRO A 1 132 ? 27.514  0.789   8.190   1.00 20.54 ? 155 PRO A CG    1 
ATOM   989  C CD    . PRO A 1 132 ? 28.240  1.936   8.942   1.00 24.13 ? 155 PRO A CD    1 
ATOM   990  N N     . VAL A 1 133 ? 24.131  2.979   7.248   1.00 22.77 ? 156 VAL A N     1 
ATOM   991  C CA    . VAL A 1 133 ? 22.781  2.460   7.429   1.00 18.79 ? 156 VAL A CA    1 
ATOM   992  C C     . VAL A 1 133 ? 22.662  1.231   6.534   1.00 20.79 ? 156 VAL A C     1 
ATOM   993  O O     . VAL A 1 133 ? 23.004  1.300   5.345   1.00 19.82 ? 156 VAL A O     1 
ATOM   994  C CB    . VAL A 1 133 ? 21.718  3.507   7.044   1.00 19.98 ? 156 VAL A CB    1 
ATOM   995  C CG1   . VAL A 1 133 ? 20.305  2.886   7.110   1.00 20.67 ? 156 VAL A CG1   1 
ATOM   996  C CG2   . VAL A 1 133 ? 21.812  4.779   7.924   1.00 19.32 ? 156 VAL A CG2   1 
ATOM   997  N N     . VAL A 1 134 ? 22.211  0.101   7.085   1.00 18.93 ? 157 VAL A N     1 
ATOM   998  C CA    . VAL A 1 134 ? 21.932  -1.082  6.270   1.00 17.24 ? 157 VAL A CA    1 
ATOM   999  C C     . VAL A 1 134 ? 20.430  -1.323  6.264   1.00 20.30 ? 157 VAL A C     1 
ATOM   1000 O O     . VAL A 1 134 ? 19.756  -1.203  7.300   1.00 20.77 ? 157 VAL A O     1 
ATOM   1001 C CB    . VAL A 1 134 ? 22.705  -2.335  6.744   1.00 20.55 ? 157 VAL A CB    1 
ATOM   1002 C CG1   . VAL A 1 134 ? 22.353  -2.685  8.148   1.00 21.27 ? 157 VAL A CG1   1 
ATOM   1003 C CG2   . VAL A 1 134 ? 22.410  -3.532  5.841   1.00 21.91 ? 157 VAL A CG2   1 
ATOM   1004 N N     . GLN A 1 135 ? 19.900  -1.635  5.086   1.00 19.71 ? 158 GLN A N     1 
ATOM   1005 C CA    . GLN A 1 135 ? 18.465  -1.759  4.863   1.00 20.73 ? 158 GLN A CA    1 
ATOM   1006 C C     . GLN A 1 135 ? 18.180  -3.030  4.065   1.00 22.86 ? 158 GLN A C     1 
ATOM   1007 O O     . GLN A 1 135 ? 18.910  -3.355  3.122   1.00 21.49 ? 158 GLN A O     1 
ATOM   1008 C CB    . GLN A 1 135 ? 17.927  -0.522  4.111   1.00 19.04 ? 158 GLN A CB    1 
ATOM   1009 C CG    . GLN A 1 135 ? 16.457  -0.618  3.628   1.00 16.34 ? 158 GLN A CG    1 
ATOM   1010 C CD    . GLN A 1 135 ? 15.473  -0.500  4.758   1.00 24.21 ? 158 GLN A CD    1 
ATOM   1011 O OE1   . GLN A 1 135 ? 15.579  0.408   5.577   1.00 20.03 ? 158 GLN A OE1   1 
ATOM   1012 N NE2   . GLN A 1 135 ? 14.510  -1.428  4.824   1.00 23.54 ? 158 GLN A NE2   1 
ATOM   1013 N N     . ILE A 1 136 ? 17.123  -3.744  4.450   1.00 22.98 ? 159 ILE A N     1 
ATOM   1014 C CA    . ILE A 1 136 ? 16.640  -4.926  3.734   1.00 17.63 ? 159 ILE A CA    1 
ATOM   1015 C C     . ILE A 1 136 ? 15.519  -4.510  2.790   1.00 22.68 ? 159 ILE A C     1 
ATOM   1016 O O     . ILE A 1 136 ? 14.691  -3.652  3.127   1.00 20.81 ? 159 ILE A O     1 
ATOM   1017 C CB    . ILE A 1 136 ? 16.154  -5.999  4.728   1.00 21.25 ? 159 ILE A CB    1 
ATOM   1018 C CG1   . ILE A 1 136 ? 15.683  -7.259  3.991   1.00 22.69 ? 159 ILE A CG1   1 
ATOM   1019 C CG2   . ILE A 1 136 ? 15.006  -5.456  5.560   1.00 22.36 ? 159 ILE A CG2   1 
ATOM   1020 C CD1   . ILE A 1 136 ? 15.462  -8.454  4.910   1.00 25.75 ? 159 ILE A CD1   1 
ATOM   1021 N N     . SER A 1 137 ? 15.510  -5.084  1.588   1.00 23.15 ? 160 SER A N     1 
ATOM   1022 C CA    . SER A 1 137 ? 14.399  -4.907  0.657   1.00 27.89 ? 160 SER A CA    1 
ATOM   1023 C C     . SER A 1 137 ? 14.330  -6.142  -0.240  1.00 26.81 ? 160 SER A C     1 
ATOM   1024 O O     . SER A 1 137 ? 15.076  -7.107  -0.049  1.00 25.82 ? 160 SER A O     1 
ATOM   1025 C CB    . SER A 1 137 ? 14.541  -3.611  -0.149  1.00 26.58 ? 160 SER A CB    1 
ATOM   1026 O OG    . SER A 1 137 ? 15.686  -3.651  -0.988  1.00 27.12 ? 160 SER A OG    1 
ATOM   1027 N N     . TYR A 1 138 ? 13.424  -6.111  -1.227  1.00 29.21 ? 161 TYR A N     1 
ATOM   1028 C CA    . TYR A 1 138 ? 13.106  -7.306  -2.013  1.00 36.19 ? 161 TYR A CA    1 
ATOM   1029 C C     . TYR A 1 138 ? 13.102  -7.091  -3.516  1.00 40.52 ? 161 TYR A C     1 
ATOM   1030 O O     . TYR A 1 138 ? 13.205  -8.078  -4.260  1.00 41.00 ? 161 TYR A O     1 
ATOM   1031 C CB    . TYR A 1 138 ? 11.746  -7.880  -1.579  1.00 31.26 ? 161 TYR A CB    1 
ATOM   1032 C CG    . TYR A 1 138 ? 11.690  -8.054  -0.077  1.00 32.44 ? 161 TYR A CG    1 
ATOM   1033 C CD1   . TYR A 1 138 ? 12.304  -9.137  0.533   1.00 30.84 ? 161 TYR A CD1   1 
ATOM   1034 C CD2   . TYR A 1 138 ? 11.088  -7.101  0.737   1.00 34.46 ? 161 TYR A CD2   1 
ATOM   1035 C CE1   . TYR A 1 138 ? 12.287  -9.288  1.911   1.00 31.68 ? 161 TYR A CE1   1 
ATOM   1036 C CE2   . TYR A 1 138 ? 11.070  -7.242  2.117   1.00 29.48 ? 161 TYR A CE2   1 
ATOM   1037 C CZ    . TYR A 1 138 ? 11.673  -8.342  2.696   1.00 31.25 ? 161 TYR A CZ    1 
ATOM   1038 O OH    . TYR A 1 138 ? 11.671  -8.501  4.068   1.00 32.17 ? 161 TYR A OH    1 
ATOM   1039 N N     . GLY A 1 139 ? 13.018  -5.858  -3.991  1.00 32.61 ? 162 GLY A N     1 
ATOM   1040 C CA    . GLY A 1 139 ? 13.063  -5.603  -5.413  1.00 41.25 ? 162 GLY A CA    1 
ATOM   1041 C C     . GLY A 1 139 ? 14.447  -5.759  -6.022  1.00 44.96 ? 162 GLY A C     1 
ATOM   1042 O O     . GLY A 1 139 ? 15.413  -6.165  -5.364  1.00 39.62 ? 162 GLY A O     1 
ATOM   1043 N N     . PRO A 1 140 ? 14.564  -5.441  -7.314  1.00 44.90 ? 163 PRO A N     1 
ATOM   1044 C CA    . PRO A 1 140 ? 15.871  -5.479  -7.973  1.00 41.47 ? 163 PRO A CA    1 
ATOM   1045 C C     . PRO A 1 140 ? 16.695  -4.216  -7.796  1.00 38.33 ? 163 PRO A C     1 
ATOM   1046 O O     . PRO A 1 140 ? 17.903  -4.249  -8.074  1.00 35.87 ? 163 PRO A O     1 
ATOM   1047 C CB    . PRO A 1 140 ? 15.491  -5.677  -9.448  1.00 47.31 ? 163 PRO A CB    1 
ATOM   1048 C CG    . PRO A 1 140 ? 14.173  -4.992  -9.577  1.00 42.25 ? 163 PRO A CG    1 
ATOM   1049 C CD    . PRO A 1 140 ? 13.466  -5.152  -8.257  1.00 43.54 ? 163 PRO A CD    1 
ATOM   1050 N N     . ILE A 1 141 ? 16.100  -3.113  -7.342  1.00 34.17 ? 164 ILE A N     1 
ATOM   1051 C CA    . ILE A 1 141 ? 16.834  -1.869  -7.170  1.00 33.27 ? 164 ILE A CA    1 
ATOM   1052 C C     . ILE A 1 141 ? 16.730  -1.415  -5.715  1.00 31.31 ? 164 ILE A C     1 
ATOM   1053 O O     . ILE A 1 141 ? 15.916  -1.917  -4.937  1.00 27.31 ? 164 ILE A O     1 
ATOM   1054 C CB    . ILE A 1 141 ? 16.352  -0.763  -8.128  1.00 34.83 ? 164 ILE A CB    1 
ATOM   1055 C CG1   . ILE A 1 141 ? 14.837  -0.570  -8.006  1.00 32.16 ? 164 ILE A CG1   1 
ATOM   1056 C CG2   . ILE A 1 141 ? 16.762  -1.100  -9.572  1.00 35.77 ? 164 ILE A CG2   1 
ATOM   1057 C CD1   . ILE A 1 141 ? 14.372  0.817   -8.401  1.00 39.06 ? 164 ILE A CD1   1 
ATOM   1058 N N     . SER A 1 142 ? 17.599  -0.465  -5.363  1.00 27.53 ? 165 SER A N     1 
ATOM   1059 C CA    . SER A 1 142 ? 17.619  0.099   -4.020  1.00 29.78 ? 165 SER A CA    1 
ATOM   1060 C C     . SER A 1 142 ? 16.252  0.673   -3.665  1.00 26.04 ? 165 SER A C     1 
ATOM   1061 O O     . SER A 1 142 ? 15.670  1.406   -4.473  1.00 23.49 ? 165 SER A O     1 
ATOM   1062 C CB    . SER A 1 142 ? 18.673  1.200   -3.934  1.00 26.25 ? 165 SER A CB    1 
ATOM   1063 O OG    . SER A 1 142 ? 18.464  2.003   -2.784  1.00 27.29 ? 165 SER A OG    1 
ATOM   1064 N N     . PRO A 1 143 ? 15.717  0.385   -2.478  1.00 27.68 ? 166 PRO A N     1 
ATOM   1065 C CA    . PRO A 1 143 ? 14.444  1.001   -2.076  1.00 23.21 ? 166 PRO A CA    1 
ATOM   1066 C C     . PRO A 1 143 ? 14.527  2.515   -1.928  1.00 27.88 ? 166 PRO A C     1 
ATOM   1067 O O     . PRO A 1 143 ? 13.485  3.176   -1.813  1.00 26.94 ? 166 PRO A O     1 
ATOM   1068 C CB    . PRO A 1 143 ? 14.145  0.326   -0.736  1.00 27.70 ? 166 PRO A CB    1 
ATOM   1069 C CG    . PRO A 1 143 ? 15.494  0.044   -0.179  1.00 24.64 ? 166 PRO A CG    1 
ATOM   1070 C CD    . PRO A 1 143 ? 16.352  -0.340  -1.364  1.00 28.01 ? 166 PRO A CD    1 
ATOM   1071 N N     . ILE A 1 144 ? 15.726  3.088   -1.921  1.00 25.77 ? 167 ILE A N     1 
ATOM   1072 C CA    . ILE A 1 144 ? 15.911  4.528   -1.817  1.00 24.85 ? 167 ILE A CA    1 
ATOM   1073 C C     . ILE A 1 144 ? 16.740  4.959   -3.012  1.00 24.65 ? 167 ILE A C     1 
ATOM   1074 O O     . ILE A 1 144 ? 17.845  4.437   -3.230  1.00 26.91 ? 167 ILE A O     1 
ATOM   1075 C CB    . ILE A 1 144 ? 16.586  4.929   -0.499  1.00 26.24 ? 167 ILE A CB    1 
ATOM   1076 C CG1   . ILE A 1 144 ? 15.877  4.247   0.677   1.00 26.70 ? 167 ILE A CG1   1 
ATOM   1077 C CG2   . ILE A 1 144 ? 16.586  6.449   -0.349  1.00 24.97 ? 167 ILE A CG2   1 
ATOM   1078 C CD1   . ILE A 1 144 ? 16.570  4.431   1.997   1.00 27.74 ? 167 ILE A CD1   1 
ATOM   1079 N N     . VAL A 1 145 ? 16.212  5.911   -3.780  1.00 25.00 ? 168 VAL A N     1 
ATOM   1080 C CA    . VAL A 1 145 ? 16.829  6.291   -5.050  1.00 27.92 ? 168 VAL A CA    1 
ATOM   1081 C C     . VAL A 1 145 ? 18.107  7.088   -4.797  1.00 26.15 ? 168 VAL A C     1 
ATOM   1082 O O     . VAL A 1 145 ? 18.262  7.752   -3.764  1.00 23.80 ? 168 VAL A O     1 
ATOM   1083 C CB    . VAL A 1 145 ? 15.823  7.085   -5.902  1.00 26.99 ? 168 VAL A CB    1 
ATOM   1084 C CG1   . VAL A 1 145 ? 15.655  8.512   -5.370  1.00 27.94 ? 168 VAL A CG1   1 
ATOM   1085 C CG2   . VAL A 1 145 ? 16.236  7.083   -7.377  1.00 30.39 ? 168 VAL A CG2   1 
ATOM   1086 N N     . ALA A 1 146 ? 19.037  7.022   -5.751  1.00 26.91 ? 169 ALA A N     1 
ATOM   1087 C CA    . ALA A 1 146 ? 20.316  7.715   -5.607  1.00 28.16 ? 169 ALA A CA    1 
ATOM   1088 C C     . ALA A 1 146 ? 20.127  9.228   -5.490  1.00 27.46 ? 169 ALA A C     1 
ATOM   1089 O O     . ALA A 1 146 ? 19.367  9.835   -6.249  1.00 28.63 ? 169 ALA A O     1 
ATOM   1090 C CB    . ALA A 1 146 ? 21.228  7.389   -6.797  1.00 28.91 ? 169 ALA A CB    1 
ATOM   1091 N N     . GLN A 1 147 ? 20.796  9.826   -4.501  1.00 23.92 ? 170 GLN A N     1 
ATOM   1092 C CA    . GLN A 1 147 ? 20.982  11.279  -4.391  1.00 24.41 ? 170 GLN A CA    1 
ATOM   1093 C C     . GLN A 1 147 ? 22.450  11.471  -4.036  1.00 26.37 ? 170 GLN A C     1 
ATOM   1094 O O     . GLN A 1 147 ? 22.801  11.574  -2.852  1.00 24.77 ? 170 GLN A O     1 
ATOM   1095 C CB    . GLN A 1 147 ? 20.071  11.909  -3.331  1.00 26.72 ? 170 GLN A CB    1 
ATOM   1096 C CG    . GLN A 1 147 ? 18.555  11.769  -3.589  1.00 24.64 ? 170 GLN A CG    1 
ATOM   1097 C CD    . GLN A 1 147 ? 18.092  12.568  -4.797  1.00 28.74 ? 170 GLN A CD    1 
ATOM   1098 O OE1   . GLN A 1 147 ? 18.721  13.555  -5.181  1.00 30.09 ? 170 GLN A OE1   1 
ATOM   1099 N NE2   . GLN A 1 147 ? 16.995  12.141  -5.405  1.00 30.70 ? 170 GLN A NE2   1 
ATOM   1100 N N     . PRO A 1 148 ? 23.340  11.487  -5.037  1.00 26.92 ? 171 PRO A N     1 
ATOM   1101 C CA    . PRO A 1 148 ? 24.784  11.364  -4.747  1.00 25.86 ? 171 PRO A CA    1 
ATOM   1102 C C     . PRO A 1 148 ? 25.383  12.525  -3.967  1.00 28.22 ? 171 PRO A C     1 
ATOM   1103 O O     . PRO A 1 148 ? 26.466  12.362  -3.391  1.00 27.92 ? 171 PRO A O     1 
ATOM   1104 C CB    . PRO A 1 148 ? 25.416  11.250  -6.146  1.00 31.72 ? 171 PRO A CB    1 
ATOM   1105 C CG    . PRO A 1 148 ? 24.296  10.702  -7.031  1.00 30.48 ? 171 PRO A CG    1 
ATOM   1106 C CD    . PRO A 1 148 ? 23.055  11.393  -6.484  1.00 27.92 ? 171 PRO A CD    1 
ATOM   1107 N N     . HIS A 1 149 ? 24.740  13.685  -3.933  1.00 26.22 ? 172 HIS A N     1 
ATOM   1108 C CA    . HIS A 1 149 ? 25.241  14.771  -3.104  1.00 27.62 ? 172 HIS A CA    1 
ATOM   1109 C C     . HIS A 1 149 ? 24.892  14.593  -1.633  1.00 25.86 ? 172 HIS A C     1 
ATOM   1110 O O     . HIS A 1 149 ? 25.369  15.381  -0.814  1.00 28.03 ? 172 HIS A O     1 
ATOM   1111 C CB    . HIS A 1 149 ? 24.686  16.110  -3.590  1.00 28.21 ? 172 HIS A CB    1 
ATOM   1112 C CG    . HIS A 1 149 ? 23.195  16.190  -3.548  1.00 28.43 ? 172 HIS A CG    1 
ATOM   1113 N ND1   . HIS A 1 149 ? 22.390  15.436  -4.375  1.00 25.97 ? 172 HIS A ND1   1 
ATOM   1114 C CD2   . HIS A 1 149 ? 22.360  16.926  -2.775  1.00 24.78 ? 172 HIS A CD2   1 
ATOM   1115 C CE1   . HIS A 1 149 ? 21.122  15.712  -4.119  1.00 26.32 ? 172 HIS A CE1   1 
ATOM   1116 N NE2   . HIS A 1 149 ? 21.078  16.616  -3.154  1.00 22.95 ? 172 HIS A NE2   1 
ATOM   1117 N N     . LEU A 1 150 ? 24.069  13.595  -1.295  1.00 21.30 ? 173 LEU A N     1 
ATOM   1118 C CA    . LEU A 1 150 ? 23.628  13.311  0.069   1.00 25.64 ? 173 LEU A CA    1 
ATOM   1119 C C     . LEU A 1 150 ? 24.205  12.028  0.648   1.00 24.40 ? 173 LEU A C     1 
ATOM   1120 O O     . LEU A 1 150 ? 24.580  12.006  1.819   1.00 24.99 ? 173 LEU A O     1 
ATOM   1121 C CB    . LEU A 1 150 ? 22.092  13.216  0.126   1.00 22.11 ? 173 LEU A CB    1 
ATOM   1122 C CG    . LEU A 1 150 ? 21.246  14.370  -0.416  1.00 27.08 ? 173 LEU A CG    1 
ATOM   1123 C CD1   . LEU A 1 150 ? 19.755  14.032  -0.300  1.00 22.89 ? 173 LEU A CD1   1 
ATOM   1124 C CD2   . LEU A 1 150 ? 21.574  15.693  0.298   1.00 25.31 ? 173 LEU A CD2   1 
ATOM   1125 N N     . TYR A 1 151 ? 24.261  10.944  -0.132  1.00 23.86 ? 174 TYR A N     1 
ATOM   1126 C CA    . TYR A 1 151 ? 24.739  9.663   0.370   1.00 21.78 ? 174 TYR A CA    1 
ATOM   1127 C C     . TYR A 1 151 ? 25.221  8.821   -0.807  1.00 23.39 ? 174 TYR A C     1 
ATOM   1128 O O     . TYR A 1 151 ? 24.927  9.124   -1.963  1.00 23.69 ? 174 TYR A O     1 
ATOM   1129 C CB    . TYR A 1 151 ? 23.633  8.942   1.164   1.00 21.82 ? 174 TYR A CB    1 
ATOM   1130 C CG    . TYR A 1 151 ? 22.279  8.997   0.484   1.00 22.03 ? 174 TYR A CG    1 
ATOM   1131 C CD1   . TYR A 1 151 ? 21.987  8.165   -0.602  1.00 23.58 ? 174 TYR A CD1   1 
ATOM   1132 C CD2   . TYR A 1 151 ? 21.308  9.883   0.908   1.00 22.83 ? 174 TYR A CD2   1 
ATOM   1133 C CE1   . TYR A 1 151 ? 20.756  8.230   -1.250  1.00 25.35 ? 174 TYR A CE1   1 
ATOM   1134 C CE2   . TYR A 1 151 ? 20.066  9.954   0.275   1.00 23.56 ? 174 TYR A CE2   1 
ATOM   1135 C CZ    . TYR A 1 151 ? 19.796  9.124   -0.795  1.00 24.60 ? 174 TYR A CZ    1 
ATOM   1136 O OH    . TYR A 1 151 ? 18.569  9.194   -1.415  1.00 23.58 ? 174 TYR A OH    1 
ATOM   1137 N N     . HIS A 1 152 ? 25.981  7.771   -0.505  1.00 22.38 ? 175 HIS A N     1 
ATOM   1138 C CA    . HIS A 1 152 ? 26.424  6.799   -1.502  1.00 27.38 ? 175 HIS A CA    1 
ATOM   1139 C C     . HIS A 1 152 ? 25.736  5.467   -1.238  1.00 24.17 ? 175 HIS A C     1 
ATOM   1140 O O     . HIS A 1 152 ? 25.717  5.005   -0.097  1.00 23.05 ? 175 HIS A O     1 
ATOM   1141 C CB    . HIS A 1 152 ? 27.951  6.592   -1.462  1.00 32.74 ? 175 HIS A CB    1 
ATOM   1142 C CG    . HIS A 1 152 ? 28.739  7.812   -1.823  1.00 38.87 ? 175 HIS A CG    1 
ATOM   1143 N ND1   . HIS A 1 152 ? 28.549  8.501   -3.005  1.00 48.84 ? 175 HIS A ND1   1 
ATOM   1144 C CD2   . HIS A 1 152 ? 29.711  8.480   -1.151  1.00 43.72 ? 175 HIS A CD2   1 
ATOM   1145 C CE1   . HIS A 1 152 ? 29.374  9.534   -3.050  1.00 44.96 ? 175 HIS A CE1   1 
ATOM   1146 N NE2   . HIS A 1 152 ? 30.093  9.541   -1.940  1.00 48.08 ? 175 HIS A NE2   1 
ATOM   1147 N N     . ILE A 1 153 ? 25.223  4.835   -2.295  1.00 25.36 ? 176 ILE A N     1 
ATOM   1148 C CA    . ILE A 1 153 ? 24.521  3.554   -2.206  1.00 29.00 ? 176 ILE A CA    1 
ATOM   1149 C C     . ILE A 1 153 ? 25.471  2.437   -2.606  1.00 28.59 ? 176 ILE A C     1 
ATOM   1150 O O     . ILE A 1 153 ? 26.067  2.498   -3.683  1.00 28.29 ? 176 ILE A O     1 
ATOM   1151 C CB    . ILE A 1 153 ? 23.287  3.529   -3.127  1.00 27.33 ? 176 ILE A CB    1 
ATOM   1152 C CG1   . ILE A 1 153 ? 22.304  4.650   -2.777  1.00 25.43 ? 176 ILE A CG1   1 
ATOM   1153 C CG2   . ILE A 1 153 ? 22.607  2.146   -3.079  1.00 20.49 ? 176 ILE A CG2   1 
ATOM   1154 C CD1   . ILE A 1 153 ? 21.069  4.646   -3.671  1.00 22.22 ? 176 ILE A CD1   1 
ATOM   1155 N N     . ARG A 1 154 ? 25.574  1.393   -1.782  1.00 25.17 ? 177 ARG A N     1 
ATOM   1156 C CA    . ARG A 1 154 ? 26.301  0.188   -2.172  1.00 28.48 ? 177 ARG A CA    1 
ATOM   1157 C C     . ARG A 1 154 ? 25.422  -1.041  -1.992  1.00 30.44 ? 177 ARG A C     1 
ATOM   1158 O O     . ARG A 1 154 ? 24.752  -1.186  -0.961  1.00 25.14 ? 177 ARG A O     1 
ATOM   1159 C CB    . ARG A 1 154 ? 27.598  0.008   -1.371  1.00 31.22 ? 177 ARG A CB    1 
ATOM   1160 C CG    . ARG A 1 154 ? 28.548  1.195   -1.450  1.00 36.82 ? 177 ARG A CG    1 
ATOM   1161 C CD    . ARG A 1 154 ? 29.781  0.898   -2.292  1.00 53.91 ? 177 ARG A CD    1 
ATOM   1162 N NE    . ARG A 1 154 ? 29.545  1.006   -3.740  1.00 58.72 ? 177 ARG A NE    1 
ATOM   1163 C CZ    . ARG A 1 154 ? 29.203  2.122   -4.395  1.00 59.81 ? 177 ARG A CZ    1 
ATOM   1164 N NH1   . ARG A 1 154 ? 29.015  2.076   -5.711  1.00 63.63 ? 177 ARG A NH1   1 
ATOM   1165 N NH2   . ARG A 1 154 ? 29.051  3.288   -3.755  1.00 53.93 ? 177 ARG A NH2   1 
ATOM   1166 N N     . HIS A 1 155 ? 25.425  -1.925  -2.992  1.00 26.10 ? 178 HIS A N     1 
ATOM   1167 C CA    . HIS A 1 155 ? 24.826  -3.243  -2.808  1.00 25.24 ? 178 HIS A CA    1 
ATOM   1168 C C     . HIS A 1 155 ? 25.695  -4.057  -1.855  1.00 27.72 ? 178 HIS A C     1 
ATOM   1169 O O     . HIS A 1 155 ? 26.908  -4.162  -2.047  1.00 27.41 ? 178 HIS A O     1 
ATOM   1170 C CB    . HIS A 1 155 ? 24.667  -3.979  -4.143  1.00 26.94 ? 178 HIS A CB    1 
ATOM   1171 C CG    . HIS A 1 155 ? 23.967  -5.300  -4.010  1.00 28.37 ? 178 HIS A CG    1 
ATOM   1172 N ND1   . HIS A 1 155 ? 24.637  -6.478  -3.758  1.00 31.39 ? 178 HIS A ND1   1 
ATOM   1173 C CD2   . HIS A 1 155 ? 22.648  -5.613  -4.018  1.00 31.22 ? 178 HIS A CD2   1 
ATOM   1174 C CE1   . HIS A 1 155 ? 23.764  -7.465  -3.652  1.00 31.49 ? 178 HIS A CE1   1 
ATOM   1175 N NE2   . HIS A 1 155 ? 22.549  -6.966  -3.804  1.00 30.98 ? 178 HIS A NE2   1 
ATOM   1176 N N     . PHE A 1 156 ? 25.074  -4.627  -0.823  1.00 22.61 ? 179 PHE A N     1 
ATOM   1177 C CA    . PHE A 1 156 ? 25.786  -5.291  0.261   1.00 24.11 ? 179 PHE A CA    1 
ATOM   1178 C C     . PHE A 1 156 ? 25.731  -6.813  0.161   1.00 27.52 ? 179 PHE A C     1 
ATOM   1179 O O     . PHE A 1 156 ? 26.765  -7.471  0.293   1.00 28.39 ? 179 PHE A O     1 
ATOM   1180 C CB    . PHE A 1 156 ? 25.216  -4.843  1.616   1.00 22.46 ? 179 PHE A CB    1 
ATOM   1181 C CG    . PHE A 1 156 ? 25.984  -5.364  2.799   1.00 26.13 ? 179 PHE A CG    1 
ATOM   1182 C CD1   . PHE A 1 156 ? 27.340  -5.096  2.941   1.00 28.46 ? 179 PHE A CD1   1 
ATOM   1183 C CD2   . PHE A 1 156 ? 25.353  -6.109  3.775   1.00 26.61 ? 179 PHE A CD2   1 
ATOM   1184 C CE1   . PHE A 1 156 ? 28.055  -5.570  4.040   1.00 29.32 ? 179 PHE A CE1   1 
ATOM   1185 C CE2   . PHE A 1 156 ? 26.064  -6.592  4.873   1.00 30.31 ? 179 PHE A CE2   1 
ATOM   1186 C CZ    . PHE A 1 156 ? 27.414  -6.318  5.005   1.00 32.48 ? 179 PHE A CZ    1 
ATOM   1187 N N     . ASP A 1 157 ? 24.549  -7.393  -0.055  1.00 22.87 ? 180 ASP A N     1 
ATOM   1188 C CA    . ASP A 1 157 ? 24.470  -8.844  -0.197  1.00 27.16 ? 180 ASP A CA    1 
ATOM   1189 C C     . ASP A 1 157 ? 23.106  -9.254  -0.744  1.00 27.92 ? 180 ASP A C     1 
ATOM   1190 O O     . ASP A 1 157 ? 22.176  -8.444  -0.847  1.00 24.33 ? 180 ASP A O     1 
ATOM   1191 C CB    . ASP A 1 157 ? 24.736  -9.551  1.133   1.00 31.13 ? 180 ASP A CB    1 
ATOM   1192 C CG    . ASP A 1 157 ? 25.236  -10.969 0.943   1.00 36.22 ? 180 ASP A CG    1 
ATOM   1193 O OD1   . ASP A 1 157 ? 25.448  -11.371 -0.218  1.00 33.30 ? 180 ASP A OD1   1 
ATOM   1194 O OD2   . ASP A 1 157 ? 25.397  -11.683 1.948   1.00 39.85 ? 180 ASP A OD2   1 
ATOM   1195 N N     . PHE A 1 158 ? 23.012  -10.540 -1.104  1.00 26.49 ? 181 PHE A N     1 
ATOM   1196 C CA    . PHE A 1 158 ? 21.800  -11.169 -1.625  1.00 29.29 ? 181 PHE A CA    1 
ATOM   1197 C C     . PHE A 1 158 ? 21.654  -12.541 -0.975  1.00 30.56 ? 181 PHE A C     1 
ATOM   1198 O O     . PHE A 1 158 ? 22.603  -13.330 -0.983  1.00 30.37 ? 181 PHE A O     1 
ATOM   1199 C CB    . PHE A 1 158 ? 21.853  -11.297 -3.161  1.00 28.59 ? 181 PHE A CB    1 
ATOM   1200 C CG    . PHE A 1 158 ? 20.617  -11.946 -3.759  1.00 31.00 ? 181 PHE A CG    1 
ATOM   1201 C CD1   . PHE A 1 158 ? 19.434  -11.225 -3.901  1.00 29.84 ? 181 PHE A CD1   1 
ATOM   1202 C CD2   . PHE A 1 158 ? 20.634  -13.274 -4.153  1.00 28.70 ? 181 PHE A CD2   1 
ATOM   1203 C CE1   . PHE A 1 158 ? 18.284  -11.813 -4.432  1.00 29.18 ? 181 PHE A CE1   1 
ATOM   1204 C CE2   . PHE A 1 158 ? 19.494  -13.875 -4.687  1.00 29.98 ? 181 PHE A CE2   1 
ATOM   1205 C CZ    . PHE A 1 158 ? 18.316  -13.139 -4.826  1.00 30.39 ? 181 PHE A CZ    1 
ATOM   1206 N N     . ILE A 1 159 ? 20.481  -12.826 -0.403  1.00 27.00 ? 182 ILE A N     1 
ATOM   1207 C CA    . ILE A 1 159 ? 20.253  -14.049 0.370   1.00 29.17 ? 182 ILE A CA    1 
ATOM   1208 C C     . ILE A 1 159 ? 19.050  -14.764 -0.234  1.00 29.59 ? 182 ILE A C     1 
ATOM   1209 O O     . ILE A 1 159 ? 17.893  -14.423 0.045   1.00 25.80 ? 182 ILE A O     1 
ATOM   1210 C CB    . ILE A 1 159 ? 20.042  -13.773 1.861   1.00 28.57 ? 182 ILE A CB    1 
ATOM   1211 C CG1   . ILE A 1 159 ? 21.242  -13.015 2.432   1.00 28.86 ? 182 ILE A CG1   1 
ATOM   1212 C CG2   . ILE A 1 159 ? 19.868  -15.079 2.607   1.00 30.78 ? 182 ILE A CG2   1 
ATOM   1213 C CD1   . ILE A 1 159 ? 21.016  -11.546 2.551   1.00 29.93 ? 182 ILE A CD1   1 
ATOM   1214 N N     . VAL A 1 160 ? 19.325  -15.791 -1.041  1.00 26.86 ? 183 VAL A N     1 
ATOM   1215 C CA    . VAL A 1 160 ? 18.271  -16.441 -1.800  1.00 29.94 ? 183 VAL A CA    1 
ATOM   1216 C C     . VAL A 1 160 ? 17.389  -17.316 -0.916  1.00 27.36 ? 183 VAL A C     1 
ATOM   1217 O O     . VAL A 1 160 ? 16.235  -17.573 -1.274  1.00 28.69 ? 183 VAL A O     1 
ATOM   1218 C CB    . VAL A 1 160 ? 18.909  -17.225 -2.967  1.00 27.25 ? 183 VAL A CB    1 
ATOM   1219 C CG1   . VAL A 1 160 ? 19.601  -18.487 -2.464  1.00 27.69 ? 183 VAL A CG1   1 
ATOM   1220 C CG2   . VAL A 1 160 ? 17.879  -17.518 -4.045  1.00 29.97 ? 183 VAL A CG2   1 
ATOM   1221 N N     . ARG A 1 161 ? 17.879  -17.743 0.250   1.00 28.09 ? 184 ARG A N     1 
ATOM   1222 C CA    . ARG A 1 161 ? 17.083  -18.586 1.141   1.00 33.99 ? 184 ARG A CA    1 
ATOM   1223 C C     . ARG A 1 161 ? 16.124  -17.794 2.028   1.00 33.92 ? 184 ARG A C     1 
ATOM   1224 O O     . ARG A 1 161 ? 15.304  -18.403 2.721   1.00 32.25 ? 184 ARG A O     1 
ATOM   1225 C CB    . ARG A 1 161 ? 17.992  -19.456 2.022   1.00 41.61 ? 184 ARG A CB    1 
ATOM   1226 C CG    . ARG A 1 161 ? 17.854  -20.969 1.757   1.00 52.15 ? 184 ARG A CG    1 
ATOM   1227 C CD    . ARG A 1 161 ? 18.939  -21.814 2.461   1.00 54.91 ? 184 ARG A CD    1 
ATOM   1228 N NE    . ARG A 1 161 ? 18.733  -21.888 3.911   1.00 65.86 ? 184 ARG A NE    1 
ATOM   1229 C CZ    . ARG A 1 161 ? 19.089  -22.918 4.682   1.00 64.84 ? 184 ARG A CZ    1 
ATOM   1230 N NH1   . ARG A 1 161 ? 18.854  -22.887 5.992   1.00 62.53 ? 184 ARG A NH1   1 
ATOM   1231 N NH2   . ARG A 1 161 ? 19.678  -23.983 4.151   1.00 62.61 ? 184 ARG A NH2   1 
ATOM   1232 N N     . ASN A 1 162 ? 16.202  -16.468 2.029   1.00 30.19 ? 185 ASN A N     1 
ATOM   1233 C CA    . ASN A 1 162 ? 15.162  -15.656 2.647   1.00 26.12 ? 185 ASN A CA    1 
ATOM   1234 C C     . ASN A 1 162 ? 13.846  -15.820 1.889   1.00 27.16 ? 185 ASN A C     1 
ATOM   1235 O O     . ASN A 1 162 ? 13.835  -16.060 0.679   1.00 28.12 ? 185 ASN A O     1 
ATOM   1236 C CB    . ASN A 1 162 ? 15.576  -14.180 2.648   1.00 25.38 ? 185 ASN A CB    1 
ATOM   1237 C CG    . ASN A 1 162 ? 14.948  -13.407 3.781   1.00 27.82 ? 185 ASN A CG    1 
ATOM   1238 O OD1   . ASN A 1 162 ? 15.457  -13.417 4.899   1.00 26.12 ? 185 ASN A OD1   1 
ATOM   1239 N ND2   . ASN A 1 162 ? 13.833  -12.731 3.500   1.00 27.20 ? 185 ASN A ND2   1 
ATOM   1240 N N     . ILE A 1 163 ? 12.734  -15.675 2.603   1.00 24.73 ? 186 ILE A N     1 
ATOM   1241 C CA    . ILE A 1 163 ? 11.399  -15.758 2.020   1.00 26.80 ? 186 ILE A CA    1 
ATOM   1242 C C     . ILE A 1 163 ? 10.755  -14.374 2.124   1.00 26.63 ? 186 ILE A C     1 
ATOM   1243 O O     . ILE A 1 163 ? 10.362  -13.961 3.222   1.00 30.86 ? 186 ILE A O     1 
ATOM   1244 C CB    . ILE A 1 163 ? 10.533  -16.821 2.712   1.00 30.10 ? 186 ILE A CB    1 
ATOM   1245 C CG1   . ILE A 1 163 ? 11.217  -18.194 2.653   1.00 29.06 ? 186 ILE A CG1   1 
ATOM   1246 C CG2   . ILE A 1 163 ? 9.130   -16.864 2.077   1.00 29.36 ? 186 ILE A CG2   1 
ATOM   1247 C CD1   . ILE A 1 163 ? 10.760  -19.180 3.734   1.00 32.70 ? 186 ILE A CD1   1 
ATOM   1248 N N     . PRO A 1 164 ? 10.643  -13.615 1.021   1.00 32.84 ? 187 PRO A N     1 
ATOM   1249 C CA    . PRO A 1 164 ? 11.222  -13.911 -0.297  1.00 24.77 ? 187 PRO A CA    1 
ATOM   1250 C C     . PRO A 1 164 ? 12.701  -13.528 -0.295  1.00 26.18 ? 187 PRO A C     1 
ATOM   1251 O O     . PRO A 1 164 ? 13.149  -12.966 0.715   1.00 24.44 ? 187 PRO A O     1 
ATOM   1252 C CB    . PRO A 1 164 ? 10.400  -13.027 -1.233  1.00 30.52 ? 187 PRO A CB    1 
ATOM   1253 C CG    . PRO A 1 164 ? 10.068  -11.852 -0.416  1.00 31.07 ? 187 PRO A CG    1 
ATOM   1254 C CD    . PRO A 1 164 ? 9.923   -12.332 1.018   1.00 31.71 ? 187 PRO A CD    1 
ATOM   1255 N N     . PRO A 1 165 ? 13.440  -13.825 -1.373  1.00 27.76 ? 188 PRO A N     1 
ATOM   1256 C CA    . PRO A 1 165 ? 14.881  -13.542 -1.372  1.00 22.09 ? 188 PRO A CA    1 
ATOM   1257 C C     . PRO A 1 165 ? 15.162  -12.074 -1.061  1.00 23.99 ? 188 PRO A C     1 
ATOM   1258 O O     . PRO A 1 165 ? 14.452  -11.175 -1.514  1.00 23.78 ? 188 PRO A O     1 
ATOM   1259 C CB    . PRO A 1 165 ? 15.311  -13.915 -2.791  1.00 23.97 ? 188 PRO A CB    1 
ATOM   1260 C CG    . PRO A 1 165 ? 14.357  -14.975 -3.190  1.00 29.31 ? 188 PRO A CG    1 
ATOM   1261 C CD    . PRO A 1 165 ? 13.041  -14.619 -2.550  1.00 29.34 ? 188 PRO A CD    1 
ATOM   1262 N N     . ALA A 1 166 ? 16.203  -11.843 -0.275  1.00 25.54 ? 189 ALA A N     1 
ATOM   1263 C CA    . ALA A 1 166 ? 16.443  -10.553 0.355   1.00 25.13 ? 189 ALA A CA    1 
ATOM   1264 C C     . ALA A 1 166 ? 17.651  -9.862  -0.265  1.00 25.66 ? 189 ALA A C     1 
ATOM   1265 O O     . ALA A 1 166 ? 18.705  -10.482 -0.445  1.00 24.72 ? 189 ALA A O     1 
ATOM   1266 C CB    . ALA A 1 166 ? 16.657  -10.732 1.857   1.00 23.19 ? 189 ALA A CB    1 
ATOM   1267 N N     . GLN A 1 167 ? 17.490  -8.581  -0.583  1.00 24.05 ? 190 GLN A N     1 
ATOM   1268 C CA    . GLN A 1 167 ? 18.591  -7.700  -0.949  1.00 25.38 ? 190 GLN A CA    1 
ATOM   1269 C C     . GLN A 1 167 ? 18.962  -6.833  0.247   1.00 25.33 ? 190 GLN A C     1 
ATOM   1270 O O     . GLN A 1 167 ? 18.085  -6.271  0.909   1.00 25.03 ? 190 GLN A O     1 
ATOM   1271 C CB    . GLN A 1 167 ? 18.212  -6.797  -2.123  1.00 28.64 ? 190 GLN A CB    1 
ATOM   1272 C CG    . GLN A 1 167 ? 17.778  -7.523  -3.380  1.00 29.83 ? 190 GLN A CG    1 
ATOM   1273 C CD    . GLN A 1 167 ? 18.896  -7.568  -4.389  1.00 32.16 ? 190 GLN A CD    1 
ATOM   1274 O OE1   . GLN A 1 167 ? 20.039  -7.855  -4.042  1.00 28.61 ? 190 GLN A OE1   1 
ATOM   1275 N NE2   . GLN A 1 167 ? 18.578  -7.278  -5.641  1.00 35.40 ? 190 GLN A NE2   1 
ATOM   1276 N N     . LEU A 1 168 ? 20.253  -6.698  0.507   1.00 26.37 ? 191 LEU A N     1 
ATOM   1277 C CA    . LEU A 1 168 ? 20.732  -5.792  1.535   1.00 22.81 ? 191 LEU A CA    1 
ATOM   1278 C C     . LEU A 1 168 ? 21.501  -4.667  0.859   1.00 24.72 ? 191 LEU A C     1 
ATOM   1279 O O     . LEU A 1 168 ? 22.340  -4.916  -0.018  1.00 23.46 ? 191 LEU A O     1 
ATOM   1280 C CB    . LEU A 1 168 ? 21.604  -6.520  2.558   1.00 21.19 ? 191 LEU A CB    1 
ATOM   1281 C CG    . LEU A 1 168 ? 20.991  -7.737  3.256   1.00 26.96 ? 191 LEU A CG    1 
ATOM   1282 C CD1   . LEU A 1 168 ? 21.956  -8.263  4.331   1.00 19.89 ? 191 LEU A CD1   1 
ATOM   1283 C CD2   . LEU A 1 168 ? 19.611  -7.420  3.861   1.00 21.06 ? 191 LEU A CD2   1 
ATOM   1284 N N     . TRP A 1 169 ? 21.209  -3.438  1.262   1.00 20.99 ? 192 TRP A N     1 
ATOM   1285 C CA    . TRP A 1 169 ? 21.874  -2.253  0.740   1.00 20.94 ? 192 TRP A CA    1 
ATOM   1286 C C     . TRP A 1 169 ? 22.482  -1.465  1.892   1.00 20.49 ? 192 TRP A C     1 
ATOM   1287 O O     . TRP A 1 169 ? 21.926  -1.429  2.987   1.00 19.34 ? 192 TRP A O     1 
ATOM   1288 C CB    . TRP A 1 169 ? 20.893  -1.371  -0.019  1.00 20.84 ? 192 TRP A CB    1 
ATOM   1289 C CG    . TRP A 1 169 ? 20.182  -2.065  -1.150  1.00 23.12 ? 192 TRP A CG    1 
ATOM   1290 C CD1   . TRP A 1 169 ? 19.015  -2.773  -1.082  1.00 23.78 ? 192 TRP A CD1   1 
ATOM   1291 C CD2   . TRP A 1 169 ? 20.584  -2.084  -2.525  1.00 22.38 ? 192 TRP A CD2   1 
ATOM   1292 N NE1   . TRP A 1 169 ? 18.672  -3.242  -2.333  1.00 24.01 ? 192 TRP A NE1   1 
ATOM   1293 C CE2   . TRP A 1 169 ? 19.619  -2.830  -3.234  1.00 26.85 ? 192 TRP A CE2   1 
ATOM   1294 C CE3   . TRP A 1 169 ? 21.676  -1.549  -3.223  1.00 25.21 ? 192 TRP A CE3   1 
ATOM   1295 C CZ2   . TRP A 1 169 ? 19.711  -3.057  -4.611  1.00 28.15 ? 192 TRP A CZ2   1 
ATOM   1296 C CZ3   . TRP A 1 169 ? 21.759  -1.762  -4.596  1.00 27.83 ? 192 TRP A CZ3   1 
ATOM   1297 C CH2   . TRP A 1 169 ? 20.782  -2.515  -5.271  1.00 30.14 ? 192 TRP A CH2   1 
ATOM   1298 N N     . THR A 1 170 ? 23.633  -0.839  1.659   1.00 21.60 ? 193 THR A N     1 
ATOM   1299 C CA    . THR A 1 170 ? 24.225  0.045   2.660   1.00 22.60 ? 193 THR A CA    1 
ATOM   1300 C C     . THR A 1 170 ? 24.316  1.467   2.120   1.00 20.62 ? 193 THR A C     1 
ATOM   1301 O O     . THR A 1 170 ? 24.480  1.691   0.915   1.00 22.86 ? 193 THR A O     1 
ATOM   1302 C CB    . THR A 1 170 ? 25.612  -0.421  3.099   1.00 23.18 ? 193 THR A CB    1 
ATOM   1303 O OG1   . THR A 1 170 ? 26.462  -0.488  1.953   1.00 26.89 ? 193 THR A OG1   1 
ATOM   1304 C CG2   . THR A 1 170 ? 25.540  -1.810  3.770   1.00 23.09 ? 193 THR A CG2   1 
ATOM   1305 N N     . TYR A 1 171 ? 24.210  2.429   3.028   1.00 19.92 ? 194 TYR A N     1 
ATOM   1306 C CA    . TYR A 1 171 ? 24.231  3.844   2.685   1.00 21.92 ? 194 TYR A CA    1 
ATOM   1307 C C     . TYR A 1 171 ? 25.172  4.559   3.636   1.00 24.12 ? 194 TYR A C     1 
ATOM   1308 O O     . TYR A 1 171 ? 25.088  4.362   4.856   1.00 22.56 ? 194 TYR A O     1 
ATOM   1309 C CB    . TYR A 1 171 ? 22.834  4.468   2.779   1.00 20.24 ? 194 TYR A CB    1 
ATOM   1310 C CG    . TYR A 1 171 ? 21.763  3.704   2.018   1.00 22.24 ? 194 TYR A CG    1 
ATOM   1311 C CD1   . TYR A 1 171 ? 21.453  4.019   0.688   1.00 23.27 ? 194 TYR A CD1   1 
ATOM   1312 C CD2   . TYR A 1 171 ? 21.057  2.685   2.628   1.00 20.82 ? 194 TYR A CD2   1 
ATOM   1313 C CE1   . TYR A 1 171 ? 20.466  3.310   -0.010  1.00 24.30 ? 194 TYR A CE1   1 
ATOM   1314 C CE2   . TYR A 1 171 ? 20.069  1.975   1.937   1.00 24.37 ? 194 TYR A CE2   1 
ATOM   1315 C CZ    . TYR A 1 171 ? 19.783  2.288   0.625   1.00 24.17 ? 194 TYR A CZ    1 
ATOM   1316 O OH    . TYR A 1 171 ? 18.802  1.574   -0.037  1.00 24.56 ? 194 TYR A OH    1 
ATOM   1317 N N     . THR A 1 172 ? 26.046  5.398   3.079   1.00 20.47 ? 195 THR A N     1 
ATOM   1318 C CA    . THR A 1 172 ? 26.989  6.196   3.849   1.00 20.15 ? 195 THR A CA    1 
ATOM   1319 C C     . THR A 1 172 ? 26.924  7.643   3.373   1.00 25.50 ? 195 THR A C     1 
ATOM   1320 O O     . THR A 1 172 ? 26.526  7.927   2.236   1.00 22.08 ? 195 THR A O     1 
ATOM   1321 C CB    . THR A 1 172 ? 28.436  5.651   3.723   1.00 21.91 ? 195 THR A CB    1 
ATOM   1322 O OG1   . THR A 1 172 ? 28.848  5.666   2.348   1.00 23.62 ? 195 THR A OG1   1 
ATOM   1323 C CG2   . THR A 1 172 ? 28.536  4.196   4.259   1.00 20.42 ? 195 THR A CG2   1 
ATOM   1324 N N     . ARG A 1 173 ? 27.351  8.563   4.241   1.00 20.69 ? 196 ARG A N     1 
ATOM   1325 C CA    . ARG A 1 173 ? 27.291  9.980   3.893   1.00 26.25 ? 196 ARG A CA    1 
ATOM   1326 C C     . ARG A 1 173 ? 28.215  10.306  2.720   1.00 30.88 ? 196 ARG A C     1 
ATOM   1327 O O     . ARG A 1 173 ? 29.341  9.810   2.635   1.00 29.36 ? 196 ARG A O     1 
ATOM   1328 C CB    . ARG A 1 173 ? 27.652  10.843  5.108   1.00 25.72 ? 196 ARG A CB    1 
ATOM   1329 C CG    . ARG A 1 173 ? 27.643  12.338  4.813   1.00 30.69 ? 196 ARG A CG    1 
ATOM   1330 C CD    . ARG A 1 173 ? 26.255  12.811  4.385   1.00 28.38 ? 196 ARG A CD    1 
ATOM   1331 N NE    . ARG A 1 173 ? 25.389  12.999  5.541   1.00 24.52 ? 196 ARG A NE    1 
ATOM   1332 C CZ    . ARG A 1 173 ? 24.064  13.107  5.481   1.00 27.61 ? 196 ARG A CZ    1 
ATOM   1333 N NH1   . ARG A 1 173 ? 23.428  13.022  4.312   1.00 23.86 ? 196 ARG A NH1   1 
ATOM   1334 N NH2   . ARG A 1 173 ? 23.380  13.304  6.594   1.00 22.44 ? 196 ARG A NH2   1 
ATOM   1335 N N     . ALA A 1 174 ? 27.729  11.148  1.806   1.00 31.43 ? 197 ALA A N     1 
ATOM   1336 C CA    . ALA A 1 174 ? 28.540  11.598  0.669   1.00 36.01 ? 197 ALA A CA    1 
ATOM   1337 C C     . ALA A 1 174 ? 29.415  12.810  1.022   1.00 44.66 ? 197 ALA A C     1 
ATOM   1338 O O     . ALA A 1 174 ? 28.997  13.715  1.756   1.00 41.48 ? 197 ALA A O     1 
ATOM   1339 C CB    . ALA A 1 174 ? 27.654  11.934  -0.516  1.00 34.71 ? 197 ALA A CB    1 
ATOM   1340 O OXT   . ALA A 1 174 ? 30.564  12.911  0.573   1.00 48.44 ? 197 ALA A OXT   1 
ATOM   1341 N N     . VAL B 1 11  ? -13.208 -10.025 18.892  1.00 52.58 ? 34  VAL B N     1 
ATOM   1342 C CA    . VAL B 1 11  ? -14.658 -10.200 18.774  1.00 47.67 ? 34  VAL B CA    1 
ATOM   1343 C C     . VAL B 1 11  ? -15.141 -9.653  17.424  1.00 43.78 ? 34  VAL B C     1 
ATOM   1344 O O     . VAL B 1 11  ? -14.754 -8.552  17.016  1.00 44.56 ? 34  VAL B O     1 
ATOM   1345 C CB    . VAL B 1 11  ? -15.382 -9.536  19.955  1.00 48.37 ? 34  VAL B CB    1 
ATOM   1346 C CG1   . VAL B 1 11  ? -16.874 -9.326  19.663  1.00 42.86 ? 34  VAL B CG1   1 
ATOM   1347 C CG2   . VAL B 1 11  ? -15.190 -10.371 21.203  1.00 49.32 ? 34  VAL B CG2   1 
ATOM   1348 N N     . PRO B 1 12  ? -15.961 -10.431 16.722  1.00 42.04 ? 35  PRO B N     1 
ATOM   1349 C CA    . PRO B 1 12  ? -16.294 -10.082 15.336  1.00 38.24 ? 35  PRO B CA    1 
ATOM   1350 C C     . PRO B 1 12  ? -17.192 -8.859  15.240  1.00 36.99 ? 35  PRO B C     1 
ATOM   1351 O O     . PRO B 1 12  ? -18.053 -8.610  16.090  1.00 34.44 ? 35  PRO B O     1 
ATOM   1352 C CB    . PRO B 1 12  ? -17.012 -11.335 14.814  1.00 38.54 ? 35  PRO B CB    1 
ATOM   1353 C CG    . PRO B 1 12  ? -16.697 -12.414 15.795  1.00 43.67 ? 35  PRO B CG    1 
ATOM   1354 C CD    . PRO B 1 12  ? -16.532 -11.731 17.108  1.00 45.67 ? 35  PRO B CD    1 
ATOM   1355 N N     . THR B 1 13  ? -16.976 -8.096  14.172  1.00 32.62 ? 36  THR B N     1 
ATOM   1356 C CA    . THR B 1 13  ? -17.837 -6.974  13.841  1.00 29.27 ? 36  THR B CA    1 
ATOM   1357 C C     . THR B 1 13  ? -19.294 -7.421  13.756  1.00 30.48 ? 36  THR B C     1 
ATOM   1358 O O     . THR B 1 13  ? -19.597 -8.529  13.314  1.00 27.44 ? 36  THR B O     1 
ATOM   1359 C CB    . THR B 1 13  ? -17.359 -6.368  12.522  1.00 30.76 ? 36  THR B CB    1 
ATOM   1360 O OG1   . THR B 1 13  ? -16.022 -5.885  12.695  1.00 30.46 ? 36  THR B OG1   1 
ATOM   1361 C CG2   . THR B 1 13  ? -18.237 -5.219  12.094  1.00 28.79 ? 36  THR B CG2   1 
ATOM   1362 N N     . SER B 1 14  ? -20.201 -6.565  14.210  1.00 31.92 ? 37  SER B N     1 
ATOM   1363 C CA    . SER B 1 14  ? -21.589 -6.985  14.290  1.00 28.57 ? 37  SER B CA    1 
ATOM   1364 C C     . SER B 1 14  ? -22.226 -7.000  12.899  1.00 28.20 ? 37  SER B C     1 
ATOM   1365 O O     . SER B 1 14  ? -21.749 -6.358  11.967  1.00 26.91 ? 37  SER B O     1 
ATOM   1366 C CB    . SER B 1 14  ? -22.366 -6.076  15.244  1.00 28.67 ? 37  SER B CB    1 
ATOM   1367 O OG    . SER B 1 14  ? -23.084 -5.085  14.545  1.00 32.98 ? 37  SER B OG    1 
ATOM   1368 N N     . SER B 1 15  ? -23.314 -7.767  12.759  1.00 25.93 ? 38  SER B N     1 
ATOM   1369 C CA    . SER B 1 15  ? -23.961 -7.860  11.453  1.00 28.63 ? 38  SER B CA    1 
ATOM   1370 C C     . SER B 1 15  ? -24.568 -6.524  11.022  1.00 30.90 ? 38  SER B C     1 
ATOM   1371 O O     . SER B 1 15  ? -24.666 -6.246  9.817   1.00 28.81 ? 38  SER B O     1 
ATOM   1372 C CB    . SER B 1 15  ? -25.009 -8.974  11.461  1.00 29.51 ? 38  SER B CB    1 
ATOM   1373 O OG    . SER B 1 15  ? -26.146 -8.603  12.201  1.00 38.65 ? 38  SER B OG    1 
ATOM   1374 N N     . ILE B 1 16  ? -24.943 -5.676  11.983  1.00 28.46 ? 39  ILE B N     1 
ATOM   1375 C CA    . ILE B 1 16  ? -25.455 -4.342  11.662  1.00 29.77 ? 39  ILE B CA    1 
ATOM   1376 C C     . ILE B 1 16  ? -24.375 -3.499  10.992  1.00 24.27 ? 39  ILE B C     1 
ATOM   1377 O O     . ILE B 1 16  ? -24.615 -2.843  9.969   1.00 25.92 ? 39  ILE B O     1 
ATOM   1378 C CB    . ILE B 1 16  ? -25.979 -3.654  12.935  1.00 30.47 ? 39  ILE B CB    1 
ATOM   1379 C CG1   . ILE B 1 16  ? -27.239 -4.357  13.448  1.00 35.22 ? 39  ILE B CG1   1 
ATOM   1380 C CG2   . ILE B 1 16  ? -26.255 -2.164  12.675  1.00 29.92 ? 39  ILE B CG2   1 
ATOM   1381 C CD1   . ILE B 1 16  ? -27.568 -4.029  14.916  1.00 34.14 ? 39  ILE B CD1   1 
ATOM   1382 N N     . THR B 1 17  ? -23.174 -3.485  11.580  1.00 23.53 ? 40  THR B N     1 
ATOM   1383 C CA    . THR B 1 17  ? -22.070 -2.723  11.016  1.00 21.49 ? 40  THR B CA    1 
ATOM   1384 C C     . THR B 1 17  ? -21.703 -3.237  9.637   1.00 23.47 ? 40  THR B C     1 
ATOM   1385 O O     . THR B 1 17  ? -21.510 -2.447  8.701   1.00 23.73 ? 40  THR B O     1 
ATOM   1386 C CB    . THR B 1 17  ? -20.868 -2.798  11.953  1.00 26.54 ? 40  THR B CB    1 
ATOM   1387 O OG1   . THR B 1 17  ? -21.240 -2.291  13.244  1.00 25.39 ? 40  THR B OG1   1 
ATOM   1388 C CG2   . THR B 1 17  ? -19.680 -2.012  11.393  1.00 20.94 ? 40  THR B CG2   1 
ATOM   1389 N N     . ALA B 1 18  ? -21.621 -4.564  9.492   1.00 21.44 ? 41  ALA B N     1 
ATOM   1390 C CA    . ALA B 1 18  ? -21.260 -5.164  8.214   1.00 22.05 ? 41  ALA B CA    1 
ATOM   1391 C C     . ALA B 1 18  ? -22.243 -4.772  7.120   1.00 25.84 ? 41  ALA B C     1 
ATOM   1392 O O     . ALA B 1 18  ? -21.840 -4.439  6.000   1.00 24.88 ? 41  ALA B O     1 
ATOM   1393 C CB    . ALA B 1 18  ? -21.194 -6.681  8.365   1.00 22.44 ? 41  ALA B CB    1 
ATOM   1394 N N     . LYS B 1 19  ? -23.540 -4.819  7.422   1.00 25.60 ? 42  LYS B N     1 
ATOM   1395 C CA    . LYS B 1 19  ? -24.543 -4.424  6.443   1.00 23.75 ? 42  LYS B CA    1 
ATOM   1396 C C     . LYS B 1 19  ? -24.356 -2.967  6.017   1.00 24.50 ? 42  LYS B C     1 
ATOM   1397 O O     . LYS B 1 19  ? -24.412 -2.642  4.825   1.00 23.53 ? 42  LYS B O     1 
ATOM   1398 C CB    . LYS B 1 19  ? -25.931 -4.653  7.033   1.00 24.68 ? 42  LYS B CB    1 
ATOM   1399 C CG    . LYS B 1 19  ? -27.088 -4.369  6.099   1.00 28.44 ? 42  LYS B CG    1 
ATOM   1400 C CD    . LYS B 1 19  ? -28.412 -4.749  6.780   1.00 36.69 ? 42  LYS B CD    1 
ATOM   1401 C CE    . LYS B 1 19  ? -29.627 -4.502  5.882   1.00 45.03 ? 42  LYS B CE    1 
ATOM   1402 N NZ    . LYS B 1 19  ? -29.525 -5.229  4.580   1.00 46.10 ? 42  LYS B NZ    1 
ATOM   1403 N N     . LYS B 1 20  ? -24.118 -2.074  6.977   1.00 23.29 ? 43  LYS B N     1 
ATOM   1404 C CA    . LYS B 1 20  ? -23.858 -0.683  6.623   1.00 23.02 ? 43  LYS B CA    1 
ATOM   1405 C C     . LYS B 1 20  ? -22.632 -0.551  5.709   1.00 27.98 ? 43  LYS B C     1 
ATOM   1406 O O     . LYS B 1 20  ? -22.673 0.166   4.693   1.00 22.59 ? 43  LYS B O     1 
ATOM   1407 C CB    . LYS B 1 20  ? -23.701 0.141   7.903   1.00 23.86 ? 43  LYS B CB    1 
ATOM   1408 C CG    . LYS B 1 20  ? -23.546 1.636   7.678   1.00 25.01 ? 43  LYS B CG    1 
ATOM   1409 C CD    . LYS B 1 20  ? -24.755 2.252   7.032   1.00 26.45 ? 43  LYS B CD    1 
ATOM   1410 C CE    . LYS B 1 20  ? -24.623 3.774   7.041   1.00 30.33 ? 43  LYS B CE    1 
ATOM   1411 N NZ    . LYS B 1 20  ? -25.663 4.417   6.203   1.00 29.67 ? 43  LYS B NZ    1 
ATOM   1412 N N     . MET B 1 21  ? -21.536 -1.251  6.029   1.00 23.27 ? 44  MET B N     1 
ATOM   1413 C CA    . MET B 1 21  ? -20.342 -1.140  5.194   1.00 25.32 ? 44  MET B CA    1 
ATOM   1414 C C     . MET B 1 21  ? -20.597 -1.642  3.773   1.00 25.11 ? 44  MET B C     1 
ATOM   1415 O O     . MET B 1 21  ? -20.138 -1.030  2.802   1.00 24.61 ? 44  MET B O     1 
ATOM   1416 C CB    . MET B 1 21  ? -19.175 -1.896  5.828   1.00 25.84 ? 44  MET B CB    1 
ATOM   1417 C CG    . MET B 1 21  ? -18.718 -1.334  7.155   1.00 21.49 ? 44  MET B CG    1 
ATOM   1418 S SD    . MET B 1 21  ? -17.394 -2.318  7.887   1.00 30.42 ? 44  MET B SD    1 
ATOM   1419 C CE    . MET B 1 21  ? -15.984 -1.704  6.930   1.00 21.29 ? 44  MET B CE    1 
ATOM   1420 N N     . ALA B 1 22  ? -21.332 -2.746  3.629   1.00 23.59 ? 45  ALA B N     1 
ATOM   1421 C CA    . ALA B 1 22  ? -21.617 -3.291  2.303   1.00 22.80 ? 45  ALA B CA    1 
ATOM   1422 C C     . ALA B 1 22  ? -22.668 -2.491  1.536   1.00 23.75 ? 45  ALA B C     1 
ATOM   1423 O O     . ALA B 1 22  ? -22.834 -2.711  0.325   1.00 22.52 ? 45  ALA B O     1 
ATOM   1424 C CB    . ALA B 1 22  ? -22.063 -4.759  2.416   1.00 23.01 ? 45  ALA B CB    1 
ATOM   1425 N N     . SER B 1 23  ? -23.352 -1.549  2.185   1.00 21.21 ? 46  SER B N     1 
ATOM   1426 C CA    . SER B 1 23  ? -24.420 -0.838  1.499   1.00 22.90 ? 46  SER B CA    1 
ATOM   1427 C C     . SER B 1 23  ? -23.914 0.101   0.414   1.00 24.57 ? 46  SER B C     1 
ATOM   1428 O O     . SER B 1 23  ? -24.718 0.532   -0.415  1.00 24.97 ? 46  SER B O     1 
ATOM   1429 C CB    . SER B 1 23  ? -25.272 -0.056  2.500   1.00 23.06 ? 46  SER B CB    1 
ATOM   1430 O OG    . SER B 1 23  ? -24.524 0.962   3.135   1.00 23.50 ? 46  SER B OG    1 
ATOM   1431 N N     . VAL B 1 24  ? -22.613 0.408   0.372   1.00 25.74 ? 47  VAL B N     1 
ATOM   1432 C CA    . VAL B 1 24  ? -22.103 1.327   -0.649  1.00 24.76 ? 47  VAL B CA    1 
ATOM   1433 C C     . VAL B 1 24  ? -21.919 0.665   -2.005  1.00 26.41 ? 47  VAL B C     1 
ATOM   1434 O O     . VAL B 1 24  ? -21.761 1.370   -3.015  1.00 26.24 ? 47  VAL B O     1 
ATOM   1435 C CB    . VAL B 1 24  ? -20.766 1.966   -0.215  1.00 26.41 ? 47  VAL B CB    1 
ATOM   1436 C CG1   . VAL B 1 24  ? -20.878 2.551   1.185   1.00 26.45 ? 47  VAL B CG1   1 
ATOM   1437 C CG2   . VAL B 1 24  ? -19.611 0.956   -0.303  1.00 25.31 ? 47  VAL B CG2   1 
ATOM   1438 N N     . ILE B 1 25  ? -21.967 -0.667  -2.061  1.00 20.20 ? 48  ILE B N     1 
ATOM   1439 C CA    . ILE B 1 25  ? -21.612 -1.394  -3.270  1.00 24.28 ? 48  ILE B CA    1 
ATOM   1440 C C     . ILE B 1 25  ? -22.711 -1.248  -4.312  1.00 24.59 ? 48  ILE B C     1 
ATOM   1441 O O     . ILE B 1 25  ? -23.901 -1.283  -3.981  1.00 21.81 ? 48  ILE B O     1 
ATOM   1442 C CB    . ILE B 1 25  ? -21.367 -2.873  -2.924  1.00 23.59 ? 48  ILE B CB    1 
ATOM   1443 C CG1   . ILE B 1 25  ? -20.147 -3.015  -2.009  1.00 24.08 ? 48  ILE B CG1   1 
ATOM   1444 C CG2   . ILE B 1 25  ? -21.194 -3.701  -4.165  1.00 26.74 ? 48  ILE B CG2   1 
ATOM   1445 C CD1   . ILE B 1 25  ? -20.052 -4.392  -1.334  1.00 20.77 ? 48  ILE B CD1   1 
ATOM   1446 N N     . ASN B 1 26  ? -22.313 -1.107  -5.585  1.00 23.35 ? 49  ASN B N     1 
ATOM   1447 C CA    . ASN B 1 26  ? -23.231 -1.121  -6.721  1.00 26.09 ? 49  ASN B CA    1 
ATOM   1448 C C     . ASN B 1 26  ? -23.096 -2.459  -7.428  1.00 25.14 ? 49  ASN B C     1 
ATOM   1449 O O     . ASN B 1 26  ? -22.134 -2.666  -8.182  1.00 26.92 ? 49  ASN B O     1 
ATOM   1450 C CB    . ASN B 1 26  ? -22.931 0.026   -7.696  1.00 21.11 ? 49  ASN B CB    1 
ATOM   1451 C CG    . ASN B 1 26  ? -23.821 -0.003  -8.934  1.00 29.96 ? 49  ASN B CG    1 
ATOM   1452 O OD1   . ASN B 1 26  ? -24.675 -0.886  -9.097  1.00 29.01 ? 49  ASN B OD1   1 
ATOM   1453 N ND2   . ASN B 1 26  ? -23.627 0.978   -9.818  1.00 30.88 ? 49  ASN B ND2   1 
ATOM   1454 N N     . PRO B 1 27  ? -24.036 -3.388  -7.251  1.00 25.67 ? 50  PRO B N     1 
ATOM   1455 C CA    . PRO B 1 27  ? -23.872 -4.715  -7.857  1.00 26.84 ? 50  PRO B CA    1 
ATOM   1456 C C     . PRO B 1 27  ? -24.073 -4.748  -9.366  1.00 28.88 ? 50  PRO B C     1 
ATOM   1457 O O     . PRO B 1 27  ? -23.855 -5.801  -9.966  1.00 31.05 ? 50  PRO B O     1 
ATOM   1458 C CB    . PRO B 1 27  ? -24.931 -5.568  -7.133  1.00 27.75 ? 50  PRO B CB    1 
ATOM   1459 C CG    . PRO B 1 27  ? -25.921 -4.582  -6.563  1.00 29.70 ? 50  PRO B CG    1 
ATOM   1460 C CD    . PRO B 1 27  ? -25.157 -3.323  -6.291  1.00 24.78 ? 50  PRO B CD    1 
ATOM   1461 N N     . HIS B 1 28  ? -24.455 -3.651  -10.014 1.00 28.25 ? 51  HIS B N     1 
ATOM   1462 C CA    . HIS B 1 28  ? -24.742 -3.671  -11.445 1.00 31.92 ? 51  HIS B CA    1 
ATOM   1463 C C     . HIS B 1 28  ? -23.647 -3.035  -12.297 1.00 31.81 ? 51  HIS B C     1 
ATOM   1464 O O     . HIS B 1 28  ? -23.848 -2.850  -13.503 1.00 31.80 ? 51  HIS B O     1 
ATOM   1465 C CB    . HIS B 1 28  ? -26.082 -2.977  -11.728 1.00 31.97 ? 51  HIS B CB    1 
ATOM   1466 C CG    . HIS B 1 28  ? -27.221 -3.531  -10.932 1.00 36.45 ? 51  HIS B CG    1 
ATOM   1467 N ND1   . HIS B 1 28  ? -27.612 -4.851  -11.016 1.00 42.03 ? 51  HIS B ND1   1 
ATOM   1468 C CD2   . HIS B 1 28  ? -28.046 -2.951  -10.028 1.00 38.70 ? 51  HIS B CD2   1 
ATOM   1469 C CE1   . HIS B 1 28  ? -28.628 -5.060  -10.196 1.00 43.48 ? 51  HIS B CE1   1 
ATOM   1470 N NE2   . HIS B 1 28  ? -28.913 -3.922  -9.588  1.00 41.48 ? 51  HIS B NE2   1 
ATOM   1471 N N     . SER B 1 29  ? -22.493 -2.710  -11.716 1.00 28.62 ? 52  SER B N     1 
ATOM   1472 C CA    . SER B 1 29  ? -21.463 -1.988  -12.457 1.00 26.09 ? 52  SER B CA    1 
ATOM   1473 C C     . SER B 1 29  ? -20.609 -2.903  -13.321 1.00 26.10 ? 52  SER B C     1 
ATOM   1474 O O     . SER B 1 29  ? -19.881 -2.414  -14.199 1.00 24.17 ? 52  SER B O     1 
ATOM   1475 C CB    . SER B 1 29  ? -20.564 -1.216  -11.481 1.00 28.64 ? 52  SER B CB    1 
ATOM   1476 O OG    . SER B 1 29  ? -19.919 -2.114  -10.580 1.00 24.69 ? 52  SER B OG    1 
ATOM   1477 N N     . GLY B 1 30  ? -20.679 -4.208  -13.097 1.00 23.99 ? 53  GLY B N     1 
ATOM   1478 C CA    . GLY B 1 30  ? -19.768 -5.121  -13.741 1.00 26.67 ? 53  GLY B CA    1 
ATOM   1479 C C     . GLY B 1 30  ? -18.368 -5.085  -13.181 1.00 25.07 ? 53  GLY B C     1 
ATOM   1480 O O     . GLY B 1 30  ? -17.471 -5.696  -13.761 1.00 27.32 ? 53  GLY B O     1 
ATOM   1481 N N     . LEU B 1 31  ? -18.144 -4.374  -12.078 1.00 23.88 ? 54  LEU B N     1 
ATOM   1482 C CA    . LEU B 1 31  ? -16.787 -4.296  -11.548 1.00 22.61 ? 54  LEU B CA    1 
ATOM   1483 C C     . LEU B 1 31  ? -16.666 -5.124  -10.272 1.00 24.49 ? 54  LEU B C     1 
ATOM   1484 O O     . LEU B 1 31  ? -17.622 -5.192  -9.487  1.00 22.81 ? 54  LEU B O     1 
ATOM   1485 C CB    . LEU B 1 31  ? -16.392 -2.842  -11.248 1.00 23.70 ? 54  LEU B CB    1 
ATOM   1486 C CG    . LEU B 1 31  ? -16.429 -1.858  -12.427 1.00 23.70 ? 54  LEU B CG    1 
ATOM   1487 C CD1   . LEU B 1 31  ? -16.092 -0.442  -11.975 1.00 23.40 ? 54  LEU B CD1   1 
ATOM   1488 C CD2   . LEU B 1 31  ? -15.485 -2.299  -13.550 1.00 23.75 ? 54  LEU B CD2   1 
ATOM   1489 N N     . PRO B 1 32  ? -15.514 -5.748  -10.033 1.00 22.40 ? 55  PRO B N     1 
ATOM   1490 C CA    . PRO B 1 32  ? -15.342 -6.544  -8.812  1.00 23.63 ? 55  PRO B CA    1 
ATOM   1491 C C     . PRO B 1 32  ? -15.259 -5.646  -7.583  1.00 21.03 ? 55  PRO B C     1 
ATOM   1492 O O     . PRO B 1 32  ? -15.134 -4.429  -7.679  1.00 23.07 ? 55  PRO B O     1 
ATOM   1493 C CB    . PRO B 1 32  ? -14.032 -7.300  -9.065  1.00 21.88 ? 55  PRO B CB    1 
ATOM   1494 C CG    . PRO B 1 32  ? -13.280 -6.433  -10.025 1.00 22.92 ? 55  PRO B CG    1 
ATOM   1495 C CD    . PRO B 1 32  ? -14.323 -5.801  -10.906 1.00 20.30 ? 55  PRO B CD    1 
ATOM   1496 N N     . VAL B 1 33  ? -15.358 -6.269  -6.407  1.00 19.96 ? 56  VAL B N     1 
ATOM   1497 C CA    . VAL B 1 33  ? -15.250 -5.580  -5.125  1.00 21.68 ? 56  VAL B CA    1 
ATOM   1498 C C     . VAL B 1 33  ? -13.963 -6.048  -4.450  1.00 22.13 ? 56  VAL B C     1 
ATOM   1499 O O     . VAL B 1 33  ? -13.546 -7.199  -4.620  1.00 20.55 ? 56  VAL B O     1 
ATOM   1500 C CB    . VAL B 1 33  ? -16.497 -5.859  -4.244  1.00 21.54 ? 56  VAL B CB    1 
ATOM   1501 C CG1   . VAL B 1 33  ? -16.349 -5.277  -2.831  1.00 17.53 ? 56  VAL B CG1   1 
ATOM   1502 C CG2   . VAL B 1 33  ? -17.781 -5.316  -4.921  1.00 23.55 ? 56  VAL B CG2   1 
ATOM   1503 N N     . LEU B 1 34  ? -13.320 -5.159  -3.690  1.00 19.01 ? 57  LEU B N     1 
ATOM   1504 C CA    . LEU B 1 34  ? -12.121 -5.520  -2.932  1.00 20.61 ? 57  LEU B CA    1 
ATOM   1505 C C     . LEU B 1 34  ? -12.397 -5.406  -1.437  1.00 17.32 ? 57  LEU B C     1 
ATOM   1506 O O     . LEU B 1 34  ? -12.872 -4.365  -0.972  1.00 19.95 ? 57  LEU B O     1 
ATOM   1507 C CB    . LEU B 1 34  ? -10.929 -4.628  -3.318  1.00 24.48 ? 57  LEU B CB    1 
ATOM   1508 C CG    . LEU B 1 34  ? -9.615  -4.836  -2.552  1.00 18.77 ? 57  LEU B CG    1 
ATOM   1509 C CD1   . LEU B 1 34  ? -9.038  -6.231  -2.865  1.00 15.60 ? 57  LEU B CD1   1 
ATOM   1510 C CD2   . LEU B 1 34  ? -8.596  -3.727  -2.878  1.00 18.62 ? 57  LEU B CD2   1 
ATOM   1511 N N     . GLU B 1 35  ? -12.098 -6.468  -0.679  1.00 18.46 ? 58  GLU B N     1 
ATOM   1512 C CA    . GLU B 1 35  ? -12.259 -6.467  0.774   1.00 19.85 ? 58  GLU B CA    1 
ATOM   1513 C C     . GLU B 1 35  ? -10.900 -6.635  1.440   1.00 21.39 ? 58  GLU B C     1 
ATOM   1514 O O     . GLU B 1 35  ? -10.120 -7.497  1.039   1.00 21.21 ? 58  GLU B O     1 
ATOM   1515 C CB    . GLU B 1 35  ? -13.214 -7.582  1.254   1.00 22.51 ? 58  GLU B CB    1 
ATOM   1516 C CG    . GLU B 1 35  ? -13.396 -7.569  2.786   1.00 23.37 ? 58  GLU B CG    1 
ATOM   1517 C CD    . GLU B 1 35  ? -14.251 -8.729  3.351   1.00 30.57 ? 58  GLU B CD    1 
ATOM   1518 O OE1   . GLU B 1 35  ? -14.499 -8.721  4.579   1.00 27.71 ? 58  GLU B OE1   1 
ATOM   1519 O OE2   . GLU B 1 35  ? -14.671 -9.643  2.596   1.00 25.56 ? 58  GLU B OE2   1 
ATOM   1520 N N     . LEU B 1 36  ? -10.621 -5.831  2.468   1.00 17.29 ? 59  LEU B N     1 
ATOM   1521 C CA    . LEU B 1 36  ? -9.385  -5.959  3.235   1.00 21.73 ? 59  LEU B CA    1 
ATOM   1522 C C     . LEU B 1 36  ? -9.680  -6.431  4.660   1.00 24.53 ? 59  LEU B C     1 
ATOM   1523 O O     . LEU B 1 36  ? -10.531 -5.860  5.351   1.00 22.05 ? 59  LEU B O     1 
ATOM   1524 C CB    . LEU B 1 36  ? -8.610  -4.635  3.248   1.00 21.59 ? 59  LEU B CB    1 
ATOM   1525 C CG    . LEU B 1 36  ? -8.453  -3.949  1.876   1.00 19.67 ? 59  LEU B CG    1 
ATOM   1526 C CD1   . LEU B 1 36  ? -7.748  -2.584  2.007   1.00 16.43 ? 59  LEU B CD1   1 
ATOM   1527 C CD2   . LEU B 1 36  ? -7.719  -4.844  0.857   1.00 20.57 ? 59  LEU B CD2   1 
ATOM   1528 N N     . GLY B 1 37  ? -8.966  -7.471  5.094   1.00 23.92 ? 60  GLY B N     1 
ATOM   1529 C CA    . GLY B 1 37  ? -9.078  -7.992  6.443   1.00 24.59 ? 60  GLY B CA    1 
ATOM   1530 C C     . GLY B 1 37  ? -10.382 -8.719  6.739   1.00 25.46 ? 60  GLY B C     1 
ATOM   1531 O O     . GLY B 1 37  ? -11.097 -8.375  7.683   1.00 24.30 ? 60  GLY B O     1 
ATOM   1532 N N     . PRO B 1 38  ? -10.714 -9.752  5.953   1.00 25.33 ? 61  PRO B N     1 
ATOM   1533 C CA    . PRO B 1 38  ? -12.033 -10.399 6.129   1.00 24.80 ? 61  PRO B CA    1 
ATOM   1534 C C     . PRO B 1 38  ? -12.217 -11.142 7.453   1.00 25.95 ? 61  PRO B C     1 
ATOM   1535 O O     . PRO B 1 38  ? -13.365 -11.321 7.879   1.00 24.28 ? 61  PRO B O     1 
ATOM   1536 C CB    . PRO B 1 38  ? -12.122 -11.361 4.933   1.00 24.19 ? 61  PRO B CB    1 
ATOM   1537 C CG    . PRO B 1 38  ? -10.685 -11.572 4.486   1.00 23.33 ? 61  PRO B CG    1 
ATOM   1538 C CD    . PRO B 1 38  ? -9.966  -10.292 4.800   1.00 22.40 ? 61  PRO B CD    1 
ATOM   1539 N N     . GLY B 1 39  ? -11.155 -11.616 8.095   1.00 24.57 ? 62  GLY B N     1 
ATOM   1540 C CA    . GLY B 1 39  ? -11.316 -12.180 9.432   1.00 26.31 ? 62  GLY B CA    1 
ATOM   1541 C C     . GLY B 1 39  ? -12.198 -13.422 9.414   1.00 30.07 ? 62  GLY B C     1 
ATOM   1542 O O     . GLY B 1 39  ? -11.950 -14.369 8.657   1.00 28.13 ? 62  GLY B O     1 
ATOM   1543 N N     . THR B 1 40  ? -13.257 -13.423 10.234  1.00 27.61 ? 63  THR B N     1 
ATOM   1544 C CA    . THR B 1 40  ? -14.194 -14.546 10.287  1.00 32.60 ? 63  THR B CA    1 
ATOM   1545 C C     . THR B 1 40  ? -15.242 -14.519 9.176   1.00 27.87 ? 63  THR B C     1 
ATOM   1546 O O     . THR B 1 40  ? -16.059 -15.446 9.094   1.00 29.77 ? 63  THR B O     1 
ATOM   1547 C CB    . THR B 1 40  ? -14.919 -14.588 11.635  1.00 28.57 ? 63  THR B CB    1 
ATOM   1548 O OG1   . THR B 1 40  ? -15.701 -13.396 11.798  1.00 31.97 ? 63  THR B OG1   1 
ATOM   1549 C CG2   . THR B 1 40  ? -13.920 -14.728 12.785  1.00 32.96 ? 63  THR B CG2   1 
ATOM   1550 N N     . GLY B 1 41  ? -15.267 -13.480 8.350   1.00 24.28 ? 64  GLY B N     1 
ATOM   1551 C CA    . GLY B 1 41  ? -16.139 -13.445 7.194   1.00 21.48 ? 64  GLY B CA    1 
ATOM   1552 C C     . GLY B 1 41  ? -17.479 -12.761 7.382   1.00 26.56 ? 64  GLY B C     1 
ATOM   1553 O O     . GLY B 1 41  ? -18.334 -12.872 6.493   1.00 24.66 ? 64  GLY B O     1 
ATOM   1554 N N     . VAL B 1 42  ? -17.692 -12.030 8.483   1.00 26.13 ? 65  VAL B N     1 
ATOM   1555 C CA    . VAL B 1 42  ? -19.001 -11.408 8.674   1.00 23.84 ? 65  VAL B CA    1 
ATOM   1556 C C     . VAL B 1 42  ? -19.243 -10.332 7.615   1.00 24.76 ? 65  VAL B C     1 
ATOM   1557 O O     . VAL B 1 42  ? -20.355 -10.208 7.083   1.00 24.11 ? 65  VAL B O     1 
ATOM   1558 C CB    . VAL B 1 42  ? -19.149 -10.871 10.114  1.00 28.55 ? 65  VAL B CB    1 
ATOM   1559 C CG1   . VAL B 1 42  ? -17.917 -10.097 10.539  1.00 37.53 ? 65  VAL B CG1   1 
ATOM   1560 C CG2   . VAL B 1 42  ? -20.398 -10.006 10.243  1.00 30.16 ? 65  VAL B CG2   1 
ATOM   1561 N N     . ILE B 1 43  ? -18.201 -9.579  7.244   1.00 23.11 ? 66  ILE B N     1 
ATOM   1562 C CA    . ILE B 1 43  ? -18.363 -8.578  6.184   1.00 19.45 ? 66  ILE B CA    1 
ATOM   1563 C C     . ILE B 1 43  ? -18.404 -9.248  4.815   1.00 22.50 ? 66  ILE B C     1 
ATOM   1564 O O     . ILE B 1 43  ? -19.112 -8.788  3.905   1.00 22.83 ? 66  ILE B O     1 
ATOM   1565 C CB    . ILE B 1 43  ? -17.243 -7.529  6.284   1.00 22.60 ? 66  ILE B CB    1 
ATOM   1566 C CG1   . ILE B 1 43  ? -17.341 -6.825  7.646   1.00 30.04 ? 66  ILE B CG1   1 
ATOM   1567 C CG2   . ILE B 1 43  ? -17.316 -6.532  5.121   1.00 24.76 ? 66  ILE B CG2   1 
ATOM   1568 C CD1   . ILE B 1 43  ? -16.177 -5.908  7.961   1.00 29.96 ? 66  ILE B CD1   1 
ATOM   1569 N N     . THR B 1 44  ? -17.654 -10.342 4.642   1.00 21.92 ? 67  THR B N     1 
ATOM   1570 C CA    . THR B 1 44  ? -17.729 -11.107 3.400   1.00 24.70 ? 67  THR B CA    1 
ATOM   1571 C C     . THR B 1 44  ? -19.162 -11.528 3.131   1.00 23.73 ? 67  THR B C     1 
ATOM   1572 O O     . THR B 1 44  ? -19.680 -11.362 2.018   1.00 23.03 ? 67  THR B O     1 
ATOM   1573 C CB    . THR B 1 44  ? -16.827 -12.342 3.489   1.00 23.81 ? 67  THR B CB    1 
ATOM   1574 O OG1   . THR B 1 44  ? -15.525 -11.938 3.923   1.00 23.76 ? 67  THR B OG1   1 
ATOM   1575 C CG2   . THR B 1 44  ? -16.729 -13.048 2.134   1.00 24.50 ? 67  THR B CG2   1 
ATOM   1576 N N     . LYS B 1 45  ? -19.824 -12.036 4.171   1.00 23.06 ? 68  LYS B N     1 
ATOM   1577 C CA    . LYS B 1 45  ? -21.208 -12.480 4.066   1.00 27.58 ? 68  LYS B CA    1 
ATOM   1578 C C     . LYS B 1 45  ? -22.130 -11.336 3.653   1.00 23.60 ? 68  LYS B C     1 
ATOM   1579 O O     . LYS B 1 45  ? -23.035 -11.524 2.837   1.00 26.49 ? 68  LYS B O     1 
