data_9NG7
# 
_entry.id   9NG7 
# 
_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   9NG7         pdb_00009ng7 10.2210/pdb9ng7/pdb 
WWPDB D_1000293332 ?            ?                   
# 
_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       2025-04-02 
_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                        9NG7 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 geiger@chemistry.msu.edu James Geiger H 'principal investigator/group leader' 0000-0002-9443-4488 
3 draths@chemistry.msu.edu Karen Draths ? 'principal investigator/group leader' 0000-0001-7852-1090 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Silva, K.'    1 ? 
'Geiger, J.H.' 2 ? 
'Draths, K.'   3 ? 
# 
_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                     'cis-CaaD H28A mutant' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Silva, K.'    1 ? 
primary 'Geiger, J.H.' 2 ? 
primary 'Draths, K.'   3 ? 
# 
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 'Cis-3-chloroacrylic acid dehalogenase' 18500.514 3   ? ? ? ? 
2 non-polymer syn 'ACETATE ION'                           59.044    2   ? ? ? ? 
3 water       nat water                                   18.015    155 ? ? ? ? 
# 
_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       
;PVYMVYVSQDRLTPSAKHAVAKAITDAARGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEHH
HHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PVYMVYVSQDRLTPSAKHAVAKAITDAARGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEHH
HHHH
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETATE ION' ACT 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   VAL n 
1 3   TYR n 
1 4   MET n 
1 5   VAL n 
1 6   TYR n 
1 7   VAL n 
1 8   SER n 
1 9   GLN n 
1 10  ASP n 
1 11  ARG n 
1 12  LEU n 
1 13  THR n 
1 14  PRO n 
1 15  SER n 
1 16  ALA n 
1 17  LYS n 
1 18  HIS n 
1 19  ALA n 
1 20  VAL n 
1 21  ALA n 
1 22  LYS n 
1 23  ALA n 
1 24  ILE n 
1 25  THR n 
1 26  ASP n 
1 27  ALA n 
1 28  ALA n 
1 29  ARG n 
1 30  GLY n 
1 31  LEU n 
1 32  THR n 
1 33  GLY n 
1 34  THR n 
1 35  GLN n 
1 36  HIS n 
1 37  PHE n 
1 38  LEU n 
1 39  ALA n 
1 40  GLN n 
1 41  VAL n 
1 42  ASN n 
1 43  PHE n 
1 44  GLN n 
1 45  GLU n 
1 46  GLN n 
1 47  PRO n 
1 48  ALA n 
1 49  GLY n 
1 50  ASN n 
1 51  VAL n 
1 52  PHE n 
1 53  LEU n 
1 54  GLY n 
1 55  GLY n 
1 56  VAL n 
1 57  GLN n 
1 58  GLN n 
1 59  GLY n 
1 60  GLY n 
1 61  ASP n 
1 62  THR n 
1 63  ILE n 
1 64  PHE n 
1 65  VAL n 
1 66  HIS n 
1 67  GLY n 
1 68  LEU n 
1 69  HIS n 
1 70  ARG n 
1 71  GLU n 
1 72  GLY n 
1 73  ARG n 
1 74  SER n 
1 75  ALA n 
1 76  ASP n 
1 77  LEU n 
1 78  LYS n 
1 79  GLY n 
1 80  GLN n 
1 81  LEU n 
1 82  ALA n 
1 83  GLN n 
1 84  ARG n 
1 85  ILE n 
1 86  VAL n 
1 87  ASP n 
1 88  ASP n 
1 89  VAL n 
1 90  SER n 
1 91  VAL n 
1 92  ALA n 
1 93  ALA n 
1 94  GLU n 
1 95  ILE n 
1 96  ASP n 
1 97  ARG n 
1 98  LYS n 
1 99  HIS n 
1 100 ILE n 
1 101 TRP n 
1 102 VAL n 
1 103 TYR n 
1 104 PHE n 
1 105 GLY n 
1 106 GLU n 
1 107 MET n 
1 108 PRO n 
1 109 ALA n 
1 110 GLN n 
1 111 GLN n 
1 112 MET n 
1 113 VAL n 
1 114 GLU n 
1 115 TYR n 
1 116 GLY n 
1 117 ARG n 
1 118 PHE n 
1 119 LEU n 
1 120 PRO n 
1 121 GLN n 
1 122 PRO n 
1 123 GLY n 
1 124 HIS n 
1 125 GLU n 
1 126 GLY n 
1 127 GLU n 
1 128 TRP n 
1 129 PHE n 
1 130 ASP n 
1 131 ASN n 
1 132 LEU n 
1 133 SER n 
1 134 SER n 
1 135 ASP n 
1 136 GLU n 
1 137 ARG n 
1 138 ALA n 
1 139 PHE n 
1 140 MET n 
1 141 GLU n 
1 142 THR n 
1 143 ASN n 
1 144 VAL n 
1 145 ASP n 
1 146 VAL n 
1 147 SER n 
1 148 ARG n 
1 149 THR n 
1 150 GLU n 
1 151 ASN n 
1 152 LEU n 
1 153 TYR n 
1 154 PHE n 
1 155 GLN n 
1 156 GLY n 
1 157 LEU n 
1 158 GLU n 
1 159 HIS n 
1 160 HIS n 
1 161 HIS n 
1 162 HIS n 
1 163 HIS n 
1 164 HIS 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                   164 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 cis-caaD 
_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      'coryneform bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1728 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'   ? 'C2 H3 O2 -1'    59.044  
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 
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   PRO 1   1   1   PRO PRO A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  HIS 69  69  69  HIS HIS A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 MET 107 107 107 MET MET A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLN 121 121 ?   ?   ?   A . n 
A 1 122 PRO 122 122 ?   ?   ?   A . n 
A 1 123 GLY 123 123 ?   ?   ?   A . n 
A 1 124 HIS 124 124 ?   ?   ?   A . n 
A 1 125 GLU 125 125 ?   ?   ?   A . n 
A 1 126 GLY 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
A 1 128 TRP 128 128 ?   ?   ?   A . n 
A 1 129 PHE 129 129 ?   ?   ?   A . n 
A 1 130 ASP 130 130 ?   ?   ?   A . n 
A 1 131 ASN 131 131 ?   ?   ?   A . n 
A 1 132 LEU 132 132 ?   ?   ?   A . n 
A 1 133 SER 133 133 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 ASP 135 135 ?   ?   ?   A . n 
A 1 136 GLU 136 136 ?   ?   ?   A . n 
A 1 137 ARG 137 137 ?   ?   ?   A . n 
A 1 138 ALA 138 138 ?   ?   ?   A . n 
A 1 139 PHE 139 139 ?   ?   ?   A . n 
A 1 140 MET 140 140 ?   ?   ?   A . n 
A 1 141 GLU 141 141 ?   ?   ?   A . n 
A 1 142 THR 142 142 ?   ?   ?   A . n 
A 1 143 ASN 143 143 ?   ?   ?   A . n 
A 1 144 VAL 144 144 ?   ?   ?   A . n 
A 1 145 ASP 145 145 ?   ?   ?   A . n 
A 1 146 VAL 146 146 ?   ?   ?   A . n 
A 1 147 SER 147 147 ?   ?   ?   A . n 
A 1 148 ARG 148 148 ?   ?   ?   A . n 
A 1 149 THR 149 149 ?   ?   ?   A . n 
A 1 150 GLU 150 150 ?   ?   ?   A . n 
A 1 151 ASN 151 151 ?   ?   ?   A . n 
A 1 152 LEU 152 152 ?   ?   ?   A . n 
A 1 153 TYR 153 153 ?   ?   ?   A . n 
A 1 154 PHE 154 154 ?   ?   ?   A . n 
A 1 155 GLN 155 155 ?   ?   ?   A . n 
A 1 156 GLY 156 156 ?   ?   ?   A . n 
A 1 157 LEU 157 157 ?   ?   ?   A . n 
A 1 158 GLU 158 158 ?   ?   ?   A . n 
A 1 159 HIS 159 159 ?   ?   ?   A . n 
A 1 160 HIS 160 160 ?   ?   ?   A . n 
A 1 161 HIS 161 161 ?   ?   ?   A . n 
A 1 162 HIS 162 162 ?   ?   ?   A . n 
A 1 163 HIS 163 163 ?   ?   ?   A . n 
A 1 164 HIS 164 164 ?   ?   ?   A . n 
B 1 1   PRO 1   1   1   PRO PRO B . n 
B 1 2   VAL 2   2   2   VAL VAL B . n 
B 1 3   TYR 3   3   3   TYR TYR B . n 
B 1 4   MET 4   4   4   MET MET B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLN 9   9   9   GLN GLN B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  HIS 18  18  18  HIS HIS B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  ARG 29  29  29  ARG ARG B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  THR 34  34  34  THR THR B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  GLN 40  40  40  GLN GLN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  GLN 46  46  46  GLN GLN B . n 
B 1 47  PRO 47  47  47  PRO PRO B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  PHE 52  52  52  PHE PHE B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  HIS 69  69  69  HIS HIS B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  GLN 80  80  80  GLN GLN B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  SER 90  90  90  SER SER B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  ARG 97  97  97  ARG ARG B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  HIS 99  99  99  HIS HIS B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 TRP 101 101 101 TRP TRP B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 PHE 104 104 104 PHE PHE B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 MET 107 107 107 MET MET B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 GLN 121 121 ?   ?   ?   B . n 
B 1 122 PRO 122 122 ?   ?   ?   B . n 
B 1 123 GLY 123 123 ?   ?   ?   B . n 
B 1 124 HIS 124 124 ?   ?   ?   B . n 
B 1 125 GLU 125 125 ?   ?   ?   B . n 
B 1 126 GLY 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
B 1 128 TRP 128 128 ?   ?   ?   B . n 
B 1 129 PHE 129 129 ?   ?   ?   B . n 
B 1 130 ASP 130 130 ?   ?   ?   B . n 
B 1 131 ASN 131 131 ?   ?   ?   B . n 
B 1 132 LEU 132 132 ?   ?   ?   B . n 
B 1 133 SER 133 133 ?   ?   ?   B . n 
B 1 134 SER 134 134 ?   ?   ?   B . n 
B 1 135 ASP 135 135 ?   ?   ?   B . n 
B 1 136 GLU 136 136 ?   ?   ?   B . n 
B 1 137 ARG 137 137 ?   ?   ?   B . n 
B 1 138 ALA 138 138 ?   ?   ?   B . n 
B 1 139 PHE 139 139 ?   ?   ?   B . n 
B 1 140 MET 140 140 ?   ?   ?   B . n 
B 1 141 GLU 141 141 ?   ?   ?   B . n 
B 1 142 THR 142 142 ?   ?   ?   B . n 
B 1 143 ASN 143 143 ?   ?   ?   B . n 
B 1 144 VAL 144 144 ?   ?   ?   B . n 
B 1 145 ASP 145 145 ?   ?   ?   B . n 
B 1 146 VAL 146 146 ?   ?   ?   B . n 
B 1 147 SER 147 147 ?   ?   ?   B . n 
B 1 148 ARG 148 148 ?   ?   ?   B . n 
B 1 149 THR 149 149 ?   ?   ?   B . n 
B 1 150 GLU 150 150 ?   ?   ?   B . n 
B 1 151 ASN 151 151 ?   ?   ?   B . n 
B 1 152 LEU 152 152 ?   ?   ?   B . n 
B 1 153 TYR 153 153 ?   ?   ?   B . n 
B 1 154 PHE 154 154 ?   ?   ?   B . n 
B 1 155 GLN 155 155 ?   ?   ?   B . n 
B 1 156 GLY 156 156 ?   ?   ?   B . n 
B 1 157 LEU 157 157 ?   ?   ?   B . n 
B 1 158 GLU 158 158 ?   ?   ?   B . n 
B 1 159 HIS 159 159 ?   ?   ?   B . n 
B 1 160 HIS 160 160 ?   ?   ?   B . n 
B 1 161 HIS 161 161 ?   ?   ?   B . n 
B 1 162 HIS 162 162 ?   ?   ?   B . n 
B 1 163 HIS 163 163 ?   ?   ?   B . n 
B 1 164 HIS 164 164 ?   ?   ?   B . n 
C 1 1   PRO 1   1   1   PRO PRO C . n 
C 1 2   VAL 2   2   2   VAL VAL C . n 
C 1 3   TYR 3   3   3   TYR TYR C . n 
C 1 4   MET 4   4   4   MET MET C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   SER 8   8   8   SER SER C . n 
C 1 9   GLN 9   9   9   GLN GLN C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  ARG 11  11  11  ARG ARG C . n 
C 1 12  LEU 12  12  12  LEU LEU C . n 
C 1 13  THR 13  13  13  THR THR C . n 
C 1 14  PRO 14  14  14  PRO PRO C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  ALA 16  16  16  ALA ALA C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  HIS 18  18  18  HIS HIS C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  VAL 20  20  20  VAL VAL C . n 
C 1 21  ALA 21  21  21  ALA ALA C . n 
C 1 22  LYS 22  22  22  LYS LYS C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  ILE 24  24  24  ILE ILE C . n 
C 1 25  THR 25  25  25  THR THR C . n 
C 1 26  ASP 26  26  26  ASP ASP C . n 
C 1 27  ALA 27  27  27  ALA ALA C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  ARG 29  29  29  ARG ARG C . n 
C 1 30  GLY 30  30  30  GLY GLY C . n 
C 1 31  LEU 31  31  31  LEU LEU C . n 
C 1 32  THR 32  32  32  THR THR C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  THR 34  34  34  THR THR C . n 
C 1 35  GLN 35  35  35  GLN GLN C . n 
C 1 36  HIS 36  36  36  HIS HIS C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  ALA 39  39  39  ALA ALA C . n 
C 1 40  GLN 40  40  40  GLN GLN C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  ASN 42  42  42  ASN ASN C . n 
C 1 43  PHE 43  43  43  PHE PHE C . n 
C 1 44  GLN 44  44  44  GLN GLN C . n 
C 1 45  GLU 45  45  45  GLU GLU C . n 
C 1 46  GLN 46  46  46  GLN GLN C . n 
C 1 47  PRO 47  47  47  PRO PRO C . n 
C 1 48  ALA 48  48  48  ALA ALA C . n 
C 1 49  GLY 49  49  49  GLY GLY C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  VAL 51  51  51  VAL VAL C . n 
C 1 52  PHE 52  52  52  PHE PHE C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  GLY 54  54  54  GLY GLY C . n 
C 1 55  GLY 55  55  55  GLY GLY C . n 
C 1 56  VAL 56  56  56  VAL VAL C . n 
C 1 57  GLN 57  57  57  GLN GLN C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  GLY 60  60  60  GLY GLY C . n 
C 1 61  ASP 61  61  61  ASP ASP C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ILE 63  63  63  ILE ILE C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  VAL 65  65  65  VAL VAL C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  GLY 67  67  67  GLY GLY C . n 
C 1 68  LEU 68  68  68  LEU LEU C . n 
C 1 69  HIS 69  69  69  HIS HIS C . n 
C 1 70  ARG 70  70  70  ARG ARG C . n 
C 1 71  GLU 71  71  71  GLU GLU C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  ARG 73  73  73  ARG ARG C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  LYS 78  78  78  LYS LYS C . n 
C 1 79  GLY 79  79  79  GLY GLY C . n 
C 1 80  GLN 80  80  80  GLN GLN C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  ALA 82  82  82  ALA ALA C . n 
C 1 83  GLN 83  83  83  GLN GLN C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  ILE 85  85  85  ILE ILE C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  ASP 87  87  87  ASP ASP C . n 
C 1 88  ASP 88  88  88  ASP ASP C . n 
C 1 89  VAL 89  89  89  VAL VAL C . n 
C 1 90  SER 90  90  90  SER SER C . n 
C 1 91  VAL 91  91  91  VAL VAL C . n 
C 1 92  ALA 92  92  92  ALA ALA C . n 
C 1 93  ALA 93  93  93  ALA ALA C . n 
C 1 94  GLU 94  94  94  GLU GLU C . n 
C 1 95  ILE 95  95  95  ILE ILE C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  ARG 97  97  97  ARG ARG C . n 
C 1 98  LYS 98  98  98  LYS LYS C . n 
C 1 99  HIS 99  99  99  HIS HIS C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 TRP 101 101 101 TRP TRP C . n 
C 1 102 VAL 102 102 102 VAL VAL C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 PHE 104 104 104 PHE PHE C . n 
C 1 105 GLY 105 105 105 GLY GLY C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 MET 107 107 107 MET MET C . n 
C 1 108 PRO 108 108 108 PRO PRO C . n 
C 1 109 ALA 109 109 109 ALA ALA C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 GLN 111 111 111 GLN GLN C . n 
C 1 112 MET 112 112 112 MET MET C . n 
C 1 113 VAL 113 113 113 VAL VAL C . n 
C 1 114 GLU 114 114 114 GLU GLU C . n 
C 1 115 TYR 115 115 115 TYR TYR C . n 
C 1 116 GLY 116 116 116 GLY GLY C . n 
C 1 117 ARG 117 117 117 ARG ARG C . n 
C 1 118 PHE 118 118 118 PHE PHE C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 PRO 120 120 120 PRO PRO C . n 
C 1 121 GLN 121 121 ?   ?   ?   C . n 
C 1 122 PRO 122 122 ?   ?   ?   C . n 
C 1 123 GLY 123 123 ?   ?   ?   C . n 
C 1 124 HIS 124 124 ?   ?   ?   C . n 
C 1 125 GLU 125 125 ?   ?   ?   C . n 
C 1 126 GLY 126 126 ?   ?   ?   C . n 
C 1 127 GLU 127 127 ?   ?   ?   C . n 
C 1 128 TRP 128 128 ?   ?   ?   C . n 
C 1 129 PHE 129 129 ?   ?   ?   C . n 
C 1 130 ASP 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 ?   ?   ?   C . n 
C 1 132 LEU 132 132 ?   ?   ?   C . n 
C 1 133 SER 133 133 ?   ?   ?   C . n 
C 1 134 SER 134 134 ?   ?   ?   C . n 
C 1 135 ASP 135 135 ?   ?   ?   C . n 
C 1 136 GLU 136 136 ?   ?   ?   C . n 
C 1 137 ARG 137 137 ?   ?   ?   C . n 
C 1 138 ALA 138 138 ?   ?   ?   C . n 
C 1 139 PHE 139 139 ?   ?   ?   C . n 
C 1 140 MET 140 140 ?   ?   ?   C . n 
C 1 141 GLU 141 141 ?   ?   ?   C . n 
C 1 142 THR 142 142 ?   ?   ?   C . n 
C 1 143 ASN 143 143 ?   ?   ?   C . n 
C 1 144 VAL 144 144 ?   ?   ?   C . n 
C 1 145 ASP 145 145 ?   ?   ?   C . n 
C 1 146 VAL 146 146 ?   ?   ?   C . n 
C 1 147 SER 147 147 ?   ?   ?   C . n 
C 1 148 ARG 148 148 ?   ?   ?   C . n 
C 1 149 THR 149 149 ?   ?   ?   C . n 
C 1 150 GLU 150 150 ?   ?   ?   C . n 
C 1 151 ASN 151 151 ?   ?   ?   C . n 
C 1 152 LEU 152 152 ?   ?   ?   C . n 
C 1 153 TYR 153 153 ?   ?   ?   C . n 
C 1 154 PHE 154 154 ?   ?   ?   C . n 
C 1 155 GLN 155 155 ?   ?   ?   C . n 
C 1 156 GLY 156 156 ?   ?   ?   C . n 
C 1 157 LEU 157 157 ?   ?   ?   C . n 
C 1 158 GLU 158 158 ?   ?   ?   C . n 
C 1 159 HIS 159 159 ?   ?   ?   C . n 
C 1 160 HIS 160 160 ?   ?   ?   C . n 
C 1 161 HIS 161 161 ?   ?   ?   C . n 
C 1 162 HIS 162 162 ?   ?   ?   C . n 
C 1 163 HIS 163 163 ?   ?   ?   C . n 
C 1 164 HIS 164 164 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 ACT 1  201 201 ACT ACT B . 
E 2 ACT 1  201 201 ACT ACT C . 
F 3 HOH 1  201 36  HOH HOH A . 
F 3 HOH 2  202 34  HOH HOH A . 
F 3 HOH 3  203 74  HOH HOH A . 
F 3 HOH 4  204 122 HOH HOH A . 
F 3 HOH 5  205 55  HOH HOH A . 
F 3 HOH 6  206 12  HOH HOH A . 
F 3 HOH 7  207 44  HOH HOH A . 
F 3 HOH 8  208 26  HOH HOH A . 
F 3 HOH 9  209 11  HOH HOH A . 
F 3 HOH 10 210 67  HOH HOH A . 
F 3 HOH 11 211 20  HOH HOH A . 
F 3 HOH 12 212 148 HOH HOH A . 
F 3 HOH 13 213 141 HOH HOH A . 
F 3 HOH 14 214 88  HOH HOH A . 
F 3 HOH 15 215 138 HOH HOH A . 
F 3 HOH 16 216 45  HOH HOH A . 
F 3 HOH 17 217 14  HOH HOH A . 
F 3 HOH 18 218 51  HOH HOH A . 
F 3 HOH 19 219 72  HOH HOH A . 
F 3 HOH 20 220 48  HOH HOH A . 
F 3 HOH 21 221 94  HOH HOH A . 
F 3 HOH 22 222 127 HOH HOH A . 
F 3 HOH 23 223 57  HOH HOH A . 
F 3 HOH 24 224 4   HOH HOH A . 
F 3 HOH 25 225 7   HOH HOH A . 
F 3 HOH 26 226 132 HOH HOH A . 
F 3 HOH 27 227 145 HOH HOH A . 
F 3 HOH 28 228 31  HOH HOH A . 
F 3 HOH 29 229 21  HOH HOH A . 
F 3 HOH 30 230 113 HOH HOH A . 
F 3 HOH 31 231 63  HOH HOH A . 
F 3 HOH 32 232 86  HOH HOH A . 
F 3 HOH 33 233 89  HOH HOH A . 
F 3 HOH 34 234 76  HOH HOH A . 
F 3 HOH 35 235 134 HOH HOH A . 
F 3 HOH 36 236 64  HOH HOH A . 
F 3 HOH 37 237 80  HOH HOH A . 
F 3 HOH 38 238 143 HOH HOH A . 
F 3 HOH 39 239 155 HOH HOH A . 
F 3 HOH 40 240 118 HOH HOH A . 
F 3 HOH 41 241 69  HOH HOH A . 
F 3 HOH 42 242 82  HOH HOH A . 
F 3 HOH 43 243 84  HOH HOH A . 
F 3 HOH 44 244 111 HOH HOH A . 
F 3 HOH 45 245 99  HOH HOH A . 
F 3 HOH 46 246 126 HOH HOH A . 
F 3 HOH 47 247 124 HOH HOH A . 
F 3 HOH 48 248 28  HOH HOH A . 
F 3 HOH 49 249 116 HOH HOH A . 
F 3 HOH 50 250 98  HOH HOH A . 
G 3 HOH 1  301 41  HOH HOH B . 
G 3 HOH 2  302 157 HOH HOH B . 
G 3 HOH 3  303 71  HOH HOH B . 
G 3 HOH 4  304 46  HOH HOH B . 
G 3 HOH 5  305 1   HOH HOH B . 
G 3 HOH 6  306 49  HOH HOH B . 
G 3 HOH 7  307 6   HOH HOH B . 
G 3 HOH 8  308 149 HOH HOH B . 
G 3 HOH 9  309 47  HOH HOH B . 
G 3 HOH 10 310 8   HOH HOH B . 
G 3 HOH 11 311 66  HOH HOH B . 
G 3 HOH 12 312 117 HOH HOH B . 
G 3 HOH 13 313 92  HOH HOH B . 
G 3 HOH 14 314 59  HOH HOH B . 
G 3 HOH 15 315 18  HOH HOH B . 
G 3 HOH 16 316 78  HOH HOH B . 
G 3 HOH 17 317 17  HOH HOH B . 
G 3 HOH 18 318 19  HOH HOH B . 
G 3 HOH 19 319 40  HOH HOH B . 
G 3 HOH 20 320 54  HOH HOH B . 
G 3 HOH 21 321 142 HOH HOH B . 
G 3 HOH 22 322 146 HOH HOH B . 
G 3 HOH 23 323 10  HOH HOH B . 
G 3 HOH 24 324 125 HOH HOH B . 
G 3 HOH 25 325 87  HOH HOH B . 
G 3 HOH 26 326 33  HOH HOH B . 
G 3 HOH 27 327 112 HOH HOH B . 
G 3 HOH 28 328 75  HOH HOH B . 
G 3 HOH 29 329 152 HOH HOH B . 
G 3 HOH 30 330 100 HOH HOH B . 
G 3 HOH 31 331 114 HOH HOH B . 
G 3 HOH 32 332 2   HOH HOH B . 
G 3 HOH 33 333 5   HOH HOH B . 
G 3 HOH 34 334 24  HOH HOH B . 
G 3 HOH 35 335 60  HOH HOH B . 
G 3 HOH 36 336 58  HOH HOH B . 
G 3 HOH 37 337 68  HOH HOH B . 
G 3 HOH 38 338 131 HOH HOH B . 
G 3 HOH 39 339 105 HOH HOH B . 
G 3 HOH 40 340 108 HOH HOH B . 
G 3 HOH 41 341 39  HOH HOH B . 
G 3 HOH 42 342 115 HOH HOH B . 
G 3 HOH 43 343 110 HOH HOH B . 
G 3 HOH 44 344 56  HOH HOH B . 
G 3 HOH 45 345 129 HOH HOH B . 
G 3 HOH 46 346 103 HOH HOH B . 
G 3 HOH 47 347 65  HOH HOH B . 
G 3 HOH 48 348 107 HOH HOH B . 
G 3 HOH 49 349 90  HOH HOH B . 
G 3 HOH 50 350 133 HOH HOH B . 
G 3 HOH 51 351 156 HOH HOH B . 
G 3 HOH 52 352 136 HOH HOH B . 
G 3 HOH 53 353 139 HOH HOH B . 
G 3 HOH 54 354 96  HOH HOH B . 
H 3 HOH 1  301 42  HOH HOH C . 
H 3 HOH 2  302 144 HOH HOH C . 
H 3 HOH 3  303 29  HOH HOH C . 
H 3 HOH 4  304 53  HOH HOH C . 
H 3 HOH 5  305 37  HOH HOH C . 
H 3 HOH 6  306 101 HOH HOH C . 
H 3 HOH 7  307 13  HOH HOH C . 
H 3 HOH 8  308 130 HOH HOH C . 
H 3 HOH 9  309 123 HOH HOH C . 
H 3 HOH 10 310 9   HOH HOH C . 
H 3 HOH 11 311 23  HOH HOH C . 
H 3 HOH 12 312 62  HOH HOH C . 
H 3 HOH 13 313 61  HOH HOH C . 
H 3 HOH 14 314 16  HOH HOH C . 
H 3 HOH 15 315 43  HOH HOH C . 
H 3 HOH 16 316 119 HOH HOH C . 
H 3 HOH 17 317 73  HOH HOH C . 
H 3 HOH 18 318 137 HOH HOH C . 
H 3 HOH 19 319 22  HOH HOH C . 
H 3 HOH 20 320 38  HOH HOH C . 
H 3 HOH 21 321 109 HOH HOH C . 
H 3 HOH 22 322 32  HOH HOH C . 
H 3 HOH 23 323 50  HOH HOH C . 
H 3 HOH 24 324 120 HOH HOH C . 
H 3 HOH 25 325 3   HOH HOH C . 
H 3 HOH 26 326 83  HOH HOH C . 
H 3 HOH 27 327 35  HOH HOH C . 
H 3 HOH 28 328 15  HOH HOH C . 
H 3 HOH 29 329 52  HOH HOH C . 
H 3 HOH 30 330 147 HOH HOH C . 
H 3 HOH 31 331 81  HOH HOH C . 
H 3 HOH 32 332 106 HOH HOH C . 
H 3 HOH 33 333 27  HOH HOH C . 
H 3 HOH 34 334 104 HOH HOH C . 
H 3 HOH 35 335 102 HOH HOH C . 
H 3 HOH 36 336 79  HOH HOH C . 
H 3 HOH 37 337 70  HOH HOH C . 
H 3 HOH 38 338 95  HOH HOH C . 
H 3 HOH 39 339 154 HOH HOH C . 
H 3 HOH 40 340 128 HOH HOH C . 
H 3 HOH 41 341 85  HOH HOH C . 
H 3 HOH 42 342 140 HOH HOH C . 
H 3 HOH 43 343 97  HOH HOH C . 
H 3 HOH 44 344 93  HOH HOH C . 
H 3 HOH 45 345 91  HOH HOH C . 
H 3 HOH 46 346 25  HOH HOH C . 
H 3 HOH 47 347 30  HOH HOH C . 
H 3 HOH 48 348 153 HOH HOH C . 
H 3 HOH 49 349 121 HOH HOH C . 
H 3 HOH 50 350 135 HOH HOH C . 
H 3 HOH 51 351 77  HOH HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NG7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.548 
_cell.length_a_esd                 ? 
_cell.length_b                     87.682 
_cell.length_b_esd                 ? 
_cell.length_c                     153.964 
_cell.length_c_esd                 ? 
_cell.volume                       682391.502 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9NG7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NG7 
_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             1.54 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          19.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium acetate 20% w/v PEG 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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 EIGER2 S 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         2022-06-09 
_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   1.13 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          18.24 
_reflns.entry_id                                       9NG7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     32217 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.66 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1575 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.346 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               25.17 
_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                                 9NG7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             28.92 
_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                     31857 
_refine.ls_number_reflns_R_free                  3005 
_refine.ls_number_reflns_R_work                  44045 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    76.21 
_refine.ls_percent_reflns_R_free                 6.39 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1923 
_refine.ls_R_factor_R_free                       0.2310 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1897 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.0813 
_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                            0.1678 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        28.92 
_refine_hist.number_atoms_solvent             155 
_refine_hist.number_atoms_total               2962 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2799 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         8 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0069  ? 2868 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8783  ? 3879 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0557  ? 417  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 515  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.3045 ? 1032 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.82  . . 85  1200 43.52  . . . . 0.2658 . . . . . . . . . . . . . . . 0.2675 
'X-RAY DIFFRACTION' 1.82 1.86  . . 94  1320 48.10  . . . . 0.2530 . . . . . . . . . . . . . . . 0.3078 
'X-RAY DIFFRACTION' 1.86 1.89  . . 86  1338 49.15  . . . . 0.2495 . . . . . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 1.89 1.93  . . 93  1396 50.36  . . . . 0.2418 . . . . . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 1.93 1.97  . . 95  1407 51.26  . . . . 0.2292 . . . . . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 1.97 2.01  . . 97  1442 52.24  . . . . 0.2109 . . . . . . . . . . . . . . . 0.2594 
'X-RAY DIFFRACTION' 2.01 2.06  . . 94  1453 52.78  . . . . 0.2072 . . . . . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 2.06 2.11  . . 101 1571 55.83  . . . . 0.2016 . . . . . . . . . . . . . . . 0.2489 
'X-RAY DIFFRACTION' 2.11 2.16  . . 112 1629 59.97  . . . . 0.1889 . . . . . . . . . . . . . . . 0.2621 
'X-RAY DIFFRACTION' 2.16 2.23  . . 143 1942 70.39  . . . . 0.1812 . . . . . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 2.23 2.30  . . 155 2250 80.38  . . . . 0.1843 . . . . . . . . . . . . . . . 0.2199 
'X-RAY DIFFRACTION' 2.30 2.38  . . 161 2475 91.81  . . . . 0.1818 . . . . . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 2.38 2.48  . . 186 2635 98.05  . . . . 0.1886 . . . . . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 2.48 2.59  . . 190 2761 99.33  . . . . 0.1851 . . . . . . . . . . . . . . . 0.2544 
'X-RAY DIFFRACTION' 2.59 2.73  . . 184 2763 99.56  . . . . 0.1835 . . . . . . . . . . . . . . . 0.2664 
'X-RAY DIFFRACTION' 2.73 2.90  . . 183 2740 100.00 . . . . 0.1889 . . . . . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 2.90 3.12  . . 191 2765 99.97  . . . . 0.1950 . . . . . . . . . . . . . . . 0.2079 
'X-RAY DIFFRACTION' 3.12 3.43  . . 181 2723 99.05  . . . . 0.1793 . . . . . . . . . . . . . . . 0.2574 
'X-RAY DIFFRACTION' 3.43 3.93  . . 198 2757 99.86  . . . . 0.1763 . . . . . . . . . . . . . . . 0.2091 
'X-RAY DIFFRACTION' 3.93 4.94  . . 186 2746 99.97  . . . . 0.1665 . . . . . . . . . . . . . . . 0.1865 
'X-RAY DIFFRACTION' 4.95 28.92 . . 190 2732 99.25  . . . . 0.2166 . . . . . . . . . . . . . . . 0.2489 
# 
_struct.entry_id                     9NG7 
_struct.title                        'cis-CaaD H28A mutant' 
_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        9NG7 
_struct_keywords.text            'Tautomerase, cis-CaaD, acetylenecaarboxylic acid, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q6VPE5_9CORY 
_struct_ref.pdbx_db_accession          Q6VPE5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRT
;
_struct_ref.pdbx_align_begin           2 
# 
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 9NG7 A 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
2 1 9NG7 B 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
3 1 9NG7 C 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
# 
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 9NG7 ALA A 28  ? UNP Q6VPE5 HIS 29 'engineered mutation' 28  1  
1 9NG7 GLU A 150 ? UNP Q6VPE5 ?   ?  'expression tag'      150 2  
1 9NG7 ASN A 151 ? UNP Q6VPE5 ?   ?  'expression tag'      151 3  
1 9NG7 LEU A 152 ? UNP Q6VPE5 ?   ?  'expression tag'      152 4  
1 9NG7 TYR A 153 ? UNP Q6VPE5 ?   ?  'expression tag'      153 5  
1 9NG7 PHE A 154 ? UNP Q6VPE5 ?   ?  'expression tag'      154 6  
1 9NG7 GLN A 155 ? UNP Q6VPE5 ?   ?  'expression tag'      155 7  
1 9NG7 GLY A 156 ? UNP Q6VPE5 ?   ?  'expression tag'      156 8  
1 9NG7 LEU A 157 ? UNP Q6VPE5 ?   ?  'expression tag'      157 9  
1 9NG7 GLU A 158 ? UNP Q6VPE5 ?   ?  'expression tag'      158 10 
1 9NG7 HIS A 159 ? UNP Q6VPE5 ?   ?  'expression tag'      159 11 
1 9NG7 HIS A 160 ? UNP Q6VPE5 ?   ?  'expression tag'      160 12 
1 9NG7 HIS A 161 ? UNP Q6VPE5 ?   ?  'expression tag'      161 13 
1 9NG7 HIS A 162 ? UNP Q6VPE5 ?   ?  'expression tag'      162 14 
1 9NG7 HIS A 163 ? UNP Q6VPE5 ?   ?  'expression tag'      163 15 
1 9NG7 HIS A 164 ? UNP Q6VPE5 ?   ?  'expression tag'      164 16 
2 9NG7 ALA B 28  ? UNP Q6VPE5 HIS 29 'engineered mutation' 28  17 
2 9NG7 GLU B 150 ? UNP Q6VPE5 ?   ?  'expression tag'      150 18 
2 9NG7 ASN B 151 ? UNP Q6VPE5 ?   ?  'expression tag'      151 19 
2 9NG7 LEU B 152 ? UNP Q6VPE5 ?   ?  'expression tag'      152 20 
2 9NG7 TYR B 153 ? UNP Q6VPE5 ?   ?  'expression tag'      153 21 
2 9NG7 PHE B 154 ? UNP Q6VPE5 ?   ?  'expression tag'      154 22 
2 9NG7 GLN B 155 ? UNP Q6VPE5 ?   ?  'expression tag'      155 23 
2 9NG7 GLY B 156 ? UNP Q6VPE5 ?   ?  'expression tag'      156 24 
2 9NG7 LEU B 157 ? UNP Q6VPE5 ?   ?  'expression tag'      157 25 
2 9NG7 GLU B 158 ? UNP Q6VPE5 ?   ?  'expression tag'      158 26 
2 9NG7 HIS B 159 ? UNP Q6VPE5 ?   ?  'expression tag'      159 27 
2 9NG7 HIS B 160 ? UNP Q6VPE5 ?   ?  'expression tag'      160 28 
2 9NG7 HIS B 161 ? UNP Q6VPE5 ?   ?  'expression tag'      161 29 
2 9NG7 HIS B 162 ? UNP Q6VPE5 ?   ?  'expression tag'      162 30 
2 9NG7 HIS B 163 ? UNP Q6VPE5 ?   ?  'expression tag'      163 31 
2 9NG7 HIS B 164 ? UNP Q6VPE5 ?   ?  'expression tag'      164 32 
3 9NG7 ALA C 28  ? UNP Q6VPE5 HIS 29 'engineered mutation' 28  33 
3 9NG7 GLU C 150 ? UNP Q6VPE5 ?   ?  'expression tag'      150 34 
3 9NG7 ASN C 151 ? UNP Q6VPE5 ?   ?  'expression tag'      151 35 
3 9NG7 LEU C 152 ? UNP Q6VPE5 ?   ?  'expression tag'      152 36 
3 9NG7 TYR C 153 ? UNP Q6VPE5 ?   ?  'expression tag'      153 37 
3 9NG7 PHE C 154 ? UNP Q6VPE5 ?   ?  'expression tag'      154 38 
3 9NG7 GLN C 155 ? UNP Q6VPE5 ?   ?  'expression tag'      155 39 
3 9NG7 GLY C 156 ? UNP Q6VPE5 ?   ?  'expression tag'      156 40 
3 9NG7 LEU C 157 ? UNP Q6VPE5 ?   ?  'expression tag'      157 41 
3 9NG7 GLU C 158 ? UNP Q6VPE5 ?   ?  'expression tag'      158 42 
3 9NG7 HIS C 159 ? UNP Q6VPE5 ?   ?  'expression tag'      159 43 
3 9NG7 HIS C 160 ? UNP Q6VPE5 ?   ?  'expression tag'      160 44 
3 9NG7 HIS C 161 ? UNP Q6VPE5 ?   ?  'expression tag'      161 45 
3 9NG7 HIS C 162 ? UNP Q6VPE5 ?   ?  'expression tag'      162 46 
3 9NG7 HIS C 163 ? UNP Q6VPE5 ?   ?  'expression tag'      163 47 
3 9NG7 HIS C 164 ? UNP Q6VPE5 ?   ?  'expression tag'      164 48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7890  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  13540 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 THR A 13  ? GLY A 33  ? THR A 13  GLY A 33  1 ? 21 
HELX_P HELX_P2  AA2 GLN A 35  ? LEU A 38  ? GLN A 35  LEU A 38  5 ? 4  
HELX_P HELX_P3  AA3 SER A 74  ? ALA A 93  ? SER A 74  ALA A 93  1 ? 20 
HELX_P HELX_P4  AA4 ASP A 96  ? LYS A 98  ? ASP A 96  LYS A 98  5 ? 3  
HELX_P HELX_P5  AA5 PRO A 108 ? GLN A 110 ? PRO A 108 GLN A 110 5 ? 3  
HELX_P HELX_P6  AA6 THR B 13  ? GLY B 33  ? THR B 13  GLY B 33  1 ? 21 
HELX_P HELX_P7  AA7 GLN B 35  ? LEU B 38  ? GLN B 35  LEU B 38  5 ? 4  
HELX_P HELX_P8  AA8 SER B 74  ? GLU B 94  ? SER B 74  GLU B 94  1 ? 21 
HELX_P HELX_P9  AA9 ASP B 96  ? LYS B 98  ? ASP B 96  LYS B 98  5 ? 3  
HELX_P HELX_P10 AB1 PRO B 108 ? GLN B 110 ? PRO B 108 GLN B 110 5 ? 3  
HELX_P HELX_P11 AB2 THR C 13  ? LEU C 31  ? THR C 13  LEU C 31  1 ? 19 
HELX_P HELX_P12 AB3 GLN C 35  ? LEU C 38  ? GLN C 35  LEU C 38  5 ? 4  
HELX_P HELX_P13 AB4 SER C 74  ? GLU C 94  ? SER C 74  GLU C 94  1 ? 21 
HELX_P HELX_P14 AB5 ASP C 96  ? LYS C 98  ? ASP C 96  LYS C 98  5 ? 3  
HELX_P HELX_P15 AB6 PRO C 108 ? GLN C 110 ? PRO C 108 GLN C 110 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL B 56  ? GLN B 57  ? VAL B 56  GLN B 57  
AA1 2 VAL B 51  ? LEU B 53  ? VAL B 51  LEU B 53  
AA1 3 GLN A 40  ? GLN A 46  ? GLN A 40  GLN A 46  
AA1 4 VAL A 2   ? SER A 8   ? VAL A 2   SER A 8   
AA1 5 ILE A 63  ? ARG A 70  ? ILE A 63  ARG A 70  
AA1 6 ILE A 100 ? MET A 107 ? ILE A 100 MET A 107 
AA1 7 MET C 112 ? GLU C 114 ? MET C 112 GLU C 114 
AA1 8 ARG C 117 ? PHE C 118 ? ARG C 117 PHE C 118 
AA2 1 VAL A 56  ? GLN A 57  ? VAL A 56  GLN A 57  
AA2 2 VAL A 51  ? LEU A 53  ? VAL A 51  LEU A 53  
AA2 3 GLN C 40  ? GLN C 46  ? GLN C 40  GLN C 46  
AA2 4 VAL C 2   ? SER C 8   ? VAL C 2   SER C 8   
AA2 5 ILE C 63  ? ARG C 70  ? ILE C 63  ARG C 70  
AA2 6 ILE C 100 ? MET C 107 ? ILE C 100 MET C 107 
AA2 7 MET B 112 ? GLU B 114 ? MET B 112 GLU B 114 
AA2 8 ARG B 117 ? PHE B 118 ? ARG B 117 PHE B 118 
AA3 1 ARG A 117 ? PHE A 118 ? ARG A 117 PHE A 118 
AA3 2 MET A 112 ? GLU A 114 ? MET A 112 GLU A 114 
AA3 3 ILE B 100 ? MET B 107 ? ILE B 100 MET B 107 
AA3 4 ILE B 63  ? ARG B 70  ? ILE B 63  ARG B 70  
AA3 5 VAL B 2   ? SER B 8   ? VAL B 2   SER B 8   
AA3 6 GLN B 40  ? GLN B 46  ? GLN B 40  GLN B 46  
AA3 7 VAL C 51  ? LEU C 53  ? VAL C 51  LEU C 53  
AA3 8 VAL C 56  ? GLN C 57  ? VAL C 56  GLN C 57  
# 
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 B 56  ? O VAL B 56  N LEU B 53  ? N LEU B 53  
AA1 2 3 O PHE B 52  ? O PHE B 52  N VAL A 41  ? N VAL A 41  
AA1 3 4 O GLN A 40  ? O GLN A 40  N TYR A 3   ? N TYR A 3   
AA1 4 5 N TYR A 6   ? N TYR A 6   O PHE A 64  ? O PHE A 64  
AA1 5 6 N GLY A 67  ? N GLY A 67  O GLY A 105 ? O GLY A 105 
AA1 6 7 N VAL A 102 ? N VAL A 102 O VAL C 113 ? O VAL C 113 
AA1 7 8 N GLU C 114 ? N GLU C 114 O ARG C 117 ? O ARG C 117 
AA2 1 2 O VAL A 56  ? O VAL A 56  N LEU A 53  ? N LEU A 53  
AA2 2 3 N PHE A 52  ? N PHE A 52  O VAL C 41  ? O VAL C 41  
AA2 3 4 O GLN C 40  ? O GLN C 40  N TYR C 3   ? N TYR C 3   
AA2 4 5 N TYR C 6   ? N TYR C 6   O PHE C 64  ? O PHE C 64  
AA2 5 6 N VAL C 65  ? N VAL C 65  O TRP C 101 ? O TRP C 101 
AA2 6 7 O VAL C 102 ? O VAL C 102 N VAL B 113 ? N VAL B 113 
AA2 7 8 N GLU B 114 ? N GLU B 114 O ARG B 117 ? O ARG B 117 
AA3 1 2 O ARG A 117 ? O ARG A 117 N GLU A 114 ? N GLU A 114 
AA3 2 3 N VAL A 113 ? N VAL A 113 O VAL B 102 ? O VAL B 102 
AA3 3 4 O GLY B 105 ? O GLY B 105 N HIS B 69  ? N HIS B 69  
AA3 4 5 O PHE B 64  ? O PHE B 64  N TYR B 6   ? N TYR B 6   
AA3 5 6 N TYR B 3   ? N TYR B 3   O ASN B 42  ? O ASN B 42  
AA3 6 7 N VAL B 41  ? N VAL B 41  O PHE C 52  ? O PHE C 52  
AA3 7 8 N LEU C 53  ? N LEU C 53  O VAL C 56  ? O VAL C 56  
# 
_pdbx_entry_details.entry_id                   9NG7 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     35 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -49.34 
_pdbx_validate_torsion.psi             153.05 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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 GLN 121 ? A GLN 121 
2   1 Y 1 A PRO 122 ? A PRO 122 
3   1 Y 1 A GLY 123 ? A GLY 123 
4   1 Y 1 A HIS 124 ? A HIS 124 
5   1 Y 1 A GLU 125 ? A GLU 125 
6   1 Y 1 A GLY 126 ? A GLY 126 
7   1 Y 1 A GLU 127 ? A GLU 127 
8   1 Y 1 A TRP 128 ? A TRP 128 
9   1 Y 1 A PHE 129 ? A PHE 129 
10  1 Y 1 A ASP 130 ? A ASP 130 
11  1 Y 1 A ASN 131 ? A ASN 131 
12  1 Y 1 A LEU 132 ? A LEU 132 
13  1 Y 1 A SER 133 ? A SER 133 
14  1 Y 1 A SER 134 ? A SER 134 
15  1 Y 1 A ASP 135 ? A ASP 135 
16  1 Y 1 A GLU 136 ? A GLU 136 
17  1 Y 1 A ARG 137 ? A ARG 137 
18  1 Y 1 A ALA 138 ? A ALA 138 
19  1 Y 1 A PHE 139 ? A PHE 139 
20  1 Y 1 A MET 140 ? A MET 140 
21  1 Y 1 A GLU 141 ? A GLU 141 
22  1 Y 1 A THR 142 ? A THR 142 
23  1 Y 1 A ASN 143 ? A ASN 143 
24  1 Y 1 A VAL 144 ? A VAL 144 
25  1 Y 1 A ASP 145 ? A ASP 145 
26  1 Y 1 A VAL 146 ? A VAL 146 
27  1 Y 1 A SER 147 ? A SER 147 
28  1 Y 1 A ARG 148 ? A ARG 148 
29  1 Y 1 A THR 149 ? A THR 149 
30  1 Y 1 A GLU 150 ? A GLU 150 
31  1 Y 1 A ASN 151 ? A ASN 151 
32  1 Y 1 A LEU 152 ? A LEU 152 
33  1 Y 1 A TYR 153 ? A TYR 153 
34  1 Y 1 A PHE 154 ? A PHE 154 
35  1 Y 1 A GLN 155 ? A GLN 155 
36  1 Y 1 A GLY 156 ? A GLY 156 
37  1 Y 1 A LEU 157 ? A LEU 157 
38  1 Y 1 A GLU 158 ? A GLU 158 
39  1 Y 1 A HIS 159 ? A HIS 159 
40  1 Y 1 A HIS 160 ? A HIS 160 
41  1 Y 1 A HIS 161 ? A HIS 161 
42  1 Y 1 A HIS 162 ? A HIS 162 
43  1 Y 1 A HIS 163 ? A HIS 163 
44  1 Y 1 A HIS 164 ? A HIS 164 
45  1 Y 1 B GLN 121 ? B GLN 121 
46  1 Y 1 B PRO 122 ? B PRO 122 
47  1 Y 1 B GLY 123 ? B GLY 123 
48  1 Y 1 B HIS 124 ? B HIS 124 
49  1 Y 1 B GLU 125 ? B GLU 125 
50  1 Y 1 B GLY 126 ? B GLY 126 
51  1 Y 1 B GLU 127 ? B GLU 127 
52  1 Y 1 B TRP 128 ? B TRP 128 
53  1 Y 1 B PHE 129 ? B PHE 129 
54  1 Y 1 B ASP 130 ? B ASP 130 
55  1 Y 1 B ASN 131 ? B ASN 131 
56  1 Y 1 B LEU 132 ? B LEU 132 
57  1 Y 1 B SER 133 ? B SER 133 
58  1 Y 1 B SER 134 ? B SER 134 
59  1 Y 1 B ASP 135 ? B ASP 135 
60  1 Y 1 B GLU 136 ? B GLU 136 
61  1 Y 1 B ARG 137 ? B ARG 137 
62  1 Y 1 B ALA 138 ? B ALA 138 
63  1 Y 1 B PHE 139 ? B PHE 139 
64  1 Y 1 B MET 140 ? B MET 140 
65  1 Y 1 B GLU 141 ? B GLU 141 
66  1 Y 1 B THR 142 ? B THR 142 
67  1 Y 1 B ASN 143 ? B ASN 143 
68  1 Y 1 B VAL 144 ? B VAL 144 
69  1 Y 1 B ASP 145 ? B ASP 145 
70  1 Y 1 B VAL 146 ? B VAL 146 
71  1 Y 1 B SER 147 ? B SER 147 
72  1 Y 1 B ARG 148 ? B ARG 148 
73  1 Y 1 B THR 149 ? B THR 149 
74  1 Y 1 B GLU 150 ? B GLU 150 
75  1 Y 1 B ASN 151 ? B ASN 151 
76  1 Y 1 B LEU 152 ? B LEU 152 
77  1 Y 1 B TYR 153 ? B TYR 153 
78  1 Y 1 B PHE 154 ? B PHE 154 
79  1 Y 1 B GLN 155 ? B GLN 155 
80  1 Y 1 B GLY 156 ? B GLY 156 
81  1 Y 1 B LEU 157 ? B LEU 157 
82  1 Y 1 B GLU 158 ? B GLU 158 
83  1 Y 1 B HIS 159 ? B HIS 159 
84  1 Y 1 B HIS 160 ? B HIS 160 
85  1 Y 1 B HIS 161 ? B HIS 161 
86  1 Y 1 B HIS 162 ? B HIS 162 
87  1 Y 1 B HIS 163 ? B HIS 163 
88  1 Y 1 B HIS 164 ? B HIS 164 
89  1 Y 1 C GLN 121 ? C GLN 121 
90  1 Y 1 C PRO 122 ? C PRO 122 
91  1 Y 1 C GLY 123 ? C GLY 123 
92  1 Y 1 C HIS 124 ? C HIS 124 
93  1 Y 1 C GLU 125 ? C GLU 125 
94  1 Y 1 C GLY 126 ? C GLY 126 
95  1 Y 1 C GLU 127 ? C GLU 127 
96  1 Y 1 C TRP 128 ? C TRP 128 
97  1 Y 1 C PHE 129 ? C PHE 129 
98  1 Y 1 C ASP 130 ? C ASP 130 
99  1 Y 1 C ASN 131 ? C ASN 131 
100 1 Y 1 C LEU 132 ? C LEU 132 
101 1 Y 1 C SER 133 ? C SER 133 
102 1 Y 1 C SER 134 ? C SER 134 
103 1 Y 1 C ASP 135 ? C ASP 135 
104 1 Y 1 C GLU 136 ? C GLU 136 
105 1 Y 1 C ARG 137 ? C ARG 137 
106 1 Y 1 C ALA 138 ? C ALA 138 
107 1 Y 1 C PHE 139 ? C PHE 139 
108 1 Y 1 C MET 140 ? C MET 140 
109 1 Y 1 C GLU 141 ? C GLU 141 
110 1 Y 1 C THR 142 ? C THR 142 
111 1 Y 1 C ASN 143 ? C ASN 143 
112 1 Y 1 C VAL 144 ? C VAL 144 
113 1 Y 1 C ASP 145 ? C ASP 145 
114 1 Y 1 C VAL 146 ? C VAL 146 
115 1 Y 1 C SER 147 ? C SER 147 
116 1 Y 1 C ARG 148 ? C ARG 148 
117 1 Y 1 C THR 149 ? C THR 149 
118 1 Y 1 C GLU 150 ? C GLU 150 
119 1 Y 1 C ASN 151 ? C ASN 151 
120 1 Y 1 C LEU 152 ? C LEU 152 
121 1 Y 1 C TYR 153 ? C TYR 153 
122 1 Y 1 C PHE 154 ? C PHE 154 
123 1 Y 1 C GLN 155 ? C GLN 155 
124 1 Y 1 C GLY 156 ? C GLY 156 
125 1 Y 1 C LEU 157 ? C LEU 157 
126 1 Y 1 C GLU 158 ? C GLU 158 
127 1 Y 1 C HIS 159 ? C HIS 159 
128 1 Y 1 C HIS 160 ? C HIS 160 
129 1 Y 1 C HIS 161 ? C HIS 161 
130 1 Y 1 C HIS 162 ? C HIS 162 
131 1 Y 1 C HIS 163 ? C HIS 163 
132 1 Y 1 C HIS 164 ? C HIS 164 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
GLN N    N N N 81  
GLN CA   C N S 82  
GLN C    C N N 83  
GLN O    O N N 84  
GLN CB   C N N 85  
GLN CG   C N N 86  
GLN CD   C N N 87  
GLN OE1  O N N 88  
GLN NE2  N N N 89  
GLN OXT  O N N 90  
GLN H    H N N 91  
GLN H2   H N N 92  
GLN HA   H N N 93  
GLN HB2  H N N 94  
GLN HB3  H N N 95  
GLN HG2  H N N 96  
GLN HG3  H N N 97  
GLN HE21 H N N 98  
GLN HE22 H N N 99  
GLN HXT  H N N 100 
GLU N    N N N 101 
GLU CA   C N S 102 
GLU C    C N N 103 
GLU O    O N N 104 
GLU CB   C N N 105 
GLU CG   C N N 106 
GLU CD   C N N 107 
GLU OE1  O N N 108 
GLU OE2  O N N 109 
GLU OXT  O N N 110 
GLU H    H N N 111 
GLU H2   H N N 112 
GLU HA   H N N 113 
GLU HB2  H N N 114 
GLU HB3  H N N 115 
GLU HG2  H N N 116 
GLU HG3  H N N 117 
GLU HE2  H N N 118 
GLU HXT  H N N 119 
GLY N    N N N 120 
GLY CA   C N N 121 
GLY C    C N N 122 
GLY O    O N N 123 
GLY OXT  O N N 124 
GLY H    H N N 125 
GLY H2   H N N 126 
GLY HA2  H N N 127 
GLY HA3  H N N 128 
GLY HXT  H N N 129 
HIS N    N N N 130 
HIS CA   C N S 131 
HIS C    C N N 132 
HIS O    O N N 133 
HIS CB   C N N 134 
HIS CG   C Y N 135 
HIS ND1  N Y N 136 
HIS CD2  C Y N 137 
HIS CE1  C Y N 138 
HIS NE2  N Y N 139 
HIS OXT  O N N 140 
HIS H    H N N 141 
HIS H2   H N N 142 
HIS HA   H N N 143 
HIS HB2  H N N 144 
HIS HB3  H N N 145 
HIS HD1  H N N 146 
HIS HD2  H N N 147 
HIS HE1  H N N 148 
HIS HE2  H N N 149 
HIS HXT  H N N 150 
HOH O    O N N 151 
HOH H1   H N N 152 
HOH H2   H N N 153 
ILE N    N N N 154 
ILE CA   C N S 155 
ILE C    C N N 156 
ILE O    O N N 157 
ILE CB   C N S 158 
ILE CG1  C N N 159 
ILE CG2  C N N 160 
ILE CD1  C N N 161 
ILE OXT  O N N 162 
ILE H    H N N 163 
ILE H2   H N N 164 
ILE HA   H N N 165 
ILE HB   H N N 166 
ILE HG12 H N N 167 
ILE HG13 H N N 168 
ILE HG21 H N N 169 
ILE HG22 H N N 170 
ILE HG23 H N N 171 
ILE HD11 H N N 172 
ILE HD12 H N N 173 
ILE HD13 H N N 174 
ILE HXT  H N N 175 
LEU N    N N N 176 
LEU CA   C N S 177 
LEU C    C N N 178 
LEU O    O N N 179 
LEU CB   C N N 180 
LEU CG   C N N 181 
LEU CD1  C N N 182 
LEU CD2  C N N 183 
LEU OXT  O N N 184 
LEU H    H N N 185 
LEU H2   H N N 186 
LEU HA   H N N 187 
LEU HB2  H N N 188 
LEU HB3  H N N 189 
LEU HG   H N N 190 
LEU HD11 H N N 191 
LEU HD12 H N N 192 
LEU HD13 H N N 193 
LEU HD21 H N N 194 
LEU HD22 H N N 195 
LEU HD23 H N N 196 
LEU HXT  H N N 197 
LYS N    N N N 198 
LYS CA   C N S 199 
LYS C    C N N 200 
LYS O    O N N 201 
LYS CB   C N N 202 
LYS CG   C N N 203 
LYS CD   C N N 204 
LYS CE   C N N 205 
LYS NZ   N N N 206 
LYS OXT  O N N 207 
LYS H    H N N 208 
LYS H2   H N N 209 
LYS HA   H N N 210 
LYS HB2  H N N 211 
LYS HB3  H N N 212 
LYS HG2  H N N 213 
LYS HG3  H N N 214 
LYS HD2  H N N 215 
LYS HD3  H N N 216 
LYS HE2  H N N 217 
LYS HE3  H N N 218 
LYS HZ1  H N N 219 
LYS HZ2  H N N 220 
LYS HZ3  H N N 221 
LYS HXT  H N N 222 
MET N    N N N 223 
MET CA   C N S 224 
MET C    C N N 225 
MET O    O N N 226 
MET CB   C N N 227 
MET CG   C N N 228 
MET SD   S N N 229 
MET CE   C N N 230 
MET OXT  O N N 231 
MET H    H N N 232 
MET H2   H N N 233 
MET HA   H N N 234 
MET HB2  H N N 235 
MET HB3  H N N 236 
MET HG2  H N N 237 
MET HG3  H N N 238 
MET HE1  H N N 239 
MET HE2  H N N 240 
MET HE3  H N N 241 
MET HXT  H N N 242 
PHE N    N N N 243 
PHE CA   C N S 244 
PHE C    C N N 245 
PHE O    O N N 246 
PHE CB   C N N 247 
PHE CG   C Y N 248 
PHE CD1  C Y N 249 
PHE CD2  C Y N 250 
PHE CE1  C Y N 251 
PHE CE2  C Y N 252 
PHE CZ   C Y N 253 
PHE OXT  O N N 254 
PHE H    H N N 255 
PHE H2   H N N 256 
PHE HA   H N N 257 
PHE HB2  H N N 258 
PHE HB3  H N N 259 
PHE HD1  H N N 260 
PHE HD2  H N N 261 
PHE HE1  H N N 262 
PHE HE2  H N N 263 
PHE HZ   H N N 264 
PHE HXT  H N N 265 
PRO N    N N N 266 
PRO CA   C N S 267 
PRO C    C N N 268 
PRO O    O N N 269 
PRO CB   C N N 270 
PRO CG   C N N 271 
PRO CD   C N N 272 
PRO OXT  O N N 273 
PRO H    H N N 274 
PRO HA   H N N 275 
PRO HB2  H N N 276 
PRO HB3  H N N 277 
PRO HG2  H N N 278 
PRO HG3  H N N 279 
PRO HD2  H N N 280 
PRO HD3  H N N 281 
PRO HXT  H N N 282 
SER N    N N N 283 
SER CA   C N S 284 
SER C    C N N 285 
SER O    O N N 286 
SER CB   C N N 287 
SER OG   O N N 288 
SER OXT  O N N 289 
SER H    H N N 290 
SER H2   H N N 291 
SER HA   H N N 292 
SER HB2  H N N 293 
SER HB3  H N N 294 
SER HG   H N N 295 
SER HXT  H N N 296 
THR N    N N N 297 
THR CA   C N S 298 
THR C    C N N 299 
THR O    O N N 300 
THR CB   C N R 301 
THR OG1  O N N 302 
THR CG2  C N N 303 
THR OXT  O N N 304 
THR H    H N N 305 
THR H2   H N N 306 
THR HA   H N N 307 
THR HB   H N N 308 
THR HG1  H N N 309 
THR HG21 H N N 310 
THR HG22 H N N 311 
THR HG23 H N N 312 
THR HXT  H N N 313 
TRP N    N N N 314 
TRP CA   C N S 315 
TRP C    C N N 316 
TRP O    O N N 317 
TRP CB   C N N 318 
TRP CG   C Y N 319 
TRP CD1  C Y N 320 
TRP CD2  C Y N 321 
TRP NE1  N Y N 322 
TRP CE2  C Y N 323 
TRP CE3  C Y N 324 
TRP CZ2  C Y N 325 
TRP CZ3  C Y N 326 
TRP CH2  C Y N 327 
TRP OXT  O N N 328 
TRP H    H N N 329 
TRP H2   H N N 330 
TRP HA   H N N 331 
TRP HB2  H N N 332 
TRP HB3  H N N 333 
TRP HD1  H N N 334 
TRP HE1  H N N 335 
TRP HE3  H N N 336 
TRP HZ2  H N N 337 
TRP HZ3  H N N 338 
TRP HH2  H N N 339 
TRP HXT  H N N 340 
TYR N    N N N 341 
TYR CA   C N S 342 
TYR C    C N N 343 
TYR O    O N N 344 
TYR CB   C N N 345 
TYR CG   C Y N 346 
TYR CD1  C Y N 347 
TYR CD2  C Y N 348 
TYR CE1  C Y N 349 
TYR CE2  C Y N 350 
TYR CZ   C Y N 351 
TYR OH   O N N 352 
TYR OXT  O N N 353 
TYR H    H N N 354 
TYR H2   H N N 355 
TYR HA   H N N 356 
TYR HB2  H N N 357 
TYR HB3  H N N 358 
TYR HD1  H N N 359 
TYR HD2  H N N 360 
TYR HE1  H N N 361 
TYR HE2  H N N 362 
TYR HH   H N N 363 
TYR HXT  H N N 364 
VAL N    N N N 365 
VAL CA   C N S 366 
VAL C    C N N 367 
VAL O    O N N 368 
VAL CB   C N N 369 
VAL CG1  C N N 370 
VAL CG2  C N N 371 
VAL OXT  O N N 372 
VAL H    H N N 373 
VAL H2   H N N 374 
VAL HA   H N N 375 
VAL HB   H N N 376 
VAL HG11 H N N 377 
VAL HG12 H N N 378 
VAL HG13 H N N 379 
VAL HG21 H N N 380 
VAL HG22 H N N 381 
VAL HG23 H N N 382 
VAL HXT  H N N 383 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
GLN N   CA   sing N N 76  
GLN N   H    sing N N 77  
GLN N   H2   sing N N 78  
GLN CA  C    sing N N 79  
GLN CA  CB   sing N N 80  
GLN CA  HA   sing N N 81  
GLN C   O    doub N N 82  
GLN C   OXT  sing N N 83  
GLN CB  CG   sing N N 84  
GLN CB  HB2  sing N N 85  
GLN CB  HB3  sing N N 86  
GLN CG  CD   sing N N 87  
GLN CG  HG2  sing N N 88  
GLN CG  HG3  sing N N 89  
GLN CD  OE1  doub N N 90  
GLN CD  NE2  sing N N 91  
GLN NE2 HE21 sing N N 92  
GLN NE2 HE22 sing N N 93  
GLN OXT HXT  sing N N 94  
GLU N   CA   sing N N 95  
GLU N   H    sing N N 96  
GLU N   H2   sing N N 97  
GLU CA  C    sing N N 98  
GLU CA  CB   sing N N 99  
GLU CA  HA   sing N N 100 
GLU C   O    doub N N 101 
GLU C   OXT  sing N N 102 
GLU CB  CG   sing N N 103 
GLU CB  HB2  sing N N 104 
GLU CB  HB3  sing N N 105 
GLU CG  CD   sing N N 106 
GLU CG  HG2  sing N N 107 
GLU CG  HG3  sing N N 108 
GLU CD  OE1  doub N N 109 
GLU CD  OE2  sing N N 110 
GLU OE2 HE2  sing N N 111 
GLU OXT HXT  sing N N 112 
GLY N   CA   sing N N 113 
GLY N   H    sing N N 114 
GLY N   H2   sing N N 115 
GLY CA  C    sing N N 116 
GLY CA  HA2  sing N N 117 
GLY CA  HA3  sing N N 118 
GLY C   O    doub N N 119 
GLY C   OXT  sing N N 120 
GLY OXT HXT  sing N N 121 
HIS N   CA   sing N N 122 
HIS N   H    sing N N 123 
HIS N   H2   sing N N 124 
HIS CA  C    sing N N 125 
HIS CA  CB   sing N N 126 
HIS CA  HA   sing N N 127 
HIS C   O    doub N N 128 
HIS C   OXT  sing N N 129 
HIS CB  CG   sing N N 130 
HIS CB  HB2  sing N N 131 
HIS CB  HB3  sing N N 132 