ATOM   1580 C CB    . LYS B 1 45  ? -21.630 -13.087 5.409   1.00 24.87 ? 68  LYS B CB    1 
ATOM   1581 C CG    . LYS B 1 45  ? -22.901 -13.898 5.393   1.00 31.59 ? 68  LYS B CG    1 
ATOM   1582 C CD    . LYS B 1 45  ? -23.235 -14.339 6.814   1.00 35.40 ? 68  LYS B CD    1 
ATOM   1583 C CE    . LYS B 1 45  ? -24.219 -15.494 6.831   1.00 45.90 ? 68  LYS B CE    1 
ATOM   1584 N NZ    . LYS B 1 45  ? -25.464 -15.140 6.093   1.00 45.87 ? 68  LYS B NZ    1 
ATOM   1585 N N     . ALA B 1 46  ? -21.896 -10.134 4.184   1.00 23.09 ? 69  ALA B N     1 
ATOM   1586 C CA    . ALA B 1 46  ? -22.726 -8.987  3.827   1.00 23.55 ? 69  ALA B CA    1 
ATOM   1587 C C     . ALA B 1 46  ? -22.437 -8.474  2.415   1.00 20.29 ? 69  ALA B C     1 
ATOM   1588 O O     . ALA B 1 46  ? -23.344 -7.978  1.747   1.00 22.53 ? 69  ALA B O     1 
ATOM   1589 C CB    . ALA B 1 46  ? -22.522 -7.865  4.852   1.00 22.91 ? 69  ALA B CB    1 
ATOM   1590 N N     . ILE B 1 47  ? -21.183 -8.542  1.958   1.00 21.21 ? 70  ILE B N     1 
ATOM   1591 C CA    . ILE B 1 47  ? -20.876 -8.205  0.564   1.00 20.94 ? 70  ILE B CA    1 
ATOM   1592 C C     . ILE B 1 47  ? -21.601 -9.159  -0.380  1.00 23.11 ? 70  ILE B C     1 
ATOM   1593 O O     . ILE B 1 47  ? -22.251 -8.737  -1.344  1.00 23.69 ? 70  ILE B O     1 
ATOM   1594 C CB    . ILE B 1 47  ? -19.353 -8.238  0.322   1.00 19.49 ? 70  ILE B CB    1 
ATOM   1595 C CG1   . ILE B 1 47  ? -18.668 -7.115  1.108   1.00 19.98 ? 70  ILE B CG1   1 
ATOM   1596 C CG2   . ILE B 1 47  ? -19.031 -8.199  -1.205  1.00 17.87 ? 70  ILE B CG2   1 
ATOM   1597 C CD1   . ILE B 1 47  ? -17.152 -7.297  1.235   1.00 20.56 ? 70  ILE B CD1   1 
ATOM   1598 N N     . LEU B 1 48  ? -21.495 -10.465 -0.118  1.00 19.88 ? 71  LEU B N     1 
ATOM   1599 C CA    . LEU B 1 48  ? -22.162 -11.444 -0.970  1.00 23.65 ? 71  LEU B CA    1 
ATOM   1600 C C     . LEU B 1 48  ? -23.685 -11.291 -0.933  1.00 23.97 ? 71  LEU B C     1 
ATOM   1601 O O     . LEU B 1 48  ? -24.354 -11.534 -1.942  1.00 26.77 ? 71  LEU B O     1 
ATOM   1602 C CB    . LEU B 1 48  ? -21.746 -12.861 -0.553  1.00 23.50 ? 71  LEU B CB    1 
ATOM   1603 C CG    . LEU B 1 48  ? -20.257 -13.184 -0.734  1.00 29.22 ? 71  LEU B CG    1 
ATOM   1604 C CD1   . LEU B 1 48  ? -19.959 -14.639 -0.428  1.00 27.25 ? 71  LEU B CD1   1 
ATOM   1605 C CD2   . LEU B 1 48  ? -19.815 -12.830 -2.165  1.00 27.69 ? 71  LEU B CD2   1 
ATOM   1606 N N     . ALA B 1 49  ? -24.245 -10.872 0.203   1.00 22.12 ? 72  ALA B N     1 
ATOM   1607 C CA    . ALA B 1 49  ? -25.686 -10.661 0.293   1.00 26.44 ? 72  ALA B CA    1 
ATOM   1608 C C     . ALA B 1 49  ? -26.170 -9.522  -0.605  1.00 27.56 ? 72  ALA B C     1 
ATOM   1609 O O     . ALA B 1 49  ? -27.373 -9.422  -0.861  1.00 27.58 ? 72  ALA B O     1 
ATOM   1610 C CB    . ALA B 1 49  ? -26.088 -10.393 1.747   1.00 23.26 ? 72  ALA B CB    1 
ATOM   1611 N N     . ARG B 1 50  ? -25.273 -8.664  -1.089  1.00 24.80 ? 73  ARG B N     1 
ATOM   1612 C CA    . ARG B 1 50  ? -25.651 -7.656  -2.072  1.00 27.09 ? 73  ARG B CA    1 
ATOM   1613 C C     . ARG B 1 50  ? -25.870 -8.245  -3.460  1.00 27.63 ? 73  ARG B C     1 
ATOM   1614 O O     . ARG B 1 50  ? -26.223 -7.505  -4.379  1.00 30.33 ? 73  ARG B O     1 
ATOM   1615 C CB    . ARG B 1 50  ? -24.589 -6.550  -2.160  1.00 23.30 ? 73  ARG B CB    1 
ATOM   1616 C CG    . ARG B 1 50  ? -24.385 -5.739  -0.869  1.00 22.39 ? 73  ARG B CG    1 
ATOM   1617 C CD    . ARG B 1 50  ? -25.664 -5.021  -0.397  1.00 24.43 ? 73  ARG B CD    1 
ATOM   1618 N NE    . ARG B 1 50  ? -26.414 -4.413  -1.496  1.00 23.15 ? 73  ARG B NE    1 
ATOM   1619 C CZ    . ARG B 1 50  ? -26.096 -3.260  -2.086  1.00 24.01 ? 73  ARG B CZ    1 
ATOM   1620 N NH1   . ARG B 1 50  ? -25.045 -2.562  -1.677  1.00 22.19 ? 73  ARG B NH1   1 
ATOM   1621 N NH2   . ARG B 1 50  ? -26.831 -2.801  -3.092  1.00 23.66 ? 73  ARG B NH2   1 
ATOM   1622 N N     . GLY B 1 51  ? -25.673 -9.546  -3.646  1.00 25.89 ? 74  GLY B N     1 
ATOM   1623 C CA    . GLY B 1 51  ? -25.804 -10.135 -4.967  1.00 28.31 ? 74  GLY B CA    1 
ATOM   1624 C C     . GLY B 1 51  ? -24.556 -10.091 -5.817  1.00 31.37 ? 74  GLY B C     1 
ATOM   1625 O O     . GLY B 1 51  ? -24.648 -10.237 -7.043  1.00 31.08 ? 74  GLY B O     1 
ATOM   1626 N N     . ILE B 1 52  ? -23.394 -9.882  -5.204  1.00 26.53 ? 75  ILE B N     1 
ATOM   1627 C CA    . ILE B 1 52  ? -22.123 -9.944  -5.911  1.00 31.15 ? 75  ILE B CA    1 
ATOM   1628 C C     . ILE B 1 52  ? -21.800 -11.400 -6.227  1.00 31.15 ? 75  ILE B C     1 
ATOM   1629 O O     . ILE B 1 52  ? -21.870 -12.271 -5.350  1.00 28.73 ? 75  ILE B O     1 
ATOM   1630 C CB    . ILE B 1 52  ? -21.019 -9.304  -5.052  1.00 27.03 ? 75  ILE B CB    1 
ATOM   1631 C CG1   . ILE B 1 52  ? -21.292 -7.808  -4.866  1.00 29.75 ? 75  ILE B CG1   1 
ATOM   1632 C CG2   . ILE B 1 52  ? -19.662 -9.523  -5.665  1.00 28.24 ? 75  ILE B CG2   1 
ATOM   1633 C CD1   . ILE B 1 52  ? -21.187 -7.011  -6.171  1.00 27.75 ? 75  ILE B CD1   1 
ATOM   1634 N N     . LYS B 1 53  ? -21.444 -11.671 -7.474  1.00 26.20 ? 76  LYS B N     1 
ATOM   1635 C CA    . LYS B 1 53  ? -20.938 -12.989 -7.823  1.00 29.81 ? 76  LYS B CA    1 
ATOM   1636 C C     . LYS B 1 53  ? -19.695 -13.294 -6.985  1.00 28.93 ? 76  LYS B C     1 
ATOM   1637 O O     . LYS B 1 53  ? -18.826 -12.418 -6.832  1.00 25.38 ? 76  LYS B O     1 
ATOM   1638 C CB    . LYS B 1 53  ? -20.606 -13.048 -9.313  1.00 32.29 ? 76  LYS B CB    1 
ATOM   1639 C CG    . LYS B 1 53  ? -20.337 -14.453 -9.793  1.00 35.80 ? 76  LYS B CG    1 
ATOM   1640 C CD    . LYS B 1 53  ? -19.389 -14.462 -10.972 1.00 43.67 ? 76  LYS B CD    1 
ATOM   1641 C CE    . LYS B 1 53  ? -19.842 -13.518 -12.061 1.00 38.59 ? 76  LYS B CE    1 
ATOM   1642 N NZ    . LYS B 1 53  ? -19.094 -13.808 -13.320 1.00 50.50 ? 76  LYS B NZ    1 
ATOM   1643 N N     . PRO B 1 54  ? -19.591 -14.487 -6.387  1.00 26.43 ? 77  PRO B N     1 
ATOM   1644 C CA    . PRO B 1 54  ? -18.454 -14.748 -5.478  1.00 26.21 ? 77  PRO B CA    1 
ATOM   1645 C C     . PRO B 1 54  ? -17.095 -14.557 -6.127  1.00 27.43 ? 77  PRO B C     1 
ATOM   1646 O O     . PRO B 1 54  ? -16.193 -13.968 -5.511  1.00 26.15 ? 77  PRO B O     1 
ATOM   1647 C CB    . PRO B 1 54  ? -18.686 -16.205 -5.048  1.00 25.56 ? 77  PRO B CB    1 
ATOM   1648 C CG    . PRO B 1 54  ? -20.179 -16.353 -5.094  1.00 30.87 ? 77  PRO B CG    1 
ATOM   1649 C CD    . PRO B 1 54  ? -20.624 -15.538 -6.294  1.00 31.69 ? 77  PRO B CD    1 
ATOM   1650 N N     . GLU B 1 55  ? -16.932 -15.022 -7.370  1.00 24.00 ? 78  GLU B N     1 
ATOM   1651 C CA    . GLU B 1 55  ? -15.681 -14.843 -8.101  1.00 27.94 ? 78  GLU B CA    1 
ATOM   1652 C C     . GLU B 1 55  ? -15.302 -13.378 -8.270  1.00 25.56 ? 78  GLU B C     1 
ATOM   1653 O O     . GLU B 1 55  ? -14.129 -13.081 -8.510  1.00 24.43 ? 78  GLU B O     1 
ATOM   1654 C CB    . GLU B 1 55  ? -15.786 -15.490 -9.488  1.00 29.74 ? 78  GLU B CB    1 
ATOM   1655 C CG    . GLU B 1 55  ? -15.853 -17.013 -9.489  1.00 38.87 ? 78  GLU B CG    1 
ATOM   1656 C CD    . GLU B 1 55  ? -17.191 -17.582 -8.969  1.00 45.03 ? 78  GLU B CD    1 
ATOM   1657 O OE1   . GLU B 1 55  ? -17.186 -18.760 -8.522  1.00 47.27 ? 78  GLU B OE1   1 
ATOM   1658 O OE2   . GLU B 1 55  ? -18.232 -16.869 -8.996  1.00 35.03 ? 78  GLU B OE2   1 
ATOM   1659 N N     . SER B 1 56  ? -16.265 -12.465 -8.188  1.00 26.28 ? 79  SER B N     1 
ATOM   1660 C CA    . SER B 1 56  ? -16.020 -11.037 -8.344  1.00 27.72 ? 79  SER B CA    1 
ATOM   1661 C C     . SER B 1 56  ? -15.642 -10.344 -7.038  1.00 24.38 ? 79  SER B C     1 
ATOM   1662 O O     . SER B 1 56  ? -15.529 -9.115  -7.018  1.00 27.29 ? 79  SER B O     1 
ATOM   1663 C CB    . SER B 1 56  ? -17.257 -10.359 -8.943  1.00 30.32 ? 79  SER B CB    1 
ATOM   1664 O OG    . SER B 1 56  ? -17.439 -10.775 -10.286 1.00 34.81 ? 79  SER B OG    1 
ATOM   1665 N N     . LEU B 1 57  ? -15.454 -11.085 -5.951  1.00 22.37 ? 80  LEU B N     1 
ATOM   1666 C CA    . LEU B 1 57  ? -14.937 -10.538 -4.701  1.00 21.19 ? 80  LEU B CA    1 
ATOM   1667 C C     . LEU B 1 57  ? -13.488 -10.982 -4.536  1.00 24.32 ? 80  LEU B C     1 
ATOM   1668 O O     . LEU B 1 57  ? -13.199 -12.186 -4.572  1.00 22.23 ? 80  LEU B O     1 
ATOM   1669 C CB    . LEU B 1 57  ? -15.771 -11.007 -3.506  1.00 21.78 ? 80  LEU B CB    1 
ATOM   1670 C CG    . LEU B 1 57  ? -15.310 -10.564 -2.113  1.00 22.03 ? 80  LEU B CG    1 
ATOM   1671 C CD1   . LEU B 1 57  ? -15.249 -9.015  -2.033  1.00 19.45 ? 80  LEU B CD1   1 
ATOM   1672 C CD2   . LEU B 1 57  ? -16.235 -11.153 -1.018  1.00 21.77 ? 80  LEU B CD2   1 
ATOM   1673 N N     . THR B 1 58  ? -12.583 -10.017 -4.367  1.00 20.92 ? 81  THR B N     1 
ATOM   1674 C CA    . THR B 1 58  ? -11.203 -10.264 -3.945  1.00 20.18 ? 81  THR B CA    1 
ATOM   1675 C C     . THR B 1 58  ? -11.065 -9.802  -2.503  1.00 19.32 ? 81  THR B C     1 
ATOM   1676 O O     . THR B 1 58  ? -11.480 -8.693  -2.177  1.00 23.71 ? 81  THR B O     1 
ATOM   1677 C CB    . THR B 1 58  ? -10.203 -9.517  -4.837  1.00 23.97 ? 81  THR B CB    1 
ATOM   1678 O OG1   . THR B 1 58  ? -10.279 -10.022 -6.172  1.00 23.27 ? 81  THR B OG1   1 
ATOM   1679 C CG2   . THR B 1 58  ? -8.759  -9.671  -4.319  1.00 20.44 ? 81  THR B CG2   1 
ATOM   1680 N N     . ALA B 1 59  ? -10.524 -10.655 -1.633  1.00 20.83 ? 82  ALA B N     1 
ATOM   1681 C CA    . ALA B 1 59  ? -10.371 -10.330 -0.217  1.00 20.02 ? 82  ALA B CA    1 
ATOM   1682 C C     . ALA B 1 59  ? -8.958  -10.689 0.226   1.00 24.50 ? 82  ALA B C     1 
ATOM   1683 O O     . ALA B 1 59  ? -8.534  -11.840 0.080   1.00 20.85 ? 82  ALA B O     1 
ATOM   1684 C CB    . ALA B 1 59  ? -11.414 -11.070 0.635   1.00 21.33 ? 82  ALA B CB    1 
ATOM   1685 N N     . ILE B 1 60  ? -8.232  -9.715  0.775   1.00 23.27 ? 83  ILE B N     1 
ATOM   1686 C CA    . ILE B 1 60  ? -6.847  -9.906  1.194   1.00 24.23 ? 83  ILE B CA    1 
ATOM   1687 C C     . ILE B 1 60  ? -6.825  -10.079 2.708   1.00 25.68 ? 83  ILE B C     1 
ATOM   1688 O O     . ILE B 1 60  ? -7.292  -9.199  3.444   1.00 26.06 ? 83  ILE B O     1 
ATOM   1689 C CB    . ILE B 1 60  ? -5.968  -8.728  0.743   1.00 23.64 ? 83  ILE B CB    1 
ATOM   1690 C CG1   . ILE B 1 60  ? -6.051  -8.565  -0.772  1.00 20.11 ? 83  ILE B CG1   1 
ATOM   1691 C CG2   . ILE B 1 60  ? -4.514  -8.946  1.134   1.00 25.46 ? 83  ILE B CG2   1 
ATOM   1692 C CD1   . ILE B 1 60  ? -5.368  -7.331  -1.286  1.00 24.52 ? 83  ILE B CD1   1 
ATOM   1693 N N     . GLU B 1 61  ? -6.275  -11.205 3.181   1.00 24.04 ? 84  GLU B N     1 
ATOM   1694 C CA    . GLU B 1 61  ? -6.275  -11.555 4.603   1.00 21.25 ? 84  GLU B CA    1 
ATOM   1695 C C     . GLU B 1 61  ? -4.881  -11.973 5.062   1.00 24.81 ? 84  GLU B C     1 
ATOM   1696 O O     . GLU B 1 61  ? -4.342  -12.985 4.596   1.00 25.55 ? 84  GLU B O     1 
ATOM   1697 C CB    . GLU B 1 61  ? -7.278  -12.683 4.891   1.00 20.76 ? 84  GLU B CB    1 
ATOM   1698 C CG    . GLU B 1 61  ? -7.196  -13.247 6.305   1.00 23.94 ? 84  GLU B CG    1 
ATOM   1699 C CD    . GLU B 1 61  ? -7.322  -12.179 7.390   1.00 28.75 ? 84  GLU B CD    1 
ATOM   1700 O OE1   . GLU B 1 61  ? -6.400  -12.057 8.234   1.00 27.00 ? 84  GLU B OE1   1 
ATOM   1701 O OE2   . GLU B 1 61  ? -8.356  -11.483 7.412   1.00 26.43 ? 84  GLU B OE2   1 
ATOM   1702 N N     . TYR B 1 62  ? -4.334  -11.239 6.031   1.00 26.47 ? 85  TYR B N     1 
ATOM   1703 C CA    . TYR B 1 62  ? -2.977  -11.499 6.509   1.00 25.50 ? 85  TYR B CA    1 
ATOM   1704 C C     . TYR B 1 62  ? -2.866  -12.836 7.251   1.00 29.25 ? 85  TYR B C     1 
ATOM   1705 O O     . TYR B 1 62  ? -1.867  -13.554 7.103   1.00 29.21 ? 85  TYR B O     1 
ATOM   1706 C CB    . TYR B 1 62  ? -2.537  -10.342 7.407   1.00 30.52 ? 85  TYR B CB    1 
ATOM   1707 C CG    . TYR B 1 62  ? -1.119  -10.431 7.902   1.00 31.30 ? 85  TYR B CG    1 
ATOM   1708 C CD1   . TYR B 1 62  ? -0.829  -11.034 9.119   1.00 35.38 ? 85  TYR B CD1   1 
ATOM   1709 C CD2   . TYR B 1 62  ? -0.072  -9.899  7.161   1.00 34.11 ? 85  TYR B CD2   1 
ATOM   1710 C CE1   . TYR B 1 62  ? 0.462   -11.114 9.579   1.00 39.32 ? 85  TYR B CE1   1 
ATOM   1711 C CE2   . TYR B 1 62  ? 1.225   -9.969  7.616   1.00 39.22 ? 85  TYR B CE2   1 
ATOM   1712 C CZ    . TYR B 1 62  ? 1.489   -10.584 8.823   1.00 42.28 ? 85  TYR B CZ    1 
ATOM   1713 O OH    . TYR B 1 62  ? 2.786   -10.665 9.284   1.00 50.22 ? 85  TYR B OH    1 
ATOM   1714 N N     . SER B 1 63  ? -3.870  -13.187 8.055   1.00 26.63 ? 86  SER B N     1 
ATOM   1715 C CA    . SER B 1 63  ? -3.806  -14.377 8.898   1.00 28.50 ? 86  SER B CA    1 
ATOM   1716 C C     . SER B 1 63  ? -4.056  -15.647 8.081   1.00 31.19 ? 86  SER B C     1 
ATOM   1717 O O     . SER B 1 63  ? -5.150  -15.842 7.539   1.00 25.21 ? 86  SER B O     1 
ATOM   1718 C CB    . SER B 1 63  ? -4.818  -14.277 10.031  1.00 27.78 ? 86  SER B CB    1 
ATOM   1719 O OG    . SER B 1 63  ? -5.043  -15.555 10.609  1.00 34.67 ? 86  SER B OG    1 
ATOM   1720 N N     . THR B 1 64  ? -3.049  -16.524 8.021   1.00 28.20 ? 87  THR B N     1 
ATOM   1721 C CA    . THR B 1 64  ? -3.204  -17.789 7.300   1.00 29.90 ? 87  THR B CA    1 
ATOM   1722 C C     . THR B 1 64  ? -4.301  -18.644 7.926   1.00 29.35 ? 87  THR B C     1 
ATOM   1723 O O     . THR B 1 64  ? -5.067  -19.306 7.215   1.00 31.93 ? 87  THR B O     1 
ATOM   1724 C CB    . THR B 1 64  ? -1.868  -18.541 7.265   1.00 28.26 ? 87  THR B CB    1 
ATOM   1725 O OG1   . THR B 1 64  ? -0.885  -17.732 6.601   1.00 28.15 ? 87  THR B OG1   1 
ATOM   1726 C CG2   . THR B 1 64  ? -2.002  -19.896 6.536   1.00 28.98 ? 87  THR B CG2   1 
ATOM   1727 N N     . ASP B 1 65  ? -4.403  -18.615 9.257   1.00 32.46 ? 88  ASP B N     1 
ATOM   1728 C CA    . ASP B 1 65  ? -5.490  -19.264 9.988   1.00 32.74 ? 88  ASP B CA    1 
ATOM   1729 C C     . ASP B 1 65  ? -6.859  -18.830 9.475   1.00 33.40 ? 88  ASP B C     1 
ATOM   1730 O O     . ASP B 1 65  ? -7.686  -19.660 9.083   1.00 31.84 ? 88  ASP B O     1 
ATOM   1731 C CB    . ASP B 1 65  ? -5.391  -18.914 11.474  1.00 38.30 ? 88  ASP B CB    1 
ATOM   1732 C CG    . ASP B 1 65  ? -4.824  -20.024 12.302  1.00 50.04 ? 88  ASP B CG    1 
ATOM   1733 O OD1   . ASP B 1 65  ? -3.998  -20.803 11.772  1.00 57.30 ? 88  ASP B OD1   1 
ATOM   1734 O OD2   . ASP B 1 65  ? -5.199  -20.105 13.493  1.00 62.21 ? 88  ASP B OD2   1 
ATOM   1735 N N     . PHE B 1 66  ? -7.140  -17.522 9.553   1.00 30.46 ? 89  PHE B N     1 
ATOM   1736 C CA    . PHE B 1 66  ? -8.421  -17.003 9.082   1.00 28.68 ? 89  PHE B CA    1 
ATOM   1737 C C     . PHE B 1 66  ? -8.650  -17.356 7.621   1.00 24.91 ? 89  PHE B C     1 
ATOM   1738 O O     . PHE B 1 66  ? -9.758  -17.741 7.225   1.00 25.87 ? 89  PHE B O     1 
ATOM   1739 C CB    . PHE B 1 66  ? -8.467  -15.484 9.260   1.00 27.00 ? 89  PHE B CB    1 
ATOM   1740 C CG    . PHE B 1 66  ? -8.779  -15.044 10.658  1.00 31.50 ? 89  PHE B CG    1 
ATOM   1741 C CD1   . PHE B 1 66  ? -9.553  -15.839 11.492  1.00 34.27 ? 89  PHE B CD1   1 
ATOM   1742 C CD2   . PHE B 1 66  ? -8.313  -13.826 11.139  1.00 29.35 ? 89  PHE B CD2   1 
ATOM   1743 C CE1   . PHE B 1 66  ? -9.848  -15.425 12.792  1.00 41.40 ? 89  PHE B CE1   1 
ATOM   1744 C CE2   . PHE B 1 66  ? -8.610  -13.405 12.436  1.00 32.89 ? 89  PHE B CE2   1 
ATOM   1745 C CZ    . PHE B 1 66  ? -9.375  -14.201 13.258  1.00 35.09 ? 89  PHE B CZ    1 
ATOM   1746 N N     . TYR B 1 67  ? -7.607  -17.210 6.811   1.00 24.42 ? 90  TYR B N     1 
ATOM   1747 C CA    . TYR B 1 67  ? -7.689  -17.470 5.380   1.00 28.67 ? 90  TYR B CA    1 
ATOM   1748 C C     . TYR B 1 67  ? -8.099  -18.915 5.104   1.00 29.97 ? 90  TYR B C     1 
ATOM   1749 O O     . TYR B 1 67  ? -8.970  -19.166 4.258   1.00 25.75 ? 90  TYR B O     1 
ATOM   1750 C CB    . TYR B 1 67  ? -6.330  -17.137 4.762   1.00 25.91 ? 90  TYR B CB    1 
ATOM   1751 C CG    . TYR B 1 67  ? -6.050  -17.619 3.355   1.00 27.22 ? 90  TYR B CG    1 
ATOM   1752 C CD1   . TYR B 1 67  ? -6.462  -16.881 2.252   1.00 22.28 ? 90  TYR B CD1   1 
ATOM   1753 C CD2   . TYR B 1 67  ? -5.317  -18.785 3.129   1.00 28.61 ? 90  TYR B CD2   1 
ATOM   1754 C CE1   . TYR B 1 67  ? -6.184  -17.312 0.962   1.00 24.27 ? 90  TYR B CE1   1 
ATOM   1755 C CE2   . TYR B 1 67  ? -5.033  -19.217 1.848   1.00 29.11 ? 90  TYR B CE2   1 
ATOM   1756 C CZ    . TYR B 1 67  ? -5.459  -18.472 0.769   1.00 27.68 ? 90  TYR B CZ    1 
ATOM   1757 O OH    . TYR B 1 67  ? -5.176  -18.901 -0.508  1.00 32.80 ? 90  TYR B OH    1 
ATOM   1758 N N     . ASN B 1 68  ? -7.498  -19.874 5.828   1.00 29.46 ? 91  ASN B N     1 
ATOM   1759 C CA    . ASN B 1 68  ? -7.802  -21.291 5.606   1.00 27.21 ? 91  ASN B CA    1 
ATOM   1760 C C     . ASN B 1 68  ? -9.268  -21.581 5.857   1.00 27.95 ? 91  ASN B C     1 
ATOM   1761 O O     . ASN B 1 68  ? -9.892  -22.353 5.121   1.00 29.26 ? 91  ASN B O     1 
ATOM   1762 C CB    . ASN B 1 68  ? -6.942  -22.178 6.515   1.00 27.37 ? 91  ASN B CB    1 
ATOM   1763 C CG    . ASN B 1 68  ? -5.509  -22.279 6.042   1.00 30.94 ? 91  ASN B CG    1 
ATOM   1764 O OD1   . ASN B 1 68  ? -5.232  -22.109 4.867   1.00 28.29 ? 91  ASN B OD1   1 
ATOM   1765 N ND2   . ASN B 1 68  ? -4.592  -22.560 6.961   1.00 33.47 ? 91  ASN B ND2   1 
ATOM   1766 N N     . GLN B 1 69  ? -9.831  -20.987 6.908   1.00 27.52 ? 92  GLN B N     1 
ATOM   1767 C CA    . GLN B 1 69  ? -11.229 -21.218 7.208   1.00 26.46 ? 92  GLN B CA    1 
ATOM   1768 C C     . GLN B 1 69  ? -12.125 -20.560 6.165   1.00 30.39 ? 92  GLN B C     1 
ATOM   1769 O O     . GLN B 1 69  ? -13.120 -21.153 5.729   1.00 28.19 ? 92  GLN B O     1 
ATOM   1770 C CB    . GLN B 1 69  ? -11.540 -20.705 8.616   1.00 31.57 ? 92  GLN B CB    1 
ATOM   1771 C CG    . GLN B 1 69  ? -12.982 -20.897 9.026   1.00 35.58 ? 92  GLN B CG    1 
ATOM   1772 C CD    . GLN B 1 69  ? -13.471 -22.335 8.818   1.00 49.64 ? 92  GLN B CD    1 
ATOM   1773 O OE1   . GLN B 1 69  ? -14.432 -22.581 8.072   1.00 44.59 ? 92  GLN B OE1   1 
ATOM   1774 N NE2   . GLN B 1 69  ? -12.805 -23.290 9.475   1.00 45.54 ? 92  GLN B NE2   1 
ATOM   1775 N N     . LEU B 1 70  ? -11.786 -19.335 5.754   1.00 26.08 ? 93  LEU B N     1 
ATOM   1776 C CA    . LEU B 1 70  ? -12.575 -18.637 4.745   1.00 26.36 ? 93  LEU B CA    1 
ATOM   1777 C C     . LEU B 1 70  ? -12.654 -19.435 3.450   1.00 27.49 ? 93  LEU B C     1 
ATOM   1778 O O     . LEU B 1 70  ? -13.694 -19.430 2.780   1.00 25.35 ? 93  LEU B O     1 
ATOM   1779 C CB    . LEU B 1 70  ? -11.974 -17.255 4.480   1.00 23.66 ? 93  LEU B CB    1 
ATOM   1780 C CG    . LEU B 1 70  ? -12.207 -16.258 5.620   1.00 26.10 ? 93  LEU B CG    1 
ATOM   1781 C CD1   . LEU B 1 70  ? -11.287 -15.042 5.490   1.00 26.68 ? 93  LEU B CD1   1 
ATOM   1782 C CD2   . LEU B 1 70  ? -13.666 -15.843 5.671   1.00 22.65 ? 93  LEU B CD2   1 
ATOM   1783 N N     . LEU B 1 71  ? -11.554 -20.107 3.065   1.00 24.77 ? 94  LEU B N     1 
ATOM   1784 C CA    . LEU B 1 71  ? -11.564 -20.911 1.844   1.00 28.61 ? 94  LEU B CA    1 
ATOM   1785 C C     . LEU B 1 71  ? -12.619 -22.005 1.910   1.00 28.02 ? 94  LEU B C     1 
ATOM   1786 O O     . LEU B 1 71  ? -13.154 -22.420 0.872   1.00 23.54 ? 94  LEU B O     1 
ATOM   1787 C CB    . LEU B 1 71  ? -10.195 -21.547 1.590   1.00 30.97 ? 94  LEU B CB    1 
ATOM   1788 C CG    . LEU B 1 71  ? -9.012  -20.700 1.112   1.00 29.10 ? 94  LEU B CG    1 
ATOM   1789 C CD1   . LEU B 1 71  ? -7.799  -21.594 0.917   1.00 33.37 ? 94  LEU B CD1   1 
ATOM   1790 C CD2   . LEU B 1 71  ? -9.327  -19.977 -0.179  1.00 33.72 ? 94  LEU B CD2   1 
ATOM   1791 N N     . ARG B 1 72  ? -12.938 -22.480 3.113   1.00 26.08 ? 95  ARG B N     1 
ATOM   1792 C CA    . ARG B 1 72  ? -13.903 -23.564 3.225   1.00 26.92 ? 95  ARG B CA    1 
ATOM   1793 C C     . ARG B 1 72  ? -15.330 -23.045 3.192   1.00 24.36 ? 95  ARG B C     1 
ATOM   1794 O O     . ARG B 1 72  ? -16.212 -23.697 2.627   1.00 23.32 ? 95  ARG B O     1 
ATOM   1795 C CB    . ARG B 1 72  ? -13.663 -24.349 4.510   1.00 29.28 ? 95  ARG B CB    1 
ATOM   1796 C CG    . ARG B 1 72  ? -12.280 -24.957 4.587   1.00 30.21 ? 95  ARG B CG    1 
ATOM   1797 C CD    . ARG B 1 72  ? -12.118 -25.691 5.899   1.00 34.15 ? 95  ARG B CD    1 
ATOM   1798 N NE    . ARG B 1 72  ? -10.954 -26.560 5.852   1.00 43.72 ? 95  ARG B NE    1 
ATOM   1799 C CZ    . ARG B 1 72  ? -10.924 -27.781 6.367   1.00 37.90 ? 95  ARG B CZ    1 
ATOM   1800 N NH1   . ARG B 1 72  ? -12.006 -28.281 6.966   1.00 31.50 ? 95  ARG B NH1   1 
ATOM   1801 N NH2   . ARG B 1 72  ? -9.806  -28.489 6.287   1.00 39.76 ? 95  ARG B NH2   1 
ATOM   1802 N N     . SER B 1 73  ? -15.574 -21.877 3.800   1.00 24.28 ? 96  SER B N     1 
ATOM   1803 C CA    . SER B 1 73  ? -16.928 -21.354 3.903   1.00 25.34 ? 96  SER B CA    1 
ATOM   1804 C C     . SER B 1 73  ? -17.380 -20.655 2.628   1.00 24.75 ? 96  SER B C     1 
ATOM   1805 O O     . SER B 1 73  ? -18.573 -20.685 2.303   1.00 23.86 ? 96  SER B O     1 
ATOM   1806 C CB    . SER B 1 73  ? -17.027 -20.379 5.076   1.00 27.91 ? 96  SER B CB    1 
ATOM   1807 O OG    . SER B 1 73  ? -16.621 -21.001 6.274   1.00 33.16 ? 96  SER B OG    1 
ATOM   1808 N N     . TYR B 1 74  ? -16.462 -20.007 1.917   1.00 24.52 ? 97  TYR B N     1 
ATOM   1809 C CA    . TYR B 1 74  ? -16.790 -19.219 0.728   1.00 21.93 ? 97  TYR B CA    1 
ATOM   1810 C C     . TYR B 1 74  ? -15.855 -19.621 -0.401  1.00 23.02 ? 97  TYR B C     1 
ATOM   1811 O O     . TYR B 1 74  ? -14.975 -18.847 -0.805  1.00 23.23 ? 97  TYR B O     1 
ATOM   1812 C CB    . TYR B 1 74  ? -16.672 -17.723 1.018   1.00 24.68 ? 97  TYR B CB    1 
ATOM   1813 C CG    . TYR B 1 74  ? -17.451 -17.285 2.230   1.00 24.22 ? 97  TYR B CG    1 
ATOM   1814 C CD1   . TYR B 1 74  ? -18.820 -17.078 2.159   1.00 25.59 ? 97  TYR B CD1   1 
ATOM   1815 C CD2   . TYR B 1 74  ? -16.812 -17.069 3.441   1.00 24.58 ? 97  TYR B CD2   1 
ATOM   1816 C CE1   . TYR B 1 74  ? -19.549 -16.655 3.282   1.00 27.61 ? 97  TYR B CE1   1 
ATOM   1817 C CE2   . TYR B 1 74  ? -17.525 -16.655 4.572   1.00 26.95 ? 97  TYR B CE2   1 
ATOM   1818 C CZ    . TYR B 1 74  ? -18.890 -16.449 4.485   1.00 29.86 ? 97  TYR B CZ    1 
ATOM   1819 O OH    . TYR B 1 74  ? -19.587 -16.033 5.607   1.00 33.39 ? 97  TYR B OH    1 
ATOM   1820 N N     . PRO B 1 75  ? -16.025 -20.829 -0.945  1.00 23.60 ? 98  PRO B N     1 
ATOM   1821 C CA    . PRO B 1 75  ? -15.041 -21.333 -1.921  1.00 25.41 ? 98  PRO B CA    1 
ATOM   1822 C C     . PRO B 1 75  ? -14.975 -20.542 -3.218  1.00 26.26 ? 98  PRO B C     1 
ATOM   1823 O O     . PRO B 1 75  ? -13.923 -20.544 -3.873  1.00 32.79 ? 98  PRO B O     1 
ATOM   1824 C CB    . PRO B 1 75  ? -15.502 -22.781 -2.165  1.00 26.82 ? 98  PRO B CB    1 
ATOM   1825 C CG    . PRO B 1 75  ? -16.971 -22.791 -1.791  1.00 22.48 ? 98  PRO B CG    1 
ATOM   1826 C CD    . PRO B 1 75  ? -17.091 -21.809 -0.661  1.00 22.63 ? 98  PRO B CD    1 
ATOM   1827 N N     . GLY B 1 76  ? -16.051 -19.880 -3.630  1.00 25.82 ? 99  GLY B N     1 
ATOM   1828 C CA    . GLY B 1 76  ? -15.972 -19.138 -4.882  1.00 33.01 ? 99  GLY B CA    1 
ATOM   1829 C C     . GLY B 1 76  ? -15.260 -17.787 -4.830  1.00 28.23 ? 99  GLY B C     1 
ATOM   1830 O O     . GLY B 1 76  ? -15.001 -17.209 -5.888  1.00 29.35 ? 99  GLY B O     1 
ATOM   1831 N N     . VAL B 1 77  ? -14.938 -17.276 -3.643  1.00 23.78 ? 100 VAL B N     1 
ATOM   1832 C CA    . VAL B 1 77  ? -14.325 -15.957 -3.488  1.00 23.54 ? 100 VAL B CA    1 
ATOM   1833 C C     . VAL B 1 77  ? -12.825 -16.020 -3.769  1.00 26.33 ? 100 VAL B C     1 
ATOM   1834 O O     . VAL B 1 77  ? -12.152 -17.011 -3.466  1.00 23.33 ? 100 VAL B O     1 
ATOM   1835 C CB    . VAL B 1 77  ? -14.619 -15.427 -2.069  1.00 26.91 ? 100 VAL B CB    1 
ATOM   1836 C CG1   . VAL B 1 77  ? -13.880 -14.101 -1.785  1.00 23.51 ? 100 VAL B CG1   1 
ATOM   1837 C CG2   . VAL B 1 77  ? -16.115 -15.250 -1.892  1.00 22.70 ? 100 VAL B CG2   1 
ATOM   1838 N N     . ASN B 1 78  ? -12.279 -14.939 -4.335  1.00 20.97 ? 101 ASN B N     1 
ATOM   1839 C CA    . ASN B 1 78  ? -10.843 -14.854 -4.632  1.00 25.41 ? 101 ASN B CA    1 
ATOM   1840 C C     . ASN B 1 78  ? -10.098 -14.338 -3.396  1.00 25.17 ? 101 ASN B C     1 
ATOM   1841 O O     . ASN B 1 78  ? -9.772  -13.153 -3.268  1.00 26.02 ? 101 ASN B O     1 
ATOM   1842 C CB    . ASN B 1 78  ? -10.604 -13.964 -5.857  1.00 21.84 ? 101 ASN B CB    1 
ATOM   1843 C CG    . ASN B 1 78  ? -9.117  -13.803 -6.194  1.00 33.19 ? 101 ASN B CG    1 
ATOM   1844 O OD1   . ASN B 1 78  ? -8.342  -14.754 -6.104  1.00 32.09 ? 101 ASN B OD1   1 
ATOM   1845 N ND2   . ASN B 1 78  ? -8.717  -12.585 -6.588  1.00 34.17 ? 101 ASN B ND2   1 
ATOM   1846 N N     . PHE B 1 79  ? -9.806  -15.256 -2.471  1.00 23.96 ? 102 PHE B N     1 
ATOM   1847 C CA    . PHE B 1 79  ? -9.030  -14.915 -1.283  1.00 24.22 ? 102 PHE B CA    1 
ATOM   1848 C C     . PHE B 1 79  ? -7.533  -14.923 -1.579  1.00 25.66 ? 102 PHE B C     1 
ATOM   1849 O O     . PHE B 1 79  ? -7.044  -15.744 -2.358  1.00 25.77 ? 102 PHE B O     1 
ATOM   1850 C CB    . PHE B 1 79  ? -9.342  -15.889 -0.142  1.00 23.85 ? 102 PHE B CB    1 
ATOM   1851 C CG    . PHE B 1 79  ? -10.718 -15.730 0.437   1.00 23.06 ? 102 PHE B CG    1 
ATOM   1852 C CD1   . PHE B 1 79  ? -11.045 -14.609 1.196   1.00 21.69 ? 102 PHE B CD1   1 
ATOM   1853 C CD2   . PHE B 1 79  ? -11.684 -16.705 0.235   1.00 23.26 ? 102 PHE B CD2   1 
ATOM   1854 C CE1   . PHE B 1 79  ? -12.313 -14.467 1.739   1.00 23.61 ? 102 PHE B CE1   1 
ATOM   1855 C CE2   . PHE B 1 79  ? -12.956 -16.574 0.773   1.00 20.63 ? 102 PHE B CE2   1 
ATOM   1856 C CZ    . PHE B 1 79  ? -13.279 -15.456 1.522   1.00 24.35 ? 102 PHE B CZ    1 
ATOM   1857 N N     . VAL B 1 80  ? -6.810  -13.982 -0.966  1.00 24.38 ? 103 VAL B N     1 
ATOM   1858 C CA    . VAL B 1 80  ? -5.355  -13.875 -1.057  1.00 20.92 ? 103 VAL B CA    1 
ATOM   1859 C C     . VAL B 1 80  ? -4.797  -13.791 0.357   1.00 25.75 ? 103 VAL B C     1 
ATOM   1860 O O     . VAL B 1 80  ? -5.218  -12.931 1.139   1.00 24.01 ? 103 VAL B O     1 
ATOM   1861 C CB    . VAL B 1 80  ? -4.919  -12.637 -1.873  1.00 25.64 ? 103 VAL B CB    1 
ATOM   1862 C CG1   . VAL B 1 80  ? -3.393  -12.529 -1.912  1.00 25.41 ? 103 VAL B CG1   1 
ATOM   1863 C CG2   . VAL B 1 80  ? -5.468  -12.699 -3.273  1.00 22.31 ? 103 VAL B CG2   1 
ATOM   1864 N N     . ASN B 1 81  ? -3.853  -14.671 0.692   1.00 23.66 ? 104 ASN B N     1 
ATOM   1865 C CA    . ASN B 1 81  ? -3.216  -14.655 2.013   1.00 25.00 ? 104 ASN B CA    1 
ATOM   1866 C C     . ASN B 1 81  ? -1.988  -13.742 1.928   1.00 28.35 ? 104 ASN B C     1 
ATOM   1867 O O     . ASN B 1 81  ? -0.952  -14.132 1.382   1.00 30.93 ? 104 ASN B O     1 
ATOM   1868 C CB    . ASN B 1 81  ? -2.867  -16.081 2.437   1.00 28.50 ? 104 ASN B CB    1 
ATOM   1869 C CG    . ASN B 1 81  ? -2.278  -16.175 3.862   1.00 31.04 ? 104 ASN B CG    1 
ATOM   1870 O OD1   . ASN B 1 81  ? -1.568  -17.128 4.179   1.00 29.52 ? 104 ASN B OD1   1 
ATOM   1871 N ND2   . ASN B 1 81  ? -2.592  -15.213 4.714   1.00 25.25 ? 104 ASN B ND2   1 
ATOM   1872 N N     . GLY B 1 82  ? -2.099  -12.521 2.449   1.00 28.89 ? 105 GLY B N     1 
ATOM   1873 C CA    . GLY B 1 82  ? -1.040  -11.540 2.250   1.00 28.32 ? 105 GLY B CA    1 
ATOM   1874 C C     . GLY B 1 82  ? -1.303  -10.228 2.969   1.00 27.68 ? 105 GLY B C     1 
ATOM   1875 O O     . GLY B 1 82  ? -2.267  -10.082 3.724   1.00 25.78 ? 105 GLY B O     1 
ATOM   1876 N N     . ASP B 1 83  ? -0.416  -9.265  2.706   1.00 26.74 ? 106 ASP B N     1 
ATOM   1877 C CA    . ASP B 1 83  ? -0.407  -7.956  3.356   1.00 28.98 ? 106 ASP B CA    1 
ATOM   1878 C C     . ASP B 1 83  ? -1.119  -6.951  2.453   1.00 25.79 ? 106 ASP B C     1 
ATOM   1879 O O     . ASP B 1 83  ? -0.729  -6.777  1.294   1.00 27.04 ? 106 ASP B O     1 
ATOM   1880 C CB    . ASP B 1 83  ? 1.039   -7.515  3.617   1.00 31.07 ? 106 ASP B CB    1 
ATOM   1881 C CG    . ASP B 1 83  ? 1.145   -6.294  4.524   1.00 34.38 ? 106 ASP B CG    1 
ATOM   1882 O OD1   . ASP B 1 83  ? 0.117   -5.643  4.811   1.00 32.99 ? 106 ASP B OD1   1 
ATOM   1883 O OD2   . ASP B 1 83  ? 2.283   -5.984  4.950   1.00 37.73 ? 106 ASP B OD2   1 
ATOM   1884 N N     . ALA B 1 84  ? -2.167  -6.300  2.975   1.00 25.60 ? 107 ALA B N     1 
ATOM   1885 C CA    . ALA B 1 84  ? -2.887  -5.319  2.161   1.00 28.49 ? 107 ALA B CA    1 
ATOM   1886 C C     . ALA B 1 84  ? -2.035  -4.099  1.820   1.00 29.08 ? 107 ALA B C     1 
ATOM   1887 O O     . ALA B 1 84  ? -2.321  -3.410  0.834   1.00 28.72 ? 107 ALA B O     1 
ATOM   1888 C CB    . ALA B 1 84  ? -4.167  -4.873  2.870   1.00 30.56 ? 107 ALA B CB    1 
ATOM   1889 N N     . PHE B 1 85  ? -0.998  -3.806  2.607   1.00 30.20 ? 108 PHE B N     1 
ATOM   1890 C CA    . PHE B 1 85  ? -0.150  -2.662  2.281   1.00 30.37 ? 108 PHE B CA    1 
ATOM   1891 C C     . PHE B 1 85  ? 0.736   -2.924  1.073   1.00 29.81 ? 108 PHE B C     1 
ATOM   1892 O O     . PHE B 1 85  ? 1.238   -1.969  0.470   1.00 30.85 ? 108 PHE B O     1 
ATOM   1893 C CB    . PHE B 1 85  ? 0.693   -2.272  3.497   1.00 25.83 ? 108 PHE B CB    1 
ATOM   1894 C CG    . PHE B 1 85  ? -0.091  -1.529  4.547   1.00 28.72 ? 108 PHE B CG    1 
ATOM   1895 C CD1   . PHE B 1 85  ? -0.880  -2.214  5.455   1.00 31.95 ? 108 PHE B CD1   1 
ATOM   1896 C CD2   . PHE B 1 85  ? -0.059  -0.147  4.604   1.00 26.09 ? 108 PHE B CD2   1 
ATOM   1897 C CE1   . PHE B 1 85  ? -1.615  -1.530  6.417   1.00 30.60 ? 108 PHE B CE1   1 
ATOM   1898 C CE2   . PHE B 1 85  ? -0.788  0.549   5.568   1.00 25.28 ? 108 PHE B CE2   1 
ATOM   1899 C CZ    . PHE B 1 85  ? -1.570  -0.140  6.470   1.00 32.16 ? 108 PHE B CZ    1 
ATOM   1900 N N     . ASP B 1 86  ? 0.910   -4.185  0.690   1.00 28.30 ? 109 ASP B N     1 
ATOM   1901 C CA    . ASP B 1 86  ? 1.704   -4.587  -0.473  1.00 29.40 ? 109 ASP B CA    1 
ATOM   1902 C C     . ASP B 1 86  ? 0.750   -4.973  -1.600  1.00 31.86 ? 109 ASP B C     1 
ATOM   1903 O O     . ASP B 1 86  ? 0.544   -6.152  -1.888  1.00 31.00 ? 109 ASP B O     1 
ATOM   1904 C CB    . ASP B 1 86  ? 2.616   -5.746  -0.083  1.00 29.17 ? 109 ASP B CB    1 
ATOM   1905 C CG    . ASP B 1 86  ? 3.762   -5.970  -1.057  1.00 36.56 ? 109 ASP B CG    1 
ATOM   1906 O OD1   . ASP B 1 86  ? 3.750   -5.407  -2.182  1.00 36.00 ? 109 ASP B OD1   1 
ATOM   1907 O OD2   . ASP B 1 86  ? 4.687   -6.723  -0.670  1.00 31.38 ? 109 ASP B OD2   1 
ATOM   1908 N N     . LEU B 1 87  ? 0.157   -3.964  -2.244  1.00 30.89 ? 110 LEU B N     1 
ATOM   1909 C CA    . LEU B 1 87  ? -0.834  -4.251  -3.278  1.00 29.27 ? 110 LEU B CA    1 
ATOM   1910 C C     . LEU B 1 87  ? -0.203  -4.933  -4.483  1.00 34.09 ? 110 LEU B C     1 
ATOM   1911 O O     . LEU B 1 87  ? -0.861  -5.735  -5.157  1.00 30.84 ? 110 LEU B O     1 
ATOM   1912 C CB    . LEU B 1 87  ? -1.560  -2.969  -3.709  1.00 30.76 ? 110 LEU B CB    1 
ATOM   1913 C CG    . LEU B 1 87  ? -2.610  -2.404  -2.739  1.00 25.75 ? 110 LEU B CG    1 
ATOM   1914 C CD1   . LEU B 1 87  ? -3.275  -1.152  -3.317  1.00 31.19 ? 110 LEU B CD1   1 
ATOM   1915 C CD2   . LEU B 1 87  ? -3.662  -3.466  -2.344  1.00 27.12 ? 110 LEU B CD2   1 
ATOM   1916 N N     . ASP B 1 88  ? 1.066   -4.638  -4.762  1.00 35.33 ? 111 ASP B N     1 
ATOM   1917 C CA    . ASP B 1 88  ? 1.732   -5.263  -5.900  1.00 35.08 ? 111 ASP B CA    1 
ATOM   1918 C C     . ASP B 1 88  ? 1.879   -6.767  -5.700  1.00 37.37 ? 111 ASP B C     1 
ATOM   1919 O O     . ASP B 1 88  ? 1.680   -7.545  -6.638  1.00 37.24 ? 111 ASP B O     1 
ATOM   1920 C CB    . ASP B 1 88  ? 3.091   -4.605  -6.130  1.00 38.81 ? 111 ASP B CB    1 
ATOM   1921 C CG    . ASP B 1 88  ? 2.966   -3.235  -6.774  1.00 47.94 ? 111 ASP B CG    1 
ATOM   1922 O OD1   . ASP B 1 88  ? 1.940   -2.989  -7.453  1.00 46.46 ? 111 ASP B OD1   1 
ATOM   1923 O OD2   . ASP B 1 88  ? 3.877   -2.400  -6.583  1.00 58.23 ? 111 ASP B OD2   1 
ATOM   1924 N N     . ALA B 1 89  ? 2.198   -7.198  -4.481  1.00 33.77 ? 112 ALA B N     1 
ATOM   1925 C CA    . ALA B 1 89  ? 2.316   -8.627  -4.224  1.00 37.47 ? 112 ALA B CA    1 
ATOM   1926 C C     . ALA B 1 89  ? 0.953   -9.310  -4.196  1.00 38.43 ? 112 ALA B C     1 
ATOM   1927 O O     . ALA B 1 89  ? 0.832   -10.464 -4.618  1.00 37.67 ? 112 ALA B O     1 
ATOM   1928 C CB    . ALA B 1 89  ? 3.058   -8.875  -2.910  1.00 38.16 ? 112 ALA B CB    1 
ATOM   1929 N N     . THR B 1 90  ? -0.086  -8.637  -3.691  1.00 35.06 ? 113 THR B N     1 
ATOM   1930 C CA    . THR B 1 90  ? -1.348  -9.348  -3.486  1.00 33.55 ? 113 THR B CA    1 
ATOM   1931 C C     . THR B 1 90  ? -2.307  -9.239  -4.658  1.00 32.54 ? 113 THR B C     1 
ATOM   1932 O O     . THR B 1 90  ? -3.086  -10.168 -4.883  1.00 38.29 ? 113 THR B O     1 
ATOM   1933 C CB    . THR B 1 90  ? -2.061  -8.867  -2.219  1.00 31.81 ? 113 THR B CB    1 
ATOM   1934 O OG1   . THR B 1 90  ? -2.217  -7.439  -2.252  1.00 32.28 ? 113 THR B OG1   1 
ATOM   1935 C CG2   . THR B 1 90  ? -1.275  -9.286  -0.984  1.00 31.74 ? 113 THR B CG2   1 
ATOM   1936 N N     . LEU B 1 91  ? -2.290  -8.128  -5.394  1.00 34.19 ? 114 LEU B N     1 
ATOM   1937 C CA    . LEU B 1 91  ? -3.138  -7.948  -6.564  1.00 35.21 ? 114 LEU B CA    1 
ATOM   1938 C C     . LEU B 1 91  ? -2.383  -8.032  -7.879  1.00 42.25 ? 114 LEU B C     1 
ATOM   1939 O O     . LEU B 1 91  ? -3.020  -8.202  -8.924  1.00 41.14 ? 114 LEU B O     1 
ATOM   1940 C CB    . LEU B 1 91  ? -3.845  -6.581  -6.529  1.00 34.58 ? 114 LEU B CB    1 
ATOM   1941 C CG    . LEU B 1 91  ? -4.681  -6.156  -5.321  1.00 35.48 ? 114 LEU B CG    1 
ATOM   1942 C CD1   . LEU B 1 91  ? -5.258  -4.757  -5.522  1.00 30.01 ? 114 LEU B CD1   1 
ATOM   1943 C CD2   . LEU B 1 91  ? -5.773  -7.172  -5.079  1.00 31.92 ? 114 LEU B CD2   1 
ATOM   1944 N N     . GLY B 1 92  ? -1.059  -7.891  -7.859  1.00 41.22 ? 115 GLY B N     1 
ATOM   1945 C CA    . GLY B 1 92  ? -0.291  -7.683  -9.067  1.00 37.04 ? 115 GLY B CA    1 
ATOM   1946 C C     . GLY B 1 92  ? -0.090  -6.206  -9.369  1.00 47.38 ? 115 GLY B C     1 
ATOM   1947 O O     . GLY B 1 92  ? -0.687  -5.311  -8.756  1.00 46.71 ? 115 GLY B O     1 
ATOM   1948 N N     . GLU B 1 93  ? 0.781   -5.950  -10.341 1.00 48.06 ? 116 GLU B N     1 
ATOM   1949 C CA    . GLU B 1 93  ? 1.032   -4.581  -10.769 1.00 56.90 ? 116 GLU B CA    1 
ATOM   1950 C C     . GLU B 1 93  ? -0.223  -3.993  -11.409 1.00 55.75 ? 116 GLU B C     1 
ATOM   1951 O O     . GLU B 1 93  ? -0.936  -4.675  -12.157 1.00 54.18 ? 116 GLU B O     1 
ATOM   1952 C CB    . GLU B 1 93  ? 2.207   -4.538  -11.749 1.00 60.10 ? 116 GLU B CB    1 
ATOM   1953 C CG    . GLU B 1 93  ? 2.143   -3.391  -12.750 1.00 65.27 ? 116 GLU B CG    1 
ATOM   1954 C CD    . GLU B 1 93  ? 3.435   -3.216  -13.521 1.00 70.18 ? 116 GLU B CD    1 
ATOM   1955 O OE1   . GLU B 1 93  ? 3.401   -3.305  -14.772 1.00 69.44 ? 116 GLU B OE1   1 
ATOM   1956 O OE2   . GLU B 1 93  ? 4.481   -2.989  -12.871 1.00 78.51 ? 116 GLU B OE2   1 
ATOM   1957 N N     . HIS B 1 94  ? -0.503  -2.726  -11.095 1.00 51.48 ? 117 HIS B N     1 
ATOM   1958 C CA    . HIS B 1 94  ? -1.691  -2.066  -11.630 1.00 52.00 ? 117 HIS B CA    1 
ATOM   1959 C C     . HIS B 1 94  ? -1.502  -1.813  -13.123 1.00 53.38 ? 117 HIS B C     1 
ATOM   1960 O O     . HIS B 1 94  ? -0.636  -1.030  -13.533 1.00 55.93 ? 117 HIS B O     1 
ATOM   1961 C CB    . HIS B 1 94  ? -1.975  -0.763  -10.887 1.00 48.68 ? 117 HIS B CB    1 
ATOM   1962 C CG    . HIS B 1 94  ? -3.343  -0.206  -11.153 1.00 45.31 ? 117 HIS B CG    1 
ATOM   1963 N ND1   . HIS B 1 94  ? -3.600  1.148   -11.223 1.00 45.66 ? 117 HIS B ND1   1 
ATOM   1964 C CD2   . HIS B 1 94  ? -4.529  -0.825  -11.370 1.00 42.52 ? 117 HIS B CD2   1 
ATOM   1965 C CE1   . HIS B 1 94  ? -4.884  1.340   -11.474 1.00 42.24 ? 117 HIS B CE1   1 
ATOM   1966 N NE2   . HIS B 1 94  ? -5.471  0.158   -11.568 1.00 46.22 ? 117 HIS B NE2   1 
ATOM   1967 N N     . LYS B 1 95  ? -2.291  -2.503  -13.938 1.00 50.44 ? 118 LYS B N     1 
ATOM   1968 C CA    . LYS B 1 95  ? -2.391  -2.219  -15.362 1.00 49.60 ? 118 LYS B CA    1 
ATOM   1969 C C     . LYS B 1 95  ? -3.821  -1.826  -15.716 1.00 44.28 ? 118 LYS B C     1 
ATOM   1970 O O     . LYS B 1 95  ? -4.273  -2.035  -16.843 1.00 43.59 ? 118 LYS B O     1 
ATOM   1971 C CB    . LYS B 1 95  ? -1.924  -3.413  -16.196 1.00 52.59 ? 118 LYS B CB    1 
ATOM   1972 C CG    . LYS B 1 95  ? -0.911  -4.286  -15.485 1.00 57.71 ? 118 LYS B CG    1 
ATOM   1973 C CD    . LYS B 1 95  ? 0.005   -4.993  -16.468 1.00 62.68 ? 118 LYS B CD    1 
ATOM   1974 C CE    . LYS B 1 95  ? 0.680   -6.188  -15.814 1.00 65.47 ? 118 LYS B CE    1 
ATOM   1975 N NZ    . LYS B 1 95  ? 2.054   -6.403  -16.339 1.00 66.27 ? 118 LYS B NZ    1 
ATOM   1976 N N     . GLY B 1 96  ? -4.538  -1.261  -14.744 1.00 43.82 ? 119 GLY B N     1 
ATOM   1977 C CA    . GLY B 1 96  ? -5.848  -0.691  -14.970 1.00 38.35 ? 119 GLY B CA    1 
ATOM   1978 C C     . GLY B 1 96  ? -7.019  -1.404  -14.318 1.00 39.64 ? 119 GLY B C     1 
ATOM   1979 O O     . GLY B 1 96  ? -8.168  -1.024  -14.584 1.00 36.37 ? 119 GLY B O     1 
ATOM   1980 N N     . GLN B 1 97  ? -6.777  -2.425  -13.489 1.00 40.41 ? 120 GLN B N     1 
ATOM   1981 C CA    . GLN B 1 97  ? -7.877  -3.109  -12.820 1.00 37.84 ? 120 GLN B CA    1 
ATOM   1982 C C     . GLN B 1 97  ? -8.640  -2.138  -11.922 1.00 34.98 ? 120 GLN B C     1 
ATOM   1983 O O     . GLN B 1 97  ? -8.052  -1.325  -11.195 1.00 35.31 ? 120 GLN B O     1 
ATOM   1984 C CB    . GLN B 1 97  ? -7.365  -4.304  -12.010 1.00 41.18 ? 120 GLN B CB    1 
ATOM   1985 C CG    . GLN B 1 97  ? -6.827  -3.966  -10.618 1.00 47.15 ? 120 GLN B CG    1 
ATOM   1986 C CD    . GLN B 1 97  ? -6.452  -5.205  -9.808  1.00 50.69 ? 120 GLN B CD    1 
ATOM   1987 O OE1   . GLN B 1 97  ? -5.567  -5.153  -8.950  1.00 55.72 ? 120 GLN B OE1   1 
ATOM   1988 N NE2   . GLN B 1 97  ? -7.123  -6.322  -10.079 1.00 43.01 ? 120 GLN B NE2   1 
ATOM   1989 N N     . MET B 1 98  ? -9.962  -2.200  -12.015 1.00 29.13 ? 121 MET B N     1 
ATOM   1990 C CA    . MET B 1 98  ? -10.851 -1.279  -11.323 1.00 28.60 ? 121 MET B CA    1 
ATOM   1991 C C     . MET B 1 98  ? -11.825 -2.062  -10.448 1.00 27.16 ? 121 MET B C     1 
ATOM   1992 O O     . MET B 1 98  ? -12.471 -3.002  -10.919 1.00 25.31 ? 121 MET B O     1 
ATOM   1993 C CB    . MET B 1 98  ? -11.630 -0.422  -12.327 1.00 26.77 ? 121 MET B CB    1 
ATOM   1994 C CG    . MET B 1 98  ? -10.840 0.702   -12.961 1.00 30.44 ? 121 MET B CG    1 
ATOM   1995 S SD    . MET B 1 98  ? -10.513 2.034   -11.779 1.00 36.30 ? 121 MET B SD    1 
ATOM   1996 C CE    . MET B 1 98  ? -10.031 3.341   -12.911 1.00 30.51 ? 121 MET B CE    1 
ATOM   1997 N N     . PHE B 1 99  ? -11.951 -1.657  -9.191  1.00 22.68 ? 122 PHE B N     1 
ATOM   1998 C CA    . PHE B 1 99  ? -12.951 -2.215  -8.305  1.00 18.81 ? 122 PHE B CA    1 
ATOM   1999 C C     . PHE B 1 99  ? -14.122 -1.249  -8.169  1.00 21.71 ? 122 PHE B C     1 
ATOM   2000 O O     . PHE B 1 99  ? -13.960 -0.029  -8.264  1.00 21.98 ? 122 PHE B O     1 
ATOM   2001 C CB    . PHE B 1 99  ? -12.345 -2.527  -6.930  1.00 18.92 ? 122 PHE B CB    1 
ATOM   2002 C CG    . PHE B 1 99  ? -11.263 -3.574  -6.978  1.00 25.56 ? 122 PHE B CG    1 
ATOM   2003 C CD1   . PHE B 1 99  ? -11.585 -4.926  -6.917  1.00 20.48 ? 122 PHE B CD1   1 
ATOM   2004 C CD2   . PHE B 1 99  ? -9.923  -3.208  -7.111  1.00 22.17 ? 122 PHE B CD2   1 
ATOM   2005 C CE1   . PHE B 1 99  ? -10.588 -5.903  -6.969  1.00 23.81 ? 122 PHE B CE1   1 
ATOM   2006 C CE2   . PHE B 1 99  ? -8.923  -4.173  -7.162  1.00 28.36 ? 122 PHE B CE2   1 
ATOM   2007 C CZ    . PHE B 1 99  ? -9.255  -5.528  -7.092  1.00 26.41 ? 122 PHE B CZ    1 
ATOM   2008 N N     . ASP B 1 100 ? -15.308 -1.810  -7.941  1.00 20.88 ? 123 ASP B N     1 
ATOM   2009 C CA    . ASP B 1 100 ? -16.488 -0.980  -7.704  1.00 22.46 ? 123 ASP B CA    1 
ATOM   2010 C C     . ASP B 1 100 ? -16.317 -0.113  -6.463  1.00 23.91 ? 123 ASP B C     1 
ATOM   2011 O O     . ASP B 1 100 ? -16.778 1.029   -6.423  1.00 21.30 ? 123 ASP B O     1 
ATOM   2012 C CB    . ASP B 1 100 ? -17.723 -1.864  -7.553  1.00 22.60 ? 123 ASP B CB    1 
ATOM   2013 C CG    . ASP B 1 100 ? -18.964 -1.072  -7.216  1.00 24.76 ? 123 ASP B CG    1 
ATOM   2014 O OD1   . ASP B 1 100 ? -19.546 -0.487  -8.159  1.00 26.34 ? 123 ASP B OD1   1 
ATOM   2015 O OD2   . ASP B 1 100 ? -19.345 -1.024  -6.016  1.00 24.04 ? 123 ASP B OD2   1 
ATOM   2016 N N     . SER B 1 101 ? -15.658 -0.646  -5.440  1.00 22.86 ? 124 SER B N     1 
ATOM   2017 C CA    . SER B 1 101 ? -15.515 -0.024  -4.135  1.00 19.70 ? 124 SER B CA    1 
ATOM   2018 C C     . SER B 1 101 ? -14.592 -0.921  -3.337  1.00 24.50 ? 124 SER B C     1 
ATOM   2019 O O     . SER B 1 101 ? -14.329 -2.066  -3.729  1.00 20.48 ? 124 SER B O     1 
ATOM   2020 C CB    . SER B 1 101 ? -16.867 0.150   -3.401  1.00 24.34 ? 124 SER B CB    1 
ATOM   2021 O OG    . SER B 1 101 ? -17.700 -0.975  -3.569  1.00 22.02 ? 124 SER B OG    1 
ATOM   2022 N N     . VAL B 1 102 ? -14.091 -0.387  -2.224  1.00 18.87 ? 125 VAL B N     1 
ATOM   2023 C CA    . VAL B 1 102 ? -13.178 -1.101  -1.344  1.00 20.85 ? 125 VAL B CA    1 
ATOM   2024 C C     . VAL B 1 102 ? -13.753 -1.064  0.062   1.00 17.15 ? 125 VAL B C     1 
ATOM   2025 O O     . VAL B 1 102 ? -14.096 0.014   0.568   1.00 17.97 ? 125 VAL B O     1 
ATOM   2026 C CB    . VAL B 1 102 ? -11.760 -0.488  -1.361  1.00 22.59 ? 125 VAL B CB    1 
ATOM   2027 C CG1   . VAL B 1 102 ? -10.808 -1.324  -0.488  1.00 18.70 ? 125 VAL B CG1   1 
ATOM   2028 C CG2   . VAL B 1 102 ? -11.224 -0.377  -2.789  1.00 18.78 ? 125 VAL B CG2   1 
ATOM   2029 N N     . ILE B 1 103 ? -13.850 -2.238  0.697   1.00 16.35 ? 126 ILE B N     1 
ATOM   2030 C CA    . ILE B 1 103 ? -14.409 -2.387  2.042   1.00 17.81 ? 126 ILE B CA    1 
ATOM   2031 C C     . ILE B 1 103 ? -13.269 -2.852  2.941   1.00 21.29 ? 126 ILE B C     1 
ATOM   2032 O O     . ILE B 1 103 ? -12.813 -3.991  2.820   1.00 21.19 ? 126 ILE B O     1 
ATOM   2033 C CB    . ILE B 1 103 ? -15.569 -3.397  2.082   1.00 22.35 ? 126 ILE B CB    1 
ATOM   2034 C CG1   . ILE B 1 103 ? -16.512 -3.230  0.887   1.00 25.99 ? 126 ILE B CG1   1 
ATOM   2035 C CG2   . ILE B 1 103 ? -16.352 -3.269  3.382   1.00 23.85 ? 126 ILE B CG2   1 
ATOM   2036 C CD1   . ILE B 1 103 ? -17.152 -1.837  0.789   1.00 23.04 ? 126 ILE B CD1   1 
ATOM   2037 N N     . SER B 1 104 ? -12.806 -2.004  3.854   1.00 24.00 ? 127 SER B N     1 
ATOM   2038 C CA    . SER B 1 104 ? -11.567 -2.271  4.568   1.00 20.38 ? 127 SER B CA    1 
ATOM   2039 C C     . SER B 1 104 ? -11.797 -2.391  6.067   1.00 24.70 ? 127 SER B C     1 
ATOM   2040 O O     . SER B 1 104 ? -12.360 -1.482  6.690   1.00 23.47 ? 127 SER B O     1 
ATOM   2041 C CB    . SER B 1 104 ? -10.533 -1.172  4.305   1.00 21.96 ? 127 SER B CB    1 
ATOM   2042 O OG    . SER B 1 104 ? -9.422  -1.336  5.179   1.00 24.66 ? 127 SER B OG    1 
ATOM   2043 N N     . ALA B 1 105 ? -11.322 -3.497  6.656   1.00 22.99 ? 128 ALA B N     1 
ATOM   2044 C CA    . ALA B 1 105 ? -11.230 -3.605  8.109   1.00 23.75 ? 128 ALA B CA    1 
ATOM   2045 C C     . ALA B 1 105 ? -9.792  -3.771  8.600   1.00 27.42 ? 128 ALA B C     1 
ATOM   2046 O O     . ALA B 1 105 ? -9.583  -4.275  9.708   1.00 30.32 ? 128 ALA B O     1 
ATOM   2047 C CB    . ALA B 1 105 ? -12.089 -4.757  8.631   1.00 23.28 ? 128 ALA B CB    1 
ATOM   2048 N N     . VAL B 1 106 ? -8.793  -3.372  7.819   1.00 25.97 ? 129 VAL B N     1 
ATOM   2049 C CA    . VAL B 1 106 ? -7.421  -3.519  8.326   1.00 29.25 ? 129 VAL B CA    1 
ATOM   2050 C C     . VAL B 1 106 ? -7.223  -2.585  9.514   1.00 28.72 ? 129 VAL B C     1 
ATOM   2051 O O     . VAL B 1 106 ? -7.744  -1.451  9.503   1.00 25.68 ? 129 VAL B O     1 
ATOM   2052 C CB    . VAL B 1 106 ? -6.400  -3.245  7.223   1.00 32.23 ? 129 VAL B CB    1 
ATOM   2053 C CG1   . VAL B 1 106 ? -6.497  -4.330  6.155   1.00 34.13 ? 129 VAL B CG1   1 
ATOM   2054 C CG2   . VAL B 1 106 ? -6.612  -1.898  6.634   1.00 30.80 ? 129 VAL B CG2   1 
ATOM   2055 N N     . PRO B 1 107 ? -6.553  -3.029  10.580  1.00 29.83 ? 130 PRO B N     1 
ATOM   2056 C CA    . PRO B 1 107 ? -6.498  -2.221  11.811  1.00 29.76 ? 130 PRO B CA    1 
ATOM   2057 C C     . PRO B 1 107 ? -5.559  -1.030  11.671  1.00 30.29 ? 130 PRO B C     1 
ATOM   2058 O O     . PRO B 1 107 ? -4.360  -1.122  11.952  1.00 31.06 ? 130 PRO B O     1 
ATOM   2059 C CB    . PRO B 1 107 ? -6.013  -3.222  12.865  1.00 27.57 ? 130 PRO B CB    1 
ATOM   2060 C CG    . PRO B 1 107 ? -5.225  -4.256  12.060  1.00 30.34 ? 130 PRO B CG    1 
ATOM   2061 C CD    . PRO B 1 107 ? -5.915  -4.352  10.734  1.00 30.60 ? 130 PRO B CD    1 
ATOM   2062 N N     . MET B 1 108 ? -6.119  0.102   11.242  1.00 27.73 ? 131 MET B N     1 
ATOM   2063 C CA    . MET B 1 108 ? -5.311  1.240   10.811  1.00 30.19 ? 131 MET B CA    1 
ATOM   2064 C C     . MET B 1 108 ? -4.347  1.716   11.896  1.00 29.47 ? 131 MET B C     1 
ATOM   2065 O O     . MET B 1 108 ? -3.252  2.189   11.581  1.00 29.24 ? 131 MET B O     1 
ATOM   2066 C CB    . MET B 1 108 ? -6.233  2.383   10.371  1.00 32.17 ? 131 MET B CB    1 
ATOM   2067 C CG    . MET B 1 108 ? -6.760  2.233   8.938   1.00 28.74 ? 131 MET B CG    1 
ATOM   2068 S SD    . MET B 1 108 ? -5.399  2.178   7.748   1.00 41.30 ? 131 MET B SD    1 
ATOM   2069 C CE    . MET B 1 108 ? -6.236  2.068   6.176   1.00 34.29 ? 131 MET B CE    1 
ATOM   2070 N N     . LEU B 1 109 ? -4.722  1.585   13.170  1.00 32.70 ? 132 LEU B N     1 
ATOM   2071 C CA    . LEU B 1 109 ? -3.898  2.081   14.268  1.00 33.87 ? 132 LEU B CA    1 
ATOM   2072 C C     . LEU B 1 109 ? -2.603  1.297   14.452  1.00 35.04 ? 132 LEU B C     1 
ATOM   2073 O O     . LEU B 1 109 ? -1.725  1.750   15.199  1.00 30.40 ? 132 LEU B O     1 
ATOM   2074 C CB    . LEU B 1 109 ? -4.683  2.043   15.575  1.00 36.46 ? 132 LEU B CB    1 
ATOM   2075 C CG    . LEU B 1 109 ? -5.872  2.977   15.794  1.00 42.56 ? 132 LEU B CG    1 
ATOM   2076 C CD1   . LEU B 1 109 ? -6.247  2.953   17.281  1.00 49.64 ? 132 LEU B CD1   1 
ATOM   2077 C CD2   . LEU B 1 109 ? -5.613  4.395   15.324  1.00 39.86 ? 132 LEU B CD2   1 
ATOM   2078 N N     . ASN B 1 110 ? -2.464  0.136   13.819  1.00 28.61 ? 133 ASN B N     1 
ATOM   2079 C CA    . ASN B 1 110 ? -1.239  -0.632  13.950  1.00 24.20 ? 133 ASN B CA    1 
ATOM   2080 C C     . ASN B 1 110 ? -0.155  -0.171  12.986  1.00 29.34 ? 133 ASN B C     1 
ATOM   2081 O O     . ASN B 1 110 ? 0.938   -0.756  12.985  1.00 25.94 ? 133 ASN B O     1 
ATOM   2082 C CB    . ASN B 1 110 ? -1.531  -2.120  13.736  1.00 30.35 ? 133 ASN B CB    1 
ATOM   2083 C CG    . ASN B 1 110 ? -2.420  -2.699  14.827  1.00 39.87 ? 133 ASN B CG    1 
ATOM   2084 O OD1   . ASN B 1 110 ? -2.544  -2.127  15.914  1.00 47.45 ? 133 ASN B OD1   1 
ATOM   2085 N ND2   . ASN B 1 110 ? -3.044  -3.834  14.543  1.00 38.59 ? 133 ASN B ND2   1 
ATOM   2086 N N     . PHE B 1 111 ? -0.421  0.860   12.183  1.00 26.71 ? 134 PHE B N     1 
ATOM   2087 C CA    . PHE B 1 111 ? 0.512   1.291   11.155  1.00 24.47 ? 134 PHE B CA    1 
ATOM   2088 C C     . PHE B 1 111 ? 0.741   2.794   11.253  1.00 27.29 ? 134 PHE B C     1 
ATOM   2089 O O     . PHE B 1 111 ? -0.165  3.541   11.648  1.00 21.71 ? 134 PHE B O     1 
ATOM   2090 C CB    . PHE B 1 111 ? -0.017  0.928   9.759   1.00 24.57 ? 134 PHE B CB    1 
ATOM   2091 C CG    . PHE B 1 111 ? -0.441  -0.515  9.635   1.00 29.08 ? 134 PHE B CG    1 
ATOM   2092 C CD1   . PHE B 1 111 ? 0.487   -1.502  9.328   1.00 34.90 ? 134 PHE B CD1   1 
ATOM   2093 C CD2   . PHE B 1 111 ? -1.759  -0.886  9.850   1.00 29.56 ? 134 PHE B CD2   1 
ATOM   2094 C CE1   . PHE B 1 111 ? 0.106   -2.836  9.231   1.00 34.68 ? 134 PHE B CE1   1 
ATOM   2095 C CE2   . PHE B 1 111 ? -2.146  -2.214  9.749   1.00 34.17 ? 134 PHE B CE2   1 
ATOM   2096 C CZ    . PHE B 1 111 ? -1.212  -3.191  9.445   1.00 32.41 ? 134 PHE B CZ    1 
ATOM   2097 N N     . PRO B 1 112 ? 1.953   3.262   10.931  1.00 23.08 ? 135 PRO B N     1 
ATOM   2098 C CA    . PRO B 1 112 ? 2.214   4.711   10.949  1.00 26.22 ? 135 PRO B CA    1 
ATOM   2099 C C     . PRO B 1 112 ? 1.285   5.461   10.004  1.00 24.27 ? 135 PRO B C     1 
ATOM   2100 O O     . PRO B 1 112 ? 0.898   4.953   8.950   1.00 22.31 ? 135 PRO B O     1 
ATOM   2101 C CB    . PRO B 1 112 ? 3.672   4.824   10.491  1.00 22.78 ? 135 PRO B CB    1 
ATOM   2102 C CG    . PRO B 1 112 ? 4.270   3.474   10.763  1.00 29.48 ? 135 PRO B CG    1 
ATOM   2103 C CD    . PRO B 1 112 ? 3.151   2.480   10.578  1.00 25.57 ? 135 PRO B CD    1 
ATOM   2104 N N     . MET B 1 113 ? 0.963   6.702   10.386  1.00 20.84 ? 136 MET B N     1 
ATOM   2105 C CA    . MET B 1 113 ? 0.012   7.508   9.623   1.00 22.94 ? 136 MET B CA    1 
ATOM   2106 C C     . MET B 1 113 ? 0.432   7.660   8.161   1.00 24.34 ? 136 MET B C     1 
ATOM   2107 O O     . MET B 1 113 ? -0.410  7.600   7.257   1.00 20.72 ? 136 MET B O     1 
ATOM   2108 C CB    . MET B 1 113 ? -0.151  8.883   10.281  1.00 22.87 ? 136 MET B CB    1 
ATOM   2109 C CG    . MET B 1 113 ? -1.095  9.805   9.541   1.00 22.90 ? 136 MET B CG    1 
ATOM   2110 S SD    . MET B 1 113 ? -2.796  9.154   9.574   1.00 23.90 ? 136 MET B SD    1 
ATOM   2111 C CE    . MET B 1 113 ? -3.239  9.614   11.248  1.00 27.66 ? 136 MET B CE    1 
ATOM   2112 N N     . ALA B 1 114 ? 1.726   7.869   7.906   1.00 22.92 ? 137 ALA B N     1 
ATOM   2113 C CA    . ALA B 1 114 ? 2.178   8.049   6.531   1.00 22.18 ? 137 ALA B CA    1 
ATOM   2114 C C     . ALA B 1 114 ? 1.919   6.810   5.686   1.00 20.56 ? 137 ALA B C     1 
ATOM   2115 O O     . ALA B 1 114 ? 1.688   6.925   4.476   1.00 22.76 ? 137 ALA B O     1 
ATOM   2116 C CB    . ALA B 1 114 ? 3.669   8.401   6.495   1.00 24.94 ? 137 ALA B CB    1 
ATOM   2117 N N     . ALA B 1 115 ? 1.973   5.621   6.289   1.00 18.93 ? 138 ALA B N     1 
ATOM   2118 C CA    . ALA B 1 115 ? 1.678   4.410   5.529   1.00 20.85 ? 138 ALA B CA    1 
ATOM   2119 C C     . ALA B 1 115 ? 0.185   4.301   5.240   1.00 20.91 ? 138 ALA B C     1 
ATOM   2120 O O     . ALA B 1 115 ? -0.213  3.825   4.165   1.00 20.92 ? 138 ALA B O     1 
ATOM   2121 C CB    . ALA B 1 115 ? 2.189   3.176   6.278   1.00 18.84 ? 138 ALA B CB    1 
ATOM   2122 N N     . ARG B 1 116 ? -0.651  4.751   6.184   1.00 19.43 ? 139 ARG B N     1 
ATOM   2123 C CA    . ARG B 1 116 ? -2.105  4.770   5.974   1.00 20.68 ? 139 ARG B CA    1 
ATOM   2124 C C     . ARG B 1 116 ? -2.486  5.673   4.804   1.00 22.17 ? 139 ARG B C     1 
ATOM   2125 O O     . ARG B 1 116 ? -3.329  5.322   3.969   1.00 20.95 ? 139 ARG B O     1 
ATOM   2126 C CB    . ARG B 1 116 ? -2.818  5.264   7.232   1.00 21.24 ? 139 ARG B CB    1 
ATOM   2127 C CG    . ARG B 1 116 ? -2.536  4.501   8.520   1.00 23.17 ? 139 ARG B CG    1 
ATOM   2128 C CD    . ARG B 1 116 ? -3.255  5.182   9.712   1.00 25.48 ? 139 ARG B CD    1 
ATOM   2129 N NE    . ARG B 1 116 ? -2.515  5.005   10.963  1.00 25.66 ? 139 ARG B NE    1 
ATOM   2130 C CZ    . ARG B 1 116 ? -2.803  5.609   12.111  1.00 28.19 ? 139 ARG B CZ    1 
ATOM   2131 N NH1   . ARG B 1 116 ? -3.835  6.434   12.194  1.00 24.48 ? 139 ARG B NH1   1 
ATOM   2132 N NH2   . ARG B 1 116 ? -2.058  5.375   13.186  1.00 29.28 ? 139 ARG B NH2   1 
ATOM   2133 N N     . ILE B 1 117 ? -1.903  6.870   4.760   1.00 23.09 ? 140 ILE B N     1 
ATOM   2134 C CA    . ILE B 1 117 ? -2.173  7.787   3.661   1.00 19.90 ? 140 ILE B CA    1 
ATOM   2135 C C     . ILE B 1 117 ? -1.776  7.156   2.334   1.00 21.50 ? 140 ILE B C     1 
ATOM   2136 O O     . ILE B 1 117 ? -2.540  7.184   1.360   1.00 20.61 ? 140 ILE B O     1 
ATOM   2137 C CB    . ILE B 1 117 ? -1.441  9.120   3.893   1.00 23.51 ? 140 ILE B CB    1 
ATOM   2138 C CG1   . ILE B 1 117 ? -2.013  9.827   5.136   1.00 21.41 ? 140 ILE B CG1   1 
ATOM   2139 C CG2   . ILE B 1 117 ? -1.540  9.994   2.643   1.00 21.17 ? 140 ILE B CG2   1 
ATOM   2140 C CD1   . ILE B 1 117 ? -1.055  10.872  5.709   1.00 25.11 ? 140 ILE B CD1   1 
ATOM   2141 N N     . LYS B 1 118 ? -0.567  6.584   2.267   1.00 20.81 ? 141 LYS B N     1 
ATOM   2142 C CA    . LYS B 1 118 ? -0.113  6.018   1.002   1.00 22.32 ? 141 LYS B CA    1 
ATOM   2143 C C     . LYS B 1 118 ? -1.002  4.853   0.573   1.00 18.96 ? 141 LYS B C     1 
ATOM   2144 O O     . LYS B 1 118 ? -1.326  4.708   -0.609  1.00 21.76 ? 141 LYS B O     1 
ATOM   2145 C CB    . LYS B 1 118 ? 1.349   5.573   1.102   1.00 25.21 ? 141 LYS B CB    1 
ATOM   2146 C CG    . LYS B 1 118 ? 1.892   4.979   -0.222  1.00 22.58 ? 141 LYS B CG    1 
ATOM   2147 C CD    . LYS B 1 118 ? 3.355   4.552   -0.121  1.00 33.56 ? 141 LYS B CD    1 
ATOM   2148 C CE    . LYS B 1 118 ? 3.837   3.810   -1.396  1.00 31.90 ? 141 LYS B CE    1 
ATOM   2149 N NZ    . LYS B 1 118 ? 4.221   4.734   -2.489  1.00 43.68 ? 141 LYS B NZ    1 
ATOM   2150 N N     . LEU B 1 119 ? -1.401  4.010   1.514   1.00 20.27 ? 142 LEU B N     1 
ATOM   2151 C CA    . LEU B 1 119 ? -2.293  2.913   1.166   1.00 20.72 ? 142 LEU B CA    1 
ATOM   2152 C C     . LEU B 1 119 ? -3.625  3.428   0.608   1.00 19.88 ? 142 LEU B C     1 
ATOM   2153 O O     . LEU B 1 119 ? -4.114  2.923   -0.407  1.00 18.42 ? 142 LEU B O     1 
ATOM   2154 C CB    . LEU B 1 119 ? -2.520  2.026   2.384   1.00 23.31 ? 142 LEU B CB    1 
ATOM   2155 C CG    . LEU B 1 119 ? -3.539  0.901   2.108   1.00 24.13 ? 142 LEU B CG    1 
ATOM   2156 C CD1   . LEU B 1 119 ? -3.074  0.005   0.965   1.00 22.68 ? 142 LEU B CD1   1 
ATOM   2157 C CD2   . LEU B 1 119 ? -3.796  0.105   3.370   1.00 27.98 ? 142 LEU B CD2   1 
ATOM   2158 N N     . LEU B 1 120 ? -4.209  4.452   1.237   1.00 18.35 ? 143 LEU B N     1 
ATOM   2159 C CA    . LEU B 1 120 ? -5.478  4.996   0.740   1.00 18.91 ? 143 LEU B CA    1 
ATOM   2160 C C     . LEU B 1 120 ? -5.308  5.607   -0.649  1.00 23.51 ? 143 LEU B C     1 
ATOM   2161 O O     . LEU B 1 120 ? -6.157  5.425   -1.535  1.00 19.73 ? 143 LEU B O     1 
ATOM   2162 C CB    . LEU B 1 120 ? -6.021  6.034   1.730   1.00 21.04 ? 143 LEU B CB    1 
ATOM   2163 C CG    . LEU B 1 120 ? -7.345  6.717   1.355   1.00 26.18 ? 143 LEU B CG    1 
ATOM   2164 C CD1   . LEU B 1 120 ? -8.479  5.694   1.152   1.00 17.95 ? 143 LEU B CD1   1 
ATOM   2165 C CD2   . LEU B 1 120 ? -7.750  7.771   2.395   1.00 22.27 ? 143 LEU B CD2   1 
ATOM   2166 N N     . ASP B 1 121 ? -4.200  6.321   -0.861  1.00 22.13 ? 144 ASP B N     1 
ATOM   2167 C CA    . ASP B 1 121 ? -3.907  6.891   -2.174  1.00 25.13 ? 144 ASP B CA    1 
ATOM   2168 C C     . ASP B 1 121 ? -3.803  5.797   -3.232  1.00 24.33 ? 144 ASP B C     1 
ATOM   2169 O O     . ASP B 1 121 ? -4.302  5.954   -4.350  1.00 25.73 ? 144 ASP B O     1 
ATOM   2170 C CB    . ASP B 1 121 ? -2.614  7.711   -2.079  1.00 23.41 ? 144 ASP B CB    1 
ATOM   2171 C CG    . ASP B 1 121 ? -2.294  8.490   -3.350  1.00 30.88 ? 144 ASP B CG    1 