HIS CG  ND1  sing Y N 133 
HIS CG  CD2  doub Y N 134 
HIS ND1 CE1  doub Y N 135 
HIS ND1 HD1  sing N N 136 
HIS CD2 NE2  sing Y N 137 
HIS CD2 HD2  sing N N 138 
HIS CE1 NE2  sing Y N 139 
HIS CE1 HE1  sing N N 140 
HIS NE2 HE2  sing N N 141 
HIS OXT HXT  sing N N 142 
HOH O   H1   sing N N 143 
HOH O   H2   sing N N 144 
ILE N   CA   sing N N 145 
ILE N   H    sing N N 146 
ILE N   H2   sing N N 147 
ILE CA  C    sing N N 148 
ILE CA  CB   sing N N 149 
ILE CA  HA   sing N N 150 
ILE C   O    doub N N 151 
ILE C   OXT  sing N N 152 
ILE CB  CG1  sing N N 153 
ILE CB  CG2  sing N N 154 
ILE CB  HB   sing N N 155 
ILE CG1 CD1  sing N N 156 
ILE CG1 HG12 sing N N 157 
ILE CG1 HG13 sing N N 158 
ILE CG2 HG21 sing N N 159 
ILE CG2 HG22 sing N N 160 
ILE CG2 HG23 sing N N 161 
ILE CD1 HD11 sing N N 162 
ILE CD1 HD12 sing N N 163 
ILE CD1 HD13 sing N N 164 
ILE OXT HXT  sing N N 165 
LEU N   CA   sing N N 166 
LEU N   H    sing N N 167 
LEU N   H2   sing N N 168 
LEU CA  C    sing N N 169 
LEU CA  CB   sing N N 170 
LEU CA  HA   sing N N 171 
LEU C   O    doub N N 172 
LEU C   OXT  sing N N 173 
LEU CB  CG   sing N N 174 
LEU CB  HB2  sing N N 175 
LEU CB  HB3  sing N N 176 
LEU CG  CD1  sing N N 177 
LEU CG  CD2  sing N N 178 
LEU CG  HG   sing N N 179 
LEU CD1 HD11 sing N N 180 
LEU CD1 HD12 sing N N 181 
LEU CD1 HD13 sing N N 182 
LEU CD2 HD21 sing N N 183 
LEU CD2 HD22 sing N N 184 
LEU CD2 HD23 sing N N 185 
LEU OXT HXT  sing N N 186 
LYS N   CA   sing N N 187 
LYS N   H    sing N N 188 
LYS N   H2   sing N N 189 
LYS CA  C    sing N N 190 
LYS CA  CB   sing N N 191 
LYS CA  HA   sing N N 192 
LYS C   O    doub N N 193 
LYS C   OXT  sing N N 194 
LYS CB  CG   sing N N 195 
LYS CB  HB2  sing N N 196 
LYS CB  HB3  sing N N 197 
LYS CG  CD   sing N N 198 
LYS CG  HG2  sing N N 199 
LYS CG  HG3  sing N N 200 
LYS CD  CE   sing N N 201 
LYS CD  HD2  sing N N 202 
LYS CD  HD3  sing N N 203 
LYS CE  NZ   sing N N 204 
LYS CE  HE2  sing N N 205 
LYS CE  HE3  sing N N 206 
LYS NZ  HZ1  sing N N 207 
LYS NZ  HZ2  sing N N 208 
LYS NZ  HZ3  sing N N 209 
LYS OXT HXT  sing N N 210 
MET N   CA   sing N N 211 
MET N   H    sing N N 212 
MET N   H2   sing N N 213 
MET CA  C    sing N N 214 
MET CA  CB   sing N N 215 
MET CA  HA   sing N N 216 
MET C   O    doub N N 217 
MET C   OXT  sing N N 218 
MET CB  CG   sing N N 219 
MET CB  HB2  sing N N 220 
MET CB  HB3  sing N N 221 
MET CG  SD   sing N N 222 
MET CG  HG2  sing N N 223 
MET CG  HG3  sing N N 224 
MET SD  CE   sing N N 225 
MET CE  HE1  sing N N 226 
MET CE  HE2  sing N N 227 
MET CE  HE3  sing N N 228 
MET OXT HXT  sing N N 229 
PHE N   CA   sing N N 230 
PHE N   H    sing N N 231 
PHE N   H2   sing N N 232 
PHE CA  C    sing N N 233 
PHE CA  CB   sing N N 234 
PHE CA  HA   sing N N 235 
PHE C   O    doub N N 236 
PHE C   OXT  sing N N 237 
PHE CB  CG   sing N N 238 
PHE CB  HB2  sing N N 239 
PHE CB  HB3  sing N N 240 
PHE CG  CD1  doub Y N 241 
PHE CG  CD2  sing Y N 242 
PHE CD1 CE1  sing Y N 243 
PHE CD1 HD1  sing N N 244 
PHE CD2 CE2  doub Y N 245 
PHE CD2 HD2  sing N N 246 
PHE CE1 CZ   doub Y N 247 
PHE CE1 HE1  sing N N 248 
PHE CE2 CZ   sing Y N 249 
PHE CE2 HE2  sing N N 250 
PHE CZ  HZ   sing N N 251 
PHE OXT HXT  sing N N 252 
PRO N   CA   sing N N 253 
PRO N   CD   sing N N 254 
PRO N   H    sing N N 255 
PRO CA  C    sing N N 256 
PRO CA  CB   sing N N 257 
PRO CA  HA   sing N N 258 
PRO C   O    doub N N 259 
PRO C   OXT  sing N N 260 
PRO CB  CG   sing N N 261 
PRO CB  HB2  sing N N 262 
PRO CB  HB3  sing N N 263 
PRO CG  CD   sing N N 264 
PRO CG  HG2  sing N N 265 
PRO CG  HG3  sing N N 266 
PRO CD  HD2  sing N N 267 
PRO CD  HD3  sing N N 268 
PRO OXT HXT  sing N N 269 
SER N   CA   sing N N 270 
SER N   H    sing N N 271 
SER N   H2   sing N N 272 
SER CA  C    sing N N 273 
SER CA  CB   sing N N 274 
SER CA  HA   sing N N 275 
SER C   O    doub N N 276 
SER C   OXT  sing N N 277 
SER CB  OG   sing N N 278 
SER CB  HB2  sing N N 279 
SER CB  HB3  sing N N 280 
SER OG  HG   sing N N 281 
SER OXT HXT  sing N N 282 
THR N   CA   sing N N 283 
THR N   H    sing N N 284 
THR N   H2   sing N N 285 
THR CA  C    sing N N 286 
THR CA  CB   sing N N 287 
THR CA  HA   sing N N 288 
THR C   O    doub N N 289 
THR C   OXT  sing N N 290 
THR CB  OG1  sing N N 291 
THR CB  CG2  sing N N 292 
THR CB  HB   sing N N 293 
THR OG1 HG1  sing N N 294 
THR CG2 HG21 sing N N 295 
THR CG2 HG22 sing N N 296 
THR CG2 HG23 sing N N 297 
THR OXT HXT  sing N N 298 
TRP N   CA   sing N N 299 
TRP N   H    sing N N 300 
TRP N   H2   sing N N 301 
TRP CA  C    sing N N 302 
TRP CA  CB   sing N N 303 
TRP CA  HA   sing N N 304 
TRP C   O    doub N N 305 
TRP C   OXT  sing N N 306 
TRP CB  CG   sing N N 307 
TRP CB  HB2  sing N N 308 
TRP CB  HB3  sing N N 309 
TRP CG  CD1  doub Y N 310 
TRP CG  CD2  sing Y N 311 
TRP CD1 NE1  sing Y N 312 
TRP CD1 HD1  sing N N 313 
TRP CD2 CE2  doub Y N 314 
TRP CD2 CE3  sing Y N 315 
TRP NE1 CE2  sing Y N 316 
TRP NE1 HE1  sing N N 317 
TRP CE2 CZ2  sing Y N 318 
TRP CE3 CZ3  doub Y N 319 
TRP CE3 HE3  sing N N 320 
TRP CZ2 CH2  doub Y N 321 
TRP CZ2 HZ2  sing N N 322 
TRP CZ3 CH2  sing Y N 323 
TRP CZ3 HZ3  sing N N 324 
TRP CH2 HH2  sing N N 325 
TRP OXT HXT  sing N N 326 
TYR N   CA   sing N N 327 
TYR N   H    sing N N 328 
TYR N   H2   sing N N 329 
TYR CA  C    sing N N 330 
TYR CA  CB   sing N N 331 
TYR CA  HA   sing N N 332 
TYR C   O    doub N N 333 
TYR C   OXT  sing N N 334 
TYR CB  CG   sing N N 335 
TYR CB  HB2  sing N N 336 
TYR CB  HB3  sing N N 337 
TYR CG  CD1  doub Y N 338 
TYR CG  CD2  sing Y N 339 
TYR CD1 CE1  sing Y N 340 
TYR CD1 HD1  sing N N 341 
TYR CD2 CE2  doub Y N 342 
TYR CD2 HD2  sing N N 343 
TYR CE1 CZ   doub Y N 344 
TYR CE1 HE1  sing N N 345 
TYR CE2 CZ   sing Y N 346 
TYR CE2 HE2  sing N N 347 
TYR CZ  OH   sing N N 348 
TYR OH  HH   sing N N 349 
TYR OXT HXT  sing N N 350 
VAL N   CA   sing N N 351 
VAL N   H    sing N N 352 
VAL N   H2   sing N N 353 
VAL CA  C    sing N N 354 
VAL CA  CB   sing N N 355 
VAL CA  HA   sing N N 356 
VAL C   O    doub N N 357 
VAL C   OXT  sing N N 358 
VAL CB  CG1  sing N N 359 
VAL CB  CG2  sing N N 360 
VAL CB  HB   sing N N 361 
VAL CG1 HG11 sing N N 362 
VAL CG1 HG12 sing N N 363 
VAL CG1 HG13 sing N N 364 
VAL CG2 HG21 sing N N 365 
VAL CG2 HG22 sing N N 366 
VAL CG2 HG23 sing N N 367 
VAL OXT HXT  sing N N 368 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3MF8 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9NG7 
_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]   0.019783 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011405 
_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]   0.006495 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 1   ? 6.70100   26.80200  -24.09200 1.000 24.75299 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 1   ? 6.54600   25.36900  -23.81800 1.000 18.76933 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 1   ? 6.28000   25.08400  -22.34700 1.000 18.39418 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 1   ? 6.58600   25.91000  -21.47300 1.000 17.62750 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 1   ? 7.89300   24.78000  -24.23600 1.000 16.38885 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 8.86200   25.92100  -24.04700 1.000 24.00285 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 8.08800   27.14100  -24.45900 1.000 27.81448 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 2   ? 5.70500   23.91600  -22.09800 1.000 12.99095 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 2   ? 5.48200   23.39600  -20.75600 1.000 12.95982 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 2   ? 6.21500   22.07400  -20.65300 1.000 13.24557 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 2   ? 6.00000   21.18100  -21.48300 1.000 10.79679 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 2   ? 3.98300   23.19400  -20.44900 1.000 13.49876 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 2   ? 3.80800   22.52300  -19.07000 1.000 13.17918 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 2   ? 3.23000   24.52800  -20.51700 1.000 13.02092 ? 2   VAL A CG2 1 
ATOM   15   N N   . TYR A 1 3   ? 7.06600   21.94100  -19.63100 1.000 9.64183  ? 3   TYR A N   1 
ATOM   16   C CA  . TYR A 1 3   ? 7.71900   20.67900  -19.30800 1.000 9.75327  ? 3   TYR A CA  1 
ATOM   17   C C   . TYR A 1 3   ? 7.10400   20.13500  -18.02900 1.000 10.53680 ? 3   TYR A C   1 
ATOM   18   O O   . TYR A 1 3   ? 7.31400   20.69700  -16.94600 1.000 12.10330 ? 3   TYR A O   1 
ATOM   19   C CB  . TYR A 1 3   ? 9.22100   20.85700  -19.14300 1.000 11.55859 ? 3   TYR A CB  1 
ATOM   20   C CG  . TYR A 1 3   ? 9.87700   21.28200  -20.42500 1.000 11.51995 ? 3   TYR A CG  1 
ATOM   21   C CD1 . TYR A 1 3   ? 10.32800  20.34400  -21.34300 1.000 14.15027 ? 3   TYR A CD1 1 
ATOM   22   C CD2 . TYR A 1 3   ? 10.00900  22.63000  -20.73500 1.000 12.56448 ? 3   TYR A CD2 1 
ATOM   23   C CE1 . TYR A 1 3   ? 10.92100  20.75100  -22.53700 1.000 15.42852 ? 3   TYR A CE1 1 
ATOM   24   C CE2 . TYR A 1 3   ? 10.59000  23.03800  -21.90800 1.000 13.48920 ? 3   TYR A CE2 1 
ATOM   25   C CZ  . TYR A 1 3   ? 11.04100  22.10200  -22.79900 1.000 19.76912 ? 3   TYR A CZ  1 
ATOM   26   O OH  . TYR A 1 3   ? 11.62200  22.55200  -23.95700 1.000 22.70804 ? 3   TYR A OH  1 
ATOM   27   N N   . MET A 1 4   ? 6.33200   19.05800  -18.15900 1.000 10.13006 ? 4   MET A N   1 
ATOM   28   C CA  . MET A 1 4   ? 5.81400   18.32600  -17.01000 1.000 8.33186  ? 4   MET A CA  1 
ATOM   29   C C   . MET A 1 4   ? 6.89300   17.36200  -16.53400 1.000 11.38380 ? 4   MET A C   1 
ATOM   30   O O   . MET A 1 4   ? 7.35100   16.52000  -17.31300 1.000 9.54010  ? 4   MET A O   1 
ATOM   31   C CB  . MET A 1 4   ? 4.54000   17.57400  -17.40700 1.000 9.36786  ? 4   MET A CB  1 
ATOM   32   C CG  . MET A 1 4   ? 3.49900   18.44000  -18.14300 1.000 10.59418 ? 4   MET A CG  1 
ATOM   33   S SD  . MET A 1 4   ? 2.86500   19.73900  -17.04700 1.000 12.78654 ? 4   MET A SD  1 
ATOM   34   C CE  . MET A 1 4   ? 2.36600   18.75600  -15.66600 1.000 9.77048  ? 4   MET A CE  1 
ATOM   35   N N   . VAL A 1 5   ? 7.30900   17.48000  -15.26900 1.000 9.03234  ? 5   VAL A N   1 
ATOM   36   C CA  . VAL A 1 5   ? 8.44500   16.71900  -14.75000 1.000 8.72410  ? 5   VAL A CA  1 
ATOM   37   C C   . VAL A 1 5   ? 7.94400   15.81000  -13.63300 1.000 9.61164  ? 5   VAL A C   1 
ATOM   38   O O   . VAL A 1 5   ? 7.64000   16.27100  -12.52200 1.000 9.57258  ? 5   VAL A O   1 
ATOM   39   C CB  . VAL A 1 5   ? 9.58900   17.63400  -14.27300 1.000 12.00579 ? 5   VAL A CB  1 
ATOM   40   C CG1 . VAL A 1 5   ? 10.78400  16.78900  -13.81600 1.000 10.48403 ? 5   VAL A CG1 1 
ATOM   41   C CG2 . VAL A 1 5   ? 10.02500  18.55500  -15.41000 1.000 9.72140  ? 5   VAL A CG2 1 
ATOM   42   N N   . TYR A 1 6   ? 7.88100   14.50800  -13.91800 1.000 9.34415  ? 6   TYR A N   1 
ATOM   43   C CA  . TYR A 1 6   ? 7.32800   13.52200  -12.99700 1.000 9.32291  ? 6   TYR A CA  1 
ATOM   44   C C   . TYR A 1 6   ? 8.45400   12.90200  -12.17400 1.000 11.84560 ? 6   TYR A C   1 
ATOM   45   O O   . TYR A 1 6   ? 9.33100   12.22800  -12.72100 1.000 11.70240 ? 6   TYR A O   1 
ATOM   46   C CB  . TYR A 1 6   ? 6.57700   12.44200  -13.77300 1.000 10.58186 ? 6   TYR A CB  1 
ATOM   47   C CG  . TYR A 1 6   ? 5.46900   13.05100  -14.58400 1.000 8.86122  ? 6   TYR A CG  1 
ATOM   48   C CD1 . TYR A 1 6   ? 4.23900   13.34100  -13.99400 1.000 10.01578 ? 6   TYR A CD1 1 
ATOM   49   C CD2 . TYR A 1 6   ? 5.66100   13.37500  -15.92200 1.000 10.42795 ? 6   TYR A CD2 1 
ATOM   50   C CE1 . TYR A 1 6   ? 3.21400   13.92600  -14.73100 1.000 9.48825  ? 6   TYR A CE1 1 
ATOM   51   C CE2 . TYR A 1 6   ? 4.63400   13.95800  -16.67300 1.000 8.89498  ? 6   TYR A CE2 1 
ATOM   52   C CZ  . TYR A 1 6   ? 3.42600   14.22700  -16.06100 1.000 8.43101  ? 6   TYR A CZ  1 
ATOM   53   O OH  . TYR A 1 6   ? 2.40000   14.79800  -16.78400 1.000 8.55957  ? 6   TYR A OH  1 
ATOM   54   N N   . VAL A 1 7   ? 8.42400   13.13700  -10.86900 1.000 11.77347 ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 7   ? 9.49500   12.73300  -9.96400  1.000 14.31349 ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 7   ? 8.84500   12.22000  -8.69100  1.000 13.16500 ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 7   ? 7.68700   12.51700  -8.40000  1.000 11.14546 ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 7   ? 10.45900  13.90400  -9.62900  1.000 14.57334 ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 7   ? 11.27600  14.31200  -10.84400 1.000 15.86586 ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 7   ? 9.67000   15.11100  -9.10400  1.000 11.50999 ? 7   VAL A CG2 1 
ATOM   61   N N   . SER A 1 8   ? 9.60600   11.44700  -7.91600  1.000 13.79015 ? 8   SER A N   1 
ATOM   62   C CA  . SER A 1 8   ? 9.11400   11.02800  -6.60700  1.000 15.77144 ? 8   SER A CA  1 
ATOM   63   C C   . SER A 1 8   ? 9.21300   12.16400  -5.58700  1.000 16.68523 ? 8   SER A C   1 
ATOM   64   O O   . SER A 1 8   ? 10.11000  13.00600  -5.64800  1.000 16.44594 ? 8   SER A O   1 
ATOM   65   C CB  . SER A 1 8   ? 9.88300   9.80600   -6.10700  1.000 19.51978 ? 8   SER A CB  1 
ATOM   66   O OG  . SER A 1 8   ? 9.65700   8.70600   -6.97400  1.000 20.56773 ? 8   SER A OG  1 
ATOM   67   N N   . GLN A 1 9   ? 8.26300   12.18100  -4.65100  1.000 17.73608 ? 9   GLN A N   1 
ATOM   68   C CA  . GLN A 1 9   ? 8.24400   13.17900  -3.58500  1.000 21.08958 ? 9   GLN A CA  1 
ATOM   69   C C   . GLN A 1 9   ? 9.57400   13.21500  -2.84100  1.000 20.99034 ? 9   GLN A C   1 
ATOM   70   O O   . GLN A 1 9   ? 10.13400  12.17600  -2.49400  1.000 19.12654 ? 9   GLN A O   1 
ATOM   71   C CB  . GLN A 1 9   ? 7.10400   12.87300  -2.60600  1.000 18.37600 ? 9   GLN A CB  1 
ATOM   72   C CG  . GLN A 1 9   ? 5.72900   13.27700  -3.12900  1.000 28.27597 ? 9   GLN A CG  1 
ATOM   73   C CD  . GLN A 1 9   ? 4.57700   12.70700  -2.30800  1.000 30.91774 ? 9   GLN A CD  1 
ATOM   74   O OE1 . GLN A 1 9   ? 4.78400   11.94400  -1.35900  1.000 28.60225 ? 9   GLN A OE1 1 
ATOM   75   N NE2 . GLN A 1 9   ? 3.35100   13.06300  -2.69000  1.000 32.01852 ? 9   GLN A NE2 1 
ATOM   76   N N   . ASP A 1 10  ? 10.08400  14.42600  -2.61600  1.000 27.14599 ? 10  ASP A N   1 
ATOM   77   C CA  . ASP A 1 10  ? 11.29800  14.67500  -1.84100  1.000 27.18904 ? 10  ASP A CA  1 
ATOM   78   C C   . ASP A 1 10  ? 12.55500  14.13200  -2.50500  1.000 25.90077 ? 10  ASP A C   1 
ATOM   79   O O   . ASP A 1 10  ? 13.62700  14.17400  -1.89600  1.000 28.87385 ? 10  ASP A O   1 
ATOM   80   C CB  . ASP A 1 10  ? 11.21200  14.08800  -0.42700  1.000 29.64753 ? 10  ASP A CB  1 
ATOM   81   C CG  . ASP A 1 10  ? 10.09200  14.69600  0.40100   1.000 39.41604 ? 10  ASP A CG  1 
ATOM   82   O OD1 . ASP A 1 10  ? 9.97400   15.94600  0.42400   1.000 42.47333 ? 10  ASP A OD1 1 
ATOM   83   O OD2 . ASP A 1 10  ? 9.33400   13.92100  1.03300   1.000 40.70634 ? 10  ASP A OD2 1 
ATOM   84   N N   . ARG A 1 11  ? 12.46900  13.59500  -3.72600  1.000 22.41597 ? 11  ARG A N   1 
ATOM   85   C CA  . ARG A 1 11  ? 13.69700  13.20800  -4.41300  1.000 21.89484 ? 11  ARG A CA  1 
ATOM   86   C C   . ARG A 1 11  ? 14.51400  14.43400  -4.80900  1.000 24.86544 ? 11  ARG A C   1 
ATOM   87   O O   . ARG A 1 11  ? 15.74600  14.36400  -4.88300  1.000 26.02850 ? 11  ARG A O   1 
ATOM   88   C CB  . ARG A 1 11  ? 13.36800  12.35100  -5.63900  1.000 23.38053 ? 11  ARG A CB  1 
ATOM   89   C CG  . ARG A 1 11  ? 14.56800  11.97800  -6.49500  1.000 25.86826 ? 11  ARG A CG  1 
ATOM   90   C CD  . ARG A 1 11  ? 15.55100  11.08300  -5.74000  1.000 28.28995 ? 11  ARG A CD  1 
ATOM   91   N NE  . ARG A 1 11  ? 16.71500  10.78400  -6.56500  1.000 31.56417 ? 11  ARG A NE  1 
ATOM   92   C CZ  . ARG A 1 11  ? 17.79800  11.54600  -6.63000  1.000 35.75390 ? 11  ARG A CZ  1 
ATOM   93   N NH1 . ARG A 1 11  ? 17.92000  12.64100  -5.89800  1.000 29.62724 ? 11  ARG A NH1 1 
ATOM   94   N NH2 . ARG A 1 11  ? 18.78600  11.20100  -7.45200  1.000 38.23492 ? 11  ARG A NH2 1 
ATOM   95   N N   . LEU A 1 12  ? 13.85600  15.56200  -5.05600  1.000 22.51637 ? 12  LEU A N   1 
ATOM   96   C CA  . LEU A 1 12  ? 14.52500  16.80400  -5.43400  1.000 25.75672 ? 12  LEU A CA  1 
ATOM   97   C C   . LEU A 1 12  ? 14.29900  17.83800  -4.33900  1.000 22.52010 ? 12  LEU A C   1 
ATOM   98   O O   . LEU A 1 12  ? 13.15500  18.20100  -4.04500  1.000 24.43667 ? 12  LEU A O   1 
ATOM   99   C CB  . LEU A 1 12  ? 14.01500  17.32700  -6.77900  1.000 22.35196 ? 12  LEU A CB  1 
ATOM   100  C CG  . LEU A 1 12  ? 14.19200  16.43100  -8.01000  1.000 19.65839 ? 12  LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 12  ? 13.65500  17.13500  -9.25600  1.000 20.07009 ? 12  LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 12  ? 15.63500  16.05100  -8.23000  1.000 23.14831 ? 12  LEU A CD2 1 
ATOM   103  N N   . THR A 1 13  ? 15.39200  18.30800  -3.73900  1.000 25.93883 ? 13  THR A N   1 
ATOM   104  C CA  . THR A 1 13  ? 15.33000  19.43100  -2.81800  1.000 25.20090 ? 13  THR A CA  1 
ATOM   105  C C   . THR A 1 13  ? 14.88300  20.68600  -3.56600  1.000 26.03006 ? 13  THR A C   1 
ATOM   106  O O   . THR A 1 13  ? 14.95300  20.73100  -4.79800  1.000 22.47295 ? 13  THR A O   1 
ATOM   107  C CB  . THR A 1 13  ? 16.70600  19.65200  -2.19300  1.000 27.34333 ? 13  THR A CB  1 
ATOM   108  O OG1 . THR A 1 13  ? 17.66300  19.85100  -3.23800  1.000 25.73465 ? 13  THR A OG1 1 
ATOM   109  C CG2 . THR A 1 13  ? 17.11300  18.43700  -1.40200  1.000 30.29759 ? 13  THR A CG2 1 
ATOM   110  N N   . PRO A 1 14  ? 14.43000  21.72700  -2.84700  1.000 25.45802 ? 14  PRO A N   1 
ATOM   111  C CA  . PRO A 1 14  ? 14.09000  22.98400  -3.53900  1.000 23.20314 ? 14  PRO A CA  1 
ATOM   112  C C   . PRO A 1 14  ? 15.21200  23.50600  -4.41900  1.000 22.66597 ? 14  PRO A C   1 
ATOM   113  O O   . PRO A 1 14  ? 14.94500  24.01100  -5.51700  1.000 21.72543 ? 14  PRO A O   1 
ATOM   114  C CB  . PRO A 1 14  ? 13.77100  23.94400  -2.38500  1.000 26.33924 ? 14  PRO A CB  1 
ATOM   115  C CG  . PRO A 1 14  ? 13.28800  23.03800  -1.29800  1.000 25.01478 ? 14  PRO A CG  1 
ATOM   116  C CD  . PRO A 1 14  ? 14.14200  21.81200  -1.40200  1.000 28.04968 ? 14  PRO A CD  1 
ATOM   117  N N   . SER A 1 15  ? 16.46900  23.37700  -3.99000  1.000 24.87761 ? 15  SER A N   1 
ATOM   118  C CA  . SER A 1 15  ? 17.55700  23.84400  -4.84100  1.000 21.90694 ? 15  SER A CA  1 
ATOM   119  C C   . SER A 1 15  ? 17.77800  22.91000  -6.02300  1.000 23.69935 ? 15  SER A C   1 
ATOM   120  O O   . SER A 1 15  ? 18.16500  23.36900  -7.10200  1.000 20.53438 ? 15  SER A O   1 
ATOM   121  C CB  . SER A 1 15  ? 18.84800  24.00600  -4.03300  1.000 35.19062 ? 15  SER A CB  1 
ATOM   122  O OG  . SER A 1 15  ? 19.29300  22.76400  -3.52400  1.000 38.39736 ? 15  SER A OG  1 
ATOM   123  N N   . ALA A 1 16  ? 17.52700  21.60700  -5.85200  1.000 20.85424 ? 16  ALA A N   1 
ATOM   124  C CA  . ALA A 1 16  ? 17.60900  20.69400  -6.98900  1.000 22.79496 ? 16  ALA A CA  1 
ATOM   125  C C   . ALA A 1 16  ? 16.47400  20.93800  -7.98600  1.000 20.17506 ? 16  ALA A C   1 
ATOM   126  O O   . ALA A 1 16  ? 16.67600  20.81500  -9.20000  1.000 17.14700 ? 16  ALA A O   1 
ATOM   127  C CB  . ALA A 1 16  ? 17.60000  19.24300  -6.50900  1.000 22.42875 ? 16  ALA A CB  1 
ATOM   128  N N   . LYS A 1 17  ? 15.27300  21.26600  -7.49600  1.000 17.05423 ? 17  LYS A N   1 
ATOM   129  C CA  . LYS A 1 17  ? 14.18000  21.63500  -8.39600  1.000 17.87139 ? 17  LYS A CA  1 
ATOM   130  C C   . LYS A 1 17  ? 14.53700  22.87600  -9.18400  1.000 18.90829 ? 17  LYS A C   1 
ATOM   131  O O   . LYS A 1 17  ? 14.31700  22.94400  -10.40100 1.000 16.75170 ? 17  LYS A O   1 
ATOM   132  C CB  . LYS A 1 17  ? 12.88400  21.87000  -7.61400  1.000 16.92570 ? 17  LYS A CB  1 
ATOM   133  C CG  . LYS A 1 17  ? 12.26700  20.61200  -7.07400  1.000 17.57936 ? 17  LYS A CG  1 
ATOM   134  C CD  . LYS A 1 17  ? 10.93300  20.88200  -6.39500  1.000 20.81660 ? 17  LYS A CD  1 
ATOM   135  C CE  . LYS A 1 17  ? 10.44800  19.62300  -5.69700  1.000 24.60202 ? 17  LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 17  ? 9.21500   19.85700  -4.88900  1.000 26.48247 ? 17  LYS A NZ  1 
ATOM   137  N N   . HIS A 1 18  ? 15.07800  23.88400  -8.49800  1.000 16.20443 ? 18  HIS A N   1 
ATOM   138  C CA  . HIS A 1 18  ? 15.47800  25.09600  -9.19700  1.000 17.46545 ? 18  HIS A CA  1 
ATOM   139  C C   . HIS A 1 18  ? 16.54500  24.79900  -10.24100 1.000 15.77236 ? 18  HIS A C   1 
ATOM   140  O O   . HIS A 1 18  ? 16.47100  25.29500  -11.37300 1.000 18.45303 ? 18  HIS A O   1 
ATOM   141  C CB  . HIS A 1 18  ? 15.98200  26.14300  -8.20700  1.000 19.96611 ? 18  HIS A CB  1 
ATOM   142  C CG  . HIS A 1 18  ? 16.44500  27.39500  -8.87400  1.000 27.03416 ? 18  HIS A CG  1 
ATOM   143  N ND1 . HIS A 1 18  ? 17.74700  27.57800  -9.29100  1.000 37.74497 ? 18  HIS A ND1 1 
ATOM   144  C CD2 . HIS A 1 18  ? 15.76100  28.49400  -9.26800  1.000 33.31694 ? 18  HIS A CD2 1 
ATOM   145  C CE1 . HIS A 1 18  ? 17.84900  28.75400  -9.88700  1.000 38.97519 ? 18  HIS A CE1 1 
ATOM   146  N NE2 . HIS A 1 18  ? 16.65900  29.33100  -9.88400  1.000 33.70031 ? 18  HIS A NE2 1 
ATOM   147  N N   . ALA A 1 19  ? 17.54400  23.98700  -9.87800  1.000 15.44365 ? 19  ALA A N   1 
ATOM   148  C CA  . ALA A 1 19  ? 18.59300  23.62900  -10.83200 1.000 17.65850 ? 19  ALA A CA  1 
ATOM   149  C C   . ALA A 1 19  ? 18.02100  22.89000  -12.04100 1.000 17.30006 ? 19  ALA A C   1 
ATOM   150  O O   . ALA A 1 19  ? 18.40600  23.16500  -13.18300 1.000 17.77871 ? 19  ALA A O   1 
ATOM   151  C CB  . ALA A 1 19  ? 19.66100  22.78200  -10.14000 1.000 17.16700 ? 19  ALA A CB  1 
ATOM   152  N N   . VAL A 1 20  ? 17.10800  21.94000  -11.80800 1.000 16.48910 ? 20  VAL A N   1 
ATOM   153  C CA  . VAL A 1 20  ? 16.50200  21.20100  -12.92100 1.000 15.30342 ? 20  VAL A CA  1 
ATOM   154  C C   . VAL A 1 20  ? 15.68600  22.14400  -13.79200 1.000 14.55405 ? 20  VAL A C   1 
ATOM   155  O O   . VAL A 1 20  ? 15.75900  22.10400  -15.02700 1.000 15.07094 ? 20  VAL A O   1 
ATOM   156  C CB  . VAL A 1 20  ? 15.64200  20.04000  -12.38400 1.000 16.40523 ? 20  VAL A CB  1 
ATOM   157  C CG1 . VAL A 1 20  ? 14.75100  19.47500  -13.47500 1.000 14.12430 ? 20  VAL A CG1 1 
ATOM   158  C CG2 . VAL A 1 20  ? 16.53200  18.94600  -11.80000 1.000 16.90956 ? 20  VAL A CG2 1 
ATOM   159  N N   . ALA A 1 21  ? 14.88300  23.00000  -13.16200 1.000 13.58720 ? 21  ALA A N   1 
ATOM   160  C CA  . ALA A 1 21  ? 14.06100  23.93500  -13.92900 1.000 15.12687 ? 21  ALA A CA  1 
ATOM   161  C C   . ALA A 1 21  ? 14.93300  24.87200  -14.74600 1.000 17.55329 ? 21  ALA A C   1 
ATOM   162  O O   . ALA A 1 21  ? 14.63800  25.15000  -15.91500 1.000 16.90077 ? 21  ALA A O   1 
ATOM   163  C CB  . ALA A 1 21  ? 13.14300  24.73700  -13.00000 1.000 16.41894 ? 21  ALA A CB  1 
ATOM   164  N N   . LYS A 1 22  ? 16.02300  25.36400  -14.14800 1.000 16.99200 ? 22  LYS A N   1 
ATOM   165  C CA  . LYS A 1 22  ? 16.95000  26.21400  -14.89000 1.000 15.49578 ? 22  LYS A CA  1 
ATOM   166  C C   . LYS A 1 22  ? 17.59800  25.44900  -16.03500 1.000 17.60294 ? 22  LYS A C   1 
ATOM   167  O O   . LYS A 1 22  ? 17.73400  25.97500  -17.14700 1.000 21.62323 ? 22  LYS A O   1 
ATOM   168  C CB  . LYS A 1 22  ? 18.01100  26.78200  -13.94200 1.000 21.30893 ? 22  LYS A CB  1 
ATOM   169  C CG  . LYS A 1 22  ? 19.17100  27.49200  -14.64600 1.000 28.46417 ? 22  LYS A CG  1 
ATOM   170  C CD  . LYS A 1 22  ? 19.97400  28.36400  -13.67100 1.000 34.98712 ? 22  LYS A CD  1 
ATOM   171  C CE  . LYS A 1 22  ? 21.25400  28.89600  -14.31800 1.000 33.14819 ? 22  LYS A CE  1 
ATOM   172  N NZ  . LYS A 1 22  ? 20.98300  29.64600  -15.56500 1.000 31.50027 ? 22  LYS A NZ  1 
ATOM   173  N N   . ALA A 1 23  ? 18.00400  24.20500  -15.78100 1.000 17.63621 ? 23  ALA A N   1 
ATOM   174  C CA  . ALA A 1 23  ? 18.66500  23.41400  -16.81700 1.000 17.93780 ? 23  ALA A CA  1 
ATOM   175  C C   . ALA A 1 23  ? 17.74200  23.18300  -18.00500 1.000 17.68598 ? 23  ALA A C   1 
ATOM   176  O O   . ALA A 1 23  ? 18.17200  23.27000  -19.16100 1.000 18.42429 ? 23  ALA A O   1 
ATOM   177  C CB  . ALA A 1 23  ? 19.13800  22.07900  -16.23500 1.000 17.39685 ? 23  ALA A CB  1 
ATOM   178  N N   . ILE A 1 24  ? 16.46600  22.89300  -17.73900 1.000 15.64655 ? 24  ILE A N   1 
ATOM   179  C CA  . ILE A 1 24  ? 15.50700  22.68400  -18.82400 1.000 14.76714 ? 24  ILE A CA  1 
ATOM   180  C C   . ILE A 1 24  ? 15.24100  23.98600  -19.55900 1.000 18.14196 ? 24  ILE A C   1 
ATOM   181  O O   . ILE A 1 24  ? 15.19600  24.02100  -20.79600 1.000 17.34931 ? 24  ILE A O   1 
ATOM   182  C CB  . ILE A 1 24  ? 14.20600  22.07600  -18.27000 1.000 13.76191 ? 24  ILE A CB  1 
ATOM   183  C CG1 . ILE A 1 24  ? 14.43700  20.63700  -17.80800 1.000 13.28895 ? 24  ILE A CG1 1 
ATOM   184  C CG2 . ILE A 1 24  ? 13.09800  22.13500  -19.32000 1.000 13.47478 ? 24  ILE A CG2 1 