ATOM   2172 O OD1   . ASP B 1 121 ? -3.216  9.007   -4.007  1.00 31.16 ? 144 ASP B OD1   1 
ATOM   2173 O OD2   . ASP B 1 121 ? -1.097  8.609   -3.681  1.00 32.91 ? 144 ASP B OD2   1 
ATOM   2174 N N     . GLU B 1 122 ? -3.165  4.675   -2.892  1.00 22.13 ? 145 GLU B N     1 
ATOM   2175 C CA    . GLU B 1 122 ? -3.053  3.569   -3.843  1.00 25.34 ? 145 GLU B CA    1 
ATOM   2176 C C     . GLU B 1 122 ? -4.412  2.919   -4.100  1.00 25.07 ? 145 GLU B C     1 
ATOM   2177 O O     . GLU B 1 122 ? -4.747  2.608   -5.252  1.00 21.02 ? 145 GLU B O     1 
ATOM   2178 C CB    . GLU B 1 122 ? -2.054  2.532   -3.331  1.00 27.21 ? 145 GLU B CB    1 
ATOM   2179 C CG    . GLU B 1 122 ? -0.591  2.963   -3.419  1.00 29.68 ? 145 GLU B CG    1 
ATOM   2180 C CD    . GLU B 1 122 ? -0.192  3.360   -4.831  1.00 37.71 ? 145 GLU B CD    1 
ATOM   2181 O OE1   . GLU B 1 122 ? 0.347   4.478   -5.001  1.00 40.68 ? 145 GLU B OE1   1 
ATOM   2182 O OE2   . GLU B 1 122 ? -0.427  2.566   -5.771  1.00 33.90 ? 145 GLU B OE2   1 
ATOM   2183 N N     . LEU B 1 123 ? -5.209  2.709   -3.039  1.00 22.61 ? 146 LEU B N     1 
ATOM   2184 C CA    . LEU B 1 123 ? -6.530  2.096   -3.207  1.00 20.36 ? 146 LEU B CA    1 
ATOM   2185 C C     . LEU B 1 123 ? -7.436  2.961   -4.079  1.00 24.26 ? 146 LEU B C     1 
ATOM   2186 O O     . LEU B 1 123 ? -8.139  2.444   -4.961  1.00 24.02 ? 146 LEU B O     1 
ATOM   2187 C CB    . LEU B 1 123 ? -7.187  1.846   -1.847  1.00 20.60 ? 146 LEU B CB    1 
ATOM   2188 C CG    . LEU B 1 123 ? -6.537  0.819   -0.914  1.00 18.49 ? 146 LEU B CG    1 
ATOM   2189 C CD1   . LEU B 1 123 ? -7.137  0.941   0.491   1.00 16.44 ? 146 LEU B CD1   1 
ATOM   2190 C CD2   . LEU B 1 123 ? -6.699  -0.598  -1.468  1.00 22.20 ? 146 LEU B CD2   1 
ATOM   2191 N N     . LEU B 1 124 ? -7.417  4.285   -3.868  1.00 21.08 ? 147 LEU B N     1 
ATOM   2192 C CA    . LEU B 1 124 ? -8.224  5.184   -4.691  1.00 22.24 ? 147 LEU B CA    1 
ATOM   2193 C C     . LEU B 1 124 ? -7.807  5.198   -6.165  1.00 23.12 ? 147 LEU B C     1 
ATOM   2194 O O     . LEU B 1 124 ? -8.637  5.519   -7.026  1.00 25.09 ? 147 LEU B O     1 
ATOM   2195 C CB    . LEU B 1 124 ? -8.171  6.606   -4.120  1.00 22.79 ? 147 LEU B CB    1 
ATOM   2196 C CG    . LEU B 1 124 ? -8.978  6.759   -2.828  1.00 25.32 ? 147 LEU B CG    1 
ATOM   2197 C CD1   . LEU B 1 124 ? -8.811  8.169   -2.227  1.00 24.80 ? 147 LEU B CD1   1 
ATOM   2198 C CD2   . LEU B 1 124 ? -10.462 6.442   -3.088  1.00 22.23 ? 147 LEU B CD2   1 
ATOM   2199 N N     . LYS B 1 125 ? -6.547  4.891   -6.479  1.00 20.73 ? 148 LYS B N     1 
ATOM   2200 C CA    . LYS B 1 125 ? -6.149  4.722   -7.876  1.00 22.99 ? 148 LYS B CA    1 
ATOM   2201 C C     . LYS B 1 125 ? -6.840  3.536   -8.541  1.00 26.71 ? 148 LYS B C     1 
ATOM   2202 O O     . LYS B 1 125 ? -6.936  3.505   -9.772  1.00 22.65 ? 148 LYS B O     1 
ATOM   2203 C CB    . LYS B 1 125 ? -4.634  4.514   -7.991  1.00 26.48 ? 148 LYS B CB    1 
ATOM   2204 C CG    . LYS B 1 125 ? -3.779  5.764   -7.781  1.00 30.04 ? 148 LYS B CG    1 
ATOM   2205 C CD    . LYS B 1 125 ? -2.289  5.407   -7.805  1.00 28.20 ? 148 LYS B CD    1 
ATOM   2206 C CE    . LYS B 1 125 ? -1.422  6.607   -7.432  1.00 32.12 ? 148 LYS B CE    1 
ATOM   2207 N NZ    . LYS B 1 125 ? 0.021   6.204   -7.355  1.00 39.21 ? 148 LYS B NZ    1 
ATOM   2208 N N     . ARG B 1 126 ? -7.320  2.561   -7.759  1.00 22.49 ? 149 ARG B N     1 
ATOM   2209 C CA    . ARG B 1 126 ? -7.918  1.342   -8.295  1.00 23.74 ? 149 ARG B CA    1 
ATOM   2210 C C     . ARG B 1 126 ? -9.450  1.319   -8.196  1.00 23.98 ? 149 ARG B C     1 
ATOM   2211 O O     . ARG B 1 126 ? -10.049 0.244   -8.297  1.00 23.38 ? 149 ARG B O     1 
ATOM   2212 C CB    . ARG B 1 126 ? -7.315  0.126   -7.586  1.00 24.46 ? 149 ARG B CB    1 
ATOM   2213 C CG    . ARG B 1 126 ? -5.839  -0.112  -7.908  1.00 28.30 ? 149 ARG B CG    1 
ATOM   2214 C CD    . ARG B 1 126 ? -5.155  -0.908  -6.803  1.00 30.20 ? 149 ARG B CD    1 
ATOM   2215 N NE    . ARG B 1 126 ? -3.824  -1.381  -7.175  1.00 33.37 ? 149 ARG B NE    1 
ATOM   2216 C CZ    . ARG B 1 126 ? -2.702  -0.671  -7.048  1.00 37.73 ? 149 ARG B CZ    1 
ATOM   2217 N NH1   . ARG B 1 126 ? -2.732  0.585   -6.570  1.00 33.81 ? 149 ARG B NH1   1 
ATOM   2218 N NH2   . ARG B 1 126 ? -1.543  -1.220  -7.413  1.00 40.78 ? 149 ARG B NH2   1 
ATOM   2219 N N     . VAL B 1 127 ? -10.100 2.465   -7.982  1.00 24.53 ? 150 VAL B N     1 
ATOM   2220 C CA    . VAL B 1 127 ? -11.549 2.556   -8.167  1.00 22.77 ? 150 VAL B CA    1 
ATOM   2221 C C     . VAL B 1 127 ? -11.855 3.757   -9.073  1.00 20.50 ? 150 VAL B C     1 
ATOM   2222 O O     . VAL B 1 127 ? -11.045 4.681   -9.184  1.00 22.66 ? 150 VAL B O     1 
ATOM   2223 C CB    . VAL B 1 127 ? -12.307 2.683   -6.825  1.00 22.88 ? 150 VAL B CB    1 
ATOM   2224 C CG1   . VAL B 1 127 ? -11.977 1.507   -5.876  1.00 21.24 ? 150 VAL B CG1   1 
ATOM   2225 C CG2   . VAL B 1 127 ? -12.054 4.033   -6.185  1.00 18.49 ? 150 VAL B CG2   1 
ATOM   2226 N N     . PRO B 1 128 ? -13.021 3.751   -9.728  1.00 21.02 ? 151 PRO B N     1 
ATOM   2227 C CA    . PRO B 1 128 ? -13.385 4.898   -10.575 1.00 21.38 ? 151 PRO B CA    1 
ATOM   2228 C C     . PRO B 1 128 ? -13.533 6.164   -9.749  1.00 21.37 ? 151 PRO B C     1 
ATOM   2229 O O     . PRO B 1 128 ? -13.916 6.119   -8.580  1.00 20.85 ? 151 PRO B O     1 
ATOM   2230 C CB    . PRO B 1 128 ? -14.726 4.475   -11.188 1.00 20.94 ? 151 PRO B CB    1 
ATOM   2231 C CG    . PRO B 1 128 ? -14.667 2.956   -11.171 1.00 25.00 ? 151 PRO B CG    1 
ATOM   2232 C CD    . PRO B 1 128 ? -13.953 2.622   -9.899  1.00 23.47 ? 151 PRO B CD    1 
ATOM   2233 N N     . HIS B 1 129 ? -13.190 7.300   -10.369 1.00 23.10 ? 152 HIS B N     1 
ATOM   2234 C CA    . HIS B 1 129 ? -13.252 8.594   -9.696  1.00 22.31 ? 152 HIS B CA    1 
ATOM   2235 C C     . HIS B 1 129 ? -14.627 8.814   -9.094  1.00 22.43 ? 152 HIS B C     1 
ATOM   2236 O O     . HIS B 1 129 ? -15.644 8.774   -9.797  1.00 23.10 ? 152 HIS B O     1 
ATOM   2237 C CB    . HIS B 1 129 ? -12.922 9.720   -10.683 1.00 27.56 ? 152 HIS B CB    1 
ATOM   2238 C CG    . HIS B 1 129 ? -12.801 11.071  -10.044 1.00 26.69 ? 152 HIS B CG    1 
ATOM   2239 N ND1   . HIS B 1 129 ? -11.656 11.491  -9.402  1.00 29.45 ? 152 HIS B ND1   1 
ATOM   2240 C CD2   . HIS B 1 129 ? -13.673 12.107  -9.973  1.00 28.20 ? 152 HIS B CD2   1 
ATOM   2241 C CE1   . HIS B 1 129 ? -11.828 12.724  -8.956  1.00 27.72 ? 152 HIS B CE1   1 
ATOM   2242 N NE2   . HIS B 1 129 ? -13.044 13.120  -9.287  1.00 28.52 ? 152 HIS B NE2   1 
ATOM   2243 N N     . GLY B 1 130 ? -14.662 9.040   -7.788  1.00 23.81 ? 153 GLY B N     1 
ATOM   2244 C CA    . GLY B 1 130 ? -15.909 9.224   -7.088  1.00 21.15 ? 153 GLY B CA    1 
ATOM   2245 C C     . GLY B 1 130 ? -16.431 7.992   -6.368  1.00 24.30 ? 153 GLY B C     1 
ATOM   2246 O O     . GLY B 1 130 ? -17.364 8.121   -5.573  1.00 23.29 ? 153 GLY B O     1 
ATOM   2247 N N     . ARG B 1 131 ? -15.880 6.807   -6.619  1.00 20.49 ? 154 ARG B N     1 
ATOM   2248 C CA    . ARG B 1 131 ? -16.298 5.642   -5.844  1.00 21.43 ? 154 ARG B CA    1 
ATOM   2249 C C     . ARG B 1 131 ? -15.510 5.573   -4.533  1.00 21.44 ? 154 ARG B C     1 
ATOM   2250 O O     . ARG B 1 131 ? -14.417 6.134   -4.434  1.00 18.23 ? 154 ARG B O     1 
ATOM   2251 C CB    . ARG B 1 131 ? -16.098 4.371   -6.668  1.00 22.88 ? 154 ARG B CB    1 
ATOM   2252 C CG    . ARG B 1 131 ? -17.000 4.320   -7.917  1.00 23.25 ? 154 ARG B CG    1 
ATOM   2253 C CD    . ARG B 1 131 ? -18.487 4.288   -7.516  1.00 24.33 ? 154 ARG B CD    1 
ATOM   2254 N NE    . ARG B 1 131 ? -18.796 3.089   -6.738  1.00 24.78 ? 154 ARG B NE    1 
ATOM   2255 C CZ    . ARG B 1 131 ? -19.784 2.980   -5.848  1.00 27.03 ? 154 ARG B CZ    1 
ATOM   2256 N NH1   . ARG B 1 131 ? -20.589 4.007   -5.598  1.00 24.71 ? 154 ARG B NH1   1 
ATOM   2257 N NH2   . ARG B 1 131 ? -19.971 1.830   -5.204  1.00 23.66 ? 154 ARG B NH2   1 
ATOM   2258 N N     . PRO B 1 132 ? -16.041 4.858   -3.491  1.00 21.20 ? 155 PRO B N     1 
ATOM   2259 C CA    . PRO B 1 132 ? -15.452 4.980   -2.147  1.00 23.10 ? 155 PRO B CA    1 
ATOM   2260 C C     . PRO B 1 132 ? -14.554 3.841   -1.682  1.00 25.87 ? 155 PRO B C     1 
ATOM   2261 O O     . PRO B 1 132 ? -14.667 2.685   -2.119  1.00 21.57 ? 155 PRO B O     1 
ATOM   2262 C CB    . PRO B 1 132 ? -16.692 5.040   -1.253  1.00 18.68 ? 155 PRO B CB    1 
ATOM   2263 C CG    . PRO B 1 132 ? -17.596 4.001   -1.914  1.00 23.33 ? 155 PRO B CG    1 
ATOM   2264 C CD    . PRO B 1 132 ? -17.349 4.172   -3.431  1.00 21.42 ? 155 PRO B CD    1 
ATOM   2265 N N     . VAL B 1 133 ? -13.678 4.188   -0.740  1.00 22.38 ? 156 VAL B N     1 
ATOM   2266 C CA    . VAL B 1 133 ? -13.078 3.243   0.197   1.00 20.95 ? 156 VAL B CA    1 
ATOM   2267 C C     . VAL B 1 133 ? -13.766 3.435   1.545   1.00 20.07 ? 156 VAL B C     1 
ATOM   2268 O O     . VAL B 1 133 ? -13.776 4.550   2.077   1.00 22.26 ? 156 VAL B O     1 
ATOM   2269 C CB    . VAL B 1 133 ? -11.564 3.484   0.345   1.00 20.83 ? 156 VAL B CB    1 
ATOM   2270 C CG1   . VAL B 1 133 ? -11.004 2.571   1.424   1.00 19.44 ? 156 VAL B CG1   1 
ATOM   2271 C CG2   . VAL B 1 133 ? -10.838 3.324   -0.984  1.00 17.57 ? 156 VAL B CG2   1 
ATOM   2272 N N     . VAL B 1 134 ? -14.307 2.357   2.117   1.00 22.96 ? 157 VAL B N     1 
ATOM   2273 C CA    . VAL B 1 134 ? -14.968 2.394   3.424   1.00 21.20 ? 157 VAL B CA    1 
ATOM   2274 C C     . VAL B 1 134 ? -14.035 1.783   4.458   1.00 23.06 ? 157 VAL B C     1 
ATOM   2275 O O     . VAL B 1 134 ? -13.531 0.672   4.257   1.00 22.01 ? 157 VAL B O     1 
ATOM   2276 C CB    . VAL B 1 134 ? -16.302 1.623   3.406   1.00 23.70 ? 157 VAL B CB    1 
ATOM   2277 C CG1   . VAL B 1 134 ? -17.033 1.808   4.734   1.00 23.60 ? 157 VAL B CG1   1 
ATOM   2278 C CG2   . VAL B 1 134 ? -17.151 2.048   2.233   1.00 26.48 ? 157 VAL B CG2   1 
ATOM   2279 N N     . GLN B 1 135 ? -13.858 2.464   5.595   1.00 18.33 ? 158 GLN B N     1 
ATOM   2280 C CA    . GLN B 1 135 ? -12.930 2.011   6.630   1.00 20.28 ? 158 GLN B CA    1 
ATOM   2281 C C     . GLN B 1 135 ? -13.618 1.983   7.989   1.00 25.51 ? 158 GLN B C     1 
ATOM   2282 O O     . GLN B 1 135 ? -14.307 2.942   8.362   1.00 23.10 ? 158 GLN B O     1 
ATOM   2283 C CB    . GLN B 1 135 ? -11.691 2.921   6.688   1.00 20.25 ? 158 GLN B CB    1 
ATOM   2284 C CG    . GLN B 1 135 ? -10.696 2.584   7.796   1.00 21.41 ? 158 GLN B CG    1 
ATOM   2285 C CD    . GLN B 1 135 ? -9.991  1.276   7.534   1.00 23.71 ? 158 GLN B CD    1 
ATOM   2286 O OE1   . GLN B 1 135 ? -9.454  1.079   6.453   1.00 22.71 ? 158 GLN B OE1   1 
ATOM   2287 N NE2   . GLN B 1 135 ? -10.001 0.364   8.519   1.00 23.43 ? 158 GLN B NE2   1 
ATOM   2288 N N     . ILE B 1 136 ? -13.424 0.883   8.738   1.00 21.81 ? 159 ILE B N     1 
ATOM   2289 C CA    . ILE B 1 136 ? -13.917 0.802   10.112  1.00 25.64 ? 159 ILE B CA    1 
ATOM   2290 C C     . ILE B 1 136 ? -12.807 1.229   11.074  1.00 23.67 ? 159 ILE B C     1 
ATOM   2291 O O     . ILE B 1 136 ? -11.637 0.899   10.874  1.00 25.67 ? 159 ILE B O     1 
ATOM   2292 C CB    . ILE B 1 136 ? -14.443 -0.616  10.422  1.00 27.35 ? 159 ILE B CB    1 
ATOM   2293 C CG1   . ILE B 1 136 ? -14.995 -0.702  11.849  1.00 22.58 ? 159 ILE B CG1   1 
ATOM   2294 C CG2   . ILE B 1 136 ? -13.363 -1.682  10.201  1.00 25.17 ? 159 ILE B CG2   1 
ATOM   2295 C CD1   . ILE B 1 136 ? -15.838 -1.989  12.110  1.00 25.69 ? 159 ILE B CD1   1 
ATOM   2296 N N     . SER B 1 137 ? -13.163 1.997   12.106  1.00 24.08 ? 160 SER B N     1 
ATOM   2297 C CA    . SER B 1 137 ? -12.229 2.332   13.172  1.00 25.06 ? 160 SER B CA    1 
ATOM   2298 C C     . SER B 1 137 ? -13.029 2.577   14.449  1.00 25.46 ? 160 SER B C     1 
ATOM   2299 O O     . SER B 1 137 ? -14.248 2.402   14.481  1.00 22.87 ? 160 SER B O     1 
ATOM   2300 C CB    . SER B 1 137 ? -11.347 3.527   12.796  1.00 25.79 ? 160 SER B CB    1 
ATOM   2301 O OG    . SER B 1 137 ? -12.092 4.723   12.686  1.00 26.22 ? 160 SER B OG    1 
ATOM   2302 N N     . TYR B 1 138 ? -12.335 2.974   15.518  1.00 20.05 ? 161 TYR B N     1 
ATOM   2303 C CA    . TYR B 1 138 ? -12.951 2.949   16.836  1.00 25.05 ? 161 TYR B CA    1 
ATOM   2304 C C     . TYR B 1 138 ? -12.785 4.234   17.653  1.00 27.14 ? 161 TYR B C     1 
ATOM   2305 O O     . TYR B 1 138 ? -13.423 4.359   18.709  1.00 29.69 ? 161 TYR B O     1 
ATOM   2306 C CB    . TYR B 1 138 ? -12.430 1.722   17.617  1.00 25.37 ? 161 TYR B CB    1 
ATOM   2307 C CG    . TYR B 1 138 ? -12.717 0.423   16.866  1.00 23.47 ? 161 TYR B CG    1 
ATOM   2308 C CD1   . TYR B 1 138 ? -14.001 -0.117  16.838  1.00 22.79 ? 161 TYR B CD1   1 
ATOM   2309 C CD2   . TYR B 1 138 ? -11.723 -0.224  16.138  1.00 28.69 ? 161 TYR B CD2   1 
ATOM   2310 C CE1   . TYR B 1 138 ? -14.283 -1.280  16.132  1.00 27.88 ? 161 TYR B CE1   1 
ATOM   2311 C CE2   . TYR B 1 138 ? -11.993 -1.405  15.426  1.00 27.29 ? 161 TYR B CE2   1 
ATOM   2312 C CZ    . TYR B 1 138 ? -13.274 -1.918  15.424  1.00 28.91 ? 161 TYR B CZ    1 
ATOM   2313 O OH    . TYR B 1 138 ? -13.551 -3.071  14.720  1.00 32.53 ? 161 TYR B OH    1 
ATOM   2314 N N     . GLY B 1 139 ? -12.034 5.218   17.167  1.00 23.90 ? 162 GLY B N     1 
ATOM   2315 C CA    . GLY B 1 139 ? -11.851 6.460   17.898  1.00 27.51 ? 162 GLY B CA    1 
ATOM   2316 C C     . GLY B 1 139 ? -12.756 7.581   17.420  1.00 27.88 ? 162 GLY B C     1 
ATOM   2317 O O     . GLY B 1 139 ? -13.571 7.401   16.516  1.00 26.56 ? 162 GLY B O     1 
ATOM   2318 N N     . PRO B 1 140 ? -12.634 8.769   18.020  1.00 27.82 ? 163 PRO B N     1 
ATOM   2319 C CA    . PRO B 1 140 ? -13.536 9.868   17.653  1.00 27.52 ? 163 PRO B CA    1 
ATOM   2320 C C     . PRO B 1 140 ? -13.203 10.576  16.344  1.00 26.44 ? 163 PRO B C     1 
ATOM   2321 O O     . PRO B 1 140 ? -14.063 11.315  15.854  1.00 28.18 ? 163 PRO B O     1 
ATOM   2322 C CB    . PRO B 1 140 ? -13.406 10.836  18.840  1.00 29.72 ? 163 PRO B CB    1 
ATOM   2323 C CG    . PRO B 1 140 ? -12.033 10.622  19.330  1.00 28.51 ? 163 PRO B CG    1 
ATOM   2324 C CD    . PRO B 1 140 ? -11.743 9.141   19.134  1.00 33.50 ? 163 PRO B CD    1 
ATOM   2325 N N     . ILE B 1 141 ? -12.013 10.401  15.754  1.00 25.40 ? 164 ILE B N     1 
ATOM   2326 C CA    . ILE B 1 141 ? -11.666 11.109  14.522  1.00 27.02 ? 164 ILE B CA    1 
ATOM   2327 C C     . ILE B 1 141 ? -11.209 10.121  13.452  1.00 26.51 ? 164 ILE B C     1 
ATOM   2328 O O     . ILE B 1 141 ? -10.925 8.957   13.724  1.00 24.34 ? 164 ILE B O     1 
ATOM   2329 C CB    . ILE B 1 141 ? -10.592 12.195  14.740  1.00 28.97 ? 164 ILE B CB    1 
ATOM   2330 C CG1   . ILE B 1 141 ? -9.267  11.571  15.194  1.00 29.79 ? 164 ILE B CG1   1 
ATOM   2331 C CG2   . ILE B 1 141 ? -11.106 13.274  15.715  1.00 30.85 ? 164 ILE B CG2   1 
ATOM   2332 C CD1   . ILE B 1 141 ? -8.089  12.501  15.040  1.00 33.79 ? 164 ILE B CD1   1 
ATOM   2333 N N     . SER B 1 142 ? -11.149 10.615  12.218  1.00 26.77 ? 165 SER B N     1 
ATOM   2334 C CA    . SER B 1 142 ? -10.784 9.771   11.083  1.00 27.57 ? 165 SER B CA    1 
ATOM   2335 C C     . SER B 1 142 ? -9.443  9.088   11.346  1.00 27.11 ? 165 SER B C     1 
ATOM   2336 O O     . SER B 1 142 ? -8.494  9.754   11.771  1.00 27.54 ? 165 SER B O     1 
ATOM   2337 C CB    . SER B 1 142 ? -10.704 10.608  9.806   1.00 25.61 ? 165 SER B CB    1 
ATOM   2338 O OG    . SER B 1 142 ? -10.104 9.858   8.759   1.00 26.65 ? 165 SER B OG    1 
ATOM   2339 N N     . PRO B 1 143 ? -9.327  7.770   11.131  1.00 28.45 ? 166 PRO B N     1 
ATOM   2340 C CA    . PRO B 1 143 ? -8.021  7.106   11.301  1.00 26.06 ? 166 PRO B CA    1 
ATOM   2341 C C     . PRO B 1 143 ? -6.988  7.530   10.274  1.00 28.44 ? 166 PRO B C     1 
ATOM   2342 O O     . PRO B 1 143 ? -5.803  7.215   10.445  1.00 30.76 ? 166 PRO B O     1 
ATOM   2343 C CB    . PRO B 1 143 ? -8.359  5.618   11.147  1.00 25.34 ? 166 PRO B CB    1 
ATOM   2344 C CG    . PRO B 1 143 ? -9.568  5.619   10.259  1.00 28.38 ? 166 PRO B CG    1 
ATOM   2345 C CD    . PRO B 1 143 ? -10.368 6.834   10.664  1.00 25.60 ? 166 PRO B CD    1 
ATOM   2346 N N     . ILE B 1 144 ? -7.403  8.213   9.213   1.00 23.97 ? 167 ILE B N     1 
ATOM   2347 C CA    . ILE B 1 144 ? -6.509  8.733   8.189   1.00 27.75 ? 167 ILE B CA    1 
ATOM   2348 C C     . ILE B 1 144 ? -6.704  10.247  8.156   1.00 29.97 ? 167 ILE B C     1 
ATOM   2349 O O     . ILE B 1 144 ? -7.825  10.729  7.972   1.00 30.10 ? 167 ILE B O     1 
ATOM   2350 C CB    . ILE B 1 144 ? -6.786  8.072   6.829   1.00 24.32 ? 167 ILE B CB    1 
ATOM   2351 C CG1   . ILE B 1 144 ? -6.977  6.563   7.052   1.00 28.10 ? 167 ILE B CG1   1 
ATOM   2352 C CG2   . ILE B 1 144 ? -5.637  8.314   5.866   1.00 28.65 ? 167 ILE B CG2   1 
ATOM   2353 C CD1   . ILE B 1 144 ? -6.943  5.686   5.789   1.00 26.65 ? 167 ILE B CD1   1 
ATOM   2354 N N     . VAL B 1 145 ? -5.624  10.991  8.392   1.00 24.91 ? 168 VAL B N     1 
ATOM   2355 C CA    . VAL B 1 145 ? -5.728  12.441  8.540   1.00 29.40 ? 168 VAL B CA    1 
ATOM   2356 C C     . VAL B 1 145 ? -6.036  13.104  7.199   1.00 30.20 ? 168 VAL B C     1 
ATOM   2357 O O     . VAL B 1 145 ? -5.771  12.565  6.115   1.00 25.74 ? 168 VAL B O     1 
ATOM   2358 C CB    . VAL B 1 145 ? -4.438  13.002  9.160   1.00 31.65 ? 168 VAL B CB    1 
ATOM   2359 C CG1   . VAL B 1 145 ? -3.301  12.998  8.133   1.00 24.98 ? 168 VAL B CG1   1 
ATOM   2360 C CG2   . VAL B 1 145 ? -4.667  14.400  9.718   1.00 35.28 ? 168 VAL B CG2   1 
ATOM   2361 N N     . ALA B 1 146 ? -6.598  14.308  7.282   1.00 29.94 ? 169 ALA B N     1 
ATOM   2362 C CA    . ALA B 1 146 ? -6.989  15.049  6.094   1.00 28.46 ? 169 ALA B CA    1 
ATOM   2363 C C     . ALA B 1 146 ? -5.789  15.297  5.181   1.00 30.63 ? 169 ALA B C     1 
ATOM   2364 O O     . ALA B 1 146 ? -4.692  15.644  5.635   1.00 28.45 ? 169 ALA B O     1 
ATOM   2365 C CB    . ALA B 1 146 ? -7.641  16.374  6.507   1.00 30.12 ? 169 ALA B CB    1 
ATOM   2366 N N     . GLN B 1 147 ? -5.995  15.075  3.885   1.00 26.51 ? 170 GLN B N     1 
ATOM   2367 C CA    . GLN B 1 147 ? -5.015  15.410  2.851   1.00 26.90 ? 170 GLN B CA    1 
ATOM   2368 C C     . GLN B 1 147 ? -5.827  15.945  1.680   1.00 27.97 ? 170 GLN B C     1 
ATOM   2369 O O     . GLN B 1 147 ? -6.095  15.227  0.711   1.00 27.51 ? 170 GLN B O     1 
ATOM   2370 C CB    . GLN B 1 147 ? -4.167  14.195  2.441   1.00 29.59 ? 170 GLN B CB    1 
ATOM   2371 C CG    . GLN B 1 147 ? -3.220  13.618  3.516   1.00 26.65 ? 170 GLN B CG    1 
ATOM   2372 C CD    . GLN B 1 147 ? -1.959  14.458  3.713   1.00 33.42 ? 170 GLN B CD    1 
ATOM   2373 O OE1   . GLN B 1 147 ? -1.101  14.510  2.847   1.00 33.07 ? 170 GLN B OE1   1 
ATOM   2374 N NE2   . GLN B 1 147 ? -1.856  15.123  4.858   1.00 37.29 ? 170 GLN B NE2   1 
ATOM   2375 N N     . PRO B 1 148 ? -6.251  17.212  1.745   1.00 28.04 ? 171 PRO B N     1 
ATOM   2376 C CA    . PRO B 1 148 ? -7.245  17.704  0.778   1.00 31.86 ? 171 PRO B CA    1 
ATOM   2377 C C     . PRO B 1 148 ? -6.827  17.559  -0.670  1.00 28.79 ? 171 PRO B C     1 
ATOM   2378 O O     . PRO B 1 148 ? -7.693  17.559  -1.553  1.00 32.79 ? 171 PRO B O     1 
ATOM   2379 C CB    . PRO B 1 148 ? -7.413  19.180  1.169   1.00 32.99 ? 171 PRO B CB    1 
ATOM   2380 C CG    . PRO B 1 148 ? -7.040  19.211  2.634   1.00 33.21 ? 171 PRO B CG    1 
ATOM   2381 C CD    . PRO B 1 148 ? -5.911  18.229  2.759   1.00 28.71 ? 171 PRO B CD    1 
ATOM   2382 N N     . HIS B 1 149 ? -5.540  17.412  -0.949  1.00 29.43 ? 172 HIS B N     1 
ATOM   2383 C CA    . HIS B 1 149 ? -5.111  17.260  -2.328  1.00 34.82 ? 172 HIS B CA    1 
ATOM   2384 C C     . HIS B 1 149 ? -5.208  15.822  -2.816  1.00 35.97 ? 172 HIS B C     1 
ATOM   2385 O O     . HIS B 1 149 ? -5.049  15.590  -4.022  1.00 32.86 ? 172 HIS B O     1 
ATOM   2386 C CB    . HIS B 1 149 ? -3.677  17.785  -2.504  1.00 39.49 ? 172 HIS B CB    1 
ATOM   2387 C CG    . HIS B 1 149 ? -2.614  16.894  -1.924  1.00 39.61 ? 172 HIS B CG    1 
ATOM   2388 N ND1   . HIS B 1 149 ? -2.408  16.759  -0.563  1.00 40.05 ? 172 HIS B ND1   1 
ATOM   2389 C CD2   . HIS B 1 149 ? -1.677  16.121  -2.524  1.00 37.66 ? 172 HIS B CD2   1 
ATOM   2390 C CE1   . HIS B 1 149 ? -1.398  15.930  -0.354  1.00 41.35 ? 172 HIS B CE1   1 
ATOM   2391 N NE2   . HIS B 1 149 ? -0.937  15.529  -1.528  1.00 41.86 ? 172 HIS B NE2   1 
ATOM   2392 N N     . LEU B 1 150 ? -5.464  14.862  -1.921  1.00 28.06 ? 173 LEU B N     1 
ATOM   2393 C CA    . LEU B 1 150 ? -5.582  13.455  -2.296  1.00 31.27 ? 173 LEU B CA    1 
ATOM   2394 C C     . LEU B 1 150 ? -6.998  12.905  -2.217  1.00 25.24 ? 173 LEU B C     1 
ATOM   2395 O O     . LEU B 1 150 ? -7.372  12.112  -3.081  1.00 24.95 ? 173 LEU B O     1 
ATOM   2396 C CB    . LEU B 1 150 ? -4.672  12.575  -1.421  1.00 24.30 ? 173 LEU B CB    1 
ATOM   2397 C CG    . LEU B 1 150 ? -3.160  12.813  -1.506  1.00 32.31 ? 173 LEU B CG    1 
ATOM   2398 C CD1   . LEU B 1 150 ? -2.437  11.956  -0.469  1.00 28.35 ? 173 LEU B CD1   1 
ATOM   2399 C CD2   . LEU B 1 150 ? -2.623  12.538  -2.906  1.00 29.54 ? 173 LEU B CD2   1 
ATOM   2400 N N     . TYR B 1 151 ? -7.790  13.275  -1.203  1.00 24.43 ? 174 TYR B N     1 
ATOM   2401 C CA    . TYR B 1 151 ? -9.091  12.643  -0.985  1.00 23.56 ? 174 TYR B CA    1 
ATOM   2402 C C     . TYR B 1 151 ? -10.000 13.507  -0.109  1.00 25.36 ? 174 TYR B C     1 
ATOM   2403 O O     . TYR B 1 151 ? -9.546  14.382  0.634   1.00 23.25 ? 174 TYR B O     1 
ATOM   2404 C CB    . TYR B 1 151 ? -8.934  11.247  -0.347  1.00 20.64 ? 174 TYR B CB    1 
ATOM   2405 C CG    . TYR B 1 151 ? -7.966  11.232  0.809   1.00 22.66 ? 174 TYR B CG    1 
ATOM   2406 C CD1   . TYR B 1 151 ? -8.330  11.720  2.066   1.00 22.79 ? 174 TYR B CD1   1 
ATOM   2407 C CD2   . TYR B 1 151 ? -6.682  10.744  0.645   1.00 22.90 ? 174 TYR B CD2   1 
ATOM   2408 C CE1   . TYR B 1 151 ? -7.417  11.728  3.130   1.00 22.29 ? 174 TYR B CE1   1 
ATOM   2409 C CE2   . TYR B 1 151 ? -5.764  10.747  1.687   1.00 23.14 ? 174 TYR B CE2   1 
ATOM   2410 C CZ    . TYR B 1 151 ? -6.129  11.227  2.918   1.00 25.33 ? 174 TYR B CZ    1 
ATOM   2411 O OH    . TYR B 1 151 ? -5.187  11.209  3.918   1.00 26.82 ? 174 TYR B OH    1 
ATOM   2412 N N     . HIS B 1 152 ? -11.303 13.222  -0.207  1.00 24.38 ? 175 HIS B N     1 
ATOM   2413 C CA    . HIS B 1 152 ? -12.344 13.761  0.660   1.00 25.41 ? 175 HIS B CA    1 
ATOM   2414 C C     . HIS B 1 152 ? -12.649 12.749  1.753   1.00 25.13 ? 175 HIS B C     1 
ATOM   2415 O O     . HIS B 1 152 ? -12.783 11.557  1.473   1.00 22.94 ? 175 HIS B O     1 
ATOM   2416 C CB    . HIS B 1 152 ? -13.655 14.017  -0.101  1.00 28.23 ? 175 HIS B CB    1 
ATOM   2417 C CG    . HIS B 1 152 ? -13.546 14.989  -1.231  1.00 33.86 ? 175 HIS B CG    1 
ATOM   2418 N ND1   . HIS B 1 152 ? -13.673 16.353  -1.053  1.00 35.06 ? 175 HIS B ND1   1 
ATOM   2419 C CD2   . HIS B 1 152 ? -13.377 14.794  -2.562  1.00 34.93 ? 175 HIS B CD2   1 
ATOM   2420 C CE1   . HIS B 1 152 ? -13.562 16.959  -2.223  1.00 33.20 ? 175 HIS B CE1   1 
ATOM   2421 N NE2   . HIS B 1 152 ? -13.384 16.036  -3.155  1.00 40.70 ? 175 HIS B NE2   1 
ATOM   2422 N N     . ILE B 1 153 ? -12.793 13.231  2.982   1.00 22.29 ? 176 ILE B N     1 
ATOM   2423 C CA    . ILE B 1 153 ? -13.210 12.414  4.117   1.00 24.06 ? 176 ILE B CA    1 
ATOM   2424 C C     . ILE B 1 153 ? -14.687 12.677  4.386   1.00 27.31 ? 176 ILE B C     1 
ATOM   2425 O O     . ILE B 1 153 ? -15.098 13.833  4.511   1.00 24.17 ? 176 ILE B O     1 
ATOM   2426 C CB    . ILE B 1 153 ? -12.371 12.735  5.370   1.00 24.25 ? 176 ILE B CB    1 
ATOM   2427 C CG1   . ILE B 1 153 ? -10.870 12.584  5.095   1.00 22.17 ? 176 ILE B CG1   1 
ATOM   2428 C CG2   . ILE B 1 153 ? -12.784 11.831  6.525   1.00 25.13 ? 176 ILE B CG2   1 
ATOM   2429 C CD1   . ILE B 1 153 ? -10.006 12.862  6.318   1.00 23.89 ? 176 ILE B CD1   1 
ATOM   2430 N N     . ARG B 1 154 ? -15.487 11.615  4.489   1.00 22.35 ? 177 ARG B N     1 
ATOM   2431 C CA    . ARG B 1 154 ? -16.885 11.736  4.896   1.00 24.94 ? 177 ARG B CA    1 
ATOM   2432 C C     . ARG B 1 154 ? -17.153 10.759  6.029   1.00 27.95 ? 177 ARG B C     1 
ATOM   2433 O O     . ARG B 1 154 ? -16.871 9.564   5.902   1.00 25.10 ? 177 ARG B O     1 
ATOM   2434 C CB    . ARG B 1 154 ? -17.850 11.464  3.734   1.00 30.06 ? 177 ARG B CB    1 
ATOM   2435 N N     . HIS B 1 155 ? -17.663 11.266  7.146   1.00 25.55 ? 178 HIS B N     1 
ATOM   2436 C CA    . HIS B 1 155 ? -18.123 10.372  8.196   1.00 23.43 ? 178 HIS B CA    1 
ATOM   2437 C C     . HIS B 1 155 ? -19.387 9.667   7.718   1.00 25.58 ? 178 HIS B C     1 
ATOM   2438 O O     . HIS B 1 155 ? -20.288 10.291  7.148   1.00 24.23 ? 178 HIS B O     1 
ATOM   2439 C CB    . HIS B 1 155 ? -18.378 11.137  9.493   1.00 24.97 ? 178 HIS B CB    1 
ATOM   2440 C CG    . HIS B 1 155 ? -18.816 10.256  10.621  1.00 30.06 ? 178 HIS B CG    1 
ATOM   2441 N ND1   . HIS B 1 155 ? -20.120 10.218  11.077  1.00 30.63 ? 178 HIS B ND1   1 
ATOM   2442 C CD2   . HIS B 1 155 ? -18.136 9.334   11.344  1.00 30.32 ? 178 HIS B CD2   1 
ATOM   2443 C CE1   . HIS B 1 155 ? -20.211 9.337   12.059  1.00 28.37 ? 178 HIS B CE1   1 
ATOM   2444 N NE2   . HIS B 1 155 ? -19.021 8.789   12.243  1.00 30.37 ? 178 HIS B NE2   1 
ATOM   2445 N N     . PHE B 1 156 ? -19.429 8.351   7.902   1.00 23.36 ? 179 PHE B N     1 
ATOM   2446 C CA    . PHE B 1 156 ? -20.484 7.511   7.350   1.00 26.49 ? 179 PHE B CA    1 
ATOM   2447 C C     . PHE B 1 156 ? -21.506 7.103   8.408   1.00 23.15 ? 179 PHE B C     1 
ATOM   2448 O O     . PHE B 1 156 ? -22.708 7.273   8.202   1.00 29.76 ? 179 PHE B O     1 
ATOM   2449 C CB    . PHE B 1 156 ? -19.843 6.277   6.688   1.00 23.42 ? 179 PHE B CB    1 
ATOM   2450 C CG    . PHE B 1 156 ? -20.780 5.469   5.808   1.00 26.26 ? 179 PHE B CG    1 
ATOM   2451 C CD1   . PHE B 1 156 ? -21.769 6.080   5.052   1.00 29.16 ? 179 PHE B CD1   1 
ATOM   2452 C CD2   . PHE B 1 156 ? -20.640 4.089   5.722   1.00 24.99 ? 179 PHE B CD2   1 
ATOM   2453 C CE1   . PHE B 1 156 ? -22.616 5.322   4.234   1.00 27.88 ? 179 PHE B CE1   1 
ATOM   2454 C CE2   . PHE B 1 156 ? -21.489 3.323   4.908   1.00 27.80 ? 179 PHE B CE2   1 
ATOM   2455 C CZ    . PHE B 1 156 ? -22.475 3.941   4.171   1.00 25.56 ? 179 PHE B CZ    1 
ATOM   2456 N N     . ASP B 1 157 ? -21.057 6.588   9.550   1.00 25.45 ? 180 ASP B N     1 
ATOM   2457 C CA    . ASP B 1 157 ? -21.971 6.198   10.622  1.00 22.51 ? 180 ASP B CA    1 
ATOM   2458 C C     . ASP B 1 157 ? -21.163 6.005   11.897  1.00 24.14 ? 180 ASP B C     1 
ATOM   2459 O O     . ASP B 1 157 ? -19.940 5.868   11.859  1.00 23.87 ? 180 ASP B O     1 
ATOM   2460 C CB    . ASP B 1 157 ? -22.739 4.918   10.279  1.00 23.72 ? 180 ASP B CB    1 
ATOM   2461 C CG    . ASP B 1 157 ? -24.071 4.804   11.018  1.00 29.83 ? 180 ASP B CG    1 
ATOM   2462 O OD1   . ASP B 1 157 ? -24.312 5.571   11.975  1.00 25.38 ? 180 ASP B OD1   1 
ATOM   2463 O OD2   . ASP B 1 157 ? -24.884 3.936   10.624  1.00 31.76 ? 180 ASP B OD2   1 
ATOM   2464 N N     . PHE B 1 158 ? -21.856 6.045   13.032  1.00 24.21 ? 181 PHE B N     1 
ATOM   2465 C CA    . PHE B 1 158 ? -21.282 5.635   14.312  1.00 23.37 ? 181 PHE B CA    1 
ATOM   2466 C C     . PHE B 1 158 ? -22.247 4.632   14.932  1.00 22.98 ? 181 PHE B C     1 
ATOM   2467 O O     . PHE B 1 158 ? -23.356 4.997   15.327  1.00 22.99 ? 181 PHE B O     1 
ATOM   2468 C CB    . PHE B 1 158 ? -21.047 6.832   15.236  1.00 22.29 ? 181 PHE B CB    1 
ATOM   2469 C CG    . PHE B 1 158 ? -20.489 6.452   16.582  1.00 26.43 ? 181 PHE B CG    1 
ATOM   2470 C CD1   . PHE B 1 158 ? -19.411 5.590   16.676  1.00 27.11 ? 181 PHE B CD1   1 
ATOM   2471 C CD2   . PHE B 1 158 ? -21.051 6.948   17.755  1.00 26.00 ? 181 PHE B CD2   1 
ATOM   2472 C CE1   . PHE B 1 158 ? -18.883 5.232   17.912  1.00 30.97 ? 181 PHE B CE1   1 
ATOM   2473 C CE2   . PHE B 1 158 ? -20.533 6.580   18.998  1.00 25.11 ? 181 PHE B CE2   1 
ATOM   2474 C CZ    . PHE B 1 158 ? -19.452 5.732   19.077  1.00 28.62 ? 181 PHE B CZ    1 
ATOM   2475 N N     . ILE B 1 159 ? -21.833 3.371   15.004  1.00 22.93 ? 182 ILE B N     1 
ATOM   2476 C CA    . ILE B 1 159 ? -22.713 2.264   15.356  1.00 23.00 ? 182 ILE B CA    1 
ATOM   2477 C C     . ILE B 1 159 ? -22.417 1.868   16.793  1.00 24.90 ? 182 ILE B C     1 
ATOM   2478 O O     . ILE B 1 159 ? -21.400 1.226   17.072  1.00 27.09 ? 182 ILE B O     1 
ATOM   2479 C CB    . ILE B 1 159 ? -22.526 1.088   14.389  1.00 26.82 ? 182 ILE B CB    1 
ATOM   2480 C CG1   . ILE B 1 159 ? -22.594 1.637   12.952  1.00 28.30 ? 182 ILE B CG1   1 
ATOM   2481 C CG2   . ILE B 1 159 ? -23.544 -0.043  14.695  1.00 24.20 ? 182 ILE B CG2   1 
ATOM   2482 C CD1   . ILE B 1 159 ? -22.921 0.651   11.898  1.00 28.48 ? 182 ILE B CD1   1 
ATOM   2483 N N     . VAL B 1 160 ? -23.312 2.237   17.712  1.00 26.20 ? 183 VAL B N     1 
ATOM   2484 C CA    . VAL B 1 160 ? -23.049 1.970   19.124  1.00 24.90 ? 183 VAL B CA    1 
ATOM   2485 C C     . VAL B 1 160 ? -23.312 0.511   19.498  1.00 26.55 ? 183 VAL B C     1 
ATOM   2486 O O     . VAL B 1 160 ? -22.804 0.045   20.524  1.00 30.05 ? 183 VAL B O     1 
ATOM   2487 C CB    . VAL B 1 160 ? -23.865 2.919   20.026  1.00 28.40 ? 183 VAL B CB    1 
ATOM   2488 C CG1   . VAL B 1 160 ? -23.762 4.391   19.540  1.00 23.78 ? 183 VAL B CG1   1 
ATOM   2489 C CG2   . VAL B 1 160 ? -25.287 2.486   20.084  1.00 27.46 ? 183 VAL B CG2   1 
ATOM   2490 N N     . ARG B 1 161 ? -24.067 -0.233  18.694  1.00 24.40 ? 184 ARG B N     1 
ATOM   2491 C CA    . ARG B 1 161 ? -24.325 -1.650  18.962  1.00 29.25 ? 184 ARG B CA    1 
ATOM   2492 C C     . ARG B 1 161 ? -23.255 -2.556  18.363  1.00 34.44 ? 184 ARG B C     1 
ATOM   2493 O O     . ARG B 1 161 ? -23.542 -3.629  17.834  1.00 49.00 ? 184 ARG B O     1 
ATOM   2494 C CB    . ARG B 1 161 ? -25.708 -2.022  18.446  1.00 28.57 ? 184 ARG B CB    1 
ATOM   2495 C CG    . ARG B 1 161 ? -26.826 -1.567  19.375  1.00 31.28 ? 184 ARG B CG    1 
ATOM   2496 C CD    . ARG B 1 161 ? -28.149 -1.443  18.630  1.00 32.36 ? 184 ARG B CD    1 
ATOM   2497 N NE    . ARG B 1 161 ? -29.164 -0.801  19.463  1.00 26.86 ? 184 ARG B NE    1 
ATOM   2498 C CZ    . ARG B 1 161 ? -29.349 0.515   19.542  1.00 31.21 ? 184 ARG B CZ    1 
ATOM   2499 N NH1   . ARG B 1 161 ? -28.596 1.342   18.823  1.00 27.36 ? 184 ARG B NH1   1 
ATOM   2500 N NH2   . ARG B 1 161 ? -30.302 1.004   20.330  1.00 27.77 ? 184 ARG B NH2   1 
ATOM   2501 N N     . ASN B 1 162 ? -22.010 -2.116  18.396  1.00 32.27 ? 185 ASN B N     1 
ATOM   2502 C CA    . ASN B 1 162 ? -20.866 -2.898  17.968  1.00 28.99 ? 185 ASN B CA    1 
ATOM   2503 C C     . ASN B 1 162 ? -19.952 -2.970  19.174  1.00 30.72 ? 185 ASN B C     1 
ATOM   2504 O O     . ASN B 1 162 ? -19.953 -2.059  20.003  1.00 28.70 ? 185 ASN B O     1 
ATOM   2505 C CB    . ASN B 1 162 ? -20.157 -2.240  16.760  1.00 26.55 ? 185 ASN B CB    1 
ATOM   2506 C CG    . ASN B 1 162 ? -19.250 -3.210  15.989  1.00 28.34 ? 185 ASN B CG    1 
ATOM   2507 O OD1   . ASN B 1 162 ? -19.701 -3.925  15.090  1.00 26.53 ? 185 ASN B OD1   1 
ATOM   2508 N ND2   . ASN B 1 162 ? -17.967 -3.195  16.310  1.00 24.26 ? 185 ASN B ND2   1 
ATOM   2509 N N     . ILE B 1 163 ? -19.195 -4.058  19.286  1.00 31.13 ? 186 ILE B N     1 
ATOM   2510 C CA    . ILE B 1 163 ? -18.277 -4.224  20.414  1.00 30.38 ? 186 ILE B CA    1 
ATOM   2511 C C     . ILE B 1 163 ? -16.837 -4.135  19.921  1.00 34.22 ? 186 ILE B C     1 
ATOM   2512 O O     . ILE B 1 163 ? -16.334 -5.091  19.317  1.00 35.96 ? 186 ILE B O     1 
ATOM   2513 C CB    . ILE B 1 163 ? -18.523 -5.555  21.143  1.00 38.79 ? 186 ILE B CB    1 
ATOM   2514 C CG1   . ILE B 1 163 ? -19.998 -5.704  21.504  1.00 35.06 ? 186 ILE B CG1   1 
ATOM   2515 C CG2   . ILE B 1 163 ? -17.669 -5.646  22.401  1.00 37.32 ? 186 ILE B CG2   1 
ATOM   2516 C CD1   . ILE B 1 163 ? -20.294 -6.921  22.358  1.00 47.57 ? 186 ILE B CD1   1 
ATOM   2517 N N     . PRO B 1 164 ? -16.134 -3.013  20.134  1.00 32.71 ? 187 PRO B N     1 
ATOM   2518 C CA    . PRO B 1 164 ? -16.610 -1.768  20.739  1.00 26.01 ? 187 PRO B CA    1 
ATOM   2519 C C     . PRO B 1 164 ? -17.351 -0.933  19.686  1.00 30.21 ? 187 PRO B C     1 
ATOM   2520 O O     . PRO B 1 164 ? -17.384 -1.363  18.525  1.00 27.84 ? 187 PRO B O     1 
ATOM   2521 C CB    . PRO B 1 164 ? -15.314 -1.105  21.198  1.00 28.55 ? 187 PRO B CB    1 
ATOM   2522 C CG    . PRO B 1 164 ? -14.320 -1.521  20.159  1.00 34.05 ? 187 PRO B CG    1 
ATOM   2523 C CD    . PRO B 1 164 ? -14.743 -2.889  19.663  1.00 30.97 ? 187 PRO B CD    1 
ATOM   2524 N N     . PRO B 1 165 ? -17.964 0.192   20.073  1.00 30.97 ? 188 PRO B N     1 
ATOM   2525 C CA    . PRO B 1 165 ? -18.689 1.008   19.086  1.00 25.66 ? 188 PRO B CA    1 
ATOM   2526 C C     . PRO B 1 165 ? -17.817 1.310   17.869  1.00 26.56 ? 188 PRO B C     1 
ATOM   2527 O O     . PRO B 1 165 ? -16.630 1.622   17.998  1.00 24.72 ? 188 PRO B O     1 
ATOM   2528 C CB    . PRO B 1 165 ? -19.039 2.274   19.876  1.00 26.77 ? 188 PRO B CB    1 
ATOM   2529 C CG    . PRO B 1 165 ? -19.245 1.757   21.285  1.00 27.13 ? 188 PRO B CG    1 
ATOM   2530 C CD    . PRO B 1 165 ? -18.224 0.645   21.459  1.00 29.58 ? 188 PRO B CD    1 
ATOM   2531 N N     . ALA B 1 166 ? -18.414 1.213   16.680  1.00 22.41 ? 189 ALA B N     1 
ATOM   2532 C CA    . ALA B 1 166 ? -17.669 1.239   15.421  1.00 26.15 ? 189 ALA B CA    1 
ATOM   2533 C C     . ALA B 1 166 ? -17.918 2.534   14.653  1.00 25.19 ? 189 ALA B C     1 
ATOM   2534 O O     . ALA B 1 166 ? -19.070 2.890   14.374  1.00 24.52 ? 189 ALA B O     1 
ATOM   2535 C CB    . ALA B 1 166 ? -18.047 0.047   14.539  1.00 23.48 ? 189 ALA B CB    1 
ATOM   2536 N N     . GLN B 1 167 ? -16.837 3.221   14.295  1.00 23.45 ? 190 GLN B N     1 
ATOM   2537 C CA    . GLN B 1 167 ? -16.903 4.347   13.379  1.00 24.16 ? 190 GLN B CA    1 
ATOM   2538 C C     . GLN B 1 167 ? -16.689 3.861   11.953  1.00 26.20 ? 190 GLN B C     1 
ATOM   2539 O O     . GLN B 1 167 ? -15.812 3.032   11.697  1.00 26.55 ? 190 GLN B O     1 
ATOM   2540 C CB    . GLN B 1 167 ? -15.843 5.386   13.722  1.00 25.41 ? 190 GLN B CB    1 
ATOM   2541 C CG    . GLN B 1 167 ? -15.974 5.927   15.105  1.00 28.01 ? 190 GLN B CG    1 
ATOM   2542 C CD    . GLN B 1 167 ? -16.828 7.176   15.140  1.00 30.65 ? 190 GLN B CD    1 
ATOM   2543 O OE1   . GLN B 1 167 ? -17.819 7.292   14.414  1.00 28.23 ? 190 GLN B OE1   1 
ATOM   2544 N NE2   . GLN B 1 167 ? -16.427 8.136   15.964  1.00 30.30 ? 190 GLN B NE2   1 
ATOM   2545 N N     . LEU B 1 168 ? -17.496 4.379   11.032  1.00 23.34 ? 191 LEU B N     1 
ATOM   2546 C CA    . LEU B 1 168 ? -17.364 4.078   9.616   1.00 23.71 ? 191 LEU B CA    1 
ATOM   2547 C C     . LEU B 1 168 ? -17.060 5.373   8.881   1.00 24.99 ? 191 LEU B C     1 
ATOM   2548 O O     . LEU B 1 168 ? -17.718 6.393   9.108   1.00 24.32 ? 191 LEU B O     1 
ATOM   2549 C CB    . LEU B 1 168 ? -18.637 3.420   9.058   1.00 18.97 ? 191 LEU B CB    1 
ATOM   2550 C CG    . LEU B 1 168 ? -19.051 2.097   9.711   1.00 23.66 ? 191 LEU B CG    1 
ATOM   2551 C CD1   . LEU B 1 168 ? -20.283 1.511   9.020   1.00 22.75 ? 191 LEU B CD1   1 
ATOM   2552 C CD2   . LEU B 1 168 ? -17.868 1.128   9.689   1.00 22.14 ? 191 LEU B CD2   1 
ATOM   2553 N N     . TRP B 1 169 ? -16.049 5.332   8.028   1.00 23.30 ? 192 TRP B N     1 
ATOM   2554 C CA    . TRP B 1 169 ? -15.602 6.476   7.253   1.00 22.29 ? 192 TRP B CA    1 
ATOM   2555 C C     . TRP B 1 169 ? -15.538 6.074   5.789   1.00 25.04 ? 192 TRP B C     1 
ATOM   2556 O O     . TRP B 1 169 ? -15.173 4.939   5.481   1.00 22.93 ? 192 TRP B O     1 
ATOM   2557 C CB    . TRP B 1 169 ? -14.212 6.939   7.711   1.00 19.98 ? 192 TRP B CB    1 
ATOM   2558 C CG    . TRP B 1 169 ? -14.133 7.191   9.150   1.00 24.66 ? 192 TRP B CG    1 
ATOM   2559 C CD1   . TRP B 1 169 ? -13.877 6.277   10.135  1.00 24.43 ? 192 TRP B CD1   1 
ATOM   2560 C CD2   . TRP B 1 169 ? -14.317 8.449   9.801   1.00 22.01 ? 192 TRP B CD2   1 
ATOM   2561 N NE1   . TRP B 1 169 ? -13.892 6.898   11.359  1.00 27.26 ? 192 TRP B NE1   1 
ATOM   2562 C CE2   . TRP B 1 169 ? -14.159 8.229   11.182  1.00 25.66 ? 192 TRP B CE2   1 
ATOM   2563 C CE3   . TRP B 1 169 ? -14.596 9.743   9.349   1.00 25.97 ? 192 TRP B CE3   1 
ATOM   2564 C CZ2   . TRP B 1 169 ? -14.283 9.255   12.121  1.00 29.31 ? 192 TRP B CZ2   1 
ATOM   2565 C CZ3   . TRP B 1 169 ? -14.719 10.763  10.282  1.00 27.36 ? 192 TRP B CZ3   1 
ATOM   2566 C CH2   . TRP B 1 169 ? -14.565 10.511  11.651  1.00 27.14 ? 192 TRP B CH2   1 
ATOM   2567 N N     . THR B 1 170 ? -15.870 6.992   4.880   1.00 22.92 ? 193 THR B N     1 
ATOM   2568 C CA    . THR B 1 170 ? -15.641 6.743   3.464   1.00 21.97 ? 193 THR B CA    1 
ATOM   2569 C C     . THR B 1 170 ? -14.691 7.795   2.911   1.00 22.43 ? 193 THR B C     1 
ATOM   2570 O O     . THR B 1 170 ? -14.718 8.951   3.337   1.00 24.27 ? 193 THR B O     1 
ATOM   2571 C CB    . THR B 1 170 ? -16.938 6.736   2.654   1.00 25.99 ? 193 THR B CB    1 
ATOM   2572 O OG1   . THR B 1 170 ? -17.447 8.063   2.576   1.00 28.78 ? 193 THR B OG1   1 
ATOM   2573 C CG2   . THR B 1 170 ? -17.980 5.825   3.314   1.00 25.53 ? 193 THR B CG2   1 
ATOM   2574 N N     . TYR B 1 171 ? -13.847 7.387   1.967   1.00 18.98 ? 194 TYR B N     1 
ATOM   2575 C CA    . TYR B 1 171 ? -12.924 8.296   1.301   1.00 19.89 ? 194 TYR B CA    1 
ATOM   2576 C C     . TYR B 1 171 ? -13.127 8.197   -0.201  1.00 21.05 ? 194 TYR B C     1 
ATOM   2577 O O     . TYR B 1 171 ? -13.314 7.097   -0.729  1.00 21.65 ? 194 TYR B O     1 
ATOM   2578 C CB    . TYR B 1 171 ? -11.459 7.970   1.662   1.00 21.04 ? 194 TYR B CB    1 
ATOM   2579 C CG    . TYR B 1 171 ? -11.234 7.836   3.158   1.00 20.54 ? 194 TYR B CG    1 
ATOM   2580 C CD1   . TYR B 1 171 ? -11.438 6.626   3.812   1.00 22.69 ? 194 TYR B CD1   1 
ATOM   2581 C CD2   . TYR B 1 171 ? -10.840 8.923   3.913   1.00 21.67 ? 194 TYR B CD2   1 
ATOM   2582 C CE1   . TYR B 1 171 ? -11.245 6.504   5.181   1.00 21.85 ? 194 TYR B CE1   1 
ATOM   2583 C CE2   . TYR B 1 171 ? -10.632 8.813   5.289   1.00 21.34 ? 194 TYR B CE2   1 
ATOM   2584 C CZ    . TYR B 1 171 ? -10.842 7.605   5.912   1.00 23.95 ? 194 TYR B CZ    1 
ATOM   2585 O OH    . TYR B 1 171 ? -10.642 7.502   7.271   1.00 25.60 ? 194 TYR B OH    1 
ATOM   2586 N N     . THR B 1 172 ? -13.078 9.346   -0.884  1.00 19.07 ? 195 THR B N     1 
ATOM   2587 C CA    . THR B 1 172 ? -13.180 9.419   -2.336  1.00 21.42 ? 195 THR B CA    1 
ATOM   2588 C C     . THR B 1 172 ? -12.070 10.323  -2.870  1.00 26.23 ? 195 THR B C     1 
ATOM   2589 O O     . THR B 1 172 ? -11.510 11.149  -2.141  1.00 22.22 ? 195 THR B O     1 
ATOM   2590 C CB    . THR B 1 172 ? -14.566 9.942   -2.804  1.00 23.70 ? 195 THR B CB    1 
ATOM   2591 O OG1   . THR B 1 172 ? -14.830 11.219  -2.200  1.00 27.76 ? 195 THR B OG1   1 
ATOM   2592 C CG2   . THR B 1 172 ? -15.674 8.970   -2.422  1.00 20.79 ? 195 THR B CG2   1 
ATOM   2593 N N     . ARG B 1 173 ? -11.749 10.156  -4.157  1.00 22.97 ? 196 ARG B N     1 
ATOM   2594 C CA    . ARG B 1 173 ? -10.670 10.929  -4.765  1.00 25.60 ? 196 ARG B CA    1 
ATOM   2595 C C     . ARG B 1 173 ? -11.040 12.406  -4.844  1.00 30.04 ? 196 ARG B C     1 
ATOM   2596 O O     . ARG B 1 173 ? -12.195 12.766  -5.109  1.00 26.09 ? 196 ARG B O     1 
ATOM   2597 C CB    . ARG B 1 173 ? -10.339 10.397  -6.159  1.00 26.47 ? 196 ARG B CB    1 
ATOM   2598 C CG    . ARG B 1 173 ? -9.181  11.131  -6.892  1.00 31.31 ? 196 ARG B CG    1 
ATOM   2599 C CD    . ARG B 1 173 ? -7.841  11.038  -6.136  1.00 30.39 ? 196 ARG B CD    1 
ATOM   2600 N NE    . ARG B 1 173 ? -7.142  9.769   -6.369  1.00 26.27 ? 196 ARG B NE    1 
ATOM   2601 C CZ    . ARG B 1 173 ? -6.215  9.268   -5.556  1.00 28.13 ? 196 ARG B CZ    1 
ATOM   2602 N NH1   . ARG B 1 173 ? -5.892  9.921   -4.445  1.00 28.10 ? 196 ARG B NH1   1 
ATOM   2603 N NH2   . ARG B 1 173 ? -5.630  8.108   -5.834  1.00 28.11 ? 196 ARG B NH2   1 
ATOM   2604 N N     . ALA B 1 174 ? -10.053 13.257  -4.564  1.00 24.68 ? 197 ALA B N     1 
ATOM   2605 C CA    . ALA B 1 174 ? -10.182 14.706  -4.708  1.00 33.19 ? 197 ALA B CA    1 
ATOM   2606 C C     . ALA B 1 174 ? -9.878  15.150  -6.148  1.00 36.35 ? 197 ALA B C     1 
ATOM   2607 O O     . ALA B 1 174 ? -10.634 15.905  -6.766  1.00 41.86 ? 197 ALA B O     1 
ATOM   2608 C CB    . ALA B 1 174 ? -9.252  15.422  -3.734  1.00 25.78 ? 197 ALA B CB    1 
ATOM   2609 O OXT   . ALA B 1 174 ? -8.858  14.765  -6.733  1.00 41.76 ? 197 ALA B OXT   1 
ATOM   2610 N N     . VAL C 1 11  ? 27.667  -25.236 -37.037 1.00 56.38 ? 34  VAL C N     1 
ATOM   2611 C CA    . VAL C 1 11  ? 26.648  -26.133 -36.493 1.00 50.70 ? 34  VAL C CA    1 
ATOM   2612 C C     . VAL C 1 11  ? 26.186  -25.607 -35.137 1.00 52.55 ? 34  VAL C C     1 
ATOM   2613 O O     . VAL C 1 11  ? 27.006  -25.317 -34.260 1.00 50.00 ? 34  VAL C O     1 
ATOM   2614 C CB    . VAL C 1 11  ? 27.169  -27.586 -36.382 1.00 52.39 ? 34  VAL C CB    1 
ATOM   2615 C CG1   . VAL C 1 11  ? 26.241  -28.431 -35.516 1.00 47.27 ? 34  VAL C CG1   1 
ATOM   2616 C CG2   . VAL C 1 11  ? 27.300  -28.209 -37.761 1.00 49.26 ? 34  VAL C CG2   1 
ATOM   2617 N N     . PRO C 1 12  ? 24.873  -25.470 -34.961 1.00 53.25 ? 35  PRO C N     1 
ATOM   2618 C CA    . PRO C 1 12  ? 24.366  -24.922 -33.700 1.00 53.71 ? 35  PRO C CA    1 
ATOM   2619 C C     . PRO C 1 12  ? 24.643  -25.873 -32.547 1.00 49.11 ? 35  PRO C C     1 
ATOM   2620 O O     . PRO C 1 12  ? 24.644  -27.101 -32.703 1.00 48.47 ? 35  PRO C O     1 
ATOM   2621 C CB    . PRO C 1 12  ? 22.857  -24.763 -33.947 1.00 52.65 ? 35  PRO C CB    1 
ATOM   2622 C CG    . PRO C 1 12  ? 22.668  -24.930 -35.437 1.00 55.28 ? 35  PRO C CG    1 
ATOM   2623 C CD    . PRO C 1 12  ? 23.784  -25.825 -35.887 1.00 49.03 ? 35  PRO C CD    1 
ATOM   2624 N N     . THR C 1 13  ? 24.925  -25.280 -31.388 1.00 46.22 ? 36  THR C N     1 
ATOM   2625 C CA    . THR C 1 13  ? 25.034  -26.046 -30.157 1.00 41.24 ? 36  THR C CA    1 
ATOM   2626 C C     . THR C 1 13  ? 23.837  -26.980 -30.022 1.00 42.16 ? 36  THR C C     1 
ATOM   2627 O O     . THR C 1 13  ? 22.694  -26.583 -30.275 1.00 41.45 ? 36  THR C O     1 
ATOM   2628 C CB    . THR C 1 13  ? 25.114  -25.090 -28.966 1.00 37.69 ? 36  THR C CB    1 
ATOM   2629 O OG1   . THR C 1 13  ? 26.208  -24.193 -29.163 1.00 36.39 ? 36  THR C OG1   1 
ATOM   2630 C CG2   . THR C 1 13  ? 25.322  -25.843 -27.666 1.00 35.34 ? 36  THR C CG2   1 
ATOM   2631 N N     . SER C 1 14  ? 24.104  -28.236 -29.669 1.00 34.09 ? 37  SER C N     1 
ATOM   2632 C CA    . SER C 1 14  ? 23.017  -29.193 -29.556 1.00 34.78 ? 37  SER C CA    1 
ATOM   2633 C C     . SER C 1 14  ? 22.113  -28.837 -28.373 1.00 35.06 ? 37  SER C C     1 
ATOM   2634 O O     . SER C 1 14  ? 22.511  -28.129 -27.442 1.00 28.96 ? 37  SER C O     1 
ATOM   2635 C CB    . SER C 1 14  ? 23.565  -30.612 -29.412 1.00 32.22 ? 37  SER C CB    1 
ATOM   2636 O OG    . SER C 1 14  ? 23.880  -30.885 -28.060 1.00 40.68 ? 37  SER C OG    1 
ATOM   2637 N N     . SER C 1 15  ? 20.868  -29.323 -28.431 1.00 30.92 ? 38  SER C N     1 
ATOM   2638 C CA    . SER C 1 15  ? 19.898  -28.948 -27.408 1.00 31.91 ? 38  SER C CA    1 
ATOM   2639 C C     . SER C 1 15  ? 20.271  -29.513 -26.038 1.00 28.82 ? 38  SER C C     1 
ATOM   2640 O O     . SER C 1 15  ? 20.047  -28.848 -25.022 1.00 24.41 ? 38  SER C O     1 
ATOM   2641 C CB    . SER C 1 15  ? 18.485  -29.376 -27.830 1.00 32.35 ? 38  SER C CB    1 
ATOM   2642 O OG    . SER C 1 15  ? 18.199  -30.716 -27.479 1.00 44.97 ? 38  SER C OG    1 
ATOM   2643 N N     . ILE C 1 16  ? 20.874  -30.706 -25.985 1.00 28.79 ? 39  ILE C N     1 
ATOM   2644 C CA    . ILE C 1 16  ? 21.286  -31.261 -24.697 1.00 31.37 ? 39  ILE C CA    1 
ATOM   2645 C C     . ILE C 1 16  ? 22.388  -30.406 -24.067 1.00 28.07 ? 39  ILE C C     1 
ATOM   2646 O O     . ILE C 1 16  ? 22.340  -30.103 -22.871 1.00 26.37 ? 39  ILE C O     1 
ATOM   2647 C CB    . ILE C 1 16  ? 21.706  -32.740 -24.846 1.00 30.55 ? 39  ILE C CB    1 
ATOM   2648 C CG1   . ILE C 1 16  ? 22.107  -33.324 -23.491 1.00 29.97 ? 39  ILE C CG1   1 
ATOM   2649 C CG2   . ILE C 1 16  ? 22.834  -32.914 -25.864 1.00 32.58 ? 39  ILE C CG2   1 
ATOM   2650 C CD1   . ILE C 1 16  ? 20.990  -33.317 -22.474 1.00 30.93 ? 39  ILE C CD1   1 
ATOM   2651 N N     . THR C 1 17  ? 23.370  -29.970 -24.863 1.00 25.81 ? 40  THR C N     1 
ATOM   2652 C CA    . THR C 1 17  ? 24.393  -29.046 -24.366 1.00 26.48 ? 40  THR C CA    1 
ATOM   2653 C C     . THR C 1 17  ? 23.774  -27.770 -23.827 1.00 25.45 ? 40  THR C C     1 
ATOM   2654 O O     . THR C 1 17  ? 24.152  -27.277 -22.751 1.00 23.37 ? 40  THR C O     1 
ATOM   2655 C CB    . THR C 1 17  ? 25.380  -28.702 -25.481 1.00 27.74 ? 40  THR C CB    1 
ATOM   2656 O OG1   . THR C 1 17  ? 25.905  -29.906 -26.037 1.00 27.87 ? 40  THR C OG1   1 
ATOM   2657 C CG2   . THR C 1 17  ? 26.526  -27.860 -24.948 1.00 20.66 ? 40  THR C CG2   1 
ATOM   2658 N N     . ALA C 1 18  ? 22.825  -27.207 -24.572 1.00 26.48 ? 41  ALA C N     1 
ATOM   2659 C CA    . ALA C 1 18  ? 22.184  -25.972 -24.138 1.00 24.03 ? 41  ALA C CA    1 
ATOM   2660 C C     . ALA C 1 18  ? 21.375  -26.184 -22.867 1.00 23.69 ? 41  ALA C C     1 
ATOM   2661 O O     . ALA C 1 18  ? 21.325  -25.304 -21.999 1.00 20.23 ? 41  ALA C O     1 
ATOM   2662 C CB    . ALA C 1 18  ? 21.286  -25.432 -25.251 1.00 25.14 ? 41  ALA C CB    1 
ATOM   2663 N N     . LYS C 1 19  ? 20.707  -27.330 -22.756 1.00 22.66 ? 42  LYS C N     1 
ATOM   2664 C CA    . LYS C 1 19  ? 19.942  -27.612 -21.548 1.00 25.21 ? 42  LYS C CA    1 
ATOM   2665 C C     . LYS C 1 19  ? 20.854  -27.719 -20.324 1.00 23.22 ? 42  LYS C C     1 
ATOM   2666 O O     . LYS C 1 19  ? 20.525  -27.199 -19.248 1.00 21.77 ? 42  LYS C O     1 
ATOM   2667 C CB    . LYS C 1 19  ? 19.124  -28.889 -21.745 1.00 21.99 ? 42  LYS C CB    1 
ATOM   2668 C CG    . LYS C 1 19  ? 17.847  -28.915 -20.923 1.00 38.33 ? 42  LYS C CG    1 
ATOM   2669 C CD    . LYS C 1 19  ? 17.350  -30.333 -20.678 1.00 34.53 ? 42  LYS C CD    1 
ATOM   2670 C CE    . LYS C 1 19  ? 16.147  -30.364 -19.728 1.00 36.02 ? 42  LYS C CE    1 
ATOM   2671 N NZ    . LYS C 1 19  ? 15.335  -31.622 -19.929 1.00 33.86 ? 42  LYS C NZ    1 
ATOM   2672 N N     . LYS C 1 20  ? 22.009  -28.382 -20.470 1.00 22.30 ? 43  LYS C N     1 
ATOM   2673 C CA    . LYS C 1 20  ? 22.941  -28.503 -19.351 1.00 20.25 ? 43  LYS C CA    1 
ATOM   2674 C C     . LYS C 1 20  ? 23.480  -27.137 -18.929 1.00 19.94 ? 43  LYS C C     1 
ATOM   2675 O O     . LYS C 1 20  ? 23.569  -26.845 -17.732 1.00 20.23 ? 43  LYS C O     1 
ATOM   2676 C CB    . LYS C 1 20  ? 24.082  -29.463 -19.718 1.00 18.98 ? 43  LYS C CB    1 
ATOM   2677 C CG    . LYS C 1 20  ? 25.136  -29.689 -18.614 1.00 19.16 ? 43  LYS C CG    1 
ATOM   2678 C CD    . LYS C 1 20  ? 24.550  -30.280 -17.301 1.00 21.36 ? 43  LYS C CD    1 
ATOM   2679 C CE    . LYS C 1 20  ? 25.673  -30.623 -16.302 1.00 21.17 ? 43  LYS C CE    1 
ATOM   2680 N NZ    . LYS C 1 20  ? 25.155  -31.082 -14.968 1.00 23.28 ? 43  LYS C NZ    1 
ATOM   2681 N N     . MET C 1 21  ? 23.830  -26.277 -19.896 1.00 18.63 ? 44  MET C N     1 
ATOM   2682 C CA    . MET C 1 21  ? 24.301  -24.932 -19.565 1.00 20.66 ? 44  MET C CA    1 
ATOM   2683 C C     . MET C 1 21  ? 23.233  -24.138 -18.827 1.00 20.54 ? 44  MET C C     1 
ATOM   2684 O O     . MET C 1 21  ? 23.514  -23.470 -17.823 1.00 22.29 ? 44  MET C O     1 
ATOM   2685 C CB    . MET C 1 21  ? 24.737  -24.188 -20.840 1.00 19.11 ? 44  MET C CB    1 
ATOM   2686 C CG    . MET C 1 21  ? 25.994  -24.765 -21.487 1.00 20.81 ? 44  MET C CG    1 
ATOM   2687 S SD    . MET C 1 21  ? 26.476  -23.921 -23.028 1.00 29.48 ? 44  MET C SD    1 
ATOM   2688 C CE    . MET C 1 21  ? 27.151  -22.390 -22.370 1.00 26.36 ? 44  MET C CE    1 
ATOM   2689 N N     . ALA C 1 22  ? 21.995  -24.188 -19.315 1.00 20.28 ? 45  ALA C N     1 
ATOM   2690 C CA    . ALA C 1 22  ? 20.931  -23.421 -18.682 1.00 22.90 ? 45  ALA C CA    1 
ATOM   2691 C C     . ALA C 1 22  ? 20.546  -23.973 -17.316 1.00 20.62 ? 45  ALA C C     1 
ATOM   2692 O O     . ALA C 1 22  ? 19.934  -23.251 -16.523 1.00 23.32 ? 45  ALA C O     1 
ATOM   2693 C CB    . ALA C 1 22  ? 19.697  -23.384 -19.594 1.00 20.07 ? 45  ALA C CB    1 
ATOM   2694 N N     . SER C 1 23  ? 20.902  -25.223 -17.008 1.00 22.42 ? 46  SER C N     1 
ATOM   2695 C CA    . SER C 1 23  ? 20.470  -25.808 -15.738 1.00 21.36 ? 46  SER C CA    1 
ATOM   2696 C C     . SER C 1 23  ? 21.106  -25.143 -14.512 1.00 27.68 ? 46  SER C C     1 
ATOM   2697 O O     . SER C 1 23  ? 20.630  -25.376 -13.396 1.00 26.34 ? 46  SER C O     1 
ATOM   2698 C CB    . SER C 1 23  ? 20.747  -27.327 -15.731 1.00 21.73 ? 46  SER C CB    1 
ATOM   2699 O OG    . SER C 1 23  ? 22.140  -27.631 -15.669 1.00 20.74 ? 46  SER C OG    1 
ATOM   2700 N N     . VAL C 1 24  ? 22.147  -24.314 -14.674 1.00 28.56 ? 47  VAL C N     1 
ATOM   2701 C CA    . VAL C 1 24  ? 22.713  -23.643 -13.505 1.00 28.70 ? 47  VAL C CA    1 
ATOM   2702 C C     . VAL C 1 24  ? 21.786  -22.553 -12.976 1.00 28.61 ? 47  VAL C C     1 
ATOM   2703 O O     . VAL C 1 24  ? 21.919  -22.140 -11.821 1.00 25.51 ? 47  VAL C O     1 
ATOM   2704 C CB    . VAL C 1 24  ? 24.098  -23.033 -13.804 1.00 25.85 ? 47  VAL C CB    1 
ATOM   2705 C CG1   . VAL C 1 24  ? 25.022  -24.049 -14.457 1.00 28.74 ? 47  VAL C CG1   1 
ATOM   2706 C CG2   . VAL C 1 24  ? 23.961  -21.777 -14.663 1.00 26.73 ? 47  VAL C CG2   1 
ATOM   2707 N N     . ILE C 1 25  ? 20.843  -22.081 -13.793 1.00 25.02 ? 48  ILE C N     1 
ATOM   2708 C CA    . ILE C 1 25  ? 20.023  -20.930 -13.441 1.00 23.57 ? 48  ILE C CA    1 
ATOM   2709 C C     . ILE C 1 25  ? 19.048  -21.283 -12.318 1.00 26.79 ? 48  ILE C C     1 
ATOM   2710 O O     . ILE C 1 25  ? 18.451  -22.366 -12.302 1.00 23.69 ? 48  ILE C O     1 
ATOM   2711 C CB    . ILE C 1 25  ? 19.278  -20.445 -14.696 1.00 27.97 ? 48  ILE C CB    1 
ATOM   2712 C CG1   . ILE C 1 25  ? 20.271  -19.831 -15.685 1.00 25.55 ? 48  ILE C CG1   1 
ATOM   2713 C CG2   . ILE C 1 25  ? 18.115  -19.485 -14.345 1.00 26.05 ? 48  ILE C CG2   1 
ATOM   2714 C CD1   . ILE C 1 25  ? 19.761  -19.801 -17.092 1.00 22.95 ? 48  ILE C CD1   1 
ATOM   2715 N N     . ASN C 1 26  ? 18.879  -20.363 -11.373 1.00 24.41 ? 49  ASN C N     1 
ATOM   2716 C CA    . ASN C 1 26  ? 17.840  -20.485 -10.358 1.00 29.05 ? 49  ASN C CA    1 
ATOM   2717 C C     . ASN C 1 26  ? 16.696  -19.553 -10.731 1.00 29.94 ? 49  ASN C C     1 
ATOM   2718 O O     . ASN C 1 26  ? 16.763  -18.349 -10.433 1.00 29.31 ? 49  ASN C O     1 
ATOM   2719 C CB    . ASN C 1 26  ? 18.375  -20.145 -8.964  1.00 29.36 ? 49  ASN C CB    1 
ATOM   2720 C CG    . ASN C 1 26  ? 17.334  -20.364 -7.862  1.00 34.53 ? 49  ASN C CG    1 
ATOM   2721 O OD1   . ASN C 1 26  ? 16.158  -20.641 -8.132  1.00 30.78 ? 49  ASN C OD1   1 
ATOM   2722 N ND2   . ASN C 1 26  ? 17.769  -20.247 -6.613  1.00 32.50 ? 49  ASN C ND2   1 
ATOM   2723 N N     . PRO C 1 27  ? 15.619  -20.050 -11.356 1.00 30.39 ? 50  PRO C N     1 
ATOM   2724 C CA    . PRO C 1 27  ? 14.534  -19.150 -11.781 1.00 29.56 ? 50  PRO C CA    1 
ATOM   2725 C C     . PRO C 1 27  ? 13.722  -18.598 -10.627 1.00 31.52 ? 50  PRO C C     1 
ATOM   2726 O O     . PRO C 1 27  ? 12.931  -17.674 -10.846 1.00 32.74 ? 50  PRO C O     1 
ATOM   2727 C CB    . PRO C 1 27  ? 13.678  -20.037 -12.691 1.00 32.76 ? 50  PRO C CB    1 
ATOM   2728 C CG    . PRO C 1 27  ? 13.874  -21.418 -12.140 1.00 33.18 ? 50  PRO C CG    1 
ATOM   2729 C CD    . PRO C 1 27  ? 15.311  -21.465 -11.635 1.00 29.11 ? 50  PRO C CD    1 
ATOM   2730 N N     . HIS C 1 28  ? 13.905  -19.110 -9.410  1.00 27.56 ? 51  HIS C N     1 
ATOM   2731 C CA    . HIS C 1 28  ? 13.206  -18.592 -8.239  1.00 32.02 ? 51  HIS C CA    1 
ATOM   2732 C C     . HIS C 1 28  ? 14.033  -17.587 -7.444  1.00 33.35 ? 51  HIS C C     1 
ATOM   2733 O O     . HIS C 1 28  ? 13.599  -17.161 -6.372  1.00 32.02 ? 51  HIS C O     1 
ATOM   2734 C CB    . HIS C 1 28  ? 12.769  -19.742 -7.323  1.00 34.36 ? 51  HIS C CB    1 
ATOM   2735 C CG    . HIS C 1 28  ? 12.109  -20.868 -8.055  1.00 34.74 ? 51  HIS C CG    1 
ATOM   2736 N ND1   . HIS C 1 28  ? 10.846  -20.759 -8.602  1.00 36.15 ? 51  HIS C ND1   1 
ATOM   2737 C CD2   . HIS C 1 28  ? 12.550  -22.111 -8.368  1.00 36.20 ? 51  HIS C CD2   1 
ATOM   2738 C CE1   . HIS C 1 28  ? 10.535  -21.891 -9.211  1.00 32.54 ? 51  HIS C CE1   1 
ATOM   2739 N NE2   . HIS C 1 28  ? 11.549  -22.727 -9.083  1.00 34.72 ? 51  HIS C NE2   1 
ATOM   2740 N N     . SER C 1 29  ? 15.215  -17.202 -7.925  1.00 32.44 ? 52  SER C N     1 
ATOM   2741 C CA    . SER C 1 29  ? 15.947  -16.159 -7.214  1.00 28.33 ? 52  SER C CA    1 
ATOM   2742 C C     . SER C 1 29  ? 15.353  -14.778 -7.464  1.00 32.04 ? 52  SER C C     1 
ATOM   2743 O O     . SER C 1 29  ? 15.538  -13.869 -6.640  1.00 31.26 ? 52  SER C O     1 
ATOM   2744 C CB    . SER C 1 29  ? 17.430  -16.180 -7.612  1.00 29.01 ? 52  SER C CB    1 
ATOM   2745 O OG    . SER C 1 29  ? 17.625  -15.550 -8.860  1.00 26.66 ? 52  SER C OG    1 
ATOM   2746 N N     . GLY C 1 30  ? 14.623  -14.609 -8.562  1.00 29.25 ? 53  GLY C N     1 
ATOM   2747 C CA    . GLY C 1 30  ? 14.101  -13.318 -8.934  1.00 32.97 ? 53  GLY C CA    1 
ATOM   2748 C C     . GLY C 1 30  ? 15.108  -12.390 -9.575  1.00 34.64 ? 53  GLY C C     1 
ATOM   2749 O O     . GLY C 1 30  ? 14.746  -11.263 -9.931  1.00 36.39 ? 53  GLY C O     1 
ATOM   2750 N N     . LEU C 1 31  ? 16.398  -12.832 -9.724  1.00 33.89 ? 54  LEU C N     1 
ATOM   2751 C CA    . LEU C 1 31  ? 17.414  -12.031 -10.383 1.00 31.22 ? 54  LEU C CA    1 
ATOM   2752 C C     . LEU C 1 31  ? 17.412  -12.310 -11.882 1.00 29.12 ? 54  LEU C C     1 
ATOM   2753 O O     . LEU C 1 31  ? 17.078  -13.421 -12.312 1.00 27.18 ? 54  LEU C O     1 
ATOM   2754 C CB    . LEU C 1 31  ? 18.794  -12.344 -9.806  1.00 27.07 ? 54  LEU C CB    1 
ATOM   2755 C CG    . LEU C 1 31  ? 18.982  -12.030 -8.319  1.00 30.43 ? 54  LEU C CG    1 
ATOM   2756 C CD1   . LEU C 1 31  ? 20.315  -12.563 -7.826  1.00 29.09 ? 54  LEU C CD1   1 
ATOM   2757 C CD2   . LEU C 1 31  ? 18.863  -10.526 -8.047  1.00 29.41 ? 54  LEU C CD2   1 
ATOM   2758 N N     . PRO C 1 32  ? 17.786  -11.331 -12.704 1.00 28.64 ? 55  PRO C N     1 
ATOM   2759 C CA    . PRO C 1 32  ? 17.874  -11.580 -14.148 1.00 26.26 ? 55  PRO C CA    1 
ATOM   2760 C C     . PRO C 1 32  ? 19.098  -12.418 -14.484 1.00 28.70 ? 55  PRO C C     1 
ATOM   2761 O O     . PRO C 1 32  ? 19.994  -12.622 -13.663 1.00 27.63 ? 55  PRO C O     1 
ATOM   2762 C CB    . PRO C 1 32  ? 17.978  -10.180 -14.759 1.00 27.90 ? 55  PRO C CB    1 
ATOM   2763 C CG    . PRO C 1 32  ? 18.532  -9.322  -13.667 1.00 27.50 ? 55  PRO C CG    1 
ATOM   2764 C CD    . PRO C 1 32  ? 18.023  -9.914  -12.365 1.00 26.34 ? 55  PRO C CD    1 