ATOM   185  C CD1 . ILE A 1 24  ? 13.28200  20.05600  -16.98300 1.000 14.87668 ? 24  ILE A CD1 1 
ATOM   186  N N   . THR A 1 25  ? 15.04900  25.07900  -18.80600 1.000 15.53393 ? 25  THR A N   1 
ATOM   187  C CA  . THR A 1 25  ? 14.78400  26.38100  -19.40700 1.000 16.74191 ? 25  THR A CA  1 
ATOM   188  C C   . THR A 1 25  ? 15.95500  26.84200  -20.26700 1.000 19.56854 ? 25  THR A C   1 
ATOM   189  O O   . THR A 1 25  ? 15.75500  27.41800  -21.34500 1.000 20.95852 ? 25  THR A O   1 
ATOM   190  C CB  . THR A 1 25  ? 14.50500  27.40600  -18.30500 1.000 24.94968 ? 25  THR A CB  1 
ATOM   191  O OG1 . THR A 1 25  ? 13.36800  26.99000  -17.52900 1.000 23.74228 ? 25  THR A OG1 1 
ATOM   192  C CG2 . THR A 1 25  ? 14.25400  28.78800  -18.89700 1.000 23.98203 ? 25  THR A CG2 1 
ATOM   193  N N   . ASP A 1 26  ? 17.18300  26.61800  -19.78700 1.000 22.09948 ? 26  ASP A N   1 
ATOM   194  C CA  . ASP A 1 26  ? 18.37700  27.05600  -20.50400 1.000 20.72309 ? 26  ASP A CA  1 
ATOM   195  C C   . ASP A 1 26  ? 18.61100  26.21600  -21.75200 1.000 26.48765 ? 26  ASP A C   1 
ATOM   196  O O   . ASP A 1 26  ? 19.11000  26.72600  -22.76200 1.000 27.78391 ? 26  ASP A O   1 
ATOM   197  C CB  . ASP A 1 26  ? 19.60000  26.97400  -19.59600 1.000 21.96415 ? 26  ASP A CB  1 
ATOM   198  C CG  . ASP A 1 26  ? 19.63100  28.06900  -18.53900 1.000 27.12654 ? 26  ASP A CG  1 
ATOM   199  O OD1 . ASP A 1 26  ? 18.90100  29.07100  -18.67900 1.000 27.85039 ? 26  ASP A OD1 1 
ATOM   200  O OD2 . ASP A 1 26  ? 20.40300  27.91600  -17.57500 1.000 27.93277 ? 26  ASP A OD2 1 
ATOM   201  N N   . ALA A 1 27  ? 18.31800  24.91400  -21.67800 1.000 21.07171 ? 27  ALA A N   1 
ATOM   202  C CA  . ALA A 1 27  ? 18.35000  24.07200  -22.86900 1.000 22.94135 ? 27  ALA A CA  1 
ATOM   203  C C   . ALA A 1 27  ? 17.41900  24.62400  -23.93800 1.000 29.85973 ? 27  ALA A C   1 
ATOM   204  O O   . ALA A 1 27  ? 17.80700  24.79400  -25.10100 1.000 31.78863 ? 27  ALA A O   1 
ATOM   205  C CB  . ALA A 1 27  ? 17.95100  22.64200  -22.49700 1.000 21.99400 ? 27  ALA A CB  1 
ATOM   206  N N   . ALA A 1 28  ? 16.17700  24.91700  -23.54400 1.000 30.98657 ? 28  ALA A N   1 
ATOM   207  C CA  . ALA A 1 28  ? 15.15000  25.35300  -24.47900 1.000 33.52714 ? 28  ALA A CA  1 
ATOM   208  C C   . ALA A 1 28  ? 15.54900  26.64800  -25.17800 1.000 39.32183 ? 28  ALA A C   1 
ATOM   209  O O   . ALA A 1 28  ? 15.41100  26.77200  -26.40100 1.000 41.03982 ? 28  ALA A O   1 
ATOM   210  C CB  . ALA A 1 28  ? 13.82000  25.51300  -23.73400 1.000 25.53941 ? 28  ALA A CB  1 
ATOM   211  N N   . ARG A 1 29  ? 16.06600  27.62500  -24.42300 1.000 39.00053 ? 29  ARG A N   1 
ATOM   212  C CA  . ARG A 1 29  ? 16.41700  28.89600  -25.05500 1.000 42.47597 ? 29  ARG A CA  1 
ATOM   213  C C   . ARG A 1 29  ? 17.73200  28.80700  -25.82500 1.000 43.92745 ? 29  ARG A C   1 
ATOM   214  O O   . ARG A 1 29  ? 17.84400  29.36300  -26.92300 1.000 48.79247 ? 29  ARG A O   1 
ATOM   215  C CB  . ARG A 1 29  ? 16.49500  30.01800  -24.01900 1.000 47.85288 ? 29  ARG A CB  1 
ATOM   216  C CG  . ARG A 1 29  ? 16.78300  31.37300  -24.66200 1.000 49.86685 ? 29  ARG A CG  1 
ATOM   217  C CD  . ARG A 1 29  ? 16.65400  32.52100  -23.68800 1.000 51.07364 ? 29  ARG A CD  1 
ATOM   218  N NE  . ARG A 1 29  ? 16.61200  33.80300  -24.38500 1.000 58.61249 ? 29  ARG A NE  1 
ATOM   219  C CZ  . ARG A 1 29  ? 16.16800  34.93200  -23.84600 1.000 52.47088 ? 29  ARG A CZ  1 
ATOM   220  N NH1 . ARG A 1 29  ? 15.72700  34.97100  -22.59800 1.000 48.16841 ? 29  ARG A NH1 1 
ATOM   221  N NH2 . ARG A 1 29  ? 16.16100  36.04400  -24.57800 1.000 42.61910 ? 29  ARG A NH2 1 
ATOM   222  N N   . GLY A 1 30  ? 18.73200  28.11900  -25.26900 1.000 40.55361 ? 30  GLY A N   1 
ATOM   223  C CA  . GLY A 1 30  ? 20.03400  28.05200  -25.90800 1.000 41.60960 ? 30  GLY A CA  1 
ATOM   224  C C   . GLY A 1 30  ? 20.03300  27.33100  -27.23800 1.000 49.81992 ? 30  GLY A C   1 
ATOM   225  O O   . GLY A 1 30  ? 20.96500  27.51400  -28.03000 1.000 54.15403 ? 30  GLY A O   1 
ATOM   226  N N   . LEU A 1 31  ? 19.00500  26.52100  -27.51100 1.000 43.19757 ? 31  LEU A N   1 
ATOM   227  C CA  . LEU A 1 31  ? 18.93700  25.73100  -28.73600 1.000 47.34287 ? 31  LEU A CA  1 
ATOM   228  C C   . LEU A 1 31  ? 17.90300  26.21800  -29.73400 1.000 45.36536 ? 31  LEU A C   1 
ATOM   229  O O   . LEU A 1 31  ? 18.11200  26.06100  -30.93800 1.000 48.80586 ? 31  LEU A O   1 
ATOM   230  C CB  . LEU A 1 31  ? 18.64200  24.26100  -28.41300 1.000 41.50871 ? 31  LEU A CB  1 
ATOM   231  C CG  . LEU A 1 31  ? 19.89600  23.40800  -28.27700 1.000 45.15380 ? 31  LEU A CG  1 
ATOM   232  C CD1 . LEU A 1 31  ? 19.53200  22.00700  -27.83000 1.000 34.88504 ? 31  LEU A CD1 1 
ATOM   233  C CD2 . LEU A 1 31  ? 20.66300  23.39800  -29.60400 1.000 41.35555 ? 31  LEU A CD2 1 
ATOM   234  N N   . THR A 1 32  ? 16.79100  26.79100  -29.26800 1.000 44.54313 ? 32  THR A N   1 
ATOM   235  C CA  . THR A 1 32  ? 15.72100  27.24200  -30.14700 1.000 51.57924 ? 32  THR A CA  1 
ATOM   236  C C   . THR A 1 32  ? 15.51900  28.74900  -30.13900 1.000 52.91002 ? 32  THR A C   1 
ATOM   237  O O   . THR A 1 32  ? 14.97000  29.28500  -31.10600 1.000 54.08123 ? 32  THR A O   1 
ATOM   238  C CB  . THR A 1 32  ? 14.38700  26.58000  -29.76100 1.000 51.83908 ? 32  THR A CB  1 
ATOM   239  O OG1 . THR A 1 32  ? 13.80800  27.29400  -28.66000 1.000 51.67551 ? 32  THR A OG1 1 
ATOM   240  C CG2 . THR A 1 32  ? 14.59700  25.12000  -29.35600 1.000 45.26332 ? 32  THR A CG2 1 
ATOM   241  N N   . GLY A 1 33  ? 15.89600  29.41800  -29.06100 1.000 54.61481 ? 33  GLY A N   1 
ATOM   242  C CA  . GLY A 1 33  ? 15.66000  30.83500  -28.97800 1.000 54.08707 ? 33  GLY A CA  1 
ATOM   243  C C   . GLY A 1 33  ? 14.42400  31.14700  -28.16600 1.000 54.23245 ? 33  GLY A C   1 
ATOM   244  O O   . GLY A 1 33  ? 14.06500  32.30100  -28.05200 1.000 56.37318 ? 33  GLY A O   1 
ATOM   245  N N   . THR A 1 34  ? 13.78700  30.12400  -27.60800 1.000 51.62969 ? 34  THR A N   1 
ATOM   246  C CA  . THR A 1 34  ? 12.60800  30.35500  -26.80200 1.000 54.50223 ? 34  THR A CA  1 
ATOM   247  C C   . THR A 1 34  ? 13.00400  31.23500  -25.66800 1.000 55.55882 ? 34  THR A C   1 
ATOM   248  O O   . THR A 1 34  ? 13.74100  30.81900  -24.80600 1.000 51.86762 ? 34  THR A O   1 
ATOM   249  C CB  . THR A 1 34  ? 11.91200  29.09100  -26.18900 1.000 52.84815 ? 34  THR A CB  1 
ATOM   250  O OG1 . THR A 1 34  ? 11.13100  29.48800  -25.06000 1.000 50.87999 ? 34  THR A OG1 1 
ATOM   251  C CG2 . THR A 1 34  ? 12.85000  28.08200  -25.70400 1.000 51.41178 ? 34  THR A CG2 1 
ATOM   252  N N   . GLN A 1 35  ? 12.40700  32.42900  -25.60900 1.000 53.18813 ? 35  GLN A N   1 
ATOM   253  C CA  . GLN A 1 35  ? 12.61900  33.45600  -24.56900 1.000 55.00103 ? 35  GLN A CA  1 
ATOM   254  C C   . GLN A 1 35  ? 12.51400  32.88400  -23.15300 1.000 56.17783 ? 35  GLN A C   1 
ATOM   255  O O   . GLN A 1 35  ? 11.65400  32.00500  -22.94300 1.000 54.65264 ? 35  GLN A O   1 
ATOM   256  C CB  . GLN A 1 35  ? 11.50200  34.52400  -24.67800 1.000 55.59932 ? 35  GLN A CB  1 
ATOM   257  C CG  . GLN A 1 35  ? 11.73500  35.77500  -25.51000 1.000 58.76295 ? 35  GLN A CG  1 
ATOM   258  C CD  . GLN A 1 35  ? 10.55500  36.04300  -26.47300 1.000 73.79977 ? 35  GLN A CD  1 
ATOM   259  O OE1 . GLN A 1 35  ? 9.94900   35.11000  -27.00000 1.000 73.87908 ? 35  GLN A OE1 1 
ATOM   260  N NE2 . GLN A 1 35  ? 10.23000  37.30700  -26.68900 1.000 68.10411 ? 35  GLN A NE2 1 
ATOM   261  N N   . HIS A 1 36  ? 13.19500  33.50900  -22.18200 1.000 50.38512 ? 36  HIS A N   1 
ATOM   262  C CA  . HIS A 1 36  ? 13.23000  32.94700  -20.83500 1.000 52.14540 ? 36  HIS A CA  1 
ATOM   263  C C   . HIS A 1 36  ? 11.82800  32.68500  -20.29500 1.000 51.68548 ? 36  HIS A C   1 
ATOM   264  O O   . HIS A 1 36  ? 11.47100  31.54400  -19.96900 1.000 47.22716 ? 36  HIS A O   1 
ATOM   265  C CB  . HIS A 1 36  ? 13.97900  33.89900  -19.90600 1.000 47.64409 ? 36  HIS A CB  1 
ATOM   266  C CG  . HIS A 1 36  ? 15.00600  33.22800  -19.05300 1.000 47.58062 ? 36  HIS A CG  1 
ATOM   267  N ND1 . HIS A 1 36  ? 14.75300  32.06300  -18.36200 1.000 45.96621 ? 36  HIS A ND1 1 
ATOM   268  C CD2 . HIS A 1 36  ? 16.29100  33.55700  -18.77600 1.000 47.77503 ? 36  HIS A CD2 1 
ATOM   269  C CE1 . HIS A 1 36  ? 15.83600  31.70200  -17.69500 1.000 47.50475 ? 36  HIS A CE1 1 
ATOM   270  N NE2 . HIS A 1 36  ? 16.78500  32.59100  -17.93200 1.000 53.31257 ? 36  HIS A NE2 1 
ATOM   271  N N   . PHE A 1 37  ? 11.01500  33.74100  -20.20600 1.000 47.99208 ? 37  PHE A N   1 
ATOM   272  C CA  . PHE A 1 37  ? 9.72100   33.65100  -19.54000 1.000 49.96401 ? 37  PHE A CA  1 
ATOM   273  C C   . PHE A 1 37  ? 8.75400   32.68500  -20.22200 1.000 47.01470 ? 37  PHE A C   1 
ATOM   274  O O   . PHE A 1 37  ? 7.73600   32.32800  -19.61500 1.000 44.75731 ? 37  PHE A O   1 
ATOM   275  C CB  . PHE A 1 37  ? 9.09300   35.05000  -19.43100 1.000 51.63519 ? 37  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 37  ? 8.83500   35.72200  -20.76100 1.000 52.93057 ? 37  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 37  ? 9.86700   36.32800  -21.46700 1.000 53.30027 ? 37  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 37  ? 7.55100   35.77500  -21.28900 1.000 55.69979 ? 37  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 37  ? 9.62800   36.95100  -22.68400 1.000 54.39139 ? 37  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 37  ? 7.30600   36.39900  -22.50600 1.000 58.18391 ? 37  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 37  ? 8.34600   36.98600  -23.20300 1.000 56.21020 ? 37  PHE A CZ  1 
ATOM   282  N N   . LEU A 1 38  ? 9.04200   32.22800  -21.44100 1.000 49.33097 ? 38  LEU A N   1 
ATOM   283  C CA  . LEU A 1 38  ? 8.09600   31.34000  -22.10100 1.000 50.26524 ? 38  LEU A CA  1 
ATOM   284  C C   . LEU A 1 38  ? 8.16300   29.89300  -21.61500 1.000 43.93065 ? 38  LEU A C   1 
ATOM   285  O O   . LEU A 1 38  ? 7.31800   29.09100  -22.03500 1.000 40.63247 ? 38  LEU A O   1 
ATOM   286  C CB  . LEU A 1 38  ? 8.30500   31.38100  -23.61900 1.000 45.26130 ? 38  LEU A CB  1 
ATOM   287  C CG  . LEU A 1 38  ? 7.61700   32.53600  -24.35400 1.000 52.15825 ? 38  LEU A CG  1 
ATOM   288  C CD1 . LEU A 1 38  ? 7.40900   32.19700  -25.82900 1.000 55.28931 ? 38  LEU A CD1 1 
ATOM   289  C CD2 . LEU A 1 38  ? 6.28900   32.89300  -23.68400 1.000 47.50678 ? 38  LEU A CD2 1 
ATOM   290  N N   . ALA A 1 39  ? 9.13700   29.52700  -20.77000 1.000 29.73072 ? 39  ALA A N   1 
ATOM   291  C CA  . ALA A 1 39  ? 9.37100   28.12600  -20.42600 1.000 24.18257 ? 39  ALA A CA  1 
ATOM   292  C C   . ALA A 1 39  ? 8.79800   27.83700  -19.04200 1.000 19.36597 ? 39  ALA A C   1 
ATOM   293  O O   . ALA A 1 39  ? 9.31000   28.33300  -18.03100 1.000 16.50188 ? 39  ALA A O   1 
ATOM   294  C CB  . ALA A 1 39  ? 10.85600  27.78400  -20.47400 1.000 29.67645 ? 39  ALA A CB  1 
ATOM   295  N N   . GLN A 1 40  ? 7.74900   27.02200  -19.00000 1.000 13.81222 ? 40  GLN A N   1 
ATOM   296  C CA  . GLN A 1 40  ? 7.16200   26.57200  -17.74500 1.000 13.24298 ? 40  GLN A CA  1 
ATOM   297  C C   . GLN A 1 40  ? 7.68200   25.17600  -17.43000 1.000 13.86512 ? 40  GLN A C   1 
ATOM   298  O O   . GLN A 1 40  ? 7.60500   24.27400  -18.27500 1.000 11.48368 ? 40  GLN A O   1 
ATOM   299  C CB  . GLN A 1 40  ? 5.62600   26.55300  -17.81300 1.000 11.51384 ? 40  GLN A CB  1 
ATOM   300  C CG  . GLN A 1 40  ? 5.02200   25.92200  -16.54000 1.000 13.68546 ? 40  GLN A CG  1 
ATOM   301  C CD  . GLN A 1 40  ? 3.50700   25.96000  -16.45600 1.000 15.08104 ? 40  GLN A CD  1 
ATOM   302  O OE1 . GLN A 1 40  ? 2.92200   25.19400  -15.69200 1.000 14.79530 ? 40  GLN A OE1 1 
ATOM   303  N NE2 . GLN A 1 40  ? 2.86600   26.86000  -17.20500 1.000 14.98706 ? 40  GLN A NE2 1 
ATOM   304  N N   . VAL A 1 41  ? 8.21600   25.00300  -16.22300 1.000 11.33599 ? 41  VAL A N   1 
ATOM   305  C CA  . VAL A 1 41  ? 8.56900   23.68700  -15.69700 1.000 10.97351 ? 41  VAL A CA  1 
ATOM   306  C C   . VAL A 1 41  ? 7.63600   23.39700  -14.53300 1.000 13.51525 ? 41  VAL A C   1 
ATOM   307  O O   . VAL A 1 41  ? 7.57300   24.16100  -13.56000 1.000 12.32976 ? 41  VAL A O   1 
ATOM   308  C CB  . VAL A 1 41  ? 10.04300  23.61800  -15.26500 1.000 12.07219 ? 41  VAL A CB  1 
ATOM   309  C CG1 . VAL A 1 41  ? 10.36400  22.24700  -14.66900 1.000 11.20132 ? 41  VAL A CG1 1 
ATOM   310  C CG2 . VAL A 1 41  ? 10.95300  23.91900  -16.46100 1.000 13.68985 ? 41  VAL A CG2 1 
ATOM   311  N N   . ASN A 1 42  ? 6.92000   22.28600  -14.62200 1.000 10.92894 ? 42  ASN A N   1 
ATOM   312  C CA  . ASN A 1 42  ? 5.83300   21.98300  -13.70300 1.000 12.01191 ? 42  ASN A CA  1 
ATOM   313  C C   . ASN A 1 42  ? 6.15700   20.62400  -13.07100 1.000 11.61161 ? 42  ASN A C   1 
ATOM   314  O O   . ASN A 1 42  ? 6.04700   19.57600  -13.72400 1.000 9.50720  ? 42  ASN A O   1 
ATOM   315  C CB  . ASN A 1 42  ? 4.51400   22.01300  -14.48100 1.000 12.27149 ? 42  ASN A CB  1 
ATOM   316  C CG  . ASN A 1 42  ? 3.30100   22.11300  -13.57600 1.000 15.33350 ? 42  ASN A CG  1 
ATOM   317  O OD1 . ASN A 1 42  ? 3.20800   21.38100  -12.60400 1.000 15.46147 ? 42  ASN A OD1 1 
ATOM   318  N ND2 . ASN A 1 42  ? 2.38200   23.03900  -13.87600 1.000 12.58127 ? 42  ASN A ND2 1 
ATOM   319  N N   . PHE A 1 43  ? 6.62600   20.63800  -11.82400 1.000 10.92886 ? 43  PHE A N   1 
ATOM   320  C CA  . PHE A 1 43  ? 6.99600   19.40100  -11.14700 1.000 11.72291 ? 43  PHE A CA  1 
ATOM   321  C C   . PHE A 1 43  ? 5.76400   18.69800  -10.60700 1.000 11.91436 ? 43  PHE A C   1 
ATOM   322  O O   . PHE A 1 43  ? 4.98900   19.28600  -9.85500  1.000 9.48397  ? 43  PHE A O   1 
ATOM   323  C CB  . PHE A 1 43  ? 7.97000   19.67000  -10.00100 1.000 10.57835 ? 43  PHE A CB  1 
ATOM   324  C CG  . PHE A 1 43  ? 9.33800   20.04400  -10.46700 1.000 11.86565 ? 43  PHE A CG  1 
ATOM   325  C CD1 . PHE A 1 43  ? 10.23100  19.06200  -10.87600 1.000 13.04793 ? 43  PHE A CD1 1 
ATOM   326  C CD2 . PHE A 1 43  ? 9.72300   21.37600  -10.52800 1.000 13.44980 ? 43  PHE A CD2 1 
ATOM   327  C CE1 . PHE A 1 43  ? 11.50400  19.40300  -11.33000 1.000 13.97976 ? 43  PHE A CE1 1 
ATOM   328  C CE2 . PHE A 1 43  ? 10.99500  21.73100  -10.98500 1.000 14.86663 ? 43  PHE A CE2 1 
ATOM   329  C CZ  . PHE A 1 43  ? 11.88200  20.74200  -11.38500 1.000 11.56593 ? 43  PHE A CZ  1 
ATOM   330  N N   . GLN A 1 44  ? 5.61600   17.42600  -10.95800 1.000 9.10539  ? 44  GLN A N   1 
ATOM   331  C CA  . GLN A 1 44  ? 4.53000   16.56300  -10.49100 1.000 11.70298 ? 44  GLN A CA  1 
ATOM   332  C C   . GLN A 1 44  ? 5.15000   15.48100  -9.60700  1.000 12.07055 ? 44  GLN A C   1 
ATOM   333  O O   . GLN A 1 44  ? 5.73900   14.52100  -10.11600 1.000 8.97767  ? 44  GLN A O   1 
ATOM   334  C CB  . GLN A 1 44  ? 3.79100   15.95700  -11.67900 1.000 11.30890 ? 44  GLN A CB  1 
ATOM   335  C CG  . GLN A 1 44  ? 3.22600   17.02900  -12.59900 1.000 10.73719 ? 44  GLN A CG  1 
ATOM   336  C CD  . GLN A 1 44  ? 1.97600   17.66700  -12.01200 1.000 14.74932 ? 44  GLN A CD  1 
ATOM   337  O OE1 . GLN A 1 44  ? 1.02700   16.96100  -11.69000 1.000 15.42820 ? 44  GLN A OE1 1 
ATOM   338  N NE2 . GLN A 1 44  ? 1.97200   18.99800  -11.86000 1.000 12.20403 ? 44  GLN A NE2 1 
ATOM   339  N N   . GLU A 1 45  ? 5.01700   15.64400  -8.28100  1.000 10.82233 ? 45  GLU A N   1 
ATOM   340  C CA  . GLU A 1 45  ? 5.55100   14.68900  -7.31400  1.000 11.75503 ? 45  GLU A CA  1 
ATOM   341  C C   . GLU A 1 45  ? 4.51900   13.63500  -6.92300  1.000 12.25324 ? 45  GLU A C   1 
ATOM   342  O O   . GLU A 1 45  ? 3.34200   13.94400  -6.71200  1.000 13.75566 ? 45  GLU A O   1 
ATOM   343  C CB  . GLU A 1 45  ? 6.03100   15.42800  -6.05500  1.000 14.65745 ? 45  GLU A CB  1 
ATOM   344  C CG  . GLU A 1 45  ? 7.29400   16.24000  -6.29000  1.000 15.94432 ? 45  GLU A CG  1 
ATOM   345  C CD  . GLU A 1 45  ? 7.65600   17.13500  -5.12000  1.000 19.22679 ? 45  GLU A CD  1 
ATOM   346  O OE1 . GLU A 1 45  ? 6.80700   17.95700  -4.72400  1.000 18.22911 ? 45  GLU A OE1 1 
ATOM   347  O OE2 . GLU A 1 45  ? 8.79100   17.01700  -4.61200  1.000 23.10477 ? 45  GLU A OE2 1 
ATOM   348  N N   . GLN A 1 46  ? 4.96900   12.38600  -6.82100  1.000 12.06530 ? 46  GLN A N   1 
ATOM   349  C CA  . GLN A 1 46  ? 4.18700   11.25700  -6.33700  1.000 12.37249 ? 46  GLN A CA  1 
ATOM   350  C C   . GLN A 1 46  ? 5.02100   10.44600  -5.35700  1.000 13.70556 ? 46  GLN A C   1 
ATOM   351  O O   . GLN A 1 46  ? 6.25100   10.44100  -5.43600  1.000 14.60006 ? 46  GLN A O   1 
ATOM   352  C CB  . GLN A 1 46  ? 3.74400   10.34400  -7.49700  1.000 14.37805 ? 46  GLN A CB  1 
ATOM   353  C CG  . GLN A 1 46  ? 2.67500   10.95600  -8.38600  1.000 11.29470 ? 46  GLN A CG  1 
ATOM   354  C CD  . GLN A 1 46  ? 1.35300   11.07400  -7.67100  1.000 13.17233 ? 46  GLN A CD  1 
ATOM   355  O OE1 . GLN A 1 46  ? 0.93500   10.15000  -6.96800  1.000 15.18575 ? 46  GLN A OE1 1 
ATOM   356  N NE2 . GLN A 1 46  ? 0.67900   12.21000  -7.84300  1.000 13.98862 ? 46  GLN A NE2 1 
ATOM   357  N N   . PRO A 1 47  ? 4.38600   9.71700   -4.44100  1.000 15.41612 ? 47  PRO A N   1 
ATOM   358  C CA  . PRO A 1 47  ? 5.16100   8.84300   -3.54300  1.000 16.72981 ? 47  PRO A CA  1 
ATOM   359  C C   . PRO A 1 47  ? 6.04900   7.86000   -4.30300  1.000 18.46986 ? 47  PRO A C   1 
ATOM   360  O O   . PRO A 1 47  ? 5.67600   7.33000   -5.35400  1.000 15.61568 ? 47  PRO A O   1 
ATOM   361  C CB  . PRO A 1 47  ? 4.08000   8.11500   -2.73300  1.000 21.00624 ? 47  PRO A CB  1 
ATOM   362  C CG  . PRO A 1 47  ? 2.81900   8.30000   -3.49800  1.000 24.04280 ? 47  PRO A CG  1 
ATOM   363  C CD  . PRO A 1 47  ? 2.93800   9.61900   -4.19800  1.000 17.62171 ? 47  PRO A CD  1 
ATOM   364  N N   . ALA A 1 48  ? 7.25100   7.63800   -3.76700  1.000 14.58898 ? 48  ALA A N   1 
ATOM   365  C CA  . ALA A 1 48  ? 8.11300   6.58900   -4.29200  1.000 18.57165 ? 48  ALA A CA  1 
ATOM   366  C C   . ALA A 1 48  ? 7.38500   5.25200   -4.22100  1.000 20.21204 ? 48  ALA A C   1 
ATOM   367  O O   . ALA A 1 48  ? 6.67400   4.96300   -3.25400  1.000 18.15204 ? 48  ALA A O   1 
ATOM   368  C CB  . ALA A 1 48  ? 9.42400   6.52900   -3.50500  1.000 22.01596 ? 48  ALA A CB  1 
ATOM   369  N N   . GLY A 1 49  ? 7.53400   4.45100   -5.26500  1.000 18.01967 ? 49  GLY A N   1 
ATOM   370  C CA  . GLY A 1 49  ? 6.77700   3.23300   -5.40800  1.000 14.81784 ? 49  GLY A CA  1 
ATOM   371  C C   . GLY A 1 49  ? 5.63100   3.33000   -6.39200  1.000 18.31841 ? 49  GLY A C   1 
ATOM   372  O O   . GLY A 1 49  ? 4.99300   2.31300   -6.66500  1.000 17.72275 ? 49  GLY A O   1 
ATOM   373  N N   . ASN A 1 50  ? 5.33500   4.52300   -6.91100  1.000 16.05442 ? 50  ASN A N   1 
ATOM   374  C CA  . ASN A 1 50  ? 4.24400   4.67900   -7.86700  1.000 17.71355 ? 50  ASN A CA  1 
ATOM   375  C C   . ASN A 1 50  ? 4.69100   4.48600   -9.31600  1.000 13.97863 ? 50  ASN A C   1 
ATOM   376  O O   . ASN A 1 50  ? 3.83800   4.48300   -10.22000 1.000 12.98046 ? 50  ASN A O   1 
ATOM   377  C CB  . ASN A 1 50  ? 3.57000   6.06000   -7.68400  1.000 14.45546 ? 50  ASN A CB  1 
ATOM   378  C CG  . ASN A 1 50  ? 2.38300   6.01300   -6.71500  1.000 17.90153 ? 50  ASN A CG  1 
ATOM   379  O OD1 . ASN A 1 50  ? 2.20900   5.03800   -5.96800  1.000 19.48314 ? 50  ASN A OD1 1 
ATOM   380  N ND2 . ASN A 1 50  ? 1.55500   7.06000   -6.73000  1.000 14.59273 ? 50  ASN A ND2 1 
ATOM   381  N N   . VAL A 1 51  ? 5.99600   4.31400   -9.56100  1.000 12.36436 ? 51  VAL A N   1 
ATOM   382  C CA  . VAL A 1 51  ? 6.52700   4.01300   -10.89200 1.000 13.67021 ? 51  VAL A CA  1 
ATOM   383  C C   . VAL A 1 51  ? 6.83500   2.52300   -10.98000 1.000 14.89412 ? 51  VAL A C   1 
ATOM   384  O O   . VAL A 1 51  ? 7.49700   1.97200   -10.09300 1.000 14.12797 ? 51  VAL A O   1 
ATOM   385  C CB  . VAL A 1 51  ? 7.79000   4.83800   -11.18900 1.000 17.19862 ? 51  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 51  ? 8.34800   4.47600   -12.56100 1.000 16.33392 ? 51  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 51  ? 7.50800   6.35300   -11.09400 1.000 13.82097 ? 51  VAL A CG2 1 
ATOM   388  N N   . PHE A 1 52  ? 6.37800   1.87300   -12.05900 1.000 14.26597 ? 52  PHE A N   1 
ATOM   389  C CA  . PHE A 1 52  ? 6.71400   0.48400   -12.37300 1.000 13.33736 ? 52  PHE A CA  1 
ATOM   390  C C   . PHE A 1 52  ? 7.40500   0.42900   -13.72800 1.000 17.45805 ? 52  PHE A C   1 
ATOM   391  O O   . PHE A 1 52  ? 7.01300   1.13000   -14.66700 1.000 13.07966 ? 52  PHE A O   1 
ATOM   392  C CB  . PHE A 1 52  ? 5.45900   -0.41900  -12.38600 1.000 14.24642 ? 52  PHE A CB  1 
ATOM   393  C CG  . PHE A 1 52  ? 4.81200   -0.58600  -11.03100 1.000 16.45512 ? 52  PHE A CG  1 
ATOM   394  C CD1 . PHE A 1 52  ? 4.13600   0.46400   -10.43700 1.000 15.33709 ? 52  PHE A CD1 1 
ATOM   395  C CD2 . PHE A 1 52  ? 4.89100   -1.79300  -10.34700 1.000 15.87495 ? 52  PHE A CD2 1 
ATOM   396  C CE1 . PHE A 1 52  ? 3.55100   0.33300   -9.19000  1.000 15.25253 ? 52  PHE A CE1 1 
ATOM   397  C CE2 . PHE A 1 52  ? 4.30100   -1.93400  -9.09300  1.000 18.52308 ? 52  PHE A CE2 1 
ATOM   398  C CZ  . PHE A 1 52  ? 3.63100   -0.87300  -8.51400  1.000 17.12872 ? 52  PHE A CZ  1 
ATOM   399  N N   . LEU A 1 53  ? 8.43900   -0.39800  -13.84000 1.000 15.32915 ? 53  LEU A N   1 
ATOM   400  C CA  . LEU A 1 53  ? 9.11600   -0.60900  -15.11600 1.000 15.91573 ? 53  LEU A CA  1 
ATOM   401  C C   . LEU A 1 53  ? 9.08800   -2.10000  -15.40600 1.000 22.50239 ? 53  LEU A C   1 
ATOM   402  O O   . LEU A 1 53  ? 9.55800   -2.89800  -14.59100 1.000 18.96235 ? 53  LEU A O   1 
ATOM   403  C CB  . LEU A 1 53  ? 10.55300  -0.07600  -15.08500 1.000 18.00202 ? 53  LEU A CB  1 
ATOM   404  C CG  . LEU A 1 53  ? 10.73900  1.43200   -14.83000 1.000 22.39218 ? 53  LEU A CG  1 
ATOM   405  C CD1 . LEU A 1 53  ? 12.20500  1.84100   -14.72400 1.000 19.18741 ? 53  LEU A CD1 1 
ATOM   406  C CD2 . LEU A 1 53  ? 10.04800  2.26400   -15.91400 1.000 18.05667 ? 53  LEU A CD2 1 
ATOM   407  N N   . GLY A 1 54  ? 8.50900   -2.48000  -16.53900 1.000 22.79854 ? 54  GLY A N   1 
ATOM   408  C CA  . GLY A 1 54  ? 8.33600   -3.89400  -16.82100 1.000 25.22289 ? 54  GLY A CA  1 
ATOM   409  C C   . GLY A 1 54  ? 7.56600   -4.61400  -15.73300 1.000 25.57610 ? 54  GLY A C   1 
ATOM   410  O O   . GLY A 1 54  ? 7.78500   -5.80300  -15.49200 1.000 25.67679 ? 54  GLY A O   1 
ATOM   411  N N   . GLY A 1 55  ? 6.66900   -3.89900  -15.05700 1.000 20.50417 ? 55  GLY A N   1 
ATOM   412  C CA  . GLY A 1 55  ? 5.89100   -4.46600  -13.97900 1.000 17.19459 ? 55  GLY A CA  1 
ATOM   413  C C   . GLY A 1 55  ? 6.58000   -4.49100  -12.63300 1.000 21.18297 ? 55  GLY A C   1 
ATOM   414  O O   . GLY A 1 55  ? 5.97200   -4.94300  -11.65200 1.000 22.46871 ? 55  GLY A O   1 
ATOM   415  N N   . VAL A 1 56  ? 7.81700   -4.00900  -12.55100 1.000 19.87057 ? 56  VAL A N   1 
ATOM   416  C CA  . VAL A 1 56  ? 8.61100   -4.04100  -11.33100 1.000 19.80800 ? 56  VAL A CA  1 
ATOM   417  C C   . VAL A 1 56  ? 8.55900   -2.67500  -10.66200 1.000 17.28499 ? 56  VAL A C   1 
ATOM   418  O O   . VAL A 1 56  ? 8.90800   -1.65700  -11.27700 1.000 16.94527 ? 56  VAL A O   1 
ATOM   419  C CB  . VAL A 1 56  ? 10.06500  -4.43900  -11.63200 1.000 21.59143 ? 56  VAL A CB  1 
ATOM   420  C CG1 . VAL A 1 56  ? 10.86900  -4.50400  -10.33100 1.000 22.86937 ? 56  VAL A CG1 1 
ATOM   421  C CG2 . VAL A 1 56  ? 10.10800  -5.77500  -12.37400 1.000 22.72833 ? 56  VAL A CG2 1 
ATOM   422  N N   . GLN A 1 57  ? 8.18000   -2.66000  -9.38700  1.000 18.56025 ? 57  GLN A N   1 
ATOM   423  C CA  . GLN A 1 57  ? 8.06300   -1.40800  -8.65200  1.000 18.83442 ? 57  GLN A CA  1 
ATOM   424  C C   . GLN A 1 57  ? 9.42800   -0.76500  -8.44800  1.000 21.82323 ? 57  GLN A C   1 
ATOM   425  O O   . GLN A 1 57  ? 10.38700  -1.42600  -8.04300  1.000 22.01007 ? 57  GLN A O   1 
ATOM   426  C CB  . GLN A 1 57  ? 7.39700   -1.65300  -7.30500  1.000 21.45567 ? 57  GLN A CB  1 
ATOM   427  C CG  . GLN A 1 57  ? 7.14500   -0.37800  -6.50700  1.000 18.53322 ? 57  GLN A CG  1 
ATOM   428  C CD  . GLN A 1 57  ? 6.41000   -0.66000  -5.22500  1.000 27.26994 ? 57  GLN A CD  1 
ATOM   429  O OE1 . GLN A 1 57  ? 6.78300   -1.55500  -4.47100  1.000 27.19444 ? 57  GLN A OE1 1 
ATOM   430  N NE2 . GLN A 1 57  ? 5.34700   0.09100   -4.97400  1.000 20.08683 ? 57  GLN A NE2 1 
ATOM   431  N N   . GLN A 1 58  ? 9.51500   0.53300   -8.71500  1.000 17.09250 ? 58  GLN A N   1 
ATOM   432  C CA  . GLN A 1 58  ? 10.76800  1.26200   -8.64600  1.000 20.24063 ? 58  GLN A CA  1 
ATOM   433  C C   . GLN A 1 58  ? 10.87600  2.03100   -7.34300  1.000 18.68548 ? 58  GLN A C   1 
ATOM   434  O O   . GLN A 1 58  ? 9.89500   2.23700   -6.62600  1.000 19.74728 ? 58  GLN A O   1 
ATOM   435  C CB  . GLN A 1 58  ? 10.89400  2.21500   -9.83300  1.000 24.67532 ? 58  GLN A CB  1 
ATOM   436  C CG  . GLN A 1 58  ? 10.84300  1.49900   -11.17200 1.000 19.38797 ? 58  GLN A CG  1 
ATOM   437  C CD  . GLN A 1 58  ? 12.01200  0.54900   -11.35200 1.000 25.22646 ? 58  GLN A CD  1 
ATOM   438  O OE1 . GLN A 1 58  ? 13.16300  0.96500   -11.32000 1.000 26.36149 ? 58  GLN A OE1 1 