ATOM   2765 N N     . VAL C 1 33  ? 19.133  -12.887 -15.731 1.00 23.13 ? 56  VAL C N     1 
ATOM   2766 C CA    . VAL C 1 33  ? 20.214  -13.717 -16.244 1.00 26.49 ? 56  VAL C CA    1 
ATOM   2767 C C     . VAL C 1 33  ? 20.945  -12.953 -17.339 1.00 26.11 ? 56  VAL C C     1 
ATOM   2768 O O     . VAL C 1 33  ? 20.328  -12.199 -18.102 1.00 26.99 ? 56  VAL C O     1 
ATOM   2769 C CB    . VAL C 1 33  ? 19.658  -15.057 -16.760 1.00 27.71 ? 56  VAL C CB    1 
ATOM   2770 C CG1   . VAL C 1 33  ? 20.729  -15.865 -17.474 1.00 23.74 ? 56  VAL C CG1   1 
ATOM   2771 C CG2   . VAL C 1 33  ? 19.075  -15.836 -15.589 1.00 24.88 ? 56  VAL C CG2   1 
ATOM   2772 N N     . LEU C 1 34  ? 22.264  -13.145 -17.412 1.00 25.96 ? 57  LEU C N     1 
ATOM   2773 C CA    . LEU C 1 34  ? 23.108  -12.539 -18.438 1.00 24.39 ? 57  LEU C CA    1 
ATOM   2774 C C     . LEU C 1 34  ? 23.648  -13.617 -19.372 1.00 24.87 ? 57  LEU C C     1 
ATOM   2775 O O     . LEU C 1 34  ? 24.263  -14.588 -18.916 1.00 24.15 ? 57  LEU C O     1 
ATOM   2776 C CB    . LEU C 1 34  ? 24.264  -11.764 -17.799 1.00 24.04 ? 57  LEU C CB    1 
ATOM   2777 C CG    . LEU C 1 34  ? 25.232  -11.107 -18.786 1.00 29.73 ? 57  LEU C CG    1 
ATOM   2778 C CD1   . LEU C 1 34  ? 24.511  -10.015 -19.610 1.00 24.48 ? 57  LEU C CD1   1 
ATOM   2779 C CD2   . LEU C 1 34  ? 26.444  -10.538 -18.042 1.00 26.14 ? 57  LEU C CD2   1 
ATOM   2780 N N     . GLU C 1 35  ? 23.426  -13.445 -20.676 1.00 22.02 ? 58  GLU C N     1 
ATOM   2781 C CA    . GLU C 1 35  ? 23.937  -14.358 -21.692 1.00 24.88 ? 58  GLU C CA    1 
ATOM   2782 C C     . GLU C 1 35  ? 24.932  -13.626 -22.592 1.00 27.41 ? 58  GLU C C     1 
ATOM   2783 O O     . GLU C 1 35  ? 24.700  -12.481 -22.983 1.00 26.45 ? 58  GLU C O     1 
ATOM   2784 C CB    . GLU C 1 35  ? 22.793  -14.955 -22.548 1.00 25.41 ? 58  GLU C CB    1 
ATOM   2785 C CG    . GLU C 1 35  ? 23.318  -15.793 -23.724 1.00 28.16 ? 58  GLU C CG    1 
ATOM   2786 C CD    . GLU C 1 35  ? 22.231  -16.473 -24.577 1.00 35.66 ? 58  GLU C CD    1 
ATOM   2787 O OE1   . GLU C 1 35  ? 22.579  -17.424 -25.316 1.00 37.43 ? 58  GLU C OE1   1 
ATOM   2788 O OE2   . GLU C 1 35  ? 21.045  -16.064 -24.533 1.00 34.29 ? 58  GLU C OE2   1 
ATOM   2789 N N     . LEU C 1 36  ? 26.037  -14.288 -22.928 1.00 28.25 ? 59  LEU C N     1 
ATOM   2790 C CA    . LEU C 1 36  ? 27.061  -13.715 -23.795 1.00 26.13 ? 59  LEU C CA    1 
ATOM   2791 C C     . LEU C 1 36  ? 27.134  -14.523 -25.083 1.00 26.85 ? 59  LEU C C     1 
ATOM   2792 O O     . LEU C 1 36  ? 27.293  -15.748 -25.042 1.00 25.76 ? 59  LEU C O     1 
ATOM   2793 C CB    . LEU C 1 36  ? 28.429  -13.695 -23.100 1.00 25.18 ? 59  LEU C CB    1 
ATOM   2794 C CG    . LEU C 1 36  ? 28.460  -13.082 -21.699 1.00 25.65 ? 59  LEU C CG    1 
ATOM   2795 C CD1   . LEU C 1 36  ? 29.881  -13.100 -21.153 1.00 27.26 ? 59  LEU C CD1   1 
ATOM   2796 C CD2   . LEU C 1 36  ? 27.899  -11.663 -21.712 1.00 26.22 ? 59  LEU C CD2   1 
ATOM   2797 N N     . GLY C 1 37  ? 27.005  -13.838 -26.223 1.00 28.82 ? 60  GLY C N     1 
ATOM   2798 C CA    . GLY C 1 37  ? 27.122  -14.467 -27.523 1.00 33.27 ? 60  GLY C CA    1 
ATOM   2799 C C     . GLY C 1 37  ? 25.993  -15.420 -27.897 1.00 29.70 ? 60  GLY C C     1 
ATOM   2800 O O     . GLY C 1 37  ? 26.226  -16.588 -28.209 1.00 34.12 ? 60  GLY C O     1 
ATOM   2801 N N     . PRO C 1 38  ? 24.750  -14.930 -27.922 1.00 27.70 ? 61  PRO C N     1 
ATOM   2802 C CA    . PRO C 1 38  ? 23.617  -15.839 -28.187 1.00 28.37 ? 61  PRO C CA    1 
ATOM   2803 C C     . PRO C 1 38  ? 23.550  -16.379 -29.611 1.00 33.72 ? 61  PRO C C     1 
ATOM   2804 O O     . PRO C 1 38  ? 22.941  -17.438 -29.814 1.00 29.40 ? 61  PRO C O     1 
ATOM   2805 C CB    . PRO C 1 38  ? 22.390  -14.983 -27.851 1.00 32.02 ? 61  PRO C CB    1 
ATOM   2806 C CG    . PRO C 1 38  ? 22.859  -13.584 -27.966 1.00 30.84 ? 61  PRO C CG    1 
ATOM   2807 C CD    . PRO C 1 38  ? 24.306  -13.566 -27.599 1.00 31.51 ? 61  PRO C CD    1 
ATOM   2808 N N     . GLY C 1 39  ? 24.130  -15.696 -30.605 1.00 32.69 ? 62  GLY C N     1 
ATOM   2809 C CA    . GLY C 1 39  ? 24.238  -16.306 -31.932 1.00 35.69 ? 62  GLY C CA    1 
ATOM   2810 C C     . GLY C 1 39  ? 22.874  -16.603 -32.539 1.00 32.49 ? 62  GLY C C     1 
ATOM   2811 O O     . GLY C 1 39  ? 22.049  -15.705 -32.718 1.00 37.88 ? 62  GLY C O     1 
ATOM   2812 N N     . THR C 1 40  ? 22.608  -17.878 -32.847 1.00 37.57 ? 63  THR C N     1 
ATOM   2813 C CA    . THR C 1 40  ? 21.320  -18.281 -33.402 1.00 34.93 ? 63  THR C CA    1 
ATOM   2814 C C     . THR C 1 40  ? 20.217  -18.406 -32.357 1.00 40.41 ? 63  THR C C     1 
ATOM   2815 O O     . THR C 1 40  ? 19.052  -18.567 -32.735 1.00 35.83 ? 63  THR C O     1 
ATOM   2816 C CB    . THR C 1 40  ? 21.439  -19.618 -34.137 1.00 42.15 ? 63  THR C CB    1 
ATOM   2817 O OG1   . THR C 1 40  ? 21.866  -20.639 -33.226 1.00 49.82 ? 63  THR C OG1   1 
ATOM   2818 C CG2   . THR C 1 40  ? 22.446  -19.512 -35.264 1.00 44.44 ? 63  THR C CG2   1 
ATOM   2819 N N     . GLY C 1 41  ? 20.549  -18.369 -31.067 1.00 35.40 ? 64  GLY C N     1 
ATOM   2820 C CA    . GLY C 1 41  ? 19.547  -18.392 -30.023 1.00 35.74 ? 64  GLY C CA    1 
ATOM   2821 C C     . GLY C 1 41  ? 19.238  -19.749 -29.435 1.00 32.78 ? 64  GLY C C     1 
ATOM   2822 O O     . GLY C 1 41  ? 18.229  -19.878 -28.732 1.00 34.69 ? 64  GLY C O     1 
ATOM   2823 N N     . VAL C 1 42  ? 20.074  -20.755 -29.685 1.00 28.61 ? 65  VAL C N     1 
ATOM   2824 C CA    . VAL C 1 42  ? 19.825  -22.092 -29.154 1.00 33.11 ? 65  VAL C CA    1 
ATOM   2825 C C     . VAL C 1 42  ? 19.894  -22.085 -27.631 1.00 31.31 ? 65  VAL C C     1 
ATOM   2826 O O     . VAL C 1 42  ? 19.050  -22.678 -26.947 1.00 29.96 ? 65  VAL C O     1 
ATOM   2827 C CB    . VAL C 1 42  ? 20.820  -23.096 -29.762 1.00 34.28 ? 65  VAL C CB    1 
ATOM   2828 C CG1   . VAL C 1 42  ? 20.706  -24.434 -29.077 1.00 38.72 ? 65  VAL C CG1   1 
ATOM   2829 C CG2   . VAL C 1 42  ? 20.569  -23.243 -31.245 1.00 39.84 ? 65  VAL C CG2   1 
ATOM   2830 N N     . ILE C 1 43  ? 20.902  -21.416 -27.073 1.00 30.95 ? 66  ILE C N     1 
ATOM   2831 C CA    . ILE C 1 43  ? 20.993  -21.331 -25.617 1.00 26.77 ? 66  ILE C CA    1 
ATOM   2832 C C     . ILE C 1 43  ? 19.946  -20.363 -25.071 1.00 28.69 ? 66  ILE C C     1 
ATOM   2833 O O     . ILE C 1 43  ? 19.403  -20.578 -23.981 1.00 29.10 ? 66  ILE C O     1 
ATOM   2834 C CB    . ILE C 1 43  ? 22.432  -20.951 -25.204 1.00 29.69 ? 66  ILE C CB    1 
ATOM   2835 C CG1   . ILE C 1 43  ? 23.414  -22.037 -25.675 1.00 29.20 ? 66  ILE C CG1   1 
ATOM   2836 C CG2   . ILE C 1 43  ? 22.547  -20.777 -23.689 1.00 30.99 ? 66  ILE C CG2   1 
ATOM   2837 C CD1   . ILE C 1 43  ? 24.864  -21.667 -25.509 1.00 28.96 ? 66  ILE C CD1   1 
ATOM   2838 N N     . THR C 1 44  ? 19.621  -19.303 -25.822 1.00 29.51 ? 67  THR C N     1 
ATOM   2839 C CA    . THR C 1 44  ? 18.544  -18.393 -25.423 1.00 28.70 ? 67  THR C CA    1 
ATOM   2840 C C     . THR C 1 44  ? 17.223  -19.138 -25.237 1.00 28.26 ? 67  THR C C     1 
ATOM   2841 O O     . THR C 1 44  ? 16.467  -18.869 -24.294 1.00 26.04 ? 67  THR C O     1 
ATOM   2842 C CB    . THR C 1 44  ? 18.380  -17.292 -26.477 1.00 32.34 ? 67  THR C CB    1 
ATOM   2843 O OG1   . THR C 1 44  ? 19.628  -16.614 -26.675 1.00 32.52 ? 67  THR C OG1   1 
ATOM   2844 C CG2   . THR C 1 44  ? 17.314  -16.297 -26.060 1.00 30.04 ? 67  THR C CG2   1 
ATOM   2845 N N     . LYS C 1 45  ? 16.929  -20.072 -26.141 1.00 26.17 ? 68  LYS C N     1 
ATOM   2846 C CA    . LYS C 1 45  ? 15.727  -20.888 -26.023 1.00 31.94 ? 68  LYS C CA    1 
ATOM   2847 C C     . LYS C 1 45  ? 15.749  -21.734 -24.747 1.00 27.26 ? 68  LYS C C     1 
ATOM   2848 O O     . LYS C 1 45  ? 14.725  -21.877 -24.068 1.00 23.77 ? 68  LYS C O     1 
ATOM   2849 C CB    . LYS C 1 45  ? 15.605  -21.764 -27.272 1.00 29.51 ? 68  LYS C CB    1 
ATOM   2850 C CG    . LYS C 1 45  ? 14.417  -22.692 -27.307 1.00 34.95 ? 68  LYS C CG    1 
ATOM   2851 C CD    . LYS C 1 45  ? 14.626  -23.756 -28.376 1.00 36.26 ? 68  LYS C CD    1 
ATOM   2852 C CE    . LYS C 1 45  ? 13.305  -24.292 -28.926 1.00 50.68 ? 68  LYS C CE    1 
ATOM   2853 N NZ    . LYS C 1 45  ? 12.909  -23.563 -30.171 1.00 59.95 ? 68  LYS C NZ    1 
ATOM   2854 N N     . ALA C 1 46  ? 16.912  -22.293 -24.401 1.00 27.73 ? 69  ALA C N     1 
ATOM   2855 C CA    . ALA C 1 46  ? 17.012  -23.104 -23.186 1.00 27.42 ? 69  ALA C CA    1 
ATOM   2856 C C     . ALA C 1 46  ? 16.847  -22.264 -21.918 1.00 23.19 ? 69  ALA C C     1 
ATOM   2857 O O     . ALA C 1 46  ? 16.292  -22.749 -20.928 1.00 30.01 ? 69  ALA C O     1 
ATOM   2858 C CB    . ALA C 1 46  ? 18.348  -23.846 -23.177 1.00 24.37 ? 69  ALA C CB    1 
ATOM   2859 N N     . ILE C 1 47  ? 17.314  -21.017 -21.931 1.00 22.41 ? 70  ILE C N     1 
ATOM   2860 C CA    . ILE C 1 47  ? 17.206  -20.136 -20.765 1.00 25.43 ? 70  ILE C CA    1 
ATOM   2861 C C     . ILE C 1 47  ? 15.746  -19.783 -20.506 1.00 26.51 ? 70  ILE C C     1 
ATOM   2862 O O     . ILE C 1 47  ? 15.260  -19.827 -19.367 1.00 24.02 ? 70  ILE C O     1 
ATOM   2863 C CB    . ILE C 1 47  ? 18.067  -18.874 -20.980 1.00 24.36 ? 70  ILE C CB    1 
ATOM   2864 C CG1   . ILE C 1 47  ? 19.553  -19.250 -20.997 1.00 24.15 ? 70  ILE C CG1   1 
ATOM   2865 C CG2   . ILE C 1 47  ? 17.755  -17.792 -19.918 1.00 23.70 ? 70  ILE C CG2   1 
ATOM   2866 C CD1   . ILE C 1 47  ? 20.484  -18.098 -21.361 1.00 24.54 ? 70  ILE C CD1   1 
ATOM   2867 N N     . LEU C 1 48  ? 15.021  -19.439 -21.568 1.00 26.45 ? 71  LEU C N     1 
ATOM   2868 C CA    . LEU C 1 48  ? 13.594  -19.172 -21.434 1.00 29.30 ? 71  LEU C CA    1 
ATOM   2869 C C     . LEU C 1 48  ? 12.837  -20.423 -20.991 1.00 27.53 ? 71  LEU C C     1 
ATOM   2870 O O     . LEU C 1 48  ? 11.878  -20.330 -20.219 1.00 30.66 ? 71  LEU C O     1 
ATOM   2871 C CB    . LEU C 1 48  ? 13.046  -18.626 -22.757 1.00 27.27 ? 71  LEU C CB    1 
ATOM   2872 C CG    . LEU C 1 48  ? 13.664  -17.290 -23.223 1.00 28.58 ? 71  LEU C CG    1 
ATOM   2873 C CD1   . LEU C 1 48  ? 13.175  -16.884 -24.625 1.00 31.36 ? 71  LEU C CD1   1 
ATOM   2874 C CD2   . LEU C 1 48  ? 13.408  -16.170 -22.230 1.00 26.69 ? 71  LEU C CD2   1 
ATOM   2875 N N     . ALA C 1 49  ? 13.274  -21.605 -21.443 1.00 26.88 ? 72  ALA C N     1 
ATOM   2876 C CA    . ALA C 1 49  ? 12.638  -22.851 -21.017 1.00 28.83 ? 72  ALA C CA    1 
ATOM   2877 C C     . ALA C 1 49  ? 12.803  -23.128 -19.520 1.00 32.83 ? 72  ALA C C     1 
ATOM   2878 O O     . ALA C 1 49  ? 12.081  -23.972 -18.973 1.00 28.03 ? 72  ALA C O     1 
ATOM   2879 C CB    . ALA C 1 49  ? 13.190  -24.032 -21.820 1.00 25.07 ? 72  ALA C CB    1 
ATOM   2880 N N     . ARG C 1 50  ? 13.732  -22.453 -18.844 1.00 29.44 ? 73  ARG C N     1 
ATOM   2881 C CA    . ARG C 1 50  ? 13.771  -22.497 -17.383 1.00 29.94 ? 73  ARG C CA    1 
ATOM   2882 C C     . ARG C 1 50  ? 12.677  -21.665 -16.736 1.00 32.31 ? 73  ARG C C     1 
ATOM   2883 O O     . ARG C 1 50  ? 12.567  -21.669 -15.509 1.00 37.14 ? 73  ARG C O     1 
ATOM   2884 C CB    . ARG C 1 50  ? 15.126  -22.007 -16.856 1.00 30.41 ? 73  ARG C CB    1 
ATOM   2885 C CG    . ARG C 1 50  ? 16.303  -22.834 -17.333 1.00 28.66 ? 73  ARG C CG    1 
ATOM   2886 C CD    . ARG C 1 50  ? 16.157  -24.291 -16.916 1.00 31.85 ? 73  ARG C CD    1 
ATOM   2887 N NE    . ARG C 1 50  ? 15.541  -24.448 -15.605 1.00 28.74 ? 73  ARG C NE    1 
ATOM   2888 C CZ    . ARG C 1 50  ? 16.173  -24.267 -14.452 1.00 32.87 ? 73  ARG C CZ    1 
ATOM   2889 N NH1   . ARG C 1 50  ? 17.456  -23.918 -14.446 1.00 27.98 ? 73  ARG C NH1   1 
ATOM   2890 N NH2   . ARG C 1 50  ? 15.520  -24.436 -13.303 1.00 31.17 ? 73  ARG C NH2   1 
ATOM   2891 N N     . GLY C 1 51  ? 11.878  -20.946 -17.512 1.00 31.16 ? 74  GLY C N     1 
ATOM   2892 C CA    . GLY C 1 51  ? 10.869  -20.091 -16.934 1.00 33.08 ? 74  GLY C CA    1 
ATOM   2893 C C     . GLY C 1 51  ? 11.330  -18.684 -16.654 1.00 38.04 ? 74  GLY C C     1 
ATOM   2894 O O     . GLY C 1 51  ? 10.584  -17.910 -16.041 1.00 41.11 ? 74  GLY C O     1 
ATOM   2895 N N     . ILE C 1 52  ? 12.544  -18.329 -17.068 1.00 34.42 ? 75  ILE C N     1 
ATOM   2896 C CA    . ILE C 1 52  ? 12.982  -16.945 -16.991 1.00 34.61 ? 75  ILE C CA    1 
ATOM   2897 C C     . ILE C 1 52  ? 12.114  -16.117 -17.925 1.00 37.59 ? 75  ILE C C     1 
ATOM   2898 O O     . ILE C 1 52  ? 11.935  -16.465 -19.098 1.00 35.59 ? 75  ILE C O     1 
ATOM   2899 C CB    . ILE C 1 52  ? 14.471  -16.845 -17.354 1.00 30.87 ? 75  ILE C CB    1 
ATOM   2900 C CG1   . ILE C 1 52  ? 15.306  -17.635 -16.341 1.00 32.16 ? 75  ILE C CG1   1 
ATOM   2901 C CG2   . ILE C 1 52  ? 14.924  -15.410 -17.424 1.00 27.24 ? 75  ILE C CG2   1 
ATOM   2902 C CD1   . ILE C 1 52  ? 15.177  -17.116 -14.907 1.00 30.39 ? 75  ILE C CD1   1 
ATOM   2903 N N     . LYS C 1 53  ? 11.544  -15.034 -17.410 1.00 37.54 ? 76  LYS C N     1 
ATOM   2904 C CA    . LYS C 1 53  ? 10.748  -14.184 -18.279 1.00 38.49 ? 76  LYS C CA    1 
ATOM   2905 C C     . LYS C 1 53  ? 11.665  -13.457 -19.258 1.00 39.48 ? 76  LYS C C     1 
ATOM   2906 O O     . LYS C 1 53  ? 12.801  -13.115 -18.909 1.00 38.90 ? 76  LYS C O     1 
ATOM   2907 C CB    . LYS C 1 53  ? 9.917   -13.190 -17.474 1.00 39.51 ? 76  LYS C CB    1 
ATOM   2908 C CG    . LYS C 1 53  ? 8.780   -13.861 -16.685 1.00 52.75 ? 76  LYS C CG    1 
ATOM   2909 C CD    . LYS C 1 53  ? 7.803   -14.646 -17.604 1.00 56.76 ? 76  LYS C CD    1 
ATOM   2910 C CE    . LYS C 1 53  ? 7.460   -16.040 -17.028 1.00 58.20 ? 76  LYS C CE    1 
ATOM   2911 N NZ    . LYS C 1 53  ? 7.096   -17.076 -18.061 1.00 56.81 ? 76  LYS C NZ    1 
ATOM   2912 N N     . PRO C 1 54  ? 11.223  -13.246 -20.498 1.00 37.29 ? 77  PRO C N     1 
ATOM   2913 C CA    . PRO C 1 54  ? 12.116  -12.637 -21.497 1.00 37.74 ? 77  PRO C CA    1 
ATOM   2914 C C     . PRO C 1 54  ? 12.735  -11.327 -21.043 1.00 37.09 ? 77  PRO C C     1 
ATOM   2915 O O     . PRO C 1 54  ? 13.944  -11.138 -21.214 1.00 36.08 ? 77  PRO C O     1 
ATOM   2916 C CB    . PRO C 1 54  ? 11.198  -12.449 -22.711 1.00 37.31 ? 77  PRO C CB    1 
ATOM   2917 C CG    . PRO C 1 54  ? 10.148  -13.510 -22.550 1.00 38.99 ? 77  PRO C CG    1 
ATOM   2918 C CD    . PRO C 1 54  ? 9.907   -13.594 -21.068 1.00 39.82 ? 77  PRO C CD    1 
ATOM   2919 N N     . GLU C 1 55  ? 11.948  -10.427 -20.445 1.00 35.65 ? 78  GLU C N     1 
ATOM   2920 C CA    . GLU C 1 55  ? 12.484  -9.147  -19.993 1.00 40.88 ? 78  GLU C CA    1 
ATOM   2921 C C     . GLU C 1 55  ? 13.598  -9.309  -18.966 1.00 37.28 ? 78  GLU C C     1 
ATOM   2922 O O     . GLU C 1 55  ? 14.406  -8.392  -18.794 1.00 38.26 ? 78  GLU C O     1 
ATOM   2923 C CB    . GLU C 1 55  ? 11.372  -8.286  -19.394 1.00 41.12 ? 78  GLU C CB    1 
ATOM   2924 C CG    . GLU C 1 55  ? 10.340  -7.808  -20.393 1.00 47.47 ? 78  GLU C CG    1 
ATOM   2925 C CD    . GLU C 1 55  ? 9.334   -8.885  -20.760 1.00 49.38 ? 78  GLU C CD    1 
ATOM   2926 O OE1   . GLU C 1 55  ? 8.785   -8.819  -21.884 1.00 53.53 ? 78  GLU C OE1   1 
ATOM   2927 O OE2   . GLU C 1 55  ? 9.108   -9.802  -19.932 1.00 48.82 ? 78  GLU C OE2   1 
ATOM   2928 N N     . SER C 1 56  ? 13.656  -10.446 -18.276 1.00 36.78 ? 79  SER C N     1 
ATOM   2929 C CA    . SER C 1 56  ? 14.689  -10.705 -17.285 1.00 34.23 ? 79  SER C CA    1 
ATOM   2930 C C     . SER C 1 56  ? 15.932  -11.384 -17.877 1.00 33.29 ? 79  SER C C     1 
ATOM   2931 O O     . SER C 1 56  ? 16.778  -11.864 -17.118 1.00 34.23 ? 79  SER C O     1 
ATOM   2932 C CB    . SER C 1 56  ? 14.111  -11.558 -16.151 1.00 31.92 ? 79  SER C CB    1 
ATOM   2933 O OG    . SER C 1 56  ? 13.287  -10.776 -15.296 1.00 39.17 ? 79  SER C OG    1 
ATOM   2934 N N     . LEU C 1 57  ? 16.054  -11.459 -19.199 1.00 26.91 ? 80  LEU C N     1 
ATOM   2935 C CA    . LEU C 1 57  ? 17.239  -12.016 -19.843 1.00 28.39 ? 80  LEU C CA    1 
ATOM   2936 C C     . LEU C 1 57  ? 17.912  -10.912 -20.644 1.00 34.13 ? 80  LEU C C     1 
ATOM   2937 O O     . LEU C 1 57  ? 17.309  -10.369 -21.574 1.00 32.48 ? 80  LEU C O     1 
ATOM   2938 C CB    . LEU C 1 57  ? 16.892  -13.201 -20.754 1.00 26.45 ? 80  LEU C CB    1 
ATOM   2939 C CG    . LEU C 1 57  ? 18.049  -13.748 -21.611 1.00 30.50 ? 80  LEU C CG    1 
ATOM   2940 C CD1   . LEU C 1 57  ? 19.228  -14.229 -20.739 1.00 26.20 ? 80  LEU C CD1   1 
ATOM   2941 C CD2   . LEU C 1 57  ? 17.616  -14.850 -22.584 1.00 27.37 ? 80  LEU C CD2   1 
ATOM   2942 N N     . THR C 1 58  ? 19.146  -10.571 -20.272 1.00 28.97 ? 81  THR C N     1 
ATOM   2943 C CA    . THR C 1 58  ? 19.992  -9.676  -21.054 1.00 28.97 ? 81  THR C CA    1 
ATOM   2944 C C     . THR C 1 58  ? 21.034  -10.508 -21.788 1.00 31.04 ? 81  THR C C     1 
ATOM   2945 O O     . THR C 1 58  ? 21.744  -11.309 -21.168 1.00 28.54 ? 81  THR C O     1 
ATOM   2946 C CB    . THR C 1 58  ? 20.682  -8.641  -20.164 1.00 29.48 ? 81  THR C CB    1 
ATOM   2947 O OG1   . THR C 1 58  ? 19.695  -7.848  -19.492 1.00 31.97 ? 81  THR C OG1   1 
ATOM   2948 C CG2   . THR C 1 58  ? 21.609  -7.734  -20.991 1.00 31.20 ? 81  THR C CG2   1 
ATOM   2949 N N     . ALA C 1 59  ? 21.123  -10.325 -23.104 1.00 30.92 ? 82  ALA C N     1 
ATOM   2950 C CA    . ALA C 1 59  ? 22.032  -11.109 -23.928 1.00 30.36 ? 82  ALA C CA    1 
ATOM   2951 C C     . ALA C 1 59  ? 22.845  -10.172 -24.811 1.00 33.80 ? 82  ALA C C     1 
ATOM   2952 O O     . ALA C 1 59  ? 22.277  -9.339  -25.527 1.00 31.50 ? 82  ALA C O     1 
ATOM   2953 C CB    . ALA C 1 59  ? 21.257  -12.139 -24.769 1.00 27.13 ? 82  ALA C CB    1 
ATOM   2954 N N     . ILE C 1 60  ? 24.170  -10.300 -24.755 1.00 30.78 ? 83  ILE C N     1 
ATOM   2955 C CA    . ILE C 1 60  ? 25.077  -9.393  -25.452 1.00 30.76 ? 83  ILE C CA    1 
ATOM   2956 C C     . ILE C 1 60  ? 25.599  -10.088 -26.697 1.00 32.77 ? 83  ILE C C     1 
ATOM   2957 O O     . ILE C 1 60  ? 26.245  -11.137 -26.605 1.00 32.35 ? 83  ILE C O     1 
ATOM   2958 C CB    . ILE C 1 60  ? 26.236  -8.944  -24.549 1.00 34.42 ? 83  ILE C CB    1 
ATOM   2959 C CG1   . ILE C 1 60  ? 25.695  -8.248  -23.294 1.00 32.09 ? 83  ILE C CG1   1 
ATOM   2960 C CG2   . ILE C 1 60  ? 27.167  -8.026  -25.320 1.00 32.98 ? 83  ILE C CG2   1 
ATOM   2961 C CD1   . ILE C 1 60  ? 26.771  -7.838  -22.301 1.00 29.85 ? 83  ILE C CD1   1 
ATOM   2962 N N     . GLU C 1 61  ? 25.336  -9.496  -27.862 1.00 35.14 ? 84  GLU C N     1 
ATOM   2963 C CA    . GLU C 1 61  ? 25.716  -10.078 -29.143 1.00 33.54 ? 84  GLU C CA    1 
ATOM   2964 C C     . GLU C 1 61  ? 26.487  -9.050  -29.958 1.00 36.31 ? 84  GLU C C     1 
ATOM   2965 O O     . GLU C 1 61  ? 26.015  -7.924  -30.148 1.00 34.38 ? 84  GLU C O     1 
ATOM   2966 C CB    . GLU C 1 61  ? 24.479  -10.547 -29.918 1.00 36.83 ? 84  GLU C CB    1 
ATOM   2967 C CG    . GLU C 1 61  ? 24.775  -11.071 -31.311 1.00 34.16 ? 84  GLU C CG    1 
ATOM   2968 C CD    . GLU C 1 61  ? 25.851  -12.144 -31.326 1.00 39.69 ? 84  GLU C CD    1 
ATOM   2969 O OE1   . GLU C 1 61  ? 26.860  -11.973 -32.051 1.00 41.52 ? 84  GLU C OE1   1 
ATOM   2970 O OE2   . GLU C 1 61  ? 25.690  -13.169 -30.623 1.00 38.56 ? 84  GLU C OE2   1 
ATOM   2971 N N     . TYR C 1 62  ? 27.665  -9.443  -30.444 1.00 37.66 ? 85  TYR C N     1 
ATOM   2972 C CA    . TYR C 1 62  ? 28.523  -8.530  -31.193 1.00 40.59 ? 85  TYR C CA    1 
ATOM   2973 C C     . TYR C 1 62  ? 28.014  -8.319  -32.616 1.00 41.49 ? 85  TYR C C     1 
ATOM   2974 O O     . TYR C 1 62  ? 27.930  -7.180  -33.087 1.00 42.88 ? 85  TYR C O     1 
ATOM   2975 C CB    . TYR C 1 62  ? 29.959  -9.061  -31.214 1.00 39.59 ? 85  TYR C CB    1 
ATOM   2976 C CG    . TYR C 1 62  ? 30.952  -8.141  -31.897 1.00 42.07 ? 85  TYR C CG    1 
ATOM   2977 C CD1   . TYR C 1 62  ? 31.236  -6.885  -31.377 1.00 42.58 ? 85  TYR C CD1   1 
ATOM   2978 C CD2   . TYR C 1 62  ? 31.602  -8.533  -33.058 1.00 43.47 ? 85  TYR C CD2   1 
ATOM   2979 C CE1   . TYR C 1 62  ? 32.138  -6.039  -31.997 1.00 49.74 ? 85  TYR C CE1   1 
ATOM   2980 C CE2   . TYR C 1 62  ? 32.507  -7.696  -33.687 1.00 50.70 ? 85  TYR C CE2   1 
ATOM   2981 C CZ    . TYR C 1 62  ? 32.776  -6.452  -33.151 1.00 51.30 ? 85  TYR C CZ    1 
ATOM   2982 O OH    . TYR C 1 62  ? 33.680  -5.620  -33.776 1.00 56.91 ? 85  TYR C OH    1 
ATOM   2983 N N     . SER C 1 63  ? 27.661  -9.399  -33.308 1.00 41.29 ? 86  SER C N     1 
ATOM   2984 C CA    . SER C 1 63  ? 27.211  -9.301  -34.694 1.00 45.57 ? 86  SER C CA    1 
ATOM   2985 C C     . SER C 1 63  ? 25.866  -8.588  -34.772 1.00 44.37 ? 86  SER C C     1 
ATOM   2986 O O     . SER C 1 63  ? 24.883  -9.037  -34.174 1.00 39.40 ? 86  SER C O     1 
ATOM   2987 C CB    . SER C 1 63  ? 27.104  -10.687 -35.317 1.00 42.39 ? 86  SER C CB    1 
ATOM   2988 O OG    . SER C 1 63  ? 26.126  -10.691 -36.342 1.00 48.54 ? 86  SER C OG    1 
ATOM   2989 N N     . THR C 1 64  ? 25.824  -7.479  -35.519 1.00 43.08 ? 87  THR C N     1 
ATOM   2990 C CA    . THR C 1 64  ? 24.563  -6.772  -35.732 1.00 43.68 ? 87  THR C CA    1 
ATOM   2991 C C     . THR C 1 64  ? 23.574  -7.625  -36.517 1.00 41.88 ? 87  THR C C     1 
ATOM   2992 O O     . THR C 1 64  ? 22.366  -7.582  -36.259 1.00 44.84 ? 87  THR C O     1 
ATOM   2993 C CB    . THR C 1 64  ? 24.811  -5.446  -36.456 1.00 46.20 ? 87  THR C CB    1 
ATOM   2994 O OG1   . THR C 1 64  ? 25.869  -4.739  -35.805 1.00 44.41 ? 87  THR C OG1   1 
ATOM   2995 C CG2   . THR C 1 64  ? 23.547  -4.582  -36.447 1.00 43.79 ? 87  THR C CG2   1 
ATOM   2996 N N     . ASP C 1 65  ? 24.064  -8.409  -37.477 1.00 41.10 ? 88  ASP C N     1 
ATOM   2997 C CA    . ASP C 1 65  ? 23.184  -9.307  -38.217 1.00 43.81 ? 88  ASP C CA    1 
ATOM   2998 C C     . ASP C 1 65  ? 22.476  -10.279 -37.275 1.00 47.99 ? 88  ASP C C     1 
ATOM   2999 O O     . ASP C 1 65  ? 21.240  -10.304 -37.202 1.00 46.20 ? 88  ASP C O     1 
ATOM   3000 C CB    . ASP C 1 65  ? 23.982  -10.064 -39.280 1.00 50.24 ? 88  ASP C CB    1 
ATOM   3001 C CG    . ASP C 1 65  ? 24.141  -9.269  -40.570 1.00 62.73 ? 88  ASP C CG    1 
ATOM   3002 O OD1   . ASP C 1 65  ? 23.987  -8.026  -40.541 1.00 62.19 ? 88  ASP C OD1   1 
ATOM   3003 O OD2   . ASP C 1 65  ? 24.410  -9.892  -41.619 1.00 72.78 ? 88  ASP C OD2   1 
ATOM   3004 N N     . PHE C 1 66  ? 23.253  -11.094 -36.545 1.00 46.57 ? 89  PHE C N     1 
ATOM   3005 C CA    . PHE C 1 66  ? 22.674  -11.990 -35.541 1.00 45.42 ? 89  PHE C CA    1 
ATOM   3006 C C     . PHE C 1 66  ? 21.768  -11.231 -34.579 1.00 40.90 ? 89  PHE C C     1 
ATOM   3007 O O     . PHE C 1 66  ? 20.681  -11.706 -34.227 1.00 42.66 ? 89  PHE C O     1 
ATOM   3008 C CB    . PHE C 1 66  ? 23.783  -12.700 -34.762 1.00 41.99 ? 89  PHE C CB    1 
ATOM   3009 C CG    . PHE C 1 66  ? 24.342  -13.914 -35.450 1.00 47.52 ? 89  PHE C CG    1 
ATOM   3010 C CD1   . PHE C 1 66  ? 23.520  -14.773 -36.159 1.00 49.74 ? 89  PHE C CD1   1 
ATOM   3011 C CD2   . PHE C 1 66  ? 25.701  -14.202 -35.376 1.00 48.85 ? 89  PHE C CD2   1 
ATOM   3012 C CE1   . PHE C 1 66  ? 24.043  -15.898 -36.793 1.00 49.41 ? 89  PHE C CE1   1 
ATOM   3013 C CE2   . PHE C 1 66  ? 26.231  -15.320 -36.005 1.00 52.02 ? 89  PHE C CE2   1 
ATOM   3014 C CZ    . PHE C 1 66  ? 25.399  -16.172 -36.716 1.00 51.04 ? 89  PHE C CZ    1 
ATOM   3015 N N     . TYR C 1 67  ? 22.196  -10.040 -34.155 1.00 38.75 ? 90  TYR C N     1 
ATOM   3016 C CA    . TYR C 1 67  ? 21.389  -9.231  -33.248 1.00 40.61 ? 90  TYR C CA    1 
ATOM   3017 C C     . TYR C 1 67  ? 20.017  -8.927  -33.848 1.00 45.00 ? 90  TYR C C     1 
ATOM   3018 O O     . TYR C 1 67  ? 18.988  -9.061  -33.173 1.00 40.88 ? 90  TYR C O     1 
ATOM   3019 C CB    . TYR C 1 67  ? 22.146  -7.944  -32.915 1.00 37.35 ? 90  TYR C CB    1 
ATOM   3020 C CG    . TYR C 1 67  ? 21.346  -6.864  -32.227 1.00 41.20 ? 90  TYR C CG    1 
ATOM   3021 C CD1   . TYR C 1 67  ? 21.078  -6.928  -30.866 1.00 37.44 ? 90  TYR C CD1   1 
ATOM   3022 C CD2   . TYR C 1 67  ? 20.896  -5.755  -32.931 1.00 42.73 ? 90  TYR C CD2   1 
ATOM   3023 C CE1   . TYR C 1 67  ? 20.359  -5.930  -30.232 1.00 39.59 ? 90  TYR C CE1   1 
ATOM   3024 C CE2   . TYR C 1 67  ? 20.182  -4.754  -32.309 1.00 41.60 ? 90  TYR C CE2   1 
ATOM   3025 C CZ    . TYR C 1 67  ? 19.912  -4.846  -30.961 1.00 41.53 ? 90  TYR C CZ    1 
ATOM   3026 O OH    . TYR C 1 67  ? 19.196  -3.848  -30.342 1.00 41.45 ? 90  TYR C OH    1 
ATOM   3027 N N     . ASN C 1 68  ? 19.985  -8.523  -35.124 1.00 45.70 ? 91  ASN C N     1 
ATOM   3028 C CA    . ASN C 1 68  ? 18.719  -8.195  -35.778 1.00 43.15 ? 91  ASN C CA    1 
ATOM   3029 C C     . ASN C 1 68  ? 17.800  -9.410  -35.862 1.00 42.30 ? 91  ASN C C     1 
ATOM   3030 O O     . ASN C 1 68  ? 16.588  -9.301  -35.644 1.00 42.75 ? 91  ASN C O     1 
ATOM   3031 C CB    . ASN C 1 68  ? 18.984  -7.640  -37.180 1.00 45.88 ? 91  ASN C CB    1 
ATOM   3032 C CG    . ASN C 1 68  ? 19.528  -6.217  -37.165 1.00 47.08 ? 91  ASN C CG    1 
ATOM   3033 O OD1   . ASN C 1 68  ? 19.155  -5.394  -36.319 1.00 42.67 ? 91  ASN C OD1   1 
ATOM   3034 N ND2   . ASN C 1 68  ? 20.413  -5.919  -38.115 1.00 47.65 ? 91  ASN C ND2   1 
ATOM   3035 N N     . GLN C 1 69  ? 18.355  -10.575 -36.190 1.00 44.62 ? 92  GLN C N     1 
ATOM   3036 C CA    . GLN C 1 69  ? 17.543  -11.785 -36.238 1.00 45.45 ? 92  GLN C CA    1 
ATOM   3037 C C     . GLN C 1 69  ? 17.025  -12.163 -34.849 1.00 49.67 ? 92  GLN C C     1 
ATOM   3038 O O     . GLN C 1 69  ? 15.878  -12.608 -34.702 1.00 46.44 ? 92  GLN C O     1 
ATOM   3039 C CB    . GLN C 1 69  ? 18.352  -12.928 -36.844 1.00 45.49 ? 92  GLN C CB    1 
ATOM   3040 C CG    . GLN C 1 69  ? 17.569  -14.228 -36.976 1.00 53.73 ? 92  GLN C CG    1 
ATOM   3041 C CD    . GLN C 1 69  ? 16.301  -14.066 -37.799 1.00 59.72 ? 92  GLN C CD    1 
ATOM   3042 O OE1   . GLN C 1 69  ? 16.351  -13.654 -38.961 1.00 61.95 ? 92  GLN C OE1   1 
ATOM   3043 N NE2   . GLN C 1 69  ? 15.155  -14.386 -37.198 1.00 55.26 ? 92  GLN C NE2   1 
ATOM   3044 N N     . LEU C 1 70  ? 17.852  -11.981 -33.814 1.00 43.87 ? 93  LEU C N     1 
ATOM   3045 C CA    . LEU C 1 70  ? 17.445  -12.388 -32.473 1.00 41.78 ? 93  LEU C CA    1 
ATOM   3046 C C     . LEU C 1 70  ? 16.249  -11.576 -31.995 1.00 41.97 ? 93  LEU C C     1 
ATOM   3047 O O     . LEU C 1 70  ? 15.351  -12.112 -31.332 1.00 41.66 ? 93  LEU C O     1 
ATOM   3048 C CB    . LEU C 1 70  ? 18.629  -12.264 -31.505 1.00 39.29 ? 93  LEU C CB    1 
ATOM   3049 C CG    . LEU C 1 70  ? 19.665  -13.389 -31.677 1.00 39.21 ? 93  LEU C CG    1 
ATOM   3050 C CD1   . LEU C 1 70  ? 20.955  -13.084 -30.943 1.00 33.90 ? 93  LEU C CD1   1 
ATOM   3051 C CD2   . LEU C 1 70  ? 19.105  -14.747 -31.228 1.00 36.13 ? 93  LEU C CD2   1 
ATOM   3052 N N     . LEU C 1 71  ? 16.209  -10.284 -32.347 1.00 41.97 ? 94  LEU C N     1 
ATOM   3053 C CA    . LEU C 1 71  ? 15.064  -9.443  -32.005 1.00 43.96 ? 94  LEU C CA    1 
ATOM   3054 C C     . LEU C 1 71  ? 13.771  -9.964  -32.625 1.00 41.41 ? 94  LEU C C     1 
ATOM   3055 O O     . LEU C 1 71  ? 12.687  -9.773  -32.059 1.00 45.18 ? 94  LEU C O     1 
ATOM   3056 C CB    . LEU C 1 71  ? 15.320  -8.001  -32.452 1.00 42.31 ? 94  LEU C CB    1 
ATOM   3057 C CG    . LEU C 1 71  ? 16.260  -7.156  -31.588 1.00 45.24 ? 94  LEU C CG    1 
ATOM   3058 C CD1   . LEU C 1 71  ? 16.958  -6.081  -32.414 1.00 38.99 ? 94  LEU C CD1   1 
ATOM   3059 C CD2   . LEU C 1 71  ? 15.480  -6.526  -30.438 1.00 46.74 ? 94  LEU C CD2   1 
ATOM   3060 N N     . ARG C 1 72  ? 13.861  -10.621 -33.779 1.00 42.80 ? 95  ARG C N     1 
ATOM   3061 C CA    . ARG C 1 72  ? 12.674  -11.188 -34.410 1.00 48.86 ? 95  ARG C CA    1 
ATOM   3062 C C     . ARG C 1 72  ? 12.301  -12.534 -33.795 1.00 45.72 ? 95  ARG C C     1 
ATOM   3063 O O     . ARG C 1 72  ? 11.117  -12.811 -33.569 1.00 42.36 ? 95  ARG C O     1 
ATOM   3064 C CB    . ARG C 1 72  ? 12.902  -11.332 -35.920 1.00 48.21 ? 95  ARG C CB    1 
ATOM   3065 C CG    . ARG C 1 72  ? 12.739  -10.028 -36.708 1.00 55.20 ? 95  ARG C CG    1 
ATOM   3066 C CD    . ARG C 1 72  ? 13.832  -9.837  -37.762 1.00 60.34 ? 95  ARG C CD    1 
ATOM   3067 N NE    . ARG C 1 72  ? 13.700  -10.763 -38.887 1.00 67.50 ? 95  ARG C NE    1 
ATOM   3068 C CZ    . ARG C 1 72  ? 14.669  -11.027 -39.764 1.00 66.27 ? 95  ARG C CZ    1 
ATOM   3069 N NH1   . ARG C 1 72  ? 15.855  -10.436 -39.652 1.00 58.23 ? 95  ARG C NH1   1 
ATOM   3070 N NH2   . ARG C 1 72  ? 14.451  -11.884 -40.758 1.00 68.79 ? 95  ARG C NH2   1 
ATOM   3071 N N     . SER C 1 73  ? 13.302  -13.379 -33.520 1.00 44.69 ? 96  SER C N     1 
ATOM   3072 C CA    . SER C 1 73  ? 13.038  -14.729 -33.031 1.00 43.31 ? 96  SER C CA    1 
ATOM   3073 C C     . SER C 1 73  ? 12.582  -14.739 -31.576 1.00 42.41 ? 96  SER C C     1 
ATOM   3074 O O     . SER C 1 73  ? 11.825  -15.633 -31.179 1.00 42.91 ? 96  SER C O     1 
ATOM   3075 C CB    . SER C 1 73  ? 14.289  -15.597 -33.181 1.00 45.10 ? 96  SER C CB    1 
ATOM   3076 O OG    . SER C 1 73  ? 14.696  -15.702 -34.531 1.00 52.64 ? 96  SER C OG    1 
ATOM   3077 N N     . TYR C 1 74  ? 13.029  -13.778 -30.766 1.00 41.40 ? 97  TYR C N     1 
ATOM   3078 C CA    . TYR C 1 74  ? 12.781  -13.789 -29.321 1.00 37.63 ? 97  TYR C CA    1 
ATOM   3079 C C     . TYR C 1 74  ? 12.403  -12.396 -28.855 1.00 41.61 ? 97  TYR C C     1 
ATOM   3080 O O     . TYR C 1 74  ? 13.169  -11.726 -28.152 1.00 39.78 ? 97  TYR C O     1 
ATOM   3081 C CB    . TYR C 1 74  ? 14.005  -14.302 -28.563 1.00 38.00 ? 97  TYR C CB    1 
ATOM   3082 C CG    . TYR C 1 74  ? 14.365  -15.694 -28.967 1.00 34.30 ? 97  TYR C CG    1 
ATOM   3083 C CD1   . TYR C 1 74  ? 13.655  -16.779 -28.466 1.00 34.46 ? 97  TYR C CD1   1 
ATOM   3084 C CD2   . TYR C 1 74  ? 15.387  -15.931 -29.880 1.00 34.02 ? 97  TYR C CD2   1 
ATOM   3085 C CE1   . TYR C 1 74  ? 13.965  -18.067 -28.845 1.00 35.75 ? 97  TYR C CE1   1 
ATOM   3086 C CE2   . TYR C 1 74  ? 15.703  -17.213 -30.270 1.00 32.83 ? 97  TYR C CE2   1 
ATOM   3087 C CZ    . TYR C 1 74  ? 14.986  -18.281 -29.747 1.00 35.54 ? 97  TYR C CZ    1 
ATOM   3088 O OH    . TYR C 1 74  ? 15.284  -19.574 -30.123 1.00 39.07 ? 97  TYR C OH    1 
ATOM   3089 N N     . PRO C 1 75  ? 11.203  -11.936 -29.203 1.00 42.43 ? 98  PRO C N     1 
ATOM   3090 C CA    . PRO C 1 75  ? 10.771  -10.614 -28.755 1.00 39.46 ? 98  PRO C CA    1 
ATOM   3091 C C     . PRO C 1 75  ? 10.686  -10.582 -27.239 1.00 41.25 ? 98  PRO C C     1 
ATOM   3092 O O     . PRO C 1 75  ? 10.392  -11.591 -26.591 1.00 44.58 ? 98  PRO C O     1 
ATOM   3093 C CB    . PRO C 1 75  ? 9.385   -10.449 -29.395 1.00 48.49 ? 98  PRO C CB    1 
ATOM   3094 C CG    . PRO C 1 75  ? 9.197   -11.626 -30.296 1.00 48.33 ? 98  PRO C CG    1 
ATOM   3095 C CD    . PRO C 1 75  ? 10.100  -12.703 -29.797 1.00 46.48 ? 98  PRO C CD    1 
ATOM   3096 N N     . GLY C 1 76  ? 10.953  -9.410  -26.672 1.00 37.85 ? 99  GLY C N     1 
ATOM   3097 C CA    . GLY C 1 76  ? 10.911  -9.226  -25.243 1.00 40.30 ? 99  GLY C CA    1 
ATOM   3098 C C     . GLY C 1 76  ? 12.239  -9.407  -24.532 1.00 38.33 ? 99  GLY C C     1 
ATOM   3099 O O     . GLY C 1 76  ? 12.429  -8.832  -23.454 1.00 39.62 ? 99  GLY C O     1 
ATOM   3100 N N     . VAL C 1 77  ? 13.157  -10.198 -25.103 1.00 37.57 ? 100 VAL C N     1 
ATOM   3101 C CA    . VAL C 1 77  ? 14.478  -10.391 -24.505 1.00 35.98 ? 100 VAL C CA    1 
ATOM   3102 C C     . VAL C 1 77  ? 15.317  -9.130  -24.682 1.00 37.88 ? 100 VAL C C     1 
ATOM   3103 O O     . VAL C 1 77  ? 15.306  -8.497  -25.746 1.00 35.69 ? 100 VAL C O     1 
ATOM   3104 C CB    . VAL C 1 77  ? 15.179  -11.611 -25.130 1.00 37.79 ? 100 VAL C CB    1 
ATOM   3105 C CG1   . VAL C 1 77  ? 16.625  -11.694 -24.661 1.00 34.77 ? 100 VAL C CG1   1 
ATOM   3106 C CG2   . VAL C 1 77  ? 14.425  -12.917 -24.796 1.00 34.57 ? 100 VAL C CG2   1 
ATOM   3107 N N     . ASN C 1 78  ? 16.066  -8.765  -23.640 1.00 33.04 ? 101 ASN C N     1 
ATOM   3108 C CA    . ASN C 1 78  ? 16.883  -7.555  -23.660 1.00 35.93 ? 101 ASN C CA    1 
ATOM   3109 C C     . ASN C 1 78  ? 18.202  -7.854  -24.368 1.00 34.82 ? 101 ASN C C     1 
ATOM   3110 O O     . ASN C 1 78  ? 19.264  -7.984  -23.756 1.00 35.63 ? 101 ASN C O     1 
ATOM   3111 C CB    . ASN C 1 78  ? 17.103  -7.036  -22.243 1.00 37.83 ? 101 ASN C CB    1 
ATOM   3112 C CG    . ASN C 1 78  ? 17.806  -5.690  -22.218 1.00 40.96 ? 101 ASN C CG    1 
ATOM   3113 O OD1   . ASN C 1 78  ? 17.685  -4.900  -23.155 1.00 43.76 ? 101 ASN C OD1   1 
ATOM   3114 N ND2   . ASN C 1 78  ? 18.538  -5.418  -21.140 1.00 39.28 ? 101 ASN C ND2   1 
ATOM   3115 N N     . PHE C 1 79  ? 18.127  -7.964  -25.691 1.00 31.54 ? 102 PHE C N     1 
ATOM   3116 C CA    . PHE C 1 79  ? 19.330  -8.107  -26.495 1.00 31.92 ? 102 PHE C CA    1 
ATOM   3117 C C     . PHE C 1 79  ? 20.094  -6.790  -26.538 1.00 38.17 ? 102 PHE C C     1 
ATOM   3118 O O     . PHE C 1 79  ? 19.504  -5.706  -26.592 1.00 36.63 ? 102 PHE C O     1 
ATOM   3119 C CB    . PHE C 1 79  ? 18.981  -8.560  -27.912 1.00 35.13 ? 102 PHE C CB    1 
ATOM   3120 C CG    . PHE C 1 79  ? 18.504  -9.980  -27.988 1.00 38.12 ? 102 PHE C CG    1 
ATOM   3121 C CD1   . PHE C 1 79  ? 19.387  -11.038 -27.783 1.00 34.35 ? 102 PHE C CD1   1 
ATOM   3122 C CD2   . PHE C 1 79  ? 17.167  -10.268 -28.247 1.00 37.95 ? 102 PHE C CD2   1 
ATOM   3123 C CE1   . PHE C 1 79  ? 18.948  -12.362 -27.846 1.00 34.10 ? 102 PHE C CE1   1 
ATOM   3124 C CE2   . PHE C 1 79  ? 16.720  -11.587 -28.306 1.00 37.67 ? 102 PHE C CE2   1 
ATOM   3125 C CZ    . PHE C 1 79  ? 17.617  -12.639 -28.102 1.00 35.40 ? 102 PHE C CZ    1 
ATOM   3126 N N     . VAL C 1 80  ? 21.416  -6.881  -26.482 1.00 36.39 ? 103 VAL C N     1 
ATOM   3127 C CA    . VAL C 1 80  ? 22.279  -5.711  -26.571 1.00 38.13 ? 103 VAL C CA    1 
ATOM   3128 C C     . VAL C 1 80  ? 23.313  -5.992  -27.644 1.00 39.02 ? 103 VAL C C     1 
ATOM   3129 O O     . VAL C 1 80  ? 23.945  -7.057  -27.642 1.00 35.84 ? 103 VAL C O     1 
ATOM   3130 C CB    . VAL C 1 80  ? 22.953  -5.372  -25.227 1.00 37.24 ? 103 VAL C CB    1 
ATOM   3131 C CG1   . VAL C 1 80  ? 23.869  -4.162  -25.370 1.00 39.38 ? 103 VAL C CG1   1 
ATOM   3132 C CG2   . VAL C 1 80  ? 21.909  -5.114  -24.159 1.00 36.26 ? 103 VAL C CG2   1 
ATOM   3133 N N     . ASN C 1 81  ? 23.466  -5.050  -28.568 1.00 39.38 ? 104 ASN C N     1 
ATOM   3134 C CA    . ASN C 1 81  ? 24.393  -5.188  -29.684 1.00 37.85 ? 104 ASN C CA    1 
ATOM   3135 C C     . ASN C 1 81  ? 25.710  -4.531  -29.282 1.00 40.23 ? 104 ASN C C     1 
ATOM   3136 O O     . ASN C 1 81  ? 25.786  -3.300  -29.175 1.00 41.90 ? 104 ASN C O     1 
ATOM   3137 C CB    . ASN C 1 81  ? 23.798  -4.541  -30.934 1.00 42.17 ? 104 ASN C CB    1 
ATOM   3138 C CG    . ASN C 1 81  ? 24.515  -4.936  -32.207 1.00 40.88 ? 104 ASN C CG    1 
ATOM   3139 O OD1   . ASN C 1 81  ? 25.288  -5.897  -32.242 1.00 42.07 ? 104 ASN C OD1   1 
ATOM   3140 N ND2   . ASN C 1 81  ? 24.255  -4.194  -33.267 1.00 42.06 ? 104 ASN C ND2   1 
ATOM   3141 N N     . GLY C 1 82  ? 26.738  -5.340  -29.049 1.00 36.71 ? 105 GLY C N     1 
ATOM   3142 C CA    . GLY C 1 82  ? 27.999  -4.794  -28.589 1.00 40.88 ? 105 GLY C CA    1 
ATOM   3143 C C     . GLY C 1 82  ? 28.969  -5.872  -28.142 1.00 40.68 ? 105 GLY C C     1 
ATOM   3144 O O     . GLY C 1 82  ? 28.746  -7.074  -28.333 1.00 36.57 ? 105 GLY C O     1 
ATOM   3145 N N     . ASP C 1 83  ? 30.053  -5.396  -27.526 1.00 41.33 ? 106 ASP C N     1 
ATOM   3146 C CA    . ASP C 1 83  ? 31.218  -6.195  -27.154 1.00 38.89 ? 106 ASP C CA    1 
ATOM   3147 C C     . ASP C 1 83  ? 31.105  -6.603  -25.687 1.00 35.79 ? 106 ASP C C     1 
ATOM   3148 O O     . ASP C 1 83  ? 31.067  -5.738  -24.801 1.00 31.63 ? 106 ASP C O     1 
ATOM   3149 C CB    . ASP C 1 83  ? 32.492  -5.375  -27.386 1.00 39.80 ? 106 ASP C CB    1 
ATOM   3150 C CG    . ASP C 1 83  ? 33.771  -6.193  -27.250 1.00 43.66 ? 106 ASP C CG    1 
ATOM   3151 O OD1   . ASP C 1 83  ? 33.718  -7.376  -26.831 1.00 40.60 ? 106 ASP C OD1   1 
ATOM   3152 O OD2   . ASP C 1 83  ? 34.849  -5.624  -27.551 1.00 46.76 ? 106 ASP C OD2   1 
ATOM   3153 N N     . ALA C 1 84  ? 31.069  -7.915  -25.428 1.00 33.20 ? 107 ALA C N     1 
ATOM   3154 C CA    . ALA C 1 84  ? 30.970  -8.379  -24.046 1.00 34.16 ? 107 ALA C CA    1 
ATOM   3155 C C     . ALA C 1 84  ? 32.199  -8.000  -23.221 1.00 36.36 ? 107 ALA C C     1 
ATOM   3156 O O     . ALA C 1 84  ? 32.101  -7.906  -21.990 1.00 33.00 ? 107 ALA C O     1 
ATOM   3157 C CB    . ALA C 1 84  ? 30.760  -9.899  -24.011 1.00 32.99 ? 107 ALA C CB    1 
ATOM   3158 N N     . PHE C 1 85  ? 33.349  -7.773  -23.866 1.00 31.84 ? 108 PHE C N     1 
ATOM   3159 C CA    . PHE C 1 85  ? 34.548  -7.368  -23.146 1.00 33.80 ? 108 PHE C CA    1 
ATOM   3160 C C     . PHE C 1 85  ? 34.511  -5.909  -22.696 1.00 37.86 ? 108 PHE C C     1 
ATOM   3161 O O     . PHE C 1 85  ? 35.388  -5.497  -21.928 1.00 33.23 ? 108 PHE C O     1 
ATOM   3162 C CB    . PHE C 1 85  ? 35.784  -7.619  -24.006 1.00 33.85 ? 108 PHE C CB    1 
ATOM   3163 C CG    . PHE C 1 85  ? 36.267  -9.039  -23.962 1.00 33.95 ? 108 PHE C CG    1 
ATOM   3164 C CD1   . PHE C 1 85  ? 35.674  -10.014 -24.756 1.00 30.47 ? 108 PHE C CD1   1 
ATOM   3165 C CD2   . PHE C 1 85  ? 37.302  -9.408  -23.111 1.00 27.20 ? 108 PHE C CD2   1 
ATOM   3166 C CE1   . PHE C 1 85  ? 36.123  -11.335 -24.718 1.00 30.45 ? 108 PHE C CE1   1 
ATOM   3167 C CE2   . PHE C 1 85  ? 37.755  -10.727 -23.063 1.00 24.12 ? 108 PHE C CE2   1 
ATOM   3168 C CZ    . PHE C 1 85  ? 37.170  -11.690 -23.871 1.00 27.61 ? 108 PHE C CZ    1 
ATOM   3169 N N     . ASP C 1 86  ? 33.520  -5.133  -23.131 1.00 33.78 ? 109 ASP C N     1 
ATOM   3170 C CA    . ASP C 1 86  ? 33.297  -3.773  -22.646 1.00 39.35 ? 109 ASP C CA    1 
ATOM   3171 C C     . ASP C 1 86  ? 31.978  -3.742  -21.874 1.00 39.17 ? 109 ASP C C     1 
ATOM   3172 O O     . ASP C 1 86  ? 30.954  -3.271  -22.368 1.00 41.73 ? 109 ASP C O     1 
ATOM   3173 C CB    . ASP C 1 86  ? 33.291  -2.785  -23.803 1.00 42.53 ? 109 ASP C CB    1 
ATOM   3174 C CG    . ASP C 1 86  ? 33.493  -1.348  -23.343 1.00 46.04 ? 109 ASP C CG    1 
ATOM   3175 O OD1   . ASP C 1 86  ? 33.403  -1.084  -22.118 1.00 40.67 ? 109 ASP C OD1   1 
ATOM   3176 O OD2   . ASP C 1 86  ? 33.745  -0.485  -24.210 1.00 50.38 ? 109 ASP C OD2   1 
ATOM   3177 N N     . LEU C 1 87  ? 32.019  -4.224  -20.631 1.00 40.89 ? 110 LEU C N     1 
ATOM   3178 C CA    . LEU C 1 87  ? 30.795  -4.329  -19.837 1.00 38.54 ? 110 LEU C CA    1 
ATOM   3179 C C     . LEU C 1 87  ? 30.214  -2.962  -19.493 1.00 41.60 ? 110 LEU C C     1 
ATOM   3180 O O     . LEU C 1 87  ? 28.991  -2.804  -19.433 1.00 43.76 ? 110 LEU C O     1 
ATOM   3181 C CB    . LEU C 1 87  ? 31.066  -5.113  -18.554 1.00 38.77 ? 110 LEU C CB    1 
ATOM   3182 C CG    . LEU C 1 87  ? 31.212  -6.624  -18.648 1.00 36.12 ? 110 LEU C CG    1 
ATOM   3183 C CD1   . LEU C 1 87  ? 31.447  -7.198  -17.252 1.00 32.49 ? 110 LEU C CD1   1 
ATOM   3184 C CD2   . LEU C 1 87  ? 29.991  -7.252  -19.314 1.00 35.48 ? 110 LEU C CD2   1 
ATOM   3185 N N     . ASP C 1 88  ? 31.067  -1.967  -19.232 1.00 43.32 ? 111 ASP C N     1 
ATOM   3186 C CA    . ASP C 1 88  ? 30.555  -0.642  -18.896 1.00 44.55 ? 111 ASP C CA    1 
ATOM   3187 C C     . ASP C 1 88  ? 29.803  -0.030  -20.071 1.00 44.00 ? 111 ASP C C     1 
ATOM   3188 O O     . ASP C 1 88  ? 28.740  0.572   -19.892 1.00 42.95 ? 111 ASP C O     1 
ATOM   3189 C CB    . ASP C 1 88  ? 31.698  0.268   -18.448 1.00 46.85 ? 111 ASP C CB    1 
ATOM   3190 C CG    . ASP C 1 88  ? 32.183  -0.052  -17.041 1.00 53.61 ? 111 ASP C CG    1 
ATOM   3191 O OD1   . ASP C 1 88  ? 31.571  -0.911  -16.369 1.00 49.43 ? 111 ASP C OD1   1 
ATOM   3192 O OD2   . ASP C 1 88  ? 33.184  0.556   -16.605 1.00 59.80 ? 111 ASP C OD2   1 
ATOM   3193 N N     . ALA C 1 89  ? 30.327  -0.191  -21.286 1.00 41.94 ? 112 ALA C N     1 
ATOM   3194 C CA    . ALA C 1 89  ? 29.617  0.303   -22.460 1.00 38.61 ? 112 ALA C CA    1 
ATOM   3195 C C     . ALA C 1 89  ? 28.298  -0.436  -22.676 1.00 44.98 ? 112 ALA C C     1 
ATOM   3196 O O     . ALA C 1 89  ? 27.297  0.174   -23.067 1.00 46.51 ? 112 ALA C O     1 
ATOM   3197 C CB    . ALA C 1 89  ? 30.503  0.173   -23.695 1.00 41.23 ? 112 ALA C CB    1 
ATOM   3198 N N     . THR C 1 90  ? 28.272  -1.751  -22.439 1.00 41.12 ? 113 THR C N     1 
ATOM   3199 C CA    . THR C 1 90  ? 27.099  -2.535  -22.809 1.00 39.12 ? 113 THR C CA    1 
ATOM   3200 C C     . THR C 1 90  ? 26.093  -2.693  -21.673 1.00 42.68 ? 113 THR C C     1 
ATOM   3201 O O     . THR C 1 90  ? 24.886  -2.716  -21.927 1.00 42.75 ? 113 THR C O     1 
ATOM   3202 C CB    . THR C 1 90  ? 27.519  -3.922  -23.313 1.00 40.31 ? 113 THR C CB    1 
ATOM   3203 O OG1   . THR C 1 90  ? 28.199  -4.620  -22.268 1.00 42.01 ? 113 THR C OG1   1 
ATOM   3204 C CG2   . THR C 1 90  ? 28.439  -3.808  -24.517 1.00 40.51 ? 113 THR C CG2   1 
ATOM   3205 N N     . LEU C 1 91  ? 26.543  -2.828  -20.427 1.00 41.05 ? 114 LEU C N     1 
ATOM   3206 C CA    . LEU C 1 91  ? 25.618  -2.952  -19.307 1.00 40.09 ? 114 LEU C CA    1 
ATOM   3207 C C     . LEU C 1 91  ? 25.496  -1.683  -18.480 1.00 46.13 ? 114 LEU C C     1 
ATOM   3208 O O     . LEU C 1 91  ? 24.615  -1.614  -17.614 1.00 52.18 ? 114 LEU C O     1 
ATOM   3209 C CB    . LEU C 1 91  ? 26.038  -4.089  -18.368 1.00 38.03 ? 114 LEU C CB    1 
ATOM   3210 C CG    . LEU C 1 91  ? 26.014  -5.517  -18.882 1.00 38.55 ? 114 LEU C CG    1 
ATOM   3211 C CD1   . LEU C 1 91  ? 26.527  -6.431  -17.795 1.00 34.15 ? 114 LEU C CD1   1 
ATOM   3212 C CD2   . LEU C 1 91  ? 24.611  -5.894  -19.311 1.00 33.82 ? 114 LEU C CD2   1 
ATOM   3213 N N     . GLY C 1 92  ? 26.341  -0.685  -18.722 1.00 43.50 ? 115 GLY C N     1 
ATOM   3214 C CA    . GLY C 1 92  ? 26.501  0.411   -17.793 1.00 51.27 ? 115 GLY C CA    1 
ATOM   3215 C C     . GLY C 1 92  ? 27.466  0.041   -16.680 1.00 51.66 ? 115 GLY C C     1 
ATOM   3216 O O     . GLY C 1 92  ? 27.806  -1.127  -16.460 1.00 47.32 ? 115 GLY C O     1 
ATOM   3217 N N     . GLU C 1 93  ? 27.925  1.066   -15.964 1.00 49.37 ? 116 GLU C N     1 
ATOM   3218 C CA    . GLU C 1 93  ? 28.825  0.833   -14.843 1.00 51.86 ? 116 GLU C CA    1 
ATOM   3219 C C     . GLU C 1 93  ? 28.078  0.177   -13.685 1.00 50.80 ? 116 GLU C C     1 
ATOM   3220 O O     . GLU C 1 93  ? 26.892  0.432   -13.454 1.00 50.00 ? 116 GLU C O     1 
ATOM   3221 C CB    . GLU C 1 93  ? 29.469  2.140   -14.386 1.00 55.35 ? 116 GLU C CB    1 
ATOM   3222 C CG    . GLU C 1 93  ? 30.718  2.504   -15.173 1.00 61.15 ? 116 GLU C CG    1 
ATOM   3223 C CD    . GLU C 1 93  ? 31.110  3.961   -15.011 1.00 71.03 ? 116 GLU C CD    1 
ATOM   3224 O OE1   . GLU C 1 93  ? 30.637  4.603   -14.043 1.00 70.79 ? 116 GLU C OE1   1 
ATOM   3225 O OE2   . GLU C 1 93  ? 31.885  4.464   -15.856 1.00 73.19 ? 116 GLU C OE2   1 
ATOM   3226 N N     . HIS C 1 94  ? 28.786  -0.689  -12.957 1.00 50.04 ? 117 HIS C N     1 
ATOM   3227 C CA    . HIS C 1 94  ? 28.143  -1.502  -11.929 1.00 49.65 ? 117 HIS C CA    1 
ATOM   3228 C C     . HIS C 1 94  ? 27.671  -0.617  -10.781 1.00 48.62 ? 117 HIS C C     1 
ATOM   3229 O O     . HIS C 1 94  ? 28.486  -0.015  -10.070 1.00 44.97 ? 117 HIS C O     1 
ATOM   3230 C CB    . HIS C 1 94  ? 29.083  -2.586  -11.415 1.00 46.70 ? 117 HIS C CB    1 
ATOM   3231 C CG    . HIS C 1 94  ? 28.384  -3.625  -10.593 1.00 48.91 ? 117 HIS C CG    1 
ATOM   3232 N ND1   . HIS C 1 94  ? 28.818  -4.007  -9.341  1.00 48.42 ? 117 HIS C ND1   1 
ATOM   3233 C CD2   . HIS C 1 94  ? 27.261  -4.345  -10.837 1.00 44.96 ? 117 HIS C CD2   1 
ATOM   3234 C CE1   . HIS C 1 94  ? 28.003  -4.928  -8.855  1.00 44.21 ? 117 HIS C CE1   1 
ATOM   3235 N NE2   . HIS C 1 94  ? 27.051  -5.152  -9.744  1.00 45.37 ? 117 HIS C NE2   1 
ATOM   3236 N N     . LYS C 1 95  ? 26.352  -0.538  -10.606 1.00 47.29 ? 118 LYS C N     1 
ATOM   3237 C CA    . LYS C 1 95  ? 25.739  0.235   -9.534  1.00 52.14 ? 118 LYS C CA    1 
ATOM   3238 C C     . LYS C 1 95  ? 25.132  -0.652  -8.458  1.00 52.15 ? 118 LYS C C     1 
ATOM   3239 O O     . LYS C 1 95  ? 24.568  -0.133  -7.485  1.00 45.83 ? 118 LYS C O     1 
ATOM   3240 C CB    . LYS C 1 95  ? 24.666  1.175   -10.102 1.00 46.54 ? 118 LYS C CB    1 
ATOM   3241 C CG    . LYS C 1 95  ? 25.208  2.306   -10.979 1.00 52.57 ? 118 LYS C CG    1 
ATOM   3242 C CD    . LYS C 1 95  ? 26.394  3.008   -10.322 1.00 55.19 ? 118 LYS C CD    1 
ATOM   3243 C CE    . LYS C 1 95  ? 26.231  4.519   -10.332 1.00 58.36 ? 118 LYS C CE    1 
ATOM   3244 N NZ    . LYS C 1 95  ? 25.854  5.056   -11.673 1.00 60.88 ? 118 LYS C NZ    1 
ATOM   3245 N N     . GLY C 1 96  ? 25.241  -1.973  -8.606  1.00 45.30 ? 119 GLY C N     1 
ATOM   3246 C CA    . GLY C 1 96  ? 24.696  -2.905  -7.643  1.00 42.20 ? 119 GLY C CA    1 
ATOM   3247 C C     . GLY C 1 96  ? 23.670  -3.848  -8.238  1.00 43.11 ? 119 GLY C C     1 
ATOM   3248 O O     . GLY C 1 96  ? 23.022  -4.593  -7.498  1.00 42.30 ? 119 GLY C O     1 
ATOM   3249 N N     . GLN C 1 97  ? 23.507  -3.837  -9.564  1.00 43.26 ? 120 GLN C N     1 
ATOM   3250 C CA    . GLN C 1 97  ? 22.603  -4.783  -10.212 1.00 44.89 ? 120 GLN C CA    1 
ATOM   3251 C C     . GLN C 1 97  ? 23.256  -6.160  -10.272 1.00 40.41 ? 120 GLN C C     1 
ATOM   3252 O O     . GLN C 1 97  ? 24.306  -6.333  -10.904 1.00 42.27 ? 120 GLN C O     1 
ATOM   3253 C CB    . GLN C 1 97  ? 22.220  -4.323  -11.619 1.00 43.14 ? 120 GLN C CB    1 
ATOM   3254 C CG    . GLN C 1 97  ? 21.382  -5.381  -12.360 1.00 46.45 ? 120 GLN C CG    1 
ATOM   3255 C CD    . GLN C 1 97  ? 21.457  -5.279  -13.880 1.00 53.10 ? 120 GLN C CD    1 
ATOM   3256 O OE1   . GLN C 1 97  ? 22.488  -4.888  -14.445 1.00 54.26 ? 120 GLN C OE1   1 
ATOM   3257 N NE2   . GLN C 1 97  ? 20.358  -5.644  -14.553 1.00 51.78 ? 120 GLN C NE2   1 
ATOM   3258 N N     . MET C 1 98  ? 22.619  -7.141  -9.640  1.00 38.93 ? 121 MET C N     1 
ATOM   3259 C CA    . MET C 1 98  ? 23.102  -8.513  -9.597  1.00 31.55 ? 121 MET C CA    1 
ATOM   3260 C C     . MET C 1 98  ? 22.388  -9.359  -10.643 1.00 33.28 ? 121 MET C C     1 
ATOM   3261 O O     . MET C 1 98  ? 21.177  -9.224  -10.839 1.00 35.33 ? 121 MET C O     1 
ATOM   3262 C CB    . MET C 1 98  ? 22.865  -9.131  -8.221  1.00 30.46 ? 121 MET C CB    1 
ATOM   3263 C CG    . MET C 1 98  ? 23.718  -8.592  -7.117  1.00 37.07 ? 121 MET C CG    1 
ATOM   3264 S SD    . MET C 1 98  ? 25.414  -9.196  -7.235  1.00 49.98 ? 121 MET C SD    1 
ATOM   3265 C CE    . MET C 1 98  ? 26.174  -7.667  -7.712  1.00 30.92 ? 121 MET C CE    1 
ATOM   3266 N N     . PHE C 1 99  ? 23.134  -10.247 -11.293 1.00 27.03 ? 122 PHE C N     1 
ATOM   3267 C CA    . PHE C 1 99  ? 22.552  -11.285 -12.135 1.00 28.24 ? 122 PHE C CA    1 
ATOM   3268 C C     . PHE C 1 99  ? 22.554  -12.603 -11.379 1.00 26.77 ? 122 PHE C C     1 
ATOM   3269 O O     . PHE C 1 99  ? 23.391  -12.828 -10.500 1.00 25.06 ? 122 PHE C O     1 
ATOM   3270 C CB    . PHE C 1 99  ? 23.317  -11.436 -13.445 1.00 23.87 ? 122 PHE C CB    1 
ATOM   3271 C CG    . PHE C 1 99  ? 23.161  -10.264 -14.362 1.00 27.26 ? 122 PHE C CG    1 
ATOM   3272 C CD1   . PHE C 1 99  ? 22.096  -10.199 -15.251 1.00 26.07 ? 122 PHE C CD1   1 
ATOM   3273 C CD2   . PHE C 1 99  ? 24.061  -9.210  -14.320 1.00 32.49 ? 122 PHE C CD2   1 
ATOM   3274 C CE1   . PHE C 1 99  ? 21.944  -9.098  -16.098 1.00 30.76 ? 122 PHE C CE1   1 
ATOM   3275 C CE2   . PHE C 1 99  ? 23.918  -8.117  -15.164 1.00 30.91 ? 122 PHE C CE2   1 
ATOM   3276 C CZ    . PHE C 1 99  ? 22.862  -8.060  -16.053 1.00 30.75 ? 122 PHE C CZ    1 
ATOM   3277 N N     . ASP C 1 100 ? 21.587  -13.462 -11.705 1.00 23.60 ? 123 ASP C N     1 
ATOM   3278 C CA    . ASP C 1 100 ? 21.536  -14.772 -11.067 1.00 26.12 ? 123 ASP C CA    1 
ATOM   3279 C C     . ASP C 1 100 ? 22.755  -15.606 -11.427 1.00 25.77 ? 123 ASP C C     1 
ATOM   3280 O O     . ASP C 1 100 ? 23.260  -16.369 -10.598 1.00 25.28 ? 123 ASP C O     1 
ATOM   3281 C CB    . ASP C 1 100 ? 20.269  -15.525 -11.475 1.00 26.37 ? 123 ASP C CB    1 
ATOM   3282 C CG    . ASP C 1 100 ? 20.245  -16.942 -10.921 1.00 28.63 ? 123 ASP C CG    1 
ATOM   3283 O OD1   . ASP C 1 100 ? 19.978  -17.086 -9.714  1.00 28.24 ? 123 ASP C OD1   1 
ATOM   3284 O OD2   . ASP C 1 100 ? 20.518  -17.905 -11.680 1.00 26.83 ? 123 ASP C OD2   1 
ATOM   3285 N N     . SER C 1 101 ? 23.211  -15.498 -12.672 1.00 20.95 ? 124 SER C N     1 
ATOM   3286 C CA    . SER C 1 101 ? 24.286  -16.315 -13.224 1.00 23.66 ? 124 SER C CA    1 
ATOM   3287 C C     . SER C 1 101 ? 24.571  -15.782 -14.621 1.00 23.50 ? 124 SER C C     1 
ATOM   3288 O O     . SER C 1 101 ? 23.778  -15.023 -15.183 1.00 22.09 ? 124 SER C O     1 
ATOM   3289 C CB    . SER C 1 101 ? 23.908  -17.796 -13.271 1.00 25.34 ? 124 SER C CB    1 
ATOM   3290 O OG    . SER C 1 101 ? 22.582  -17.960 -13.760 1.00 26.70 ? 124 SER C OG    1 
ATOM   3291 N N     . VAL C 1 102 ? 25.709  -16.182 -15.179 1.00 23.02 ? 125 VAL C N     1 
ATOM   3292 C CA    . VAL C 1 102 ? 26.112  -15.776 -16.522 1.00 22.54 ? 125 VAL C CA    1 
ATOM   3293 C C     . VAL C 1 102 ? 26.330  -17.026 -17.365 1.00 24.25 ? 125 VAL C C     1 
ATOM   3294 O O     . VAL C 1 102 ? 26.996  -17.965 -16.919 1.00 22.00 ? 125 VAL C O     1 
ATOM   3295 C CB    . VAL C 1 102 ? 27.386  -14.916 -16.494 1.00 22.89 ? 125 VAL C CB    1 
ATOM   3296 C CG1   . VAL C 1 102 ? 27.735  -14.437 -17.907 1.00 21.10 ? 125 VAL C CG1   1 
ATOM   3297 C CG2   . VAL C 1 102 ? 27.213  -13.743 -15.538 1.00 19.04 ? 125 VAL C CG2   1 
ATOM   3298 N N     . ILE C 1 103 ? 25.780  -17.030 -18.581 1.00 21.83 ? 126 ILE C N     1 
ATOM   3299 C CA    . ILE C 1 103 ? 25.925  -18.138 -19.523 1.00 21.34 ? 126 ILE C CA    1 
ATOM   3300 C C     . ILE C 1 103 ? 26.653  -17.601 -20.747 1.00 23.26 ? 126 ILE C C     1 
ATOM   3301 O O     . ILE C 1 103 ? 26.131  -16.718 -21.432 1.00 26.52 ? 126 ILE C O     1 
ATOM   3302 C CB    . ILE C 1 103 ? 24.565  -18.721 -19.937 1.00 22.68 ? 126 ILE C CB    1 
ATOM   3303 C CG1   . ILE C 1 103 ? 23.548  -18.677 -18.784 1.00 29.63 ? 126 ILE C CG1   1 
ATOM   3304 C CG2   . ILE C 1 103 ? 24.745  -20.097 -20.498 1.00 19.92 ? 126 ILE C CG2   1 
ATOM   3305 C CD1   . ILE C 1 103 ? 23.812  -19.668 -17.685 1.00 25.92 ? 126 ILE C CD1   1 
ATOM   3306 N N     . SER C 1 104 ? 27.847  -18.122 -21.031 1.00 20.02 ? 127 SER C N     1 
ATOM   3307 C CA    . SER C 1 104 ? 28.719  -17.510 -22.024 1.00 22.39 ? 127 SER C CA    1 
ATOM   3308 C C     . SER C 1 104 ? 29.119  -18.502 -23.108 1.00 24.84 ? 127 SER C C     1 
ATOM   3309 O O     . SER C 1 104 ? 29.632  -19.591 -22.813 1.00 26.54 ? 127 SER C O     1 
ATOM   3310 C CB    . SER C 1 104 ? 29.968  -16.920 -21.370 1.00 27.36 ? 127 SER C CB    1 
ATOM   3311 O OG    . SER C 1 104 ? 30.920  -16.585 -22.363 1.00 26.36 ? 127 SER C OG    1 
ATOM   3312 N N     . ALA C 1 105 ? 28.907  -18.107 -24.367 1.00 24.03 ? 128 ALA C N     1 
ATOM   3313 C CA    . ALA C 1 105 ? 29.403  -18.864 -25.509 1.00 26.11 ? 128 ALA C CA    1 
ATOM   3314 C C     . ALA C 1 105 ? 30.367  -18.038 -26.354 1.00 33.90 ? 128 ALA C C     1 
ATOM   3315 O O     . ALA C 1 105 ? 30.682  -18.427 -27.486 1.00 36.76 ? 128 ALA C O     1 
ATOM   3316 C CB    . ALA C 1 105 ? 28.240  -19.370 -26.367 1.00 30.06 ? 128 ALA C CB    1 
ATOM   3317 N N     . VAL C 1 106 ? 30.825  -16.905 -25.837 1.00 33.87 ? 129 VAL C N     1 
ATOM   3318 C CA    . VAL C 1 106 ? 31.822  -16.075 -26.525 1.00 35.67 ? 129 VAL C CA    1 
ATOM   3319 C C     . VAL C 1 106 ? 33.139  -16.843 -26.602 1.00 35.20 ? 129 VAL C C     1 
ATOM   3320 O O     . VAL C 1 106 ? 33.632  -17.320 -25.563 1.00 31.65 ? 129 VAL C O     1 
ATOM   3321 C CB    . VAL C 1 106 ? 31.999  -14.747 -25.790 1.00 31.79 ? 129 VAL C CB    1 
ATOM   3322 C CG1   . VAL C 1 106 ? 33.181  -13.975 -26.368 1.00 38.80 ? 129 VAL C CG1   1 
ATOM   3323 C CG2   . VAL C 1 106 ? 30.734  -13.911 -25.887 1.00 33.87 ? 129 VAL C CG2   1 
ATOM   3324 N N     . PRO C 1 107 ? 33.736  -17.003 -27.791 1.00 40.64 ? 130 PRO C N     1 
ATOM   3325 C CA    . PRO C 1 107 ? 34.897  -17.909 -27.904 1.00 39.59 ? 130 PRO C CA    1 
ATOM   3326 C C     . PRO C 1 107 ? 36.194  -17.351 -27.317 1.00 37.36 ? 130 PRO C C     1 
ATOM   3327 O O     . PRO C 1 107 ? 37.022  -18.143 -26.849 1.00 36.13 ? 130 PRO C O     1 
ATOM   3328 C CB    . PRO C 1 107 ? 35.005  -18.155 -29.416 1.00 41.73 ? 130 PRO C CB    1 
ATOM   3329 C CG    . PRO C 1 107 ? 34.330  -16.970 -30.044 1.00 41.25 ? 130 PRO C CG    1 
ATOM   3330 C CD    . PRO C 1 107 ? 33.255  -16.531 -29.104 1.00 39.30 ? 130 PRO C CD    1 
ATOM   3331 N N     . MET C 1 108 ? 36.400  -16.030 -27.339 1.00 31.72 ? 131 MET C N     1 
ATOM   3332 C CA    . MET C 1 108 ? 37.503  -15.358 -26.640 1.00 39.21 ? 131 MET C CA    1 
ATOM   3333 C C     . MET C 1 108 ? 38.877  -15.507 -27.292 1.00 40.36 ? 131 MET C C     1 
ATOM   3334 O O     . MET C 1 108 ? 39.843  -14.879 -26.841 1.00 36.20 ? 131 MET C O     1 
ATOM   3335 C CB    . MET C 1 108 ? 37.623  -15.838 -25.188 1.00 34.07 ? 131 MET C CB    1 
ATOM   3336 C CG    . MET C 1 108 ? 36.361  -15.719 -24.379 1.00 37.48 ? 131 MET C CG    1 
ATOM   3337 S SD    . MET C 1 108 ? 36.651  -15.524 -22.608 1.00 33.33 ? 131 MET C SD    1 
ATOM   3338 C CE    . MET C 1 108 ? 35.000  -15.051 -22.124 1.00 34.50 ? 131 MET C CE    1 
ATOM   3339 N N     . LEU C 1 109 ? 38.999  -16.327 -28.339 1.00 40.82 ? 132 LEU C N     1 
ATOM   3340 C CA    . LEU C 1 109 ? 40.338  -16.702 -28.785 1.00 41.09 ? 132 LEU C CA    1 
ATOM   3341 C C     . LEU C 1 109 ? 41.091  -15.536 -29.421 1.00 41.04 ? 132 LEU C C     1 
ATOM   3342 O O     . LEU C 1 109 ? 42.327  -15.570 -29.482 1.00 40.66 ? 132 LEU C O     1 
ATOM   3343 C CB    . LEU C 1 109 ? 40.247  -17.904 -29.723 1.00 41.90 ? 132 LEU C CB    1 
ATOM   3344 C CG    . LEU C 1 109 ? 39.711  -19.140 -28.964 1.00 45.35 ? 132 LEU C CG    1 
ATOM   3345 C CD1   . LEU C 1 109 ? 39.887  -20.439 -29.739 1.00 40.24 ? 132 LEU C CD1   1 
ATOM   3346 C CD2   . LEU C 1 109 ? 40.324  -19.262 -27.552 1.00 38.38 ? 132 LEU C CD2   1 
ATOM   3347 N N     . ASN C 1 110 ? 40.385  -14.496 -29.855 1.00 35.76 ? 133 ASN C N     1 
ATOM   3348 C CA    . ASN C 1 110 ? 41.007  -13.285 -30.379 1.00 38.10 ? 133 ASN C CA    1 
ATOM   3349 C C     . ASN C 1 110 ? 41.461  -12.321 -29.288 1.00 39.52 ? 133 ASN C C     1 
ATOM   3350 O O     . ASN C 1 110 ? 41.949  -11.233 -29.613 1.00 39.99 ? 133 ASN C O     1 
ATOM   3351 C CB    . ASN C 1 110 ? 40.034  -12.561 -31.314 1.00 42.69 ? 133 ASN C CB    1 
ATOM   3352 C CG    . ASN C 1 110 ? 38.619  -12.458 -30.729 1.00 47.48 ? 133 ASN C CG    1 
ATOM   3353 O OD1   . ASN C 1 110 ? 38.161  -13.349 -30.003 1.00 46.55 ? 133 ASN C OD1   1 
ATOM   3354 N ND2   . ASN C 1 110 ? 37.924  -11.367 -31.048 1.00 48.36 ? 133 ASN C ND2   1 
ATOM   3355 N N     . PHE C 1 111 ? 41.304  -12.681 -28.001 1.00 30.85 ? 134 PHE C N     1 
ATOM   3356 C CA    . PHE C 1 111 ? 41.628  -11.778 -26.909 1.00 30.88 ? 134 PHE C CA    1 