ATOM   439  N NE2 . GLN A 1 58  ? 11.71600  -0.73800  -11.51500 1.000 22.66437 ? 58  GLN A NE2 1 
ATOM   440  N N   . GLY A 1 59  ? 12.10100  2.45600   -7.04400  1.000 21.38923 ? 59  GLY A N   1 
ATOM   441  C CA  . GLY A 1 59  ? 12.36000  3.35400   -5.93400  1.000 24.82435 ? 59  GLY A CA  1 
ATOM   442  C C   . GLY A 1 59  ? 11.98900  4.76600   -6.33200  1.000 29.77058 ? 59  GLY A C   1 
ATOM   443  O O   . GLY A 1 59  ? 11.05900  4.99000   -7.11700  1.000 30.05753 ? 59  GLY A O   1 
ATOM   444  N N   . GLY A 1 60  ? 12.73200  5.73500   -5.81600  1.000 29.88043 ? 60  GLY A N   1 
ATOM   445  C CA  . GLY A 1 60  ? 12.38200  7.11100   -6.10900  1.000 28.96871 ? 60  GLY A CA  1 
ATOM   446  C C   . GLY A 1 60  ? 13.23700  7.77900   -7.15700  1.000 24.76924 ? 60  GLY A C   1 
ATOM   447  O O   . GLY A 1 60  ? 13.21300  9.00200   -7.26600  1.000 24.86509 ? 60  GLY A O   1 
ATOM   448  N N   . ASP A 1 61  ? 13.98200  7.01600   -7.95300  1.000 26.47636 ? 61  ASP A N   1 
ATOM   449  C CA  . ASP A 1 61  ? 14.97600  7.63500   -8.81400  1.000 25.00725 ? 61  ASP A CA  1 
ATOM   450  C C   . ASP A 1 61  ? 14.48500  7.95300   -10.22300 1.000 27.94820 ? 61  ASP A C   1 
ATOM   451  O O   . ASP A 1 61  ? 15.20000  8.62800   -10.95600 1.000 28.68374 ? 61  ASP A O   1 
ATOM   452  C CB  . ASP A 1 61  ? 16.22200  6.74600   -8.91600  1.000 34.13250 ? 61  ASP A CB  1 
ATOM   453  C CG  . ASP A 1 61  ? 17.33100  7.16900   -7.95600  1.000 40.34129 ? 61  ASP A CG  1 
ATOM   454  O OD1 . ASP A 1 61  ? 17.05800  7.94500   -7.01200  1.000 36.51229 ? 61  ASP A OD1 1 
ATOM   455  O OD2 . ASP A 1 61  ? 18.48600  6.73200   -8.16000  1.000 51.86592 ? 61  ASP A OD2 1 
ATOM   456  N N   . THR A 1 62  ? 13.31300  7.50400   -10.64700 1.000 21.60833 ? 62  THR A N   1 
ATOM   457  C CA  . THR A 1 62  ? 12.97900  7.76600   -12.04000 1.000 19.66234 ? 62  THR A CA  1 
ATOM   458  C C   . THR A 1 62  ? 12.58300  9.22700   -12.22800 1.000 17.24799 ? 62  THR A C   1 
ATOM   459  O O   . THR A 1 62  ? 12.01700  9.86300   -11.33000 1.000 17.35635 ? 62  THR A O   1 
ATOM   460  C CB  . THR A 1 62  ? 11.86000  6.83700   -12.52200 1.000 22.79161 ? 62  THR A CB  1 
ATOM   461  O OG1 . THR A 1 62  ? 12.17400  5.48200   -12.16300 1.000 28.75682 ? 62  THR A OG1 1 
ATOM   462  C CG2 . THR A 1 62  ? 11.71900  6.93000   -14.04700 1.000 22.32357 ? 62  THR A CG2 1 
ATOM   463  N N   . ILE A 1 63  ? 12.92900  9.77300   -13.39300 1.000 14.62410 ? 63  ILE A N   1 
ATOM   464  C CA  . ILE A 1 63  ? 12.46300  11.08500  -13.82500 1.000 15.60041 ? 63  ILE A CA  1 
ATOM   465  C C   . ILE A 1 63  ? 11.89800  10.94200  -15.23100 1.000 17.18547 ? 63  ILE A C   1 
ATOM   466  O O   . ILE A 1 63  ? 12.57600  10.42700  -16.12800 1.000 15.99786 ? 63  ILE A O   1 
ATOM   467  C CB  . ILE A 1 63  ? 13.58300  12.14100  -13.82000 1.000 16.18401 ? 63  ILE A CB  1 
ATOM   468  C CG1 . ILE A 1 63  ? 14.21800  12.26400  -12.44500 1.000 21.61039 ? 63  ILE A CG1 1 
ATOM   469  C CG2 . ILE A 1 63  ? 13.03200  13.50000  -14.18000 1.000 13.69747 ? 63  ILE A CG2 1 
ATOM   470  C CD1 . ILE A 1 63  ? 15.39600  13.23800  -12.46100 1.000 26.01986 ? 63  ILE A CD1 1 
ATOM   471  N N   . PHE A 1 64  ? 10.66600  11.39900  -15.42900 1.000 11.68903 ? 64  PHE A N   1 
ATOM   472  C CA  . PHE A 1 64  ? 10.07600  11.44600  -16.76000 1.000 9.29540  ? 64  PHE A CA  1 
ATOM   473  C C   . PHE A 1 64  ? 9.71700   12.89100  -17.07800 1.000 10.65192 ? 64  PHE A C   1 
ATOM   474  O O   . PHE A 1 64  ? 8.99200   13.53900  -16.31900 1.000 10.59555 ? 64  PHE A O   1 
ATOM   475  C CB  . PHE A 1 64  ? 8.84700   10.53400  -16.85600 1.000 11.66359 ? 64  PHE A CB  1 
ATOM   476  C CG  . PHE A 1 64  ? 8.04500   10.71200  -18.13100 1.000 11.82530 ? 64  PHE A CG  1 
ATOM   477  C CD1 . PHE A 1 64  ? 8.66800   10.67600  -19.37100 1.000 11.64782 ? 64  PHE A CD1 1 
ATOM   478  C CD2 . PHE A 1 64  ? 6.66100   10.89500  -18.07500 1.000 11.21890 ? 64  PHE A CD2 1 
ATOM   479  C CE1 . PHE A 1 64  ? 7.94100   10.83700  -20.55400 1.000 10.83637 ? 64  PHE A CE1 1 
ATOM   480  C CE2 . PHE A 1 64  ? 5.90400   11.05400  -19.26000 1.000 10.84180 ? 64  PHE A CE2 1 
ATOM   481  C CZ  . PHE A 1 64  ? 6.54000   11.03000  -20.49300 1.000 10.69305 ? 64  PHE A CZ  1 
ATOM   482  N N   . VAL A 1 65  ? 10.22600  13.38800  -18.19700 1.000 9.08036  ? 65  VAL A N   1 
ATOM   483  C CA  . VAL A 1 65  ? 9.99400   14.75300  -18.64700 1.000 10.83895 ? 65  VAL A CA  1 
ATOM   484  C C   . VAL A 1 65  ? 9.10600   14.68600  -19.88600 1.000 12.01449 ? 65  VAL A C   1 
ATOM   485  O O   . VAL A 1 65  ? 9.51000   14.14200  -20.91900 1.000 10.88192 ? 65  VAL A O   1 
ATOM   486  C CB  . VAL A 1 65  ? 11.30800  15.49000  -18.96500 1.000 11.43536 ? 65  VAL A CB  1 
ATOM   487  C CG1 . VAL A 1 65  ? 11.01300  16.89200  -19.45700 1.000 11.30394 ? 65  VAL A CG1 1 
ATOM   488  C CG2 . VAL A 1 65  ? 12.25700  15.53500  -17.76300 1.000 11.72185 ? 65  VAL A CG2 1 
ATOM   489  N N   . HIS A 1 66  ? 7.90800   15.25200  -19.79800 1.000 8.75971  ? 66  HIS A N   1 
ATOM   490  C CA  . HIS A 1 66  ? 7.00800   15.34500  -20.94600 1.000 9.76554  ? 66  HIS A CA  1 
ATOM   491  C C   . HIS A 1 66  ? 6.97500   16.80400  -21.38400 1.000 9.53696  ? 66  HIS A C   1 
ATOM   492  O O   . HIS A 1 66  ? 6.37900   17.64800  -20.70200 1.000 9.32948  ? 66  HIS A O   1 
ATOM   493  C CB  . HIS A 1 66  ? 5.61000   14.81900  -20.60800 1.000 10.53996 ? 66  HIS A CB  1 
ATOM   494  C CG  . HIS A 1 66  ? 4.72900   14.61600  -21.80600 1.000 11.68701 ? 66  HIS A CG  1 
ATOM   495  N ND1 . HIS A 1 66  ? 3.36400   14.43800  -21.69900 1.000 11.22187 ? 66  HIS A ND1 1 
ATOM   496  C CD2 . HIS A 1 66  ? 5.01600   14.55100  -23.13100 1.000 10.09196 ? 66  HIS A CD2 1 
ATOM   497  C CE1 . HIS A 1 66  ? 2.84700   14.28200  -22.90900 1.000 12.56369 ? 66  HIS A CE1 1 
ATOM   498  N NE2 . HIS A 1 66  ? 3.82700   14.33900  -23.79300 1.000 12.81682 ? 66  HIS A NE2 1 
ATOM   499  N N   . GLY A 1 67  ? 7.64500   17.09500  -22.49500 1.000 8.80052  ? 67  GLY A N   1 
ATOM   500  C CA  . GLY A 1 67  ? 7.70600   18.44300  -23.02200 1.000 11.26865 ? 67  GLY A CA  1 
ATOM   501  C C   . GLY A 1 67  ? 6.57500   18.66900  -24.00200 1.000 13.13159 ? 67  GLY A C   1 
ATOM   502  O O   . GLY A 1 67  ? 6.33500   17.84200  -24.88500 1.000 11.87115 ? 67  GLY A O   1 
ATOM   503  N N   . LEU A 1 68  ? 5.86900   19.78800  -23.83500 1.000 9.23038  ? 68  LEU A N   1 
ATOM   504  C CA  . LEU A 1 68  ? 4.72800   20.12700  -24.68200 1.000 9.80434  ? 68  LEU A CA  1 
ATOM   505  C C   . LEU A 1 68  ? 5.08900   21.37500  -25.47700 1.000 11.82879 ? 68  LEU A C   1 
ATOM   506  O O   . LEU A 1 68  ? 5.19300   22.46600  -24.91100 1.000 10.87299 ? 68  LEU A O   1 
ATOM   507  C CB  . LEU A 1 68  ? 3.47000   20.33400  -23.84600 1.000 10.15654 ? 68  LEU A CB  1 
ATOM   508  C CG  . LEU A 1 68  ? 3.15200   19.08800  -23.01100 1.000 12.87628 ? 68  LEU A CG  1 
ATOM   509  C CD1 . LEU A 1 68  ? 2.01500   19.38400  -22.02900 1.000 13.77126 ? 68  LEU A CD1 1 
ATOM   510  C CD2 . LEU A 1 68  ? 2.80400   17.92300  -23.93800 1.000 14.23560 ? 68  LEU A CD2 1 
ATOM   511  N N   . HIS A 1 69  ? 5.25100   21.20800  -26.79000 1.000 10.21824 ? 69  HIS A N   1 
ATOM   512  C CA  . HIS A 1 69  ? 5.84700   22.20000  -27.66800 1.000 14.39601 ? 69  HIS A CA  1 
ATOM   513  C C   . HIS A 1 69  ? 4.89400   22.61500  -28.77900 1.000 14.25766 ? 69  HIS A C   1 
ATOM   514  O O   . HIS A 1 69  ? 3.97900   21.88200  -29.16000 1.000 12.51646 ? 69  HIS A O   1 
ATOM   515  C CB  . HIS A 1 69  ? 7.13200   21.66500  -28.32400 1.000 15.30177 ? 69  HIS A CB  1 
ATOM   516  C CG  . HIS A 1 69  ? 8.22200   21.36300  -27.34600 1.000 17.93024 ? 69  HIS A CG  1 
ATOM   517  N ND1 . HIS A 1 69  ? 9.13000   22.31400  -26.93100 1.000 23.45690 ? 69  HIS A ND1 1 
ATOM   518  C CD2 . HIS A 1 69  ? 8.54100   20.22500  -26.68800 1.000 21.92316 ? 69  HIS A CD2 1 
ATOM   519  C CE1 . HIS A 1 69  ? 9.97000   21.77100  -26.06900 1.000 19.68760 ? 69  HIS A CE1 1 
ATOM   520  N NE2 . HIS A 1 69  ? 9.63300   20.50600  -25.90100 1.000 21.36451 ? 69  HIS A NE2 1 
ATOM   521  N N   . ARG A 1 70  ? 5.17000   23.77700  -29.35600 1.000 13.24581 ? 70  ARG A N   1 
ATOM   522  C CA  . ARG A 1 70  ? 4.49900   24.14200  -30.58800 1.000 15.49728 ? 70  ARG A CA  1 
ATOM   523  C C   . ARG A 1 70  ? 5.16700   23.41200  -31.75300 1.000 16.75824 ? 70  ARG A C   1 
ATOM   524  O O   . ARG A 1 70  ? 6.38000   23.16800  -31.74300 1.000 14.45470 ? 70  ARG A O   1 
ATOM   525  C CB  . ARG A 1 70  ? 4.50600   25.66700  -30.77300 1.000 21.79058 ? 70  ARG A CB  1 
ATOM   526  C CG  . ARG A 1 70  ? 5.54100   26.22300  -31.69700 1.000 35.04484 ? 70  ARG A CG  1 
ATOM   527  C CD  . ARG A 1 70  ? 5.20300   27.67500  -32.06500 1.000 34.76285 ? 70  ARG A CD  1 
ATOM   528  N NE  . ARG A 1 70  ? 6.39800   28.51000  -32.14600 1.000 50.82303 ? 70  ARG A NE  1 
ATOM   529  C CZ  . ARG A 1 70  ? 7.22400   28.54700  -33.18400 1.000 52.92255 ? 70  ARG A CZ  1 
ATOM   530  N NH1 . ARG A 1 70  ? 7.01400   27.80600  -34.26100 1.000 43.23990 ? 70  ARG A NH1 1 
ATOM   531  N NH2 . ARG A 1 70  ? 8.29300   29.33900  -33.13500 1.000 52.43764 ? 70  ARG A NH2 1 
ATOM   532  N N   . GLU A 1 71  ? 4.34900   22.97500  -32.70500 1.000 15.25179 ? 71  GLU A N   1 
ATOM   533  C CA  . GLU A 1 71  ? 4.85000   22.37100  -33.93100 1.000 17.94678 ? 71  GLU A CA  1 
ATOM   534  C C   . GLU A 1 71  ? 5.75100   23.34900  -34.67600 1.000 16.59266 ? 71  GLU A C   1 
ATOM   535  O O   . GLU A 1 71  ? 5.66700   24.56600  -34.50100 1.000 21.27698 ? 71  GLU A O   1 
ATOM   536  C CB  . GLU A 1 71  ? 3.68600   21.95100  -34.84000 1.000 16.76421 ? 71  GLU A CB  1 
ATOM   537  C CG  . GLU A 1 71  ? 3.00600   20.66100  -34.41900 1.000 22.37840 ? 71  GLU A CG  1 
ATOM   538  C CD  . GLU A 1 71  ? 1.68900   20.39500  -35.14400 1.000 29.67323 ? 71  GLU A CD  1 
ATOM   539  O OE1 . GLU A 1 71  ? 1.37000   21.11300  -36.12700 1.000 29.15720 ? 71  GLU A OE1 1 
ATOM   540  O OE2 . GLU A 1 71  ? 0.97500   19.46200  -34.71600 1.000 28.96738 ? 71  GLU A OE2 1 
ATOM   541  N N   . GLY A 1 72  ? 6.62300   22.80300  -35.52300 1.000 18.36923 ? 72  GLY A N   1 
ATOM   542  C CA  . GLY A 1 72  ? 7.40300   23.61100  -36.44900 1.000 18.80817 ? 72  GLY A CA  1 
ATOM   543  C C   . GLY A 1 72  ? 8.90600   23.47200  -36.34200 1.000 17.83453 ? 72  GLY A C   1 
ATOM   544  O O   . GLY A 1 72  ? 9.61500   23.94000  -37.24500 1.000 20.56677 ? 72  GLY A O   1 
ATOM   545  N N   . ARG A 1 73  ? 9.44700   22.85400  -35.29500 1.000 19.45892 ? 73  ARG A N   1 
ATOM   546  C CA  . ARG A 1 73  ? 10.89000  22.68200  -35.23400 1.000 18.82749 ? 73  ARG A CA  1 
ATOM   547  C C   . ARG A 1 73  ? 11.31600  21.47200  -36.05800 1.000 17.73369 ? 73  ARG A C   1 
ATOM   548  O O   . ARG A 1 73  ? 10.54800  20.52700  -36.27700 1.000 14.91397 ? 73  ARG A O   1 
ATOM   549  C CB  . ARG A 1 73  ? 11.37500  22.50600  -33.78500 1.000 18.54385 ? 73  ARG A CB  1 
ATOM   550  C CG  . ARG A 1 73  ? 10.99800  23.63100  -32.83500 1.000 26.82155 ? 73  ARG A CG  1 
ATOM   551  C CD  . ARG A 1 73  ? 11.68500  24.93300  -33.19000 1.000 35.37334 ? 73  ARG A CD  1 
ATOM   552  N NE  . ARG A 1 73  ? 11.40200  25.95800  -32.19100 1.000 45.09473 ? 73  ARG A NE  1 
ATOM   553  C CZ  . ARG A 1 73  ? 11.86700  27.19900  -32.23400 1.000 46.80564 ? 73  ARG A CZ  1 
ATOM   554  N NH1 . ARG A 1 73  ? 12.65600  27.60600  -33.21500 1.000 43.79188 ? 73  ARG A NH1 1 
ATOM   555  N NH2 . ARG A 1 73  ? 11.52900  28.05200  -31.26900 1.000 45.56768 ? 73  ARG A NH2 1 
ATOM   556  N N   . SER A 1 74  ? 12.57600  21.48900  -36.48500 1.000 18.44329 ? 74  SER A N   1 
ATOM   557  C CA  . SER A 1 74  ? 13.11100  20.36000  -37.22700 1.000 17.59349 ? 74  SER A CA  1 
ATOM   558  C C   . SER A 1 74  ? 13.30200  19.16300  -36.30400 1.000 19.25595 ? 74  SER A C   1 
ATOM   559  O O   . SER A 1 74  ? 13.47000  19.30700  -35.08700 1.000 16.58914 ? 74  SER A O   1 
ATOM   560  C CB  . SER A 1 74  ? 14.44600  20.73200  -37.85800 1.000 18.64985 ? 74  SER A CB  1 
ATOM   561  O OG  . SER A 1 74  ? 15.45000  20.74300  -36.86200 1.000 18.16791 ? 74  SER A OG  1 
ATOM   562  N N   . ALA A 1 75  ? 13.29600  17.96500  -36.90100 1.000 17.01933 ? 75  ALA A N   1 
ATOM   563  C CA  . ALA A 1 75  ? 13.59300  16.76100  -36.13100 1.000 18.61082 ? 75  ALA A CA  1 
ATOM   564  C C   . ALA A 1 75  ? 14.97100  16.84600  -35.47900 1.000 18.66420 ? 75  ALA A C   1 
ATOM   565  O O   . ALA A 1 75  ? 15.16400  16.37400  -34.35200 1.000 20.13937 ? 75  ALA A O   1 
ATOM   566  C CB  . ALA A 1 75  ? 13.49200  15.52800  -37.02400 1.000 23.64439 ? 75  ALA A CB  1 
ATOM   567  N N   . ASP A 1 76  ? 15.94100  17.46400  -36.16200 1.000 18.46208 ? 76  ASP A N   1 
ATOM   568  C CA  . ASP A 1 76  ? 17.28900  17.56500  -35.60000 1.000 24.19329 ? 76  ASP A CA  1 
ATOM   569  C C   . ASP A 1 76  ? 17.30200  18.43000  -34.34200 1.000 19.58423 ? 76  ASP A C   1 
ATOM   570  O O   . ASP A 1 76  ? 17.91500  18.07100  -33.32900 1.000 22.35564 ? 76  ASP A O   1 
ATOM   571  C CB  . ASP A 1 76  ? 18.25500  18.13000  -36.64500 1.000 28.63758 ? 76  ASP A CB  1 
ATOM   572  C CG  . ASP A 1 76  ? 19.70000  18.19000  -36.14400 1.000 40.38627 ? 76  ASP A CG  1 
ATOM   573  O OD1 . ASP A 1 76  ? 20.03500  17.50500  -35.15000 1.000 40.87585 ? 76  ASP A OD1 1 
ATOM   574  O OD2 . ASP A 1 76  ? 20.50900  18.92900  -36.74700 1.000 49.28170 ? 76  ASP A OD2 1 
ATOM   575  N N   . LEU A 1 77  ? 16.64900  19.58900  -34.39100 1.000 20.29334 ? 77  LEU A N   1 
ATOM   576  C CA  . LEU A 1 77  ? 16.62600  20.44700  -33.21200 1.000 21.37231 ? 77  LEU A CA  1 
ATOM   577  C C   . LEU A 1 77  ? 15.90900  19.76100  -32.05500 1.000 20.29740 ? 77  LEU A C   1 
ATOM   578  O O   . LEU A 1 77  ? 16.38300  19.80400  -30.91300 1.000 20.60848 ? 77  LEU A O   1 
ATOM   579  C CB  . LEU A 1 77  ? 15.97300  21.78600  -33.54800 1.000 19.50985 ? 77  LEU A CB  1 
ATOM   580  C CG  . LEU A 1 77  ? 15.66500  22.76300  -32.40800 1.000 29.23837 ? 77  LEU A CG  1 
ATOM   581  C CD1 . LEU A 1 77  ? 16.83500  22.92000  -31.43900 1.000 37.56383 ? 77  LEU A CD1 1 
ATOM   582  C CD2 . LEU A 1 77  ? 15.26200  24.11200  -32.97200 1.000 34.25740 ? 77  LEU A CD2 1 
ATOM   583  N N   . LYS A 1 78  ? 14.77900  19.10400  -32.32900 1.000 16.51035 ? 78  LYS A N   1 
ATOM   584  C CA  . LYS A 1 78  ? 14.04000  18.44600  -31.25500 1.000 17.13990 ? 78  LYS A CA  1 
ATOM   585  C C   . LYS A 1 78  ? 14.86900  17.34500  -30.61100 1.000 21.31463 ? 78  LYS A C   1 
ATOM   586  O O   . LYS A 1 78  ? 14.85700  17.18500  -29.38500 1.000 20.16773 ? 78  LYS A O   1 
ATOM   587  C CB  . LYS A 1 78  ? 12.70900  17.89700  -31.79000 1.000 18.00134 ? 78  LYS A CB  1 
ATOM   588  C CG  . LYS A 1 78  ? 11.71100  19.01000  -32.11200 1.000 19.46361 ? 78  LYS A CG  1 
ATOM   589  C CD  . LYS A 1 78  ? 10.36500  18.49300  -32.64800 1.000 21.21539 ? 78  LYS A CD  1 
ATOM   590  C CE  . LYS A 1 78  ? 10.50100  17.78400  -33.98900 1.000 20.09113 ? 78  LYS A CE  1 
ATOM   591  N NZ  . LYS A 1 78  ? 9.15000   17.42200  -34.53600 1.000 21.46770 ? 78  LYS A NZ  1 
ATOM   592  N N   . GLY A 1 79  ? 15.59900  16.57700  -31.42000 1.000 19.69376 ? 79  GLY A N   1 
ATOM   593  C CA  . GLY A 1 79  ? 16.45300  15.54400  -30.86000 1.000 20.30502 ? 79  GLY A CA  1 
ATOM   594  C C   . GLY A 1 79  ? 17.61800  16.12400  -30.08200 1.000 19.64274 ? 79  GLY A C   1 
ATOM   595  O O   . GLY A 1 79  ? 17.99200  15.59500  -29.03200 1.000 24.60478 ? 79  GLY A O   1 
ATOM   596  N N   . GLN A 1 80  ? 18.19400  17.22800  -30.57700 1.000 17.18230 ? 80  GLN A N   1 
ATOM   597  C CA  . GLN A 1 80  ? 19.25100  17.92000  -29.83700 1.000 21.86207 ? 80  GLN A CA  1 
ATOM   598  C C   . GLN A 1 80  ? 18.74200  18.42400  -28.48800 1.000 22.56502 ? 80  GLN A C   1 
ATOM   599  O O   . GLN A 1 80  ? 19.43700  18.31600  -27.46900 1.000 19.31896 ? 80  GLN A O   1 
ATOM   600  C CB  . GLN A 1 80  ? 19.78900  19.09300  -30.65400 1.000 24.56057 ? 80  GLN A CB  1 
ATOM   601  C CG  . GLN A 1 80  ? 20.67100  18.71800  -31.83600 1.000 29.45717 ? 80  GLN A CG  1 
ATOM   602  C CD  . GLN A 1 80  ? 21.37900  19.92800  -32.42500 1.000 41.42268 ? 80  GLN A CD  1 
ATOM   603  O OE1 . GLN A 1 80  ? 22.11500  20.63500  -31.72500 1.000 43.63790 ? 80  GLN A OE1 1 
ATOM   604  N NE2 . GLN A 1 80  ? 21.15100  20.18400  -33.71600 1.000 43.05152 ? 80  GLN A NE2 1 
ATOM   605  N N   . LEU A 1 81  ? 17.54300  19.01100  -28.47500 1.000 18.51059 ? 81  LEU A N   1 
ATOM   606  C CA  . LEU A 1 81  ? 16.97100  19.51400  -27.22900 1.000 18.83060 ? 81  LEU A CA  1 
ATOM   607  C C   . LEU A 1 81  ? 16.68400  18.38300  -26.24900 1.000 18.51468 ? 81  LEU A C   1 
ATOM   608  O O   . LEU A 1 81  ? 16.97800  18.50300  -25.05400 1.000 15.66063 ? 81  LEU A O   1 
ATOM   609  C CB  . LEU A 1 81  ? 15.70400  20.31500  -27.53300 1.000 19.13770 ? 81  LEU A CB  1 
ATOM   610  C CG  . LEU A 1 81  ? 14.95200  20.92600  -26.33800 1.000 22.36863 ? 81  LEU A CG  1 
ATOM   611  C CD1 . LEU A 1 81  ? 15.87500  21.81700  -25.50200 1.000 22.90977 ? 81  LEU A CD1 1 
ATOM   612  C CD2 . LEU A 1 81  ? 13.72400  21.72700  -26.80600 1.000 20.21162 ? 81  LEU A CD2 1 
ATOM   613  N N   . ALA A 1 82  ? 16.10300  17.28000  -26.72000 1.000 15.55381 ? 82  ALA A N   1 
ATOM   614  C CA  . ALA A 1 82  ? 15.82600  16.16600  -25.81600 1.000 17.52293 ? 82  ALA A CA  1 
ATOM   615  C C   . ALA A 1 82  ? 17.11600  15.61700  -25.20500 1.000 20.50326 ? 82  ALA A C   1 
ATOM   616  O O   . ALA A 1 82  ? 17.18800  15.36300  -23.99500 1.000 20.42006 ? 82  ALA A O   1 
ATOM   617  C CB  . ALA A 1 82  ? 15.06100  15.06700  -26.54900 1.000 19.58928 ? 82  ALA A CB  1 
ATOM   618  N N   . GLN A 1 83  ? 18.15000  15.44000  -26.03000 1.000 20.70839 ? 83  GLN A N   1 
ATOM   619  C CA  . GLN A 1 83  ? 19.43900  14.95600  -25.53500 1.000 23.96604 ? 83  GLN A CA  1 
ATOM   620  C C   . GLN A 1 83  ? 20.06100  15.93600  -24.54000 1.000 21.64854 ? 83  GLN A C   1 
ATOM   621  O O   . GLN A 1 83  ? 20.62400  15.52800  -23.51400 1.000 24.05366 ? 83  GLN A O   1 
ATOM   622  C CB  . GLN A 1 83  ? 20.37600  14.71400  -26.72400 1.000 28.49779 ? 83  GLN A CB  1 
ATOM   623  C CG  . GLN A 1 83  ? 21.71500  14.07600  -26.38000 1.000 42.97686 ? 83  GLN A CG  1 
ATOM   624  C CD  . GLN A 1 83  ? 22.69800  14.11800  -27.54600 1.000 53.85614 ? 83  GLN A CD  1 
ATOM   625  O OE1 . GLN A 1 83  ? 23.42600  13.15600  -27.79400 1.000 59.86804 ? 83  GLN A OE1 1 
ATOM   626  N NE2 . GLN A 1 83  ? 22.72400  15.24300  -28.26300 1.000 50.70233 ? 83  GLN A NE2 1 
ATOM   627  N N   . ARG A 1 84  ? 19.98400  17.23300  -24.83800 1.000 19.59507 ? 84  ARG A N   1 
ATOM   628  C CA  . ARG A 1 84  ? 20.48400  18.25900  -23.92500 1.000 22.71923 ? 84  ARG A CA  1 
ATOM   629  C C   . ARG A 1 84  ? 19.75700  18.23000  -22.58200 1.000 22.03959 ? 84  ARG A C   1 
ATOM   630  O O   . ARG A 1 84  ? 20.37300  18.42700  -21.52700 1.000 21.34070 ? 84  ARG A O   1 
ATOM   631  C CB  . ARG A 1 84  ? 20.34900  19.62900  -24.59000 1.000 23.95193 ? 84  ARG A CB  1 
ATOM   632  C CG  . ARG A 1 84  ? 20.65600  20.83400  -23.70800 1.000 28.70889 ? 84  ARG A CG  1 
ATOM   633  C CD  . ARG A 1 84  ? 22.12500  20.92200  -23.38100 1.000 41.93686 ? 84  ARG A CD  1 
ATOM   634  N NE  . ARG A 1 84  ? 22.93000  20.46800  -24.50500 1.000 51.76789 ? 84  ARG A NE  1 
ATOM   635  C CZ  . ARG A 1 84  ? 23.48200  21.26500  -25.40900 1.000 55.82749 ? 84  ARG A CZ  1 
ATOM   636  N NH1 . ARG A 1 84  ? 23.40600  22.58300  -25.30800 1.000 56.09150 ? 84  ARG A NH1 1 
ATOM   637  N NH2 . ARG A 1 84  ? 24.12000  20.72400  -26.44400 1.000 60.86944 ? 84  ARG A NH2 1 
ATOM   638  N N   . ILE A 1 85  ? 18.44000  18.01500  -22.59900 1.000 17.61568 ? 85  ILE A N   1 
ATOM   639  C CA  . ILE A 1 85  ? 17.69400  17.91700  -21.34600 1.000 16.36501 ? 85  ILE A CA  1 
ATOM   640  C C   . ILE A 1 85  ? 18.13900  16.70000  -20.53900 1.000 17.27566 ? 85  ILE A C   1 
ATOM   641  O O   . ILE A 1 85  ? 18.32600  16.78600  -19.32100 1.000 17.71986 ? 85  ILE A O   1 
ATOM   642  C CB  . ILE A 1 85  ? 16.17700  17.89500  -21.62400 1.000 15.50387 ? 85  ILE A CB  1 
ATOM   643  C CG1 . ILE A 1 85  ? 15.70900  19.27000  -22.10800 1.000 15.54928 ? 85  ILE A CG1 1 
ATOM   644  C CG2 . ILE A 1 85  ? 15.43200  17.45500  -20.37600 1.000 14.78867 ? 85  ILE A CG2 1 
ATOM   645  C CD1 . ILE A 1 85  ? 14.23000  19.31200  -22.57200 1.000 17.47217 ? 85  ILE A CD1 1 
ATOM   646  N N   . VAL A 1 86  ? 18.31300  15.54800  -21.19100 1.000 15.64322 ? 86  VAL A N   1 
ATOM   647  C CA  . VAL A 1 86  ? 18.81100  14.37400  -20.48100 1.000 21.30102 ? 86  VAL A CA  1 
ATOM   648  C C   . VAL A 1 86  ? 20.13800  14.69400  -19.79500 1.000 23.17544 ? 86  VAL A C   1 
ATOM   649  O O   . VAL A 1 86  ? 20.31900  14.42400  -18.60300 1.000 21.91873 ? 86  VAL A O   1 
ATOM   650  C CB  . VAL A 1 86  ? 18.94400  13.18300  -21.44500 1.000 23.77449 ? 86  VAL A CB  1 
ATOM   651  C CG1 . VAL A 1 86  ? 19.60500  11.99700  -20.74600 1.000 24.02402 ? 86  VAL A CG1 1 
ATOM   652  C CG2 . VAL A 1 86  ? 17.57200  12.78100  -21.97300 1.000 17.94285 ? 86  VAL A CG2 1 
ATOM   653  N N   . ASP A 1 87  ? 21.06800  15.31100  -20.53100 1.000 22.24995 ? 87  ASP A N   1 
ATOM   654  C CA  . ASP A 1 87  ? 22.40200  15.56700  -19.98800 1.000 27.79534 ? 87  ASP A CA  1 
ATOM   655  C C   . ASP A 1 87  ? 22.35400  16.56600  -18.83700 1.000 24.02372 ? 87  ASP A C   1 
ATOM   656  O O   . ASP A 1 87  ? 22.90700  16.31700  -17.76400 1.000 26.94105 ? 87  ASP A O   1 
ATOM   657  C CB  . ASP A 1 87  ? 23.33300  16.06700  -21.09400 1.000 27.66875 ? 87  ASP A CB  1 
ATOM   658  C CG  . ASP A 1 87  ? 23.64100  14.99700  -22.13200 1.000 37.58688 ? 87  ASP A CG  1 
ATOM   659  O OD1 . ASP A 1 87  ? 23.92300  13.84900  -21.74400 1.000 39.79644 ? 87  ASP A OD1 1 
ATOM   660  O OD2 . ASP A 1 87  ? 23.59400  15.29300  -23.34300 1.000 43.66681 ? 87  ASP A OD2 1 
ATOM   661  N N   . ASP A 1 88  ? 21.68800  17.70100  -19.03900 1.000 24.03794 ? 88  ASP A N   1 
ATOM   662  C CA  . ASP A 1 88  ? 21.70100  18.75200  -18.02800 1.000 25.05022 ? 88  ASP A CA  1 
ATOM   663  C C   . ASP A 1 88  ? 20.81800  18.41300  -16.82900 1.000 23.58067 ? 88  ASP A C   1 
ATOM   664  O O   . ASP A 1 88  ? 21.14000  18.81000  -15.70300 1.000 21.80375 ? 88  ASP A O   1 
ATOM   665  C CB  . ASP A 1 88  ? 21.29600  20.07900  -18.66600 1.000 21.91078 ? 88  ASP A CB  1 
ATOM   666  C CG  . ASP A 1 88  ? 22.29000  20.53500  -19.71500 1.000 34.53236 ? 88  ASP A CG  1 
ATOM   667  O OD1 . ASP A 1 88  ? 23.32900  19.85900  -19.87500 1.000 33.41077 ? 88  ASP A OD1 1 
ATOM   668  O OD2 . ASP A 1 88  ? 22.04000  21.55100  -20.39300 1.000 30.60454 ? 88  ASP A OD2 1 
ATOM   669  N N   . VAL A 1 89  ? 19.71400  17.68400  -17.02900 1.000 19.71394 ? 89  VAL A N   1 
ATOM   670  C CA  . VAL A 1 89  ? 18.94800  17.21600  -15.87700 1.000 18.61425 ? 89  VAL A CA  1 
ATOM   671  C C   . VAL A 1 89  ? 19.74600  16.17100  -15.10600 1.000 21.56314 ? 89  VAL A C   1 
ATOM   672  O O   . VAL A 1 89  ? 19.69000  16.11300  -13.87100 1.000 22.62088 ? 89  VAL A O   1 
ATOM   673  C CB  . VAL A 1 89  ? 17.57300  16.67600  -16.32600 1.000 19.49983 ? 89  VAL A CB  1 
ATOM   674  C CG1 . VAL A 1 89  ? 16.88100  15.92900  -15.19100 1.000 18.70254 ? 89  VAL A CG1 1 
ATOM   675  C CG2 . VAL A 1 89  ? 16.70000  17.82800  -16.82400 1.000 15.10503 ? 89  VAL A CG2 1 
ATOM   676  N N   . SER A 1 90  ? 20.51600  15.34400  -15.82000 1.000 20.76757 ? 90  SER A N   1 
ATOM   677  C CA  . SER A 1 90  ? 21.38000  14.36400  -15.16400 1.000 28.87139 ? 90  SER A CA  1 
ATOM   678  C C   . SER A 1 90  ? 22.33000  15.03700  -14.17600 1.000 24.92582 ? 90  SER A C   1 
ATOM   679  O O   . SER A 1 90  ? 22.48900  14.57300  -13.03700 1.000 26.33442 ? 90  SER A O   1 
ATOM   680  C CB  . SER A 1 90  ? 22.17200  13.58900  -16.21900 1.000 27.04688 ? 90  SER A CB  1 
ATOM   681  O OG  . SER A 1 90  ? 22.93300  12.56200  -15.62800 1.000 31.90028 ? 90  SER A OG  1 
ATOM   682  N N   . VAL A 1 91  ? 22.95400  16.13900  -14.59600 1.000 23.75941 ? 91  VAL A N   1 
ATOM   683  C CA  . VAL A 1 91  ? 23.86300  16.88000  -13.72600 1.000 26.22704 ? 91  VAL A CA  1 
ATOM   684  C C   . VAL A 1 91  ? 23.09400  17.58000  -12.61300 1.000 29.51845 ? 91  VAL A C   1 
ATOM   685  O O   . VAL A 1 91  ? 23.41400  17.42600  -11.43000 1.000 31.69171 ? 91  VAL A O   1 
ATOM   686  C CB  . VAL A 1 91  ? 24.68900  17.87900  -14.55300 1.000 26.97831 ? 91  VAL A CB  1 
ATOM   687  C CG1 . VAL A 1 91  ? 25.38500  18.87500  -13.63800 1.000 29.95977 ? 91  VAL A CG1 1 
ATOM   688  C CG2 . VAL A 1 91  ? 25.68400  17.13600  -15.44000 1.000 27.61870 ? 91  VAL A CG2 1 
ATOM   689  N N   . ALA A 1 92  ? 22.06300  18.35700  -12.97100 1.000 25.77584 ? 92  ALA A N   1 
ATOM   690  C CA  . ALA A 1 92  ? 21.38500  19.19300  -11.98000 1.000 27.43220 ? 92  ALA A CA  1 
ATOM   691  C C   . ALA A 1 92  ? 20.71000  18.36800  -10.89300 1.000 32.51797 ? 92  ALA A C   1 
ATOM   692  O O   . ALA A 1 92  ? 20.54900  18.84100  -9.76000  1.000 32.24780 ? 92  ALA A O   1 