ATOM   3357 C C     . PHE C 1 111 ? 42.793  -12.326 -26.098 1.00 28.20 ? 134 PHE C C     1 
ATOM   3358 O O     . PHE C 1 111 ? 42.872  -13.540 -25.884 1.00 29.66 ? 134 PHE C O     1 
ATOM   3359 C CB    . PHE C 1 111 ? 40.423  -11.575 -25.984 1.00 29.06 ? 134 PHE C CB    1 
ATOM   3360 C CG    . PHE C 1 111 ? 39.342  -10.680 -26.557 1.00 32.13 ? 134 PHE C CG    1 
ATOM   3361 C CD1   . PHE C 1 111 ? 38.356  -11.196 -27.378 1.00 33.51 ? 134 PHE C CD1   1 
ATOM   3362 C CD2   . PHE C 1 111 ? 39.301  -9.330  -26.236 1.00 37.36 ? 134 PHE C CD2   1 
ATOM   3363 C CE1   . PHE C 1 111 ? 37.350  -10.387 -27.883 1.00 35.08 ? 134 PHE C CE1   1 
ATOM   3364 C CE2   . PHE C 1 111 ? 38.305  -8.505  -26.741 1.00 38.07 ? 134 PHE C CE2   1 
ATOM   3365 C CZ    . PHE C 1 111 ? 37.328  -9.037  -27.569 1.00 38.54 ? 134 PHE C CZ    1 
ATOM   3366 N N     . PRO C 1 112 ? 43.716  -11.474 -25.653 1.00 30.00 ? 135 PRO C N     1 
ATOM   3367 C CA    . PRO C 1 112 ? 44.816  -11.956 -24.808 1.00 29.64 ? 135 PRO C CA    1 
ATOM   3368 C C     . PRO C 1 112 ? 44.259  -12.576 -23.537 1.00 26.13 ? 135 PRO C C     1 
ATOM   3369 O O     . PRO C 1 112 ? 43.192  -12.187 -23.059 1.00 24.83 ? 135 PRO C O     1 
ATOM   3370 C CB    . PRO C 1 112 ? 45.617  -10.681 -24.495 1.00 29.42 ? 135 PRO C CB    1 
ATOM   3371 C CG    . PRO C 1 112 ? 45.153  -9.671  -25.496 1.00 28.51 ? 135 PRO C CG    1 
ATOM   3372 C CD    . PRO C 1 112 ? 43.743  -10.010 -25.821 1.00 25.98 ? 135 PRO C CD    1 
ATOM   3373 N N     . MET C 1 113 ? 44.996  -13.546 -22.987 1.00 24.30 ? 136 MET C N     1 
ATOM   3374 C CA    . MET C 1 113 ? 44.540  -14.204 -21.763 1.00 22.05 ? 136 MET C CA    1 
ATOM   3375 C C     . MET C 1 113 ? 44.306  -13.195 -20.644 1.00 25.91 ? 136 MET C C     1 
ATOM   3376 O O     . MET C 1 113 ? 43.333  -13.313 -19.890 1.00 23.80 ? 136 MET C O     1 
ATOM   3377 C CB    . MET C 1 113 ? 45.548  -15.263 -21.316 1.00 24.96 ? 136 MET C CB    1 
ATOM   3378 C CG    . MET C 1 113 ? 45.050  -16.130 -20.147 1.00 26.49 ? 136 MET C CG    1 
ATOM   3379 S SD    . MET C 1 113 ? 43.499  -17.027 -20.487 1.00 26.58 ? 136 MET C SD    1 
ATOM   3380 C CE    . MET C 1 113 ? 44.086  -18.290 -21.612 1.00 25.04 ? 136 MET C CE    1 
ATOM   3381 N N     . ALA C 1 114 ? 45.177  -12.185 -20.531 1.00 23.63 ? 137 ALA C N     1 
ATOM   3382 C CA    . ALA C 1 114 ? 45.008  -11.189 -19.477 1.00 25.56 ? 137 ALA C CA    1 
ATOM   3383 C C     . ALA C 1 114 ? 43.652  -10.498 -19.574 1.00 22.65 ? 137 ALA C C     1 
ATOM   3384 O O     . ALA C 1 114 ? 43.051  -10.159 -18.548 1.00 23.80 ? 137 ALA C O     1 
ATOM   3385 C CB    . ALA C 1 114 ? 46.151  -10.168 -19.530 1.00 25.80 ? 137 ALA C CB    1 
ATOM   3386 N N     . ALA C 1 115 ? 43.140  -10.309 -20.790 1.00 22.73 ? 138 ALA C N     1 
ATOM   3387 C CA    . ALA C 1 115 ? 41.836  -9.680  -20.949 1.00 21.54 ? 138 ALA C CA    1 
ATOM   3388 C C     . ALA C 1 115 ? 40.700  -10.638 -20.579 1.00 24.09 ? 138 ALA C C     1 
ATOM   3389 O O     . ALA C 1 115 ? 39.666  -10.212 -20.045 1.00 24.36 ? 138 ALA C O     1 
ATOM   3390 C CB    . ALA C 1 115 ? 41.687  -9.174  -22.381 1.00 22.49 ? 138 ALA C CB    1 
ATOM   3391 N N     . ARG C 1 116 ? 40.863  -11.931 -20.868 1.00 23.43 ? 139 ARG C N     1 
ATOM   3392 C CA    . ARG C 1 116 ? 39.864  -12.917 -20.459 1.00 23.05 ? 139 ARG C CA    1 
ATOM   3393 C C     . ARG C 1 116 ? 39.779  -13.015 -18.945 1.00 22.43 ? 139 ARG C C     1 
ATOM   3394 O O     . ARG C 1 116 ? 38.687  -13.155 -18.385 1.00 24.98 ? 139 ARG C O     1 
ATOM   3395 C CB    . ARG C 1 116 ? 40.198  -14.295 -21.035 1.00 21.64 ? 139 ARG C CB    1 
ATOM   3396 C CG    . ARG C 1 116 ? 40.468  -14.303 -22.529 1.00 26.34 ? 139 ARG C CG    1 
ATOM   3397 C CD    . ARG C 1 116 ? 40.880  -15.683 -22.959 1.00 23.15 ? 139 ARG C CD    1 
ATOM   3398 N NE    . ARG C 1 116 ? 41.532  -15.673 -24.264 1.00 32.24 ? 139 ARG C NE    1 
ATOM   3399 C CZ    . ARG C 1 116 ? 42.027  -16.754 -24.854 1.00 36.18 ? 139 ARG C CZ    1 
ATOM   3400 N NH1   . ARG C 1 116 ? 41.928  -17.949 -24.259 1.00 27.39 ? 139 ARG C NH1   1 
ATOM   3401 N NH2   . ARG C 1 116 ? 42.608  -16.642 -26.042 1.00 36.81 ? 139 ARG C NH2   1 
ATOM   3402 N N     . ILE C 1 117 ? 40.931  -12.999 -18.269 1.00 20.71 ? 140 ILE C N     1 
ATOM   3403 C CA    . ILE C 1 117 ? 40.925  -13.078 -16.814 1.00 23.51 ? 140 ILE C CA    1 
ATOM   3404 C C     . ILE C 1 117 ? 40.197  -11.881 -16.230 1.00 23.52 ? 140 ILE C C     1 
ATOM   3405 O O     . ILE C 1 117 ? 39.424  -12.014 -15.271 1.00 23.07 ? 140 ILE C O     1 
ATOM   3406 C CB    . ILE C 1 117 ? 42.363  -13.172 -16.268 1.00 24.12 ? 140 ILE C CB    1 
ATOM   3407 C CG1   . ILE C 1 117 ? 43.032  -14.495 -16.665 1.00 22.12 ? 140 ILE C CG1   1 
ATOM   3408 C CG2   . ILE C 1 117 ? 42.376  -12.930 -14.736 1.00 21.24 ? 140 ILE C CG2   1 
ATOM   3409 C CD1   . ILE C 1 117 ? 44.587  -14.466 -16.466 1.00 25.27 ? 140 ILE C CD1   1 
ATOM   3410 N N     . LYS C 1 118 ? 40.441  -10.689 -16.791 1.00 23.07 ? 141 LYS C N     1 
ATOM   3411 C CA    . LYS C 1 118 ? 39.825  -9.467  -16.262 1.00 22.39 ? 141 LYS C CA    1 
ATOM   3412 C C     . LYS C 1 118 ? 38.318  -9.452  -16.493 1.00 24.10 ? 141 LYS C C     1 
ATOM   3413 O O     . LYS C 1 118 ? 37.562  -9.009  -15.628 1.00 24.22 ? 141 LYS C O     1 
ATOM   3414 C CB    . LYS C 1 118 ? 40.454  -8.228  -16.901 1.00 26.75 ? 141 LYS C CB    1 
ATOM   3415 C CG    . LYS C 1 118 ? 39.823  -6.907  -16.445 1.00 32.62 ? 141 LYS C CG    1 
ATOM   3416 C CD    . LYS C 1 118 ? 40.633  -5.727  -16.902 1.00 34.38 ? 141 LYS C CD    1 
ATOM   3417 C CE    . LYS C 1 118 ? 40.394  -4.513  -16.022 1.00 48.94 ? 141 LYS C CE    1 
ATOM   3418 N NZ    . LYS C 1 118 ? 40.759  -4.782  -14.594 1.00 51.37 ? 141 LYS C NZ    1 
ATOM   3419 N N     . LEU C 1 119 ? 37.868  -9.894  -17.670 1.00 22.74 ? 142 LEU C N     1 
ATOM   3420 C CA    . LEU C 1 119 ? 36.433  -9.993  -17.917 1.00 23.42 ? 142 LEU C CA    1 
ATOM   3421 C C     . LEU C 1 119 ? 35.772  -10.907 -16.891 1.00 26.23 ? 142 LEU C C     1 
ATOM   3422 O O     . LEU C 1 119 ? 34.767  -10.541 -16.267 1.00 27.23 ? 142 LEU C O     1 
ATOM   3423 C CB    . LEU C 1 119 ? 36.179  -10.514 -19.335 1.00 26.02 ? 142 LEU C CB    1 
ATOM   3424 C CG    . LEU C 1 119 ? 34.715  -10.814 -19.702 1.00 27.57 ? 142 LEU C CG    1 
ATOM   3425 C CD1   . LEU C 1 119 ? 33.844  -9.610  -19.385 1.00 25.09 ? 142 LEU C CD1   1 
ATOM   3426 C CD2   . LEU C 1 119 ? 34.589  -11.210 -21.178 1.00 25.81 ? 142 LEU C CD2   1 
ATOM   3427 N N     . LEU C 1 120 ? 36.343  -12.100 -16.690 1.00 21.13 ? 143 LEU C N     1 
ATOM   3428 C CA    . LEU C 1 120 ? 35.772  -13.037 -15.730 1.00 22.22 ? 143 LEU C CA    1 
ATOM   3429 C C     . LEU C 1 120 ? 35.760  -12.457 -14.318 1.00 24.40 ? 143 LEU C C     1 
ATOM   3430 O O     . LEU C 1 120 ? 34.764  -12.582 -13.597 1.00 23.76 ? 143 LEU C O     1 
ATOM   3431 C CB    . LEU C 1 120 ? 36.554  -14.343 -15.767 1.00 21.25 ? 143 LEU C CB    1 
ATOM   3432 C CG    . LEU C 1 120 ? 35.885  -15.492 -15.043 1.00 33.11 ? 143 LEU C CG    1 
ATOM   3433 C CD1   . LEU C 1 120 ? 34.662  -15.981 -15.830 1.00 32.77 ? 143 LEU C CD1   1 
ATOM   3434 C CD2   . LEU C 1 120 ? 36.922  -16.567 -14.918 1.00 30.84 ? 143 LEU C CD2   1 
ATOM   3435 N N     . ASP C 1 121 ? 36.861  -11.824 -13.904 1.00 24.40 ? 144 ASP C N     1 
ATOM   3436 C CA    . ASP C 1 121 ? 36.893  -11.183 -12.590 1.00 25.30 ? 144 ASP C CA    1 
ATOM   3437 C C     . ASP C 1 121 ? 35.785  -10.141 -12.453 1.00 27.40 ? 144 ASP C C     1 
ATOM   3438 O O     . ASP C 1 121 ? 35.149  -10.043 -11.398 1.00 29.45 ? 144 ASP C O     1 
ATOM   3439 C CB    . ASP C 1 121 ? 38.271  -10.555 -12.345 1.00 25.46 ? 144 ASP C CB    1 
ATOM   3440 C CG    . ASP C 1 121 ? 38.424  -9.992  -10.935 1.00 33.26 ? 144 ASP C CG    1 
ATOM   3441 O OD1   . ASP C 1 121 ? 38.093  -10.696 -9.957  1.00 33.64 ? 144 ASP C OD1   1 
ATOM   3442 O OD2   . ASP C 1 121 ? 38.881  -8.838  -10.806 1.00 38.37 ? 144 ASP C OD2   1 
ATOM   3443 N N     . GLU C 1 122 ? 35.519  -9.374  -13.516 1.00 24.68 ? 145 GLU C N     1 
ATOM   3444 C CA    . GLU C 1 122 ? 34.470  -8.361  -13.455 1.00 25.36 ? 145 GLU C CA    1 
ATOM   3445 C C     . GLU C 1 122 ? 33.071  -8.984  -13.510 1.00 27.27 ? 145 GLU C C     1 
ATOM   3446 O O     . GLU C 1 122 ? 32.134  -8.474  -12.880 1.00 25.86 ? 145 GLU C O     1 
ATOM   3447 C CB    . GLU C 1 122 ? 34.651  -7.350  -14.594 1.00 26.65 ? 145 GLU C CB    1 
ATOM   3448 C CG    . GLU C 1 122 ? 35.873  -6.422  -14.458 1.00 32.07 ? 145 GLU C CG    1 
ATOM   3449 C CD    . GLU C 1 122 ? 35.753  -5.437  -13.291 1.00 40.60 ? 145 GLU C CD    1 
ATOM   3450 O OE1   . GLU C 1 122 ? 36.499  -5.587  -12.297 1.00 43.93 ? 145 GLU C OE1   1 
ATOM   3451 O OE2   . GLU C 1 122 ? 34.916  -4.511  -13.361 1.00 45.49 ? 145 GLU C OE2   1 
ATOM   3452 N N     . LEU C 1 123 ? 32.897  -10.066 -14.281 1.00 23.89 ? 146 LEU C N     1 
ATOM   3453 C CA    . LEU C 1 123 ? 31.602  -10.748 -14.314 1.00 24.63 ? 146 LEU C CA    1 
ATOM   3454 C C     . LEU C 1 123 ? 31.242  -11.299 -12.944 1.00 25.41 ? 146 LEU C C     1 
ATOM   3455 O O     . LEU C 1 123 ? 30.082  -11.215 -12.513 1.00 25.42 ? 146 LEU C O     1 
ATOM   3456 C CB    . LEU C 1 123 ? 31.609  -11.874 -15.349 1.00 22.10 ? 146 LEU C CB    1 
ATOM   3457 C CG    . LEU C 1 123 ? 31.570  -11.471 -16.824 1.00 25.12 ? 146 LEU C CG    1 
ATOM   3458 C CD1   . LEU C 1 123 ? 31.928  -12.666 -17.717 1.00 22.29 ? 146 LEU C CD1   1 
ATOM   3459 C CD2   . LEU C 1 123 ? 30.189  -10.896 -17.194 1.00 28.60 ? 146 LEU C CD2   1 
ATOM   3460 N N     . LEU C 1 124 ? 32.227  -11.841 -12.229 1.00 22.09 ? 147 LEU C N     1 
ATOM   3461 C CA    . LEU C 1 124 ? 31.969  -12.412 -10.916 1.00 21.56 ? 147 LEU C CA    1 
ATOM   3462 C C     . LEU C 1 124 ? 31.656  -11.351 -9.863  1.00 25.66 ? 147 LEU C C     1 
ATOM   3463 O O     . LEU C 1 124 ? 31.164  -11.701 -8.781  1.00 25.01 ? 147 LEU C O     1 
ATOM   3464 C CB    . LEU C 1 124 ? 33.157  -13.281 -10.488 1.00 21.57 ? 147 LEU C CB    1 
ATOM   3465 C CG    . LEU C 1 124 ? 33.217  -14.609 -11.271 1.00 22.49 ? 147 LEU C CG    1 
ATOM   3466 C CD1   . LEU C 1 124 ? 34.527  -15.332 -11.039 1.00 23.25 ? 147 LEU C CD1   1 
ATOM   3467 C CD2   . LEU C 1 124 ? 32.032  -15.508 -10.910 1.00 21.89 ? 147 LEU C CD2   1 
ATOM   3468 N N     . LYS C 1 125 ? 31.893  -10.073 -10.152 1.00 25.44 ? 148 LYS C N     1 
ATOM   3469 C CA    . LYS C 1 125 ? 31.401  -9.008  -9.280  1.00 24.53 ? 148 LYS C CA    1 
ATOM   3470 C C     . LYS C 1 125 ? 29.927  -8.675  -9.521  1.00 26.97 ? 148 LYS C C     1 
ATOM   3471 O O     . LYS C 1 125 ? 29.337  -7.935  -8.730  1.00 28.97 ? 148 LYS C O     1 
ATOM   3472 C CB    . LYS C 1 125 ? 32.248  -7.744  -9.458  1.00 25.96 ? 148 LYS C CB    1 
ATOM   3473 C CG    . LYS C 1 125 ? 33.687  -7.907  -8.991  1.00 30.02 ? 148 LYS C CG    1 
ATOM   3474 C CD    . LYS C 1 125 ? 34.598  -6.775  -9.484  1.00 30.58 ? 148 LYS C CD    1 
ATOM   3475 C CE    . LYS C 1 125 ? 36.013  -7.020  -8.979  1.00 33.46 ? 148 LYS C CE    1 
ATOM   3476 N NZ    . LYS C 1 125 ? 36.936  -5.908  -9.302  1.00 44.52 ? 148 LYS C NZ    1 
ATOM   3477 N N     . ARG C 1 126 ? 29.316  -9.204  -10.578 1.00 25.29 ? 149 ARG C N     1 
ATOM   3478 C CA    . ARG C 1 126 ? 27.929  -8.907  -10.897 1.00 26.52 ? 149 ARG C CA    1 
ATOM   3479 C C     . ARG C 1 126 ? 26.994  -10.063 -10.587 1.00 25.67 ? 149 ARG C C     1 
ATOM   3480 O O     . ARG C 1 126 ? 25.822  -10.021 -10.986 1.00 27.65 ? 149 ARG C O     1 
ATOM   3481 C CB    . ARG C 1 126 ? 27.803  -8.502  -12.364 1.00 25.86 ? 149 ARG C CB    1 
ATOM   3482 C CG    . ARG C 1 126 ? 28.833  -7.466  -12.754 1.00 31.23 ? 149 ARG C CG    1 
ATOM   3483 C CD    . ARG C 1 126 ? 28.309  -6.508  -13.775 1.00 33.65 ? 149 ARG C CD    1 
ATOM   3484 N NE    . ARG C 1 126 ? 29.330  -5.558  -14.194 1.00 40.13 ? 149 ARG C NE    1 
ATOM   3485 C CZ    . ARG C 1 126 ? 29.066  -4.391  -14.778 1.00 46.06 ? 149 ARG C CZ    1 
ATOM   3486 N NH1   . ARG C 1 126 ? 27.807  -4.030  -15.005 1.00 40.24 ? 149 ARG C NH1   1 
ATOM   3487 N NH2   . ARG C 1 126 ? 30.059  -3.582  -15.129 1.00 43.61 ? 149 ARG C NH2   1 
ATOM   3488 N N     . VAL C 1 127 ? 27.483  -11.105 -9.915  1.00 22.19 ? 150 VAL C N     1 
ATOM   3489 C CA    . VAL C 1 127 ? 26.625  -12.190 -9.435  1.00 22.78 ? 150 VAL C CA    1 
ATOM   3490 C C     . VAL C 1 127 ? 26.884  -12.384 -7.942  1.00 24.91 ? 150 VAL C C     1 
ATOM   3491 O O     . VAL C 1 127 ? 27.979  -12.061 -7.457  1.00 26.07 ? 150 VAL C O     1 
ATOM   3492 C CB    . VAL C 1 127 ? 26.857  -13.501 -10.214 1.00 22.23 ? 150 VAL C CB    1 
ATOM   3493 C CG1   . VAL C 1 127 ? 26.640  -13.305 -11.703 1.00 20.65 ? 150 VAL C CG1   1 
ATOM   3494 C CG2   . VAL C 1 127 ? 28.254  -14.050 -9.955  1.00 22.66 ? 150 VAL C CG2   1 
ATOM   3495 N N     . PRO C 1 128 ? 25.920  -12.901 -7.179  1.00 24.54 ? 151 PRO C N     1 
ATOM   3496 C CA    . PRO C 1 128 ? 26.172  -13.180 -5.756  1.00 26.30 ? 151 PRO C CA    1 
ATOM   3497 C C     . PRO C 1 128 ? 27.296  -14.191 -5.567  1.00 29.66 ? 151 PRO C C     1 
ATOM   3498 O O     . PRO C 1 128 ? 27.561  -15.036 -6.429  1.00 25.19 ? 151 PRO C O     1 
ATOM   3499 C CB    . PRO C 1 128 ? 24.832  -13.741 -5.258  1.00 26.83 ? 151 PRO C CB    1 
ATOM   3500 C CG    . PRO C 1 128 ? 23.808  -13.166 -6.224  1.00 30.63 ? 151 PRO C CG    1 
ATOM   3501 C CD    . PRO C 1 128 ? 24.517  -13.139 -7.560  1.00 24.53 ? 151 PRO C CD    1 
ATOM   3502 N N     . HIS C 1 129 ? 27.952  -14.099 -4.409  1.00 30.71 ? 152 HIS C N     1 
ATOM   3503 C CA    . HIS C 1 129 ? 29.082  -14.967 -4.116  1.00 31.26 ? 152 HIS C CA    1 
ATOM   3504 C C     . HIS C 1 129 ? 28.673  -16.434 -4.179  1.00 24.49 ? 152 HIS C C     1 
ATOM   3505 O O     . HIS C 1 129 ? 27.697  -16.853 -3.555  1.00 28.75 ? 152 HIS C O     1 
ATOM   3506 C CB    . HIS C 1 129 ? 29.666  -14.640 -2.738  1.00 33.90 ? 152 HIS C CB    1 
ATOM   3507 C CG    . HIS C 1 129 ? 30.896  -15.432 -2.422  1.00 34.92 ? 152 HIS C CG    1 
ATOM   3508 N ND1   . HIS C 1 129 ? 32.165  -14.969 -2.689  1.00 37.57 ? 152 HIS C ND1   1 
ATOM   3509 C CD2   . HIS C 1 129 ? 31.049  -16.674 -1.902  1.00 40.96 ? 152 HIS C CD2   1 
ATOM   3510 C CE1   . HIS C 1 129 ? 33.050  -15.881 -2.328  1.00 38.00 ? 152 HIS C CE1   1 
ATOM   3511 N NE2   . HIS C 1 129 ? 32.399  -16.927 -1.854  1.00 36.13 ? 152 HIS C NE2   1 
ATOM   3512 N N     . GLY C 1 130 ? 29.414  -17.215 -4.951  1.00 28.18 ? 153 GLY C N     1 
ATOM   3513 C CA    . GLY C 1 130 ? 29.106  -18.617 -5.135  1.00 23.53 ? 153 GLY C CA    1 
ATOM   3514 C C     . GLY C 1 130 ? 28.286  -18.928 -6.370  1.00 25.00 ? 153 GLY C C     1 
ATOM   3515 O O     . GLY C 1 130 ? 28.129  -20.106 -6.702  1.00 26.19 ? 153 GLY C O     1 
ATOM   3516 N N     . ARG C 1 131 ? 27.765  -17.897 -7.077  1.00 23.51 ? 154 ARG C N     1 
ATOM   3517 C CA    . ARG C 1 131 ? 26.995  -18.146 -8.289  1.00 22.69 ? 154 ARG C CA    1 
ATOM   3518 C C     . ARG C 1 131 ? 27.939  -18.215 -9.488  1.00 25.54 ? 154 ARG C C     1 
ATOM   3519 O O     . ARG C 1 131 ? 29.016  -17.611 -9.471  1.00 21.36 ? 154 ARG C O     1 
ATOM   3520 C CB    . ARG C 1 131 ? 25.952  -17.045 -8.498  1.00 20.46 ? 154 ARG C CB    1 
ATOM   3521 C CG    . ARG C 1 131 ? 24.823  -17.065 -7.428  1.00 24.03 ? 154 ARG C CG    1 
ATOM   3522 C CD    . ARG C 1 131 ? 24.111  -18.429 -7.407  1.00 23.75 ? 154 ARG C CD    1 
ATOM   3523 N NE    . ARG C 1 131 ? 23.379  -18.650 -8.657  1.00 24.27 ? 154 ARG C NE    1 
ATOM   3524 C CZ    . ARG C 1 131 ? 23.041  -19.841 -9.140  1.00 28.05 ? 154 ARG C CZ    1 
ATOM   3525 N NH1   . ARG C 1 131 ? 23.365  -20.946 -8.490  1.00 27.07 ? 154 ARG C NH1   1 
ATOM   3526 N NH2   . ARG C 1 131 ? 22.372  -19.926 -10.282 1.00 27.11 ? 154 ARG C NH2   1 
ATOM   3527 N N     . PRO C 1 132 ? 27.587  -18.958 -10.535 1.00 24.15 ? 155 PRO C N     1 
ATOM   3528 C CA    . PRO C 1 132 ? 28.583  -19.276 -11.561 1.00 23.05 ? 155 PRO C CA    1 
ATOM   3529 C C     . PRO C 1 132 ? 28.525  -18.422 -12.816 1.00 24.16 ? 155 PRO C C     1 
ATOM   3530 O O     . PRO C 1 132 ? 27.492  -17.834 -13.158 1.00 21.03 ? 155 PRO C O     1 
ATOM   3531 C CB    . PRO C 1 132 ? 28.237  -20.724 -11.903 1.00 23.56 ? 155 PRO C CB    1 
ATOM   3532 C CG    . PRO C 1 132 ? 26.719  -20.692 -11.886 1.00 22.76 ? 155 PRO C CG    1 
ATOM   3533 C CD    . PRO C 1 132 ? 26.351  -19.746 -10.738 1.00 22.57 ? 155 PRO C CD    1 
ATOM   3534 N N     . VAL C 1 133 ? 29.667  -18.367 -13.498 1.00 19.22 ? 156 VAL C N     1 
ATOM   3535 C CA    . VAL C 1 133 ? 29.750  -18.119 -14.926 1.00 19.01 ? 156 VAL C CA    1 
ATOM   3536 C C     . VAL C 1 133 ? 29.981  -19.481 -15.581 1.00 23.38 ? 156 VAL C C     1 
ATOM   3537 O O     . VAL C 1 133 ? 30.924  -20.199 -15.214 1.00 21.81 ? 156 VAL C O     1 
ATOM   3538 C CB    . VAL C 1 133 ? 30.885  -17.129 -15.252 1.00 21.21 ? 156 VAL C CB    1 
ATOM   3539 C CG1   . VAL C 1 133 ? 30.974  -16.833 -16.760 1.00 20.53 ? 156 VAL C CG1   1 
ATOM   3540 C CG2   . VAL C 1 133 ? 30.712  -15.822 -14.460 1.00 21.15 ? 156 VAL C CG2   1 
ATOM   3541 N N     . VAL C 1 134 ? 29.108  -19.864 -16.520 1.00 18.67 ? 157 VAL C N     1 
ATOM   3542 C CA    . VAL C 1 134 ? 29.258  -21.109 -17.283 1.00 20.82 ? 157 VAL C CA    1 
ATOM   3543 C C     . VAL C 1 134 ? 29.804  -20.770 -18.659 1.00 21.77 ? 157 VAL C C     1 
ATOM   3544 O O     . VAL C 1 134 ? 29.340  -19.819 -19.302 1.00 23.20 ? 157 VAL C O     1 
ATOM   3545 C CB    . VAL C 1 134 ? 27.923  -21.875 -17.412 1.00 22.88 ? 157 VAL C CB    1 
ATOM   3546 C CG1   . VAL C 1 134 ? 28.177  -23.307 -17.904 1.00 23.18 ? 157 VAL C CG1   1 
ATOM   3547 C CG2   . VAL C 1 134 ? 27.212  -21.887 -16.100 1.00 26.63 ? 157 VAL C CG2   1 
ATOM   3548 N N     . GLN C 1 135 ? 30.769  -21.561 -19.132 1.00 23.69 ? 158 GLN C N     1 
ATOM   3549 C CA    . GLN C 1 135 ? 31.447  -21.274 -20.390 1.00 19.36 ? 158 GLN C CA    1 
ATOM   3550 C C     . GLN C 1 135 ? 31.644  -22.563 -21.187 1.00 23.88 ? 158 GLN C C     1 
ATOM   3551 O O     . GLN C 1 135 ? 32.017  -23.590 -20.622 1.00 22.66 ? 158 GLN C O     1 
ATOM   3552 C CB    . GLN C 1 135 ? 32.795  -20.587 -20.108 1.00 23.24 ? 158 GLN C CB    1 
ATOM   3553 C CG    . GLN C 1 135 ? 33.728  -20.407 -21.312 1.00 25.36 ? 158 GLN C CG    1 
ATOM   3554 C CD    . GLN C 1 135 ? 33.297  -19.302 -22.229 1.00 26.13 ? 158 GLN C CD    1 
ATOM   3555 O OE1   . GLN C 1 135 ? 33.049  -18.175 -21.792 1.00 31.76 ? 158 GLN C OE1   1 
ATOM   3556 N NE2   . GLN C 1 135 ? 33.197  -19.612 -23.527 1.00 32.14 ? 158 GLN C NE2   1 
ATOM   3557 N N     . ILE C 1 136 ? 31.407  -22.500 -22.504 1.00 24.01 ? 159 ILE C N     1 
ATOM   3558 C CA    . ILE C 1 136 ? 31.590  -23.634 -23.409 1.00 26.51 ? 159 ILE C CA    1 
ATOM   3559 C C     . ILE C 1 136 ? 32.936  -23.521 -24.120 1.00 27.87 ? 159 ILE C C     1 
ATOM   3560 O O     . ILE C 1 136 ? 33.368  -22.420 -24.494 1.00 27.79 ? 159 ILE C O     1 
ATOM   3561 C CB    . ILE C 1 136 ? 30.422  -23.727 -24.419 1.00 28.37 ? 159 ILE C CB    1 
ATOM   3562 C CG1   . ILE C 1 136 ? 30.558  -24.965 -25.316 1.00 25.87 ? 159 ILE C CG1   1 
ATOM   3563 C CG2   . ILE C 1 136 ? 30.314  -22.480 -25.265 1.00 29.47 ? 159 ILE C CG2   1 
ATOM   3564 C CD1   . ILE C 1 136 ? 29.274  -25.251 -26.085 1.00 28.02 ? 159 ILE C CD1   1 
ATOM   3565 N N     . SER C 1 137 ? 33.613  -24.663 -24.284 1.00 26.76 ? 160 SER C N     1 
ATOM   3566 C CA    . SER C 1 137 ? 34.833  -24.788 -25.082 1.00 29.58 ? 160 SER C CA    1 
ATOM   3567 C C     . SER C 1 137 ? 34.770  -26.108 -25.855 1.00 30.07 ? 160 SER C C     1 
ATOM   3568 O O     . SER C 1 137 ? 33.803  -26.882 -25.741 1.00 24.68 ? 160 SER C O     1 
ATOM   3569 C CB    . SER C 1 137 ? 36.101  -24.699 -24.208 1.00 29.49 ? 160 SER C CB    1 
ATOM   3570 O OG    . SER C 1 137 ? 36.521  -25.983 -23.726 1.00 33.95 ? 160 SER C OG    1 
ATOM   3571 N N     . TYR C 1 138 ? 35.810  -26.383 -26.649 1.00 26.66 ? 161 TYR C N     1 
ATOM   3572 C CA    . TYR C 1 138 ? 35.737  -27.517 -27.569 1.00 31.09 ? 161 TYR C CA    1 
ATOM   3573 C C     . TYR C 1 138 ? 36.961  -28.424 -27.507 1.00 36.33 ? 161 TYR C C     1 
ATOM   3574 O O     . TYR C 1 138 ? 37.171  -29.251 -28.404 1.00 37.73 ? 161 TYR C O     1 
ATOM   3575 C CB    . TYR C 1 138 ? 35.492  -27.016 -28.991 1.00 30.63 ? 161 TYR C CB    1 
ATOM   3576 C CG    . TYR C 1 138 ? 34.152  -26.313 -29.084 1.00 32.15 ? 161 TYR C CG    1 
ATOM   3577 C CD1   . TYR C 1 138 ? 32.966  -27.036 -29.037 1.00 28.49 ? 161 TYR C CD1   1 
ATOM   3578 C CD2   . TYR C 1 138 ? 34.073  -24.937 -29.179 1.00 30.97 ? 161 TYR C CD2   1 
ATOM   3579 C CE1   . TYR C 1 138 ? 31.743  -26.403 -29.104 1.00 28.64 ? 161 TYR C CE1   1 
ATOM   3580 C CE2   . TYR C 1 138 ? 32.846  -24.289 -29.249 1.00 30.28 ? 161 TYR C CE2   1 
ATOM   3581 C CZ    . TYR C 1 138 ? 31.689  -25.029 -29.212 1.00 34.07 ? 161 TYR C CZ    1 
ATOM   3582 O OH    . TYR C 1 138 ? 30.465  -24.396 -29.281 1.00 37.60 ? 161 TYR C OH    1 
ATOM   3583 N N     . GLY C 1 139 ? 37.750  -28.321 -26.458 1.00 37.76 ? 162 GLY C N     1 
ATOM   3584 C CA    . GLY C 1 139 ? 38.837  -29.236 -26.243 1.00 31.82 ? 162 GLY C CA    1 
ATOM   3585 C C     . GLY C 1 139 ? 39.160  -29.265 -24.768 1.00 31.10 ? 162 GLY C C     1 
ATOM   3586 O O     . GLY C 1 139 ? 38.399  -28.761 -23.940 1.00 33.58 ? 162 GLY C O     1 
ATOM   3587 N N     . PRO C 1 140 ? 40.299  -29.826 -24.417 1.00 32.25 ? 163 PRO C N     1 
ATOM   3588 C CA    . PRO C 1 140 ? 40.652  -29.952 -22.997 1.00 29.48 ? 163 PRO C CA    1 
ATOM   3589 C C     . PRO C 1 140 ? 41.362  -28.729 -22.433 1.00 31.46 ? 163 PRO C C     1 
ATOM   3590 O O     . PRO C 1 140 ? 42.195  -28.864 -21.533 1.00 34.63 ? 163 PRO C O     1 
ATOM   3591 C CB    . PRO C 1 140 ? 41.576  -31.175 -22.990 1.00 34.49 ? 163 PRO C CB    1 
ATOM   3592 C CG    . PRO C 1 140 ? 42.284  -31.089 -24.359 1.00 34.82 ? 163 PRO C CG    1 
ATOM   3593 C CD    . PRO C 1 140 ? 41.266  -30.497 -25.313 1.00 33.01 ? 163 PRO C CD    1 
ATOM   3594 N N     . ILE C 1 141 ? 41.078  -27.545 -22.972 1.00 31.72 ? 164 ILE C N     1 
ATOM   3595 C CA    . ILE C 1 141 ? 41.724  -26.294 -22.571 1.00 26.61 ? 164 ILE C CA    1 
ATOM   3596 C C     . ILE C 1 141 ? 40.620  -25.326 -22.138 1.00 31.08 ? 164 ILE C C     1 
ATOM   3597 O O     . ILE C 1 141 ? 39.754  -24.970 -22.943 1.00 31.79 ? 164 ILE C O     1 
ATOM   3598 C CB    . ILE C 1 141 ? 42.565  -25.703 -23.718 1.00 30.74 ? 164 ILE C CB    1 
ATOM   3599 C CG1   . ILE C 1 141 ? 43.607  -26.723 -24.213 1.00 34.90 ? 164 ILE C CG1   1 
ATOM   3600 C CG2   . ILE C 1 141 ? 43.259  -24.400 -23.303 1.00 30.61 ? 164 ILE C CG2   1 
ATOM   3601 C CD1   . ILE C 1 141 ? 44.402  -26.264 -25.425 1.00 29.02 ? 164 ILE C CD1   1 
ATOM   3602 N N     . SER C 1 142 ? 40.615  -24.931 -20.866 1.00 26.32 ? 165 SER C N     1 
ATOM   3603 C CA    . SER C 1 142 ? 39.629  -23.943 -20.458 1.00 25.65 ? 165 SER C CA    1 
ATOM   3604 C C     . SER C 1 142 ? 39.933  -22.617 -21.156 1.00 26.70 ? 165 SER C C     1 
ATOM   3605 O O     . SER C 1 142 ? 41.102  -22.245 -21.305 1.00 28.24 ? 165 SER C O     1 
ATOM   3606 C CB    . SER C 1 142 ? 39.606  -23.776 -18.936 1.00 27.32 ? 165 SER C CB    1 
ATOM   3607 O OG    . SER C 1 142 ? 40.819  -23.226 -18.435 1.00 32.00 ? 165 SER C OG    1 
ATOM   3608 N N     . PRO C 1 143 ? 38.915  -21.905 -21.640 1.00 26.49 ? 166 PRO C N     1 
ATOM   3609 C CA    . PRO C 1 143 ? 39.192  -20.657 -22.372 1.00 27.58 ? 166 PRO C CA    1 
ATOM   3610 C C     . PRO C 1 143 ? 39.850  -19.604 -21.512 1.00 25.83 ? 166 PRO C C     1 
ATOM   3611 O O     . PRO C 1 143 ? 40.570  -18.742 -22.035 1.00 26.06 ? 166 PRO C O     1 
ATOM   3612 C CB    . PRO C 1 143 ? 37.801  -20.206 -22.841 1.00 28.71 ? 166 PRO C CB    1 
ATOM   3613 C CG    . PRO C 1 143 ? 36.952  -21.453 -22.756 1.00 27.62 ? 166 PRO C CG    1 
ATOM   3614 C CD    . PRO C 1 143 ? 37.474  -22.186 -21.566 1.00 27.39 ? 166 PRO C CD    1 
ATOM   3615 N N     . ILE C 1 144 ? 39.612  -19.642 -20.204 1.00 24.15 ? 167 ILE C N     1 
ATOM   3616 C CA    . ILE C 1 144 ? 40.253  -18.745 -19.253 1.00 26.15 ? 167 ILE C CA    1 
ATOM   3617 C C     . ILE C 1 144 ? 41.062  -19.602 -18.292 1.00 26.16 ? 167 ILE C C     1 
ATOM   3618 O O     . ILE C 1 144 ? 40.529  -20.539 -17.685 1.00 25.21 ? 167 ILE C O     1 
ATOM   3619 C CB    . ILE C 1 144 ? 39.238  -17.866 -18.491 1.00 25.70 ? 167 ILE C CB    1 
ATOM   3620 C CG1   . ILE C 1 144 ? 38.186  -17.279 -19.437 1.00 27.04 ? 167 ILE C CG1   1 
ATOM   3621 C CG2   . ILE C 1 144 ? 39.950  -16.702 -17.821 1.00 23.75 ? 167 ILE C CG2   1 
ATOM   3622 C CD1   . ILE C 1 144 ? 36.844  -17.954 -19.337 1.00 32.43 ? 167 ILE C CD1   1 
ATOM   3623 N N     . VAL C 1 145 ? 42.349  -19.291 -18.165 1.00 23.70 ? 168 VAL C N     1 
ATOM   3624 C CA    . VAL C 1 145 ? 43.239  -20.126 -17.378 1.00 25.66 ? 168 VAL C CA    1 
ATOM   3625 C C     . VAL C 1 145 ? 42.865  -20.048 -15.894 1.00 25.44 ? 168 VAL C C     1 
ATOM   3626 O O     . VAL C 1 145 ? 42.304  -19.052 -15.419 1.00 21.27 ? 168 VAL C O     1 
ATOM   3627 C CB    . VAL C 1 145 ? 44.696  -19.692 -17.643 1.00 28.23 ? 168 VAL C CB    1 
ATOM   3628 C CG1   . VAL C 1 145 ? 44.951  -18.258 -17.136 1.00 21.39 ? 168 VAL C CG1   1 
ATOM   3629 C CG2   . VAL C 1 145 ? 45.688  -20.693 -17.034 1.00 30.40 ? 168 VAL C CG2   1 
ATOM   3630 N N     . ALA C 1 146 ? 43.170  -21.118 -15.155 1.00 23.33 ? 169 ALA C N     1 
ATOM   3631 C CA    . ALA C 1 146 ? 42.978  -21.113 -13.708 1.00 27.39 ? 169 ALA C CA    1 
ATOM   3632 C C     . ALA C 1 146 ? 43.739  -19.964 -13.057 1.00 25.04 ? 169 ALA C C     1 
ATOM   3633 O O     . ALA C 1 146 ? 44.900  -19.707 -13.381 1.00 24.69 ? 169 ALA C O     1 
ATOM   3634 C CB    . ALA C 1 146 ? 43.427  -22.446 -13.104 1.00 24.02 ? 169 ALA C CB    1 
ATOM   3635 N N     . GLN C 1 147 ? 43.065  -19.267 -12.147 1.00 26.45 ? 170 GLN C N     1 
ATOM   3636 C CA    . GLN C 1 147 ? 43.674  -18.230 -11.308 1.00 20.80 ? 170 GLN C CA    1 
ATOM   3637 C C     . GLN C 1 147 ? 43.086  -18.410 -9.915  1.00 23.82 ? 170 GLN C C     1 
ATOM   3638 O O     . GLN C 1 147 ? 42.158  -17.692 -9.514  1.00 21.84 ? 170 GLN C O     1 
ATOM   3639 C CB    . GLN C 1 147 ? 43.395  -16.824 -11.846 1.00 21.62 ? 170 GLN C CB    1 
ATOM   3640 C CG    . GLN C 1 147 ? 44.027  -16.505 -13.194 1.00 22.82 ? 170 GLN C CG    1 
ATOM   3641 C CD    . GLN C 1 147 ? 45.510  -16.197 -13.095 1.00 27.57 ? 170 GLN C CD    1 
ATOM   3642 O OE1   . GLN C 1 147 ? 45.900  -15.058 -12.845 1.00 29.10 ? 170 GLN C OE1   1 
ATOM   3643 N NE2   . GLN C 1 147 ? 46.343  -17.208 -13.309 1.00 23.21 ? 170 GLN C NE2   1 
ATOM   3644 N N     . PRO C 1 148 ? 43.599  -19.383 -9.151  1.00 23.98 ? 171 PRO C N     1 
ATOM   3645 C CA    . PRO C 1 148 ? 42.923  -19.792 -7.907  1.00 23.67 ? 171 PRO C CA    1 
ATOM   3646 C C     . PRO C 1 148 ? 42.780  -18.692 -6.870  1.00 26.33 ? 171 PRO C C     1 
ATOM   3647 O O     . PRO C 1 148 ? 41.972  -18.853 -5.952  1.00 26.66 ? 171 PRO C O     1 
ATOM   3648 C CB    . PRO C 1 148 ? 43.811  -20.928 -7.374  1.00 26.71 ? 171 PRO C CB    1 
ATOM   3649 C CG    . PRO C 1 148 ? 44.581  -21.409 -8.544  1.00 25.03 ? 171 PRO C CG    1 
ATOM   3650 C CD    . PRO C 1 148 ? 44.709  -20.284 -9.515  1.00 23.96 ? 171 PRO C CD    1 
ATOM   3651 N N     . HIS C 1 149 ? 43.545  -17.602 -6.958  1.00 24.19 ? 172 HIS C N     1 
ATOM   3652 C CA    . HIS C 1 149 ? 43.366  -16.479 -6.043  1.00 29.36 ? 172 HIS C CA    1 
ATOM   3653 C C     . HIS C 1 149 ? 42.182  -15.590 -6.415  1.00 31.13 ? 172 HIS C C     1 
ATOM   3654 O O     . HIS C 1 149 ? 41.832  -14.693 -5.635  1.00 30.00 ? 172 HIS C O     1 
ATOM   3655 C CB    . HIS C 1 149 ? 44.640  -15.624 -5.991  1.00 29.74 ? 172 HIS C CB    1 
ATOM   3656 C CG    . HIS C 1 149 ? 44.931  -14.900 -7.268  1.00 25.94 ? 172 HIS C CG    1 
ATOM   3657 N ND1   . HIS C 1 149 ? 45.353  -15.544 -8.411  1.00 29.15 ? 172 HIS C ND1   1 
ATOM   3658 C CD2   . HIS C 1 149 ? 44.848  -13.588 -7.585  1.00 28.72 ? 172 HIS C CD2   1 
ATOM   3659 C CE1   . HIS C 1 149 ? 45.526  -14.658 -9.376  1.00 28.04 ? 172 HIS C CE1   1 
ATOM   3660 N NE2   . HIS C 1 149 ? 45.228  -13.462 -8.900  1.00 30.80 ? 172 HIS C NE2   1 
ATOM   3661 N N     . LEU C 1 150 ? 41.575  -15.806 -7.583  1.00 27.20 ? 173 LEU C N     1 
ATOM   3662 C CA    . LEU C 1 150 ? 40.396  -15.072 -8.034  1.00 26.63 ? 173 LEU C CA    1 
ATOM   3663 C C     . LEU C 1 150 ? 39.145  -15.930 -8.128  1.00 25.70 ? 173 LEU C C     1 
ATOM   3664 O O     . LEU C 1 150 ? 38.053  -15.454 -7.822  1.00 27.45 ? 173 LEU C O     1 
ATOM   3665 C CB    . LEU C 1 150 ? 40.663  -14.447 -9.412  1.00 22.34 ? 173 LEU C CB    1 
ATOM   3666 C CG    . LEU C 1 150 ? 41.853  -13.507 -9.515  1.00 29.52 ? 173 LEU C CG    1 
ATOM   3667 C CD1   . LEU C 1 150 ? 41.879  -12.836 -10.874 1.00 28.49 ? 173 LEU C CD1   1 
ATOM   3668 C CD2   . LEU C 1 150 ? 41.765  -12.451 -8.419  1.00 30.68 ? 173 LEU C CD2   1 
ATOM   3669 N N     . TYR C 1 151 ? 39.262  -17.181 -8.574  1.00 26.92 ? 174 TYR C N     1 
ATOM   3670 C CA    . TYR C 1 151 ? 38.082  -17.997 -8.825  1.00 19.62 ? 174 TYR C CA    1 
ATOM   3671 C C     . TYR C 1 151 ? 38.505  -19.459 -8.899  1.00 24.21 ? 174 TYR C C     1 
ATOM   3672 O O     . TYR C 1 151 ? 39.696  -19.781 -9.009  1.00 21.99 ? 174 TYR C O     1 
ATOM   3673 C CB    . TYR C 1 151 ? 37.376  -17.545 -10.113 1.00 21.70 ? 174 TYR C CB    1 
ATOM   3674 C CG    . TYR C 1 151 ? 38.325  -17.350 -11.286 1.00 22.62 ? 174 TYR C CG    1 
ATOM   3675 C CD1   . TYR C 1 151 ? 38.900  -18.443 -11.922 1.00 19.35 ? 174 TYR C CD1   1 
ATOM   3676 C CD2   . TYR C 1 151 ? 38.647  -16.079 -11.750 1.00 27.23 ? 174 TYR C CD2   1 
ATOM   3677 C CE1   . TYR C 1 151 ? 39.777  -18.289 -12.995 1.00 22.79 ? 174 TYR C CE1   1 
ATOM   3678 C CE2   . TYR C 1 151 ? 39.537  -15.902 -12.824 1.00 23.84 ? 174 TYR C CE2   1 
ATOM   3679 C CZ    . TYR C 1 151 ? 40.090  -17.016 -13.442 1.00 24.08 ? 174 TYR C CZ    1 
ATOM   3680 O OH    . TYR C 1 151 ? 40.966  -16.862 -14.497 1.00 25.98 ? 174 TYR C OH    1 
ATOM   3681 N N     . HIS C 1 152 ? 37.507  -20.342 -8.825  1.00 23.00 ? 175 HIS C N     1 
ATOM   3682 C CA    . HIS C 1 152 ? 37.671  -21.781 -8.999  1.00 23.44 ? 175 HIS C CA    1 
ATOM   3683 C C     . HIS C 1 152 ? 37.087  -22.198 -10.336 1.00 21.15 ? 175 HIS C C     1 
ATOM   3684 O O     . HIS C 1 152 ? 35.987  -21.777 -10.693 1.00 22.05 ? 175 HIS C O     1 
ATOM   3685 C CB    . HIS C 1 152 ? 36.945  -22.568 -7.904  1.00 24.01 ? 175 HIS C CB    1 
ATOM   3686 C CG    . HIS C 1 152 ? 37.439  -22.280 -6.524  1.00 32.03 ? 175 HIS C CG    1 
ATOM   3687 N ND1   . HIS C 1 152 ? 38.778  -22.149 -6.226  1.00 32.12 ? 175 HIS C ND1   1 
ATOM   3688 C CD2   . HIS C 1 152 ? 36.771  -22.091 -5.361  1.00 31.16 ? 175 HIS C CD2   1 
ATOM   3689 C CE1   . HIS C 1 152 ? 38.913  -21.895 -4.936  1.00 30.22 ? 175 HIS C CE1   1 
ATOM   3690 N NE2   . HIS C 1 152 ? 37.711  -21.861 -4.390  1.00 35.74 ? 175 HIS C NE2   1 
ATOM   3691 N N     . ILE C 1 153 ? 37.796  -23.050 -11.061 1.00 22.07 ? 176 ILE C N     1 
ATOM   3692 C CA    . ILE C 1 153 ? 37.274  -23.638 -12.287 1.00 18.80 ? 176 ILE C CA    1 
ATOM   3693 C C     . ILE C 1 153 ? 36.847  -25.066 -11.992 1.00 22.87 ? 176 ILE C C     1 
ATOM   3694 O O     . ILE C 1 153 ? 37.692  -25.914 -11.679 1.00 21.46 ? 176 ILE C O     1 
ATOM   3695 C CB    . ILE C 1 153 ? 38.315  -23.635 -13.412 1.00 24.86 ? 176 ILE C CB    1 
ATOM   3696 C CG1   . ILE C 1 153 ? 38.911  -22.247 -13.614 1.00 25.39 ? 176 ILE C CG1   1 
ATOM   3697 C CG2   . ILE C 1 153 ? 37.669  -24.145 -14.673 1.00 23.92 ? 176 ILE C CG2   1 
ATOM   3698 C CD1   . ILE C 1 153 ? 39.799  -22.180 -14.844 1.00 24.49 ? 176 ILE C CD1   1 
ATOM   3699 N N     . ARG C 1 154 ? 35.556  -25.347 -12.140 1.00 18.44 ? 177 ARG C N     1 
ATOM   3700 C CA    . ARG C 1 154 ? 35.045  -26.703 -12.064 1.00 18.71 ? 177 ARG C CA    1 
ATOM   3701 C C     . ARG C 1 154 ? 34.787  -27.229 -13.464 1.00 22.26 ? 177 ARG C C     1 
ATOM   3702 O O     . ARG C 1 154 ? 34.416  -26.478 -14.366 1.00 20.94 ? 177 ARG C O     1 
ATOM   3703 C CB    . ARG C 1 154 ? 33.752  -26.756 -11.251 1.00 26.27 ? 177 ARG C CB    1 
ATOM   3704 C CG    . ARG C 1 154 ? 33.981  -26.631 -9.754  1.00 26.83 ? 177 ARG C CG    1 
ATOM   3705 C CD    . ARG C 1 154 ? 32.676  -26.497 -8.989  1.00 29.34 ? 177 ARG C CD    1 
ATOM   3706 N NE    . ARG C 1 154 ? 32.959  -26.466 -7.558  1.00 30.81 ? 177 ARG C NE    1 
ATOM   3707 C CZ    . ARG C 1 154 ? 33.229  -25.361 -6.874  1.00 32.80 ? 177 ARG C CZ    1 
ATOM   3708 N NH1   . ARG C 1 154 ? 33.490  -25.439 -5.571  1.00 36.28 ? 177 ARG C NH1   1 
ATOM   3709 N NH2   . ARG C 1 154 ? 33.223  -24.176 -7.483  1.00 30.57 ? 177 ARG C NH2   1 
ATOM   3710 N N     . HIS C 1 155 ? 35.001  -28.528 -13.640 1.00 21.59 ? 178 HIS C N     1 
ATOM   3711 C CA    . HIS C 1 155 ? 34.611  -29.196 -14.870 1.00 22.92 ? 178 HIS C CA    1 
ATOM   3712 C C     . HIS C 1 155 ? 33.132  -29.528 -14.746 1.00 23.76 ? 178 HIS C C     1 
ATOM   3713 O O     . HIS C 1 155 ? 32.758  -30.403 -13.971 1.00 22.84 ? 178 HIS C O     1 
ATOM   3714 C CB    . HIS C 1 155 ? 35.445  -30.452 -15.089 1.00 22.77 ? 178 HIS C CB    1 
ATOM   3715 C CG    . HIS C 1 155 ? 35.252  -31.073 -16.434 1.00 21.16 ? 178 HIS C CG    1 
ATOM   3716 N ND1   . HIS C 1 155 ? 35.396  -32.426 -16.658 1.00 24.04 ? 178 HIS C ND1   1 
ATOM   3717 C CD2   . HIS C 1 155 ? 34.935  -30.525 -17.630 1.00 22.04 ? 178 HIS C CD2   1 
ATOM   3718 C CE1   . HIS C 1 155 ? 35.171  -32.685 -17.934 1.00 23.24 ? 178 HIS C CE1   1 
ATOM   3719 N NE2   . HIS C 1 155 ? 34.878  -31.548 -18.543 1.00 22.96 ? 178 HIS C NE2   1 
ATOM   3720 N N     . PHE C 1 156 ? 32.287  -28.812 -15.485 1.00 21.01 ? 179 PHE C N     1 
ATOM   3721 C CA    . PHE C 1 156 ? 30.842  -28.953 -15.328 1.00 18.83 ? 179 PHE C CA    1 
ATOM   3722 C C     . PHE C 1 156 ? 30.322  -30.188 -16.057 1.00 23.46 ? 179 PHE C C     1 
ATOM   3723 O O     . PHE C 1 156 ? 29.507  -30.938 -15.505 1.00 23.33 ? 179 PHE C O     1 
ATOM   3724 C CB    . PHE C 1 156 ? 30.168  -27.679 -15.837 1.00 21.16 ? 179 PHE C CB    1 
ATOM   3725 C CG    . PHE C 1 156 ? 28.695  -27.569 -15.533 1.00 23.07 ? 179 PHE C CG    1 
ATOM   3726 C CD1   . PHE C 1 156 ? 28.178  -27.914 -14.288 1.00 25.40 ? 179 PHE C CD1   1 
ATOM   3727 C CD2   . PHE C 1 156 ? 27.824  -27.069 -16.498 1.00 21.04 ? 179 PHE C CD2   1 
ATOM   3728 C CE1   . PHE C 1 156 ? 26.817  -27.781 -14.019 1.00 22.58 ? 179 PHE C CE1   1 
ATOM   3729 C CE2   . PHE C 1 156 ? 26.459  -26.940 -16.232 1.00 22.20 ? 179 PHE C CE2   1 
ATOM   3730 C CZ    . PHE C 1 156 ? 25.960  -27.297 -14.989 1.00 20.15 ? 179 PHE C CZ    1 
ATOM   3731 N N     . ASP C 1 157 ? 30.802  -30.442 -17.275 1.00 17.97 ? 180 ASP C N     1 
ATOM   3732 C CA    . ASP C 1 157 ? 30.399  -31.644 -18.000 1.00 22.81 ? 180 ASP C CA    1 
ATOM   3733 C C     . ASP C 1 157 ? 31.224  -31.744 -19.279 1.00 24.49 ? 180 ASP C C     1 
ATOM   3734 O O     . ASP C 1 157 ? 31.906  -30.798 -19.686 1.00 21.84 ? 180 ASP C O     1 
ATOM   3735 C CB    . ASP C 1 157 ? 28.899  -31.632 -18.342 1.00 21.62 ? 180 ASP C CB    1 
ATOM   3736 C CG    . ASP C 1 157 ? 28.249  -33.014 -18.238 1.00 26.82 ? 180 ASP C CG    1 
ATOM   3737 O OD1   . ASP C 1 157 ? 28.968  -34.037 -18.317 1.00 25.86 ? 180 ASP C OD1   1 
ATOM   3738 O OD2   . ASP C 1 157 ? 26.998  -33.070 -18.101 1.00 24.86 ? 180 ASP C OD2   1 
ATOM   3739 N N     . PHE C 1 158 ? 31.124  -32.911 -19.907 1.00 21.66 ? 181 PHE C N     1 
ATOM   3740 C CA    . PHE C 1 158 ? 31.647  -33.204 -21.239 1.00 23.98 ? 181 PHE C CA    1 
ATOM   3741 C C     . PHE C 1 158 ? 30.472  -33.769 -22.026 1.00 26.66 ? 181 PHE C C     1 
ATOM   3742 O O     . PHE C 1 158 ? 29.854  -34.744 -21.589 1.00 22.10 ? 181 PHE C O     1 
ATOM   3743 C CB    . PHE C 1 158 ? 32.809  -34.209 -21.140 1.00 21.93 ? 181 PHE C CB    1 
ATOM   3744 C CG    . PHE C 1 158 ? 33.398  -34.652 -22.466 1.00 25.27 ? 181 PHE C CG    1 
ATOM   3745 C CD1   . PHE C 1 158 ? 33.635  -33.749 -23.493 1.00 24.34 ? 181 PHE C CD1   1 
ATOM   3746 C CD2   . PHE C 1 158 ? 33.753  -35.981 -22.656 1.00 27.81 ? 181 PHE C CD2   1 
ATOM   3747 C CE1   . PHE C 1 158 ? 34.197  -34.176 -24.698 1.00 30.65 ? 181 PHE C CE1   1 
ATOM   3748 C CE2   . PHE C 1 158 ? 34.317  -36.415 -23.854 1.00 32.13 ? 181 PHE C CE2   1 
ATOM   3749 C CZ    . PHE C 1 158 ? 34.537  -35.506 -24.879 1.00 26.24 ? 181 PHE C CZ    1 
ATOM   3750 N N     . ILE C 1 159 ? 30.114  -33.126 -23.139 1.00 21.53 ? 182 ILE C N     1 
ATOM   3751 C CA    . ILE C 1 159 ? 28.931  -33.491 -23.918 1.00 24.73 ? 182 ILE C CA    1 
ATOM   3752 C C     . ILE C 1 159 ? 29.420  -34.061 -25.245 1.00 31.16 ? 182 ILE C C     1 
ATOM   3753 O O     . ILE C 1 159 ? 29.730  -33.300 -26.173 1.00 26.23 ? 182 ILE C O     1 
ATOM   3754 C CB    . ILE C 1 159 ? 27.997  -32.292 -24.147 1.00 25.06 ? 182 ILE C CB    1 
ATOM   3755 C CG1   . ILE C 1 159 ? 27.798  -31.487 -22.855 1.00 25.85 ? 182 ILE C CG1   1 
ATOM   3756 C CG2   . ILE C 1 159 ? 26.661  -32.747 -24.730 1.00 28.60 ? 182 ILE C CG2   1 
ATOM   3757 C CD1   . ILE C 1 159 ? 27.031  -32.207 -21.780 1.00 24.34 ? 182 ILE C CD1   1 
ATOM   3758 N N     . VAL C 1 160 ? 29.456  -35.393 -25.363 1.00 27.68 ? 183 VAL C N     1 
ATOM   3759 C CA    . VAL C 1 160 ? 29.959  -35.996 -26.597 1.00 33.75 ? 183 VAL C CA    1 
ATOM   3760 C C     . VAL C 1 160 ? 28.972  -35.817 -27.748 1.00 31.50 ? 183 VAL C C     1 
ATOM   3761 O O     . VAL C 1 160 ? 29.379  -35.777 -28.913 1.00 34.80 ? 183 VAL C O     1 
ATOM   3762 C CB    . VAL C 1 160 ? 30.317  -37.484 -26.395 1.00 34.03 ? 183 VAL C CB    1 
ATOM   3763 C CG1   . VAL C 1 160 ? 31.432  -37.631 -25.369 1.00 37.27 ? 183 VAL C CG1   1 
ATOM   3764 C CG2   . VAL C 1 160 ? 29.106  -38.297 -25.996 1.00 42.72 ? 183 VAL C CG2   1 
ATOM   3765 N N     . ARG C 1 161 ? 27.674  -35.682 -27.460 1.00 31.01 ? 184 ARG C N     1 
ATOM   3766 C CA    . ARG C 1 161 ? 26.703  -35.546 -28.544 1.00 38.91 ? 184 ARG C CA    1 
ATOM   3767 C C     . ARG C 1 161 ? 26.843  -34.229 -29.312 1.00 37.76 ? 184 ARG C C     1 
ATOM   3768 O O     . ARG C 1 161 ? 26.338  -34.127 -30.433 1.00 45.75 ? 184 ARG C O     1 
ATOM   3769 C CB    . ARG C 1 161 ? 25.277  -35.684 -28.005 1.00 36.18 ? 184 ARG C CB    1 
ATOM   3770 N N     . ASN C 1 162 ? 27.514  -33.231 -28.753 1.00 37.13 ? 185 ASN C N     1 
ATOM   3771 C CA    . ASN C 1 162 ? 27.681  -31.955 -29.438 1.00 32.30 ? 185 ASN C CA    1 
ATOM   3772 C C     . ASN C 1 162 ? 28.597  -32.102 -30.652 1.00 32.29 ? 185 ASN C C     1 
ATOM   3773 O O     . ASN C 1 162 ? 29.450  -32.987 -30.712 1.00 31.97 ? 185 ASN C O     1 
ATOM   3774 C CB    . ASN C 1 162 ? 28.256  -30.925 -28.474 1.00 28.26 ? 185 ASN C CB    1 
ATOM   3775 C CG    . ASN C 1 162 ? 27.888  -29.508 -28.840 1.00 29.74 ? 185 ASN C CG    1 
ATOM   3776 O OD1   . ASN C 1 162 ? 26.763  -29.062 -28.618 1.00 27.44 ? 185 ASN C OD1   1 
ATOM   3777 N ND2   . ASN C 1 162 ? 28.850  -28.781 -29.382 1.00 30.12 ? 185 ASN C ND2   1 
ATOM   3778 N N     . ILE C 1 163 ? 28.418  -31.219 -31.628 1.00 30.47 ? 186 ILE C N     1 
ATOM   3779 C CA    . ILE C 1 163 ? 29.295  -31.220 -32.799 1.00 33.27 ? 186 ILE C CA    1 
ATOM   3780 C C     . ILE C 1 163 ? 30.020  -29.883 -32.857 1.00 31.23 ? 186 ILE C C     1 
ATOM   3781 O O     . ILE C 1 163 ? 29.387  -28.856 -33.133 1.00 33.72 ? 186 ILE C O     1 
ATOM   3782 C CB    . ILE C 1 163 ? 28.511  -31.466 -34.099 1.00 34.66 ? 186 ILE C CB    1 
ATOM   3783 C CG1   . ILE C 1 163 ? 27.659  -32.729 -33.986 1.00 35.85 ? 186 ILE C CG1   1 
ATOM   3784 C CG2   . ILE C 1 163 ? 29.470  -31.523 -35.306 1.00 33.62 ? 186 ILE C CG2   1 
ATOM   3785 C CD1   . ILE C 1 163 ? 26.466  -32.735 -34.928 1.00 38.72 ? 186 ILE C CD1   1 
ATOM   3786 N N     . PRO C 1 164 ? 31.328  -29.832 -32.570 1.00 32.13 ? 187 PRO C N     1 
ATOM   3787 C CA    . PRO C 1 164 ? 32.153  -30.941 -32.073 1.00 29.64 ? 187 PRO C CA    1 
ATOM   3788 C C     . PRO C 1 164 ? 31.864  -31.191 -30.577 1.00 30.21 ? 187 PRO C C     1 
ATOM   3789 O O     . PRO C 1 164 ? 31.159  -30.370 -29.976 1.00 29.55 ? 187 PRO C O     1 
ATOM   3790 C CB    . PRO C 1 164 ? 33.576  -30.424 -32.296 1.00 32.02 ? 187 PRO C CB    1 
ATOM   3791 C CG    . PRO C 1 164 ? 33.443  -28.954 -32.088 1.00 30.45 ? 187 PRO C CG    1 
ATOM   3792 C CD    . PRO C 1 164 ? 32.093  -28.579 -32.653 1.00 30.50 ? 187 PRO C CD    1 
ATOM   3793 N N     . PRO C 1 165 ? 32.378  -32.277 -30.002 1.00 28.09 ? 188 PRO C N     1 
ATOM   3794 C CA    . PRO C 1 165 ? 32.169  -32.514 -28.564 1.00 26.80 ? 188 PRO C CA    1 
ATOM   3795 C C     . PRO C 1 165 ? 32.530  -31.279 -27.742 1.00 31.02 ? 188 PRO C C     1 
ATOM   3796 O O     . PRO C 1 165 ? 33.572  -30.646 -27.957 1.00 27.83 ? 188 PRO C O     1 
ATOM   3797 C CB    . PRO C 1 165 ? 33.101  -33.692 -28.264 1.00 27.91 ? 188 PRO C CB    1 
ATOM   3798 C CG    . PRO C 1 165 ? 33.154  -34.454 -29.574 1.00 30.76 ? 188 PRO C CG    1 
ATOM   3799 C CD    . PRO C 1 165 ? 33.146  -33.369 -30.639 1.00 30.17 ? 188 PRO C CD    1 
ATOM   3800 N N     . ALA C 1 166 ? 31.649  -30.930 -26.805 1.00 26.93 ? 189 ALA C N     1 
ATOM   3801 C CA    . ALA C 1 166 ? 31.745  -29.697 -26.033 1.00 27.22 ? 189 ALA C CA    1 
ATOM   3802 C C     . ALA C 1 166 ? 32.205  -29.965 -24.604 1.00 27.52 ? 189 ALA C C     1 
ATOM   3803 O O     . ALA C 1 166 ? 31.743  -30.910 -23.954 1.00 25.93 ? 189 ALA C O     1 
ATOM   3804 C CB    . ALA C 1 166 ? 30.399  -28.972 -25.989 1.00 27.01 ? 189 ALA C CB    1 
ATOM   3805 N N     . GLN C 1 167 ? 33.107  -29.121 -24.117 1.00 22.16 ? 190 GLN C N     1 
ATOM   3806 C CA    . GLN C 1 167 ? 33.482  -29.103 -22.715 1.00 23.48 ? 190 GLN C CA    1 
ATOM   3807 C C     . GLN C 1 167 ? 32.816  -27.909 -22.056 1.00 20.81 ? 190 GLN C C     1 
ATOM   3808 O O     . GLN C 1 167 ? 32.747  -26.826 -22.644 1.00 25.05 ? 190 GLN C O     1 
ATOM   3809 C CB    . GLN C 1 167 ? 35.004  -29.033 -22.553 1.00 22.82 ? 190 GLN C CB    1 
ATOM   3810 C CG    . GLN C 1 167 ? 35.704  -30.271 -23.078 1.00 25.18 ? 190 GLN C CG    1 
ATOM   3811 C CD    . GLN C 1 167 ? 35.613  -31.440 -22.098 1.00 29.54 ? 190 GLN C CD    1 
ATOM   3812 O OE1   . GLN C 1 167 ? 34.757  -31.456 -21.201 1.00 25.98 ? 190 GLN C OE1   1 
ATOM   3813 N NE2   . GLN C 1 167 ? 36.501  -32.420 -22.259 1.00 26.28 ? 190 GLN C NE2   1 
ATOM   3814 N N     . LEU C 1 168 ? 32.277  -28.126 -20.857 1.00 23.05 ? 191 LEU C N     1 
ATOM   3815 C CA    . LEU C 1 168 ? 31.549  -27.102 -20.115 1.00 18.43 ? 191 LEU C CA    1 
ATOM   3816 C C     . LEU C 1 168 ? 32.283  -26.831 -18.811 1.00 21.36 ? 191 LEU C C     1 
ATOM   3817 O O     . LEU C 1 168 ? 32.605  -27.771 -18.080 1.00 19.10 ? 191 LEU C O     1 
ATOM   3818 C CB    . LEU C 1 168 ? 30.104  -27.545 -19.838 1.00 18.03 ? 191 LEU C CB    1 
ATOM   3819 C CG    . LEU C 1 168 ? 29.207  -27.809 -21.050 1.00 19.74 ? 191 LEU C CG    1 
ATOM   3820 C CD1   . LEU C 1 168 ? 27.754  -28.133 -20.615 1.00 19.09 ? 191 LEU C CD1   1 
ATOM   3821 C CD2   . LEU C 1 168 ? 29.232  -26.616 -22.016 1.00 21.26 ? 191 LEU C CD2   1 
ATOM   3822 N N     . TRP C 1 169 ? 32.557  -25.554 -18.537 1.00 23.30 ? 192 TRP C N     1 
ATOM   3823 C CA    . TRP C 1 169 ? 33.300  -25.092 -17.368 1.00 20.73 ? 192 TRP C CA    1 
ATOM   3824 C C     . TRP C 1 169 ? 32.448  -24.122 -16.567 1.00 20.49 ? 192 TRP C C     1 
ATOM   3825 O O     . TRP C 1 169 ? 31.754  -23.291 -17.154 1.00 22.23 ? 192 TRP C O     1 
ATOM   3826 C CB    . TRP C 1 169 ? 34.584  -24.363 -17.793 1.00 19.18 ? 192 TRP C CB    1 
ATOM   3827 C CG    . TRP C 1 169 ? 35.389  -25.147 -18.772 1.00 23.82 ? 192 TRP C CG    1 
ATOM   3828 C CD1   . TRP C 1 169 ? 35.387  -25.023 -20.129 1.00 20.99 ? 192 TRP C CD1   1 
ATOM   3829 C CD2   . TRP C 1 169 ? 36.285  -26.223 -18.462 1.00 20.80 ? 192 TRP C CD2   1 
ATOM   3830 N NE1   . TRP C 1 169 ? 36.252  -25.945 -20.684 1.00 23.19 ? 192 TRP C NE1   1 
ATOM   3831 C CE2   . TRP C 1 169 ? 36.816  -26.690 -19.680 1.00 24.83 ? 192 TRP C CE2   1 
ATOM   3832 C CE3   . TRP C 1 169 ? 36.702  -26.820 -17.270 1.00 21.57 ? 192 TRP C CE3   1 
ATOM   3833 C CZ2   . TRP C 1 169 ? 37.740  -27.733 -19.741 1.00 24.95 ? 192 TRP C CZ2   1 
ATOM   3834 C CZ3   . TRP C 1 169 ? 37.614  -27.859 -17.330 1.00 21.57 ? 192 TRP C CZ3   1 
ATOM   3835 C CH2   . TRP C 1 169 ? 38.122  -28.306 -18.560 1.00 26.35 ? 192 TRP C CH2   1 
ATOM   3836 N N     . THR C 1 170 ? 32.530  -24.185 -15.232 1.00 18.73 ? 193 THR C N     1 
ATOM   3837 C CA    . THR C 1 170 ? 31.952  -23.136 -14.386 1.00 21.15 ? 193 THR C CA    1 
ATOM   3838 C C     . THR C 1 170 ? 33.037  -22.418 -13.596 1.00 20.57 ? 193 THR C C     1 
ATOM   3839 O O     . THR C 1 170 ? 33.997  -23.037 -13.122 1.00 24.16 ? 193 THR C O     1 
ATOM   3840 C CB    . THR C 1 170 ? 30.912  -23.669 -13.402 1.00 23.18 ? 193 THR C CB    1 
ATOM   3841 O OG1   . THR C 1 170 ? 31.496  -24.699 -12.596 1.00 23.22 ? 193 THR C OG1   1 
ATOM   3842 C CG2   . THR C 1 170 ? 29.654  -24.190 -14.159 1.00 20.33 ? 193 THR C CG2   1 
ATOM   3843 N N     . TYR C 1 171 ? 32.868  -21.109 -13.456 1.00 22.45 ? 194 TYR C N     1 
ATOM   3844 C CA    . TYR C 1 171 ? 33.780  -20.244 -12.721 1.00 21.03 ? 194 TYR C CA    1 
ATOM   3845 C C     . TYR C 1 171 ? 33.016  -19.601 -11.570 1.00 23.78 ? 194 TYR C C     1 
ATOM   3846 O O     . TYR C 1 171 ? 31.956  -19.004 -11.786 1.00 23.69 ? 194 TYR C O     1 
ATOM   3847 C CB    . TYR C 1 171 ? 34.355  -19.163 -13.636 1.00 18.69 ? 194 TYR C CB    1 
ATOM   3848 C CG    . TYR C 1 171 ? 35.168  -19.677 -14.798 1.00 21.98 ? 194 TYR C CG    1 
ATOM   3849 C CD1   . TYR C 1 171 ? 34.565  -20.099 -15.975 1.00 21.14 ? 194 TYR C CD1   1 
ATOM   3850 C CD2   . TYR C 1 171 ? 36.561  -19.725 -14.721 1.00 25.64 ? 194 TYR C CD2   1 
ATOM   3851 C CE1   . TYR C 1 171 ? 35.347  -20.567 -17.061 1.00 23.27 ? 194 TYR C CE1   1 
ATOM   3852 C CE2   . TYR C 1 171 ? 37.331  -20.158 -15.791 1.00 26.45 ? 194 TYR C CE2   1 
ATOM   3853 C CZ    . TYR C 1 171 ? 36.727  -20.587 -16.947 1.00 25.52 ? 194 TYR C CZ    1 
ATOM   3854 O OH    . TYR C 1 171 ? 37.540  -21.027 -17.966 1.00 28.14 ? 194 TYR C OH    1 
ATOM   3855 N N     . THR C 1 172 ? 33.545  -19.721 -10.353 1.00 22.90 ? 195 THR C N     1 
ATOM   3856 C CA    . THR C 1 172 ? 32.900  -19.166 -9.167  1.00 18.37 ? 195 THR C CA    1 
ATOM   3857 C C     . THR C 1 172 ? 33.946  -18.482 -8.294  1.00 24.15 ? 195 THR C C     1 
ATOM   3858 O O     . THR C 1 172 ? 35.106  -18.901 -8.252  1.00 24.46 ? 195 THR C O     1 
ATOM   3859 C CB    . THR C 1 172 ? 32.179  -20.248 -8.344  1.00 25.54 ? 195 THR C CB    1 
ATOM   3860 O OG1   . THR C 1 172 ? 33.117  -21.259 -7.976  1.00 32.35 ? 195 THR C OG1   1 
ATOM   3861 C CG2   . THR C 1 172 ? 31.061  -20.893 -9.150  1.00 28.09 ? 195 THR C CG2   1 
ATOM   3862 N N     . ARG C 1 173 ? 33.515  -17.439 -7.577  1.00 21.34 ? 196 ARG C N     1 
ATOM   3863 C CA    . ARG C 1 173 ? 34.450  -16.586 -6.850  1.00 25.59 ? 196 ARG C CA    1 
ATOM   3864 C C     . ARG C 1 173 ? 35.160  -17.378 -5.762  1.00 27.61 ? 196 ARG C C     1 
ATOM   3865 O O     . ARG C 1 173 ? 34.530  -18.141 -5.027  1.00 28.52 ? 196 ARG C O     1 
ATOM   3866 C CB    . ARG C 1 173 ? 33.710  -15.383 -6.241  1.00 27.88 ? 196 ARG C CB    1 
ATOM   3867 C CG    . ARG C 1 173 ? 34.570  -14.510 -5.341  1.00 27.16 ? 196 ARG C CG    1 
ATOM   3868 C CD    . ARG C 1 173 ? 35.669  -13.825 -6.123  1.00 28.16 ? 196 ARG C CD    1 
ATOM   3869 N NE    . ARG C 1 173 ? 35.159  -12.690 -6.891  1.00 29.91 ? 196 ARG C NE    1 
ATOM   3870 C CZ    . ARG C 1 173 ? 35.694  -12.251 -8.029  1.00 28.72 ? 196 ARG C CZ    1 
ATOM   3871 N NH1   . ARG C 1 173 ? 36.763  -12.856 -8.538  1.00 28.18 ? 196 ARG C NH1   1 
ATOM   3872 N NH2   . ARG C 1 173 ? 35.173  -11.199 -8.658  1.00 25.76 ? 196 ARG C NH2   1 
ATOM   3873 N N     . ALA C 1 174 ? 36.485  -17.227 -5.689  1.00 29.51 ? 197 ALA C N     1 
ATOM   3874 C CA    . ALA C 1 174 ? 37.251  -17.907 -4.653  1.00 33.79 ? 197 ALA C CA    1 
ATOM   3875 C C     . ALA C 1 174 ? 37.049  -17.182 -3.327  1.00 42.83 ? 197 ALA C C     1 
ATOM   3876 O O     . ALA C 1 174 ? 37.005  -15.945 -3.285  1.00 42.56 ? 197 ALA C O     1 
ATOM   3877 C CB    . ALA C 1 174 ? 38.724  -17.966 -5.008  1.00 31.79 ? 197 ALA C CB    1 
ATOM   3878 O OXT   . ALA C 1 174 ? 36.919  -17.819 -2.278  1.00 48.73 ? 197 ALA C OXT   1 
ATOM   3879 N N     . VAL D 1 11  ? -17.995 -7.846  -35.026 1.00 53.21 ? 34  VAL D N     1 
ATOM   3880 C CA    . VAL D 1 11  ? -19.309 -7.235  -34.859 1.00 50.78 ? 34  VAL D CA    1 
ATOM   3881 C C     . VAL D 1 11  ? -19.164 -5.747  -34.564 1.00 47.84 ? 34  VAL D C     1 
ATOM   3882 O O     . VAL D 1 11  ? -18.325 -5.350  -33.757 1.00 45.31 ? 34  VAL D O     1 
ATOM   3883 C CB    . VAL D 1 11  ? -20.117 -7.934  -33.738 1.00 52.36 ? 34  VAL D CB    1 
ATOM   3884 C CG1   . VAL D 1 11  ? -21.606 -7.627  -33.870 1.00 51.85 ? 34  VAL D CG1   1 
ATOM   3885 C CG2   . VAL D 1 11  ? -19.872 -9.435  -33.761 1.00 55.64 ? 34  VAL D CG2   1 
ATOM   3886 N N     . PRO D 1 12  ? -19.972 -4.918  -35.221 1.00 46.80 ? 35  PRO D N     1 
ATOM   3887 C CA    . PRO D 1 12  ? -19.948 -3.485  -34.916 1.00 45.88 ? 35  PRO D CA    1 
ATOM   3888 C C     . PRO D 1 12  ? -20.609 -3.195  -33.579 1.00 45.57 ? 35  PRO D C     1 
ATOM   3889 O O     . PRO D 1 12  ? -21.470 -3.938  -33.098 1.00 43.55 ? 35  PRO D O     1 
ATOM   3890 C CB    . PRO D 1 12  ? -20.734 -2.849  -36.072 1.00 49.29 ? 35  PRO D CB    1 
ATOM   3891 C CG    . PRO D 1 12  ? -20.864 -3.927  -37.115 1.00 57.45 ? 35  PRO D CG    1 
ATOM   3892 C CD    . PRO D 1 12  ? -20.834 -5.227  -36.371 1.00 49.51 ? 35  PRO D CD    1 
ATOM   3893 N N     . THR D 1 13  ? -20.172 -2.099  -32.973 1.00 46.65 ? 36  THR D N     1 
ATOM   3894 C CA    . THR D 1 13  ? -20.769 -1.621  -31.737 1.00 34.52 ? 36  THR D CA    1 
ATOM   3895 C C     . THR D 1 13  ? -22.273 -1.416  -31.910 1.00 36.78 ? 36  THR D C     1 
ATOM   3896 O O     . THR D 1 13  ? -22.738 -0.924  -32.943 1.00 36.01 ? 36  THR D O     1 
ATOM   3897 C CB    . THR D 1 13  ? -20.057 -0.327  -31.331 1.00 36.13 ? 36  THR D CB    1 
ATOM   3898 O OG1   . THR D 1 13  ? -18.678 -0.627  -31.076 1.00 31.88 ? 36  THR D OG1   1 
ATOM   3899 C CG2   . THR D 1 13  ? -20.676 0.319   -30.081 1.00 30.87 ? 36  THR D CG2   1 
ATOM   3900 N N     . SER D 1 14  ? -23.042 -1.813  -30.898 1.00 32.85 ? 37  SER D N     1 
ATOM   3901 C CA    . SER D 1 14  ? -24.489 -1.674  -30.989 1.00 33.83 ? 37  SER D CA    1 
ATOM   3902 C C     . SER D 1 14  ? -24.916 -0.205  -30.894 1.00 34.33 ? 37  SER D C     1 
ATOM   3903 O O     . SER D 1 14  ? -24.190 0.659   -30.386 1.00 27.64 ? 37  SER D O     1 
ATOM   3904 C CB    . SER D 1 14  ? -25.178 -2.501  -29.902 1.00 35.81 ? 37  SER D CB    1 
ATOM   3905 O OG    . SER D 1 14  ? -25.563 -1.697  -28.813 1.00 36.12 ? 37  SER D OG    1 
ATOM   3906 N N     . SER D 1 15  ? -26.124 0.062   -31.406 1.00 35.24 ? 38  SER D N     1 
ATOM   3907 C CA    . SER D 1 15  ? -26.660 1.423   -31.449 1.00 37.55 ? 38  SER D CA    1 
ATOM   3908 C C     . SER D 1 15  ? -26.865 2.004   -30.062 1.00 35.33 ? 38  SER D C     1 
ATOM   3909 O O     . SER D 1 15  ? -26.724 3.219   -29.874 1.00 32.18 ? 38  SER D O     1 
ATOM   3910 C CB    . SER D 1 15  ? -27.992 1.447   -32.197 1.00 41.79 ? 38  SER D CB    1 
ATOM   3911 O OG    . SER D 1 15  ? -27.799 1.101   -33.554 1.00 52.18 ? 38  SER D OG    1 
ATOM   3912 N N     . ILE D 1 16  ? -27.241 1.172   -29.091 1.00 31.44 ? 39  ILE D N     1 
ATOM   3913 C CA    . ILE D 1 16  ? -27.404 1.673   -27.727 1.00 32.96 ? 39  ILE D CA    1 
ATOM   3914 C C     . ILE D 1 16  ? -26.081 2.227   -27.216 1.00 30.20 ? 39  ILE D C     1 
ATOM   3915 O O     . ILE D 1 16  ? -26.016 3.319   -26.642 1.00 31.97 ? 39  ILE D O     1 
ATOM   3916 C CB    . ILE D 1 16  ? -27.933 0.562   -26.800 1.00 37.01 ? 39  ILE D CB    1 
ATOM   3917 C CG1   . ILE D 1 16  ? -29.231 -0.020  -27.334 1.00 40.20 ? 39  ILE D CG1   1 
ATOM   3918 C CG2   . ILE D 1 16  ? -28.169 1.102   -25.398 1.00 40.46 ? 39  ILE D CG2   1 
ATOM   3919 C CD1   . ILE D 1 16  ? -29.726 -1.204  -26.519 1.00 46.65 ? 39  ILE D CD1   1 
ATOM   3920 N N     . THR D 1 17  ? -25.005 1.472   -27.421 1.00 28.72 ? 40  THR D N     1 
ATOM   3921 C CA    . THR D 1 17  ? -23.696 1.893   -26.949 1.00 30.21 ? 40  THR D CA    1 
ATOM   3922 C C     . THR D 1 17  ? -23.247 3.175   -27.639 1.00 30.18 ? 40  THR D C     1 
ATOM   3923 O O     . THR D 1 17  ? -22.696 4.076   -26.995 1.00 25.76 ? 40  THR D O     1 
ATOM   3924 C CB    . THR D 1 17  ? -22.692 0.775   -27.193 1.00 29.75 ? 40  THR D CB    1 
ATOM   3925 O OG1   . THR D 1 17  ? -23.170 -0.424  -26.571 1.00 32.80 ? 40  THR D OG1   1 
ATOM   3926 C CG2   . THR D 1 17  ? -21.327 1.134   -26.633 1.00 29.10 ? 40  THR D CG2   1 
ATOM   3927 N N     . ALA D 1 18  ? -23.469 3.269   -28.955 1.00 26.64 ? 41  ALA D N     1 
ATOM   3928 C CA    . ALA D 1 18  ? -22.982 4.424   -29.704 1.00 25.18 ? 41  ALA D CA    1 
ATOM   3929 C C     . ALA D 1 18  ? -23.696 5.689   -29.273 1.00 29.48 ? 41  ALA D C     1 
ATOM   3930 O O     . ALA D 1 18  ? -23.081 6.758   -29.184 1.00 26.48 ? 41  ALA D O     1 
ATOM   3931 C CB    . ALA D 1 18  ? -23.165 4.202   -31.204 1.00 28.11 ? 41  ALA D CB    1 
ATOM   3932 N N     . LYS D 1 19  ? -24.992 5.585   -28.995 1.00 29.63 ? 42  LYS D N     1 
ATOM   3933 C CA    . LYS D 1 19  ? -25.721 6.758   -28.554 1.00 31.16 ? 42  LYS D CA    1 
ATOM   3934 C C     . LYS D 1 19  ? -25.210 7.228   -27.195 1.00 29.88 ? 42  LYS D C     1 
ATOM   3935 O O     . LYS D 1 19  ? -25.029 8.426   -26.973 1.00 31.45 ? 42  LYS D O     1 
ATOM   3936 C CB    . LYS D 1 19  ? -27.220 6.466   -28.531 1.00 33.93 ? 42  LYS D CB    1 
ATOM   3937 C CG    . LYS D 1 19  ? -28.013 7.565   -27.838 1.00 36.13 ? 42  LYS D CG    1 
ATOM   3938 C CD    . LYS D 1 19  ? -29.380 7.100   -27.417 1.00 40.47 ? 42  LYS D CD    1 
ATOM   3939 C CE    . LYS D 1 19  ? -30.422 7.472   -28.447 1.00 47.57 ? 42  LYS D CE    1 
ATOM   3940 N NZ    . LYS D 1 19  ? -31.272 8.593   -27.938 1.00 51.04 ? 42  LYS D NZ    1 
ATOM   3941 N N     . LYS D 1 20  ? -24.936 6.299   -26.277 1.00 28.12 ? 43  LYS D N     1 
ATOM   3942 C CA    . LYS D 1 20  ? -24.398 6.693   -24.973 1.00 27.11 ? 43  LYS D CA    1 
ATOM   3943 C C     . LYS D 1 20  ? -23.035 7.373   -25.108 1.00 30.47 ? 43  LYS D C     1 
ATOM   3944 O O     . LYS D 1 20  ? -22.775 8.392   -24.453 1.00 27.93 ? 43  LYS D O     1 
ATOM   3945 C CB    . LYS D 1 20  ? -24.306 5.465   -24.059 1.00 28.71 ? 43  LYS D CB    1 
ATOM   3946 C CG    . LYS D 1 20  ? -23.803 5.742   -22.660 1.00 27.96 ? 43  LYS D CG    1 
ATOM   3947 C CD    . LYS D 1 20  ? -24.727 6.705   -21.910 1.00 30.50 ? 43  LYS D CD    1 
ATOM   3948 C CE    . LYS D 1 20  ? -24.456 6.659   -20.407 1.00 33.03 ? 43  LYS D CE    1 