ATOM   693  C CB  . ALA A 1 92  ? 20.35500  20.09400  -12.65900 1.000 23.07681 ? 92  ALA A CB  1 
ATOM   694  N N   . ALA A 1 93  ? 20.28400  17.15200  -11.21000 1.000 26.14663 ? 93  ALA A N   1 
ATOM   695  C CA  . ALA A 1 93  ? 19.67100  16.28700  -10.21800 1.000 24.58337 ? 93  ALA A CA  1 
ATOM   696  C C   . ALA A 1 93  ? 20.64200  15.24300  -9.69300  1.000 26.52210 ? 93  ALA A C   1 
ATOM   697  O O   . ALA A 1 93  ? 20.26900  14.46000  -8.81400  1.000 34.51182 ? 93  ALA A O   1 
ATOM   698  C CB  . ALA A 1 93  ? 18.43100  15.60600  -10.79400 1.000 24.51969 ? 93  ALA A CB  1 
ATOM   699  N N   . GLU A 1 94  ? 21.87700  15.24100  -10.19800 1.000 30.27870 ? 94  GLU A N   1 
ATOM   700  C CA  . GLU A 1 94  ? 22.87900  14.22700  -9.89100  1.000 34.26992 ? 94  GLU A CA  1 
ATOM   701  C C   . GLU A 1 94  ? 22.22600  12.85600  -9.89600  1.000 34.89615 ? 94  GLU A C   1 
ATOM   702  O O   . GLU A 1 94  ? 22.11400  12.18600  -8.86500  1.000 34.92545 ? 94  GLU A O   1 
ATOM   703  C CB  . GLU A 1 94  ? 23.57100  14.54700  -8.57000  1.000 38.76788 ? 94  GLU A CB  1 
ATOM   704  C CG  . GLU A 1 94  ? 24.54600  15.71300  -8.73100  1.000 40.19437 ? 94  GLU A CG  1 
ATOM   705  C CD  . GLU A 1 94  ? 25.31300  16.03800  -7.46900  1.000 46.78712 ? 94  GLU A CD  1 
ATOM   706  O OE1 . GLU A 1 94  ? 24.74300  15.89900  -6.36400  1.000 56.75388 ? 94  GLU A OE1 1 
ATOM   707  O OE2 . GLU A 1 94  ? 26.48800  16.43100  -7.59100  1.000 49.38627 ? 94  GLU A OE2 1 
ATOM   708  N N   . ILE A 1 95  ? 21.74300  12.46200  -11.06600 1.000 29.66392 ? 95  ILE A N   1 
ATOM   709  C CA  . ILE A 1 95  ? 20.99400  11.23000  -11.23400 1.000 26.90817 ? 95  ILE A CA  1 
ATOM   710  C C   . ILE A 1 95  ? 21.44700  10.59100  -12.53500 1.000 27.35073 ? 95  ILE A C   1 
ATOM   711  O O   . ILE A 1 95  ? 21.68300  11.28700  -13.52800 1.000 27.58946 ? 95  ILE A O   1 
ATOM   712  C CB  . ILE A 1 95  ? 19.48200  11.49900  -11.23100 1.000 32.95692 ? 95  ILE A CB  1 
ATOM   713  C CG1 . ILE A 1 95  ? 18.70900  10.21200  -11.44500 1.000 31.01672 ? 95  ILE A CG1 1 
ATOM   714  C CG2 . ILE A 1 95  ? 19.11000  12.50900  -12.31200 1.000 29.70138 ? 95  ILE A CG2 1 
ATOM   715  C CD1 . ILE A 1 95  ? 17.30000  10.44100  -11.22700 1.000 36.07745 ? 95  ILE A CD1 1 
ATOM   716  N N   . ASP A 1 96  ? 21.59400  9.27000   -12.51600 1.000 25.96167 ? 96  ASP A N   1 
ATOM   717  C CA  . ASP A 1 96  ? 22.11100  8.54600   -13.66700 1.000 27.63163 ? 96  ASP A CA  1 
ATOM   718  C C   . ASP A 1 96  ? 21.21300  8.77600   -14.87300 1.000 30.35002 ? 96  ASP A C   1 
ATOM   719  O O   . ASP A 1 96  ? 19.98600  8.71400   -14.76000 1.000 29.54741 ? 96  ASP A O   1 
ATOM   720  C CB  . ASP A 1 96  ? 22.19600  7.05500   -13.35000 1.000 34.36791 ? 96  ASP A CB  1 
ATOM   721  C CG  . ASP A 1 96  ? 23.06100  6.29500   -14.34100 1.000 43.44398 ? 96  ASP A CG  1 
ATOM   722  O OD1 . ASP A 1 96  ? 22.89100  6.47500   -15.56800 1.000 39.34591 ? 96  ASP A OD1 1 
ATOM   723  O OD2 . ASP A 1 96  ? 23.92200  5.51000   -13.88600 1.000 53.78248 ? 96  ASP A OD2 1 
ATOM   724  N N   . ARG A 1 97  ? 21.83700  9.04700   -16.02600 1.000 27.23198 ? 97  ARG A N   1 
ATOM   725  C CA  . ARG A 1 97  ? 21.09200  9.29100   -17.26100 1.000 30.10086 ? 97  ARG A CA  1 
ATOM   726  C C   . ARG A 1 97  ? 20.12100  8.16800   -17.58000 1.000 27.67111 ? 97  ARG A C   1 
ATOM   727  O O   . ARG A 1 97  ? 19.08800  8.40600   -18.21300 1.000 32.92862 ? 97  ARG A O   1 
ATOM   728  C CB  . ARG A 1 97  ? 22.05200  9.47500   -18.43100 1.000 32.59064 ? 97  ARG A CB  1 
ATOM   729  C CG  . ARG A 1 97  ? 22.68400  10.85300  -18.52200 1.000 37.85949 ? 97  ARG A CG  1 
ATOM   730  C CD  . ARG A 1 97  ? 23.71600  10.90900  -19.65000 1.000 41.12065 ? 97  ARG A CD  1 
ATOM   731  N NE  . ARG A 1 97  ? 23.16100  11.50200  -20.86100 1.000 44.37693 ? 97  ARG A NE  1 
ATOM   732  C CZ  . ARG A 1 97  ? 22.86500  10.83900  -21.97100 1.000 47.60107 ? 97  ARG A CZ  1 
ATOM   733  N NH1 . ARG A 1 97  ? 23.07400  9.53600   -22.07400 1.000 52.56355 ? 97  ARG A NH1 1 
ATOM   734  N NH2 . ARG A 1 97  ? 22.34200  11.50100  -23.00300 1.000 49.33295 ? 97  ARG A NH2 1 
ATOM   735  N N   . LYS A 1 98  ? 20.42100  6.94400   -17.14800 1.000 28.69182 ? 98  LYS A N   1 
ATOM   736  C CA  . LYS A 1 98  ? 19.55100  5.80600   -17.42100 1.000 33.35986 ? 98  LYS A CA  1 
ATOM   737  C C   . LYS A 1 98  ? 18.22200  5.88400   -16.68200 1.000 32.24202 ? 98  LYS A C   1 
ATOM   738  O O   . LYS A 1 98  ? 17.31800  5.09900   -16.99200 1.000 28.54138 ? 98  LYS A O   1 
ATOM   739  C CB  . LYS A 1 98  ? 20.25900  4.49800   -17.05300 1.000 34.04904 ? 98  LYS A CB  1 
ATOM   740  C CG  . LYS A 1 98  ? 20.18400  4.14200   -15.56800 1.000 39.86458 ? 98  LYS A CG  1 
ATOM   741  C CD  . LYS A 1 98  ? 21.35100  3.24600   -15.14600 1.000 46.13443 ? 98  LYS A CD  1 
ATOM   742  C CE  . LYS A 1 98  ? 21.25800  2.85700   -13.67300 1.000 44.67310 ? 98  LYS A CE  1 
ATOM   743  N NZ  . LYS A 1 98  ? 22.60400  2.54100   -13.10100 1.000 48.16338 ? 98  LYS A NZ  1 
ATOM   744  N N   . HIS A 1 99  ? 18.08500  6.78600   -15.71100 1.000 26.07643 ? 99  HIS A N   1 
ATOM   745  C CA  . HIS A 1 99  ? 16.82700  6.98100   -15.00600 1.000 24.91652 ? 99  HIS A CA  1 
ATOM   746  C C   . HIS A 1 99  ? 15.96800  8.07000   -15.62900 1.000 20.70999 ? 99  HIS A C   1 
ATOM   747  O O   . HIS A 1 99  ? 14.89300  8.36300   -15.10500 1.000 20.00926 ? 99  HIS A O   1 
ATOM   748  C CB  . HIS A 1 99  ? 17.08900  7.33800   -13.53800 1.000 28.00213 ? 99  HIS A CB  1 
ATOM   749  C CG  . HIS A 1 99  ? 17.61700  6.20000   -12.72000 1.000 32.19273 ? 99  HIS A CG  1 
ATOM   750  N ND1 . HIS A 1 99  ? 18.78300  6.28800   -11.99000 1.000 34.11492 ? 99  HIS A ND1 1 
ATOM   751  C CD2 . HIS A 1 99  ? 17.12900  4.95700   -12.50200 1.000 32.66630 ? 99  HIS A CD2 1 
ATOM   752  C CE1 . HIS A 1 99  ? 18.99900  5.14100   -11.37100 1.000 32.46290 ? 99  HIS A CE1 1 
ATOM   753  N NE2 . HIS A 1 99  ? 18.01000  4.31700   -11.66400 1.000 38.67769 ? 99  HIS A NE2 1 
ATOM   754  N N   . ILE A 1 100 ? 16.41700  8.68900   -16.71100 1.000 21.04397 ? 100 ILE A N   1 
ATOM   755  C CA  . ILE A 1 100 ? 15.76700  9.87100   -17.26300 1.000 20.39037 ? 100 ILE A CA  1 
ATOM   756  C C   . ILE A 1 100 ? 15.08900  9.49400   -18.57200 1.000 23.15983 ? 100 ILE A C   1 
ATOM   757  O O   . ILE A 1 100 ? 15.72800  8.94200   -19.47500 1.000 23.58190 ? 100 ILE A O   1 
ATOM   758  C CB  . ILE A 1 100 ? 16.77500  11.01100  -17.46900 1.000 22.69667 ? 100 ILE A CB  1 
ATOM   759  C CG1 . ILE A 1 100 ? 17.51900  11.30000  -16.15600 1.000 24.62344 ? 100 ILE A CG1 1 
ATOM   760  C CG2 . ILE A 1 100 ? 16.07600  12.26400  -17.96200 1.000 22.60929 ? 100 ILE A CG2 1 
ATOM   761  C CD1 . ILE A 1 100 ? 18.42300  12.49900  -16.24700 1.000 22.07335 ? 100 ILE A CD1 1 
ATOM   762  N N   . TRP A 1 101 ? 13.78900  9.78400   -18.66600 1.000 15.16364 ? 101 TRP A N   1 
ATOM   763  C CA  . TRP A 1 101 ? 13.01700  9.62600   -19.89100 1.000 15.77365 ? 101 TRP A CA  1 
ATOM   764  C C   . TRP A 1 101 ? 12.50900  10.99700  -20.31600 1.000 15.15409 ? 101 TRP A C   1 
ATOM   765  O O   . TRP A 1 101 ? 12.09800  11.80500  -19.47300 1.000 11.71495 ? 101 TRP A O   1 
ATOM   766  C CB  . TRP A 1 101 ? 11.82600  8.67200   -19.69900 1.000 16.71464 ? 101 TRP A CB  1 
ATOM   767  C CG  . TRP A 1 101 ? 12.15700  7.25300   -19.29400 1.000 22.07015 ? 101 TRP A CG  1 
ATOM   768  C CD1 . TRP A 1 101 ? 13.19400  6.82800   -18.49800 1.000 28.36253 ? 101 TRP A CD1 1 
ATOM   769  C CD2 . TRP A 1 101 ? 11.43100  6.07500   -19.66300 1.000 20.77332 ? 101 TRP A CD2 1 
ATOM   770  N NE1 . TRP A 1 101 ? 13.15200  5.46200   -18.36000 1.000 29.32327 ? 101 TRP A NE1 1 
ATOM   771  C CE2 . TRP A 1 101 ? 12.07900  4.97700   -19.06400 1.000 26.64750 ? 101 TRP A CE2 1 
ATOM   772  C CE3 . TRP A 1 101 ? 10.29100  5.84500   -20.44600 1.000 19.85591 ? 101 TRP A CE3 1 
ATOM   773  C CZ2 . TRP A 1 101 ? 11.62500  3.66800   -19.21700 1.000 24.38649 ? 101 TRP A CZ2 1 
ATOM   774  C CZ3 . TRP A 1 101 ? 9.84000   4.54800   -20.60100 1.000 21.17203 ? 101 TRP A CZ3 1 
ATOM   775  C CH2 . TRP A 1 101 ? 10.51100  3.47100   -19.99100 1.000 27.25383 ? 101 TRP A CH2 1 
ATOM   776  N N   . VAL A 1 102 ? 12.54800  11.27500  -21.61600 1.000 11.68026 ? 102 VAL A N   1 
ATOM   777  C CA  . VAL A 1 102 ? 12.12900  12.57500  -22.13300 1.000 12.50210 ? 102 VAL A CA  1 
ATOM   778  C C   . VAL A 1 102 ? 11.33700  12.33300  -23.40900 1.000 14.80086 ? 102 VAL A C   1 
ATOM   779  O O   . VAL A 1 102 ? 11.87700  11.78700  -24.37900 1.000 11.83242 ? 102 VAL A O   1 
ATOM   780  C CB  . VAL A 1 102 ? 13.31700  13.51300  -22.42200 1.000 14.10381 ? 102 VAL A CB  1 
ATOM   781  C CG1 . VAL A 1 102 ? 12.81300  14.87500  -22.90500 1.000 13.40860 ? 102 VAL A CG1 1 
ATOM   782  C CG2 . VAL A 1 102 ? 14.21300  13.66400  -21.17500 1.000 14.75246 ? 102 VAL A CG2 1 
ATOM   783  N N   . TYR A 1 103 ? 10.06200  12.72200  -23.40600 1.000 10.85968 ? 103 TYR A N   1 
ATOM   784  C CA  . TYR A 1 103 ? 9.21200   12.68000  -24.59500 1.000 13.56214 ? 103 TYR A CA  1 
ATOM   785  C C   . TYR A 1 103 ? 8.78000   14.09200  -24.96400 1.000 12.86467 ? 103 TYR A C   1 
ATOM   786  O O   . TYR A 1 103 ? 8.36300   14.85300  -24.09200 1.000 9.14642  ? 103 TYR A O   1 
ATOM   787  C CB  . TYR A 1 103 ? 7.93400   11.88100  -24.35200 1.000 12.45831 ? 103 TYR A CB  1 
ATOM   788  C CG  . TYR A 1 103 ? 8.05100   10.38700  -24.17200 1.000 11.32523 ? 103 TYR A CG  1 
ATOM   789  C CD1 . TYR A 1 103 ? 9.27500   9.72500   -24.22400 1.000 11.55157 ? 103 TYR A CD1 1 
ATOM   790  C CD2 . TYR A 1 103 ? 6.90600   9.64100   -23.94100 1.000 11.16570 ? 103 TYR A CD2 1 
ATOM   791  C CE1 . TYR A 1 103 ? 9.34100   8.34500   -24.05600 1.000 12.88024 ? 103 TYR A CE1 1 
ATOM   792  C CE2 . TYR A 1 103 ? 6.95700   8.28200   -23.76900 1.000 13.02295 ? 103 TYR A CE2 1 
ATOM   793  C CZ  . TYR A 1 103 ? 8.16800   7.63900   -23.83500 1.000 16.72659 ? 103 TYR A CZ  1 
ATOM   794  O OH  . TYR A 1 103 ? 8.15500   6.28300   -23.66100 1.000 18.77060 ? 103 TYR A OH  1 
ATOM   795  N N   . PHE A 1 104 ? 8.80700   14.42400  -26.25700 1.000 13.39119 ? 104 PHE A N   1 
ATOM   796  C CA  . PHE A 1 104 ? 8.28300   15.69800  -26.74600 1.000 13.87937 ? 104 PHE A CA  1 
ATOM   797  C C   . PHE A 1 104 ? 6.99600   15.48200  -27.52600 1.000 14.64785 ? 104 PHE A C   1 
ATOM   798  O O   . PHE A 1 104 ? 6.97500   14.71500  -28.49000 1.000 13.91979 ? 104 PHE A O   1 
ATOM   799  C CB  . PHE A 1 104 ? 9.28700   16.41600  -27.64900 1.000 14.56405 ? 104 PHE A CB  1 
ATOM   800  C CG  . PHE A 1 104 ? 10.45900  16.97800  -26.93000 1.000 17.86527 ? 104 PHE A CG  1 
ATOM   801  C CD1 . PHE A 1 104 ? 10.50300  17.01100  -25.54500 1.000 19.06062 ? 104 PHE A CD1 1 
ATOM   802  C CD2 . PHE A 1 104 ? 11.52500  17.48900  -27.65000 1.000 22.59469 ? 104 PHE A CD2 1 
ATOM   803  C CE1 . PHE A 1 104 ? 11.60400  17.54200  -24.88300 1.000 22.00176 ? 104 PHE A CE1 1 
ATOM   804  C CE2 . PHE A 1 104 ? 12.62600  18.01300  -27.00000 1.000 22.88682 ? 104 PHE A CE2 1 
ATOM   805  C CZ  . PHE A 1 104 ? 12.67200  18.03800  -25.61900 1.000 20.23769 ? 104 PHE A CZ  1 
ATOM   806  N N   . GLY A 1 105 ? 5.93400   16.17500  -27.12100 1.000 12.26530 ? 105 GLY A N   1 
ATOM   807  C CA  . GLY A 1 105 ? 4.71600   16.27500  -27.90600 1.000 15.47417 ? 105 GLY A CA  1 
ATOM   808  C C   . GLY A 1 105 ? 4.62200   17.66500  -28.50500 1.000 15.60634 ? 105 GLY A C   1 
ATOM   809  O O   . GLY A 1 105 ? 5.17400   18.63000  -27.96100 1.000 15.96478 ? 105 GLY A O   1 
ATOM   810  N N   . GLU A 1 106 ? 3.94100   17.76400  -29.64100 1.000 13.72803 ? 106 GLU A N   1 
ATOM   811  C CA  . GLU A 1 106 ? 3.78900   19.02800  -30.35200 1.000 13.55100 ? 106 GLU A CA  1 
ATOM   812  C C   . GLU A 1 106 ? 2.33000   19.25700  -30.71500 1.000 17.01839 ? 106 GLU A C   1 
ATOM   813  O O   . GLU A 1 106 ? 1.58300   18.30900  -30.97300 1.000 14.99046 ? 106 GLU A O   1 
ATOM   814  C CB  . GLU A 1 106 ? 4.59300   19.06300  -31.64500 1.000 19.63004 ? 106 GLU A CB  1 
ATOM   815  C CG  . GLU A 1 106 ? 6.06900   18.86100  -31.51700 1.000 19.25940 ? 106 GLU A CG  1 
ATOM   816  C CD  . GLU A 1 106 ? 6.64800   18.39200  -32.83000 1.000 21.82568 ? 106 GLU A CD  1 
ATOM   817  O OE1 . GLU A 1 106 ? 6.50700   17.18400  -33.14300 1.000 20.84770 ? 106 GLU A OE1 1 
ATOM   818  O OE2 . GLU A 1 106 ? 7.21300   19.23300  -33.55300 1.000 22.67696 ? 106 GLU A OE2 1 
ATOM   819  N N   . MET A 1 107 ? 1.95200   20.53000  -30.78800 1.000 14.77756 ? 107 MET A N   1 
ATOM   820  C CA  . MET A 1 107 ? 0.61600   20.96900  -31.16100 1.000 17.69687 ? 107 MET A CA  1 
ATOM   821  C C   . MET A 1 107 ? 0.70900   22.21900  -32.02000 1.000 18.28883 ? 107 MET A C   1 
ATOM   822  O O   . MET A 1 107 ? 1.66600   22.99400  -31.89100 1.000 14.40696 ? 107 MET A O   1 
ATOM   823  C CB  . MET A 1 107 ? -0.23600  21.30200  -29.92900 1.000 16.01416 ? 107 MET A CB  1 
ATOM   824  C CG  . MET A 1 107 ? -0.45100  20.15600  -29.03000 1.000 18.73831 ? 107 MET A CG  1 
ATOM   825  S SD  . MET A 1 107 ? -0.45300  20.78600  -27.33700 1.000 19.61039 ? 107 MET A SD  1 
ATOM   826  C CE  . MET A 1 107 ? 1.29200   20.94000  -27.03000 1.000 15.56268 ? 107 MET A CE  1 
ATOM   827  N N   . PRO A 1 108 ? -0.28400  22.46100  -32.87500 1.000 14.95471 ? 108 PRO A N   1 
ATOM   828  C CA  . PRO A 1 108 ? -0.32200  23.73400  -33.59900 1.000 17.18548 ? 108 PRO A CA  1 
ATOM   829  C C   . PRO A 1 108 ? -0.36800  24.90300  -32.62600 1.000 20.19009 ? 108 PRO A C   1 
ATOM   830  O O   . PRO A 1 108 ? -1.07800  24.87200  -31.61600 1.000 16.79330 ? 108 PRO A O   1 
ATOM   831  C CB  . PRO A 1 108 ? -1.61300  23.63400  -34.43000 1.000 18.07056 ? 108 PRO A CB  1 
ATOM   832  C CG  . PRO A 1 108 ? -1.87100  22.17800  -34.56200 1.000 18.37981 ? 108 PRO A CG  1 
ATOM   833  C CD  . PRO A 1 108 ? -1.40000  21.57800  -33.25700 1.000 18.66640 ? 108 PRO A CD  1 
ATOM   834  N N   . ALA A 1 109 ? 0.39700   25.95000  -32.94700 1.000 16.63555 ? 109 ALA A N   1 
ATOM   835  C CA  . ALA A 1 109 ? 0.38900   27.15200  -32.12000 1.000 21.26989 ? 109 ALA A CA  1 
ATOM   836  C C   . ALA A 1 109 ? -1.01700  27.70700  -31.95300 1.000 20.40022 ? 109 ALA A C   1 
ATOM   837  O O   . ALA A 1 109 ? -1.31100  28.35200  -30.93900 1.000 22.26720 ? 109 ALA A O   1 
ATOM   838  C CB  . ALA A 1 109 ? 1.30300   28.21800  -32.72600 1.000 22.71492 ? 109 ALA A CB  1 
ATOM   839  N N   . GLN A 1 110 ? -1.89800  27.46200  -32.92800 1.000 17.10123 ? 110 GLN A N   1 
ATOM   840  C CA  . GLN A 1 110 ? -3.24000  28.02600  -32.93300 1.000 23.87848 ? 110 GLN A CA  1 
ATOM   841  C C   . GLN A 1 110 ? -4.13700  27.44500  -31.85000 1.000 24.26366 ? 110 GLN A C   1 
ATOM   842  O O   . GLN A 1 110 ? -5.21000  28.00300  -31.60300 1.000 23.04501 ? 110 GLN A O   1 
ATOM   843  C CB  . GLN A 1 110 ? -3.90100  27.81800  -34.30600 1.000 27.70773 ? 110 GLN A CB  1 
ATOM   844  C CG  . GLN A 1 110 ? -3.23900  28.58500  -35.44200 1.000 36.23434 ? 110 GLN A CG  1 
ATOM   845  C CD  . GLN A 1 110 ? -2.04300  27.85700  -36.04900 1.000 39.18347 ? 110 GLN A CD  1 
ATOM   846  O OE1 . GLN A 1 110 ? -1.81900  26.66900  -35.79200 1.000 32.56246 ? 110 GLN A OE1 1 
ATOM   847  N NE2 . GLN A 1 110 ? -1.26900  28.57400  -36.86700 1.000 41.07412 ? 110 GLN A NE2 1 
ATOM   848  N N   . GLN A 1 111 ? -3.74200  26.34400  -31.21100 1.000 19.08692 ? 111 GLN A N   1 
ATOM   849  C CA  . GLN A 1 111 ? -4.50000  25.77900  -30.10000 1.000 18.67872 ? 111 GLN A CA  1 
ATOM   850  C C   . GLN A 1 111 ? -3.65100  25.73900  -28.82900 1.000 19.62712 ? 111 GLN A C   1 
ATOM   851  O O   . GLN A 1 111 ? -3.77900  24.83300  -28.00000 1.000 18.46346 ? 111 GLN A O   1 
ATOM   852  C CB  . GLN A 1 111 ? -5.04600  24.39800  -30.47300 1.000 19.12137 ? 111 GLN A CB  1 
ATOM   853  C CG  . GLN A 1 111 ? -3.98900  23.33100  -30.78400 1.000 15.94670 ? 111 GLN A CG  1 
ATOM   854  C CD  . GLN A 1 111 ? -4.51400  22.20000  -31.66800 1.000 17.27152 ? 111 GLN A CD  1 
ATOM   855  O OE1 . GLN A 1 111 ? -5.01800  22.44500  -32.76300 1.000 20.58362 ? 111 GLN A OE1 1 
ATOM   856  N NE2 . GLN A 1 111 ? -4.37900  20.95500  -31.20600 1.000 14.94194 ? 111 GLN A NE2 1 
ATOM   857  N N   . MET A 1 112 ? -2.76100  26.72400  -28.67100 1.000 15.81286 ? 112 MET A N   1 
ATOM   858  C CA  . MET A 1 112 ? -1.90200  26.85100  -27.50200 1.000 15.17829 ? 112 MET A CA  1 
ATOM   859  C C   . MET A 1 112 ? -1.96300  28.27900  -26.98900 1.000 20.02091 ? 112 MET A C   1 
ATOM   860  O O   . MET A 1 112 ? -1.72400  29.22600  -27.74700 1.000 19.72360 ? 112 MET A O   1 
ATOM   861  C CB  . MET A 1 112 ? -0.44600  26.48800  -27.81100 1.000 15.47325 ? 112 MET A CB  1 
ATOM   862  C CG  . MET A 1 112 ? -0.26400  25.05600  -28.28200 1.000 15.42613 ? 112 MET A CG  1 
ATOM   863  S SD  . MET A 1 112 ? 1.44400   24.69400  -28.71000 1.000 15.78237 ? 112 MET A SD  1 
ATOM   864  C CE  . MET A 1 112 ? 2.30400   24.78000  -27.13200 1.000 15.18593 ? 112 MET A CE  1 
ATOM   865  N N   . VAL A 1 113 ? -2.25900  28.42500  -25.70000 1.000 19.10680 ? 113 VAL A N   1 
ATOM   866  C CA  . VAL A 1 113 ? -2.38600  29.72100  -25.04400 1.000 19.61679 ? 113 VAL A CA  1 
ATOM   867  C C   . VAL A 1 113 ? -1.42400  29.74400  -23.86600 1.000 24.09879 ? 113 VAL A C   1 
ATOM   868  O O   . VAL A 1 113 ? -1.44900  28.84100  -23.01700 1.000 21.04543 ? 113 VAL A O   1 
ATOM   869  C CB  . VAL A 1 113 ? -3.83400  29.98100  -24.58700 1.000 20.82237 ? 113 VAL A CB  1 
ATOM   870  C CG1 . VAL A 1 113 ? -3.92600  31.28100  -23.83200 1.000 28.00333 ? 113 VAL A CG1 1 
ATOM   871  C CG2 . VAL A 1 113 ? -4.78400  29.99800  -25.77200 1.000 20.11119 ? 113 VAL A CG2 1 
ATOM   872  N N   . GLU A 1 114 ? -0.54900  30.74700  -23.83600 1.000 23.80917 ? 114 GLU A N   1 
ATOM   873  C CA  . GLU A 1 114 ? 0.34200   30.96700  -22.71100 1.000 22.65043 ? 114 GLU A CA  1 
ATOM   874  C C   . GLU A 1 114 ? 0.10500   32.37900  -22.19700 1.000 30.35305 ? 114 GLU A C   1 
ATOM   875  O O   . GLU A 1 114 ? -0.14600  33.29700  -22.98400 1.000 30.51886 ? 114 GLU A O   1 
ATOM   876  C CB  . GLU A 1 114 ? 1.81100   30.77000  -23.10000 1.000 24.34051 ? 114 GLU A CB  1 
ATOM   877  C CG  . GLU A 1 114 ? 2.15100   29.36800  -23.58100 1.000 23.05103 ? 114 GLU A CG  1 
ATOM   878  C CD  . GLU A 1 114 ? 3.62900   29.20000  -23.85400 1.000 31.73346 ? 114 GLU A CD  1 
ATOM   879  O OE1 . GLU A 1 114 ? 4.39400   30.11300  -23.48600 1.000 41.35941 ? 114 GLU A OE1 1 
ATOM   880  O OE2 . GLU A 1 114 ? 4.03400   28.16400  -24.43000 1.000 33.48365 ? 114 GLU A OE2 1 
ATOM   881  N N   . TYR A 1 115 ? 0.16400   32.54600  -20.87200 1.000 35.13633 ? 115 TYR A N   1 
ATOM   882  C CA  . TYR A 1 115 ? -0.12200  33.83300  -20.23300 1.000 32.39225 ? 115 TYR A CA  1 
ATOM   883  C C   . TYR A 1 115 ? -1.44400  34.41300  -20.69900 1.000 33.06437 ? 115 TYR A C   1 
ATOM   884  O O   . TYR A 1 115 ? -1.55900  35.62900  -20.89000 1.000 34.10864 ? 115 TYR A O   1 
ATOM   885  C CB  . TYR A 1 115 ? 0.99000   34.84500  -20.49300 1.000 36.53688 ? 115 TYR A CB  1 
ATOM   886  C CG  . TYR A 1 115 ? 2.29600   34.39000  -19.94600 1.000 33.14540 ? 115 TYR A CG  1 
ATOM   887  C CD1 . TYR A 1 115 ? 2.61700   34.63900  -18.62600 1.000 36.73325 ? 115 TYR A CD1 1 
ATOM   888  C CD2 . TYR A 1 115 ? 3.19900   33.68600  -20.73400 1.000 37.04200 ? 115 TYR A CD2 1 
ATOM   889  C CE1 . TYR A 1 115 ? 3.79200   34.22700  -18.10300 1.000 38.45834 ? 115 TYR A CE1 1 
ATOM   890  C CE2 . TYR A 1 115 ? 4.40300   33.26100  -20.21100 1.000 38.21649 ? 115 TYR A CE2 1 
ATOM   891  C CZ  . TYR A 1 115 ? 4.68500   33.54400  -18.88500 1.000 41.54293 ? 115 TYR A CZ  1 
ATOM   892  O OH  . TYR A 1 115 ? 5.86100   33.15300  -18.29000 1.000 40.73346 ? 115 TYR A OH  1 
ATOM   893  N N   . GLY A 1 116 ? -2.43200  33.54700  -20.91900 1.000 31.41499 ? 116 GLY A N   1 
ATOM   894  C CA  . GLY A 1 116 ? -3.71400  33.99400  -21.42800 1.000 35.16810 ? 116 GLY A CA  1 
ATOM   895  C C   . GLY A 1 116 ? -3.70100  34.59400  -22.82200 1.000 35.06214 ? 116 GLY A C   1 
ATOM   896  O O   . GLY A 1 116 ? -4.63400  35.32300  -23.16900 1.000 37.26850 ? 116 GLY A O   1 
ATOM   897  N N   . ARG A 1 117 ? -2.68500  34.30700  -23.64600 1.000 34.89208 ? 117 ARG A N   1 
ATOM   898  C CA  . ARG A 1 117 ? -2.71300  34.73800  -25.04600 1.000 29.80509 ? 117 ARG A CA  1 
ATOM   899  C C   . ARG A 1 117 ? -2.18700  33.63100  -25.95900 1.000 32.89768 ? 117 ARG A C   1 
ATOM   900  O O   . ARG A 1 117 ? -1.40000  32.77700  -25.54300 1.000 31.08146 ? 117 ARG A O   1 
ATOM   901  C CB  . ARG A 1 117 ? -1.92100  36.04100  -25.26600 1.000 42.91270 ? 117 ARG A CB  1 
ATOM   902  C CG  . ARG A 1 117 ? -0.59200  36.16100  -24.53600 1.000 41.11993 ? 117 ARG A CG  1 
ATOM   903  C CD  . ARG A 1 117 ? 0.01600   37.54800  -24.78800 1.000 58.11925 ? 117 ARG A CD  1 
ATOM   904  N NE  . ARG A 1 117 ? 1.14200   37.86000  -23.91000 1.000 64.20404 ? 117 ARG A NE  1 
ATOM   905  C CZ  . ARG A 1 117 ? 1.85000   38.98300  -23.96400 1.000 66.59455 ? 117 ARG A CZ  1 
ATOM   906  N NH1 . ARG A 1 117 ? 1.57800   39.93200  -24.84600 1.000 67.82543 ? 117 ARG A NH1 1 
ATOM   907  N NH2 . ARG A 1 117 ? 2.85800   39.15800  -23.11200 1.000 65.44226 ? 117 ARG A NH2 1 
ATOM   908  N N   . PHE A 1 118 ? -2.62400  33.66900  -27.22000 1.000 28.67988 ? 118 PHE A N   1 
ATOM   909  C CA  . PHE A 1 118 ? -2.25200  32.66400  -28.21300 1.000 33.15712 ? 118 PHE A CA  1 
ATOM   910  C C   . PHE A 1 118 ? -0.79800  32.79400  -28.64700 1.000 35.76934 ? 118 PHE A C   1 
ATOM   911  O O   . PHE A 1 118 ? -0.22200  33.88400  -28.66000 1.000 33.23322 ? 118 PHE A O   1 
ATOM   912  C CB  . PHE A 1 118 ? -3.14300  32.76800  -29.44800 1.000 32.80859 ? 118 PHE A CB  1 
ATOM   913  C CG  . PHE A 1 118 ? -4.49200  32.15100  -29.26800 1.000 39.05645 ? 118 PHE A CG  1 
ATOM   914  C CD1 . PHE A 1 118 ? -4.67900  30.79000  -29.47300 1.000 30.64039 ? 118 PHE A CD1 1 
ATOM   915  C CD2 . PHE A 1 118 ? -5.57500  32.92700  -28.87400 1.000 39.57197 ? 118 PHE A CD2 1 
ATOM   916  C CE1 . PHE A 1 118 ? -5.92200  30.21300  -29.30000 1.000 29.99799 ? 118 PHE A CE1 1 
ATOM   917  C CE2 . PHE A 1 118 ? -6.82300  32.35500  -28.70200 1.000 36.36978 ? 118 PHE A CE2 1 
ATOM   918  C CZ  . PHE A 1 118 ? -6.99500  30.99400  -28.91800 1.000 34.50050 ? 118 PHE A CZ  1 
ATOM   919  N N   . LEU A 1 119 ? -0.22000  31.66000  -29.04600 1.000 29.15124 ? 119 LEU A N   1 
ATOM   920  C CA  . LEU A 1 119 ? 1.19500   31.57900  -29.37200 1.000 30.10034 ? 119 LEU A CA  1 
ATOM   921  C C   . LEU A 1 119 ? 1.44200   31.93300  -30.83400 1.000 31.50558 ? 119 LEU A C   1 
ATOM   922  O O   . LEU A 1 119 ? 0.55700   31.76600  -31.67800 1.000 30.66579 ? 119 LEU A O   1 
ATOM   923  C CB  . LEU A 1 119 ? 1.71900   30.17600  -29.09900 1.000 26.73208 ? 119 LEU A CB  1 
ATOM   924  C CG  . LEU A 1 119 ? 2.29100   29.98700  -27.70000 1.000 32.93476 ? 119 LEU A CG  1 
ATOM   925  C CD1 . LEU A 1 119 ? 1.40400   30.67900  -26.66400 1.000 31.20181 ? 119 LEU A CD1 1 
ATOM   926  C CD2 . LEU A 1 119 ? 2.43900   28.50500  -27.40900 1.000 30.25636 ? 119 LEU A CD2 1 
ATOM   927  N N   . PRO A 1 120 ? 2.64400   32.43600  -31.15700 1.000 33.90972 ? 120 PRO A N   1 
ATOM   928  C CA  . PRO A 1 120 ? 3.00900   32.72200  -32.55300 1.000 35.52311 ? 120 PRO A CA  1 
ATOM   929  C C   . PRO A 1 120 ? 3.32700   31.45400  -33.35100 1.000 34.36914 ? 120 PRO A C   1 
ATOM   930  O O   . PRO A 1 120 ? 3.88900   30.52300  -32.76500 1.000 35.58643 ? 120 PRO A O   1 
ATOM   931  C CB  . PRO A 1 120 ? 4.25100   33.60800  -32.41300 1.000 36.75932 ? 120 PRO A CB  1 
ATOM   932  C CG  . PRO A 1 120 ? 4.83500   33.23900  -31.08500 1.000 42.19491 ? 120 PRO A CG  1 
ATOM   933  C CD  . PRO A 1 120 ? 3.65300   32.92800  -30.20100 1.000 35.72888 ? 120 PRO A CD  1 
ATOM   934  N N   . PRO B 1 1   ? -13.96600 14.43000  -24.05100 1.000 30.33587 ? 1   PRO B N   1 
ATOM   935  C CA  . PRO B 1 1   ? -12.60200 14.89800  -23.78000 1.000 21.10053 ? 1   PRO B CA  1 
ATOM   936  C C   . PRO B 1 1   ? -12.20100 14.82500  -22.31200 1.000 17.45745 ? 1   PRO B C   1 
ATOM   937  O O   . PRO B 1 1   ? -13.05000 14.68000  -21.43200 1.000 15.20612 ? 1   PRO B O   1 
ATOM   938  C CB  . PRO B 1 1   ? -12.63100 16.35100  -24.25200 1.000 19.62139 ? 1   PRO B CB  1 
ATOM   939  C CG  . PRO B 1 1   ? -14.06500 16.75900  -24.09300 1.000 27.14608 ? 1   PRO B CG  1 
ATOM   940  C CD  . PRO B 1 1   ? -14.86200 15.53900  -24.42800 1.000 29.91314 ? 1   PRO B CD  1 
ATOM   941  N N   . VAL B 1 2   ? -10.90000 14.91800  -22.07900 1.000 13.26674 ? 2   VAL B N   1 
ATOM   942  C CA  . VAL B 1 2   ? -10.33200 14.99000  -20.74200 1.000 11.60980 ? 2   VAL B CA  1 
ATOM   943  C C   . VAL B 1 2   ? -9.54900  16.28600  -20.64700 1.000 13.22796 ? 2   VAL B C   1 
ATOM   944  O O   . VAL B 1 2   ? -8.68100  16.55000  -21.48800 1.000 11.42535 ? 2   VAL B O   1 
ATOM   945  C CB  . VAL B 1 2   ? -9.41300  13.79100  -20.42900 1.000 13.47996 ? 2   VAL B CB  1 
ATOM   946  C CG1 . VAL B 1 2   ? -8.74100  13.99300  -19.06400 1.000 13.06059 ? 2   VAL B CG1 1 
ATOM   947  C CG2 . VAL B 1 2   ? -10.20000 12.47200  -20.47200 1.000 13.52071 ? 2   VAL B CG2 1 
ATOM   948  N N   . TYR B 1 3   ? -9.85500  17.09000  -19.63000 1.000 8.41732  ? 3   TYR B N   1 
ATOM   949  C CA  . TYR B 1 3   ? -9.09200  18.28800  -19.30500 1.000 9.06255  ? 3   TYR B CA  1 
ATOM   950  C C   . TYR B 1 3   ? -8.32100  18.02400  -18.02300 1.000 10.76701 ? 3   TYR B C   1 
ATOM   951  O O   . TYR B 1 3   ? -8.91600  17.93100  -16.94200 1.000 11.07266 ? 3   TYR B O   1 
ATOM   952  C CB  . TYR B 1 3   ? -10.00200 19.49700  -19.14700 1.000 10.88867 ? 3   TYR B CB  1 
ATOM   953  C CG  . TYR B 1 3   ? -10.69700 19.84800  -20.43100 1.000 12.07020 ? 3   TYR B CG  1 
ATOM   954  C CD1 . TYR B 1 3   ? -10.10900 20.70800  -21.35500 1.000 13.60759 ? 3   TYR B CD1 1 
ATOM   955  C CD2 . TYR B 1 3   ? -11.93700 19.29600  -20.73400 1.000 12.71313 ? 3   TYR B CD2 1 
ATOM   956  C CE1 . TYR B 1 3   ? -10.76200 21.03400  -22.54900 1.000 14.37279 ? 3   TYR B CE1 1 
ATOM   957  C CE2 . TYR B 1 3   ? -12.58700 19.60900  -21.91200 1.000 14.97706 ? 3   TYR B CE2 1 
ATOM   958  C CZ  . TYR B 1 3   ? -11.99700 20.47000  -22.80900 1.000 18.99230 ? 3   TYR B CZ  1 
ATOM   959  O OH  . TYR B 1 3   ? -12.67300 20.75400  -23.97100 1.000 24.60741 ? 3   TYR B OH  1 
ATOM   960  N N   . MET B 1 4   ? -7.00600  17.87500  -18.15400 1.000 9.51416  ? 4   MET B N   1 
ATOM   961  C CA  . MET B 1 4   ? -6.11100  17.80400  -17.00800 1.000 9.13393  ? 4   MET B CA  1 
ATOM   962  C C   . MET B 1 4   ? -5.83600  19.22300  -16.53500 1.000 10.47251 ? 4   MET B C   1 
ATOM   963  O O   . MET B 1 4   ? -5.32800  20.04300  -17.30600 1.000 9.80525  ? 4   MET B O   1 
ATOM   964  C CB  . MET B 1 4   ? -4.81100  17.09800  -17.40400 1.000 9.12218  ? 4   MET B CB  1 
ATOM   965  C CG  . MET B 1 4   ? -5.02500  15.75900  -18.12200 1.000 10.89236 ? 4   MET B CG  1 
ATOM   966  S SD  . MET B 1 4   ? -5.87800  14.54800  -17.05100 1.000 13.51771 ? 4   MET B SD  1 
ATOM   967  C CE  . MET B 1 4   ? -4.88500  14.66800  -15.59500 1.000 9.05939  ? 4   MET B CE  1 
ATOM   968  N N   . VAL B 1 5   ? -6.15200  19.52100  -15.27700 1.000 7.74857  ? 5   VAL B N   1 
ATOM   969  C CA  . VAL B 1 5   ? -6.05900  20.88700  -14.76000 1.000 8.96629  ? 5   VAL B CA  1 
ATOM   970  C C   . VAL B 1 5   ? -5.02500  20.91100  -13.64300 1.000 9.99532  ? 5   VAL B C   1 
ATOM   971  O O   . VAL B 1 5   ? -5.27100  20.40500  -12.53700 1.000 10.42591 ? 5   VAL B O   1 
ATOM   972  C CB  . VAL B 1 5   ? -7.42000  21.42500  -14.27900 1.000 11.78332 ? 5   VAL B CB  1 
ATOM   973  C CG1 . VAL B 1 5   ? -7.26300  22.84800  -13.79200 1.000 12.25560 ? 5   VAL B CG1 1 
ATOM   974  C CG2 . VAL B 1 5   ? -8.42600  21.40900  -15.43300 1.000 10.19218 ? 5   VAL B CG2 1 
ATOM   975  N N   . TYR B 1 6   ? -3.87700  21.52800  -13.91800 1.000 7.91533  ? 6   TYR B N   1 
ATOM   976  C CA  . TYR B 1 6   ? -2.72900  21.52200  -13.01600 1.000 10.34533 ? 6   TYR B CA  1 
ATOM   977  C C   . TYR B 1 6   ? -2.74900  22.80400  -12.18500 1.000 12.14795 ? 6   TYR B C   1 
ATOM   978  O O   . TYR B 1 6   ? -2.55600  23.89900  -12.71800 1.000 11.67713 ? 6   TYR B O   1 
ATOM   979  C CB  . TYR B 1 6   ? -1.43200  21.40400  -13.81200 1.000 10.22663 ? 6   TYR B CB  1 
ATOM   980  C CG  . TYR B 1 6   ? -1.40300  20.12000  -14.59900 1.000 9.83318  ? 6   TYR B CG  1 
ATOM   981  C CD1 . TYR B 1 6   ? -1.00700  18.93000  -13.99600 1.000 10.63681 ? 6   TYR B CD1 1 
ATOM   982  C CD2 . TYR B 1 6   ? -1.80100  20.09000  -15.93100 1.000 8.74014  ? 6   TYR B CD2 1 
ATOM   983  C CE1 . TYR B 1 6   ? -0.99700  17.72800  -14.71700 1.000 9.94870  ? 6   TYR B CE1 1 
ATOM   984  C CE2 . TYR B 1 6   ? -1.78600  18.90900  -16.65900 1.000 7.64319  ? 6   TYR B CE2 1 
ATOM   985  C CZ  . TYR B 1 6   ? -1.39000  17.74100  -16.04300 1.000 9.39612  ? 6   TYR B CZ  1 
ATOM   986  O OH  . TYR B 1 6   ? -1.37100  16.56600  -16.75500 1.000 8.74085  ? 6   TYR B OH  1 
ATOM   987  N N   . VAL B 1 7   ? -2.99700  22.65800  -10.88800 1.000 11.08587 ? 7   VAL B N   1 
ATOM   988  C CA  . VAL B 1 7   ? -3.17700  23.78300  -9.97800  1.000 13.55910 ? 7   VAL B CA  1 
ATOM   989  C C   . VAL B 1 7   ? -2.38300  23.47900  -8.71800  1.000 12.98132 ? 7   VAL B C   1 
ATOM   990  O O   . VAL B 1 7   ? -2.02100  22.33400  -8.45200  1.000 12.50277 ? 7   VAL B O   1 
ATOM   991  C CB  . VAL B 1 7   ? -4.67300  24.02000  -9.62900  1.000 14.50913 ? 7   VAL B CB  1 
ATOM   992  C CG1 . VAL B 1 7   ? -5.46100  24.45400  -10.85600 1.000 16.53057 ? 7   VAL B CG1 1 
ATOM   993  C CG2 . VAL B 1 7   ? -5.29500  22.74300  -9.05100  1.000 12.18860 ? 7   VAL B CG2 1 
ATOM   994  N N   . SER B 1 8   ? -2.11600  24.52000  -7.92800  1.000 12.70139 ? 8   SER B N   1 
ATOM   995  C CA  . SER B 1 8   ? -1.48300  24.31700  -6.62700  1.000 14.62074 ? 8   SER B CA  1 
ATOM   996  C C   . SER B 1 8   ? -2.49900  23.84600  -5.58800  1.000 16.85848 ? 8   SER B C   1 
ATOM   997  O O   . SER B 1 8   ? -3.67300  24.21300  -5.63500  1.000 17.42707 ? 8   SER B O   1 
ATOM   998  C CB  . SER B 1 8   ? -0.81900  25.60500  -6.14200  1.000 17.43305 ? 8   SER B CB  1 
ATOM   999  O OG  . SER B 1 8   ? 0.23800   25.97200  -7.01100  1.000 19.78136 ? 8   SER B OG  1 
ATOM   1000 N N   . GLN B 1 9   ? -2.03300  23.00500  -4.66100  1.000 15.69705 ? 9   GLN B N   1 
ATOM   1001 C CA  . GLN B 1 9   ? -2.87300  22.48500  -3.58300  1.000 19.30638 ? 9   GLN B CA  1 
ATOM   1002 C C   . GLN B 1 9   ? -3.54000  23.62200  -2.81600  1.000 21.45378 ? 9   GLN B C   1 
ATOM   1003 O O   . GLN B 1 9   ? -2.89000  24.60300  -2.45600  1.000 19.34834 ? 9   GLN B O   1 
ATOM   1004 C CB  . GLN B 1 9   ? -2.03000  21.63600  -2.62000  1.000 16.68624 ? 9   GLN B CB  1 
ATOM   1005 C CG  . GLN B 1 9   ? -1.77800  20.19600  -3.07600  1.000 28.94447 ? 9   GLN B CG  1 
ATOM   1006 C CD  . GLN B 1 9   ? -0.64800  19.50700  -2.29500  1.000 31.87823 ? 9   GLN B CD  1 
ATOM   1007 O OE1 . GLN B 1 9   ? -0.01700  20.10300  -1.41300  1.000 30.24994 ? 9   GLN B OE1 1 
ATOM   1008 N NE2 . GLN B 1 9   ? -0.37900  18.25100  -2.63800  1.000 35.09158 ? 9   GLN B NE2 1 
ATOM   1009 N N   . ASP B 1 10  ? -4.84900  23.49200  -2.58600  1.000 26.56072 ? 10  ASP B N   1 
ATOM   1010 C CA  . ASP B 1 10  ? -5.66100  24.43200  -1.81300  1.000 26.23009 ? 10  ASP B CA  1 
ATOM   1011 C C   . ASP B 1 10  ? -5.85800  25.77100  -2.51100  1.000 26.44849 ? 10  ASP B C   1 
ATOM   1012 O O   . ASP B 1 10  ? -6.47000  26.66300  -1.92300  1.000 28.72115 ? 10  ASP B O   1 
ATOM   1013 C CB  . ASP B 1 10  ? -5.08100  24.72400  -0.41800  1.000 29.56242 ? 10  ASP B CB  1 
ATOM   1014 C CG  . ASP B 1 10  ? -4.96800  23.48600  0.45400   1.000 37.86975 ? 10  ASP B CG  1 
ATOM   1015 O OD1 . ASP B 1 10  ? -5.91400  22.66500  0.45900   1.000 41.19919 ? 10  ASP B OD1 1 
ATOM   1016 O OD2 . ASP B 1 10  ? -3.93300  23.34800  1.14700   1.000 40.74100 ? 10  ASP B OD2 1 
ATOM   1017 N N   . ARG B 1 11  ? -5.34400  25.96400  -3.72900  1.000 23.09910 ? 11  ARG B N   1 
ATOM   1018 C CA  . ARG B 1 11  ? -5.63500  27.21300  -4.42600  1.000 23.00631 ? 11  ARG B CA  1 
ATOM   1019 C C   . ARG B 1 11  ? -7.11000  27.29500  -4.81000  1.000 25.55042 ? 11  ARG B C   1 
ATOM   1020 O O   . ARG B 1 11  ? -7.68100  28.39200  -4.85800  1.000 26.54037 ? 11  ARG B O   1 
ATOM   1021 C CB  . ARG B 1 11  ? -4.75000  27.35100  -5.66300  1.000 25.83194 ? 11  ARG B CB  1 
ATOM   1022 C CG  . ARG B 1 11  ? -5.02100  28.59500  -6.49400  1.000 26.59341 ? 11  ARG B CG  1 
ATOM   1023 C CD  . ARG B 1 11  ? -4.68500  29.87200  -5.72900  1.000 29.11943 ? 11  ARG B CD  1 
ATOM   1024 N NE  . ARG B 1 11  ? -4.96300  31.05000  -6.54200  1.000 31.81377 ? 11  ARG B NE  1 
ATOM   1025 C CZ  . ARG B 1 11  ? -6.14000  31.65900  -6.58600  1.000 38.52032 ? 11  ARG B CZ  1 
ATOM   1026 N NH1 . ARG B 1 11  ? -7.15900  31.24600  -5.84900  1.000 31.69510 ? 11  ARG B NH1 1 
ATOM   1027 N NH2 . ARG B 1 11  ? -6.30200  32.70700  -7.39000  1.000 41.58804 ? 11  ARG B NH2 1 
ATOM   1028 N N   . LEU B 1 12  ? -7.74200  26.15600  -5.08200  1.000 22.53313 ? 12  LEU B N   1 
ATOM   1029 C CA  . LEU B 1 12  ? -9.15600  26.10400  -5.44000  1.000 23.36350 ? 12  LEU B CA  1 
ATOM   1030 C C   . LEU B 1 12  ? -9.91700  25.36600  -4.34400  1.000 22.86848 ? 12  LEU B C   1 
ATOM   1031 O O   . LEU B 1 12  ? -9.62100  24.20200  -4.04400  1.000 21.75851 ? 12  LEU B O   1 
ATOM   1032 C CB  . LEU B 1 12  ? -9.36700  25.42500  -6.79500  1.000 23.52459 ? 12  LEU B CB  1 
ATOM   1033 C CG  . LEU B 1 12  ? -8.68100  25.96800  -8.05700  1.000 19.57443 ? 12  LEU B CG  1 
ATOM   1034 C CD1 . LEU B 1 12  ? -9.09600  25.10800  -9.25800  1.000 16.74967 ? 12  LEU B CD1 1 
ATOM   1035 C CD2 . LEU B 1 12  ? -9.00300  27.43000  -8.32700  1.000 23.73990 ? 12  LEU B CD2 1 
ATOM   1036 N N   . THR B 1 13  ? -10.89300 26.04800  -3.74600  1.000 27.55774 ? 13  THR B N   1 
ATOM   1037 C CA  . THR B 1 13  ? -11.80400 25.42000  -2.79800  1.000 24.05447 ? 13  THR B CA  1 
ATOM   1038 C C   . THR B 1 13  ? -12.70500 24.44100  -3.53900  1.000 25.55841 ? 13  THR B C   1 
ATOM   1039 O O   . THR B 1 13  ? -12.79900 24.49300  -4.76800  1.000 22.45503 ? 13  THR B O   1 
ATOM   1040 C CB  . THR B 1 13  ? -12.63400 26.49400  -2.10400  1.000 29.21339 ? 13  THR B CB  1 
ATOM   1041 O OG1 . THR B 1 13  ? -13.33500 27.25600  -3.09500  1.000 26.75785 ? 13  THR B OG1 1 
ATOM   1042 C CG2 . THR B 1 13  ? -11.72400 27.41200  -1.32200  1.000 29.68859 ? 13  THR B CG2 1 
ATOM   1043 N N   . PRO B 1 14  ? -13.39700 23.53700  -2.82100  1.000 25.18274 ? 14  PRO B N   1 
ATOM   1044 C CA  . PRO B 1 14  ? -14.33800 22.63900  -3.51200  1.000 25.35121 ? 14  PRO B CA  1 
ATOM   1045 C C   . PRO B 1 14  ? -15.32400 23.36400  -4.41200  1.000 23.45041 ? 14  PRO B C   1 
ATOM   1046 O O   . PRO B 1 14  ? -15.60400 22.88300  -5.52000  1.000 23.70458 ? 14  PRO B O   1 
ATOM   1047 C CB  . PRO B 1 14  ? -15.04600 21.92000  -2.35400  1.000 29.11208 ? 14  PRO B CB  1 
ATOM   1048 C CG  . PRO B 1 14  ? -14.01700 21.89400  -1.28100  1.000 28.22744 ? 14  PRO B CG  1 
ATOM   1049 C CD  . PRO B 1 14  ? -13.32200 23.22200  -1.38000  1.000 27.35302 ? 14  PRO B CD  1 
ATOM   1050 N N   . SER B 1 15  ? -15.84200 24.52100  -3.98700  1.000 25.02107 ? 15  SER B N   1 
ATOM   1051 C CA  . SER B 1 15  ? -16.77600 25.23500  -4.85000  1.000 24.79429 ? 15  SER B CA  1 
ATOM   1052 C C   . SER B 1 15  ? -16.06300 25.88500  -6.03200  1.000 23.01117 ? 15  SER B C   1 
ATOM   1053 O O   . SER B 1 15  ? -16.64300 25.98100  -7.11900  1.000 18.96633 ? 15  SER B O   1 
ATOM   1054 C CB  . SER B 1 15  ? -17.56900 26.27700  -4.05000  1.000 34.84836 ? 15  SER B CB  1 
ATOM   1055 O OG  . SER B 1 15  ? -16.73400 27.31000  -3.56400  1.000 37.15438 ? 15  SER B OG  1 
ATOM   1056 N N   . ALA B 1 16  ? -14.81200 26.32600  -5.85300  1.000 21.97079 ? 16  ALA B N   1 
ATOM   1057 C CA  . ALA B 1 16  ? -14.05200 26.84900  -6.98800  1.000 22.65562 ? 16  ALA B CA  1 
ATOM   1058 C C   . ALA B 1 16  ? -13.70800 25.74500  -7.98800  1.000 20.56155 ? 16  ALA B C   1 
ATOM   1059 O O   . ALA B 1 16  ? -13.72300 25.98200  -9.20200  1.000 18.03794 ? 16  ALA B O   1 
ATOM   1060 C CB  . ALA B 1 16  ? -12.78200 27.54200  -6.50000  1.000 23.67205 ? 16  ALA B CB  1 
ATOM   1061 N N   . LYS B 1 17  ? -13.37500 24.54000  -7.50100  1.000 16.65231 ? 17  LYS B N   1 
ATOM   1062 C CA  . LYS B 1 17  ? -13.14000 23.41500  -8.40600  1.000 17.94823 ? 17  LYS B CA  1 
ATOM   1063 C C   . LYS B 1 17  ? -14.39400 23.08100  -9.18500  1.000 17.49210 ? 17  LYS B C   1 
ATOM   1064 O O   . LYS B 1 17  ? -14.33600 22.81200  -10.39200 1.000 15.76544 ? 17  LYS B O   1 
ATOM   1065 C CB  . LYS B 1 17  ? -12.67700 22.17500  -7.63700  1.000 15.43498 ? 17  LYS B CB  1 
ATOM   1066 C CG  . LYS B 1 17  ? -11.30500 22.30800  -7.02000  1.000 17.19995 ? 17  LYS B CG  1 
ATOM   1067 C CD  . LYS B 1 17  ? -10.85500 21.00300  -6.36800  1.000 21.57712 ? 17  LYS B CD  1 
ATOM   1068 C CE  . LYS B 1 17  ? -9.53300  21.21000  -5.64300  1.000 22.71372 ? 17  LYS B CE  1 
ATOM   1069 N NZ  . LYS B 1 17  ? -9.10200  20.00400  -4.89500  1.000 27.70779 ? 17  LYS B NZ  1 
ATOM   1070 N N   . HIS B 1 18  ? -15.54100 23.07000  -8.50400  1.000 17.08027 ? 18  HIS B N   1 
ATOM   1071 C CA  . HIS B 1 18  ? -16.79100 22.78600  -9.19300  1.000 18.08811 ? 18  HIS B CA  1 
ATOM   1072 C C   . HIS B 1 18  ? -17.10000 23.86100  -10.22900 1.000 16.33067 ? 18  HIS B C   1 
ATOM   1073 O O   . HIS B 1 18  ? -17.52600 23.54900  -11.35000 1.000 17.89339 ? 18  HIS B O   1 
ATOM   1074 C CB  . HIS B 1 18  ? -17.93500 22.66300  -8.18500  1.000 21.48386 ? 18  HIS B CB  1 
ATOM   1075 C CG  . HIS B 1 18  ? -19.27000 22.53900  -8.83700  1.000 27.20709 ? 18  HIS B CG  1 
ATOM   1076 N ND1 . HIS B 1 18  ? -20.11100 23.61600  -9.02000  1.000 36.08473 ? 18  HIS B ND1 1 
ATOM   1077 C CD2 . HIS B 1 18  ? -19.87700 21.48000  -9.42400  1.000 34.05029 ? 18  HIS B CD2 1 
ATOM   1078 C CE1 . HIS B 1 18  ? -21.19700 23.21700  -9.66100  1.000 39.24876 ? 18  HIS B CE1 1 
ATOM   1079 N NE2 . HIS B 1 18  ? -21.08000 21.92400  -9.91600  1.000 34.31050 ? 18  HIS B NE2 1 
ATOM   1080 N N   . ALA B 1 19  ? -16.86700 25.13200  -9.88100  1.000 15.04686 ? 19  ALA B N   1 
ATOM   1081 C CA  . ALA B 1 19  ? -17.08500 26.22000  -10.83100 1.000 19.68560 ? 19  ALA B CA  1 
ATOM   1082 C C   . ALA B 1 19  ? -16.15200 26.11000  -12.03500 1.000 17.80161 ? 19  ALA B C   1 
ATOM   1083 O O   . ALA B 1 19  ? -16.58000 26.30400  -13.17900 1.000 15.44859 ? 19  ALA B O   1 
ATOM   1084 C CB  . ALA B 1 19  ? -16.90200 27.56500  -10.12700 1.000 15.62915 ? 19  ALA B CB  1 
ATOM   1085 N N   . VAL B 1 20  ? -14.86900 25.81500  -11.79600 1.000 17.01456 ? 20  VAL B N   1 
ATOM   1086 C CA  . VAL B 1 20  ? -13.92600 25.65300  -12.90800 1.000 14.48020 ? 20  VAL B CA  1 
ATOM   1087 C C   . VAL B 1 20  ? -14.34100 24.47800  -13.78400 1.000 13.93489 ? 20  VAL B C   1 
ATOM   1088 O O   . VAL B 1 20  ? -14.35700 24.57200  -15.01900 1.000 15.37898 ? 20  VAL B O   1 
ATOM   1089 C CB  . VAL B 1 20  ? -12.49000 25.48800  -12.36900 1.000 15.38902 ? 20  VAL B CB  1 
ATOM   1090 C CG1 . VAL B 1 20  ? -11.54900 24.98600  -13.46900 1.000 12.68600 ? 20  VAL B CG1 1 
ATOM   1091 C CG2 . VAL B 1 20  ? -11.99300 26.81700  -11.79600 1.000 16.07719 ? 20  VAL B CG2 1 
ATOM   1092 N N   . ALA B 1 21  ? -14.67700 23.34700  -13.16000 1.000 13.97061 ? 21  ALA B N   1 
ATOM   1093 C CA  . ALA B 1 21  ? -15.06700 22.17200  -13.94300 1.000 13.94132 ? 21  ALA B CA  1 
ATOM   1094 C C   . ALA B 1 21  ? -16.31000 22.46200  -14.76200 1.000 17.12214 ? 21  ALA B C   1 
ATOM   1095 O O   . ALA B 1 21  ? -16.40300 22.06700  -15.93200 1.000 16.26468 ? 21  ALA B O   1 
ATOM   1096 C CB  . ALA B 1 21  ? -15.31500 20.97100  -13.02600 1.000 17.30675 ? 21  ALA B CB  1 
ATOM   1097 N N   . LYS B 1 22  ? -17.28500 23.14700  -14.15200 1.000 16.84235 ? 22  LYS B N   1 
ATOM   1098 C CA  . LYS B 1 22  ? -18.48400 23.54700  -14.87600 1.000 16.92731 ? 22  LYS B CA  1 
ATOM   1099 C C   . LYS B 1 22  ? -18.14000 24.48200  -16.02600 1.000 16.23084 ? 22  LYS B C   1 
ATOM   1100 O O   . LYS B 1 22  ? -18.68400 24.34800  -17.13000 1.000 20.16211 ? 22  LYS B O   1 
ATOM   1101 C CB  . LYS B 1 22  ? -19.46500 24.21900  -13.91000 1.000 21.83608 ? 22  LYS B CB  1 
ATOM   1102 C CG  . LYS B 1 22  ? -20.91000 24.01600  -14.26000 1.000 30.80456 ? 22  LYS B CG  1 
ATOM   1103 C CD  . LYS B 1 22  ? -21.60000 25.34400  -14.46600 1.000 36.32609 ? 22  LYS B CD  1 
ATOM   1104 C CE  . LYS B 1 22  ? -23.10300 25.16300  -14.57500 1.000 36.65049 ? 22  LYS B CE  1 
ATOM   1105 N NZ  . LYS B 1 22  ? -23.69400 26.16100  -15.49400 1.000 40.50873 ? 22  LYS B NZ  1 
ATOM   1106 N N   . ALA B 1 23  ? -17.26000 25.45100  -15.78000 1.000 17.48906 ? 23  ALA B N   1 
ATOM   1107 C CA  . ALA B 1 23  ? -16.91100 26.41700  -16.82000 1.000 17.31601 ? 23  ALA B CA  1 
ATOM   1108 C C   . ALA B 1 23  ? -16.24400 25.73600  -18.00800 1.000 16.43252 ? 23  ALA B C   1 
ATOM   1109 O O   . ALA B 1 23  ? -16.50900 26.08600  -19.16300 1.000 18.46008 ? 23  ALA B O   1 
ATOM   1110 C CB  . ALA B 1 23  ? -15.99600 27.50000  -16.24900 1.000 18.06130 ? 23  ALA B CB  1 
ATOM   1111 N N   . ILE B 1 24  ? -15.36700 24.76500  -17.74700 1.000 15.10629 ? 24  ILE B N   1 
ATOM   1112 C CA  . ILE B 1 24  ? -14.72200 24.03500  -18.83800 1.000 14.60202 ? 24  ILE B CA  1 
ATOM   1113 C C   . ILE B 1 24  ? -15.72900 23.15200  -19.56000 1.000 19.14711 ? 24  ILE B C   1 
ATOM   1114 O O   . ILE B 1 24  ? -15.74200 23.07600  -20.79600 1.000 15.72906 ? 24  ILE B O   1 
ATOM   1115 C CB  . ILE B 1 24  ? -13.54600 23.21000  -18.29200 1.000 13.49211 ? 24  ILE B CB  1 
ATOM   1116 C CG1 . ILE B 1 24  ? -12.42400 24.13300  -17.82600 1.000 13.68316 ? 24  ILE B CG1 1 
ATOM   1117 C CG2 . ILE B 1 24  ? -13.05200 22.22900  -19.34400 1.000 14.23546 ? 24  ILE B CG2 1 
ATOM   1118 C CD1 . ILE B 1 24  ? -11.39900 23.44700  -16.93600 1.000 15.60170 ? 24  ILE B CD1 1 
ATOM   1119 N N   . THR B 1 25  ? -16.58000 22.45800  -18.79600 1.000 15.28093 ? 25  THR B N   1 
ATOM   1120 C CA  . THR B 1 25  ? -17.57300 21.56200  -19.38200 1.000 16.30426 ? 25  THR B CA  1 
ATOM   1121 C C   . THR B 1 25  ? -18.57500 22.33500  -20.23600 1.000 19.82768 ? 25  THR B C   1 
ATOM   1122 O O   . THR B 1 25  ? -18.97300 21.87600  -21.31600 1.000 21.41985 ? 25  THR B O   1 
ATOM   1123 C CB  . THR B 1 25  ? -18.29100 20.79800  -18.26500 1.000 22.85681 ? 25  THR B CB  1 
ATOM   1124 O OG1 . THR B 1 25  ? -17.34500 20.00200  -17.53300 1.000 22.50905 ? 25  THR B OG1 1 
ATOM   1125 C CG2 . THR B 1 25  ? -19.36400 19.89800  -18.82700 1.000 23.30071 ? 25  THR B CG2 1 
ATOM   1126 N N   . ASP B 1 26  ? -18.99100 23.51300  -19.76000 1.000 21.40881 ? 26  ASP B N   1 
ATOM   1127 C CA  . ASP B 1 26  ? -19.96100 24.33000  -20.48400 1.000 20.42272 ? 26  ASP B CA  1 
ATOM   1128 C C   . ASP B 1 26  ? -19.34800 24.93000  -21.74200 1.000 25.58763 ? 26  ASP B C   1 
ATOM   1129 O O   . ASP B 1 26  ? -20.04200 25.11200  -22.74900 1.000 26.19838 ? 26  ASP B O   1 
ATOM   1130 C CB  . ASP B 1 26  ? -20.48200 25.46100  -19.60000 1.000 21.39583 ? 26  ASP B CB  1 
ATOM   1131 C CG  . ASP B 1 26  ? -21.44700 24.98800  -18.52100 1.000 27.06315 ? 26  ASP B CG  1 
ATOM   1132 O OD1 . ASP B 1 26  ? -21.98400 23.86200  -18.62500 1.000 29.25011 ? 26  ASP B OD1 1 
ATOM   1133 O OD2 . ASP B 1 26  ? -21.67000 25.77100  -17.57100 1.000 26.40870 ? 26  ASP B OD2 1 
ATOM   1134 N N   . ALA B 1 27  ? -18.06900 25.30600  -21.68000 1.000 21.41534 ? 27  ALA B N   1 
ATOM   1135 C CA  . ALA B 1 27  ? -17.37700 25.80200  -22.86600 1.000 25.21118 ? 27  ALA B CA  1 
ATOM   1136 C C   . ALA B 1 27  ? -17.37000 24.74700  -23.95800 1.000 31.79557 ? 27  ALA B C   1 
ATOM   1137 O O   . ALA B 1 27  ? -17.68500 25.02800  -25.12000 1.000 33.50627 ? 27  ALA B O   1 
ATOM   1138 C CB  . ALA B 1 27  ? -15.94500 26.20100  -22.50500 1.000 22.29488 ? 27  ALA B CB  1 
ATOM   1139 N N   . ALA B 1 28  ? -17.01300 23.51600  -23.58600 1.000 30.38911 ? 28  ALA B N   1 
ATOM   1140 C CA  . ALA B 1 28  ? -16.87600 22.43700  -24.55200 1.000 34.39974 ? 28  ALA B CA  1 
ATOM   1141 C C   . ALA B 1 28  ? -18.20700 22.12600  -25.23300 1.000 41.60202 ? 28  ALA B C   1 
ATOM   1142 O O   . ALA B 1 28  ? -18.27400 22.03300  -26.46500 1.000 43.44423 ? 28  ALA B O   1 
ATOM   1143 C CB  . ALA B 1 28  ? -16.30000 21.19900  -23.86100 1.000 27.31018 ? 28  ALA B CB  1 
ATOM   1144 N N   . ARG B 1 29  ? -19.28800 21.98000  -24.45500 1.000 36.96007 ? 29  ARG B N   1 
ATOM   1145 C CA  . ARG B 1 29  ? -20.56100 21.63800  -25.09500 1.000 41.14123 ? 29  ARG B CA  1 
ATOM   1146 C C   . ARG B 1 29  ? -21.17200 22.83200  -25.82100 1.000 42.42203 ? 29  ARG B C   1 
ATOM   1147 O O   . ARG B 1 29  ? -21.77400 22.66700  -26.88700 1.000 46.03395 ? 29  ARG B O   1 
ATOM   1148 C CB  . ARG B 1 29  ? -21.56600 21.08500  -24.08600 1.000 48.02947 ? 29  ARG B CB  1 
ATOM   1149 C CG  . ARG B 1 29  ? -22.58600 20.15700  -24.74800 1.000 53.19679 ? 29  ARG B CG  1 
ATOM   1150 C CD  . ARG B 1 29  ? -23.96100 20.13300  -24.08500 1.000 56.03580 ? 29  ARG B CD  1 
ATOM   1151 N NE  . ARG B 1 29  ? -24.62000 18.82600  -24.15100 1.000 65.48408 ? 29  ARG B NE  1 
ATOM   1152 C CZ  . ARG B 1 29  ? -24.95200 18.17900  -25.26600 1.000 65.49282 ? 29  ARG B CZ  1 
ATOM   1153 N NH1 . ARG B 1 29  ? -24.62700 18.64300  -26.46500 1.000 62.30892 ? 29  ARG B NH1 1 
ATOM   1154 N NH2 . ARG B 1 29  ? -25.61500 17.02600  -25.17600 1.000 57.79649 ? 29  ARG B NH2 1 
ATOM   1155 N N   . GLY B 1 30  ? -21.02700 24.03800  -25.26800 1.000 36.98784 ? 30  GLY B N   1 
ATOM   1156 C CA  . GLY B 1 30  ? -21.58900 25.22300  -25.88600 1.000 40.70456 ? 30  GLY B CA  1 
ATOM   1157 C C   . GLY B 1 30  ? -20.97300 25.59500  -27.21700 1.000 49.84323 ? 30  GLY B C   1 
ATOM   1158 O O   . GLY B 1 30  ? -21.52800 26.45800  -27.90700 1.000 55.14464 ? 30  GLY B O   1 
ATOM   1159 N N   . LEU B 1 31  ? -19.85200 24.96600  -27.59600 1.000 41.56212 ? 31  LEU B N   1 
ATOM   1160 C CA  . LEU B 1 31  ? -19.15500 25.28000  -28.83900 1.000 48.17186 ? 31  LEU B CA  1 
ATOM   1161 C C   . LEU B 1 31  ? -19.04200 24.11200  -29.80400 1.000 47.87404 ? 31  LEU B C   1 
ATOM   1162 O O   . LEU B 1 31  ? -18.95700 24.34400  -31.01200 1.000 52.29826 ? 31  LEU B O   1 
ATOM   1163 C CB  . LEU B 1 31  ? -17.74000 25.80700  -28.54800 1.000 42.69373 ? 31  LEU B CB  1 
ATOM   1164 C CG  . LEU B 1 31  ? -17.63200 27.30900  -28.30100 1.000 44.71612 ? 31  LEU B CG  1 
ATOM   1165 C CD1 . LEU B 1 31  ? -16.23100 27.64700  -27.85900 1.000 31.72556 ? 31  LEU B CD1 1 
ATOM   1166 C CD2 . LEU B 1 31  ? -18.00500 28.08400  -29.56300 1.000 38.63618 ? 31  LEU B CD2 1 
ATOM   1167 N N   . THR B 1 32  ? -19.02700 22.87000  -29.31200 1.000 49.58354 ? 32  THR B N   1 
ATOM   1168 C CA  . THR B 1 32  ? -18.97800 21.69000  -30.16800 1.000 52.01412 ? 32  THR B CA  1 
ATOM   1169 C C   . THR B 1 32  ? -20.22000 20.81600  -30.08600 1.000 54.40638 ? 32  THR B C   1 
ATOM   1170 O O   . THR B 1 32  ? -20.50000 20.08500  -31.04300 1.000 57.22232 ? 32  THR B O   1 
ATOM   1171 C CB  . THR B 1 32  ? -17.75800 20.81500  -29.82700 1.000 53.03082 ? 32  THR B CB  1 
ATOM   1172 O OG1 . THR B 1 32  ? -17.93900 20.23200  -28.53300 1.000 53.96874 ? 32  THR B OG1 1 
ATOM   1173 C CG2 . THR B 1 32  ? -16.47800 21.64600  -29.82500 1.000 48.97634 ? 32  THR B CG2 1 
ATOM   1174 N N   . GLY B 1 33  ? -20.96400 20.86400  -28.98300 1.000 54.90646 ? 33  GLY B N   1 
ATOM   1175 C CA  . GLY B 1 33  ? -22.12400 20.01800  -28.80200 1.000 58.19832 ? 33  GLY B CA  1 
ATOM   1176 C C   . GLY B 1 33  ? -21.84100 18.64900  -28.22500 1.000 55.36510 ? 33  GLY B C   1 
ATOM   1177 O O   . GLY B 1 33  ? -22.71600 17.77800  -28.29000 1.000 59.03620 ? 33  GLY B O   1 
ATOM   1178 N N   . THR B 1 34  ? -20.64800 18.50100  -27.62200 1.000 56.21243 ? 34  THR B N   1 
ATOM   1179 C CA  . THR B 1 34  ? -20.20300 17.26100  -26.92400 1.000 59.70426 ? 34  THR B CA  1 
ATOM   1180 C C   . THR B 1 34  ? -21.09900 17.16200  -25.72700 1.000 58.92883 ? 34  THR B C   1 
ATOM   1181 O O   . THR B 1 34  ? -21.07800 18.08500  -24.93600 1.000 56.65891 ? 34  THR B O   1 
ATOM   1182 C CB  . THR B 1 34  ? -18.70600 17.25200  -26.39600 1.000 54.83744 ? 34  THR B CB  1 
ATOM   1183 O OG1 . THR B 1 34  ? -18.60500 16.80500  -25.03500 1.000 49.98653 ? 34  THR B OG1 1 
ATOM   1184 C CG2 . THR B 1 34  ? -18.03600 18.56900  -26.48500 1.000 48.09566 ? 34  THR B CG2 1 
ATOM   1185 N N   . GLN B 1 35  ? -21.75800 16.01800  -25.48100 1.000 57.56539 ? 35  GLN B N   1 
ATOM   1186 C CA  . GLN B 1 35  ? -22.63900 15.93300  -24.32000 1.000 56.75222 ? 35  GLN B CA  1 
ATOM   1187 C C   . GLN B 1 35  ? -21.88700 16.15500  -23.01000 1.000 56.94414 ? 35  GLN B C   1 
ATOM   1188 O O   . GLN B 1 35  ? -20.70200 15.82300  -22.88300 1.000 52.99341 ? 35  GLN B O   1 
ATOM   1189 C CB  . GLN B 1 35  ? -23.32600 14.56600  -24.29300 1.000 57.21806 ? 35  GLN B CB  1 
ATOM   1190 C CG  . GLN B 1 35  ? -24.03400 14.16500  -25.58400 1.000 59.78431 ? 35  GLN B CG  1 
ATOM   1191 C CD  . GLN B 1 35  ? -23.60900 12.78300  -26.07600 1.000 68.14140 ? 35  GLN B CD  1 
ATOM   1192 O OE1 . GLN B 1 35  ? -22.41700 12.50600  -26.23900 1.000 66.71777 ? 35  GLN B OE1 1 
ATOM   1193 N NE2 . GLN B 1 35  ? -24.58600 11.90900  -26.31000 1.000 63.69970 ? 35  GLN B NE2 1 
ATOM   1194 N N   . HIS B 1 36  ? -22.60300 16.72100  -22.02800 1.000 50.64146 ? 36  HIS B N   1 
ATOM   1195 C CA  . HIS B 1 36  ? -22.06400 16.97500  -20.69300 1.000 52.51795 ? 36  HIS B CA  1 
ATOM   1196 C C   . HIS B 1 36  ? -21.25100 15.80200  -20.15600 1.000 50.68201 ? 36  HIS B C   1 
ATOM   1197 O O   . HIS B 1 36  ? -20.06400 15.94500  -19.83600 1.000 45.80617 ? 36  HIS B O   1 
ATOM   1198 C CB  . HIS B 1 36  ? -23.20700 17.29500  -19.71800 1.000 46.89513 ? 36  HIS B CB  1 
ATOM   1199 C CG  . HIS B 1 36  ? -23.40200 18.75700  -19.45800 1.000 50.81219 ? 36  HIS B CG  1 
ATOM   1200 N ND1 . HIS B 1 36  ? -24.55100 19.26400  -18.88500 1.000 51.64734 ? 36  HIS B ND1 1 
ATOM   1201 C CD2 . HIS B 1 36  ? -22.59700 19.82100  -19.69100 1.000 48.10013 ? 36  HIS B CD2 1 