ATOM   3949 N NZ    . LYS D 1 20  ? -24.981 7.862   -19.680 1.00 28.68 ? 43  LYS D NZ    1 
ATOM   3950 N N     . MET D 1 21  ? -22.157 6.829   -25.960 1.00 23.06 ? 44  MET D N     1 
ATOM   3951 C CA    . MET D 1 21  ? -20.869 7.468   -26.207 1.00 27.33 ? 44  MET D CA    1 
ATOM   3952 C C     . MET D 1 21  ? -21.049 8.882   -26.750 1.00 30.35 ? 44  MET D C     1 
ATOM   3953 O O     . MET D 1 21  ? -20.339 9.808   -26.341 1.00 26.37 ? 44  MET D O     1 
ATOM   3954 C CB    . MET D 1 21  ? -20.049 6.618   -27.173 1.00 27.58 ? 44  MET D CB    1 
ATOM   3955 C CG    . MET D 1 21  ? -19.600 5.305   -26.555 1.00 27.15 ? 44  MET D CG    1 
ATOM   3956 S SD    . MET D 1 21  ? -18.618 4.275   -27.663 1.00 30.69 ? 44  MET D SD    1 
ATOM   3957 C CE    . MET D 1 21  ? -17.007 5.089   -27.613 1.00 24.09 ? 44  MET D CE    1 
ATOM   3958 N N     . ALA D 1 22  ? -22.009 9.072   -27.657 1.00 27.38 ? 45  ALA D N     1 
ATOM   3959 C CA    . ALA D 1 22  ? -22.223 10.362  -28.296 1.00 25.27 ? 45  ALA D CA    1 
ATOM   3960 C C     . ALA D 1 22  ? -22.943 11.353  -27.400 1.00 28.55 ? 45  ALA D C     1 
ATOM   3961 O O     . ALA D 1 22  ? -22.995 12.543  -27.730 1.00 27.67 ? 45  ALA D O     1 
ATOM   3962 C CB    . ALA D 1 22  ? -23.013 10.179  -29.591 1.00 29.96 ? 45  ALA D CB    1 
ATOM   3963 N N     . SER D 1 23  ? -23.488 10.906  -26.272 1.00 28.19 ? 46  SER D N     1 
ATOM   3964 C CA    . SER D 1 23  ? -24.272 11.806  -25.443 1.00 29.31 ? 46  SER D CA    1 
ATOM   3965 C C     . SER D 1 23  ? -23.403 12.808  -24.695 1.00 25.85 ? 46  SER D C     1 
ATOM   3966 O O     . SER D 1 23  ? -23.930 13.809  -24.208 1.00 31.41 ? 46  SER D O     1 
ATOM   3967 C CB    . SER D 1 23  ? -25.132 10.991  -24.475 1.00 30.76 ? 46  SER D CB    1 
ATOM   3968 O OG    . SER D 1 23  ? -24.327 10.381  -23.488 1.00 29.83 ? 46  SER D OG    1 
ATOM   3969 N N     . VAL D 1 24  ? -22.085 12.591  -24.617 1.00 27.04 ? 47  VAL D N     1 
ATOM   3970 C CA    . VAL D 1 24  ? -21.215 13.570  -23.959 1.00 23.48 ? 47  VAL D CA    1 
ATOM   3971 C C     . VAL D 1 24  ? -21.055 14.852  -24.774 1.00 29.19 ? 47  VAL D C     1 
ATOM   3972 O O     . VAL D 1 24  ? -20.659 15.885  -24.222 1.00 28.92 ? 47  VAL D O     1 
ATOM   3973 C CB    . VAL D 1 24  ? -19.828 12.967  -23.658 1.00 26.17 ? 47  VAL D CB    1 
ATOM   3974 C CG1   . VAL D 1 24  ? -19.968 11.627  -22.942 1.00 30.15 ? 47  VAL D CG1   1 
ATOM   3975 C CG2   . VAL D 1 24  ? -19.007 12.805  -24.934 1.00 25.91 ? 47  VAL D CG2   1 
ATOM   3976 N N     . ILE D 1 25  ? -21.361 14.820  -26.072 1.00 29.67 ? 48  ILE D N     1 
ATOM   3977 C CA    . ILE D 1 25  ? -21.096 15.957  -26.947 1.00 24.99 ? 48  ILE D CA    1 
ATOM   3978 C C     . ILE D 1 25  ? -21.981 17.141  -26.571 1.00 31.11 ? 48  ILE D C     1 
ATOM   3979 O O     . ILE D 1 25  ? -23.170 16.986  -26.254 1.00 31.87 ? 48  ILE D O     1 
ATOM   3980 C CB    . ILE D 1 25  ? -21.306 15.538  -28.413 1.00 28.76 ? 48  ILE D CB    1 
ATOM   3981 C CG1   . ILE D 1 25  ? -20.272 14.478  -28.794 1.00 27.10 ? 48  ILE D CG1   1 
ATOM   3982 C CG2   . ILE D 1 25  ? -21.233 16.742  -29.355 1.00 29.76 ? 48  ILE D CG2   1 
ATOM   3983 C CD1   . ILE D 1 25  ? -20.511 13.840  -30.142 1.00 28.56 ? 48  ILE D CD1   1 
ATOM   3984 N N     . ASN D 1 26  ? -21.393 18.336  -26.585 1.00 29.54 ? 49  ASN D N     1 
ATOM   3985 C CA    . ASN D 1 26  ? -22.149 19.571  -26.470 1.00 31.78 ? 49  ASN D CA    1 
ATOM   3986 C C     . ASN D 1 26  ? -22.266 20.181  -27.864 1.00 33.75 ? 49  ASN D C     1 
ATOM   3987 O O     . ASN D 1 26  ? -21.317 20.820  -28.337 1.00 30.99 ? 49  ASN D O     1 
ATOM   3988 C CB    . ASN D 1 26  ? -21.463 20.541  -25.504 1.00 28.93 ? 49  ASN D CB    1 
ATOM   3989 C CG    . ASN D 1 26  ? -22.213 21.857  -25.361 1.00 36.85 ? 49  ASN D CG    1 
ATOM   3990 O OD1   . ASN D 1 26  ? -23.276 22.061  -25.963 1.00 37.52 ? 49  ASN D OD1   1 
ATOM   3991 N ND2   . ASN D 1 26  ? -21.671 22.752  -24.550 1.00 34.03 ? 49  ASN D ND2   1 
ATOM   3992 N N     . PRO D 1 27  ? -23.392 20.012  -28.563 1.00 32.55 ? 50  PRO D N     1 
ATOM   3993 C CA    . PRO D 1 27  ? -23.482 20.502  -29.947 1.00 33.10 ? 50  PRO D CA    1 
ATOM   3994 C C     . PRO D 1 27  ? -23.520 22.021  -30.065 1.00 40.00 ? 50  PRO D C     1 
ATOM   3995 O O     . PRO D 1 27  ? -23.470 22.536  -31.189 1.00 36.42 ? 50  PRO D O     1 
ATOM   3996 C CB    . PRO D 1 27  ? -24.781 19.868  -30.456 1.00 35.80 ? 50  PRO D CB    1 
ATOM   3997 C CG    . PRO D 1 27  ? -25.605 19.685  -29.229 1.00 39.34 ? 50  PRO D CG    1 
ATOM   3998 C CD    . PRO D 1 27  ? -24.639 19.379  -28.110 1.00 33.99 ? 50  PRO D CD    1 
ATOM   3999 N N     . HIS D 1 28  ? -23.571 22.755  -28.955 1.00 37.74 ? 51  HIS D N     1 
ATOM   4000 C CA    . HIS D 1 28  ? -23.637 24.209  -28.997 1.00 38.31 ? 51  HIS D CA    1 
ATOM   4001 C C     . HIS D 1 28  ? -22.357 24.871  -28.514 1.00 38.39 ? 51  HIS D C     1 
ATOM   4002 O O     . HIS D 1 28  ? -22.345 26.088  -28.313 1.00 36.53 ? 51  HIS D O     1 
ATOM   4003 C CB    . HIS D 1 28  ? -24.833 24.703  -28.175 1.00 42.13 ? 51  HIS D CB    1 
ATOM   4004 C CG    . HIS D 1 28  ? -26.134 24.092  -28.593 1.00 45.06 ? 51  HIS D CG    1 
ATOM   4005 N ND1   . HIS D 1 28  ? -26.718 24.350  -29.815 1.00 50.26 ? 51  HIS D ND1   1 
ATOM   4006 C CD2   . HIS D 1 28  ? -26.950 23.211  -27.966 1.00 44.31 ? 51  HIS D CD2   1 
ATOM   4007 C CE1   . HIS D 1 28  ? -27.842 23.664  -29.919 1.00 42.12 ? 51  HIS D CE1   1 
ATOM   4008 N NE2   . HIS D 1 28  ? -28.007 22.965  -28.811 1.00 46.59 ? 51  HIS D NE2   1 
ATOM   4009 N N     . SER D 1 29  ? -21.282 24.104  -28.312 1.00 33.54 ? 52  SER D N     1 
ATOM   4010 C CA    . SER D 1 29  ? -20.026 24.689  -27.855 1.00 33.84 ? 52  SER D CA    1 
ATOM   4011 C C     . SER D 1 29  ? -19.286 25.460  -28.942 1.00 35.07 ? 52  SER D C     1 
ATOM   4012 O O     . SER D 1 29  ? -18.321 26.165  -28.622 1.00 29.56 ? 52  SER D O     1 
ATOM   4013 C CB    . SER D 1 29  ? -19.101 23.596  -27.328 1.00 33.46 ? 52  SER D CB    1 
ATOM   4014 O OG    . SER D 1 29  ? -18.721 22.740  -28.397 1.00 33.94 ? 52  SER D OG    1 
ATOM   4015 N N     . GLY D 1 30  ? -19.672 25.319  -30.209 1.00 31.52 ? 53  GLY D N     1 
ATOM   4016 C CA    . GLY D 1 30  ? -18.930 25.950  -31.284 1.00 29.21 ? 53  GLY D CA    1 
ATOM   4017 C C     . GLY D 1 30  ? -17.607 25.298  -31.628 1.00 35.56 ? 53  GLY D C     1 
ATOM   4018 O O     . GLY D 1 30  ? -16.868 25.842  -32.459 1.00 32.23 ? 53  GLY D O     1 
ATOM   4019 N N     . LEU D 1 31  ? -17.275 24.141  -31.012 1.00 30.46 ? 54  LEU D N     1 
ATOM   4020 C CA    . LEU D 1 31  ? -16.054 23.395  -31.297 1.00 31.90 ? 54  LEU D CA    1 
ATOM   4021 C C     . LEU D 1 31  ? -16.373 22.111  -32.068 1.00 29.43 ? 54  LEU D C     1 
ATOM   4022 O O     . LEU D 1 31  ? -17.432 21.503  -31.872 1.00 28.75 ? 54  LEU D O     1 
ATOM   4023 C CB    . LEU D 1 31  ? -15.304 23.029  -30.009 1.00 28.82 ? 54  LEU D CB    1 
ATOM   4024 C CG    . LEU D 1 31  ? -14.832 24.200  -29.152 1.00 30.21 ? 54  LEU D CG    1 
ATOM   4025 C CD1   . LEU D 1 31  ? -14.293 23.706  -27.807 1.00 24.19 ? 54  LEU D CD1   1 
ATOM   4026 C CD2   . LEU D 1 31  ? -13.776 24.987  -29.901 1.00 29.54 ? 54  LEU D CD2   1 
ATOM   4027 N N     . PRO D 1 32  ? -15.479 21.675  -32.950 1.00 31.93 ? 55  PRO D N     1 
ATOM   4028 C CA    . PRO D 1 32  ? -15.692 20.408  -33.657 1.00 31.40 ? 55  PRO D CA    1 
ATOM   4029 C C     . PRO D 1 32  ? -15.444 19.212  -32.744 1.00 28.18 ? 55  PRO D C     1 
ATOM   4030 O O     . PRO D 1 32  ? -14.928 19.337  -31.634 1.00 29.39 ? 55  PRO D O     1 
ATOM   4031 C CB    . PRO D 1 32  ? -14.667 20.473  -34.793 1.00 28.39 ? 55  PRO D CB    1 
ATOM   4032 C CG    . PRO D 1 32  ? -13.565 21.305  -34.243 1.00 29.78 ? 55  PRO D CG    1 
ATOM   4033 C CD    . PRO D 1 32  ? -14.234 22.343  -33.378 1.00 32.88 ? 55  PRO D CD    1 
ATOM   4034 N N     . VAL D 1 33  ? -15.794 18.030  -33.247 1.00 29.37 ? 56  VAL D N     1 
ATOM   4035 C CA    . VAL D 1 33  ? -15.694 16.775  -32.503 1.00 25.84 ? 56  VAL D CA    1 
ATOM   4036 C C     . VAL D 1 33  ? -14.637 15.893  -33.158 1.00 31.29 ? 56  VAL D C     1 
ATOM   4037 O O     . VAL D 1 33  ? -14.536 15.842  -34.391 1.00 29.19 ? 56  VAL D O     1 
ATOM   4038 C CB    . VAL D 1 33  ? -17.060 16.057  -32.452 1.00 31.51 ? 56  VAL D CB    1 
ATOM   4039 C CG1   . VAL D 1 33  ? -16.929 14.649  -31.868 1.00 26.74 ? 56  VAL D CG1   1 
ATOM   4040 C CG2   . VAL D 1 33  ? -18.056 16.874  -31.639 1.00 30.43 ? 56  VAL D CG2   1 
ATOM   4041 N N     . LEU D 1 34  ? -13.841 15.205  -32.331 1.00 27.58 ? 57  LEU D N     1 
ATOM   4042 C CA    . LEU D 1 34  ? -12.816 14.278  -32.797 1.00 24.26 ? 57  LEU D CA    1 
ATOM   4043 C C     . LEU D 1 34  ? -13.259 12.853  -32.493 1.00 28.48 ? 57  LEU D C     1 
ATOM   4044 O O     . LEU D 1 34  ? -13.631 12.541  -31.346 1.00 26.35 ? 57  LEU D O     1 
ATOM   4045 C CB    . LEU D 1 34  ? -11.456 14.566  -32.139 1.00 25.47 ? 57  LEU D CB    1 
ATOM   4046 C CG    . LEU D 1 34  ? -10.257 13.679  -32.520 1.00 24.85 ? 57  LEU D CG    1 
ATOM   4047 C CD1   . LEU D 1 34  ? -10.009 13.721  -34.024 1.00 27.23 ? 57  LEU D CD1   1 
ATOM   4048 C CD2   . LEU D 1 34  ? -8.975  14.065  -31.774 1.00 24.79 ? 57  LEU D CD2   1 
ATOM   4049 N N     . GLU D 1 35  ? -13.242 12.002  -33.521 1.00 25.88 ? 58  GLU D N     1 
ATOM   4050 C CA    . GLU D 1 35  ? -13.554 10.583  -33.400 1.00 28.07 ? 58  GLU D CA    1 
ATOM   4051 C C     . GLU D 1 35  ? -12.342 9.753   -33.805 1.00 29.57 ? 58  GLU D C     1 
ATOM   4052 O O     . GLU D 1 35  ? -11.687 10.039  -34.818 1.00 27.75 ? 58  GLU D O     1 
ATOM   4053 C CB    . GLU D 1 35  ? -14.767 10.188  -34.270 1.00 28.97 ? 58  GLU D CB    1 
ATOM   4054 C CG    . GLU D 1 35  ? -15.055 8.681   -34.227 1.00 31.67 ? 58  GLU D CG    1 
ATOM   4055 C CD    . GLU D 1 35  ? -16.252 8.231   -35.070 1.00 37.50 ? 58  GLU D CD    1 
ATOM   4056 O OE1   . GLU D 1 35  ? -16.686 7.069   -34.877 1.00 37.99 ? 58  GLU D OE1   1 
ATOM   4057 O OE2   . GLU D 1 35  ? -16.758 9.006   -35.924 1.00 34.37 ? 58  GLU D OE2   1 
ATOM   4058 N N     . LEU D 1 36  ? -12.037 8.725   -33.015 1.00 23.55 ? 59  LEU D N     1 
ATOM   4059 C CA    . LEU D 1 36  ? -10.892 7.860   -33.276 1.00 27.05 ? 59  LEU D CA    1 
ATOM   4060 C C     . LEU D 1 36  ? -11.377 6.445   -33.571 1.00 31.76 ? 59  LEU D C     1 
ATOM   4061 O O     . LEU D 1 36  ? -12.094 5.849   -32.757 1.00 28.18 ? 59  LEU D O     1 
ATOM   4062 C CB    . LEU D 1 36  ? -9.921  7.872   -32.091 1.00 23.49 ? 59  LEU D CB    1 
ATOM   4063 C CG    . LEU D 1 36  ? -9.486  9.250   -31.567 1.00 27.73 ? 59  LEU D CG    1 
ATOM   4064 C CD1   . LEU D 1 36  ? -8.529  9.103   -30.378 1.00 25.37 ? 59  LEU D CD1   1 
ATOM   4065 C CD2   . LEU D 1 36  ? -8.845  10.110  -32.676 1.00 23.34 ? 59  LEU D CD2   1 
ATOM   4066 N N     . GLY D 1 37  ? -10.972 5.907   -34.726 1.00 27.07 ? 60  GLY D N     1 
ATOM   4067 C CA    . GLY D 1 37  ? -11.333 4.569   -35.154 1.00 29.63 ? 60  GLY D CA    1 
ATOM   4068 C C     . GLY D 1 37  ? -12.795 4.379   -35.536 1.00 34.09 ? 60  GLY D C     1 
ATOM   4069 O O     . GLY D 1 37  ? -13.491 3.537   -34.965 1.00 32.42 ? 60  GLY D O     1 
ATOM   4070 N N     . PRO D 1 38  ? -13.291 5.134   -36.527 1.00 35.23 ? 61  PRO D N     1 
ATOM   4071 C CA    . PRO D 1 38  ? -14.731 5.044   -36.861 1.00 30.03 ? 61  PRO D CA    1 
ATOM   4072 C C     . PRO D 1 38  ? -15.169 3.699   -37.442 1.00 34.92 ? 61  PRO D C     1 
ATOM   4073 O O     . PRO D 1 38  ? -16.356 3.371   -37.337 1.00 32.06 ? 61  PRO D O     1 
ATOM   4074 C CB    . PRO D 1 38  ? -14.935 6.178   -37.877 1.00 33.66 ? 61  PRO D CB    1 
ATOM   4075 C CG    . PRO D 1 38  ? -13.573 6.408   -38.484 1.00 30.40 ? 61  PRO D CG    1 
ATOM   4076 C CD    . PRO D 1 38  ? -12.561 6.065   -37.412 1.00 31.36 ? 61  PRO D CD    1 
ATOM   4077 N N     . GLY D 1 39  ? -14.280 2.922   -38.061 1.00 35.65 ? 62  GLY D N     1 
ATOM   4078 C CA    . GLY D 1 39  ? -14.653 1.575   -38.496 1.00 34.38 ? 62  GLY D CA    1 
ATOM   4079 C C     . GLY D 1 39  ? -15.784 1.584   -39.519 1.00 37.19 ? 62  GLY D C     1 
ATOM   4080 O O     . GLY D 1 39  ? -15.674 2.168   -40.604 1.00 37.68 ? 62  GLY D O     1 
ATOM   4081 N N     . THR D 1 40  ? -16.904 0.942   -39.191 1.00 36.99 ? 63  THR D N     1 
ATOM   4082 C CA    . THR D 1 40  ? -18.040 0.959   -40.102 1.00 39.53 ? 63  THR D CA    1 
ATOM   4083 C C     . THR D 1 40  ? -18.884 2.220   -39.978 1.00 43.54 ? 63  THR D C     1 
ATOM   4084 O O     . THR D 1 40  ? -19.781 2.427   -40.803 1.00 42.39 ? 63  THR D O     1 
ATOM   4085 C CB    . THR D 1 40  ? -18.924 -0.267  -39.880 1.00 41.14 ? 63  THR D CB    1 
ATOM   4086 O OG1   . THR D 1 40  ? -19.378 -0.295  -38.519 1.00 43.41 ? 63  THR D OG1   1 
ATOM   4087 C CG2   . THR D 1 40  ? -18.149 -1.534  -40.182 1.00 42.51 ? 63  THR D CG2   1 
ATOM   4088 N N     . GLY D 1 41  ? -18.629 3.061   -38.978 1.00 38.78 ? 64  GLY D N     1 
ATOM   4089 C CA    . GLY D 1 41  ? -19.321 4.323   -38.855 1.00 34.41 ? 64  GLY D CA    1 
ATOM   4090 C C     . GLY D 1 41  ? -20.550 4.338   -37.973 1.00 37.35 ? 64  GLY D C     1 
ATOM   4091 O O     . GLY D 1 41  ? -21.304 5.316   -38.020 1.00 35.98 ? 64  GLY D O     1 
ATOM   4092 N N     . VAL D 1 42  ? -20.777 3.306   -37.154 1.00 33.99 ? 65  VAL D N     1 
ATOM   4093 C CA    . VAL D 1 42  ? -21.967 3.326   -36.307 1.00 33.54 ? 65  VAL D CA    1 
ATOM   4094 C C     . VAL D 1 42  ? -21.894 4.462   -35.282 1.00 30.40 ? 65  VAL D C     1 
ATOM   4095 O O     . VAL D 1 42  ? -22.913 5.083   -34.958 1.00 28.42 ? 65  VAL D O     1 
ATOM   4096 C CB    . VAL D 1 42  ? -22.170 1.946   -35.645 1.00 35.93 ? 65  VAL D CB    1 
ATOM   4097 C CG1   . VAL D 1 42  ? -20.898 1.479   -34.974 1.00 39.86 ? 65  VAL D CG1   1 
ATOM   4098 C CG2   . VAL D 1 42  ? -23.328 1.984   -34.659 1.00 35.01 ? 65  VAL D CG2   1 
ATOM   4099 N N     . ILE D 1 43  ? -20.696 4.777   -34.784 1.00 29.87 ? 66  ILE D N     1 
ATOM   4100 C CA    . ILE D 1 43  ? -20.557 5.885   -33.840 1.00 29.12 ? 66  ILE D CA    1 
ATOM   4101 C C     . ILE D 1 43  ? -20.593 7.223   -34.572 1.00 30.16 ? 66  ILE D C     1 
ATOM   4102 O O     . ILE D 1 43  ? -21.177 8.194   -34.077 1.00 31.16 ? 66  ILE D O     1 
ATOM   4103 C CB    . ILE D 1 43  ? -19.264 5.713   -33.018 1.00 31.25 ? 66  ILE D CB    1 
ATOM   4104 C CG1   . ILE D 1 43  ? -19.357 4.463   -32.135 1.00 28.35 ? 66  ILE D CG1   1 
ATOM   4105 C CG2   . ILE D 1 43  ? -18.958 6.968   -32.191 1.00 28.97 ? 66  ILE D CG2   1 
ATOM   4106 C CD1   . ILE D 1 43  ? -18.120 4.246   -31.281 1.00 32.28 ? 66  ILE D CD1   1 
ATOM   4107 N N     . THR D 1 44  ? -19.969 7.292   -35.757 1.00 31.55 ? 67  THR D N     1 
ATOM   4108 C CA    . THR D 1 44  ? -20.116 8.459   -36.628 1.00 31.18 ? 67  THR D CA    1 
ATOM   4109 C C     . THR D 1 44  ? -21.584 8.824   -36.804 1.00 30.82 ? 67  THR D C     1 
ATOM   4110 O O     . THR D 1 44  ? -21.980 9.982   -36.626 1.00 34.12 ? 67  THR D O     1 
ATOM   4111 C CB    . THR D 1 44  ? -19.472 8.182   -37.993 1.00 34.72 ? 67  THR D CB    1 
ATOM   4112 O OG1   . THR D 1 44  ? -18.164 7.624   -37.818 1.00 34.44 ? 67  THR D OG1   1 
ATOM   4113 C CG2   . THR D 1 44  ? -19.357 9.467   -38.814 1.00 34.51 ? 67  THR D CG2   1 
ATOM   4114 N N     . LYS D 1 45  ? -22.414 7.832   -37.123 1.00 29.57 ? 68  LYS D N     1 
ATOM   4115 C CA    . LYS D 1 45  ? -23.843 8.081   -37.292 1.00 31.90 ? 68  LYS D CA    1 
ATOM   4116 C C     . LYS D 1 45  ? -24.464 8.679   -36.032 1.00 33.37 ? 68  LYS D C     1 
ATOM   4117 O O     . LYS D 1 45  ? -25.289 9.596   -36.116 1.00 36.41 ? 68  LYS D O     1 
ATOM   4118 C CB    . LYS D 1 45  ? -24.548 6.777   -37.674 1.00 36.54 ? 68  LYS D CB    1 
ATOM   4119 C CG    . LYS D 1 45  ? -26.066 6.883   -37.882 1.00 38.81 ? 68  LYS D CG    1 
ATOM   4120 C CD    . LYS D 1 45  ? -26.622 5.588   -38.502 1.00 44.89 ? 68  LYS D CD    1 
ATOM   4121 C CE    . LYS D 1 45  ? -28.084 5.743   -38.929 1.00 52.11 ? 68  LYS D CE    1 
ATOM   4122 N NZ    . LYS D 1 45  ? -29.026 5.599   -37.783 1.00 56.63 ? 68  LYS D NZ    1 
ATOM   4123 N N     . ALA D 1 46  ? -24.087 8.175   -34.851 1.00 29.86 ? 69  ALA D N     1 
ATOM   4124 C CA    . ALA D 1 46  ? -24.659 8.703   -33.613 1.00 31.78 ? 69  ALA D CA    1 
ATOM   4125 C C     . ALA D 1 46  ? -24.146 10.108  -33.302 1.00 33.42 ? 69  ALA D C     1 
ATOM   4126 O O     . ALA D 1 46  ? -24.866 10.905  -32.684 1.00 32.65 ? 69  ALA D O     1 
ATOM   4127 C CB    . ALA D 1 46  ? -24.366 7.758   -32.442 1.00 30.53 ? 69  ALA D CB    1 
ATOM   4128 N N     . ILE D 1 47  ? -22.914 10.429  -33.712 1.00 32.67 ? 70  ILE D N     1 
ATOM   4129 C CA    . ILE D 1 47  ? -22.407 11.789  -33.544 1.00 31.91 ? 70  ILE D CA    1 
ATOM   4130 C C     . ILE D 1 47  ? -23.178 12.755  -34.435 1.00 33.23 ? 70  ILE D C     1 
ATOM   4131 O O     . ILE D 1 47  ? -23.590 13.834  -33.995 1.00 31.18 ? 70  ILE D O     1 
ATOM   4132 C CB    . ILE D 1 47  ? -20.899 11.855  -33.836 1.00 29.48 ? 70  ILE D CB    1 
ATOM   4133 C CG1   . ILE D 1 47  ? -20.100 11.084  -32.787 1.00 28.17 ? 70  ILE D CG1   1 
ATOM   4134 C CG2   . ILE D 1 47  ? -20.437 13.307  -33.880 1.00 29.48 ? 70  ILE D CG2   1 
ATOM   4135 C CD1   . ILE D 1 47  ? -18.644 10.870  -33.191 1.00 25.74 ? 70  ILE D CD1   1 
ATOM   4136 N N     . LEU D 1 48  ? -23.368 12.387  -35.708 1.00 36.07 ? 71  LEU D N     1 
ATOM   4137 C CA    . LEU D 1 48  ? -24.124 13.241  -36.623 1.00 37.41 ? 71  LEU D CA    1 
ATOM   4138 C C     . LEU D 1 48  ? -25.566 13.416  -36.158 1.00 35.39 ? 71  LEU D C     1 
ATOM   4139 O O     . LEU D 1 48  ? -26.168 14.472  -36.384 1.00 39.42 ? 71  LEU D O     1 
ATOM   4140 C CB    . LEU D 1 48  ? -24.069 12.673  -38.046 1.00 31.66 ? 71  LEU D CB    1 
ATOM   4141 C CG    . LEU D 1 48  ? -22.662 12.612  -38.656 1.00 37.25 ? 71  LEU D CG    1 
ATOM   4142 C CD1   . LEU D 1 48  ? -22.639 11.918  -40.016 1.00 33.12 ? 71  LEU D CD1   1 
ATOM   4143 C CD2   . LEU D 1 48  ? -22.049 14.000  -38.764 1.00 37.41 ? 71  LEU D CD2   1 
ATOM   4144 N N     . ALA D 1 49  ? -26.124 12.414  -35.476 1.00 37.07 ? 72  ALA D N     1 
ATOM   4145 C CA    . ALA D 1 49  ? -27.477 12.524  -34.937 1.00 34.68 ? 72  ALA D CA    1 
ATOM   4146 C C     . ALA D 1 49  ? -27.600 13.541  -33.802 1.00 38.65 ? 72  ALA D C     1 
ATOM   4147 O O     . ALA D 1 49  ? -28.725 13.904  -33.447 1.00 39.31 ? 72  ALA D O     1 
ATOM   4148 C CB    . ALA D 1 49  ? -27.959 11.159  -34.451 1.00 38.47 ? 72  ALA D CB    1 
ATOM   4149 N N     . ARG D 1 50  ? -26.489 14.001  -33.217 1.00 36.81 ? 73  ARG D N     1 
ATOM   4150 C CA    . ARG D 1 50  ? -26.555 15.048  -32.201 1.00 36.52 ? 73  ARG D CA    1 
ATOM   4151 C C     . ARG D 1 50  ? -26.747 16.441  -32.793 1.00 40.26 ? 73  ARG D C     1 
ATOM   4152 O O     . ARG D 1 50  ? -26.910 17.400  -32.034 1.00 37.91 ? 73  ARG D O     1 
ATOM   4153 C CB    . ARG D 1 50  ? -25.283 15.059  -31.341 1.00 31.84 ? 73  ARG D CB    1 
ATOM   4154 C CG    . ARG D 1 50  ? -25.060 13.817  -30.487 1.00 35.04 ? 73  ARG D CG    1 
ATOM   4155 C CD    . ARG D 1 50  ? -26.203 13.564  -29.507 1.00 34.61 ? 73  ARG D CD    1 
ATOM   4156 N NE    . ARG D 1 50  ? -26.615 14.760  -28.770 1.00 32.66 ? 73  ARG D NE    1 
ATOM   4157 C CZ    . ARG D 1 50  ? -25.926 15.304  -27.772 1.00 34.24 ? 73  ARG D CZ    1 
ATOM   4158 N NH1   . ARG D 1 50  ? -24.769 14.773  -27.383 1.00 31.74 ? 73  ARG D NH1   1 
ATOM   4159 N NH2   . ARG D 1 50  ? -26.389 16.391  -27.170 1.00 34.76 ? 73  ARG D NH2   1 
ATOM   4160 N N     . GLY D 1 51  ? -26.724 16.580  -34.112 1.00 38.79 ? 74  GLY D N     1 
ATOM   4161 C CA    . GLY D 1 51  ? -26.768 17.882  -34.738 1.00 40.64 ? 74  GLY D CA    1 
ATOM   4162 C C     . GLY D 1 51  ? -25.420 18.447  -35.113 1.00 44.69 ? 74  GLY D C     1 
ATOM   4163 O O     . GLY D 1 51  ? -25.348 19.613  -35.513 1.00 50.62 ? 74  GLY D O     1 
ATOM   4164 N N     . ILE D 1 52  ? -24.349 17.665  -34.978 1.00 41.49 ? 75  ILE D N     1 
ATOM   4165 C CA    . ILE D 1 52  ? -23.028 18.102  -35.399 1.00 39.48 ? 75  ILE D CA    1 
ATOM   4166 C C     . ILE D 1 52  ? -22.982 18.143  -36.920 1.00 43.95 ? 75  ILE D C     1 
ATOM   4167 O O     . ILE D 1 52  ? -23.348 17.173  -37.597 1.00 40.88 ? 75  ILE D O     1 
ATOM   4168 C CB    . ILE D 1 52  ? -21.959 17.162  -34.822 1.00 41.15 ? 75  ILE D CB    1 
ATOM   4169 C CG1   . ILE D 1 52  ? -21.918 17.300  -33.298 1.00 40.21 ? 75  ILE D CG1   1 
ATOM   4170 C CG2   . ILE D 1 52  ? -20.587 17.420  -35.448 1.00 35.45 ? 75  ILE D CG2   1 
ATOM   4171 C CD1   . ILE D 1 52  ? -21.800 18.723  -32.830 1.00 36.19 ? 75  ILE D CD1   1 
ATOM   4172 N N     . LYS D 1 53  ? -22.553 19.271  -37.467 1.00 41.89 ? 76  LYS D N     1 
ATOM   4173 C CA    . LYS D 1 53  ? -22.430 19.360  -38.912 1.00 44.03 ? 76  LYS D CA    1 
ATOM   4174 C C     . LYS D 1 53  ? -21.325 18.421  -39.395 1.00 41.66 ? 76  LYS D C     1 
ATOM   4175 O O     . LYS D 1 53  ? -20.284 18.300  -38.739 1.00 38.62 ? 76  LYS D O     1 
ATOM   4176 C CB    . LYS D 1 53  ? -22.139 20.801  -39.344 1.00 44.74 ? 76  LYS D CB    1 
ATOM   4177 C CG    . LYS D 1 53  ? -23.310 21.756  -39.118 1.00 46.41 ? 76  LYS D CG    1 
ATOM   4178 C CD    . LYS D 1 53  ? -24.572 21.267  -39.842 1.00 55.81 ? 76  LYS D CD    1 
ATOM   4179 C CE    . LYS D 1 53  ? -25.697 20.875  -38.864 1.00 61.17 ? 76  LYS D CE    1 
ATOM   4180 N NZ    . LYS D 1 53  ? -26.556 19.759  -39.395 1.00 60.06 ? 76  LYS D NZ    1 
ATOM   4181 N N     . PRO D 1 54  ? -21.531 17.732  -40.523 1.00 40.57 ? 77  PRO D N     1 
ATOM   4182 C CA    . PRO D 1 54  ? -20.503 16.805  -41.027 1.00 38.77 ? 77  PRO D CA    1 
ATOM   4183 C C     . PRO D 1 54  ? -19.102 17.392  -41.081 1.00 39.44 ? 77  PRO D C     1 
ATOM   4184 O O     . PRO D 1 54  ? -18.137 16.712  -40.711 1.00 34.01 ? 77  PRO D O     1 
ATOM   4185 C CB    . PRO D 1 54  ? -21.026 16.463  -42.427 1.00 39.56 ? 77  PRO D CB    1 
ATOM   4186 C CG    . PRO D 1 54  ? -22.492 16.540  -42.284 1.00 42.74 ? 77  PRO D CG    1 
ATOM   4187 C CD    . PRO D 1 54  ? -22.766 17.668  -41.323 1.00 42.17 ? 77  PRO D CD    1 
ATOM   4188 N N     . GLU D 1 55  ? -18.964 18.644  -41.530 1.00 38.22 ? 78  GLU D N     1 
ATOM   4189 C CA    . GLU D 1 55  ? -17.650 19.269  -41.607 1.00 39.33 ? 78  GLU D CA    1 
ATOM   4190 C C     . GLU D 1 55  ? -17.039 19.490  -40.232 1.00 36.50 ? 78  GLU D C     1 
ATOM   4191 O O     . GLU D 1 55  ? -15.818 19.614  -40.122 1.00 36.06 ? 78  GLU D O     1 
ATOM   4192 C CB    . GLU D 1 55  ? -17.745 20.610  -42.353 1.00 41.55 ? 78  GLU D CB    1 
ATOM   4193 C CG    . GLU D 1 55  ? -18.677 20.593  -43.570 1.00 50.69 ? 78  GLU D CG    1 
ATOM   4194 C CD    . GLU D 1 55  ? -20.156 20.694  -43.196 1.00 51.04 ? 78  GLU D CD    1 
ATOM   4195 O OE1   . GLU D 1 55  ? -20.823 19.638  -43.144 1.00 52.30 ? 78  GLU D OE1   1 
ATOM   4196 O OE2   . GLU D 1 55  ? -20.649 21.826  -42.951 1.00 59.66 ? 78  GLU D OE2   1 
ATOM   4197 N N     . SER D 1 56  ? -17.855 19.542  -39.185 1.00 38.14 ? 79  SER D N     1 
ATOM   4198 C CA    . SER D 1 56  ? -17.366 19.723  -37.827 1.00 38.85 ? 79  SER D CA    1 
ATOM   4199 C C     . SER D 1 56  ? -16.976 18.408  -37.144 1.00 35.95 ? 79  SER D C     1 
ATOM   4200 O O     . SER D 1 56  ? -16.767 18.397  -35.924 1.00 35.30 ? 79  SER D O     1 
ATOM   4201 C CB    . SER D 1 56  ? -18.423 20.450  -36.992 1.00 39.38 ? 79  SER D CB    1 
ATOM   4202 O OG    . SER D 1 56  ? -18.634 21.757  -37.488 1.00 43.25 ? 79  SER D OG    1 
ATOM   4203 N N     . LEU D 1 57  ? -16.883 17.303  -37.887 1.00 35.52 ? 80  LEU D N     1 
ATOM   4204 C CA    . LEU D 1 57  ? -16.461 16.021  -37.327 1.00 28.92 ? 80  LEU D CA    1 
ATOM   4205 C C     . LEU D 1 57  ? -15.186 15.568  -38.019 1.00 29.11 ? 80  LEU D C     1 
ATOM   4206 O O     . LEU D 1 57  ? -15.177 15.341  -39.235 1.00 34.82 ? 80  LEU D O     1 
ATOM   4207 C CB    . LEU D 1 57  ? -17.558 14.962  -37.458 1.00 26.94 ? 80  LEU D CB    1 
ATOM   4208 C CG    . LEU D 1 57  ? -17.176 13.554  -36.969 1.00 29.77 ? 80  LEU D CG    1 
ATOM   4209 C CD1   . LEU D 1 57  ? -16.936 13.520  -35.465 1.00 25.27 ? 80  LEU D CD1   1 
ATOM   4210 C CD2   . LEU D 1 57  ? -18.235 12.545  -37.372 1.00 30.34 ? 80  LEU D CD2   1 
ATOM   4211 N N     . THR D 1 58  ? -14.102 15.475  -37.259 1.00 28.96 ? 81  THR D N     1 
ATOM   4212 C CA    . THR D 1 58  ? -12.856 14.894  -37.741 1.00 31.13 ? 81  THR D CA    1 
ATOM   4213 C C     . THR D 1 58  ? -12.729 13.489  -37.164 1.00 30.56 ? 81  THR D C     1 
ATOM   4214 O O     . THR D 1 58  ? -12.820 13.304  -35.946 1.00 28.70 ? 81  THR D O     1 
ATOM   4215 C CB    . THR D 1 58  ? -11.652 15.751  -37.342 1.00 30.81 ? 81  THR D CB    1 
ATOM   4216 O OG1   . THR D 1 58  ? -11.718 17.015  -38.013 1.00 31.54 ? 81  THR D OG1   1 
ATOM   4217 C CG2   . THR D 1 58  ? -10.360 15.056  -37.716 1.00 35.33 ? 81  THR D CG2   1 
ATOM   4218 N N     . ALA D 1 59  ? -12.535 12.501  -38.037 1.00 31.03 ? 82  ALA D N     1 
ATOM   4219 C CA    . ALA D 1 59  ? -12.517 11.100  -37.631 1.00 29.24 ? 82  ALA D CA    1 
ATOM   4220 C C     . ALA D 1 59  ? -11.279 10.431  -38.212 1.00 31.61 ? 82  ALA D C     1 
ATOM   4221 O O     . ALA D 1 59  ? -11.100 10.408  -39.435 1.00 34.18 ? 82  ALA D O     1 
ATOM   4222 C CB    . ALA D 1 59  ? -13.792 10.395  -38.084 1.00 24.74 ? 82  ALA D CB    1 
ATOM   4223 N N     . ILE D 1 60  ? -10.425 9.900   -37.341 1.00 24.89 ? 83  ILE D N     1 
ATOM   4224 C CA    . ILE D 1 60  ? -9.129  9.345   -37.733 1.00 31.15 ? 83  ILE D CA    1 
ATOM   4225 C C     . ILE D 1 60  ? -9.235  7.823   -37.811 1.00 34.58 ? 83  ILE D C     1 
ATOM   4226 O O     . ILE D 1 60  ? -9.552  7.160   -36.813 1.00 31.20 ? 83  ILE D O     1 
ATOM   4227 C CB    . ILE D 1 60  ? -8.026  9.763   -36.750 1.00 31.41 ? 83  ILE D CB    1 
ATOM   4228 C CG1   . ILE D 1 60  ? -7.919  11.290  -36.677 1.00 27.42 ? 83  ILE D CG1   1 
ATOM   4229 C CG2   . ILE D 1 60  ? -6.693  9.133   -37.156 1.00 33.38 ? 83  ILE D CG2   1 
ATOM   4230 C CD1   . ILE D 1 60  ? -6.954  11.789  -35.603 1.00 29.51 ? 83  ILE D CD1   1 
ATOM   4231 N N     . GLU D 1 61  ? -8.928  7.266   -38.983 1.00 33.28 ? 84  GLU D N     1 
ATOM   4232 C CA    . GLU D 1 61  ? -9.108  5.843   -39.271 1.00 29.74 ? 84  GLU D CA    1 
ATOM   4233 C C     . GLU D 1 61  ? -7.832  5.285   -39.892 1.00 36.79 ? 84  GLU D C     1 
ATOM   4234 O O     . GLU D 1 61  ? -7.388  5.768   -40.939 1.00 34.71 ? 84  GLU D O     1 
ATOM   4235 C CB    . GLU D 1 61  ? -10.299 5.633   -40.213 1.00 29.39 ? 84  GLU D CB    1 
ATOM   4236 C CG    . GLU D 1 61  ? -10.490 4.202   -40.694 1.00 34.87 ? 84  GLU D CG    1 
ATOM   4237 C CD    . GLU D 1 61  ? -10.535 3.191   -39.564 1.00 37.74 ? 84  GLU D CD    1 
ATOM   4238 O OE1   . GLU D 1 61  ? -9.647  2.313   -39.512 1.00 36.73 ? 84  GLU D OE1   1 
ATOM   4239 O OE2   . GLU D 1 61  ? -11.461 3.265   -38.736 1.00 35.99 ? 84  GLU D OE2   1 
ATOM   4240 N N     . TYR D 1 62  ? -7.260  4.255   -39.261 1.00 37.47 ? 85  TYR D N     1 
ATOM   4241 C CA    . TYR D 1 62  ? -5.994  3.688   -39.728 1.00 40.58 ? 85  TYR D CA    1 
ATOM   4242 C C     . TYR D 1 62  ? -6.180  2.759   -40.924 1.00 38.17 ? 85  TYR D C     1 
ATOM   4243 O O     . TYR D 1 62  ? -5.308  2.692   -41.793 1.00 40.37 ? 85  TYR D O     1 
ATOM   4244 C CB    . TYR D 1 62  ? -5.291  2.936   -38.591 1.00 38.08 ? 85  TYR D CB    1 
ATOM   4245 C CG    . TYR D 1 62  ? -3.950  2.334   -38.974 1.00 39.64 ? 85  TYR D CG    1 
ATOM   4246 C CD1   . TYR D 1 62  ? -2.769  3.056   -38.808 1.00 43.91 ? 85  TYR D CD1   1 
ATOM   4247 C CD2   . TYR D 1 62  ? -3.862  1.043   -39.502 1.00 44.26 ? 85  TYR D CD2   1 
ATOM   4248 C CE1   . TYR D 1 62  ? -1.541  2.517   -39.156 1.00 44.64 ? 85  TYR D CE1   1 
ATOM   4249 C CE2   . TYR D 1 62  ? -2.637  0.494   -39.858 1.00 44.13 ? 85  TYR D CE2   1 
ATOM   4250 C CZ    . TYR D 1 62  ? -1.480  1.237   -39.679 1.00 49.43 ? 85  TYR D CZ    1 
ATOM   4251 O OH    . TYR D 1 62  ? -0.257  0.707   -40.022 1.00 53.81 ? 85  TYR D OH    1 
ATOM   4252 N N     . SER D 1 63  ? -7.284  2.025   -40.985 1.00 39.59 ? 86  SER D N     1 
ATOM   4253 C CA    . SER D 1 63  ? -7.496  1.100   -42.093 1.00 38.98 ? 86  SER D CA    1 
ATOM   4254 C C     . SER D 1 63  ? -7.846  1.867   -43.363 1.00 37.45 ? 86  SER D C     1 
ATOM   4255 O O     . SER D 1 63  ? -8.856  2.578   -43.415 1.00 37.23 ? 86  SER D O     1 
ATOM   4256 C CB    . SER D 1 63  ? -8.600  0.103   -41.754 1.00 39.88 ? 86  SER D CB    1 
ATOM   4257 O OG    . SER D 1 63  ? -9.239  -0.360  -42.934 1.00 39.87 ? 86  SER D OG    1 
ATOM   4258 N N     . THR D 1 64  ? -7.020  1.708   -44.400 1.00 42.55 ? 87  THR D N     1 
ATOM   4259 C CA    . THR D 1 64  ? -7.306  2.365   -45.672 1.00 38.77 ? 87  THR D CA    1 
ATOM   4260 C C     . THR D 1 64  ? -8.625  1.870   -46.265 1.00 36.48 ? 87  THR D C     1 
ATOM   4261 O O     . THR D 1 64  ? -9.394  2.660   -46.826 1.00 37.89 ? 87  THR D O     1 
ATOM   4262 C CB    . THR D 1 64  ? -6.131  2.158   -46.635 1.00 43.75 ? 87  THR D CB    1 
ATOM   4263 O OG1   . THR D 1 64  ? -4.989  2.881   -46.146 1.00 42.21 ? 87  THR D OG1   1 
ATOM   4264 C CG2   . THR D 1 64  ? -6.468  2.658   -48.033 1.00 38.16 ? 87  THR D CG2   1 
ATOM   4265 N N     . ASP D 1 65  ? -8.930  0.574   -46.104 1.00 38.57 ? 88  ASP D N     1 
ATOM   4266 C CA    . ASP D 1 65  ? -10.194 0.022   -46.602 1.00 38.75 ? 88  ASP D CA    1 
ATOM   4267 C C     . ASP D 1 65  ? -11.399 0.671   -45.930 1.00 38.97 ? 88  ASP D C     1 
ATOM   4268 O O     . ASP D 1 65  ? -12.385 1.015   -46.592 1.00 38.61 ? 88  ASP D O     1 
ATOM   4269 C CB    . ASP D 1 65  ? -10.242 -1.487  -46.375 1.00 42.36 ? 88  ASP D CB    1 
ATOM   4270 C CG    . ASP D 1 65  ? -9.254  -2.237  -47.227 1.00 56.00 ? 88  ASP D CG    1 
ATOM   4271 O OD1   . ASP D 1 65  ? -8.034  -2.005  -47.071 1.00 61.94 ? 88  ASP D OD1   1 
ATOM   4272 O OD2   . ASP D 1 65  ? -9.698  -3.078  -48.036 1.00 62.15 ? 88  ASP D OD2   1 
ATOM   4273 N N     . PHE D 1 66  ? -11.366 0.797   -44.601 1.00 37.27 ? 89  PHE D N     1 
ATOM   4274 C CA    . PHE D 1 66  ? -12.473 1.455   -43.915 1.00 36.05 ? 89  PHE D CA    1 
ATOM   4275 C C     . PHE D 1 66  ? -12.566 2.918   -44.329 1.00 32.53 ? 89  PHE D C     1 
ATOM   4276 O O     . PHE D 1 66  ? -13.662 3.438   -44.568 1.00 32.57 ? 89  PHE D O     1 
ATOM   4277 C CB    . PHE D 1 66  ? -12.297 1.342   -42.401 1.00 36.94 ? 89  PHE D CB    1 
ATOM   4278 C CG    . PHE D 1 66  ? -12.785 0.046   -41.819 1.00 41.97 ? 89  PHE D CG    1 
ATOM   4279 C CD1   . PHE D 1 66  ? -14.023 -0.473  -42.170 1.00 45.62 ? 89  PHE D CD1   1 
ATOM   4280 C CD2   . PHE D 1 66  ? -12.011 -0.642  -40.892 1.00 42.51 ? 89  PHE D CD2   1 
ATOM   4281 C CE1   . PHE D 1 66  ? -14.476 -1.674  -41.612 1.00 50.42 ? 89  PHE D CE1   1 
ATOM   4282 C CE2   . PHE D 1 66  ? -12.453 -1.836  -40.332 1.00 44.75 ? 89  PHE D CE2   1 
ATOM   4283 C CZ    . PHE D 1 66  ? -13.688 -2.353  -40.694 1.00 45.00 ? 89  PHE D CZ    1 
ATOM   4284 N N     . TYR D 1 67  ? -11.419 3.594   -44.427 1.00 33.28 ? 90  TYR D N     1 
ATOM   4285 C CA    . TYR D 1 67  ? -11.409 5.011   -44.787 1.00 34.71 ? 90  TYR D CA    1 
ATOM   4286 C C     . TYR D 1 67  ? -12.064 5.240   -46.147 1.00 36.06 ? 90  TYR D C     1 
ATOM   4287 O O     . TYR D 1 67  ? -12.958 6.085   -46.284 1.00 34.71 ? 90  TYR D O     1 
ATOM   4288 C CB    . TYR D 1 67  ? -9.967  5.528   -44.756 1.00 33.59 ? 90  TYR D CB    1 
ATOM   4289 C CG    . TYR D 1 67  ? -9.740  6.868   -45.413 1.00 38.61 ? 90  TYR D CG    1 
ATOM   4290 C CD1   . TYR D 1 67  ? -9.928  8.046   -44.711 1.00 33.57 ? 90  TYR D CD1   1 
ATOM   4291 C CD2   . TYR D 1 67  ? -9.303  6.950   -46.738 1.00 37.73 ? 90  TYR D CD2   1 
ATOM   4292 C CE1   . TYR D 1 67  ? -9.713  9.280   -45.313 1.00 36.69 ? 90  TYR D CE1   1 
ATOM   4293 C CE2   . TYR D 1 67  ? -9.087  8.170   -47.342 1.00 35.96 ? 90  TYR D CE2   1 
ATOM   4294 C CZ    . TYR D 1 67  ? -9.293  9.331   -46.632 1.00 35.05 ? 90  TYR D CZ    1 
ATOM   4295 O OH    . TYR D 1 67  ? -9.063  10.544  -47.237 1.00 36.37 ? 90  TYR D OH    1 
ATOM   4296 N N     . ASN D 1 68  ? -11.648 4.470   -47.164 1.00 36.31 ? 91  ASN D N     1 
ATOM   4297 C CA    . ASN D 1 68  ? -12.268 4.565   -48.486 1.00 36.77 ? 91  ASN D CA    1 
ATOM   4298 C C     . ASN D 1 68  ? -13.782 4.380   -48.412 1.00 39.60 ? 91  ASN D C     1 
ATOM   4299 O O     . ASN D 1 68  ? -14.538 5.102   -49.071 1.00 39.15 ? 91  ASN D O     1 
ATOM   4300 C CB    . ASN D 1 68  ? -11.653 3.529   -49.429 1.00 34.39 ? 91  ASN D CB    1 
ATOM   4301 C CG    . ASN D 1 68  ? -10.235 3.885   -49.845 1.00 38.39 ? 91  ASN D CG    1 
ATOM   4302 O OD1   . ASN D 1 68  ? -9.823  5.045   -49.775 1.00 38.35 ? 91  ASN D OD1   1 
ATOM   4303 N ND2   . ASN D 1 68  ? -9.480  2.886   -50.280 1.00 33.78 ? 91  ASN D ND2   1 
ATOM   4304 N N     . GLN D 1 69  ? -14.245 3.426   -47.597 1.00 38.37 ? 92  GLN D N     1 
ATOM   4305 C CA    . GLN D 1 69  ? -15.681 3.168   -47.509 1.00 38.57 ? 92  GLN D CA    1 
ATOM   4306 C C     . GLN D 1 69  ? -16.413 4.293   -46.780 1.00 39.48 ? 92  GLN D C     1 
ATOM   4307 O O     . GLN D 1 69  ? -17.517 4.683   -47.177 1.00 40.06 ? 92  GLN D O     1 
ATOM   4308 C CB    . GLN D 1 69  ? -15.925 1.830   -46.812 1.00 46.95 ? 92  GLN D CB    1 
ATOM   4309 C CG    . GLN D 1 69  ? -17.392 1.431   -46.743 1.00 50.35 ? 92  GLN D CG    1 
ATOM   4310 C CD    . GLN D 1 69  ? -18.049 1.402   -48.114 1.00 54.75 ? 92  GLN D CD    1 
ATOM   4311 O OE1   . GLN D 1 69  ? -17.574 0.719   -49.030 1.00 59.83 ? 92  GLN D OE1   1 
ATOM   4312 N NE2   . GLN D 1 69  ? -19.139 2.151   -48.265 1.00 46.35 ? 92  GLN D NE2   1 
ATOM   4313 N N     . LEU D 1 70  ? -15.819 4.818   -45.707 1.00 37.00 ? 93  LEU D N     1 
ATOM   4314 C CA    . LEU D 1 70  ? -16.475 5.868   -44.931 1.00 35.37 ? 93  LEU D CA    1 
ATOM   4315 C C     . LEU D 1 70  ? -16.713 7.122   -45.766 1.00 37.19 ? 93  LEU D C     1 
ATOM   4316 O O     . LEU D 1 70  ? -17.721 7.816   -45.577 1.00 33.74 ? 93  LEU D O     1 
ATOM   4317 C CB    . LEU D 1 70  ? -15.636 6.205   -43.696 1.00 34.08 ? 93  LEU D CB    1 
ATOM   4318 C CG    . LEU D 1 70  ? -15.583 5.116   -42.615 1.00 32.68 ? 93  LEU D CG    1 
ATOM   4319 C CD1   . LEU D 1 70  ? -14.316 5.276   -41.786 1.00 34.68 ? 93  LEU D CD1   1 
ATOM   4320 C CD2   . LEU D 1 70  ? -16.823 5.156   -41.737 1.00 29.65 ? 93  LEU D CD2   1 
ATOM   4321 N N     . LEU D 1 71  ? -15.784 7.441   -46.683 1.00 37.39 ? 94  LEU D N     1 
ATOM   4322 C CA    . LEU D 1 71  ? -15.947 8.621   -47.536 1.00 36.69 ? 94  LEU D CA    1 
ATOM   4323 C C     . LEU D 1 71  ? -17.203 8.523   -48.385 1.00 37.27 ? 94  LEU D C     1 
ATOM   4324 O O     . LEU D 1 71  ? -17.801 9.548   -48.727 1.00 39.67 ? 94  LEU D O     1 
ATOM   4325 C CB    . LEU D 1 71  ? -14.728 8.805   -48.448 1.00 34.06 ? 94  LEU D CB    1 
ATOM   4326 C CG    . LEU D 1 71  ? -13.408 9.291   -47.852 1.00 37.24 ? 94  LEU D CG    1 
ATOM   4327 C CD1   . LEU D 1 71  ? -12.305 9.183   -48.898 1.00 39.11 ? 94  LEU D CD1   1 
ATOM   4328 C CD2   . LEU D 1 71  ? -13.523 10.727  -47.345 1.00 32.55 ? 94  LEU D CD2   1 
ATOM   4329 N N     . ARG D 1 72  ? -17.609 7.306   -48.751 1.00 40.36 ? 95  ARG D N     1 
ATOM   4330 C CA    . ARG D 1 72  ? -18.842 7.141   -49.514 1.00 42.58 ? 95  ARG D CA    1 
ATOM   4331 C C     . ARG D 1 72  ? -20.055 7.110   -48.598 1.00 43.65 ? 95  ARG D C     1 
ATOM   4332 O O     . ARG D 1 72  ? -21.116 7.632   -48.954 1.00 45.31 ? 95  ARG D O     1 
ATOM   4333 C CB    . ARG D 1 72  ? -18.780 5.864   -50.366 1.00 47.21 ? 95  ARG D CB    1 
ATOM   4334 C CG    . ARG D 1 72  ? -18.059 6.054   -51.714 1.00 55.43 ? 95  ARG D CG    1 
ATOM   4335 C CD    . ARG D 1 72  ? -18.256 4.880   -52.689 1.00 57.36 ? 95  ARG D CD    1 
ATOM   4336 N NE    . ARG D 1 72  ? -18.183 3.569   -52.044 1.00 62.65 ? 95  ARG D NE    1 
ATOM   4337 C CZ    . ARG D 1 72  ? -17.054 2.891   -51.850 1.00 63.75 ? 95  ARG D CZ    1 
ATOM   4338 N NH1   . ARG D 1 72  ? -15.894 3.405   -52.247 1.00 61.71 ? 95  ARG D NH1   1 
ATOM   4339 N NH2   . ARG D 1 72  ? -17.083 1.702   -51.253 1.00 63.68 ? 95  ARG D NH2   1 
ATOM   4340 N N     . SER D 1 73  ? -19.914 6.513   -47.412 1.00 40.56 ? 96  SER D N     1 
ATOM   4341 C CA    . SER D 1 73  ? -21.056 6.369   -46.517 1.00 41.71 ? 96  SER D CA    1 
ATOM   4342 C C     . SER D 1 73  ? -21.440 7.685   -45.852 1.00 39.43 ? 96  SER D C     1 
ATOM   4343 O O     . SER D 1 73  ? -22.623 7.901   -45.568 1.00 39.42 ? 96  SER D O     1 
ATOM   4344 C CB    . SER D 1 73  ? -20.757 5.322   -45.449 1.00 40.33 ? 96  SER D CB    1 
ATOM   4345 O OG    . SER D 1 73  ? -20.527 4.062   -46.041 1.00 50.60 ? 96  SER D OG    1 
ATOM   4346 N N     . TYR D 1 74  ? -20.475 8.567   -45.580 1.00 39.66 ? 97  TYR D N     1 
ATOM   4347 C CA    . TYR D 1 74  ? -20.731 9.805   -44.836 1.00 40.36 ? 97  TYR D CA    1 
ATOM   4348 C C     . TYR D 1 74  ? -20.014 10.978  -45.495 1.00 42.53 ? 97  TYR D C     1 
ATOM   4349 O O     . TYR D 1 74  ? -18.980 11.458  -45.008 1.00 38.66 ? 97  TYR D O     1 
ATOM   4350 C CB    . TYR D 1 74  ? -20.321 9.652   -43.366 1.00 37.61 ? 97  TYR D CB    1 
ATOM   4351 C CG    . TYR D 1 74  ? -21.104 8.562   -42.651 1.00 41.68 ? 97  TYR D CG    1 
ATOM   4352 C CD1   . TYR D 1 74  ? -22.367 8.820   -42.120 1.00 38.16 ? 97  TYR D CD1   1 
ATOM   4353 C CD2   . TYR D 1 74  ? -20.592 7.269   -42.530 1.00 38.34 ? 97  TYR D CD2   1 
ATOM   4354 C CE1   . TYR D 1 74  ? -23.095 7.826   -41.484 1.00 39.50 ? 97  TYR D CE1   1 
ATOM   4355 C CE2   . TYR D 1 74  ? -21.317 6.266   -41.895 1.00 39.20 ? 97  TYR D CE2   1 
ATOM   4356 C CZ    . TYR D 1 74  ? -22.567 6.552   -41.374 1.00 40.07 ? 97  TYR D CZ    1 
ATOM   4357 O OH    . TYR D 1 74  ? -23.297 5.567   -40.741 1.00 37.18 ? 97  TYR D OH    1 
ATOM   4358 N N     . PRO D 1 75  ? -20.554 11.483  -46.606 1.00 44.29 ? 98  PRO D N     1 
ATOM   4359 C CA    . PRO D 1 75  ? -19.898 12.597  -47.306 1.00 42.61 ? 98  PRO D CA    1 
ATOM   4360 C C     . PRO D 1 75  ? -19.934 13.876  -46.480 1.00 42.57 ? 98  PRO D C     1 
ATOM   4361 O O     . PRO D 1 75  ? -20.913 14.168  -45.787 1.00 44.93 ? 98  PRO D O     1 
ATOM   4362 C CB    . PRO D 1 75  ? -20.719 12.746  -48.596 1.00 40.84 ? 98  PRO D CB    1 
ATOM   4363 C CG    . PRO D 1 75  ? -21.540 11.494  -48.701 1.00 48.79 ? 98  PRO D CG    1 
ATOM   4364 C CD    . PRO D 1 75  ? -21.772 11.030  -47.296 1.00 43.89 ? 98  PRO D CD    1 
ATOM   4365 N N     . GLY D 1 76  ? -18.853 14.648  -46.573 1.00 41.50 ? 99  GLY D N     1 
ATOM   4366 C CA    . GLY D 1 76  ? -18.702 15.881  -45.838 1.00 44.02 ? 99  GLY D CA    1 
ATOM   4367 C C     . GLY D 1 76  ? -17.944 15.727  -44.534 1.00 41.97 ? 99  GLY D C     1 
ATOM   4368 O O     . GLY D 1 76  ? -17.297 16.683  -44.084 1.00 41.58 ? 99  GLY D O     1 
ATOM   4369 N N     . VAL D 1 77  ? -18.007 14.543  -43.920 1.00 37.53 ? 100 VAL D N     1 
ATOM   4370 C CA    . VAL D 1 77  ? -17.241 14.290  -42.708 1.00 35.21 ? 100 VAL D CA    1 
ATOM   4371 C C     . VAL D 1 77  ? -15.756 14.348  -43.026 1.00 36.44 ? 100 VAL D C     1 
ATOM   4372 O O     . VAL D 1 77  ? -15.302 13.857  -44.064 1.00 37.33 ? 100 VAL D O     1 
ATOM   4373 C CB    . VAL D 1 77  ? -17.623 12.929  -42.103 1.00 33.85 ? 100 VAL D CB    1 
ATOM   4374 C CG1   . VAL D 1 77  ? -16.681 12.570  -40.944 1.00 27.29 ? 100 VAL D CG1   1 
ATOM   4375 C CG2   . VAL D 1 77  ? -19.066 12.942  -41.662 1.00 30.98 ? 100 VAL D CG2   1 
ATOM   4376 N N     . ASN D 1 78  ? -14.987 14.942  -42.118 1.00 34.28 ? 101 ASN D N     1 
ATOM   4377 C CA    . ASN D 1 78  ? -13.553 15.131  -42.318 1.00 32.47 ? 101 ASN D CA    1 
ATOM   4378 C C     . ASN D 1 78  ? -12.787 13.889  -41.847 1.00 34.04 ? 101 ASN D C     1 
ATOM   4379 O O     . ASN D 1 78  ? -12.102 13.878  -40.821 1.00 33.16 ? 101 ASN D O     1 
ATOM   4380 C CB    . ASN D 1 78  ? -13.102 16.398  -41.600 1.00 37.85 ? 101 ASN D CB    1 
ATOM   4381 C CG    . ASN D 1 78  ? -11.629 16.651  -41.740 1.00 40.52 ? 101 ASN D CG    1 
ATOM   4382 O OD1   . ASN D 1 78  ? -11.019 16.287  -42.747 1.00 42.43 ? 101 ASN D OD1   1 
ATOM   4383 N ND2   . ASN D 1 78  ? -11.035 17.265  -40.719 1.00 40.59 ? 101 ASN D ND2   1 
ATOM   4384 N N     . PHE D 1 79  ? -12.903 12.821  -42.637 1.00 32.43 ? 102 PHE D N     1 
ATOM   4385 C CA    . PHE D 1 79  ? -12.141 11.619  -42.340 1.00 28.45 ? 102 PHE D CA    1 
ATOM   4386 C C     . PHE D 1 79  ? -10.660 11.836  -42.628 1.00 35.69 ? 102 PHE D C     1 
ATOM   4387 O O     . PHE D 1 79  ? -10.280 12.584  -43.532 1.00 32.55 ? 102 PHE D O     1 
ATOM   4388 C CB    . PHE D 1 79  ? -12.668 10.434  -43.145 1.00 31.33 ? 102 PHE D CB    1 
ATOM   4389 C CG    . PHE D 1 79  ? -14.056 10.019  -42.765 1.00 33.29 ? 102 PHE D CG    1 
ATOM   4390 C CD1   . PHE D 1 79  ? -14.289 9.361   -41.565 1.00 26.99 ? 102 PHE D CD1   1 
ATOM   4391 C CD2   . PHE D 1 79  ? -15.133 10.305  -43.596 1.00 31.83 ? 102 PHE D CD2   1 
ATOM   4392 C CE1   . PHE D 1 79  ? -15.569 8.975   -41.206 1.00 28.30 ? 102 PHE D CE1   1 
ATOM   4393 C CE2   . PHE D 1 79  ? -16.417 9.920   -43.249 1.00 33.11 ? 102 PHE D CE2   1 
ATOM   4394 C CZ    . PHE D 1 79  ? -16.640 9.254   -42.050 1.00 32.82 ? 102 PHE D CZ    1 
ATOM   4395 N N     . VAL D 1 80  ? -9.818  11.179  -41.833 1.00 32.07 ? 103 VAL D N     1 
ATOM   4396 C CA    . VAL D 1 80  ? -8.370  11.202  -42.006 1.00 30.67 ? 103 VAL D CA    1 
ATOM   4397 C C     . VAL D 1 80  ? -7.872  9.768   -41.948 1.00 34.85 ? 103 VAL D C     1 
ATOM   4398 O O     . VAL D 1 80  ? -8.230  9.022   -41.029 1.00 32.08 ? 103 VAL D O     1 
ATOM   4399 C CB    . VAL D 1 80  ? -7.672  12.051  -40.924 1.00 34.35 ? 103 VAL D CB    1 
ATOM   4400 C CG1   . VAL D 1 80  ? -6.147  12.016  -41.109 1.00 34.61 ? 103 VAL D CG1   1 
ATOM   4401 C CG2   . VAL D 1 80  ? -8.199  13.476  -40.934 1.00 30.85 ? 103 VAL D CG2   1 
ATOM   4402 N N     . ASN D 1 81  ? -7.046  9.378   -42.921 1.00 33.90 ? 104 ASN D N     1 
ATOM   4403 C CA    . ASN D 1 81  ? -6.448  8.047   -42.945 1.00 33.74 ? 104 ASN D CA    1 
ATOM   4404 C C     . ASN D 1 81  ? -5.068  8.145   -42.304 1.00 38.80 ? 104 ASN D C     1 
ATOM   4405 O O     . ASN D 1 81  ? -4.136  8.685   -42.906 1.00 39.14 ? 104 ASN D O     1 
ATOM   4406 C CB    . ASN D 1 81  ? -6.372  7.502   -44.371 1.00 37.58 ? 104 ASN D CB    1 
ATOM   4407 C CG    . ASN D 1 81  ? -5.762  6.102   -44.440 1.00 39.39 ? 104 ASN D CG    1 
ATOM   4408 O OD1   . ASN D 1 81  ? -5.925  5.281   -43.531 1.00 37.93 ? 104 ASN D OD1   1 
ATOM   4409 N ND2   . ASN D 1 81  ? -5.055  5.826   -45.528 1.00 38.62 ? 104 ASN D ND2   1 
ATOM   4410 N N     . GLY D 1 82  ? -4.939  7.631   -41.087 1.00 37.64 ? 105 GLY D N     1 
ATOM   4411 C CA    . GLY D 1 82  ? -3.676  7.735   -40.383 1.00 33.67 ? 105 GLY D CA    1 
ATOM   4412 C C     . GLY D 1 82  ? -3.736  7.059   -39.028 1.00 38.89 ? 105 GLY D C     1 
ATOM   4413 O O     . GLY D 1 82  ? -4.731  6.429   -38.661 1.00 32.28 ? 105 GLY D O     1 
ATOM   4414 N N     . ASP D 1 83  ? -2.651  7.232   -38.282 1.00 37.14 ? 106 ASP D N     1 
ATOM   4415 C CA    . ASP D 1 83  ? -2.441  6.595   -36.989 1.00 39.11 ? 106 ASP D CA    1 
ATOM   4416 C C     . ASP D 1 83  ? -2.800  7.583   -35.885 1.00 38.42 ? 106 ASP D C     1 
ATOM   4417 O O     . ASP D 1 83  ? -2.159  8.632   -35.751 1.00 39.32 ? 106 ASP D O     1 
ATOM   4418 C CB    . ASP D 1 83  ? -0.985  6.141   -36.868 1.00 41.05 ? 106 ASP D CB    1 
ATOM   4419 C CG    . ASP D 1 83  ? -0.694  5.396   -35.575 1.00 45.00 ? 106 ASP D CG    1 
ATOM   4420 O OD1   . ASP D 1 83  ? -1.608  5.213   -34.741 1.00 43.24 ? 106 ASP D OD1   1 
ATOM   4421 O OD2   . ASP D 1 83  ? 0.472   4.992   -35.393 1.00 48.91 ? 106 ASP D OD2   1 
ATOM   4422 N N     . ALA D 1 84  ? -3.822  7.246   -35.093 1.00 38.51 ? 107 ALA D N     1 
ATOM   4423 C CA    . ALA D 1 84  ? -4.258  8.158   -34.041 1.00 37.18 ? 107 ALA D CA    1 
ATOM   4424 C C     . ALA D 1 84  ? -3.162  8.401   -33.011 1.00 38.26 ? 107 ALA D C     1 
ATOM   4425 O O     . ALA D 1 84  ? -3.139  9.456   -32.367 1.00 39.28 ? 107 ALA D O     1 
ATOM   4426 C CB    . ALA D 1 84  ? -5.513  7.611   -33.363 1.00 39.38 ? 107 ALA D CB    1 
ATOM   4427 N N     . PHE D 1 85  ? -2.241  7.446   -32.845 1.00 37.64 ? 108 PHE D N     1 
ATOM   4428 C CA    . PHE D 1 85  ? -1.184  7.599   -31.851 1.00 41.60 ? 108 PHE D CA    1 
ATOM   4429 C C     . PHE D 1 85  ? -0.147  8.639   -32.269 1.00 45.16 ? 108 PHE D C     1 
ATOM   4430 O O     . PHE D 1 85  ? 0.612   9.115   -31.418 1.00 45.13 ? 108 PHE D O     1 
ATOM   4431 C CB    . PHE D 1 85  ? -0.530  6.235   -31.568 1.00 40.13 ? 108 PHE D CB    1 
ATOM   4432 C CG    . PHE D 1 85  ? -1.344  5.355   -30.638 1.00 39.60 ? 108 PHE D CG    1 
ATOM   4433 C CD1   . PHE D 1 85  ? -2.402  4.595   -31.124 1.00 36.94 ? 108 PHE D CD1   1 
ATOM   4434 C CD2   . PHE D 1 85  ? -1.079  5.328   -29.271 1.00 36.96 ? 108 PHE D CD2   1 
ATOM   4435 C CE1   . PHE D 1 85  ? -3.172  3.810   -30.267 1.00 39.68 ? 108 PHE D CE1   1 
ATOM   4436 C CE2   . PHE D 1 85  ? -1.838  4.544   -28.406 1.00 34.67 ? 108 PHE D CE2   1 
ATOM   4437 C CZ    . PHE D 1 85  ? -2.888  3.782   -28.906 1.00 38.92 ? 108 PHE D CZ    1 
ATOM   4438 N N     . ASP D 1 86  ? -0.123  9.023   -33.543 1.00 42.97 ? 109 ASP D N     1 
ATOM   4439 C CA    . ASP D 1 86  ? 0.753   10.076  -34.047 1.00 47.27 ? 109 ASP D CA    1 
ATOM   4440 C C     . ASP D 1 86  ? -0.094  11.302  -34.387 1.00 45.43 ? 109 ASP D C     1 
ATOM   4441 O O     . ASP D 1 86  ? -0.332  11.629  -35.555 1.00 44.20 ? 109 ASP D O     1 
ATOM   4442 C CB    . ASP D 1 86  ? 1.540   9.561   -35.262 1.00 47.99 ? 109 ASP D CB    1 
ATOM   4443 C CG    . ASP D 1 86  ? 2.620   10.528  -35.724 1.00 53.07 ? 109 ASP D CG    1 
ATOM   4444 O OD1   . ASP D 1 86  ? 2.796   11.597  -35.101 1.00 54.65 ? 109 ASP D OD1   1 
ATOM   4445 O OD2   . ASP D 1 86  ? 3.294   10.217  -36.728 1.00 56.30 ? 109 ASP D OD2   1 
ATOM   4446 N N     . LEU D 1 87  ? -0.546  11.990  -33.336 1.00 41.22 ? 110 LEU D N     1 
ATOM   4447 C CA    . LEU D 1 87  ? -1.506  13.077  -33.509 1.00 45.55 ? 110 LEU D CA    1 
ATOM   4448 C C     . LEU D 1 87  ? -0.938  14.199  -34.366 1.00 50.06 ? 110 LEU D C     1 
ATOM   4449 O O     . LEU D 1 87  ? -1.672  14.841  -35.127 1.00 50.64 ? 110 LEU D O     1 
ATOM   4450 C CB    . LEU D 1 87  ? -1.930  13.629  -32.150 1.00 43.05 ? 110 LEU D CB    1 
ATOM   4451 C CG    . LEU D 1 87  ? -3.096  12.957  -31.429 1.00 46.27 ? 110 LEU D CG    1 
ATOM   4452 C CD1   . LEU D 1 87  ? -3.589  13.854  -30.291 1.00 39.16 ? 110 LEU D CD1   1 
ATOM   4453 C CD2   . LEU D 1 87  ? -4.222  12.627  -32.405 1.00 41.37 ? 110 LEU D CD2   1 
ATOM   4454 N N     . ASP D 1 88  ? 0.360   14.470  -34.241 1.00 50.99 ? 111 ASP D N     1 
ATOM   4455 C CA    . ASP D 1 88  ? 0.949   15.538  -35.040 1.00 54.90 ? 111 ASP D CA    1 
ATOM   4456 C C     . ASP D 1 88  ? 0.897   15.201  -36.526 1.00 51.25 ? 111 ASP D C     1 
ATOM   4457 O O     . ASP D 1 88  ? 0.578   16.063  -37.350 1.00 56.29 ? 111 ASP D O     1 
ATOM   4458 C CB    . ASP D 1 88  ? 2.382   15.804  -34.578 1.00 58.44 ? 111 ASP D CB    1 
ATOM   4459 C CG    . ASP D 1 88  ? 2.437   16.578  -33.262 1.00 63.02 ? 111 ASP D CG    1 
ATOM   4460 O OD1   . ASP D 1 88  ? 1.373   17.056  -32.801 1.00 57.48 ? 111 ASP D OD1   1 
ATOM   4461 O OD2   . ASP D 1 88  ? 3.546   16.703  -32.690 1.00 67.25 ? 111 ASP D OD2   1 
ATOM   4462 N N     . ALA D 1 89  ? 1.171   13.947  -36.886 1.00 49.39 ? 112 ALA D N     1 
ATOM   4463 C CA    . ALA D 1 89  ? 1.090   13.550  -38.288 1.00 53.10 ? 112 ALA D CA    1 
ATOM   4464 C C     . ALA D 1 89  ? -0.334  13.614  -38.826 1.00 53.59 ? 112 ALA D C     1 
ATOM   4465 O O     . ALA D 1 89  ? -0.533  13.890  -40.014 1.00 53.54 ? 112 ALA D O     1 
ATOM   4466 C CB    . ALA D 1 89  ? 1.640   12.137  -38.476 1.00 53.10 ? 112 ALA D CB    1 
ATOM   4467 N N     . THR D 1 90  ? -1.332  13.344  -37.988 1.00 51.16 ? 113 THR D N     1 
ATOM   4468 C CA    . THR D 1 90  ? -2.702  13.219  -38.473 1.00 48.70 ? 113 THR D CA    1 
ATOM   4469 C C     . THR D 1 90  ? -3.521  14.491  -38.307 1.00 46.55 ? 113 THR D C     1 
ATOM   4470 O O     . THR D 1 90  ? -4.405  14.755  -39.127 1.00 45.76 ? 113 THR D O     1 
ATOM   4471 C CB    . THR D 1 90  ? -3.412  12.063  -37.753 1.00 46.20 ? 113 THR D CB    1 
ATOM   4472 O OG1   . THR D 1 90  ? -3.338  12.263  -36.334 1.00 48.18 ? 113 THR D OG1   1 
ATOM   4473 C CG2   . THR D 1 90  ? -2.751  10.736  -38.096 1.00 39.96 ? 113 THR D CG2   1 
ATOM   4474 N N     . LEU D 1 91  ? -3.258  15.280  -37.263 1.00 45.03 ? 114 LEU D N     1 
ATOM   4475 C CA    . LEU D 1 91  ? -3.974  16.525  -37.028 1.00 48.96 ? 114 LEU D CA    1 
ATOM   4476 C C     . LEU D 1 91  ? -3.138  17.765  -37.293 1.00 51.29 ? 114 LEU D C     1 
ATOM   4477 O O     . LEU D 1 91  ? -3.702  18.855  -37.417 1.00 54.59 ? 114 LEU D O     1 
ATOM   4478 C CB    . LEU D 1 91  ? -4.477  16.590  -35.577 1.00 46.19 ? 114 LEU D CB    1 
ATOM   4479 C CG    . LEU D 1 91  ? -5.583  15.620  -35.156 1.00 46.68 ? 114 LEU D CG    1 
ATOM   4480 C CD1   . LEU D 1 91  ? -5.853  15.740  -33.661 1.00 39.88 ? 114 LEU D CD1   1 
ATOM   4481 C CD2   . LEU D 1 91  ? -6.851  15.863  -35.952 1.00 39.85 ? 114 LEU D CD2   1 
ATOM   4482 N N     . GLY D 1 92  ? -1.823  17.626  -37.381 1.00 56.96 ? 115 GLY D N     1 
ATOM   4483 C CA    . GLY D 1 92  ? -0.929  18.762  -37.341 1.00 62.16 ? 115 GLY D CA    1 
ATOM   4484 C C     . GLY D 1 92  ? -0.422  19.030  -35.934 1.00 59.50 ? 115 GLY D C     1 
ATOM   4485 O O     . GLY D 1 92  ? -0.985  18.574  -34.937 1.00 59.69 ? 115 GLY D O     1 
ATOM   4486 N N     . GLU D 1 93  ? 0.688   19.765  -35.865 1.00 58.60 ? 116 GLU D N     1 
ATOM   4487 C CA    . GLU D 1 93  ? 1.186   20.223  -34.576 1.00 64.02 ? 116 GLU D CA    1 
ATOM   4488 C C     . GLU D 1 93  ? 0.106   21.041  -33.872 1.00 68.69 ? 116 GLU D C     1 
ATOM   4489 O O     . GLU D 1 93  ? -0.706  21.719  -34.515 1.00 67.55 ? 116 GLU D O     1 
ATOM   4490 C CB    . GLU D 1 93  ? 2.455   21.061  -34.754 1.00 60.21 ? 116 GLU D CB    1 
ATOM   4491 N N     . HIS D 1 94  ? 0.087   20.968  -32.537 1.00 65.92 ? 117 HIS D N     1 
ATOM   4492 C CA    . HIS D 1 94  ? -0.946  21.692  -31.808 1.00 64.13 ? 117 HIS D CA    1 
ATOM   4493 C C     . HIS D 1 94  ? -0.745  23.200  -31.924 1.00 66.93 ? 117 HIS D C     1 
ATOM   4494 O O     . HIS D 1 94  ? -0.339  23.866  -30.962 1.00 66.91 ? 117 HIS D O     1 
ATOM   4495 C CB    . HIS D 1 94  ? -1.013  21.270  -30.333 1.00 59.62 ? 117 HIS D CB    1 
ATOM   4496 C CG    . HIS D 1 94  ? -2.245  21.763  -29.628 1.00 62.34 ? 117 HIS D CG    1 
ATOM   4497 N ND1   . HIS D 1 94  ? -2.235  22.215  -28.323 1.00 62.02 ? 117 HIS D ND1   1 
ATOM   4498 C CD2   . HIS D 1 94  ? -3.526  21.890  -30.057 1.00 57.57 ? 117 HIS D CD2   1 
ATOM   4499 C CE1   . HIS D 1 94  ? -3.456  22.588  -27.976 1.00 54.13 ? 117 HIS D CE1   1 
ATOM   4500 N NE2   . HIS D 1 94  ? -4.257  22.405  -29.012 1.00 55.45 ? 117 HIS D NE2   1 
ATOM   4501 N N     . LYS D 1 95  ? -0.988  23.733  -33.121 1.00 69.55 ? 118 LYS D N     1 
ATOM   4502 C CA    . LYS D 1 95  ? -1.547  25.069  -33.216 1.00 70.18 ? 118 LYS D CA    1 
ATOM   4503 C C     . LYS D 1 95  ? -2.998  24.962  -32.744 1.00 69.82 ? 118 LYS D C     1 
ATOM   4504 O O     . LYS D 1 95  ? -3.732  24.053  -33.158 1.00 62.83 ? 118 LYS D O     1 
ATOM   4505 C CB    . LYS D 1 95  ? -1.447  25.607  -34.644 1.00 62.51 ? 118 LYS D CB    1 
ATOM   4506 N N     . GLY D 1 96  ? -3.395  25.867  -31.855 1.00 62.27 ? 119 GLY D N     1 
ATOM   4507 C CA    . GLY D 1 96  ? -4.427  25.567  -30.882 1.00 56.65 ? 119 GLY D CA    1 
ATOM   4508 C C     . GLY D 1 96  ? -5.884  25.367  -31.264 1.00 47.22 ? 119 GLY D C     1 
ATOM   4509 O O     . GLY D 1 96  ? -6.753  25.973  -30.634 1.00 49.18 ? 119 GLY D O     1 
ATOM   4510 N N     . GLN D 1 97  ? -6.194  24.492  -32.222 1.00 49.88 ? 120 GLN D N     1 
ATOM   4511 C CA    . GLN D 1 97  ? -7.586  24.140  -32.485 1.00 47.13 ? 120 GLN D CA    1 
ATOM   4512 C C     . GLN D 1 97  ? -8.075  23.189  -31.398 1.00 39.76 ? 120 GLN D C     1 
ATOM   4513 O O     . GLN D 1 97  ? -7.486  22.124  -31.178 1.00 41.96 ? 120 GLN D O     1 
ATOM   4514 C CB    . GLN D 1 97  ? -7.758  23.496  -33.860 1.00 46.45 ? 120 GLN D CB    1 
ATOM   4515 C CG    . GLN D 1 97  ? -9.179  22.918  -34.093 1.00 44.14 ? 120 GLN D CG    1 
ATOM   4516 C CD    . GLN D 1 97  ? -10.237 24.009  -34.304 1.00 47.88 ? 120 GLN D CD    1 
ATOM   4517 O OE1   . GLN D 1 97  ? -10.109 24.851  -35.198 1.00 48.72 ? 120 GLN D OE1   1 
ATOM   4518 N NE2   . GLN D 1 97  ? -11.280 24.002  -33.474 1.00 44.20 ? 120 GLN D NE2   1 
ATOM   4519 N N     . MET D 1 98  ? -9.150  23.566  -30.727 1.00 37.66 ? 121 MET D N     1 
ATOM   4520 C CA    . MET D 1 98  ? -9.727  22.741  -29.681 1.00 35.33 ? 121 MET D CA    1 
ATOM   4521 C C     . MET D 1 98  ? -10.899 21.937  -30.230 1.00 32.46 ? 121 MET D C     1 
ATOM   4522 O O     . MET D 1 98  ? -11.583 22.359  -31.167 1.00 29.60 ? 121 MET D O     1 
ATOM   4523 C CB    . MET D 1 98  ? -10.191 23.607  -28.506 1.00 34.21 ? 121 MET D CB    1 
ATOM   4524 C CG    . MET D 1 98  ? -9.115  24.507  -27.930 1.00 37.38 ? 121 MET D CG    1 
ATOM   4525 S SD    . MET D 1 98  ? -7.707  23.625  -27.227 1.00 37.48 ? 121 MET D SD    1 
ATOM   4526 C CE    . MET D 1 98  ? -8.454  22.951  -25.762 1.00 30.39 ? 121 MET D CE    1 
ATOM   4527 N N     . PHE D 1 99  ? -11.131 20.777  -29.625 1.00 28.30 ? 122 PHE D N     1 
ATOM   4528 C CA    . PHE D 1 99  ? -12.267 19.930  -29.933 1.00 29.34 ? 122 PHE D CA    1 
ATOM   4529 C C     . PHE D 1 99  ? -13.211 19.896  -28.740 1.00 28.55 ? 122 PHE D C     1 
ATOM   4530 O O     . PHE D 1 99  ? -12.794 20.063  -27.592 1.00 28.41 ? 122 PHE D O     1 
ATOM   4531 C CB    . PHE D 1 99  ? -11.819 18.507  -30.297 1.00 25.35 ? 122 PHE D CB    1 
ATOM   4532 C CG    . PHE D 1 99  ? -11.031 18.443  -31.568 1.00 28.45 ? 122 PHE D CG    1 
ATOM   4533 C CD1   . PHE D 1 99  ? -11.673 18.346  -32.792 1.00 27.04 ? 122 PHE D CD1   1 
ATOM   4534 C CD2   . PHE D 1 99  ? -9.644  18.496  -31.539 1.00 29.29 ? 122 PHE D CD2   1 
ATOM   4535 C CE1   . PHE D 1 99  ? -10.936 18.294  -33.969 1.00 29.63 ? 122 PHE D CE1   1 
ATOM   4536 C CE2   . PHE D 1 99  ? -8.910  18.448  -32.705 1.00 31.72 ? 122 PHE D CE2   1 
ATOM   4537 C CZ    . PHE D 1 99  ? -9.551  18.349  -33.915 1.00 26.07 ? 122 PHE D CZ    1 
ATOM   4538 N N     . ASP D 1 100 ? -14.490 19.678  -29.025 1.00 25.61 ? 123 ASP D N     1 
ATOM   4539 C CA    . ASP D 1 100 ? -15.495 19.685  -27.968 1.00 26.77 ? 123 ASP D CA    1 
ATOM   4540 C C     . ASP D 1 100 ? -15.312 18.507  -27.016 1.00 31.99 ? 123 ASP D C     1 
ATOM   4541 O O     . ASP D 1 100 ? -15.556 18.632  -25.807 1.00 28.38 ? 123 ASP D O     1 
ATOM   4542 C CB    . ASP D 1 100 ? -16.888 19.650  -28.594 1.00 30.30 ? 123 ASP D CB    1 
ATOM   4543 C CG    . ASP D 1 100 ? -17.991 19.522  -27.561 1.00 37.06 ? 123 ASP D CG    1 
ATOM   4544 O OD1   . ASP D 1 100 ? -18.380 18.376  -27.223 1.00 32.36 ? 123 ASP D OD1   1 
ATOM   4545 O OD2   . ASP D 1 100 ? -18.486 20.574  -27.104 1.00 34.65 ? 123 ASP D OD2   1 
ATOM   4546 N N     . SER D 1 101 ? -14.887 17.362  -27.557 1.00 25.05 ? 124 SER D N     1 
ATOM   4547 C CA    . SER D 1 101 ? -14.762 16.079  -26.881 1.00 25.89 ? 124 SER D CA    1 
ATOM   4548 C C     . SER D 1 101 ? -14.123 15.114  -27.873 1.00 28.75 ? 124 SER D C     1 
ATOM   4549 O O     . SER D 1 101 ? -14.099 15.372  -29.081 1.00 25.05 ? 124 SER D O     1 
ATOM   4550 C CB    . SER D 1 101 ? -16.124 15.548  -26.401 1.00 31.26 ? 124 SER D CB    1 
ATOM   4551 O OG    . SER D 1 101 ? -17.126 15.680  -27.402 1.00 27.37 ? 124 SER D OG    1 
ATOM   4552 N N     . VAL D 1 102 ? -13.601 14.005  -27.357 1.00 24.61 ? 125 VAL D N     1 
ATOM   4553 C CA    . VAL D 1 102 ? -13.021 12.942  -28.180 1.00 22.64 ? 125 VAL D CA    1 
ATOM   4554 C C     . VAL D 1 102 ? -13.812 11.662  -27.928 1.00 25.00 ? 125 VAL D C     1 
ATOM   4555 O O     . VAL D 1 102 ? -14.040 11.288  -26.772 1.00 23.07 ? 125 VAL D O     1 
ATOM   4556 C CB    . VAL D 1 102 ? -11.530 12.729  -27.862 1.00 24.13 ? 125 VAL D CB    1 
ATOM   4557 C CG1   . VAL D 1 102 ? -10.918 11.690  -28.805 1.00 23.92 ? 125 VAL D CG1   1 
ATOM   4558 C CG2   . VAL D 1 102 ? -10.756 14.045  -27.923 1.00 19.94 ? 125 VAL D CG2   1 
ATOM   4559 N N     . ILE D 1 103 ? -14.228 10.993  -29.002 1.00 25.66 ? 126 ILE D N     1 
ATOM   4560 C CA    . ILE D 1 103 ? -14.969 9.736   -28.931 1.00 23.90 ? 126 ILE D CA    1 
ATOM   4561 C C     . ILE D 1 103 ? -14.068 8.658   -29.523 1.00 26.49 ? 126 ILE D C     1 
ATOM   4562 O O     . ILE D 1 103 ? -13.805 8.664   -30.730 1.00 24.43 ? 126 ILE D O     1 
ATOM   4563 C CB    . ILE D 1 103 ? -16.303 9.809   -29.694 1.00 27.14 ? 126 ILE D CB    1 
ATOM   4564 C CG1   . ILE D 1 103 ? -17.055 11.119  -29.432 1.00 25.19 ? 126 ILE D CG1   1 
ATOM   4565 C CG2   . ILE D 1 103 ? -17.173 8.626   -29.374 1.00 22.02 ? 126 ILE D CG2   1 
ATOM   4566 C CD1   . ILE D 1 103 ? -17.340 11.398  -27.972 1.00 27.03 ? 126 ILE D CD1   1 
ATOM   4567 N N     . SER D 1 104 ? -13.590 7.721   -28.703 1.00 23.67 ? 127 SER D N     1 
ATOM   4568 C CA    . SER D 1 104 ? -12.544 6.801   -29.137 1.00 26.56 ? 127 SER D CA    1 
ATOM   4569 C C     . SER D 1 104 ? -13.005 5.350   -29.061 1.00 30.14 ? 127 SER D C     1 
ATOM   4570 O O     . SER D 1 104 ? -13.477 4.891   -28.014 1.00 24.84 ? 127 SER D O     1 
ATOM   4571 C CB    . SER D 1 104 ? -11.269 6.980   -28.303 1.00 22.76 ? 127 SER D CB    1 
ATOM   4572 O OG    . SER D 1 104 ? -10.297 6.009   -28.665 1.00 26.95 ? 127 SER D OG    1 
ATOM   4573 N N     . ALA D 1 105 ? -12.860 4.626   -30.176 1.00 27.67 ? 128 ALA D N     1 
ATOM   4574 C CA    . ALA D 1 105 ? -12.949 3.169   -30.186 1.00 31.45 ? 128 ALA D CA    1 
ATOM   4575 C C     . ALA D 1 105 ? -11.642 2.533   -30.660 1.00 31.40 ? 128 ALA D C     1 
ATOM   4576 O O     . ALA D 1 105 ? -11.645 1.399   -31.147 1.00 34.85 ? 128 ALA D O     1 
ATOM   4577 C CB    . ALA D 1 105 ? -14.119 2.691   -31.051 1.00 32.82 ? 128 ALA D CB    1 
ATOM   4578 N N     . VAL D 1 106 ? -10.529 3.250   -30.539 1.00 28.67 ? 129 VAL D N     1 
ATOM   4579 C CA    . VAL D 1 106 ? -9.230  2.656   -30.876 1.00 35.71 ? 129 VAL D CA    1 
ATOM   4580 C C     . VAL D 1 106 ? -8.971  1.464   -29.960 1.00 36.71 ? 129 VAL D C     1 
ATOM   4581 O O     . VAL D 1 106 ? -9.246  1.544   -28.747 1.00 32.23 ? 129 VAL D O     1 
ATOM   4582 C CB    . VAL D 1 106 ? -8.114  3.707   -30.754 1.00 31.91 ? 129 VAL D CB    1 
ATOM   4583 C CG1   . VAL D 1 106 ? -6.737  3.053   -30.627 1.00 42.41 ? 129 VAL D CG1   1 
ATOM   4584 C CG2   . VAL D 1 106 ? -8.158  4.618   -31.945 1.00 38.20 ? 129 VAL D CG2   1 
ATOM   4585 N N     . PRO D 1 107 ? -8.481  0.327   -30.473 1.00 42.24 ? 130 PRO D N     1 
ATOM   4586 C CA    . PRO D 1 107 ? -8.239  -0.831  -29.597 1.00 38.74 ? 130 PRO D CA    1 
ATOM   4587 C C     . PRO D 1 107 ? -6.952  -0.670  -28.799 1.00 38.86 ? 130 PRO D C     1 
ATOM   4588 O O     . PRO D 1 107 ? -5.872  -1.048  -29.257 1.00 43.16 ? 130 PRO D O     1 
ATOM   4589 C CB    . PRO D 1 107 ? -8.167  -2.000  -30.584 1.00 41.65 ? 130 PRO D CB    1 
ATOM   4590 C CG    . PRO D 1 107 ? -7.630  -1.374  -31.851 1.00 41.48 ? 130 PRO D CG    1 
ATOM   4591 C CD    . PRO D 1 107 ? -8.158  0.044   -31.886 1.00 41.43 ? 130 PRO D CD    1 
ATOM   4592 N N     . MET D 1 108 ? -7.066  -0.104  -27.595 1.00 41.16 ? 131 MET D N     1 
ATOM   4593 C CA    . MET D 1 108 ? -5.889  0.340   -26.851 1.00 41.99 ? 131 MET D CA    1 
ATOM   4594 C C     . MET D 1 108 ? -4.981  -0.815  -26.449 1.00 44.91 ? 131 MET D C     1 
ATOM   4595 O O     . MET D 1 108 ? -3.761  -0.628  -26.336 1.00 40.41 ? 131 MET D O     1 
ATOM   4596 C CB    . MET D 1 108 ? -6.322  1.103   -25.599 1.00 41.05 ? 131 MET D CB    1 
ATOM   4597 C CG    . MET D 1 108 ? -7.041  2.393   -25.878 1.00 36.79 ? 131 MET D CG    1 
ATOM   4598 S SD    . MET D 1 108 ? -5.840  3.697   -26.084 1.00 42.98 ? 131 MET D SD    1 
ATOM   4599 C CE    . MET D 1 108 ? -6.859  5.064   -26.649 1.00 36.62 ? 131 MET D CE    1 
ATOM   4600 N N     . LEU D 1 109 ? -5.557  -2.001  -26.212 1.00 43.57 ? 132 LEU D N     1 
ATOM   4601 C CA    . LEU D 1 109 ? -4.806  -3.148  -25.716 1.00 46.05 ? 132 LEU D CA    1 
ATOM   4602 C C     . LEU D 1 109 ? -3.770  -3.659  -26.704 1.00 46.45 ? 132 LEU D C     1 
ATOM   4603 O O     . LEU D 1 109 ? -2.958  -4.512  -26.330 1.00 50.32 ? 132 LEU D O     1 
ATOM   4604 C CB    . LEU D 1 109 ? -5.762  -4.288  -25.357 1.00 45.52 ? 132 LEU D CB    1 
ATOM   4605 C CG    . LEU D 1 109 ? -6.791  -4.012  -24.264 1.00 49.47 ? 132 LEU D CG    1 
ATOM   4606 C CD1   . LEU D 1 109 ? -7.484  -5.307  -23.845 1.00 49.01 ? 132 LEU D CD1   1 
ATOM   4607 C CD2   . LEU D 1 109 ? -6.129  -3.338  -23.071 1.00 46.96 ? 132 LEU D CD2   1 
ATOM   4608 N N     . ASN D 1 110 ? -3.781  -3.179  -27.944 1.00 45.22 ? 133 ASN D N     1 
ATOM   4609 C CA    . ASN D 1 110 ? -2.777  -3.571  -28.927 1.00 46.13 ? 133 ASN D CA    1 
ATOM   4610 C C     . ASN D 1 110 ? -1.474  -2.796  -28.784 1.00 46.72 ? 133 ASN D C     1 
ATOM   4611 O O     . ASN D 1 110 ? -0.513  -3.097  -29.503 1.00 46.25 ? 133 ASN D O     1 
ATOM   4612 C CB    . ASN D 1 110 ? -3.331  -3.381  -30.341 1.00 46.01 ? 133 ASN D CB    1 
ATOM   4613 C CG    . ASN D 1 110 ? -4.584  -4.212  -30.599 1.00 49.09 ? 133 ASN D CG    1 
ATOM   4614 O OD1   . ASN D 1 110 ? -4.903  -5.133  -29.844 1.00 50.04 ? 133 ASN D OD1   1 
ATOM   4615 N ND2   . ASN D 1 110 ? -5.288  -3.897  -31.683 1.00 44.88 ? 133 ASN D ND2   1 
ATOM   4616 N N     . PHE D 1 111 ? -1.418  -1.821  -27.880 1.00 39.43 ? 134 PHE D N     1 
ATOM   4617 C CA    . PHE D 1 111 ? -0.305  -0.895  -27.768 1.00 40.24 ? 134 PHE D CA    1 
ATOM   4618 C C     . PHE D 1 111 ? 0.252   -0.898  -26.354 1.00 39.74 ? 134 PHE D C     1 
ATOM   4619 O O     . PHE D 1 111 ? -0.468  -1.204  -25.400 1.00 40.89 ? 134 PHE D O     1 
ATOM   4620 C CB    . PHE D 1 111 ? -0.752  0.529   -28.138 1.00 44.59 ? 134 PHE D CB    1 
ATOM   4621 C CG    . PHE D 1 111 ? -1.331  0.636   -29.515 1.00 43.66 ? 134 PHE D CG    1 
ATOM   4622 C CD1   . PHE D 1 111 ? -2.669  0.346   -29.745 1.00 42.95 ? 134 PHE D CD1   1 
ATOM   4623 C CD2   . PHE D 1 111 ? -0.533  1.018   -30.585 1.00 40.00 ? 134 PHE D CD2   1 
ATOM   4624 C CE1   . PHE D 1 111 ? -3.203  0.438   -31.022 1.00 47.42 ? 134 PHE D CE1   1 
ATOM   4625 C CE2   . PHE D 1 111 ? -1.053  1.115   -31.856 1.00 42.52 ? 134 PHE D CE2   1 
ATOM   4626 C CZ    . PHE D 1 111 ? -2.386  0.821   -32.082 1.00 45.30 ? 134 PHE D CZ    1 
ATOM   4627 N N     . PRO D 1 112 ? 1.532   -0.560  -26.191 1.00 41.04 ? 135 PRO D N     1 
ATOM   4628 C CA    . PRO D 1 112 ? 2.114   -0.510  -24.844 1.00 34.93 ? 135 PRO D CA    1 
ATOM   4629 C C     . PRO D 1 112 ? 1.454   0.562   -23.985 1.00 39.24 ? 135 PRO D C     1 
ATOM   4630 O O     . PRO D 1 112 ? 1.021   1.605   -24.480 1.00 36.42 ? 135 PRO D O     1 
ATOM   4631 C CB    . PRO D 1 112 ? 3.589   -0.180  -25.105 1.00 39.20 ? 135 PRO D CB    1 
ATOM   4632 C CG    . PRO D 1 112 ? 3.833   -0.619  -26.534 1.00 38.59 ? 135 PRO D CG    1 
ATOM   4633 C CD    . PRO D 1 112 ? 2.540   -0.373  -27.252 1.00 40.62 ? 135 PRO D CD    1 
ATOM   4634 N N     . MET D 1 113 ? 1.406   0.304   -22.672 1.00 35.20 ? 136 MET D N     1 
ATOM   4635 C CA    . MET D 1 113 ? 0.731   1.231   -21.765 1.00 35.87 ? 136 MET D CA    1 
ATOM   4636 C C     . MET D 1 113 ? 1.346   2.621   -21.825 1.00 36.46 ? 136 MET D C     1 
ATOM   4637 O O     . MET D 1 113 ? 0.628   3.623   -21.763 1.00 36.99 ? 136 MET D O     1 
ATOM   4638 C CB    . MET D 1 113 ? 0.766   0.707   -20.334 1.00 34.77 ? 136 MET D CB    1 
ATOM   4639 C CG    . MET D 1 113 ? -0.030  1.566   -19.358 1.00 37.83 ? 136 MET D CG    1 
ATOM   4640 S SD    . MET D 1 113 ? -1.828  1.504   -19.658 1.00 35.40 ? 136 MET D SD    1 
ATOM   4641 C CE    . MET D 1 113 ? -2.215  -0.108  -18.982 1.00 33.97 ? 136 MET D CE    1 
ATOM   4642 N N     . ALA D 1 114 ? 2.675   2.707   -21.939 1.00 39.76 ? 137 ALA D N     1 
ATOM   4643 C CA    . ALA D 1 114 ? 3.306   4.020   -22.037 1.00 40.01 ? 137 ALA D CA    1 
ATOM   4644 C C     . ALA D 1 114 ? 2.742   4.810   -23.214 1.00 36.52 ? 137 ALA D C     1 
ATOM   4645 O O     . ALA D 1 114 ? 2.408   5.992   -23.075 1.00 38.83 ? 137 ALA D O     1 
ATOM   4646 C CB    . ALA D 1 114 ? 4.822   3.868   -22.155 1.00 41.95 ? 137 ALA D CB    1 
ATOM   4647 N N     . ALA D 1 115 ? 2.584   4.160   -24.368 1.00 32.85 ? 138 ALA D N     1 
ATOM   4648 C CA    . ALA D 1 115 ? 1.996   4.825   -25.525 1.00 35.11 ? 138 ALA D CA    1 
ATOM   4649 C C     . ALA D 1 115 ? 0.562   5.271   -25.250 1.00 36.55 ? 138 ALA D C     1 
ATOM   4650 O O     . ALA D 1 115 ? 0.149   6.351   -25.690 1.00 34.01 ? 138 ALA D O     1 
ATOM   4651 C CB    . ALA D 1 115 ? 2.040   3.896   -26.737 1.00 33.33 ? 138 ALA D CB    1 
ATOM   4652 N N     . ARG D 1 116 ? -0.219  4.450   -24.536 1.00 31.55 ? 139 ARG D N     1 
ATOM   4653 C CA    . ARG D 1 116 ? -1.605  4.819   -24.249 1.00 33.62 ? 139 ARG D CA    1 
ATOM   4654 C C     . ARG D 1 116 ? -1.677  6.050   -23.363 1.00 32.49 ? 139 ARG D C     1 
ATOM   4655 O O     . ARG D 1 116 ? -2.517  6.927   -23.586 1.00 32.07 ? 139 ARG D O     1 
ATOM   4656 C CB    . ARG D 1 116 ? -2.346  3.668   -23.573 1.00 30.87 ? 139 ARG D CB    1 
ATOM   4657 C CG    . ARG D 1 116 ? -2.273  2.346   -24.289 1.00 34.65 ? 139 ARG D CG    1 
ATOM   4658 C CD    . ARG D 1 116 ? -2.890  1.286   -23.414 1.00 34.61 ? 139 ARG D CD    1 
ATOM   4659 N NE    . ARG D 1 116 ? -2.345  -0.035  -23.686 1.00 37.41 ? 139 ARG D NE    1 
ATOM   4660 C CZ    . ARG D 1 116 ? -2.645  -1.120  -22.983 1.00 39.58 ? 139 ARG D CZ    1 
ATOM   4661 N NH1   . ARG D 1 116 ? -3.494  -1.040  -21.961 1.00 37.74 ? 139 ARG D NH1   1 
ATOM   4662 N NH2   . ARG D 1 116 ? -2.096  -2.284  -23.300 1.00 41.89 ? 139 ARG D NH2   1 
ATOM   4663 N N     . ILE D 1 117 ? -0.828  6.113   -22.332 1.00 33.86 ? 140 ILE D N     1 
ATOM   4664 C CA    . ILE D 1 117 ? -0.816  7.272   -21.443 1.00 33.99 ? 140 ILE D CA    1 
ATOM   4665 C C     . ILE D 1 117 ? -0.404  8.524   -22.207 1.00 36.56 ? 140 ILE D C     1 
ATOM   4666 O O     . ILE D 1 117 ? -0.966  9.608   -22.003 1.00 36.67 ? 140 ILE D O     1 
ATOM   4667 C CB    . ILE D 1 117 ? 0.108   7.014   -20.237 1.00 33.88 ? 140 ILE D CB    1 
ATOM   4668 C CG1   . ILE D 1 117 ? -0.390  5.810   -19.431 1.00 35.59 ? 140 ILE D CG1   1 
ATOM   4669 C CG2   . ILE D 1 117 ? 0.224   8.276   -19.360 1.00 32.29 ? 140 ILE D CG2   1 
ATOM   4670 C CD1   . ILE D 1 117 ? 0.610   5.312   -18.401 1.00 34.92 ? 140 ILE D CD1   1 
ATOM   4671 N N     . LYS D 1 118 ? 0.576   8.397   -23.103 1.00 34.83 ? 141 LYS D N     1 
ATOM   4672 C CA    . LYS D 1 118 ? 1.018   9.558   -23.870 1.00 38.24 ? 141 LYS D CA    1 
ATOM   4673 C C     . LYS D 1 118 ? -0.091  10.065  -24.790 1.00 36.48 ? 141 LYS D C     1 
ATOM   4674 O O     . LYS D 1 118 ? -0.375  11.269  -24.831 1.00 37.70 ? 141 LYS D O     1 
ATOM   4675 C CB    . LYS D 1 118 ? 2.275   9.210   -24.668 1.00 38.63 ? 141 LYS D CB    1 
ATOM   4676 C CG    . LYS D 1 118 ? 2.957   10.419  -25.317 1.00 45.25 ? 141 LYS D CG    1 
ATOM   4677 C CD    . LYS D 1 118 ? 4.155   9.988   -26.170 1.00 50.71 ? 141 LYS D CD    1 
ATOM   4678 C CE    . LYS D 1 118 ? 4.789   11.184  -26.878 1.00 59.70 ? 141 LYS D CE    1 
ATOM   4679 N NZ    . LYS D 1 118 ? 5.897   10.769  -27.782 1.00 63.55 ? 141 LYS D NZ    1 
ATOM   4680 N N     . LEU D 1 119 ? -0.736  9.159   -25.527 1.00 32.74 ? 142 LEU D N     1 
ATOM   4681 C CA    . LEU D 1 119 ? -1.834  9.567   -26.398 1.00 33.96 ? 142 LEU D CA    1 
ATOM   4682 C C     . LEU D 1 119 ? -2.929  10.277  -25.610 1.00 30.14 ? 142 LEU D C     1 
ATOM   4683 O O     . LEU D 1 119 ? -3.429  11.325  -26.033 1.00 27.35 ? 142 LEU D O     1 
ATOM   4684 C CB    . LEU D 1 119 ? -2.399  8.350   -27.130 1.00 34.87 ? 142 LEU D CB    1 
ATOM   4685 C CG    . LEU D 1 119 ? -3.673  8.626   -27.923 1.00 36.09 ? 142 LEU D CG    1 
ATOM   4686 C CD1   . LEU D 1 119 ? -3.405  9.693   -28.999 1.00 35.47 ? 142 LEU D CD1   1 
ATOM   4687 C CD2   . LEU D 1 119 ? -4.210  7.342   -28.525 1.00 30.92 ? 142 LEU D CD2   1 
ATOM   4688 N N     . LEU D 1 120 ? -3.302  9.731   -24.449 1.00 31.75 ? 143 LEU D N     1 
ATOM   4689 C CA    . LEU D 1 120 ? -4.360  10.337  -23.643 1.00 31.44 ? 143 LEU D CA    1 
ATOM   4690 C C     . LEU D 1 120 ? -3.976  11.735  -23.164 1.00 35.75 ? 143 LEU D C     1 
ATOM   4691 O O     . LEU D 1 120 ? -4.806  12.656  -23.172 1.00 29.46 ? 143 LEU D O     1 
ATOM   4692 C CB    . LEU D 1 120 ? -4.682  9.439   -22.446 1.00 32.76 ? 143 LEU D CB    1 
ATOM   4693 C CG    . LEU D 1 120 ? -5.850  9.927   -21.596 1.00 38.29 ? 143 LEU D CG    1 
ATOM   4694 C CD1   . LEU D 1 120 ? -7.115  10.073  -22.447 1.00 33.88 ? 143 LEU D CD1   1 
ATOM   4695 C CD2   . LEU D 1 120 ? -6.078  8.969   -20.431 1.00 37.37 ? 143 LEU D CD2   1 
ATOM   4696 N N     . ASP D 1 121 ? -2.730  11.909  -22.719 1.00 32.23 ? 144 ASP D N     1 
ATOM   4697 C CA    . ASP D 1 121 ? -2.300  13.227  -22.269 1.00 38.48 ? 144 ASP D CA    1 
ATOM   4698 C C     . ASP D 1 121 ? -2.303  14.220  -23.427 1.00 35.10 ? 144 ASP D C     1 
ATOM   4699 O O     . ASP D 1 121 ? -2.710  15.374  -23.263 1.00 38.08 ? 144 ASP D O     1 
ATOM   4700 C CB    . ASP D 1 121 ? -0.918  13.137  -21.621 1.00 38.94 ? 144 ASP D CB    1 
ATOM   4701 C CG    . ASP D 1 121 ? -0.511  14.432  -20.930 1.00 42.28 ? 144 ASP D CG    1 
ATOM   4702 O OD1   . ASP D 1 121 ? -1.351  15.017  -20.207 1.00 48.29 ? 144 ASP D OD1   1 
ATOM   4703 O OD2   . ASP D 1 121 ? 0.648   14.861  -21.108 1.00 46.46 ? 144 ASP D OD2   1 
ATOM   4704 N N     . GLU D 1 122 ? -1.902  13.770  -24.613 1.00 34.15 ? 145 GLU D N     1 
ATOM   4705 C CA    . GLU D 1 122 ? -1.943  14.634  -25.785 1.00 33.40 ? 145 GLU D CA    1 
ATOM   4706 C C     . GLU D 1 122 ? -3.381  14.976  -26.188 1.00 37.00 ? 145 GLU D C     1 
ATOM   4707 O O     . GLU D 1 122 ? -3.686  16.141  -26.475 1.00 37.45 ? 145 GLU D O     1 
ATOM   4708 C CB    . GLU D 1 122 ? -1.179  13.972  -26.933 1.00 35.37 ? 145 GLU D CB    1 
ATOM   4709 C CG    . GLU D 1 122 ? 0.350   14.129  -26.819 1.00 42.41 ? 145 GLU D CG    1 
ATOM   4710 C CD    . GLU D 1 122 ? 0.810   15.597  -26.630 1.00 53.20 ? 145 GLU D CD    1 
ATOM   4711 O OE1   . GLU D 1 122 ? 0.347   16.488  -27.383 1.00 53.18 ? 145 GLU D OE1   1 
ATOM   4712 O OE2   . GLU D 1 122 ? 1.628   15.864  -25.714 1.00 50.88 ? 145 GLU D OE2   1 
ATOM   4713 N N     . LEU D 1 123 ? -4.279  13.983  -26.215 1.00 30.23 ? 146 LEU D N     1 
ATOM   4714 C CA    . LEU D 1 123 ? -5.690  14.260  -26.497 1.00 28.35 ? 146 LEU D CA    1 
ATOM   4715 C C     . LEU D 1 123 ? -6.264  15.294  -25.532 1.00 28.97 ? 146 LEU D C     1 
ATOM   4716 O O     . LEU D 1 123 ? -6.983  16.213  -25.946 1.00 26.57 ? 146 LEU D O     1 
ATOM   4717 C CB    . LEU D 1 123 ? -6.507  12.964  -26.423 1.00 29.87 ? 146 LEU D CB    1 
ATOM   4718 C CG    . LEU D 1 123 ? -6.268  11.968  -27.560 1.00 32.81 ? 146 LEU D CG    1 
ATOM   4719 C CD1   . LEU D 1 123 ? -6.960  10.619  -27.298 1.00 27.62 ? 146 LEU D CD1   1 
ATOM   4720 C CD2   . LEU D 1 123 ? -6.711  12.562  -28.898 1.00 28.51 ? 146 LEU D CD2   1 
ATOM   4721 N N     . LEU D 1 124 ? -5.958  15.166  -24.238 1.00 27.04 ? 147 LEU D N     1 
ATOM   4722 C CA    . LEU D 1 124 ? -6.537  16.085  -23.265 1.00 27.22 ? 147 LEU D CA    1 
ATOM   4723 C C     . LEU D 1 124 ? -6.010  17.508  -23.418 1.00 28.72 ? 147 LEU D C     1 
ATOM   4724 O O     . LEU D 1 124 ? -6.645  18.444  -22.927 1.00 31.34 ? 147 LEU D O     1 
ATOM   4725 C CB    . LEU D 1 124 ? -6.291  15.571  -21.844 1.00 26.69 ? 147 LEU D CB    1 
ATOM   4726 C CG    . LEU D 1 124 ? -7.194  14.380  -21.468 1.00 27.36 ? 147 LEU D CG    1 
ATOM   4727 C CD1   . LEU D 1 124 ? -6.776  13.741  -20.144 1.00 28.25 ? 147 LEU D CD1   1 
ATOM   4728 C CD2   . LEU D 1 124 ? -8.646  14.792  -21.423 1.00 24.11 ? 147 LEU D CD2   1 
ATOM   4729 N N     . LYS D 1 125 ? -4.868  17.698  -24.076 1.00 32.47 ? 148 LYS D N     1 
ATOM   4730 C CA    . LYS D 1 125 ? -4.447  19.060  -24.375 1.00 34.65 ? 148 LYS D CA    1 
ATOM   4731 C C     . LYS D 1 125 ? -5.294  19.705  -25.462 1.00 34.77 ? 148 LYS D C     1 
ATOM   4732 O O     . LYS D 1 125 ? -5.206  20.921  -25.651 1.00 35.49 ? 148 LYS D O     1 
ATOM   4733 C CB    . LYS D 1 125 ? -2.979  19.075  -24.789 1.00 33.77 ? 148 LYS D CB    1 
ATOM   4734 C CG    . LYS D 1 125 ? -2.038  18.764  -23.636 1.00 36.29 ? 148 LYS D CG    1 
ATOM   4735 C CD    . LYS D 1 125 ? -0.659  18.451  -24.137 1.00 41.64 ? 148 LYS D CD    1 
ATOM   4736 C CE    . LYS D 1 125 ? 0.242   18.030  -22.997 1.00 43.88 ? 148 LYS D CE    1 
ATOM   4737 N NZ    . LYS D 1 125 ? 1.612   17.768  -23.493 1.00 49.70 ? 148 LYS D NZ    1 
ATOM   4738 N N     . ARG D 1 126 ? -6.112  18.929  -26.173 1.00 29.78 ? 149 ARG D N     1 
ATOM   4739 C CA    . ARG D 1 126 ? -6.852  19.428  -27.321 1.00 30.56 ? 149 ARG D CA    1 
ATOM   4740 C C     . ARG D 1 126 ? -8.346  19.540  -27.061 1.00 28.66 ? 149 ARG D C     1 
ATOM   4741 O O     . ARG D 1 126 ? -9.108  19.783  -28.003 1.00 28.44 ? 149 ARG D O     1 
ATOM   4742 C CB    . ARG D 1 126 ? -6.588  18.538  -28.535 1.00 35.28 ? 149 ARG D CB    1 
ATOM   4743 C CG    . ARG D 1 126 ? -5.175  18.687  -29.093 1.00 36.60 ? 149 ARG D CG    1 
ATOM   4744 C CD    . ARG D 1 126 ? -4.889  17.550  -30.035 1.00 42.81 ? 149 ARG D CD    1 
ATOM   4745 N NE    . ARG D 1 126 ? -3.813  17.824  -30.976 1.00 49.06 ? 149 ARG D NE    1 
ATOM   4746 C CZ    . ARG D 1 126 ? -2.524  17.693  -30.693 1.00 52.81 ? 149 ARG D CZ    1 
ATOM   4747 N NH1   . ARG D 1 126 ? -2.146  17.309  -29.475 1.00 53.91 ? 149 ARG D NH1   1 
ATOM   4748 N NH2   . ARG D 1 126 ? -1.614  17.942  -31.629 1.00 55.44 ? 149 ARG D NH2   1 
ATOM   4749 N N     . VAL D 1 127 ? -8.784  19.376  -25.817 1.00 25.80 ? 150 VAL D N     1 
ATOM   4750 C CA    . VAL D 1 127 ? -10.171 19.666  -25.458 1.00 25.50 ? 150 VAL D CA    1 
ATOM   4751 C C     . VAL D 1 127 ? -10.152 20.610  -24.269 1.00 26.54 ? 150 VAL D C     1 
ATOM   4752 O O     . VAL D 1 127 ? -9.158  20.669  -23.522 1.00 27.80 ? 150 VAL D O     1 
ATOM   4753 C CB    . VAL D 1 127 ? -10.969 18.376  -25.145 1.00 30.77 ? 150 VAL D CB    1 
ATOM   4754 C CG1   . VAL D 1 127 ? -11.044 17.480  -26.378 1.00 26.87 ? 150 VAL D CG1   1 
ATOM   4755 C CG2   . VAL D 1 127 ? -10.381 17.641  -23.925 1.00 24.12 ? 150 VAL D CG2   1 
ATOM   4756 N N     . PRO D 1 128 ? -11.213 21.393  -24.078 1.00 23.55 ? 151 PRO D N     1 
ATOM   4757 C CA    . PRO D 1 128 ? -11.211 22.345  -22.964 1.00 28.17 ? 151 PRO D CA    1 
ATOM   4758 C C     . PRO D 1 128 ? -11.095 21.629  -21.629 1.00 31.50 ? 151 PRO D C     1 
ATOM   4759 O O     . PRO D 1 128 ? -11.527 20.485  -21.464 1.00 28.91 ? 151 PRO D O     1 
ATOM   4760 C CB    . PRO D 1 128 ? -12.556 23.065  -23.098 1.00 24.30 ? 151 PRO D CB    1 
ATOM   4761 C CG    . PRO D 1 128 ? -12.922 22.913  -24.553 1.00 27.84 ? 151 PRO D CG    1 
ATOM   4762 C CD    . PRO D 1 128 ? -12.418 21.542  -24.925 1.00 28.76 ? 151 PRO D CD    1 
ATOM   4763 N N     . HIS D 1 129 ? -10.478 22.318  -20.676 1.00 32.10 ? 152 HIS D N     1 
ATOM   4764 C CA    . HIS D 1 129 ? -10.300 21.769  -19.344 1.00 30.05 ? 152 HIS D CA    1 
ATOM   4765 C C     . HIS D 1 129 ? -11.647 21.328  -18.788 1.00 33.57 ? 152 HIS D C     1 
ATOM   4766 O O     . HIS D 1 129 ? -12.594 22.122  -18.740 1.00 25.69 ? 152 HIS D O     1 
ATOM   4767 C CB    . HIS D 1 129 ? -9.647  22.820  -18.440 1.00 36.07 ? 152 HIS D CB    1 
ATOM   4768 C CG    . HIS D 1 129 ? -9.119  22.256  -17.163 1.00 36.26 ? 152 HIS D CG    1 
ATOM   4769 N ND1   . HIS D 1 129 ? -9.919  22.047  -16.059 1.00 38.54 ? 152 HIS D ND1   1 
ATOM   4770 C CD2   . HIS D 1 129 ? -7.883  21.826  -16.822 1.00 40.14 ? 152 HIS D CD2   1 
ATOM   4771 C CE1   . HIS D 1 129 ? -9.193  21.526  -15.086 1.00 40.05 ? 152 HIS D CE1   1 
ATOM   4772 N NE2   . HIS D 1 129 ? -7.956  21.376  -15.525 1.00 44.82 ? 152 HIS D NE2   1 
ATOM   4773 N N     . GLY D 1 130 ? -11.751 20.039  -18.418 1.00 27.53 ? 153 GLY D N     1 
ATOM   4774 C CA    . GLY D 1 130 ? -13.002 19.490  -17.933 1.00 27.62 ? 153 GLY D CA    1 
ATOM   4775 C C     . GLY D 1 130 ? -13.853 18.778  -18.968 1.00 28.52 ? 153 GLY D C     1 
ATOM   4776 O O     . GLY D 1 130 ? -14.925 18.271  -18.620 1.00 27.75 ? 153 GLY D O     1 
ATOM   4777 N N     . ARG D 1 131 ? -13.421 18.723  -20.213 1.00 26.86 ? 154 ARG D N     1 
ATOM   4778 C CA    . ARG D 1 131 ? -14.170 17.964  -21.199 1.00 28.08 ? 154 ARG D CA    1 
ATOM   4779 C C     . ARG D 1 131 ? -13.552 16.585  -21.373 1.00 25.29 ? 154 ARG D C     1 
ATOM   4780 O O     . ARG D 1 131 ? -12.374 16.379  -21.060 1.00 22.93 ? 154 ARG D O     1 
ATOM   4781 C CB    . ARG D 1 131 ? -14.203 18.723  -22.530 1.00 27.54 ? 154 ARG D CB    1 
ATOM   4782 C CG    . ARG D 1 131 ? -14.983 20.040  -22.428 1.00 28.62 ? 154 ARG D CG    1 
ATOM   4783 C CD    . ARG D 1 131 ? -16.457 19.769  -22.134 1.00 31.08 ? 154 ARG D CD    1 
ATOM   4784 N NE    . ARG D 1 131 ? -17.116 19.135  -23.275 1.00 29.34 ? 154 ARG D NE    1 
ATOM   4785 C CZ    . ARG D 1 131 ? -18.160 18.318  -23.176 1.00 32.50 ? 154 ARG D CZ    1 
ATOM   4786 N NH1   . ARG D 1 131 ? -18.664 18.024  -21.977 1.00 27.37 ? 154 ARG D NH1   1 
ATOM   4787 N NH2   . ARG D 1 131 ? -18.700 17.793  -24.273 1.00 27.57 ? 154 ARG D NH2   1 
ATOM   4788 N N     . PRO D 1 132 ? -14.339 15.591  -21.848 1.00 22.76 ? 155 PRO D N     1 
ATOM   4789 C CA    . PRO D 1 132 ? -13.892 14.192  -21.766 1.00 22.12 ? 155 PRO D CA    1 
ATOM   4790 C C     . PRO D 1 132 ? -13.308 13.626  -23.053 1.00 26.85 ? 155 PRO D C     1 
ATOM   4791 O O     . PRO D 1 132 ? -13.630 14.093  -24.149 1.00 24.61 ? 155 PRO D O     1 
ATOM   4792 C CB    . PRO D 1 132 ? -15.186 13.460  -21.405 1.00 28.89 ? 155 PRO D CB    1 
ATOM   4793 C CG    . PRO D 1 132 ? -16.240 14.219  -22.191 1.00 27.06 ? 155 PRO D CG    1 
ATOM   4794 C CD    . PRO D 1 132 ? -15.761 15.674  -22.242 1.00 24.61 ? 155 PRO D CD    1 
ATOM   4795 N N     . VAL D 1 133 ? -12.436 12.631  -22.905 1.00 23.13 ? 156 VAL D N     1 
ATOM   4796 C CA    . VAL D 1 133 ? -12.215 11.573  -23.891 1.00 22.81 ? 156 VAL D CA    1 
ATOM   4797 C C     . VAL D 1 133 ? -13.070 10.374  -23.467 1.00 24.90 ? 156 VAL D C     1 
ATOM   4798 O O     . VAL D 1 133 ? -12.902 9.846   -22.361 1.00 24.20 ? 156 VAL D O     1 
ATOM   4799 C CB    . VAL D 1 133 ? -10.729 11.172  -23.964 1.00 24.92 ? 156 VAL D CB    1 
ATOM   4800 C CG1   . VAL D 1 133 ? -10.512 9.969   -24.905 1.00 18.52 ? 156 VAL D CG1   1 
ATOM   4801 C CG2   . VAL D 1 133 ? -9.843  12.351  -24.355 1.00 24.88 ? 156 VAL D CG2   1 
ATOM   4802 N N     . VAL D 1 134 ? -13.985 9.935   -24.318 1.00 22.18 ? 157 VAL D N     1 
ATOM   4803 C CA    . VAL D 1 134 ? -14.752 8.716   -24.060 1.00 22.25 ? 157 VAL D CA    1 
ATOM   4804 C C     . VAL D 1 134 ? -14.087 7.541   -24.762 1.00 25.81 ? 157 VAL D C     1 
ATOM   4805 O O     . VAL D 1 134 ? -13.679 7.647   -25.934 1.00 23.51 ? 157 VAL D O     1 
ATOM   4806 C CB    . VAL D 1 134 ? -16.208 8.878   -24.521 1.00 25.80 ? 157 VAL D CB    1 
ATOM   4807 C CG1   . VAL D 1 134 ? -17.079 7.723   -23.983 1.00 25.94 ? 157 VAL D CG1   1 
ATOM   4808 C CG2   . VAL D 1 134 ? -16.722 10.214  -24.058 1.00 31.74 ? 157 VAL D CG2   1 
ATOM   4809 N N     . GLN D 1 135 ? -13.983 6.411   -24.055 1.00 21.67 ? 158 GLN D N     1 
ATOM   4810 C CA    . GLN D 1 135 ? -13.282 5.238   -24.564 1.00 20.67 ? 158 GLN D CA    1 
ATOM   4811 C C     . GLN D 1 135 ? -14.088 3.977   -24.270 1.00 26.27 ? 158 GLN D C     1 
ATOM   4812 O O     . GLN D 1 135 ? -14.494 3.750   -23.126 1.00 21.79 ? 158 GLN D O     1 
ATOM   4813 C CB    . GLN D 1 135 ? -11.876 5.117   -23.944 1.00 21.74 ? 158 GLN D CB    1 
ATOM   4814 C CG    . GLN D 1 135 ? -11.127 3.802   -24.298 1.00 20.54 ? 158 GLN D CG    1 
ATOM   4815 C CD    . GLN D 1 135 ? -10.668 3.753   -25.756 1.00 27.21 ? 158 GLN D CD    1 
ATOM   4816 O OE1   . GLN D 1 135 ? -10.139 4.735   -26.291 1.00 24.29 ? 158 GLN D OE1   1 
ATOM   4817 N NE2   . GLN D 1 135 ? -10.849 2.602   -26.398 1.00 27.22 ? 158 GLN D NE2   1 
ATOM   4818 N N     . ILE D 1 136 ? -14.331 3.162   -25.304 1.00 25.09 ? 159 ILE D N     1 
ATOM   4819 C CA    . ILE D 1 136 ? -15.021 1.887   -25.131 1.00 21.74 ? 159 ILE D CA    1 
ATOM   4820 C C     . ILE D 1 136 ? -13.978 0.804   -24.911 1.00 25.86 ? 159 ILE D C     1 
ATOM   4821 O O     . ILE D 1 136 ? -12.924 0.798   -25.562 1.00 28.72 ? 159 ILE D O     1 
ATOM   4822 C CB    . ILE D 1 136 ? -15.920 1.560   -26.343 1.00 25.10 ? 159 ILE D CB    1 
ATOM   4823 C CG1   . ILE D 1 136 ? -16.569 0.183   -26.173 1.00 22.99 ? 159 ILE D CG1   1 
ATOM   4824 C CG2   . ILE D 1 136 ? -15.110 1.571   -27.660 1.00 27.45 ? 159 ILE D CG2   1 
ATOM   4825 C CD1   . ILE D 1 136 ? -17.728 -0.043  -27.104 1.00 27.14 ? 159 ILE D CD1   1 
ATOM   4826 N N     . SER D 1 137 ? -14.256 -0.114  -23.985 1.00 27.85 ? 160 SER D N     1 
ATOM   4827 C CA    . SER D 1 137 ? -13.414 -1.292  -23.814 1.00 25.56 ? 160 SER D CA    1 
ATOM   4828 C C     . SER D 1 137 ? -14.289 -2.437  -23.305 1.00 26.57 ? 160 SER D C     1 
ATOM   4829 O O     . SER D 1 137 ? -15.517 -2.326  -23.249 1.00 26.67 ? 160 SER D O     1 
ATOM   4830 C CB    . SER D 1 137 ? -12.222 -0.982  -22.898 1.00 27.15 ? 160 SER D CB    1 
ATOM   4831 O OG    . SER D 1 137 ? -12.575 -1.115  -21.535 1.00 39.53 ? 160 SER D OG    1 
ATOM   4832 N N     . TYR D 1 138 ? -13.654 -3.557  -22.975 1.00 27.73 ? 161 TYR D N     1 
ATOM   4833 C CA    . TYR D 1 138 ? -14.363 -4.792  -22.668 1.00 32.23 ? 161 TYR D CA    1 
ATOM   4834 C C     . TYR D 1 138 ? -13.737 -5.417  -21.434 1.00 33.45 ? 161 TYR D C     1 
ATOM   4835 O O     . TYR D 1 138 ? -12.513 -5.548  -21.360 1.00 34.36 ? 161 TYR D O     1 
ATOM   4836 C CB    . TYR D 1 138 ? -14.316 -5.746  -23.865 1.00 30.60 ? 161 TYR D CB    1 
ATOM   4837 C CG    . TYR D 1 138 ? -14.727 -5.035  -25.132 1.00 29.25 ? 161 TYR D CG    1 
ATOM   4838 C CD1   . TYR D 1 138 ? -16.069 -4.886  -25.456 1.00 26.22 ? 161 TYR D CD1   1 
ATOM   4839 C CD2   . TYR D 1 138 ? -13.776 -4.457  -25.977 1.00 27.16 ? 161 TYR D CD2   1 
ATOM   4840 C CE1   . TYR D 1 138 ? -16.461 -4.198  -26.599 1.00 29.88 ? 161 TYR D CE1   1 
ATOM   4841 C CE2   . TYR D 1 138 ? -14.157 -3.769  -27.124 1.00 27.43 ? 161 TYR D CE2   1 
ATOM   4842 C CZ    . TYR D 1 138 ? -15.500 -3.643  -27.433 1.00 31.02 ? 161 TYR D CZ    1 
ATOM   4843 O OH    . TYR D 1 138 ? -15.907 -2.964  -28.576 1.00 33.61 ? 161 TYR D OH    1 
ATOM   4844 N N     . GLY D 1 139 ? -14.568 -5.756  -20.452 1.00 33.94 ? 162 GLY D N     1 
ATOM   4845 C CA    . GLY D 1 139 ? -14.084 -6.345  -19.226 1.00 29.96 ? 162 GLY D CA    1 
ATOM   4846 C C     . GLY D 1 139 ? -13.819 -5.290  -18.179 1.00 34.26 ? 162 GLY D C     1 
ATOM   4847 O O     . GLY D 1 139 ? -13.874 -4.090  -18.450 1.00 34.28 ? 162 GLY D O     1 
ATOM   4848 N N     . PRO D 1 140 ? -13.511 -5.719  -16.955 1.00 37.87 ? 163 PRO D N     1 
ATOM   4849 C CA    . PRO D 1 140 ? -13.415 -4.779  -15.829 1.00 34.25 ? 163 PRO D CA    1 
ATOM   4850 C C     . PRO D 1 140 ? -12.112 -3.997  -15.735 1.00 35.39 ? 163 PRO D C     1 
ATOM   4851 O O     . PRO D 1 140 ? -11.933 -3.261  -14.761 1.00 37.41 ? 163 PRO D O     1 
ATOM   4852 C CB    . PRO D 1 140 ? -13.580 -5.706  -14.609 1.00 35.17 ? 163 PRO D CB    1 
ATOM   4853 C CG    . PRO D 1 140 ? -13.014 -7.034  -15.066 1.00 30.84 ? 163 PRO D CG    1 
ATOM   4854 C CD    . PRO D 1 140 ? -13.303 -7.129  -16.549 1.00 33.22 ? 163 PRO D CD    1 
ATOM   4855 N N     . ILE D 1 141 ? -11.190 -4.118  -16.688 1.00 37.86 ? 164 ILE D N     1 
ATOM   4856 C CA    . ILE D 1 141 ? -9.887  -3.457  -16.611 1.00 35.86 ? 164 ILE D CA    1 
ATOM   4857 C C     . ILE D 1 141 ? -9.924  -2.196  -17.461 1.00 34.30 ? 164 ILE D C     1 
ATOM   4858 O O     . ILE D 1 141 ? -10.244 -2.258  -18.653 1.00 32.21 ? 164 ILE D O     1 
ATOM   4859 C CB    . ILE D 1 141 ? -8.758  -4.385  -17.081 1.00 38.78 ? 164 ILE D CB    1 
ATOM   4860 C CG1   . ILE D 1 141 ? -8.757  -5.686  -16.271 1.00 39.64 ? 164 ILE D CG1   1 
ATOM   4861 C CG2   . ILE D 1 141 ? -7.415  -3.678  -16.967 1.00 39.94 ? 164 ILE D CG2   1 
ATOM   4862 C CD1   . ILE D 1 141 ? -7.823  -6.734  -16.837 1.00 42.64 ? 164 ILE D CD1   1 
ATOM   4863 N N     . SER D 1 142 ? -9.594  -1.055  -16.856 1.00 32.64 ? 165 SER D N     1 
ATOM   4864 C CA    . SER D 1 142 ? -9.477  0.182   -17.623 1.00 35.76 ? 165 SER D CA    1 
ATOM   4865 C C     . SER D 1 142 ? -8.411  0.011   -18.706 1.00 35.65 ? 165 SER D C     1 
ATOM   4866 O O     . SER D 1 142 ? -7.368  -0.594  -18.452 1.00 36.67 ? 165 SER D O     1 
ATOM   4867 C CB    . SER D 1 142 ? -9.099  1.354   -16.713 1.00 32.29 ? 165 SER D CB    1 
ATOM   4868 O OG    . SER D 1 142 ? -8.867  2.524   -17.482 1.00 40.35 ? 165 SER D OG    1 
ATOM   4869 N N     . PRO D 1 143 ? -8.643  0.497   -19.927 1.00 32.00 ? 166 PRO D N     1 
ATOM   4870 C CA    . PRO D 1 143 ? -7.604  0.356   -20.956 1.00 35.10 ? 166 PRO D CA    1 
ATOM   4871 C C     . PRO D 1 143 ? -6.402  1.262   -20.723 1.00 37.21 ? 166 PRO D C     1 
ATOM   4872 O O     . PRO D 1 143 ? -5.304  0.928   -21.189 1.00 36.32 ? 166 PRO D O     1 
ATOM   4873 C CB    . PRO D 1 143 ? -8.339  0.688   -22.261 1.00 34.58 ? 166 PRO D CB    1 
ATOM   4874 C CG    . PRO D 1 143 ? -9.566  1.417   -21.852 1.00 30.54 ? 166 PRO D CG    1 
ATOM   4875 C CD    . PRO D 1 143 ? -9.927  0.950   -20.480 1.00 30.47 ? 166 PRO D CD    1 
ATOM   4876 N N     . ILE D 1 144 ? -6.549  2.361   -19.981 1.00 31.90 ? 167 ILE D N     1 
ATOM   4877 C CA    . ILE D 1 144 ? -5.411  3.187   -19.586 1.00 33.74 ? 167 ILE D CA    1 
ATOM   4878 C C     . ILE D 1 144 ? -5.325  3.215   -18.068 1.00 34.73 ? 167 ILE D C     1 
ATOM   4879 O O     . ILE D 1 144 ? -6.336  3.405   -17.381 1.00 36.22 ? 167 ILE D O     1 
ATOM   4880 C CB    . ILE D 1 144 ? -5.508  4.609   -20.163 1.00 36.61 ? 167 ILE D CB    1 
ATOM   4881 C CG1   . ILE D 1 144 ? -5.672  4.539   -21.676 1.00 32.84 ? 167 ILE D CG1   1 
ATOM   4882 C CG2   . ILE D 1 144 ? -4.266  5.412   -19.822 1.00 34.58 ? 167 ILE D CG2   1 
ATOM   4883 C CD1   . ILE D 1 144 ? -7.044  4.909   -22.144 1.00 35.97 ? 167 ILE D CD1   1 
ATOM   4884 N N     . VAL D 1 145 ? -4.115  3.027   -17.546 1.00 32.16 ? 168 VAL D N     1 
ATOM   4885 C CA    . VAL D 1 145 ? -3.921  2.982   -16.105 1.00 36.48 ? 168 VAL D CA    1 
ATOM   4886 C C     . VAL D 1 145 ? -4.150  4.366   -15.505 1.00 35.68 ? 168 VAL D C     1 
ATOM   4887 O O     . VAL D 1 145 ? -3.919  5.398   -16.151 1.00 32.13 ? 168 VAL D O     1 
ATOM   4888 C CB    . VAL D 1 145 ? -2.512  2.452   -15.781 1.00 38.16 ? 168 VAL D CB    1 
ATOM   4889 C CG1   . VAL D 1 145 ? -1.447  3.450   -16.223 1.00 34.92 ? 168 VAL D CG1   1 
ATOM   4890 C CG2   . VAL D 1 145 ? -2.377  2.128   -14.298 1.00 43.30 ? 168 VAL D CG2   1 
ATOM   4891 N N     . ALA D 1 146 ? -4.615  4.393   -14.258 1.00 36.19 ? 169 ALA D N     1 
ATOM   4892 C CA    . ALA D 1 146 ? -4.869  5.663   -13.594 1.00 33.22 ? 169 ALA D CA    1 
ATOM   4893 C C     . ALA D 1 146 ? -3.566  6.415   -13.374 1.00 33.03 ? 169 ALA D C     1 
ATOM   4894 O O     . ALA D 1 146 ? -2.542  5.827   -13.018 1.00 36.48 ? 169 ALA D O     1 
ATOM   4895 C CB    . ALA D 1 146 ? -5.579  5.450   -12.259 1.00 28.45 ? 169 ALA D CB    1 
ATOM   4896 N N     . GLN D 1 147 ? -3.613  7.721   -13.621 1.00 32.73 ? 170 GLN D N     1 
ATOM   4897 C CA    . GLN D 1 147 ? -2.508  8.637   -13.339 1.00 32.00 ? 170 GLN D CA    1 
ATOM   4898 C C     . GLN D 1 147 ? -3.134  9.889   -12.755 1.00 32.24 ? 170 GLN D C     1 
ATOM   4899 O O     . GLN D 1 147 ? -3.314  10.897  -13.453 1.00 33.18 ? 170 GLN D O     1 
ATOM   4900 C CB    . GLN D 1 147 ? -1.701  8.955   -14.601 1.00 37.52 ? 170 GLN D CB    1 
ATOM   4901 C CG    . GLN D 1 147 ? -1.106  7.750   -15.304 1.00 40.87 ? 170 GLN D CG    1 
ATOM   4902 C CD    . GLN D 1 147 ? 0.303   7.459   -14.839 1.00 43.98 ? 170 GLN D CD    1 
ATOM   4903 O OE1   . GLN D 1 147 ? 0.548   6.449   -14.179 1.00 51.10 ? 170 GLN D OE1   1 
ATOM   4904 N NE2   . GLN D 1 147 ? 1.240   8.350   -15.171 1.00 39.92 ? 170 GLN D NE2   1 
ATOM   4905 N N     . PRO D 1 148 ? -3.479  9.861   -11.461 1.00 30.02 ? 171 PRO D N     1 
ATOM   4906 C CA    . PRO D 1 148 ? -4.321  10.925  -10.882 1.00 33.58 ? 171 PRO D CA    1 
ATOM   4907 C C     . PRO D 1 148 ? -3.752  12.325  -11.009 1.00 35.98 ? 171 PRO D C     1 
ATOM   4908 O O     . PRO D 1 148 ? -4.504  13.293  -10.830 1.00 33.26 ? 171 PRO D O     1 
ATOM   4909 C CB    . PRO D 1 148 ? -4.437  10.526  -9.399  1.00 32.70 ? 171 PRO D CB    1 
ATOM   4910 C CG    . PRO D 1 148 ? -4.018  9.136   -9.322  1.00 27.32 ? 171 PRO D CG    1 
ATOM   4911 C CD    . PRO D 1 148 ? -3.099  8.849   -10.463 1.00 31.28 ? 171 PRO D CD    1 
ATOM   4912 N N     . HIS D 1 149 ? -2.451  12.476  -11.271 1.00 32.02 ? 172 HIS D N     1 
ATOM   4913 C CA    . HIS D 1 149 ? -1.901  13.811  -11.465 1.00 37.32 ? 172 HIS D CA    1 
ATOM   4914 C C     . HIS D 1 149 ? -2.120  14.322  -12.882 1.00 37.60 ? 172 HIS D C     1 
ATOM   4915 O O     . HIS D 1 149 ? -1.943  15.519  -13.133 1.00 40.34 ? 172 HIS D O     1 
ATOM   4916 C CB    . HIS D 1 149 ? -0.399  13.829  -11.127 1.00 37.92 ? 172 HIS D CB    1 
ATOM   4917 C CG    . HIS D 1 149 ? 0.442   13.017  -12.061 1.00 36.98 ? 172 HIS D CG    1 
ATOM   4918 N ND1   . HIS D 1 149 ? 0.316   11.648  -12.180 1.00 39.83 ? 172 HIS D ND1   1 
ATOM   4919 C CD2   . HIS D 1 149 ? 1.414   13.383  -12.930 1.00 35.75 ? 172 HIS D CD2   1 
ATOM   4920 C CE1   . HIS D 1 149 ? 1.180   11.205  -13.080 1.00 42.10 ? 172 HIS D CE1   1 
ATOM   4921 N NE2   . HIS D 1 149 ? 1.857   12.239  -13.551 1.00 41.08 ? 172 HIS D NE2   1 
ATOM   4922 N N     . LEU D 1 150 ? -2.511  13.447  -13.802 1.00 34.72 ? 173 LEU D N     1 
ATOM   4923 C CA    . LEU D 1 150 ? -2.756  13.801  -15.190 1.00 32.21 ? 173 LEU D CA    1 
ATOM   4924 C C     . LEU D 1 150 ? -4.244  13.902  -15.516 1.00 33.82 ? 173 LEU D C     1 
ATOM   4925 O O     . LEU D 1 150 ? -4.665  14.848  -16.179 1.00 30.47 ? 173 LEU D O     1 
ATOM   4926 C CB    . LEU D 1 150 ? -2.093  12.764  -16.103 1.00 31.91 ? 173 LEU D CB    1 
ATOM   4927 C CG    . LEU D 1 150 ? -0.566  12.777  -16.167 1.00 36.15 ? 173 LEU D CG    1 
ATOM   4928 C CD1   . LEU D 1 150 ? -0.074  11.650  -17.057 1.00 37.99 ? 173 LEU D CD1   1 
ATOM   4929 C CD2   . LEU D 1 150 ? -0.073  14.138  -16.673 1.00 37.34 ? 173 LEU D CD2   1 
ATOM   4930 N N     . TYR D 1 151 ? -5.046  12.934  -15.069 1.00 27.80 ? 174 TYR D N     1 
ATOM   4931 C CA    . TYR D 1 151 ? -6.453  12.860  -15.430 1.00 29.49 ? 174 TYR D CA    1 
ATOM   4932 C C     . TYR D 1 151 ? -7.199  12.037  -14.386 1.00 29.30 ? 174 TYR D C     1 
ATOM   4933 O O     . TYR D 1 151 ? -6.600  11.327  -13.573 1.00 26.81 ? 174 TYR D O     1 
ATOM   4934 C CB    . TYR D 1 151 ? -6.636  12.241  -16.822 1.00 30.54 ? 174 TYR D CB    1 
ATOM   4935 C CG    . TYR D 1 151 ? -5.775  11.021  -17.040 1.00 30.67 ? 174 TYR D CG    1 
ATOM   4936 C CD1   . TYR D 1 151 ? -6.137  9.772   -16.513 1.00 28.31 ? 174 TYR D CD1   1 
ATOM   4937 C CD2   . TYR D 1 151 ? -4.590  11.107  -17.765 1.00 32.72 ? 174 TYR D CD2   1 
ATOM   4938 C CE1   . TYR D 1 151 ? -5.332  8.643   -16.706 1.00 26.28 ? 174 TYR D CE1   1 
ATOM   4939 C CE2   . TYR D 1 151 ? -3.779  9.987   -17.963 1.00 32.63 ? 174 TYR D CE2   1 
ATOM   4940 C CZ    . TYR D 1 151 ? -4.153  8.760   -17.432 1.00 33.06 ? 174 TYR D CZ    1 
ATOM   4941 O OH    . TYR D 1 151 ? -3.347  7.662   -17.642 1.00 32.48 ? 174 TYR D OH    1 
ATOM   4942 N N     . HIS D 1 152 ? -8.523  12.118  -14.448 1.00 27.65 ? 175 HIS D N     1 
ATOM   4943 C CA    . HIS D 1 152 ? -9.414  11.315  -13.622 1.00 28.38 ? 175 HIS D CA    1 
ATOM   4944 C C     . HIS D 1 152 ? -10.174 10.344  -14.513 1.00 29.10 ? 175 HIS D C     1 
ATOM   4945 O O     . HIS D 1 152 ? -10.696 10.747  -15.559 1.00 27.13 ? 175 HIS D O     1 
ATOM   4946 C CB    . HIS D 1 152 ? -10.381 12.218  -12.859 1.00 29.85 ? 175 HIS D CB    1 
ATOM   4947 C CG    . HIS D 1 152 ? -9.704  13.075  -11.833 1.00 35.46 ? 175 HIS D CG    1 
ATOM   4948 N ND1   . HIS D 1 152 ? -10.060 14.386  -11.599 1.00 39.03 ? 175 HIS D ND1   1 
ATOM   4949 C CD2   . HIS D 1 152 ? -8.685  12.802  -10.981 1.00 37.08 ? 175 HIS D CD2   1 
ATOM   4950 C CE1   . HIS D 1 152 ? -9.295  14.882  -10.642 1.00 40.12 ? 175 HIS D CE1   1 
ATOM   4951 N NE2   . HIS D 1 152 ? -8.453  13.941  -10.249 1.00 41.24 ? 175 HIS D NE2   1 
ATOM   4952 N N     . ILE D 1 153 ? -10.235 9.074   -14.105 1.00 26.71 ? 176 ILE D N     1 
ATOM   4953 C CA    . ILE D 1 153 ? -10.976 8.042   -14.834 1.00 23.70 ? 176 ILE D CA    1 
ATOM   4954 C C     . ILE D 1 153 ? -12.349 7.862   -14.192 1.00 27.42 ? 176 ILE D C     1 
ATOM   4955 O O     . ILE D 1 153 ? -12.453 7.431   -13.034 1.00 23.15 ? 176 ILE D O     1 
ATOM   4956 C CB    . ILE D 1 153 ? -10.222 6.704   -14.846 1.00 25.99 ? 176 ILE D CB    1 
ATOM   4957 C CG1   . ILE D 1 153 ? -8.809  6.862   -15.411 1.00 27.39 ? 176 ILE D CG1   1 
ATOM   4958 C CG2   . ILE D 1 153 ? -11.032 5.647   -15.615 1.00 22.54 ? 176 ILE D CG2   1 
ATOM   4959 C CD1   . ILE D 1 153 ? -7.988  5.588   -15.288 1.00 27.72 ? 176 ILE D CD1   1 
ATOM   4960 N N     . ARG D 1 154 ? -13.406 8.138   -14.952 1.00 23.04 ? 177 ARG D N     1 
ATOM   4961 C CA    . ARG D 1 154 ? -14.775 7.933   -14.500 1.00 24.18 ? 177 ARG D CA    1 
ATOM   4962 C C     . ARG D 1 154 ? -15.365 6.720   -15.212 1.00 26.22 ? 177 ARG D C     1 
ATOM   4963 O O     . ARG D 1 154 ? -15.108 6.504   -16.399 1.00 22.15 ? 177 ARG D O     1 
ATOM   4964 C CB    . ARG D 1 154 ? -15.644 9.171   -14.766 1.00 24.75 ? 177 ARG D CB    1 
ATOM   4965 C CG    . ARG D 1 154 ? -15.366 10.365  -13.815 1.00 27.30 ? 177 ARG D CG    1 
ATOM   4966 C CD    . ARG D 1 154 ? -16.239 11.577  -14.139 1.00 31.22 ? 177 ARG D CD    1 
ATOM   4967 N NE    . ARG D 1 154 ? -15.990 12.694  -13.225 1.00 29.59 ? 177 ARG D NE    1 
ATOM   4968 C CZ    . ARG D 1 154 ? -15.013 13.585  -13.373 1.00 31.36 ? 177 ARG D CZ    1 
ATOM   4969 N NH1   . ARG D 1 154 ? -14.176 13.502  -14.406 1.00 31.38 ? 177 ARG D NH1   1 
ATOM   4970 N NH2   . ARG D 1 154 ? -14.862 14.556  -12.483 1.00 34.67 ? 177 ARG D NH2   1 
ATOM   4971 N N     . HIS D 1 155 ? -16.137 5.925   -14.474 1.00 27.05 ? 178 HIS D N     1 
ATOM   4972 C CA    . HIS D 1 155 ? -16.915 4.829   -15.045 1.00 26.08 ? 178 HIS D CA    1 
ATOM   4973 C C     . HIS D 1 155 ? -18.214 5.414   -15.580 1.00 24.21 ? 178 HIS D C     1 
ATOM   4974 O O     . HIS D 1 155 ? -19.037 5.922   -14.814 1.00 24.21 ? 178 HIS D O     1 
ATOM   4975 C CB    . HIS D 1 155 ? -17.177 3.753   -13.993 1.00 26.33 ? 178 HIS D CB    1 
ATOM   4976 C CG    . HIS D 1 155 ? -17.781 2.497   -14.543 1.00 25.02 ? 178 HIS D CG    1 
ATOM   4977 N ND1   . HIS D 1 155 ? -18.691 1.738   -13.839 1.00 27.75 ? 178 HIS D ND1   1 
ATOM   4978 C CD2   . HIS D 1 155 ? -17.602 1.866   -15.726 1.00 24.44 ? 178 HIS D CD2   1 
ATOM   4979 C CE1   . HIS D 1 155 ? -19.048 0.692   -14.564 1.00 26.36 ? 178 HIS D CE1   1 
ATOM   4980 N NE2   . HIS D 1 155 ? -18.403 0.747   -15.716 1.00 29.56 ? 178 HIS D NE2   1 
ATOM   4981 N N     . PHE D 1 156 ? -18.395 5.360   -16.894 1.00 25.25 ? 179 PHE D N     1 
ATOM   4982 C CA    . PHE D 1 156 ? -19.486 6.066   -17.559 1.00 23.61 ? 179 PHE D CA    1 
ATOM   4983 C C     . PHE D 1 156 ? -20.721 5.192   -17.739 1.00 28.22 ? 179 PHE D C     1 
ATOM   4984 O O     . PHE D 1 156 ? -21.848 5.674   -17.541 1.00 27.02 ? 179 PHE D O     1 
ATOM   4985 C CB    . PHE D 1 156 ? -18.996 6.586   -18.917 1.00 23.85 ? 179 PHE D CB    1 
ATOM   4986 C CG    . PHE D 1 156 ? -19.942 7.531   -19.599 1.00 27.25 ? 179 PHE D CG    1 
ATOM   4987 C CD1   . PHE D 1 156 ? -20.575 8.551   -18.891 1.00 27.08 ? 179 PHE D CD1   1 
ATOM   4988 C CD2   . PHE D 1 156 ? -20.172 7.421   -20.965 1.00 26.11 ? 179 PHE D CD2   1 
ATOM   4989 C CE1   . PHE D 1 156 ? -21.434 9.431   -19.528 1.00 28.42 ? 179 PHE D CE1   1 
ATOM   4990 C CE2   . PHE D 1 156 ? -21.021 8.299   -21.614 1.00 24.59 ? 179 PHE D CE2   1 
ATOM   4991 C CZ    . PHE D 1 156 ? -21.662 9.305   -20.893 1.00 28.24 ? 179 PHE D CZ    1 
ATOM   4992 N N     . ASP D 1 157 ? -20.539 3.915   -18.097 1.00 23.60 ? 180 ASP D N     1 
ATOM   4993 C CA    . ASP D 1 157 ? -21.664 3.002   -18.287 1.00 24.83 ? 180 ASP D CA    1 
ATOM   4994 C C     . ASP D 1 157 ? -21.156 1.570   -18.458 1.00 26.69 ? 180 ASP D C     1 
ATOM   4995 O O     . ASP D 1 157 ? -19.977 1.333   -18.761 1.00 26.27 ? 180 ASP D O     1 
ATOM   4996 C CB    . ASP D 1 157 ? -22.512 3.413   -19.496 1.00 27.55 ? 180 ASP D CB    1 
ATOM   4997 C CG    . ASP D 1 157 ? -23.989 3.065   -19.336 1.00 32.89 ? 180 ASP D CG    1 
ATOM   4998 O OD1   . ASP D 1 157 ? -24.353 2.334   -18.392 1.00 31.45 ? 180 ASP D OD1   1 
ATOM   4999 O OD2   . ASP D 1 157 ? -24.787 3.526   -20.179 1.00 36.00 ? 180 ASP D OD2   1 
ATOM   5000 N N     . PHE D 1 158 ? -22.069 0.618   -18.236 1.00 24.58 ? 181 PHE D N     1 
ATOM   5001 C CA    . PHE D 1 158 ? -21.854 -0.813  -18.480 1.00 26.62 ? 181 PHE D CA    1 
ATOM   5002 C C     . PHE D 1 158 ? -23.059 -1.285  -19.281 1.00 27.42 ? 181 PHE D C     1 
ATOM   5003 O O     . PHE D 1 158 ? -24.194 -1.171  -18.812 1.00 27.28 ? 181 PHE D O     1 
ATOM   5004 C CB    . PHE D 1 158 ? -21.713 -1.600  -17.156 1.00 29.15 ? 181 PHE D CB    1 
ATOM   5005 C CG    . PHE D 1 158 ? -21.557 -3.120  -17.320 1.00 26.38 ? 181 PHE D CG    1 
ATOM   5006 C CD1   . PHE D 1 158 ? -20.798 -3.659  -18.349 1.00 24.91 ? 181 PHE D CD1   1 
ATOM   5007 C CD2   . PHE D 1 158 ? -22.161 -3.994  -16.425 1.00 31.03 ? 181 PHE D CD2   1 
ATOM   5008 C CE1   . PHE D 1 158 ? -20.655 -5.024  -18.497 1.00 25.16 ? 181 PHE D CE1   1 
ATOM   5009 C CE2   . PHE D 1 158 ? -22.020 -5.373  -16.559 1.00 26.92 ? 181 PHE D CE2   1 
ATOM   5010 C CZ    . PHE D 1 158 ? -21.265 -5.888  -17.593 1.00 31.20 ? 181 PHE D CZ    1 
ATOM   5011 N N     . ILE D 1 159 ? -22.831 -1.768  -20.497 1.00 23.28 ? 182 ILE D N     1 
ATOM   5012 C CA    . ILE D 1 159 ? -23.919 -2.046  -21.432 1.00 28.08 ? 182 ILE D CA    1 
ATOM   5013 C C     . ILE D 1 159 ? -23.822 -3.515  -21.828 1.00 27.69 ? 182 ILE D C     1 
ATOM   5014 O O     . ILE D 1 159 ? -23.031 -3.890  -22.700 1.00 24.84 ? 182 ILE D O     1 
ATOM   5015 C CB    . ILE D 1 159 ? -23.876 -1.109  -22.642 1.00 26.47 ? 182 ILE D CB    1 
ATOM   5016 C CG1   . ILE D 1 159 ? -24.008 0.328   -22.120 1.00 26.40 ? 182 ILE D CG1   1 
ATOM   5017 C CG2   . ILE D 1 159 ? -24.997 -1.433  -23.647 1.00 24.47 ? 182 ILE D CG2   1 
ATOM   5018 C CD1   . ILE D 1 159 ? -23.643 1.379   -23.089 1.00 29.22 ? 182 ILE D CD1   1 
ATOM   5019 N N     . VAL D 1 160 ? -24.621 -4.356  -21.166 1.00 26.50 ? 183 VAL D N     1 
ATOM   5020 C CA    . VAL D 1 160 ? -24.560 -5.801  -21.382 1.00 27.54 ? 183 VAL D CA    1 
ATOM   5021 C C     . VAL D 1 160 ? -25.192 -6.250  -22.688 1.00 23.41 ? 183 VAL D C     1 
ATOM   5022 O O     . VAL D 1 160 ? -24.998 -7.396  -23.080 1.00 25.98 ? 183 VAL D O     1 
ATOM   5023 C CB    . VAL D 1 160 ? -25.252 -6.555  -20.227 1.00 26.56 ? 183 VAL D CB    1 
ATOM   5024 C CG1   . VAL D 1 160 ? -24.475 -6.370  -18.921 1.00 28.65 ? 183 VAL D CG1   1 
ATOM   5025 C CG2   . VAL D 1 160 ? -26.712 -6.091  -20.079 1.00 27.06 ? 183 VAL D CG2   1 
ATOM   5026 N N     . ARG D 1 161 ? -25.975 -5.399  -23.350 1.00 25.22 ? 184 ARG D N     1 
ATOM   5027 C CA    . ARG D 1 161 ? -26.582 -5.763  -24.625 1.00 31.62 ? 184 ARG D CA    1 
ATOM   5028 C C     . ARG D 1 161 ? -25.610 -5.655  -25.789 1.00 33.84 ? 184 ARG D C     1 
ATOM   5029 O O     . ARG D 1 161 ? -25.874 -6.228  -26.855 1.00 35.64 ? 184 ARG D O     1 
ATOM   5030 C CB    . ARG D 1 161 ? -27.792 -4.878  -24.918 1.00 36.15 ? 184 ARG D CB    1 
ATOM   5031 C CG    . ARG D 1 161 ? -28.997 -5.163  -24.051 1.00 39.29 ? 184 ARG D CG    1 
ATOM   5032 C CD    . ARG D 1 161 ? -30.184 -4.329  -24.517 1.00 47.51 ? 184 ARG D CD    1 
ATOM   5033 N NE    . ARG D 1 161 ? -30.500 -4.591  -25.919 1.00 51.09 ? 184 ARG D NE    1 
ATOM   5034 C CZ    . ARG D 1 161 ? -31.736 -4.666  -26.397 1.00 45.66 ? 184 ARG D CZ    1 
ATOM   5035 N NH1   . ARG D 1 161 ? -32.762 -4.497  -25.578 1.00 45.03 ? 184 ARG D NH1   1 
ATOM   5036 N NH2   . ARG D 1 161 ? -31.945 -4.915  -27.686 1.00 47.75 ? 184 ARG D NH2   1 
ATOM   5037 N N     . ASN D 1 162 ? -24.508 -4.933  -25.613 1.00 31.94 ? 185 ASN D N     1 
ATOM   5038 C CA    . ASN D 1 162 ? -23.491 -4.856  -26.650 1.00 30.44 ? 185 ASN D CA    1 
ATOM   5039 C C     . ASN D 1 162 ? -22.858 -6.226  -26.865 1.00 28.13 ? 185 ASN D C     1 
ATOM   5040 O O     . ASN D 1 162 ? -22.752 -7.038  -25.942 1.00 28.80 ? 185 ASN D O     1 
ATOM   5041 C CB    . ASN D 1 162 ? -22.421 -3.829  -26.267 1.00 26.19 ? 185 ASN D CB    1 
ATOM   5042 C CG    . ASN D 1 162 ? -21.624 -3.340  -27.471 1.00 27.12 ? 185 ASN D CG    1 
ATOM   5043 O OD1   . ASN D 1 162 ? -22.060 -2.441  -28.181 1.00 27.97 ? 185 ASN D OD1   1 
ATOM   5044 N ND2   . ASN D 1 162 ? -20.452 -3.926  -27.694 1.00 24.63 ? 185 ASN D ND2   1 
ATOM   5045 N N     . ILE D 1 163 ? -22.445 -6.483  -28.101 1.00 28.50 ? 186 ILE D N     1 
ATOM   5046 C CA    . ILE D 1 163 ? -21.788 -7.736  -28.469 1.00 30.50 ? 186 ILE D CA    1 
ATOM   5047 C C     . ILE D 1 163 ? -20.311 -7.478  -28.749 1.00 31.57 ? 186 ILE D C     1 
ATOM   5048 O O     . ILE D 1 163 ? -19.971 -6.971  -29.827 1.00 33.50 ? 186 ILE D O     1 
ATOM   5049 C CB    . ILE D 1 163 ? -22.461 -8.373  -29.696 1.00 32.07 ? 186 ILE D CB    1 
ATOM   5050 C CG1   . ILE D 1 163 ? -23.934 -8.681  -29.404 1.00 31.44 ? 186 ILE D CG1   1 
ATOM   5051 C CG2   . ILE D 1 163 ? -21.711 -9.634  -30.107 1.00 34.18 ? 186 ILE D CG2   1 
ATOM   5052 C CD1   . ILE D 1 163 ? -24.736 -8.994  -30.627 1.00 40.64 ? 186 ILE D CD1   1 
ATOM   5053 N N     . PRO D 1 164 ? -19.392 -7.794  -27.828 1.00 30.00 ? 187 PRO D N     1 
ATOM   5054 C CA    . PRO D 1 164 ? -19.566 -8.308  -26.470 1.00 30.67 ? 187 PRO D CA    1 
ATOM   5055 C C     . PRO D 1 164 ? -19.879 -7.170  -25.481 1.00 30.94 ? 187 PRO D C     1 
ATOM   5056 O O     . PRO D 1 164 ? -19.748 -6.005  -25.866 1.00 29.31 ? 187 PRO D O     1 
ATOM   5057 C CB    . PRO D 1 164 ? -18.208 -8.953  -26.176 1.00 31.37 ? 187 PRO D CB    1 
ATOM   5058 C CG    . PRO D 1 164 ? -17.249 -8.091  -26.917 1.00 30.79 ? 187 PRO D CG    1 
ATOM   5059 C CD    . PRO D 1 164 ? -17.966 -7.623  -28.167 1.00 30.06 ? 187 PRO D CD    1 
ATOM   5060 N N     . PRO D 1 165 ? -20.319 -7.502  -24.264 1.00 28.33 ? 188 PRO D N     1 
ATOM   5061 C CA    . PRO D 1 165 ? -20.653 -6.455  -23.287 1.00 25.21 ? 188 PRO D CA    1 
ATOM   5062 C C     . PRO D 1 165 ? -19.546 -5.415  -23.162 1.00 27.21 ? 188 PRO D C     1 
ATOM   5063 O O     . PRO D 1 165 ? -18.358 -5.743  -23.086 1.00 27.19 ? 188 PRO D O     1 
ATOM   5064 C CB    . PRO D 1 165 ? -20.844 -7.242  -21.986 1.00 25.56 ? 188 PRO D CB    1 
ATOM   5065 C CG    . PRO D 1 165 ? -21.429 -8.562  -22.474 1.00 28.57 ? 188 PRO D CG    1 
ATOM   5066 C CD    . PRO D 1 165 ? -20.772 -8.838  -23.820 1.00 29.89 ? 188 PRO D CD    1 
ATOM   5067 N N     . ALA D 1 166 ? -19.950 -4.148  -23.151 1.00 24.36 ? 189 ALA D N     1 
ATOM   5068 C CA    . ALA D 1 166 ? -19.037 -3.024  -23.291 1.00 25.14 ? 189 ALA D CA    1 
ATOM   5069 C C     . ALA D 1 166 ? -19.005 -2.209  -22.010 1.00 26.53 ? 189 ALA D C     1 
ATOM   5070 O O     . ALA D 1 166 ? -20.049 -1.971  -21.390 1.00 24.70 ? 189 ALA D O     1 
ATOM   5071 C CB    . ALA D 1 166 ? -19.452 -2.115  -24.461 1.00 24.89 ? 189 ALA D CB    1 
ATOM   5072 N N     . GLN D 1 167 ? -17.804 -1.786  -21.621 1.00 25.07 ? 190 GLN D N     1 
ATOM   5073 C CA    . GLN D 1 167 ? -17.613 -0.811  -20.555 1.00 26.63 ? 190 GLN D CA    1 
ATOM   5074 C C     . GLN D 1 167 ? -17.184 0.515   -21.178 1.00 24.80 ? 190 GLN D C     1 
ATOM   5075 O O     . GLN D 1 167 ? -16.304 0.538   -22.044 1.00 24.00 ? 190 GLN D O     1 
ATOM   5076 C CB    . GLN D 1 167 ? -16.569 -1.296  -19.541 1.00 25.32 ? 190 GLN D CB    1 
ATOM   5077 C CG    . GLN D 1 167 ? -17.023 -2.520  -18.740 1.00 30.42 ? 190 GLN D CG    1 
ATOM   5078 C CD    . GLN D 1 167 ? -17.821 -2.140  -17.497 1.00 28.87 ? 190 GLN D CD    1 
ATOM   5079 O OE1   . GLN D 1 167 ? -18.482 -1.099  -17.463 1.00 29.23 ? 190 GLN D OE1   1 
ATOM   5080 N NE2   . GLN D 1 167 ? -17.750 -2.979  -16.465 1.00 26.11 ? 190 GLN D NE2   1 
ATOM   5081 N N     . LEU D 1 168 ? -17.796 1.609   -20.726 1.00 21.92 ? 191 LEU D N     1 
ATOM   5082 C CA    . LEU D 1 168 ? -17.501 2.950   -21.217 1.00 20.15 ? 191 LEU D CA    1 
ATOM   5083 C C     . LEU D 1 168 ? -16.804 3.741   -20.121 1.00 25.76 ? 191 LEU D C     1 
ATOM   5084 O O     . LEU D 1 168 ? -17.265 3.763   -18.971 1.00 24.08 ? 191 LEU D O     1 
ATOM   5085 C CB    . LEU D 1 168 ? -18.771 3.681   -21.656 1.00 23.21 ? 191 LEU D CB    1 
ATOM   5086 C CG    . LEU D 1 168 ? -19.558 3.082   -22.819 1.00 23.62 ? 191 LEU D CG    1 
ATOM   5087 C CD1   . LEU D 1 168 ? -20.668 4.029   -23.274 1.00 26.59 ? 191 LEU D CD1   1 
ATOM   5088 C CD2   . LEU D 1 168 ? -18.646 2.737   -23.989 1.00 24.13 ? 191 LEU D CD2   1 
ATOM   5089 N N     . TRP D 1 169 ? -15.707 4.398   -20.486 1.00 20.50 ? 192 TRP D N     1 
ATOM   5090 C CA    . TRP D 1 169 ? -14.897 5.184   -19.565 1.00 24.79 ? 192 TRP D CA    1 
ATOM   5091 C C     . TRP D 1 169 ? -14.728 6.602   -20.104 1.00 26.19 ? 192 TRP D C     1 
ATOM   5092 O O     . TRP D 1 169 ? -14.630 6.812   -21.318 1.00 23.83 ? 192 TRP D O     1 
ATOM   5093 C CB    . TRP D 1 169 ? -13.504 4.563   -19.381 1.00 22.84 ? 192 TRP D CB    1 
ATOM   5094 C CG    . TRP D 1 169 ? -13.505 3.119   -19.026 1.00 22.78 ? 192 TRP D CG    1 
ATOM   5095 C CD1   . TRP D 1 169 ? -13.419 2.054   -19.888 1.00 27.27 ? 192 TRP D CD1   1 
ATOM   5096 C CD2   . TRP D 1 169 ? -13.587 2.565   -17.708 1.00 22.85 ? 192 TRP D CD2   1 
ATOM   5097 N NE1   . TRP D 1 169 ? -13.449 0.870   -19.181 1.00 22.03 ? 192 TRP D NE1   1 
ATOM   5098 C CE2   . TRP D 1 169 ? -13.554 1.156   -17.843 1.00 26.90 ? 192 TRP D CE2   1 
ATOM   5099 C CE3   . TRP D 1 169 ? -13.702 3.120   -16.430 1.00 24.03 ? 192 TRP D CE3   1 
ATOM   5100 C CZ2   . TRP D 1 169 ? -13.618 0.303   -16.747 1.00 26.20 ? 192 TRP D CZ2   1 
ATOM   5101 C CZ3   . TRP D 1 169 ? -13.771 2.264   -15.338 1.00 28.55 ? 192 TRP D CZ3   1 
ATOM   5102 C CH2   . TRP D 1 169 ? -13.729 0.869   -15.508 1.00 25.61 ? 192 TRP D CH2   1 
ATOM   5103 N N     . THR D 1 170 ? -14.671 7.579   -19.199 1.00 26.19 ? 193 THR D N     1 
ATOM   5104 C CA    . THR D 1 170 ? -14.238 8.917   -19.580 1.00 26.13 ? 193 THR D CA    1 
ATOM   5105 C C     . THR D 1 170 ? -12.962 9.292   -18.840 1.00 27.10 ? 193 THR D C     1 
ATOM   5106 O O     . THR D 1 170 ? -12.741 8.897   -17.688 1.00 25.35 ? 193 THR D O     1 
ATOM   5107 C CB    . THR D 1 170 ? -15.296 9.982   -19.314 1.00 23.84 ? 193 THR D CB    1 
ATOM   5108 O OG1   . THR D 1 170 ? -15.497 10.106  -17.906 1.00 29.26 ? 193 THR D OG1   1 
ATOM   5109 C CG2   . THR D 1 170 ? -16.610 9.635   -20.017 1.00 25.83 ? 193 THR D CG2   1 
ATOM   5110 N N     . TYR D 1 171 ? -12.123 10.059  -19.523 1.00 24.15 ? 194 TYR D N     1 
ATOM   5111 C CA    . TYR D 1 171 ? -10.891 10.589  -18.962 1.00 25.35 ? 194 TYR D CA    1 
ATOM   5112 C C     . TYR D 1 171 ? -10.970 12.099  -19.056 1.00 26.14 ? 194 TYR D C     1 
ATOM   5113 O O     . TYR D 1 171 ? -11.316 12.625  -20.115 1.00 26.35 ? 194 TYR D O     1 
ATOM   5114 C CB    . TYR D 1 171 ? -9.670  10.055  -19.727 1.00 23.17 ? 194 TYR D CB    1 
ATOM   5115 C CG    . TYR D 1 171 ? -9.606  8.542   -19.764 1.00 27.47 ? 194 TYR D CG    1 
ATOM   5116 C CD1   . TYR D 1 171 ? -10.340 7.817   -20.693 1.00 27.18 ? 194 TYR D CD1   1 
ATOM   5117 C CD2   . TYR D 1 171 ? -8.822  7.841   -18.859 1.00 29.40 ? 194 TYR D CD2   1 
ATOM   5118 C CE1   . TYR D 1 171 ? -10.287 6.438   -20.723 1.00 28.59 ? 194 TYR D CE1   1 
ATOM   5119 C CE2   . TYR D 1 171 ? -8.760  6.461   -18.886 1.00 31.46 ? 194 TYR D CE2   1 
ATOM   5120 C CZ    . TYR D 1 171 ? -9.498  5.766   -19.816 1.00 27.10 ? 194 TYR D CZ    1 
ATOM   5121 O OH    . TYR D 1 171 ? -9.437  4.390   -19.838 1.00 36.63 ? 194 TYR D OH    1 
ATOM   5122 N N     . THR D 1 172 ? -10.698 12.795  -17.955 1.00 27.54 ? 195 THR D N     1 
ATOM   5123 C CA    . THR D 1 172 ? -10.756 14.254  -17.962 1.00 29.37 ? 195 THR D CA    1 
ATOM   5124 C C     . THR D 1 172 ? -9.558  14.810  -17.214 1.00 30.61 ? 195 THR D C     1 
ATOM   5125 O O     . THR D 1 172 ? -9.099  14.224  -16.230 1.00 32.80 ? 195 THR D O     1 
ATOM   5126 C CB    . THR D 1 172 ? -12.039 14.817  -17.327 1.00 30.64 ? 195 THR D CB    1 
ATOM   5127 O OG1   . THR D 1 172 ? -12.161 14.317  -15.995 1.00 46.30 ? 195 THR D OG1   1 
ATOM   5128 C CG2   . THR D 1 172 ? -13.264 14.397  -18.102 1.00 29.89 ? 195 THR D CG2   1 
ATOM   5129 N N     . ARG D 1 173 ? -9.066  15.957  -17.692 1.00 32.59 ? 196 ARG D N     1 
ATOM   5130 C CA    . ARG D 1 173 ? -7.891  16.597  -17.115 1.00 31.95 ? 196 ARG D CA    1 
ATOM   5131 C C     . ARG D 1 173 ? -8.055  16.781  -15.614 1.00 33.67 ? 196 ARG D C     1 
ATOM   5132 O O     . ARG D 1 173 ? -9.084  17.282  -15.145 1.00 34.75 ? 196 ARG D O     1 
ATOM   5133 C CB    . ARG D 1 173 ? -7.652  17.955  -17.787 1.00 34.89 ? 196 ARG D CB    1 
ATOM   5134 C CG    . ARG D 1 173 ? -6.440  18.695  -17.253 1.00 37.07 ? 196 ARG D CG    1 
ATOM   5135 C CD    . ARG D 1 173 ? -5.183  17.895  -17.471 1.00 32.01 ? 196 ARG D CD    1 
ATOM   5136 N NE    . ARG D 1 173 ? -4.764  17.912  -18.868 1.00 33.19 ? 196 ARG D NE    1 
ATOM   5137 C CZ    . ARG D 1 173 ? -3.990  16.994  -19.434 1.00 34.94 ? 196 ARG D CZ    1 
ATOM   5138 N NH1   . ARG D 1 173 ? -3.550  15.960  -18.727 1.00 34.50 ? 196 ARG D NH1   1 
ATOM   5139 N NH2   . ARG D 1 173 ? -3.652  17.107  -20.713 1.00 40.51 ? 196 ARG D NH2   1 
ATOM   5140 N N     . ALA D 1 174 ? -7.038  16.365  -14.865 1.00 33.30 ? 197 ALA D N     1 
ATOM   5141 C CA    . ALA D 1 174 ? -7.085  16.429  -13.402 1.00 38.72 ? 197 ALA D CA    1 
ATOM   5142 C C     . ALA D 1 174 ? -7.012  17.866  -12.882 1.00 51.43 ? 197 ALA D C     1 
ATOM   5143 O O     . ALA D 1 174 ? -6.362  18.735  -13.474 1.00 47.14 ? 197 ALA D O     1 
ATOM   5144 C CB    . ALA D 1 174 ? -5.966  15.601  -12.805 1.00 41.31 ? 197 ALA D CB    1 
ATOM   5145 O OXT   . ALA D 1 174 ? -7.608  18.184  -11.846 1.00 59.56 ? 197 ALA D OXT   1 
HETATM 5146 C CS    . MTA E 2 .   ? 10.377  -6.835  10.636  1.00 39.83 ? 201 MTA A CS    1 
HETATM 5147 S "S5'" . MTA E 2 .   ? 8.905   -6.339  9.675   1.00 45.74 ? 201 MTA A "S5'" 1 
HETATM 5148 C "C5'" . MTA E 2 .   ? 8.693   -4.538  9.742   1.00 34.99 ? 201 MTA A "C5'" 1 
HETATM 5149 C "C4'" . MTA E 2 .   ? 8.600   -4.097  11.229  1.00 34.76 ? 201 MTA A "C4'" 1 
HETATM 5150 O "O4'" . MTA E 2 .   ? 8.787   -2.800  11.322  1.00 29.60 ? 201 MTA A "O4'" 1 
HETATM 5151 C "C2'" . MTA E 2 .   ? 6.532   -2.981  11.850  1.00 31.57 ? 201 MTA A "C2'" 1 
HETATM 5152 O "O2'" . MTA E 2 .   ? 5.519   -2.883  12.947  1.00 27.06 ? 201 MTA A "O2'" 1 
HETATM 5153 C "C3'" . MTA E 2 .   ? 7.192   -4.376  11.809  1.00 30.34 ? 201 MTA A "C3'" 1 
HETATM 5154 O "O3'" . MTA E 2 .   ? 7.357   -4.897  13.058  1.00 31.04 ? 201 MTA A "O3'" 1 
HETATM 5155 C "C1'" . MTA E 2 .   ? 7.534   -2.169  12.111  1.00 30.58 ? 201 MTA A "C1'" 1 
HETATM 5156 N N9    . MTA E 2 .   ? 7.403   -0.846  11.541  1.00 30.92 ? 201 MTA A N9    1 
HETATM 5157 C C8    . MTA E 2 .   ? 6.858   -0.587  10.344  1.00 29.70 ? 201 MTA A C8    1 
HETATM 5158 N N7    . MTA E 2 .   ? 6.943   0.725   10.131  1.00 28.66 ? 201 MTA A N7    1 
HETATM 5159 C C5    . MTA E 2 .   ? 7.564   1.277   11.189  1.00 28.01 ? 201 MTA A C5    1 
HETATM 5160 C C6    . MTA E 2 .   ? 7.919   2.573   11.477  1.00 22.17 ? 201 MTA A C6    1 
HETATM 5161 N N6    . MTA E 2 .   ? 7.722   3.810   10.764  1.00 23.70 ? 201 MTA A N6    1 
HETATM 5162 N N1    . MTA E 2 .   ? 8.529   2.870   12.617  1.00 25.82 ? 201 MTA A N1    1 
HETATM 5163 C C2    . MTA E 2 .   ? 8.821   1.894   13.512  1.00 23.13 ? 201 MTA A C2    1 
HETATM 5164 N N3    . MTA E 2 .   ? 8.486   0.611   13.232  1.00 24.01 ? 201 MTA A N3    1 
HETATM 5165 C C4    . MTA E 2 .   ? 7.863   0.308   12.062  1.00 30.62 ? 201 MTA A C4    1 
HETATM 5166 C CS    . MTA F 2 .   ? -11.638 -8.015  11.384  1.00 41.67 ? 201 MTA B CS    1 
HETATM 5167 S "S5'" . MTA F 2 .   ? -10.195 -7.580  12.408  1.00 45.08 ? 201 MTA B "S5'" 1 
HETATM 5168 C "C5'" . MTA F 2 .   ? -8.864  -6.998  11.309  1.00 32.27 ? 201 MTA B "C5'" 1 
HETATM 5169 C "C4'" . MTA F 2 .   ? -8.595  -8.037  10.183  1.00 35.03 ? 201 MTA B "C4'" 1 
HETATM 5170 O "O4'" . MTA F 2 .   ? -7.645  -7.581  9.397   1.00 29.07 ? 201 MTA B "O4'" 1 
HETATM 5171 C "C2'" . MTA F 2 .   ? -6.535  -9.286  10.534  1.00 32.59 ? 201 MTA B "C2'" 1 
HETATM 5172 O "O2'" . MTA F 2 .   ? -6.008  -10.678 10.445  1.00 27.25 ? 201 MTA B "O2'" 1 
HETATM 5173 C "C3'" . MTA F 2 .   ? -8.048  -9.360  10.786  1.00 34.64 ? 201 MTA B "C3'" 1 
HETATM 5174 O "O3'" . MTA F 2 .   ? -8.552  -10.454 10.151  1.00 31.92 ? 201 MTA B "O3'" 1 
HETATM 5175 C "C1'" . MTA F 2 .   ? -6.484  -8.705  9.358   1.00 30.46 ? 201 MTA B "C1'" 1 
HETATM 5176 N N9    . MTA F 2 .   ? -5.266  -7.991  9.098   1.00 32.73 ? 201 MTA B N9    1 
HETATM 5177 C C8    . MTA F 2 .   ? -4.458  -7.393  9.993   1.00 32.91 ? 201 MTA B C8    1 
HETATM 5178 N N7    . MTA F 2 .   ? -3.453  -6.804  9.314   1.00 30.68 ? 201 MTA B N7    1 
HETATM 5179 C C5    . MTA F 2 .   ? -3.651  -7.031  8.001   1.00 32.86 ? 201 MTA B C5    1 
HETATM 5180 C C6    . MTA F 2 .   ? -2.950  -6.671  6.864   1.00 32.88 ? 201 MTA B C6    1 
HETATM 5181 N N6    . MTA F 2 .   ? -1.725  -5.920  6.647   1.00 31.45 ? 201 MTA B N6    1 
HETATM 5182 N N1    . MTA F 2 .   ? -3.393  -7.057  5.671   1.00 30.57 ? 201 MTA B N1    1 
HETATM 5183 C C2    . MTA F 2 .   ? -4.532  -7.790  5.545   1.00 24.22 ? 201 MTA B C2    1 
HETATM 5184 N N3    . MTA F 2 .   ? -5.221  -8.145  6.653   1.00 27.64 ? 201 MTA B N3    1 
HETATM 5185 C C4    . MTA F 2 .   ? -4.779  -7.757  7.870   1.00 33.71 ? 201 MTA B C4    1 
HETATM 5186 C CS    . MTA G 2 .   ? 27.636  -19.268 -30.498 1.00 51.55 ? 201 MTA C CS    1 
HETATM 5187 S "S5'" . MTA G 2 .   ? 29.083  -18.754 -31.478 1.00 59.38 ? 201 MTA C "S5'" 1 
HETATM 5188 C "C5'" . MTA G 2 .   ? 29.906  -17.349 -30.656 1.00 39.40 ? 201 MTA C "C5'" 1 
HETATM 5189 C "C4'" . MTA G 2 .   ? 28.943  -16.130 -30.612 1.00 44.14 ? 201 MTA C "C4'" 1 
HETATM 5190 O "O4'" . MTA G 2 .   ? 29.431  -15.170 -29.868 1.00 40.13 ? 201 MTA C "O4'" 1 
HETATM 5191 C "C2'" . MTA G 2 .   ? 29.501  -14.180 -31.987 1.00 41.96 ? 201 MTA C "C2'" 1 
HETATM 5192 O "O2'" . MTA G 2 .   ? 28.820  -13.202 -32.889 1.00 38.13 ? 201 MTA C "O2'" 1 
HETATM 5193 C "C3'" . MTA G 2 .   ? 28.741  -15.521 -32.020 1.00 42.71 ? 201 MTA C "C3'" 1 
HETATM 5194 O "O3'" . MTA G 2 .   ? 27.406  -15.342 -32.221 1.00 43.75 ? 201 MTA C "O3'" 1 
HETATM 5195 C "C1'" . MTA G 2 .   ? 29.421  -13.803 -30.727 1.00 41.43 ? 201 MTA C "C1'" 1 
HETATM 5196 N N9    . MTA G 2 .   ? 30.559  -13.047 -30.239 1.00 40.06 ? 201 MTA C N9    1 
HETATM 5197 C C8    . MTA G 2 .   ? 31.840  -13.263 -30.578 1.00 39.65 ? 201 MTA C C8    1 
HETATM 5198 N N7    . MTA G 2 .   ? 32.601  -12.391 -29.903 1.00 39.56 ? 201 MTA C N7    1 
HETATM 5199 C C5    . MTA G 2 .   ? 31.792  -11.647 -29.133 1.00 37.44 ? 201 MTA C C5    1 
HETATM 5200 C C6    . MTA G 2 .   ? 32.051  -10.622 -28.242 1.00 38.34 ? 201 MTA C C6    1 
HETATM 5201 N N6    . MTA G 2 .   ? 33.292  -9.983  -27.829 1.00 36.74 ? 201 MTA C N6    1 
HETATM 5202 N N1    . MTA G 2 .   ? 31.043  -10.037 -27.588 1.00 37.45 ? 201 MTA C N1    1 
HETATM 5203 C C2    . MTA G 2 .   ? 29.765  -10.454 -27.796 1.00 34.54 ? 201 MTA C C2    1 
HETATM 5204 N N3    . MTA G 2 .   ? 29.516  -11.466 -28.668 1.00 34.65 ? 201 MTA C N3    1 
HETATM 5205 C C4    . MTA G 2 .   ? 30.531  -12.056 -29.334 1.00 33.24 ? 201 MTA C C4    1 
HETATM 5206 C CS    . MTA H 2 .   ? -14.395 -0.052  -34.380 1.00 40.93 ? 201 MTA D CS    1 
HETATM 5207 S "S5'" . MTA H 2 .   ? -13.111 -1.326  -34.141 1.00 48.29 ? 201 MTA D "S5'" 1 
HETATM 5208 C "C5'" . MTA H 2 .   ? -11.454 -0.587  -34.016 1.00 40.95 ? 201 MTA D "C5'" 1 
HETATM 5209 C "C4'" . MTA H 2 .   ? -11.277 0.492   -35.127 1.00 41.97 ? 201 MTA D "C4'" 1 
HETATM 5210 O "O4'" . MTA H 2 .   ? -10.261 1.274   -34.867 1.00 38.76 ? 201 MTA D "O4'" 1 
HETATM 5211 C "C2'" . MTA H 2 .   ? -9.472  0.092   -36.702 1.00 40.64 ? 201 MTA D "C2'" 1 
HETATM 5212 O "O2'" . MTA H 2 .   ? -9.198  0.202   -38.158 1.00 38.29 ? 201 MTA D "O2'" 1 
HETATM 5213 C "C3'" . MTA H 2 .   ? -10.973 -0.160  -36.496 1.00 41.12 ? 201 MTA D "C3'" 1 
HETATM 5214 O "O3'" . MTA H 2 .   ? -11.718 0.472   -37.443 1.00 40.67 ? 201 MTA D "O3'" 1 
HETATM 5215 C "C1'" . MTA H 2 .   ? -9.284  1.262   -36.145 1.00 39.99 ? 201 MTA D "C1'" 1 
HETATM 5216 N N9    . MTA H 2 .   ? -7.930  1.452   -35.684 1.00 40.89 ? 201 MTA D N9    1 
HETATM 5217 C C8    . MTA H 2 .   ? -7.107  0.494   -35.236 1.00 37.48 ? 201 MTA D C8    1 
HETATM 5218 N N7    . MTA H 2 .   ? -5.951  1.078   -34.900 1.00 38.19 ? 201 MTA D N7    1 
HETATM 5219 C C5    . MTA H 2 .   ? -6.057  2.392   -35.137 1.00 39.08 ? 201 MTA D C5    1 
HETATM 5220 C C6    . MTA H 2 .   ? -5.180  3.442   -34.973 1.00 39.78 ? 201 MTA D C6    1 
HETATM 5221 N N6    . MTA H 2 .   ? -3.821  3.513   -34.482 1.00 38.11 ? 201 MTA D N6    1 
HETATM 5222 N N1    . MTA H 2 .   ? -5.548  4.674   -35.295 1.00 38.85 ? 201 MTA D N1    1 
HETATM 5223 C C2    . MTA H 2 .   ? -6.789  4.908   -35.784 1.00 37.52 ? 201 MTA D C2    1 
HETATM 5224 N N3    . MTA H 2 .   ? -7.652  3.883   -35.948 1.00 37.85 ? 201 MTA D N3    1 
HETATM 5225 C C4    . MTA H 2 .   ? -7.281  2.626   -35.618 1.00 41.68 ? 201 MTA D C4    1 
HETATM 5226 O O     . HOH I 3 .   ? 35.027  -4.358  22.794  1.00 44.88 ? 301 HOH A O     1 
HETATM 5227 O O     . HOH I 3 .   ? 30.989  8.695   3.953   1.00 34.39 ? 302 HOH A O     1 
HETATM 5228 O O     . HOH I 3 .   ? 12.899  -13.210 19.374  1.00 30.98 ? 303 HOH A O     1 
HETATM 5229 O O     . HOH I 3 .   ? 16.041  -4.301  -3.335  1.00 33.83 ? 304 HOH A O     1 
HETATM 5230 O O     . HOH I 3 .   ? 18.642  13.372  12.692  1.00 31.55 ? 305 HOH A O     1 
HETATM 5231 O O     . HOH I 3 .   ? 15.384  16.876  7.870   1.00 40.29 ? 306 HOH A O     1 
HETATM 5232 O O     . HOH I 3 .   ? 6.402   -14.104 3.178   1.00 42.61 ? 307 HOH A O     1 
HETATM 5233 O O     . HOH I 3 .   ? 18.097  9.275   22.139  1.00 40.19 ? 308 HOH A O     1 
HETATM 5234 O O     . HOH I 3 .   ? 5.633   7.648   9.273   1.00 33.40 ? 309 HOH A O     1 
HETATM 5235 O O     . HOH I 3 .   ? 9.432   -11.064 19.876  1.00 35.51 ? 310 HOH A O     1 
HETATM 5236 O O     . HOH I 3 .   ? 21.101  2.544   23.184  1.00 30.37 ? 311 HOH A O     1 
HETATM 5237 O O     . HOH I 3 .   ? 14.438  -7.879  15.082  1.00 31.22 ? 312 HOH A O     1 
HETATM 5238 O O     . HOH I 3 .   ? 31.468  -1.247  22.145  1.00 41.00 ? 313 HOH A O     1 
HETATM 5239 O O     . HOH I 3 .   ? 5.615   -17.096 2.225   1.00 41.67 ? 314 HOH A O     1 
HETATM 5240 O O     . HOH I 3 .   ? 32.645  4.453   4.655   1.00 37.75 ? 315 HOH A O     1 
HETATM 5241 O O     . HOH I 3 .   ? 13.086  -8.556  9.901   1.00 38.85 ? 316 HOH A O     1 
HETATM 5242 O O     . HOH I 3 .   ? 10.130  -10.189 12.877  1.00 35.24 ? 317 HOH A O     1 
HETATM 5243 O O     . HOH I 3 .   ? 18.641  9.786   -8.790  1.00 43.25 ? 318 HOH A O     1 
HETATM 5244 O O     . HOH I 3 .   ? 29.771  -0.793  19.229  1.00 30.12 ? 319 HOH A O     1 
HETATM 5245 O O     . HOH I 3 .   ? 27.455  16.956  -1.239  1.00 47.49 ? 320 HOH A O     1 
HETATM 5246 O O     . HOH I 3 .   ? 31.375  12.005  -1.785  1.00 46.05 ? 321 HOH A O     1 
HETATM 5247 O O     . HOH I 3 .   ? 12.214  -10.828 5.225   1.00 30.95 ? 322 HOH A O     1 
HETATM 5248 O O     . HOH I 3 .   ? 14.708  -4.655  30.829  1.00 45.00 ? 323 HOH A O     1 
HETATM 5249 O O     . HOH I 3 .   ? 9.861   -11.980 4.932   1.00 35.82 ? 324 HOH A O     1 
HETATM 5250 O O     . HOH I 3 .   ? 19.402  17.996  5.244   1.00 35.91 ? 325 HOH A O     1 
HETATM 5251 O O     . HOH I 3 .   ? 16.454  15.278  5.788   1.00 36.56 ? 326 HOH A O     1 
HETATM 5252 O O     . HOH I 3 .   ? 32.538  1.999   14.275  1.00 29.12 ? 327 HOH A O     1 
HETATM 5253 O O     . HOH I 3 .   ? 25.078  -9.048  23.966  1.00 32.76 ? 328 HOH A O     1 
HETATM 5254 O O     . HOH I 3 .   ? 5.640   10.648  15.771  1.00 38.85 ? 329 HOH A O     1 
HETATM 5255 O O     . HOH I 3 .   ? 19.761  2.087   27.375  1.00 39.52 ? 330 HOH A O     1 
HETATM 5256 O O     . HOH I 3 .   ? -3.087  -16.643 -1.365  1.00 28.83 ? 331 HOH A O     1 
HETATM 5257 O O     . HOH I 3 .   ? 26.574  -10.733 12.482  1.00 26.78 ? 332 HOH A O     1 
HETATM 5258 O O     . HOH I 3 .   ? 21.480  20.245  19.020  1.00 38.47 ? 333 HOH A O     1 
HETATM 5259 O O     . HOH I 3 .   ? 34.107  8.195   11.115  1.00 21.66 ? 334 HOH A O     1 
HETATM 5260 O O     . HOH I 3 .   ? 3.632   -1.258  11.924  1.00 35.23 ? 335 HOH A O     1 
HETATM 5261 O O     . HOH I 3 .   ? 17.661  -0.364  28.819  1.00 39.60 ? 336 HOH A O     1 
HETATM 5262 O O     . HOH I 3 .   ? 12.069  -3.028  3.101   1.00 32.56 ? 337 HOH A O     1 
HETATM 5263 O O     . HOH I 3 .   ? 31.134  -2.019  8.928   1.00 32.17 ? 338 HOH A O     1 
HETATM 5264 O O     . HOH I 3 .   ? 21.171  -14.629 12.978  1.00 33.28 ? 339 HOH A O     1 
HETATM 5265 O O     . HOH I 3 .   ? 15.987  14.014  13.224  1.00 40.21 ? 340 HOH A O     1 
HETATM 5266 O O     . HOH I 3 .   ? 21.393  13.543  20.993  1.00 29.65 ? 341 HOH A O     1 
HETATM 5267 O O     . HOH I 3 .   ? 9.372   -13.223 21.541  1.00 31.78 ? 342 HOH A O     1 
HETATM 5268 O O     . HOH I 3 .   ? 22.119  -15.949 -1.561  1.00 29.17 ? 343 HOH A O     1 
HETATM 5269 O O     . HOH I 3 .   ? 16.023  -13.521 24.856  1.00 33.70 ? 344 HOH A O     1 
HETATM 5270 O O     . HOH I 3 .   ? 15.688  13.096  -7.603  1.00 35.91 ? 345 HOH A O     1 
HETATM 5271 O O     . HOH I 3 .   ? 19.430  0.524   -7.131  1.00 32.52 ? 346 HOH A O     1 
HETATM 5272 O O     . HOH I 3 .   ? 11.688  14.064  13.769  1.00 34.31 ? 347 HOH A O     1 
HETATM 5273 O O     . HOH I 3 .   ? 11.400  18.915  5.267   1.00 42.28 ? 348 HOH A O     1 
HETATM 5274 O O     . HOH I 3 .   ? 12.336  11.544  8.799   1.00 27.79 ? 349 HOH A O     1 
HETATM 5275 O O     . HOH I 3 .   ? 19.166  5.871   22.443  1.00 33.73 ? 350 HOH A O     1 
HETATM 5276 O O     . HOH I 3 .   ? 10.135  -11.786 30.682  1.00 40.49 ? 351 HOH A O     1 
HETATM 5277 O O     . HOH I 3 .   ? 3.307   -0.404  26.364  1.00 41.01 ? 352 HOH A O     1 
HETATM 5278 O O     . HOH I 3 .   ? 1.346   7.445   13.274  1.00 30.08 ? 353 HOH A O     1 
HETATM 5279 O O     . HOH I 3 .   ? 17.931  14.758  22.993  1.00 38.06 ? 354 HOH A O     1 
HETATM 5280 O O     . HOH I 3 .   ? 31.546  6.241   2.185   1.00 40.40 ? 355 HOH A O     1 
HETATM 5281 O O     . HOH I 3 .   ? 17.126  16.875  15.819  1.00 35.35 ? 356 HOH A O     1 
HETATM 5282 O O     . HOH I 3 .   ? 13.911  -4.534  27.146  1.00 26.22 ? 357 HOH A O     1 
HETATM 5283 O O     . HOH I 3 .   ? 10.917  11.039  6.460   1.00 27.22 ? 358 HOH A O     1 
HETATM 5284 O O     . HOH I 3 .   ? 27.436  9.970   8.667   1.00 21.06 ? 359 HOH A O     1 
HETATM 5285 O O     . HOH I 3 .   ? 22.282  16.796  13.605  1.00 34.61 ? 360 HOH A O     1 
HETATM 5286 O O     . HOH I 3 .   ? 8.602   3.735   24.231  1.00 31.40 ? 361 HOH A O     1 
HETATM 5287 O O     . HOH I 3 .   ? 27.201  7.449   -5.199  1.00 39.71 ? 362 HOH A O     1 
HETATM 5288 O O     . HOH I 3 .   ? 28.067  7.980   6.967   1.00 19.99 ? 363 HOH A O     1 
HETATM 5289 O O     . HOH I 3 .   ? 1.541   2.214   2.551   1.00 20.97 ? 364 HOH A O     1 
HETATM 5290 O O     . HOH I 3 .   ? 15.845  3.326   -6.508  1.00 31.70 ? 365 HOH A O     1 
HETATM 5291 O O     . HOH I 3 .   ? 31.544  -8.544  10.976  1.00 42.23 ? 366 HOH A O     1 
HETATM 5292 O O     . HOH I 3 .   ? -1.171  -25.105 1.892   1.00 46.02 ? 367 HOH A O     1 
HETATM 5293 O O     . HOH I 3 .   ? 3.725   1.864   24.740  1.00 37.64 ? 368 HOH A O     1 
HETATM 5294 O O     . HOH I 3 .   ? 15.336  -4.604  12.316  1.00 30.89 ? 369 HOH A O     1 
HETATM 5295 O O     . HOH I 3 .   ? 27.391  -7.070  -3.681  1.00 36.56 ? 370 HOH A O     1 
HETATM 5296 O O     . HOH I 3 .   ? 25.608  2.377   -6.461  1.00 39.96 ? 371 HOH A O     1 
HETATM 5297 O O     . HOH I 3 .   ? 20.558  10.433  18.228  1.00 41.91 ? 372 HOH A O     1 
HETATM 5298 O O     . HOH I 3 .   ? 18.475  15.294  -7.388  1.00 43.14 ? 373 HOH A O     1 
HETATM 5299 O O     . HOH I 3 .   ? 5.632   -5.819  28.316  1.00 35.94 ? 374 HOH A O     1 
HETATM 5300 O O     . HOH I 3 .   ? 14.015  16.501  22.312  1.00 42.09 ? 375 HOH A O     1 
HETATM 5301 O O     . HOH I 3 .   ? 33.053  -6.307  13.171  1.00 39.02 ? 376 HOH A O     1 
HETATM 5302 O O     . HOH I 3 .   ? 1.976   -8.225  23.013  1.00 40.80 ? 377 HOH A O     1 
HETATM 5303 O O     . HOH I 3 .   ? 22.647  16.572  4.996   1.00 32.83 ? 378 HOH A O     1 
HETATM 5304 O O     . HOH I 3 .   ? 18.874  -14.248 14.607  1.00 33.14 ? 379 HOH A O     1 
HETATM 5305 O O     . HOH I 3 .   ? 12.431  -11.044 -3.514  1.00 34.57 ? 380 HOH A O     1 
HETATM 5306 O O     . HOH I 3 .   ? 13.424  -18.310 -1.023  1.00 32.77 ? 381 HOH A O     1 
HETATM 5307 O O     . HOH I 3 .   ? 24.745  17.506  24.376  1.00 43.77 ? 382 HOH A O     1 
HETATM 5308 O O     . HOH I 3 .   ? 23.028  8.148   -3.919  1.00 23.76 ? 383 HOH A O     1 
HETATM 5309 O O     . HOH I 3 .   ? 27.375  12.733  11.424  1.00 23.77 ? 384 HOH A O     1 
HETATM 5310 O O     . HOH I 3 .   ? 26.118  13.327  8.355   1.00 25.20 ? 385 HOH A O     1 
HETATM 5311 O O     . HOH I 3 .   ? 20.646  -17.962 1.030   1.00 33.45 ? 386 HOH A O     1 
HETATM 5312 O O     . HOH I 3 .   ? 7.769   -9.197  19.452  1.00 29.72 ? 387 HOH A O     1 
HETATM 5313 O O     . HOH I 3 .   ? 6.939   7.203   -3.828  1.00 35.75 ? 388 HOH A O     1 
HETATM 5314 O O     . HOH I 3 .   ? 30.598  1.873   6.645   1.00 36.95 ? 389 HOH A O     1 
HETATM 5315 O O     . HOH I 3 .   ? 21.676  -13.230 20.912  1.00 28.42 ? 390 HOH A O     1 
HETATM 5316 O O     . HOH I 3 .   ? 15.263  1.414   28.336  1.00 42.12 ? 391 HOH A O     1 
HETATM 5317 O O     . HOH I 3 .   ? 8.594   12.803  10.456  1.00 44.77 ? 392 HOH A O     1 
HETATM 5318 O O     . HOH I 3 .   ? 20.298  -6.182  -7.743  1.00 41.52 ? 393 HOH A O     1 
HETATM 5319 O O     . HOH I 3 .   ? 10.986  -4.633  5.546   1.00 33.61 ? 394 HOH A O     1 
HETATM 5320 O O     . HOH I 3 .   ? 25.186  -12.082 14.569  1.00 26.61 ? 395 HOH A O     1 
HETATM 5321 O O     . HOH I 3 .   ? 8.465   15.376  16.552  1.00 42.42 ? 396 HOH A O     1 
HETATM 5322 O O     . HOH I 3 .   ? 6.493   8.354   17.376  1.00 31.63 ? 397 HOH A O     1 
HETATM 5323 O O     . HOH I 3 .   ? 12.526  -15.233 5.599   1.00 32.45 ? 398 HOH A O     1 
HETATM 5324 O O     . HOH I 3 .   ? 32.047  -8.042  21.207  1.00 45.85 ? 399 HOH A O     1 
HETATM 5325 O O     . HOH I 3 .   ? 23.347  14.889  -7.139  1.00 37.54 ? 400 HOH A O     1 
HETATM 5326 O O     . HOH I 3 .   ? 19.171  5.121   -8.037  1.00 26.48 ? 401 HOH A O     1 
HETATM 5327 O O     . HOH I 3 .   ? 32.909  2.237   8.179   1.00 40.24 ? 402 HOH A O     1 
HETATM 5328 O O     . HOH I 3 .   ? 18.557  -9.390  26.445  1.00 42.09 ? 403 HOH A O     1 
HETATM 5329 O O     . HOH I 3 .   ? 26.837  -11.775 -2.840  1.00 41.77 ? 404 HOH A O     1 
HETATM 5330 O O     . HOH I 3 .   ? 12.929  0.095   26.873  1.00 36.03 ? 405 HOH A O     1 
HETATM 5331 O O     . HOH I 3 .   ? 23.740  6.653   23.845  1.00 47.27 ? 406 HOH A O     1 
HETATM 5332 O O     . HOH I 3 .   ? 0.344   -6.424  24.198  1.00 45.23 ? 407 HOH A O     1 
HETATM 5333 O O     . HOH I 3 .   ? 11.553  -10.053 10.657  1.00 41.33 ? 408 HOH A O     1 
HETATM 5334 O O     . HOH I 3 .   ? 25.076  6.152   -5.008  1.00 32.52 ? 409 HOH A O     1 
HETATM 5335 O O     . HOH I 3 .   ? 4.201   0.318   7.632   1.00 28.87 ? 410 HOH A O     1 
HETATM 5336 O O     . HOH I 3 .   ? 13.384  12.554  11.968  1.00 39.39 ? 411 HOH A O     1 
HETATM 5337 O O     . HOH I 3 .   ? 18.649  16.540  13.309  1.00 45.64 ? 412 HOH A O     1 
HETATM 5338 O O     . HOH I 3 .   ? 4.465   9.762   13.512  1.00 44.99 ? 413 HOH A O     1 
HETATM 5339 O O     . HOH I 3 .   ? 7.510   10.897  -2.783  1.00 35.46 ? 414 HOH A O     1 
HETATM 5340 O O     . HOH I 3 .   ? 18.879  12.301  20.301  1.00 34.37 ? 415 HOH A O     1 
HETATM 5341 O O     . HOH I 3 .   ? -5.580  -25.106 0.538   1.00 44.37 ? 416 HOH A O     1 
HETATM 5342 O O     . HOH I 3 .   ? 28.230  -2.583  23.477  1.00 37.78 ? 417 HOH A O     1 
HETATM 5343 O O     . HOH I 3 .   ? 16.590  -14.663 21.879  1.00 33.03 ? 418 HOH A O     1 
HETATM 5344 O O     . HOH I 3 .   ? 11.169  -4.010  -0.959  1.00 33.98 ? 419 HOH A O     1 
HETATM 5345 O O     . HOH I 3 .   ? 27.976  3.262   24.864  1.00 40.99 ? 420 HOH A O     1 
HETATM 5346 O O     . HOH I 3 .   ? 34.172  0.617   12.374  1.00 38.25 ? 421 HOH A O     1 
HETATM 5347 O O     . HOH I 3 .   ? 9.788   -2.568  1.562   1.00 39.86 ? 422 HOH A O     1 
HETATM 5348 O O     . HOH I 3 .   ? 32.453  -4.642  11.124  1.00 40.96 ? 423 HOH A O     1 
HETATM 5349 O O     . HOH I 3 .   ? 13.197  -7.291  12.074  1.00 37.87 ? 424 HOH A O     1 
HETATM 5350 O O     . HOH I 3 .   ? 0.364   2.170   18.430  1.00 47.97 ? 425 HOH A O     1 
HETATM 5351 O O     . HOH I 3 .   ? 20.034  19.514  16.091  1.00 46.64 ? 426 HOH A O     1 
HETATM 5352 O O     . HOH I 3 .   ? 0.273   0.031   17.691  1.00 36.16 ? 427 HOH A O     1 
HETATM 5353 O O     . HOH I 3 .   ? 15.427  -8.946  -6.836  1.00 43.78 ? 428 HOH A O     1 
HETATM 5354 O O     . HOH I 3 .   ? 3.196   3.896   18.166  1.00 37.30 ? 429 HOH A O     1 
HETATM 5355 O O     . HOH I 3 .   ? -0.462  -3.076  18.300  1.00 38.33 ? 430 HOH A O     1 
HETATM 5356 O O     . HOH I 3 .   ? 30.353  -11.796 16.564  1.00 43.32 ? 431 HOH A O     1 
HETATM 5357 O O     . HOH I 3 .   ? 35.391  8.726   7.144   1.00 36.04 ? 432 HOH A O     1 
HETATM 5358 O O     . HOH I 3 .   ? 6.238   15.268  16.816  1.00 46.32 ? 433 HOH A O     1 
HETATM 5359 O O     . HOH I 3 .   ? -0.101  -15.634 9.250   1.00 45.39 ? 434 HOH A O     1 
HETATM 5360 O O     . HOH I 3 .   ? 8.078   7.623   21.513  1.00 42.54 ? 435 HOH A O     1 
HETATM 5361 O O     . HOH I 3 .   ? 8.864   14.432  8.270   1.00 38.69 ? 436 HOH A O     1 
HETATM 5362 O O     . HOH I 3 .   ? 6.652   12.022  2.075   1.00 36.83 ? 437 HOH A O     1 
HETATM 5363 O O     . HOH I 3 .   ? 6.401   10.934  10.329  1.00 48.56 ? 438 HOH A O     1 
HETATM 5364 O O     . HOH I 3 .   ? 32.047  -10.231 17.239  1.00 44.32 ? 439 HOH A O     1 
HETATM 5365 O O     . HOH I 3 .   ? 28.893  -0.465  22.887  1.00 38.38 ? 440 HOH A O     1 
HETATM 5366 O O     . HOH I 3 .   ? 27.551  -13.156 15.615  1.00 35.41 ? 441 HOH A O     1 
HETATM 5367 O O     . HOH I 3 .   ? 21.442  -14.720 16.254  1.00 40.92 ? 442 HOH A O     1 
HETATM 5368 O O     . HOH I 3 .   ? 33.967  -2.074  10.693  1.00 45.58 ? 443 HOH A O     1 
HETATM 5369 O O     . HOH I 3 .   ? 5.555   3.394   25.800  1.00 45.00 ? 444 HOH A O     1 
HETATM 5370 O O     . HOH I 3 .   ? 22.704  -16.391 1.289   1.00 41.89 ? 445 HOH A O     1 
HETATM 5371 O O     . HOH I 3 .   ? 22.114  4.334   24.472  1.00 41.43 ? 446 HOH A O     1 
HETATM 5372 O O     . HOH I 3 .   ? -3.210  -27.216 1.469   1.00 43.93 ? 447 HOH A O     1 
HETATM 5373 O O     . HOH I 3 .   ? 6.591   8.582   19.850  1.00 41.76 ? 448 HOH A O     1 
HETATM 5374 O O     . HOH I 3 .   ? 17.682  2.530   -8.049  1.00 40.40 ? 449 HOH A O     1 
HETATM 5375 O O     . HOH I 3 .   ? 7.279   5.378   -5.440  1.00 45.39 ? 450 HOH A O     1 
HETATM 5376 O O     . HOH I 3 .   ? 3.956   -1.920  9.239   1.00 36.60 ? 451 HOH A O     1 
HETATM 5377 O O     . HOH I 3 .   ? 7.244   -3.953  1.532   1.00 44.21 ? 452 HOH A O     1 
HETATM 5378 O O     . HOH I 3 .   ? 3.593   6.766   17.494  1.00 44.62 ? 453 HOH A O     1 
HETATM 5379 O O     . HOH I 3 .   ? 36.678  -2.378  23.566  1.00 46.15 ? 454 HOH A O     1 
HETATM 5380 O O     . HOH I 3 .   ? 18.852  6.790   -9.994  1.00 43.10 ? 455 HOH A O     1 
HETATM 5381 O O     . HOH I 3 .   ? 23.560  -14.072 14.239  1.00 31.52 ? 456 HOH A O     1 
HETATM 5382 O O     . HOH I 3 .   ? 23.074  15.301  25.758  1.00 46.74 ? 457 HOH A O     1 
HETATM 5383 O O     . HOH I 3 .   ? 24.247  4.826   -7.086  1.00 37.53 ? 458 HOH A O     1 
HETATM 5384 O O     . HOH I 3 .   ? 35.797  5.833   7.008   1.00 44.87 ? 459 HOH A O     1 
HETATM 5385 O O     . HOH I 3 .   ? 6.915   8.273   7.232   1.00 35.11 ? 460 HOH A O     1 
HETATM 5386 O O     . HOH I 3 .   ? 28.304  16.496  -5.025  1.00 44.51 ? 461 HOH A O     1 
HETATM 5387 O O     . HOH I 3 .   ? 13.669  4.174   -7.672  1.00 32.78 ? 462 HOH A O     1 
HETATM 5388 O O     . HOH I 3 .   ? 8.616   12.672  6.189   1.00 32.82 ? 463 HOH A O     1 
HETATM 5389 O O     . HOH I 3 .   ? 21.792  3.906   -8.040  1.00 39.69 ? 464 HOH A O     1 
HETATM 5390 O O     . HOH I 3 .   ? 6.676   10.985  6.702   1.00 38.47 ? 465 HOH A O     1 
HETATM 5391 O O     . HOH J 3 .   ? -3.380  -3.361  -8.222  1.00 38.67 ? 301 HOH B O     1 
HETATM 5392 O O     . HOH J 3 .   ? 1.107   6.276   -3.718  1.00 39.11 ? 302 HOH B O     1 
HETATM 5393 O O     . HOH J 3 .   ? -12.903 16.404  -6.044  1.00 44.48 ? 303 HOH B O     1 
HETATM 5394 O O     . HOH J 3 .   ? 4.271   -6.847  3.770   1.00 46.53 ? 304 HOH B O     1 
HETATM 5395 O O     . HOH J 3 .   ? -15.913 -6.096  17.029  1.00 42.75 ? 305 HOH B O     1 
HETATM 5396 O O     . HOH J 3 .   ? -14.569 -6.774  10.798  1.00 35.98 ? 306 HOH B O     1 
HETATM 5397 O O     . HOH J 3 .   ? -15.148 2.692   19.779  1.00 26.65 ? 307 HOH B O     1 
HETATM 5398 O O     . HOH J 3 .   ? -15.652 -4.532  14.897  1.00 28.08 ? 308 HOH B O     1 
HETATM 5399 O O     . HOH J 3 .   ? -13.272 -6.975  6.003   1.00 30.57 ? 309 HOH B O     1 
HETATM 5400 O O     . HOH J 3 .   ? -15.432 -10.152 6.904   1.00 33.18 ? 310 HOH B O     1 
HETATM 5401 O O     . HOH J 3 .   ? 4.601   -8.169  1.453   1.00 38.43 ? 311 HOH B O     1 
HETATM 5402 O O     . HOH J 3 .   ? -23.639 -13.326 -3.806  1.00 31.36 ? 312 HOH B O     1 
HETATM 5403 O O     . HOH J 3 .   ? -18.883 -16.020 8.085   1.00 34.56 ? 313 HOH B O     1 
HETATM 5404 O O     . HOH J 3 .   ? -14.065 17.050  1.399   1.00 39.78 ? 314 HOH B O     1 
HETATM 5405 O O     . HOH J 3 .   ? -29.444 -10.779 -0.091  1.00 43.69 ? 315 HOH B O     1 
HETATM 5406 O O     . HOH J 3 .   ? -24.164 -13.752 2.132   1.00 27.03 ? 316 HOH B O     1 
HETATM 5407 O O     . HOH J 3 .   ? -12.352 6.726   14.321  1.00 32.79 ? 317 HOH B O     1 
HETATM 5408 O O     . HOH J 3 .   ? -20.282 1.710   -9.347  1.00 30.30 ? 318 HOH B O     1 
HETATM 5409 O O     . HOH J 3 .   ? -19.815 -10.227 17.132  1.00 42.28 ? 319 HOH B O     1 
HETATM 5410 O O     . HOH J 3 .   ? -5.929  -15.626 -5.517  1.00 45.73 ? 320 HOH B O     1 
HETATM 5411 O O     . HOH J 3 .   ? -22.230 11.560  10.246  1.00 42.35 ? 321 HOH B O     1 
HETATM 5412 O O     . HOH J 3 .   ? -14.648 12.084  -5.813  1.00 30.05 ? 322 HOH B O     1 
HETATM 5413 O O     . HOH J 3 .   ? 3.279   -3.779  6.019   1.00 37.61 ? 323 HOH B O     1 
HETATM 5414 O O     . HOH J 3 .   ? -8.760  15.101  3.059   1.00 22.09 ? 324 HOH B O     1 
HETATM 5415 O O     . HOH J 3 .   ? -12.059 -23.521 -1.281  1.00 27.12 ? 325 HOH B O     1 
HETATM 5416 O O     . HOH J 3 .   ? -8.829  -24.625 4.241   1.00 35.62 ? 326 HOH B O     1 
HETATM 5417 O O     . HOH J 3 .   ? -22.369 3.961   -3.190  1.00 33.44 ? 327 HOH B O     1 
HETATM 5418 O O     . HOH J 3 .   ? -10.170 17.089  -0.668  1.00 36.15 ? 328 HOH B O     1 
HETATM 5419 O O     . HOH J 3 .   ? -12.016 -14.549 -9.236  1.00 39.30 ? 329 HOH B O     1 
HETATM 5420 O O     . HOH J 3 .   ? -4.350  -21.389 -1.084  1.00 42.32 ? 330 HOH B O     1 
HETATM 5421 O O     . HOH J 3 .   ? -1.225  4.099   16.423  1.00 33.40 ? 331 HOH B O     1 
HETATM 5422 O O     . HOH J 3 .   ? -20.775 -10.800 14.168  1.00 33.57 ? 332 HOH B O     1 
HETATM 5423 O O     . HOH J 3 .   ? -8.955  5.664   -10.607 1.00 25.35 ? 333 HOH B O     1 
HETATM 5424 O O     . HOH J 3 .   ? -5.426  -23.365 9.418   1.00 45.13 ? 334 HOH B O     1 
HETATM 5425 O O     . HOH J 3 .   ? 0.943   -0.303  -15.629 1.00 52.24 ? 335 HOH B O     1 
HETATM 5426 O O     . HOH J 3 .   ? -16.699 7.271   -11.809 1.00 24.75 ? 336 HOH B O     1 
HETATM 5427 O O     . HOH J 3 .   ? -12.388 -10.441 -7.847  1.00 28.93 ? 337 HOH B O     1 
HETATM 5428 O O     . HOH J 3 .   ? -10.879 6.997   -7.502  1.00 21.85 ? 338 HOH B O     1 
HETATM 5429 O O     . HOH J 3 .   ? -25.539 -6.765  2.831   1.00 23.22 ? 339 HOH B O     1 
HETATM 5430 O O     . HOH J 3 .   ? -16.976 10.813  16.090  1.00 29.00 ? 340 HOH B O     1 
HETATM 5431 O O     . HOH J 3 .   ? -13.554 -7.964  8.816   1.00 28.31 ? 341 HOH B O     1 
HETATM 5432 O O     . HOH J 3 .   ? 0.502   8.869   -5.896  1.00 46.02 ? 342 HOH B O     1 
HETATM 5433 O O     . HOH J 3 .   ? 1.844   -9.869  1.262   1.00 29.17 ? 343 HOH B O     1 
HETATM 5434 O O     . HOH J 3 .   ? -17.633 -16.135 -13.455 1.00 49.91 ? 344 HOH B O     1 
HETATM 5435 O O     . HOH J 3 .   ? -23.041 -10.359 7.685   1.00 27.06 ? 345 HOH B O     1 
HETATM 5436 O O     . HOH J 3 .   ? -13.846 15.708  -8.730  1.00 39.53 ? 346 HOH B O     1 
HETATM 5437 O O     . HOH J 3 .   ? -11.452 -21.511 -3.078  1.00 37.58 ? 347 HOH B O     1 
HETATM 5438 O O     . HOH J 3 .   ? 3.845   -1.277  -0.199  1.00 39.59 ? 348 HOH B O     1 
HETATM 5439 O O     . HOH J 3 .   ? -25.647 -4.009  2.743   1.00 22.25 ? 349 HOH B O     1 
HETATM 5440 O O     . HOH J 3 .   ? 3.598   8.566   9.847   1.00 31.74 ? 350 HOH B O     1 
HETATM 5441 O O     . HOH J 3 .   ? -16.237 13.027  -3.788  1.00 42.87 ? 351 HOH B O     1 
HETATM 5442 O O     . HOH J 3 .   ? -12.798 8.048   -5.654  1.00 19.64 ? 352 HOH B O     1 
HETATM 5443 O O     . HOH J 3 .   ? -10.011 -2.867  12.077  1.00 31.41 ? 353 HOH B O     1 
HETATM 5444 O O     . HOH J 3 .   ? -21.162 -1.867  22.513  1.00 35.25 ? 354 HOH B O     1 
HETATM 5445 O O     . HOH J 3 .   ? 2.237   9.203   2.923   1.00 27.93 ? 355 HOH B O     1 
HETATM 5446 O O     . HOH J 3 .   ? -26.974 -1.566  9.128   1.00 30.09 ? 356 HOH B O     1 
HETATM 5447 O O     . HOH J 3 .   ? -20.510 -4.809  -9.007  1.00 31.21 ? 357 HOH B O     1 
HETATM 5448 O O     . HOH J 3 .   ? -31.771 -1.023  21.628  1.00 35.81 ? 358 HOH B O     1 
HETATM 5449 O O     . HOH J 3 .   ? -26.061 3.396   3.601   1.00 38.61 ? 359 HOH B O     1 
HETATM 5450 O O     . HOH J 3 .   ? -24.767 -8.305  7.876   1.00 32.49 ? 360 HOH B O     1 
HETATM 5451 O O     . HOH J 3 .   ? -2.613  10.720  -6.181  1.00 35.77 ? 361 HOH B O     1 
HETATM 5452 O O     . HOH J 3 .   ? -8.485  -9.255  -8.241  1.00 34.13 ? 362 HOH B O     1 
HETATM 5453 O O     . HOH J 3 .   ? -9.506  2.687   15.422  1.00 30.20 ? 363 HOH B O     1 
HETATM 5454 O O     . HOH J 3 .   ? -4.286  -4.176  -12.777 1.00 42.60 ? 364 HOH B O     1 
HETATM 5455 O O     . HOH J 3 .   ? -18.144 -14.449 12.830  1.00 34.96 ? 365 HOH B O     1 
HETATM 5456 O O     . HOH J 3 .   ? -0.101  2.309   -8.604  1.00 44.39 ? 366 HOH B O     1 
HETATM 5457 O O     . HOH J 3 .   ? -19.266 -6.405  17.479  1.00 35.88 ? 367 HOH B O     1 
HETATM 5458 O O     . HOH J 3 .   ? -13.719 -11.353 12.229  1.00 40.53 ? 368 HOH B O     1 
HETATM 5459 O O     . HOH J 3 .   ? -12.082 -17.220 9.109   1.00 30.86 ? 369 HOH B O     1 
HETATM 5460 O O     . HOH J 3 .   ? -12.385 13.212  11.798  1.00 33.35 ? 370 HOH B O     1 
HETATM 5461 O O     . HOH J 3 .   ? -25.033 7.259   6.249   1.00 37.63 ? 371 HOH B O     1 
HETATM 5462 O O     . HOH J 3 .   ? -7.755  12.581  11.486  1.00 39.29 ? 372 HOH B O     1 
HETATM 5463 O O     . HOH J 3 .   ? -20.498 6.798   -6.505  1.00 37.94 ? 373 HOH B O     1 
HETATM 5464 O O     . HOH J 3 .   ? -9.346  9.710   -9.748  1.00 41.22 ? 374 HOH B O     1 
HETATM 5465 O O     . HOH J 3 .   ? -8.536  7.538   14.684  1.00 42.45 ? 375 HOH B O     1 
HETATM 5466 O O     . HOH J 3 .   ? -9.406  -0.371  12.314  1.00 30.00 ? 376 HOH B O     1 
HETATM 5467 O O     . HOH J 3 .   ? -21.367 -9.640  -9.610  1.00 33.90 ? 377 HOH B O     1 
HETATM 5468 O O     . HOH J 3 .   ? -26.093 4.043   13.766  1.00 30.92 ? 378 HOH B O     1 
HETATM 5469 O O     . HOH J 3 .   ? -12.196 -19.405 -1.736  1.00 35.55 ? 379 HOH B O     1 
HETATM 5470 O O     . HOH J 3 .   ? -7.445  7.969   -8.692  1.00 25.28 ? 380 HOH B O     1 
HETATM 5471 O O     . HOH J 3 .   ? -12.376 16.107  3.516   1.00 29.25 ? 381 HOH B O     1 
HETATM 5472 O O     . HOH J 3 .   ? -21.737 3.367   -8.250  1.00 39.88 ? 382 HOH B O     1 
HETATM 5473 O O     . HOH J 3 .   ? 1.144   0.999   0.376   1.00 27.26 ? 383 HOH B O     1 
HETATM 5474 O O     . HOH J 3 .   ? -26.230 0.842   16.963  1.00 27.20 ? 384 HOH B O     1 
HETATM 5475 O O     . HOH J 3 .   ? -17.784 14.194  7.673   1.00 34.70 ? 385 HOH B O     1 
HETATM 5476 O O     . HOH J 3 .   ? -18.534 10.750  -4.732  1.00 40.56 ? 386 HOH B O     1 
HETATM 5477 O O     . HOH J 3 .   ? -20.626 -18.039 -10.402 1.00 43.60 ? 387 HOH B O     1 
HETATM 5478 O O     . HOH J 3 .   ? -1.445  -6.122  11.455  1.00 47.23 ? 388 HOH B O     1 
HETATM 5479 O O     . HOH J 3 .   ? -9.187  -17.622 -6.512  1.00 42.88 ? 389 HOH B O     1 
HETATM 5480 O O     . HOH J 3 .   ? -7.738  15.271  9.942   1.00 40.23 ? 390 HOH B O     1 
HETATM 5481 O O     . HOH J 3 .   ? -24.212 -9.615  15.022  1.00 30.80 ? 391 HOH B O     1 
HETATM 5482 O O     . HOH J 3 .   ? -2.235  -17.596 11.166  1.00 42.31 ? 392 HOH B O     1 
HETATM 5483 O O     . HOH J 3 .   ? -25.865 -3.902  -15.560 1.00 40.48 ? 393 HOH B O     1 
HETATM 5484 O O     . HOH J 3 .   ? -18.677 -19.004 -2.269  1.00 31.12 ? 394 HOH B O     1 
HETATM 5485 O O     . HOH J 3 .   ? -9.454  5.269   15.400  1.00 37.20 ? 395 HOH B O     1 
HETATM 5486 O O     . HOH J 3 .   ? -12.523 -31.234 7.996   1.00 38.22 ? 396 HOH B O     1 
HETATM 5487 O O     . HOH J 3 .   ? -28.694 -5.520  -3.833  1.00 37.87 ? 397 HOH B O     1 
HETATM 5488 O O     . HOH J 3 .   ? -15.923 10.635  0.786   1.00 29.15 ? 398 HOH B O     1 
HETATM 5489 O O     . HOH J 3 .   ? -14.824 -8.878  11.884  1.00 39.31 ? 399 HOH B O     1 
HETATM 5490 O O     . HOH J 3 .   ? -7.844  0.801   13.933  1.00 38.08 ? 400 HOH B O     1 
HETATM 5491 O O     . HOH J 3 .   ? -9.417  8.636   16.906  1.00 35.80 ? 401 HOH B O     1 
HETATM 5492 O O     . HOH J 3 .   ? -28.198 -7.001  2.068   1.00 34.57 ? 402 HOH B O     1 
HETATM 5493 O O     . HOH J 3 .   ? -19.978 -7.545  -10.438 1.00 43.85 ? 403 HOH B O     1 
HETATM 5494 O O     . HOH J 3 .   ? 0.145   -6.455  9.514   1.00 44.39 ? 404 HOH B O     1 
HETATM 5495 O O     . HOH J 3 .   ? -27.341 -0.663  6.704   1.00 32.98 ? 405 HOH B O     1 
HETATM 5496 O O     . HOH J 3 .   ? -19.189 7.552   -8.678  1.00 33.11 ? 406 HOH B O     1 
HETATM 5497 O O     . HOH J 3 .   ? -28.365 -8.107  -7.275  1.00 46.45 ? 407 HOH B O     1 
HETATM 5498 O O     . HOH J 3 .   ? -25.191 -10.760 5.687   1.00 37.86 ? 408 HOH B O     1 
HETATM 5499 O O     . HOH J 3 .   ? -30.104 -9.306  1.650   1.00 49.58 ? 409 HOH B O     1 
HETATM 5500 O O     . HOH J 3 .   ? -16.414 12.839  -7.639  1.00 44.23 ? 410 HOH B O     1 
HETATM 5501 O O     . HOH J 3 .   ? -27.941 -2.766  2.204   1.00 35.07 ? 411 HOH B O     1 
HETATM 5502 O O     . HOH J 3 .   ? -13.390 2.069   21.776  1.00 38.09 ? 412 HOH B O     1 
HETATM 5503 O O     . HOH J 3 .   ? -28.178 0.186   15.077  1.00 39.32 ? 413 HOH B O     1 
HETATM 5504 O O     . HOH J 3 .   ? -21.303 -7.679  18.232  1.00 45.02 ? 414 HOH B O     1 
HETATM 5505 O O     . HOH J 3 .   ? -10.704 18.549  1.051   1.00 40.61 ? 415 HOH B O     1 
HETATM 5506 O O     . HOH J 3 .   ? -12.518 -11.075 14.539  1.00 44.14 ? 416 HOH B O     1 
HETATM 5507 O O     . HOH J 3 .   ? 1.440   9.575   0.204   1.00 35.41 ? 417 HOH B O     1 
HETATM 5508 O O     . HOH J 3 .   ? -24.290 10.493  11.490  1.00 30.70 ? 418 HOH B O     1 
HETATM 5509 O O     . HOH J 3 .   ? -10.107 17.314  3.672   1.00 32.65 ? 419 HOH B O     1 
HETATM 5510 O O     . HOH J 3 .   ? -28.313 -0.821  4.248   1.00 39.02 ? 420 HOH B O     1 
HETATM 5511 O O     . HOH J 3 .   ? -23.383 -15.726 -2.713  1.00 35.62 ? 421 HOH B O     1 
HETATM 5512 O O     . HOH J 3 .   ? -26.038 -8.067  5.353   1.00 28.81 ? 422 HOH B O     1 
HETATM 5513 O O     . HOH J 3 .   ? -20.635 -18.690 -1.280  1.00 43.41 ? 423 HOH B O     1 
HETATM 5514 O O     . HOH J 3 .   ? -26.793 -19.458 5.107   1.00 50.34 ? 424 HOH B O     1 
HETATM 5515 O O     . HOH J 3 .   ? -20.341 -13.290 13.930  1.00 43.63 ? 425 HOH B O     1 
HETATM 5516 O O     . HOH J 3 .   ? 4.655   11.298  3.869   1.00 48.07 ? 426 HOH B O     1 
HETATM 5517 O O     . HOH K 3 .   ? 35.788  -31.091 -29.161 1.00 40.74 ? 301 HOH C O     1 
HETATM 5518 O O     . HOH K 3 .   ? 29.714  -22.093 -29.372 1.00 43.81 ? 302 HOH C O     1 
HETATM 5519 O O     . HOH K 3 .   ? 24.806  -2.085  -11.671 1.00 47.41 ? 303 HOH C O     1 
HETATM 5520 O O     . HOH K 3 .   ? 35.515  -14.170 -28.714 1.00 41.94 ? 304 HOH C O     1 
HETATM 5521 O O     . HOH K 3 .   ? 10.238  -17.931 -20.190 1.00 35.22 ? 305 HOH C O     1 
HETATM 5522 O O     . HOH K 3 .   ? 14.465  -10.417 -13.121 1.00 39.78 ? 306 HOH C O     1 
HETATM 5523 O O     . HOH K 3 .   ? 25.810  -34.711 -16.636 1.00 25.92 ? 307 HOH C O     1 
HETATM 5524 O O     . HOH K 3 .   ? 9.589   -24.361 -19.233 1.00 41.52 ? 308 HOH C O     1 
HETATM 5525 O O     . HOH K 3 .   ? 25.038  -18.137 -25.468 1.00 38.26 ? 309 HOH C O     1 
HETATM 5526 O O     . HOH K 3 .   ? 30.428  -13.677 -7.313  1.00 21.48 ? 310 HOH C O     1 
HETATM 5527 O O     . HOH K 3 .   ? 28.211  -26.723 -32.312 1.00 45.14 ? 311 HOH C O     1 
HETATM 5528 O O     . HOH K 3 .   ? 15.510  -8.854  -9.439  1.00 44.49 ? 312 HOH C O     1 
HETATM 5529 O O     . HOH K 3 .   ? 22.576  -2.235  -33.301 1.00 44.64 ? 313 HOH C O     1 
HETATM 5530 O O     . HOH K 3 .   ? 8.128   -18.593 -15.618 1.00 51.05 ? 314 HOH C O     1 
HETATM 5531 O O     . HOH K 3 .   ? 38.401  -9.860  -7.501  1.00 37.27 ? 315 HOH C O     1 
HETATM 5532 O O     . HOH K 3 .   ? 22.781  -2.874  -16.240 1.00 52.54 ? 316 HOH C O     1 
HETATM 5533 O O     . HOH K 3 .   ? 38.615  -14.091 -4.190  1.00 45.88 ? 317 HOH C O     1 
HETATM 5534 O O     . HOH K 3 .   ? 27.739  -31.641 -13.704 1.00 29.96 ? 318 HOH C O     1 
HETATM 5535 O O     . HOH K 3 .   ? 29.427  -35.233 -16.021 1.00 34.24 ? 319 HOH C O     1 
HETATM 5536 O O     . HOH K 3 .   ? 15.941  -16.105 -11.544 1.00 35.91 ? 320 HOH C O     1 
HETATM 5537 O O     . HOH K 3 .   ? 36.462  -6.644  -19.812 1.00 35.08 ? 321 HOH C O     1 
HETATM 5538 O O     . HOH K 3 .   ? 28.295  -25.668 -30.124 1.00 37.62 ? 322 HOH C O     1 
HETATM 5539 O O     . HOH K 3 .   ? 12.189  -21.905 -24.849 1.00 32.27 ? 323 HOH C O     1 
HETATM 5540 O O     . HOH K 3 .   ? 16.952  -20.578 -31.971 1.00 45.29 ? 324 HOH C O     1 
HETATM 5541 O O     . HOH K 3 .   ? 17.685  -24.990 -26.965 1.00 31.53 ? 325 HOH C O     1 
HETATM 5542 O O     . HOH K 3 .   ? 38.901  -6.763  -12.564 1.00 43.86 ? 326 HOH C O     1 
HETATM 5543 O O     . HOH K 3 .   ? 45.447  -11.248 -10.411 1.00 32.44 ? 327 HOH C O     1 
HETATM 5544 O O     . HOH K 3 .   ? 23.049  -23.535 -9.815  1.00 36.92 ? 328 HOH C O     1 
HETATM 5545 O O     . HOH K 3 .   ? 31.937  -20.621 -28.416 1.00 42.15 ? 329 HOH C O     1 
HETATM 5546 O O     . HOH K 3 .   ? 31.919  -5.789  -13.008 1.00 33.42 ? 330 HOH C O     1 
HETATM 5547 O O     . HOH K 3 .   ? 39.425  -7.311  -8.647  1.00 43.04 ? 331 HOH C O     1 
HETATM 5548 O O     . HOH K 3 .   ? 41.250  -21.012 -10.843 1.00 22.33 ? 332 HOH C O     1 
HETATM 5549 O O     . HOH K 3 .   ? 44.092  -18.844 -26.557 1.00 48.32 ? 333 HOH C O     1 
HETATM 5550 O O     . HOH K 3 .   ? 44.352  -9.654  -16.204 1.00 32.71 ? 334 HOH C O     1 
HETATM 5551 O O     . HOH K 3 .   ? 29.625  -10.416 -5.994  1.00 32.99 ? 335 HOH C O     1 
HETATM 5552 O O     . HOH K 3 .   ? 26.235  -29.565 -31.894 1.00 35.62 ? 336 HOH C O     1 
HETATM 5553 O O     . HOH K 3 .   ? 24.598  -19.800 -32.770 1.00 48.49 ? 337 HOH C O     1 
HETATM 5554 O O     . HOH K 3 .   ? 20.300  -5.783  -17.746 1.00 47.80 ? 338 HOH C O     1 
HETATM 5555 O O     . HOH K 3 .   ? 33.247  -23.251 -10.098 1.00 25.99 ? 339 HOH C O     1 
HETATM 5556 O O     . HOH K 3 .   ? 27.516  3.728   -16.635 1.00 53.66 ? 340 HOH C O     1 
HETATM 5557 O O     . HOH K 3 .   ? 17.980  -26.580 -18.318 1.00 29.35 ? 341 HOH C O     1 
HETATM 5558 O O     . HOH K 3 .   ? 17.807  -26.472 -13.373 1.00 34.86 ? 342 HOH C O     1 
HETATM 5559 O O     . HOH K 3 .   ? 30.730  -16.562 -7.509  1.00 22.32 ? 343 HOH C O     1 
HETATM 5560 O O     . HOH K 3 .   ? 34.088  -21.264 -26.965 1.00 36.06 ? 344 HOH C O     1 
HETATM 5561 O O     . HOH K 3 .   ? 30.049  -35.135 -32.441 1.00 35.26 ? 345 HOH C O     1 
HETATM 5562 O O     . HOH K 3 .   ? 42.646  -13.158 -3.409  1.00 40.78 ? 346 HOH C O     1 
HETATM 5563 O O     . HOH K 3 .   ? 11.979  -10.712 -10.173 1.00 42.37 ? 347 HOH C O     1 
HETATM 5564 O O     . HOH K 3 .   ? 23.268  -29.191 -13.587 1.00 23.52 ? 348 HOH C O     1 
HETATM 5565 O O     . HOH K 3 .   ? 20.490  -17.913 -7.050  1.00 34.78 ? 349 HOH C O     1 
HETATM 5566 O O     . HOH K 3 .   ? 44.417  -17.258 -28.537 1.00 46.24 ? 350 HOH C O     1 
HETATM 5567 O O     . HOH K 3 .   ? 42.845  -23.672 -16.475 1.00 27.84 ? 351 HOH C O     1 
HETATM 5568 O O     . HOH K 3 .   ? 19.177  -7.292  -10.193 1.00 44.71 ? 352 HOH C O     1 
HETATM 5569 O O     . HOH K 3 .   ? 15.743  -20.831 -4.645  1.00 36.68 ? 353 HOH C O     1 
HETATM 5570 O O     . HOH K 3 .   ? 38.131  -32.502 -24.641 1.00 31.09 ? 354 HOH C O     1 
HETATM 5571 O O     . HOH K 3 .   ? 15.026  -11.115 -5.920  1.00 38.32 ? 355 HOH C O     1 
HETATM 5572 O O     . HOH K 3 .   ? 33.031  -3.581  -15.357 1.00 47.61 ? 356 HOH C O     1 
HETATM 5573 O O     . HOH K 3 .   ? 39.144  -7.367  -20.272 1.00 26.89 ? 357 HOH C O     1 
HETATM 5574 O O     . HOH K 3 .   ? 26.890  -35.987 -32.599 1.00 43.69 ? 358 HOH C O     1 
HETATM 5575 O O     . HOH K 3 .   ? 26.339  -36.285 -24.947 1.00 40.52 ? 359 HOH C O     1 
HETATM 5576 O O     . HOH K 3 .   ? 14.403  -5.722  -19.977 1.00 40.10 ? 360 HOH C O     1 
HETATM 5577 O O     . HOH K 3 .   ? 20.155  -31.067 -30.668 1.00 39.06 ? 361 HOH C O     1 
HETATM 5578 O O     . HOH K 3 .   ? 17.250  -8.407  -17.975 1.00 38.76 ? 362 HOH C O     1 
HETATM 5579 O O     . HOH K 3 .   ? 21.809  -2.629  -28.591 1.00 44.12 ? 363 HOH C O     1 
HETATM 5580 O O     . HOH K 3 .   ? 40.618  -1.903  -14.034 1.00 45.01 ? 364 HOH C O     1 
HETATM 5581 O O     . HOH K 3 .   ? 33.059  -10.683 -6.452  1.00 30.66 ? 365 HOH C O     1 
HETATM 5582 O O     . HOH K 3 .   ? 30.700  -2.523  -27.470 1.00 42.84 ? 366 HOH C O     1 
HETATM 5583 O O     . HOH K 3 .   ? 47.081  -14.794 -24.652 1.00 28.97 ? 367 HOH C O     1 
HETATM 5584 O O     . HOH K 3 .   ? 15.218  -23.313 -7.315  1.00 37.14 ? 368 HOH C O     1 
HETATM 5585 O O     . HOH K 3 .   ? 16.329  -25.668 -20.503 1.00 26.27 ? 369 HOH C O     1 
HETATM 5586 O O     . HOH K 3 .   ? 47.865  -12.102 -21.756 1.00 28.12 ? 370 HOH C O     1 
HETATM 5587 O O     . HOH K 3 .   ? 36.944  -33.467 -14.366 1.00 28.19 ? 371 HOH C O     1 
HETATM 5588 O O     . HOH K 3 .   ? 12.093  -14.294 -14.592 1.00 37.80 ? 372 HOH C O     1 
HETATM 5589 O O     . HOH K 3 .   ? 46.997  -18.004 -8.196  1.00 35.46 ? 373 HOH C O     1 
HETATM 5590 O O     . HOH K 3 .   ? 15.111  -4.277  -24.544 1.00 43.70 ? 374 HOH C O     1 
HETATM 5591 O O     . HOH K 3 .   ? 40.618  -23.636 -10.228 1.00 20.20 ? 375 HOH C O     1 
HETATM 5592 O O     . HOH K 3 .   ? 13.357  -6.026  -22.896 1.00 45.11 ? 376 HOH C O     1 
HETATM 5593 O O     . HOH K 3 .   ? 28.092  -36.835 -22.852 1.00 32.37 ? 377 HOH C O     1 
HETATM 5594 O O     . HOH K 3 .   ? 34.086  -1.942  -19.169 1.00 44.84 ? 378 HOH C O     1 
HETATM 5595 O O     . HOH K 3 .   ? 25.347  -19.473 -28.421 1.00 40.49 ? 379 HOH C O     1 
HETATM 5596 O O     . HOH K 3 .   ? 32.833  -22.464 -5.018  1.00 43.59 ? 380 HOH C O     1 
HETATM 5597 O O     . HOH K 3 .   ? 22.491  -0.236  -15.949 1.00 55.49 ? 381 HOH C O     1 
HETATM 5598 O O     . HOH K 3 .   ? 16.814  -33.749 -21.533 1.00 36.58 ? 382 HOH C O     1 
HETATM 5599 O O     . HOH K 3 .   ? 16.608  -4.652  -25.998 1.00 46.34 ? 383 HOH C O     1 
HETATM 5600 O O     . HOH K 3 .   ? 20.800  -20.245 -6.261  1.00 36.32 ? 384 HOH C O     1 
HETATM 5601 O O     . HOH K 3 .   ? 31.827  -1.099  -13.329 1.00 41.30 ? 385 HOH C O     1 
HETATM 5602 O O     . HOH K 3 .   ? 42.252  -20.978 -23.896 1.00 36.14 ? 386 HOH C O     1 
HETATM 5603 O O     . HOH K 3 .   ? 20.617  -32.845 -28.251 1.00 41.66 ? 387 HOH C O     1 
HETATM 5604 O O     . HOH K 3 .   ? 34.664  -4.448  -18.945 1.00 44.39 ? 388 HOH C O     1 
HETATM 5605 O O     . HOH K 3 .   ? 40.846  -23.991 -7.745  1.00 26.76 ? 389 HOH C O     1 
HETATM 5606 O O     . HOH K 3 .   ? 13.967  -18.637 -3.558  1.00 44.63 ? 390 HOH C O     1 
HETATM 5607 O O     . HOH K 3 .   ? 36.703  -0.548  -25.550 1.00 47.10 ? 391 HOH C O     1 
HETATM 5608 O O     . HOH K 3 .   ? 27.688  -22.592 -8.753  1.00 41.46 ? 392 HOH C O     1 
HETATM 5609 O O     . HOH K 3 .   ? 21.713  1.262   -6.595  1.00 41.02 ? 393 HOH C O     1 
HETATM 5610 O O     . HOH K 3 .   ? 24.660  6.871   -9.101  1.00 52.02 ? 394 HOH C O     1 
HETATM 5611 O O     . HOH K 3 .   ? 21.217  -1.178  -31.126 1.00 52.86 ? 395 HOH C O     1 
HETATM 5612 O O     . HOH K 3 .   ? 13.685  -14.021 -12.636 1.00 47.28 ? 396 HOH C O     1 
HETATM 5613 O O     . HOH K 3 .   ? 9.953   -21.448 -22.914 1.00 43.19 ? 397 HOH C O     1 
HETATM 5614 O O     . HOH K 3 .   ? 45.990  -12.694 -28.145 1.00 32.49 ? 398 HOH C O     1 
HETATM 5615 O O     . HOH K 3 .   ? 49.160  -19.593 -13.445 1.00 47.35 ? 399 HOH C O     1 
HETATM 5616 O O     . HOH K 3 .   ? 30.492  -29.191 -11.219 1.00 36.47 ? 400 HOH C O     1 
HETATM 5617 O O     . HOH K 3 .   ? 17.028  -6.851  -15.912 1.00 44.47 ? 401 HOH C O     1 
HETATM 5618 O O     . HOH K 3 .   ? 32.912  -30.227 -10.113 1.00 32.39 ? 402 HOH C O     1 
HETATM 5619 O O     . HOH K 3 .   ? 45.987  -18.203 -24.864 1.00 45.87 ? 403 HOH C O     1 
HETATM 5620 O O     . HOH K 3 .   ? 9.422   -18.747 -5.517  1.00 36.68 ? 404 HOH C O     1 
HETATM 5621 O O     . HOH K 3 .   ? 38.765  -11.682 -5.205  1.00 46.62 ? 405 HOH C O     1 
HETATM 5622 O O     . HOH K 3 .   ? 35.858  -6.002  -17.768 1.00 41.07 ? 406 HOH C O     1 
HETATM 5623 O O     . HOH K 3 .   ? 8.168   -22.655 -17.683 1.00 43.85 ? 407 HOH C O     1 
HETATM 5624 O O     . HOH K 3 .   ? 45.705  -13.370 -30.366 1.00 50.60 ? 408 HOH C O     1 
HETATM 5625 O O     . HOH K 3 .   ? 37.125  -33.213 -27.049 1.00 40.34 ? 409 HOH C O     1 
HETATM 5626 O O     . HOH K 3 .   ? 35.646  -32.722 -11.931 1.00 27.56 ? 410 HOH C O     1 
HETATM 5627 O O     . HOH K 3 .   ? 47.300  -19.233 -5.668  1.00 31.34 ? 411 HOH C O     1 
HETATM 5628 O O     . HOH K 3 .   ? 45.896  -11.175 -15.455 1.00 38.96 ? 412 HOH C O     1 
HETATM 5629 O O     . HOH K 3 .   ? 15.741  -26.778 -22.491 1.00 30.35 ? 413 HOH C O     1 
HETATM 5630 O O     . HOH K 3 .   ? 22.076  -16.750 -4.905  1.00 37.98 ? 414 HOH C O     1 
HETATM 5631 O O     . HOH K 3 .   ? 48.145  -16.754 -23.820 1.00 43.75 ? 415 HOH C O     1 
HETATM 5632 O O     . HOH K 3 .   ? 7.992   -21.961 -15.205 1.00 45.37 ? 416 HOH C O     1 
HETATM 5633 O O     . HOH K 3 .   ? 49.742  -11.025 -20.164 1.00 44.28 ? 417 HOH C O     1 
HETATM 5634 O O     . HOH K 3 .   ? 36.753  -25.667 -32.702 1.00 50.07 ? 418 HOH C O     1 
HETATM 5635 O O     . HOH L 3 .   ? -14.732 21.882  -19.392 1.00 39.17 ? 301 HOH D O     1 
HETATM 5636 O O     . HOH L 3 .   ? -22.424 3.290   -40.872 1.00 46.30 ? 302 HOH D O     1 
HETATM 5637 O O     . HOH L 3 .   ? -25.551 16.145  -38.221 1.00 41.67 ? 303 HOH D O     1 
HETATM 5638 O O     . HOH L 3 .   ? -18.498 -5.281  -31.244 1.00 40.23 ? 304 HOH D O     1 
HETATM 5639 O O     . HOH L 3 .   ? -17.926 4.824   -35.957 1.00 36.48 ? 305 HOH D O     1 
HETATM 5640 O O     . HOH L 3 .   ? -25.347 4.476   -34.252 1.00 35.94 ? 306 HOH D O     1 
HETATM 5641 O O     . HOH L 3 .   ? -17.031 0.784   -32.551 1.00 40.96 ? 307 HOH D O     1 
HETATM 5642 O O     . HOH L 3 .   ? -15.004 17.833  -44.708 1.00 47.33 ? 308 HOH D O     1 
HETATM 5643 O O     . HOH L 3 .   ? -17.343 -5.342  -20.682 1.00 32.06 ? 309 HOH D O     1 
HETATM 5644 O O     . HOH L 3 .   ? -19.437 22.128  -23.267 1.00 38.93 ? 310 HOH D O     1 
HETATM 5645 O O     . HOH L 3 .   ? -13.687 18.794  -38.000 1.00 37.47 ? 311 HOH D O     1 
HETATM 5646 O O     . HOH L 3 .   ? -23.567 7.680   -17.190 1.00 39.63 ? 312 HOH D O     1 
HETATM 5647 O O     . HOH L 3 .   ? -10.937 -5.921  -19.224 1.00 36.82 ? 313 HOH D O     1 
HETATM 5648 O O     . HOH L 3 .   ? -26.848 10.210  -31.010 1.00 30.02 ? 314 HOH D O     1 
HETATM 5649 O O     . HOH L 3 .   ? -2.889  -3.992  -21.382 1.00 50.31 ? 315 HOH D O     1 
HETATM 5650 O O     . HOH L 3 .   ? -8.513  19.230  -21.157 1.00 26.46 ? 316 HOH D O     1 
HETATM 5651 O O     . HOH L 3 .   ? -18.346 -2.949  -29.732 1.00 29.92 ? 317 HOH D O     1 
HETATM 5652 O O     . HOH L 3 .   ? -25.930 17.430  -24.718 1.00 44.34 ? 318 HOH D O     1 
HETATM 5653 O O     . HOH L 3 .   ? -17.182 -8.197  -23.068 1.00 34.18 ? 319 HOH D O     1 
HETATM 5654 O O     . HOH L 3 .   ? -15.207 5.694   -33.047 1.00 31.29 ? 320 HOH D O     1 
HETATM 5655 O O     . HOH L 3 .   ? -6.465  -1.581  -44.880 1.00 48.26 ? 321 HOH D O     1 
HETATM 5656 O O     . HOH L 3 .   ? -25.156 10.463  -20.887 1.00 36.58 ? 322 HOH D O     1 
HETATM 5657 O O     . HOH L 3 .   ? -11.917 -0.913  -29.718 1.00 34.90 ? 323 HOH D O     1 
HETATM 5658 O O     . HOH L 3 .   ? 2.250   8.260   -38.333 1.00 50.43 ? 324 HOH D O     1 
HETATM 5659 O O     . HOH L 3 .   ? -16.513 12.221  -45.938 1.00 45.51 ? 325 HOH D O     1 
HETATM 5660 O O     . HOH L 3 .   ? -6.291  8.641   -13.078 1.00 30.49 ? 326 HOH D O     1 
HETATM 5661 O O     . HOH L 3 .   ? -18.543 2.517   -11.196 1.00 28.52 ? 327 HOH D O     1 
HETATM 5662 O O     . HOH L 3 .   ? -7.839  -3.148  -27.275 1.00 44.58 ? 328 HOH D O     1 
HETATM 5663 O O     . HOH L 3 .   ? -22.230 -4.906  -30.594 1.00 37.34 ? 329 HOH D O     1 
HETATM 5664 O O     . HOH L 3 .   ? -8.883  8.031   -11.886 1.00 27.80 ? 330 HOH D O     1 
HETATM 5665 O O     . HOH L 3 .   ? -10.448 17.704  -19.517 1.00 28.21 ? 331 HOH D O     1 
HETATM 5666 O O     . HOH L 3 .   ? -27.009 5.005   -32.016 1.00 39.81 ? 332 HOH D O     1 
HETATM 5667 O O     . HOH L 3 .   ? -27.041 10.524  -38.113 1.00 36.27 ? 333 HOH D O     1 
HETATM 5668 O O     . HOH L 3 .   ? -20.058 21.173  -30.891 1.00 36.84 ? 334 HOH D O     1 
HETATM 5669 O O     . HOH L 3 .   ? -26.251 10.563  -28.366 1.00 29.53 ? 335 HOH D O     1 
HETATM 5670 O O     . HOH L 3 .   ? -26.322 -3.049  -18.882 1.00 40.82 ? 336 HOH D O     1 
HETATM 5671 O O     . HOH L 3 .   ? -15.675 17.842  -15.906 1.00 38.50 ? 337 HOH D O     1 
HETATM 5672 O O     . HOH L 3 .   ? -16.791 -5.667  -16.667 1.00 37.68 ? 338 HOH D O     1 
HETATM 5673 O O     . HOH L 3 .   ? -16.425 1.811   -43.357 1.00 40.85 ? 339 HOH D O     1 
HETATM 5674 O O     . HOH L 3 .   ? -21.030 23.747  -32.199 1.00 39.64 ? 340 HOH D O     1 
HETATM 5675 O O     . HOH L 3 .   ? -28.066 4.807   -25.231 1.00 38.42 ? 341 HOH D O     1 
HETATM 5676 O O     . HOH L 3 .   ? -13.457 11.494  -16.381 1.00 26.97 ? 342 HOH D O     1 
HETATM 5677 O O     . HOH L 3 .   ? -11.490 -1.054  -27.287 1.00 35.34 ? 343 HOH D O     1 
HETATM 5678 O O     . HOH L 3 .   ? -16.058 2.557   -33.995 1.00 40.31 ? 344 HOH D O     1 
HETATM 5679 O O     . HOH L 3 .   ? 0.841   10.186  -28.706 1.00 41.02 ? 345 HOH D O     1 
HETATM 5680 O O     . HOH L 3 .   ? -17.881 -0.705  -34.145 1.00 45.99 ? 346 HOH D O     1 
HETATM 5681 O O     . HOH L 3 .   ? -25.054 -1.326  -34.723 1.00 43.87 ? 347 HOH D O     1 
HETATM 5682 O O     . HOH L 3 .   ? -17.956 11.580  -17.159 1.00 45.83 ? 348 HOH D O     1 
HETATM 5683 O O     . HOH L 3 .   ? -0.372  8.567   -39.628 1.00 47.21 ? 349 HOH D O     1 
HETATM 5684 O O     . HOH L 3 .   ? -20.841 2.920   -50.892 1.00 54.46 ? 350 HOH D O     1 
HETATM 5685 O O     . HOH L 3 .   ? 4.643   0.472   -21.864 1.00 42.67 ? 351 HOH D O     1 
HETATM 5686 O O     . HOH L 3 .   ? -4.688  -0.116  -43.988 1.00 44.15 ? 352 HOH D O     1 
HETATM 5687 O O     . HOH L 3 .   ? 1.488   7.895   -27.897 1.00 39.44 ? 353 HOH D O     1 
HETATM 5688 O O     . HOH L 3 .   ? -14.062 26.449  -33.373 1.00 43.91 ? 354 HOH D O     1 
HETATM 5689 O O     . HOH L 3 .   ? -27.311 3.007   -21.772 1.00 40.68 ? 355 HOH D O     1 
HETATM 5690 O O     . HOH L 3 .   ? -27.594 -2.008  -33.066 1.00 53.23 ? 356 HOH D O     1 
HETATM 5691 O O     . HOH L 3 .   ? -29.142 16.298  -29.449 1.00 51.50 ? 357 HOH D O     1 
HETATM 5692 O O     . HOH L 3 .   ? -18.980 2.748   -43.783 1.00 47.37 ? 358 HOH D O     1 
HETATM 5693 O O     . HOH L 3 .   ? 1.804   -2.423  -21.397 1.00 40.79 ? 359 HOH D O     1 
HETATM 5694 O O     . HOH L 3 .   ? -17.157 22.126  -24.839 1.00 37.19 ? 360 HOH D O     1 
HETATM 5695 O O     . HOH L 3 .   ? -26.738 0.558   -19.077 1.00 41.36 ? 361 HOH D O     1 
HETATM 5696 O O     . HOH L 3 .   ? -0.456  17.422  -18.531 1.00 46.31 ? 362 HOH D O     1 
HETATM 5697 O O     . HOH L 3 .   ? -5.688  20.279  -32.846 1.00 44.91 ? 363 HOH D O     1 
HETATM 5698 O O     . HOH L 3 .   ? -21.328 21.478  -35.681 1.00 46.78 ? 364 HOH D O     1 
HETATM 5699 O O     . HOH L 3 .   ? -30.336 -0.456  -34.489 1.00 50.41 ? 365 HOH D O     1 
HETATM 5700 O O     . HOH L 3 .   ? -23.267 25.271  -23.480 1.00 38.42 ? 366 HOH D O     1 
HETATM 5701 O O     . HOH L 3 .   ? -27.750 -3.226  -21.793 1.00 28.50 ? 367 HOH D O     1 
HETATM 5702 O O     . HOH L 3 .   ? -9.455  19.418  -37.941 1.00 46.90 ? 368 HOH D O     1 
HETATM 5703 O O     . HOH L 3 .   ? -22.839 27.667  -25.318 1.00 46.17 ? 369 HOH D O     1 
HETATM 5704 O O     . HOH L 3 .   ? -19.440 9.531   -15.431 1.00 37.29 ? 370 HOH D O     1 
HETATM 5705 O O     . HOH L 3 .   ? -7.716  18.757  -40.143 1.00 46.75 ? 371 HOH D O     1 
HETATM 5706 O O     . HOH L 3 .   ? -27.847 7.420   -24.159 1.00 36.46 ? 372 HOH D O     1 
HETATM 5707 O O     . HOH L 3 .   ? -18.732 9.030   -12.694 1.00 35.80 ? 373 HOH D O     1 
HETATM 5708 O O     . HOH L 3 .   ? -1.293  19.867  -19.507 1.00 46.23 ? 374 HOH D O     1 
HETATM 5709 O O     . HOH L 3 .   ? -18.738 5.187   -11.034 1.00 31.45 ? 375 HOH D O     1 
HETATM 5710 O O     . HOH L 3 .   ? -19.295 24.873  -22.346 1.00 39.05 ? 376 HOH D O     1 
HETATM 5711 O O     . HOH L 3 .   ? -17.863 -7.354  -18.856 1.00 36.95 ? 377 HOH D O     1 
HETATM 5712 O O     . HOH L 3 .   ? -19.448 26.415  -24.692 1.00 44.50 ? 378 HOH D O     1 
HETATM 5713 O O     . HOH L 3 .   ? -27.990 11.475  -26.630 1.00 40.60 ? 379 HOH D O     1 
HETATM 5714 O O     . HOH L 3 .   ? -21.199 -11.439 -26.874 1.00 31.13 ? 380 HOH D O     1 
HETATM 5715 O O     . HOH L 3 .   ? -8.433  -5.628  -20.423 1.00 44.49 ? 381 HOH D O     1 
HETATM 5716 O O     . HOH L 3 .   ? -27.703 7.836   -31.939 1.00 38.80 ? 382 HOH D O     1 
HETATM 5717 O O     . HOH L 3 .   ? -12.381 21.236  -38.034 1.00 51.17 ? 383 HOH D O     1 
HETATM 5718 O O     . HOH L 3 .   ? -19.300 -12.037 -28.548 1.00 41.93 ? 384 HOH D O     1 
HETATM 5719 O O     . HOH L 3 .   ? -28.641 9.586   -24.633 1.00 45.26 ? 385 HOH D O     1 
HETATM 5720 O O     . HOH L 3 .   ? -22.203 22.435  -20.117 1.00 40.16 ? 386 HOH D O     1 
HETATM 5721 O O     . HOH L 3 .   ? -8.303  20.816  -40.183 1.00 54.25 ? 387 HOH D O     1 
HETATM 5722 O O     . HOH L 3 .   ? -29.795 -4.845  -20.908 1.00 33.34 ? 388 HOH D O     1 
HETATM 5723 O O     . HOH L 3 .   ? -10.884 12.919  -50.827 1.00 51.18 ? 389 HOH D O     1 
HETATM 5724 O O     . HOH L 3 .   ? -14.854 -9.432  -24.301 1.00 43.99 ? 390 HOH D O     1 
# 