ATOM   1202 C CE1 . HIS B 1 36  ? -24.44600 20.57800  -18.78200 1.000 50.61221 ? 36  HIS B CE1 1 
ATOM   1203 N NE2 . HIS B 1 36  ? -23.27000 20.94100  -19.26500 1.000 52.59855 ? 36  HIS B NE2 1 
ATOM   1204 N N   . PHE B 1 37  ? -21.88400 14.62700  -20.06100 1.000 48.11991 ? 37  PHE B N   1 
ATOM   1205 C CA  . PHE B 1 37  ? -21.24400 13.46800  -19.44600 1.000 50.38237 ? 37  PHE B CA  1 
ATOM   1206 C C   . PHE B 1 37  ? -19.97100 13.03700  -20.16800 1.000 48.03672 ? 37  PHE B C   1 
ATOM   1207 O O   . PHE B 1 37  ? -19.22200 12.21000  -19.63700 1.000 46.78879 ? 37  PHE B O   1 
ATOM   1208 C CB  . PHE B 1 37  ? -22.23600 12.29400  -19.37300 1.000 51.36839 ? 37  PHE B CB  1 
ATOM   1209 C CG  . PHE B 1 37  ? -22.69300 11.77800  -20.72200 1.000 53.37980 ? 37  PHE B CG  1 
ATOM   1210 C CD1 . PHE B 1 37  ? -23.77700 12.34900  -21.37100 1.000 53.43731 ? 37  PHE B CD1 1 
ATOM   1211 C CD2 . PHE B 1 37  ? -22.05300 10.70200  -21.32500 1.000 56.58851 ? 37  PHE B CD2 1 
ATOM   1212 C CE1 . PHE B 1 37  ? -24.20400 11.86400  -22.60100 1.000 55.00346 ? 37  PHE B CE1 1 
ATOM   1213 C CE2 . PHE B 1 37  ? -22.47400 10.22000  -22.55700 1.000 56.76407 ? 37  PHE B CE2 1 
ATOM   1214 C CZ  . PHE B 1 37  ? -23.54800 10.80500  -23.19500 1.000 54.12951 ? 37  PHE B CZ  1 
ATOM   1215 N N   . LEU B 1 38  ? -19.69400 13.57600  -21.34900 1.000 48.19380 ? 38  LEU B N   1 
ATOM   1216 C CA  . LEU B 1 38  ? -18.48000 13.19700  -22.05300 1.000 49.42307 ? 38  LEU B CA  1 
ATOM   1217 C C   . LEU B 1 38  ? -17.26000 14.01600  -21.64400 1.000 43.74067 ? 38  LEU B C   1 
ATOM   1218 O O   . LEU B 1 38  ? -16.15800 13.71400  -22.12300 1.000 37.65568 ? 38  LEU B O   1 
ATOM   1219 C CB  . LEU B 1 38  ? -18.69100 13.31800  -23.56400 1.000 46.55848 ? 38  LEU B CB  1 
ATOM   1220 C CG  . LEU B 1 38  ? -19.50200 12.19200  -24.20600 1.000 55.17823 ? 38  LEU B CG  1 
ATOM   1221 C CD1 . LEU B 1 38  ? -19.25700 12.16300  -25.71200 1.000 56.22741 ? 38  LEU B CD1 1 
ATOM   1222 C CD2 . LEU B 1 38  ? -19.16400 10.84400  -23.57100 1.000 49.00137 ? 38  LEU B CD2 1 
ATOM   1223 N N   . ALA B 1 39  ? -17.41800 15.04400  -20.79700 1.000 28.16797 ? 39  ALA B N   1 
ATOM   1224 C CA  . ALA B 1 39  ? -16.31100 15.93600  -20.46400 1.000 23.05957 ? 39  ALA B CA  1 
ATOM   1225 C C   . ALA B 1 39  ? -15.80400 15.58600  -19.06900 1.000 16.35470 ? 39  ALA B C   1 
ATOM   1226 O O   . ALA B 1 39  ? -16.51300 15.76600  -18.07700 1.000 18.08959 ? 39  ALA B O   1 
ATOM   1227 C CB  . ALA B 1 39  ? -16.72000 17.40300  -20.54500 1.000 27.08584 ? 39  ALA B CB  1 
ATOM   1228 N N   . GLN B 1 40  ? -14.58000 15.08500  -19.00400 1.000 13.19137 ? 40  GLN B N   1 
ATOM   1229 C CA  . GLN B 1 40  ? -13.90400 14.81700  -17.74100 1.000 14.17159 ? 40  GLN B CA  1 
ATOM   1230 C C   . GLN B 1 40  ? -12.99200 15.99600  -17.42600 1.000 12.46731 ? 40  GLN B C   1 
ATOM   1231 O O   . GLN B 1 40  ? -12.19700 16.41200  -18.27900 1.000 12.40688 ? 40  GLN B O   1 
ATOM   1232 C CB  . GLN B 1 40  ? -13.08600 13.52000  -17.81600 1.000 12.76642 ? 40  GLN B CB  1 
ATOM   1233 C CG  . GLN B 1 40  ? -12.29000 13.28300  -16.51700 1.000 12.97959 ? 40  GLN B CG  1 
ATOM   1234 C CD  . GLN B 1 40  ? -11.56700 11.94900  -16.41800 1.000 17.05145 ? 40  GLN B CD  1 
ATOM   1235 O OE1 . GLN B 1 40  ? -10.60700 11.84600  -15.65800 1.000 17.14583 ? 40  GLN B OE1 1 
ATOM   1236 N NE2 . GLN B 1 40  ? -12.03200 10.92100  -17.14800 1.000 15.98707 ? 40  GLN B NE2 1 
ATOM   1237 N N   . VAL B 1 41  ? -13.11900 16.54500  -16.22200 1.000 11.27180 ? 41  VAL B N   1 
ATOM   1238 C CA  . VAL B 1 41  ? -12.16100 17.51300  -15.69100 1.000 11.36322 ? 41  VAL B CA  1 
ATOM   1239 C C   . VAL B 1 41  ? -11.44100 16.86000  -14.52300 1.000 13.17954 ? 41  VAL B C   1 
ATOM   1240 O O   . VAL B 1 41  ? -12.07200 16.43600  -13.54300 1.000 14.61522 ? 41  VAL B O   1 
ATOM   1241 C CB  . VAL B 1 41  ? -12.83400 18.82500  -15.25800 1.000 12.54002 ? 41  VAL B CB  1 
ATOM   1242 C CG1 . VAL B 1 41  ? -11.81400 19.74500  -14.61600 1.000 11.07375 ? 41  VAL B CG1 1 
ATOM   1243 C CG2 . VAL B 1 41  ? -13.47800 19.50400  -16.45800 1.000 13.53937 ? 41  VAL B CG2 1 
ATOM   1244 N N   . ASN B 1 42  ? -10.12000 16.77500  -14.62300 1.000 11.48283 ? 42  ASN B N   1 
ATOM   1245 C CA  . ASN B 1 42  ? -9.32700  15.98700  -13.69000 1.000 12.24473 ? 42  ASN B CA  1 
ATOM   1246 C C   . ASN B 1 42  ? -8.30200  16.93300  -13.06000 1.000 10.50538 ? 42  ASN B C   1 
ATOM   1247 O O   . ASN B 1 42  ? -7.33300  17.33200  -13.71600 1.000 10.05719 ? 42  ASN B O   1 
ATOM   1248 C CB  . ASN B 1 42  ? -8.70800  14.81300  -14.45200 1.000 11.63673 ? 42  ASN B CB  1 
ATOM   1249 C CG  . ASN B 1 42  ? -8.16100  13.74200  -13.53400 1.000 17.71281 ? 42  ASN B CG  1 
ATOM   1250 O OD1 . ASN B 1 42  ? -7.47300  14.05600  -12.57400 1.000 16.56435 ? 42  ASN B OD1 1 
ATOM   1251 N ND2 . ASN B 1 42  ? -8.47200  12.46900  -13.82100 1.000 13.14070 ? 42  ASN B ND2 1 
ATOM   1252 N N   . PHE B 1 43  ? -8.53100  17.33700  -11.80700 1.000 11.05437 ? 43  PHE B N   1 
ATOM   1253 C CA  . PHE B 1 43  ? -7.63700  18.28000  -11.15100 1.000 9.87373  ? 43  PHE B CA  1 
ATOM   1254 C C   . PHE B 1 43  ? -6.41800  17.55300  -10.61000 1.000 12.97706 ? 43  PHE B C   1 
ATOM   1255 O O   . PHE B 1 43  ? -6.54300  16.57500  -9.87300  1.000 10.12665 ? 43  PHE B O   1 
ATOM   1256 C CB  . PHE B 1 43  ? -8.33600  19.03000  -10.01300 1.000 10.21685 ? 43  PHE B CB  1 
ATOM   1257 C CG  . PHE B 1 43  ? -9.36800  20.00300  -10.48500 1.000 11.84704 ? 43  PHE B CG  1 
ATOM   1258 C CD1 . PHE B 1 43  ? -9.00000  21.27200  -10.90100 1.000 13.91593 ? 43  PHE B CD1 1 
ATOM   1259 C CD2 . PHE B 1 43  ? -10.70700 19.64300  -10.54100 1.000 12.81357 ? 43  PHE B CD2 1 
ATOM   1260 C CE1 . PHE B 1 43  ? -9.94900  22.17700  -11.35600 1.000 14.24114 ? 43  PHE B CE1 1 
ATOM   1261 C CE2 . PHE B 1 43  ? -11.67300 20.55100  -10.99900 1.000 14.52995 ? 43  PHE B CE2 1 
ATOM   1262 C CZ  . PHE B 1 43  ? -11.29200 21.81100  -11.40600 1.000 11.50731 ? 43  PHE B CZ  1 
ATOM   1263 N N   . GLN B 1 44  ? -5.24500  18.05100  -10.96400 1.000 8.89416  ? 44  GLN B N   1 
ATOM   1264 C CA  . GLN B 1 44  ? -3.96100  17.54500  -10.48200 1.000 10.83504 ? 44  GLN B CA  1 
ATOM   1265 C C   . GLN B 1 44  ? -3.35300  18.63200  -9.60300  1.000 12.08442 ? 44  GLN B C   1 
ATOM   1266 O O   . GLN B 1 44  ? -2.83900  19.62800  -10.12000 1.000 9.45078  ? 44  GLN B O   1 
ATOM   1267 C CB  . GLN B 1 44  ? -3.05200  17.21800  -11.65900 1.000 11.02151 ? 44  GLN B CB  1 
ATOM   1268 C CG  . GLN B 1 44  ? -3.69900  16.21000  -12.58200 1.000 9.29000  ? 44  GLN B CG  1 
ATOM   1269 C CD  . GLN B 1 44  ? -3.64500  14.81200  -11.99400 1.000 15.36313 ? 44  GLN B CD  1 
ATOM   1270 O OE1 . GLN B 1 44  ? -2.56500  14.32900  -11.67200 1.000 14.68377 ? 44  GLN B OE1 1 
ATOM   1271 N NE2 . GLN B 1 44  ? -4.80000  14.16300  -11.83800 1.000 12.31241 ? 44  GLN B NE2 1 
ATOM   1272 N N   . GLU B 1 45  ? -3.42000  18.44100  -8.27600  1.000 9.89859  ? 45  GLU B N   1 
ATOM   1273 C CA  . GLU B 1 45  ? -2.85900  19.39300  -7.32400  1.000 11.66423 ? 45  GLU B CA  1 
ATOM   1274 C C   . GLU B 1 45  ? -1.43500  19.02100  -6.93600  1.000 12.63356 ? 45  GLU B C   1 
ATOM   1275 O O   . GLU B 1 45  ? -1.12400  17.84400  -6.73700  1.000 14.64340 ? 45  GLU B O   1 
ATOM   1276 C CB  . GLU B 1 45  ? -3.73300  19.46200  -6.06900  1.000 14.47617 ? 45  GLU B CB  1 
ATOM   1277 C CG  . GLU B 1 45  ? -5.08600  20.09700  -6.33000  1.000 16.20718 ? 45  GLU B CG  1 
ATOM   1278 C CD  . GLU B 1 45  ? -6.02200  19.99800  -5.13800  1.000 20.17826 ? 45  GLU B CD  1 
ATOM   1279 O OE1 . GLU B 1 45  ? -6.30200  18.85900  -4.71500  1.000 19.61805 ? 45  GLU B OE1 1 
ATOM   1280 O OE2 . GLU B 1 45  ? -6.47200  21.05300  -4.64300  1.000 20.58329 ? 45  GLU B OE2 1 
ATOM   1281 N N   . GLN B 1 46  ? -0.57900  20.03200  -6.81900  1.000 12.76991 ? 46  GLN B N   1 
ATOM   1282 C CA  . GLN B 1 46  ? 0.79000   19.92200  -6.33200  1.000 13.09112 ? 46  GLN B CA  1 
ATOM   1283 C C   . GLN B 1 46  ? 1.06400   21.05800  -5.35700  1.000 13.10382 ? 46  GLN B C   1 
ATOM   1284 O O   . GLN B 1 46  ? 0.44400   22.12000  -5.44500  1.000 14.73568 ? 46  GLN B O   1 
ATOM   1285 C CB  . GLN B 1 46  ? 1.81100   19.99500  -7.48400  1.000 12.70696 ? 46  GLN B CB  1 
ATOM   1286 C CG  . GLN B 1 46  ? 1.82800   18.76400  -8.38600  1.000 10.43975 ? 46  GLN B CG  1 
ATOM   1287 C CD  . GLN B 1 46  ? 2.37800   17.54700  -7.68300  1.000 12.12860 ? 46  GLN B CD  1 
ATOM   1288 O OE1 . GLN B 1 46  ? 3.34900   17.64100  -6.93300  1.000 16.34055 ? 46  GLN B OE1 1 
ATOM   1289 N NE2 . GLN B 1 46  ? 1.75800   16.38500  -7.91200  1.000 13.34630 ? 46  GLN B NE2 1 
ATOM   1290 N N   . PRO B 1 47  ? 2.01000   20.88100  -4.43500  1.000 15.44397 ? 47  PRO B N   1 
ATOM   1291 C CA  . PRO B 1 47  ? 2.35300   21.98800  -3.52900  1.000 17.63805 ? 47  PRO B CA  1 
ATOM   1292 C C   . PRO B 1 47  ? 2.79400   23.24300  -4.28100  1.000 19.78919 ? 47  PRO B C   1 
ATOM   1293 O O   . PRO B 1 47  ? 3.43500   23.17900  -5.33600  1.000 16.39298 ? 47  PRO B O   1 
ATOM   1294 C CB  . PRO B 1 47  ? 3.48700   21.41100  -2.67300  1.000 21.98321 ? 47  PRO B CB  1 
ATOM   1295 C CG  . PRO B 1 47  ? 3.96700   20.21200  -3.38300  1.000 23.75000 ? 47  PRO B CG  1 
ATOM   1296 C CD  . PRO B 1 47  ? 2.81000   19.67400  -4.17200  1.000 16.98887 ? 47  PRO B CD  1 
ATOM   1297 N N   . ALA B 1 48  ? 2.40800   24.39800  -3.74000  1.000 15.20739 ? 48  ALA B N   1 
ATOM   1298 C CA  . ALA B 1 48  ? 2.89900   25.66200  -4.26700  1.000 17.16702 ? 48  ALA B CA  1 
ATOM   1299 C C   . ALA B 1 48  ? 4.41900   25.67600  -4.20600  1.000 17.89650 ? 48  ALA B C   1 
ATOM   1300 O O   . ALA B 1 48  ? 5.02500   25.17900  -3.25400  1.000 18.63086 ? 48  ALA B O   1 
ATOM   1301 C CB  . ALA B 1 48  ? 2.31800   26.83800  -3.47600  1.000 18.75207 ? 48  ALA B CB  1 
ATOM   1302 N N   . GLY B 1 49  ? 5.03400   26.22700  -5.23800  1.000 16.72790 ? 49  GLY B N   1 
ATOM   1303 C CA  . GLY B 1 49  ? 6.46400   26.17000  -5.39500  1.000 15.00680 ? 49  GLY B CA  1 
ATOM   1304 C C   . GLY B 1 49  ? 6.93500   25.16400  -6.41800  1.000 18.70532 ? 49  GLY B C   1 
ATOM   1305 O O   . GLY B 1 49  ? 8.11500   25.18200  -6.76800  1.000 15.57875 ? 49  GLY B O   1 
ATOM   1306 N N   . ASN B 1 50  ? 6.05300   24.27400  -6.89500  1.000 15.36429 ? 50  ASN B N   1 
ATOM   1307 C CA  . ASN B 1 50  ? 6.45100   23.26000  -7.87400  1.000 17.21947 ? 50  ASN B CA  1 
ATOM   1308 C C   . ASN B 1 50  ? 6.40500   23.76000  -9.31900  1.000 12.05960 ? 50  ASN B C   1 
ATOM   1309 O O   . ASN B 1 50  ? 6.84200   23.03000  -10.21900 1.000 11.54085 ? 50  ASN B O   1 
ATOM   1310 C CB  . ASN B 1 50  ? 5.57900   21.99500  -7.71300  1.000 14.32124 ? 50  ASN B CB  1 
ATOM   1311 C CG  . ASN B 1 50  ? 6.19700   20.97600  -6.74100  1.000 17.53963 ? 50  ASN B CG  1 
ATOM   1312 O OD1 . ASN B 1 50  ? 7.10700   21.30800  -5.97700  1.000 19.61246 ? 50  ASN B OD1 1 
ATOM   1313 N ND2 . ASN B 1 50  ? 5.71700   19.73200  -6.78300  1.000 13.50783 ? 50  ASN B ND2 1 
ATOM   1314 N N   . VAL B 1 51  ? 5.91800   24.98100  -9.56500  1.000 11.17905 ? 51  VAL B N   1 
ATOM   1315 C CA  . VAL B 1 51  ? 5.90400   25.58700  -10.89800 1.000 12.84687 ? 51  VAL B CA  1 
ATOM   1316 C C   . VAL B 1 51  ? 7.03200   26.60800  -10.99900 1.000 14.69994 ? 51  VAL B C   1 
ATOM   1317 O O   . VAL B 1 51  ? 7.18600   27.46300  -10.11800 1.000 14.01580 ? 51  VAL B O   1 
ATOM   1318 C CB  . VAL B 1 51  ? 4.54800   26.24900  -11.19600 1.000 16.54164 ? 51  VAL B CB  1 
ATOM   1319 C CG1 . VAL B 1 51  ? 4.57200   26.92500  -12.56700 1.000 17.39302 ? 51  VAL B CG1 1 
ATOM   1320 C CG2 . VAL B 1 51  ? 3.40900   25.21900  -11.12700 1.000 14.68486 ? 51  VAL B CG2 1 
ATOM   1321 N N   . PHE B 1 52  ? 7.82600   26.52100  -12.06800 1.000 13.29227 ? 52  PHE B N   1 
ATOM   1322 C CA  . PHE B 1 52  ? 8.86000   27.50800  -12.37100 1.000 14.13019 ? 52  PHE B CA  1 
ATOM   1323 C C   . PHE B 1 52  ? 8.54900   28.13700  -13.72200 1.000 17.06739 ? 52  PHE B C   1 
ATOM   1324 O O   . PHE B 1 52  ? 8.12300   27.44700  -14.65300 1.000 13.60111 ? 52  PHE B O   1 
ATOM   1325 C CB  . PHE B 1 52  ? 10.26700  26.87200  -12.38000 1.000 12.80631 ? 52  PHE B CB  1 
ATOM   1326 C CG  . PHE B 1 52  ? 10.72200  26.38100  -11.02000 1.000 17.09980 ? 52  PHE B CG  1 
ATOM   1327 C CD1 . PHE B 1 52  ? 10.12900  25.27500  -10.43300 1.000 16.60635 ? 52  PHE B CD1 1 
ATOM   1328 C CD2 . PHE B 1 52  ? 11.72900  27.04700  -10.31800 1.000 15.23061 ? 52  PHE B CD2 1 
ATOM   1329 C CE1 . PHE B 1 52  ? 10.52400  24.83100  -9.17600  1.000 15.40548 ? 52  PHE B CE1 1 
ATOM   1330 C CE2 . PHE B 1 52  ? 12.13500  26.60400  -9.06500  1.000 18.10700 ? 52  PHE B CE2 1 
ATOM   1331 C CZ  . PHE B 1 52  ? 11.53500  25.49900  -8.49000  1.000 16.45366 ? 52  PHE B CZ  1 
ATOM   1332 N N   . LEU B 1 53  ? 8.74500   29.44800  -13.83800 1.000 15.57278 ? 53  LEU B N   1 
ATOM   1333 C CA  . LEU B 1 53  ? 8.58700   30.13800  -15.11400 1.000 17.42924 ? 53  LEU B CA  1 
ATOM   1334 C C   . LEU B 1 53  ? 9.89300   30.86200  -15.40300 1.000 23.48673 ? 53  LEU B C   1 
ATOM   1335 O O   . LEU B 1 53  ? 10.34800  31.66900  -14.58700 1.000 18.11522 ? 53  LEU B O   1 
ATOM   1336 C CB  . LEU B 1 53  ? 7.41600   31.11700  -15.08700 1.000 18.50655 ? 53  LEU B CB  1 
ATOM   1337 C CG  . LEU B 1 53  ? 6.02100   30.51700  -14.86900 1.000 23.62677 ? 53  LEU B CG  1 
ATOM   1338 C CD1 . LEU B 1 53  ? 4.94100   31.59300  -14.74300 1.000 21.26500 ? 53  LEU B CD1 1 
ATOM   1339 C CD2 . LEU B 1 53  ? 5.66800   29.55100  -15.99900 1.000 17.78412 ? 53  LEU B CD2 1 
ATOM   1340 N N   . GLY B 1 54  ? 10.51200  30.55600  -16.54000 1.000 23.61249 ? 54  GLY B N   1 
ATOM   1341 C CA  . GLY B 1 54  ? 11.83300  31.09400  -16.81000 1.000 26.40780 ? 54  GLY B CA  1 
ATOM   1342 C C   . GLY B 1 54  ? 12.81900  30.77100  -15.70800 1.000 26.26293 ? 54  GLY B C   1 
ATOM   1343 O O   . GLY B 1 54  ? 13.73900  31.54500  -15.43300 1.000 26.58593 ? 54  GLY B O   1 
ATOM   1344 N N   . GLY B 1 55  ? 12.62900  29.62800  -15.05400 1.000 20.46053 ? 55  GLY B N   1 
ATOM   1345 C CA  . GLY B 1 55  ? 13.49100  29.22000  -13.96900 1.000 18.97899 ? 55  GLY B CA  1 
ATOM   1346 C C   . GLY B 1 55  ? 13.21900  29.89400  -12.64500 1.000 21.43066 ? 55  GLY B C   1 
ATOM   1347 O O   . GLY B 1 55  ? 13.96000  29.65200  -11.68100 1.000 24.02491 ? 55  GLY B O   1 
ATOM   1348 N N   . VAL B 1 56  ? 12.18300  30.72200  -12.56100 1.000 21.33427 ? 56  VAL B N   1 
ATOM   1349 C CA  . VAL B 1 56  ? 11.82800  31.42800  -11.33900 1.000 20.37983 ? 56  VAL B CA  1 
ATOM   1350 C C   . VAL B 1 56  ? 10.66000  30.71000  -10.67600 1.000 18.35243 ? 56  VAL B C   1 
ATOM   1351 O O   . VAL B 1 56  ? 9.60100   30.53500  -11.29000 1.000 17.00209 ? 56  VAL B O   1 
ATOM   1352 C CB  . VAL B 1 56  ? 11.47200  32.89500  -11.62000 1.000 22.19515 ? 56  VAL B CB  1 
ATOM   1353 C CG1 . VAL B 1 56  ? 11.05800  33.58400  -10.31600 1.000 20.67387 ? 56  VAL B CG1 1 
ATOM   1354 C CG2 . VAL B 1 56  ? 12.65500  33.61100  -12.28100 1.000 21.55767 ? 56  VAL B CG2 1 
ATOM   1355 N N   . GLN B 1 57  ? 10.83700  30.35000  -9.40800  1.000 18.91259 ? 57  GLN B N   1 
ATOM   1356 C CA  . GLN B 1 57  ? 9.80000   29.63500  -8.67800  1.000 17.83017 ? 57  GLN B CA  1 
ATOM   1357 C C   . GLN B 1 57  ? 8.56200   30.49900  -8.49200  1.000 22.55449 ? 57  GLN B C   1 
ATOM   1358 O O   . GLN B 1 57  ? 8.65100   31.67000  -8.11100  1.000 21.65282 ? 57  GLN B O   1 
ATOM   1359 C CB  . GLN B 1 57  ? 10.33300  29.19000  -7.32300  1.000 20.40468 ? 57  GLN B CB  1 
ATOM   1360 C CG  . GLN B 1 57  ? 9.36900   28.30200  -6.55700  1.000 18.16030 ? 57  GLN B CG  1 
ATOM   1361 C CD  . GLN B 1 57  ? 9.95500   27.84400  -5.24900  1.000 27.48291 ? 57  GLN B CD  1 
ATOM   1362 O OE1 . GLN B 1 57  ? 10.53100  28.63600  -4.50700  1.000 24.70945 ? 57  GLN B OE1 1 
ATOM   1363 N NE2 . GLN B 1 57  ? 9.83000   26.55500  -4.96300  1.000 21.70209 ? 57  GLN B NE2 1 
ATOM   1364 N N   . GLN B 1 58  ? 7.39800   29.91400  -8.74700  1.000 16.44574 ? 58  GLN B N   1 
ATOM   1365 C CA  . GLN B 1 58  ? 6.13700   30.63100  -8.67600  1.000 20.30827 ? 58  GLN B CA  1 
ATOM   1366 C C   . GLN B 1 58  ? 5.41600   30.33000  -7.37000  1.000 19.43787 ? 58  GLN B C   1 
ATOM   1367 O O   . GLN B 1 58  ? 5.74000   29.37500  -6.65600  1.000 20.13381 ? 58  GLN B O   1 
ATOM   1368 C CB  . GLN B 1 58  ? 5.25000   30.25900  -9.86100  1.000 22.79979 ? 58  GLN B CB  1 
ATOM   1369 C CG  . GLN B 1 58  ? 5.91300   30.58600  -11.19800 1.000 18.07482 ? 58  GLN B CG  1 
ATOM   1370 C CD  . GLN B 1 58  ? 6.13100   32.08200  -11.36200 1.000 27.04765 ? 58  GLN B CD  1 
ATOM   1371 O OE1 . GLN B 1 58  ? 5.17600   32.85000  -11.34300 1.000 27.44997 ? 58  GLN B OE1 1 
ATOM   1372 N NE2 . GLN B 1 58  ? 7.39100   32.50100  -11.49200 1.000 22.45230 ? 58  GLN B NE2 1 
ATOM   1373 N N   . GLY B 1 59  ? 4.43200   31.17900  -7.06000  1.000 22.14197 ? 59  GLY B N   1 
ATOM   1374 C CA  . GLY B 1 59  ? 3.52900   30.94300  -5.94900  1.000 24.50923 ? 59  GLY B CA  1 
ATOM   1375 C C   . GLY B 1 59  ? 2.48600   29.92700  -6.35400  1.000 29.15110 ? 59  GLY B C   1 
ATOM   1376 O O   . GLY B 1 59  ? 2.74600   29.02000  -7.15000  1.000 31.46551 ? 59  GLY B O   1 
ATOM   1377 N N   . GLY B 1 60  ? 1.28300   30.08600  -5.83600  1.000 31.54717 ? 60  GLY B N   1 
ATOM   1378 C CA  . GLY B 1 60  ? 0.26800   29.09800  -6.13700  1.000 26.14858 ? 60  GLY B CA  1 
ATOM   1379 C C   . GLY B 1 60  ? -0.75100  29.51300  -7.17100  1.000 24.49242 ? 60  GLY B C   1 
ATOM   1380 O O   . GLY B 1 60  ? -1.80800  28.89300  -7.26100  1.000 24.57347 ? 60  GLY B O   1 
ATOM   1381 N N   . ASP B 1 61  ? -0.46700  30.53500  -7.97600  1.000 26.39352 ? 61  ASP B N   1 
ATOM   1382 C CA  . ASP B 1 61  ? -1.50800  31.06700  -8.84100  1.000 24.58507 ? 61  ASP B CA  1 
ATOM   1383 C C   . ASP B 1 61  ? -1.54100  30.46300  -10.24300 1.000 26.77216 ? 61  ASP B C   1 
ATOM   1384 O O   . ASP B 1 61  ? -2.53200  30.65300  -10.94900 1.000 26.46494 ? 61  ASP B O   1 
ATOM   1385 C CB  . ASP B 1 61  ? -1.38300  32.59000  -8.95200  1.000 31.51088 ? 61  ASP B CB  1 
ATOM   1386 C CG  . ASP B 1 61  ? -2.35400  33.31500  -8.03300  1.000 39.79946 ? 61  ASP B CG  1 
ATOM   1387 O OD1 . ASP B 1 61  ? -2.55300  32.85100  -6.88800  1.000 35.32349 ? 61  ASP B OD1 1 
ATOM   1388 O OD2 . ASP B 1 61  ? -2.92300  34.34800  -8.45700  1.000 48.46493 ? 61  ASP B OD2 1 
ATOM   1389 N N   . THR B 1 62  ? -0.52300  29.73700  -10.68300 1.000 22.31375 ? 62  THR B N   1 
ATOM   1390 C CA  . THR B 1 62  ? -0.56800  29.28500  -12.06700 1.000 20.65972 ? 62  THR B CA  1 
ATOM   1391 C C   . THR B 1 62  ? -1.64700  28.22300  -12.24700 1.000 17.19769 ? 62  THR B C   1 
ATOM   1392 O O   . THR B 1 62  ? -1.90600  27.41400  -11.35000 1.000 15.27169 ? 62  THR B O   1 
ATOM   1393 C CB  . THR B 1 62  ? 0.79000   28.74400  -12.51500 1.000 25.02684 ? 62  THR B CB  1 
ATOM   1394 O OG1 . THR B 1 62  ? 1.81500   29.69500  -12.19700 1.000 28.05429 ? 62  THR B OG1 1 
ATOM   1395 C CG2 . THR B 1 62  ? 0.78000   28.50500  -14.02500 1.000 22.31209 ? 62  THR B CG2 1 
ATOM   1396 N N   . ILE B 1 63  ? -2.30600  28.25700  -13.40400 1.000 14.69035 ? 63  ILE B N   1 
ATOM   1397 C CA  . ILE B 1 63  ? -3.20700  27.20400  -13.83400 1.000 16.06596 ? 63  ILE B CA  1 
ATOM   1398 C C   . ILE B 1 63  ? -2.78700  26.78700  -15.23600 1.000 15.80083 ? 63  ILE B C   1 
ATOM   1399 O O   . ILE B 1 63  ? -2.65600  27.63600  -16.12500 1.000 14.82868 ? 63  ILE B O   1 
ATOM   1400 C CB  . ILE B 1 63  ? -4.67800  27.65300  -13.83600 1.000 15.33851 ? 63  ILE B CB  1 
ATOM   1401 C CG1 . ILE B 1 63  ? -5.10600  28.09200  -12.44400 1.000 20.65301 ? 63  ILE B CG1 1 
ATOM   1402 C CG2 . ILE B 1 63  ? -5.57100  26.51900  -14.24400 1.000 14.58655 ? 63  ILE B CG2 1 
ATOM   1403 C CD1 . ILE B 1 63  ? -6.56900  28.50200  -12.40700 1.000 26.67346 ? 63  ILE B CD1 1 
ATOM   1404 N N   . PHE B 1 64  ? -2.57800  25.48800  -15.43300 1.000 11.21471 ? 64  PHE B N   1 
ATOM   1405 C CA  . PHE B 1 64  ? -2.30800  24.94100  -16.75800 1.000 9.41138  ? 64  PHE B CA  1 
ATOM   1406 C C   . PHE B 1 64  ? -3.38400  23.91500  -17.08100 1.000 10.24222 ? 64  PHE B C   1 
ATOM   1407 O O   . PHE B 1 64  ? -3.58600  22.96400  -16.32000 1.000 10.35771 ? 64  PHE B O   1 
ATOM   1408 C CB  . PHE B 1 64  ? -0.91100  24.32200  -16.82900 1.000 12.19758 ? 64  PHE B CB  1 
ATOM   1409 C CG  . PHE B 1 64  ? -0.65300  23.54000  -18.10500 1.000 11.99948 ? 64  PHE B CG  1 
ATOM   1410 C CD1 . PHE B 1 64  ? -0.93500  24.09800  -19.34400 1.000 11.61326 ? 64  PHE B CD1 1 
ATOM   1411 C CD2 . PHE B 1 64  ? -0.11500  22.25600  -18.05400 1.000 10.98239 ? 64  PHE B CD2 1 
ATOM   1412 C CE1 . PHE B 1 64  ? -0.70200  23.39600  -20.53200 1.000 10.60776 ? 64  PHE B CE1 1 
ATOM   1413 C CE2 . PHE B 1 64  ? 0.13600   21.53100  -19.25300 1.000 11.53088 ? 64  PHE B CE2 1 
ATOM   1414 C CZ  . PHE B 1 64  ? -0.16600  22.10000  -20.48100 1.000 12.88438 ? 64  PHE B CZ  1 
ATOM   1415 N N   . VAL B 1 65  ? -4.07300  24.11000  -18.20000 1.000 8.88728  ? 65  VAL B N   1 
ATOM   1416 C CA  . VAL B 1 65  ? -5.13400  23.21500  -18.64900 1.000 11.74146 ? 65  VAL B CA  1 
ATOM   1417 C C   . VAL B 1 65  ? -4.62900  22.48300  -19.88400 1.000 11.97386 ? 65  VAL B C   1 
ATOM   1418 O O   . VAL B 1 65  ? -4.34600  23.11400  -20.90800 1.000 10.47961 ? 65  VAL B O   1 
ATOM   1419 C CB  . VAL B 1 65  ? -6.43600  23.96700  -18.97800 1.000 9.56270  ? 65  VAL B CB  1 
ATOM   1420 C CG1 . VAL B 1 65  ? -7.47800  22.99100  -19.50000 1.000 11.02159 ? 65  VAL B CG1 1 
ATOM   1421 C CG2 . VAL B 1 65  ? -6.98500  24.75400  -17.76700 1.000 10.67583 ? 65  VAL B CG2 1 
ATOM   1422 N N   . HIS B 1 66  ? -4.52700  21.15600  -19.80200 1.000 9.41557  ? 66  HIS B N   1 
ATOM   1423 C CA  . HIS B 1 66  ? -4.15200  20.33700  -20.95400 1.000 11.20478 ? 66  HIS B CA  1 
ATOM   1424 C C   . HIS B 1 66  ? -5.39400  19.57800  -21.39600 1.000 10.53469 ? 66  HIS B C   1 
ATOM   1425 O O   . HIS B 1 66  ? -5.82500  18.63300  -20.72700 1.000 10.47221 ? 66  HIS B O   1 
ATOM   1426 C CB  . HIS B 1 66  ? -2.99800  19.39000  -20.62100 1.000 11.37098 ? 66  HIS B CB  1 
ATOM   1427 C CG  . HIS B 1 66  ? -2.39300  18.73000  -21.82400 1.000 13.48801 ? 66  HIS B CG  1 
ATOM   1428 N ND1 . HIS B 1 66  ? -1.56600  17.63000  -21.72700 1.000 13.86502 ? 66  HIS B ND1 1 
ATOM   1429 C CD2 . HIS B 1 66  ? -2.48300  19.01800  -23.14600 1.000 11.48257 ? 66  HIS B CD2 1 
ATOM   1430 C CE1 . HIS B 1 66  ? -1.17500  17.26700  -22.93900 1.000 14.05836 ? 66  HIS B CE1 1 
ATOM   1431 N NE2 . HIS B 1 66  ? -1.71300  18.09400  -23.81600 1.000 11.99057 ? 66  HIS B NE2 1 
ATOM   1432 N N   . GLY B 1 67  ? -5.98200  20.01300  -22.51000 1.000 8.87810  ? 67  GLY B N   1 
ATOM   1433 C CA  . GLY B 1 67  ? -7.18300  19.38900  -23.02800 1.000 11.57036 ? 67  GLY B CA  1 
ATOM   1434 C C   . GLY B 1 67  ? -6.80200  18.31200  -24.01700 1.000 12.89079 ? 67  GLY B C   1 
ATOM   1435 O O   . GLY B 1 67  ? -5.97700  18.53900  -24.90400 1.000 14.03237 ? 67  GLY B O   1 
ATOM   1436 N N   . LEU B 1 68  ? -7.38200  17.12300  -23.84100 1.000 9.68068  ? 68  LEU B N   1 
ATOM   1437 C CA  . LEU B 1 68  ? -7.10400  15.96800  -24.69400 1.000 9.63475  ? 68  LEU B CA  1 
ATOM   1438 C C   . LEU B 1 68  ? -8.36500  15.65300  -25.48600 1.000 14.03222 ? 68  LEU B C   1 
ATOM   1439 O O   . LEU B 1 68  ? -9.36800  15.21600  -24.91300 1.000 12.38365 ? 68  LEU B O   1 
ATOM   1440 C CB  . LEU B 1 68  ? -6.65500  14.77500  -23.85800 1.000 9.73123  ? 68  LEU B CB  1 
ATOM   1441 C CG  . LEU B 1 68  ? -5.42600  15.14100  -23.02600 1.000 12.27073 ? 68  LEU B CG  1 
ATOM   1442 C CD1 . LEU B 1 68  ? -5.13500  14.02400  -22.03100 1.000 13.11214 ? 68  LEU B CD1 1 
ATOM   1443 C CD2 . LEU B 1 68  ? -4.21100  15.41900  -23.93900 1.000 13.90339 ? 68  LEU B CD2 1 
ATOM   1444 N N   . HIS B 1 69  ? -8.29800  15.86500  -26.80100 1.000 11.75789 ? 69  HIS B N   1 
ATOM   1445 C CA  . HIS B 1 69  ? -9.45600  15.89300  -27.67700 1.000 16.19421 ? 69  HIS B CA  1 
ATOM   1446 C C   . HIS B 1 69  ? -9.35500  14.87200  -28.80100 1.000 15.88228 ? 69  HIS B C   1 
ATOM   1447 O O   . HIS B 1 69  ? -8.27100  14.46200  -29.21600 1.000 13.60603 ? 69  HIS B O   1 
ATOM   1448 C CB  . HIS B 1 69  ? -9.63600  17.28000  -28.32200 1.000 15.79380 ? 69  HIS B CB  1 
ATOM   1449 C CG  . HIS B 1 69  ? -9.94800  18.36300  -27.34100 1.000 17.79027 ? 69  HIS B CG  1 
ATOM   1450 N ND1 . HIS B 1 69  ? -8.97100  19.05800  -26.66400 1.000 22.47748 ? 69  HIS B ND1 1 
ATOM   1451 C CD2 . HIS B 1 69  ? -11.13300 18.86000  -26.91000 1.000 21.55818 ? 69  HIS B CD2 1 
ATOM   1452 C CE1 . HIS B 1 69  ? -9.54000  19.94700  -25.86600 1.000 20.60290 ? 69  HIS B CE1 1 
ATOM   1453 N NE2 . HIS B 1 69  ? -10.85100 19.84500  -25.99500 1.000 20.05124 ? 69  HIS B NE2 1 
ATOM   1454 N N   . ARG B 1 70  ? -10.52300 14.51900  -29.32400 1.000 13.66933 ? 70  ARG B N   1 
ATOM   1455 C CA  . ARG B 1 70  ? -10.61100 13.81400  -30.59000 1.000 16.12656 ? 70  ARG B CA  1 
ATOM   1456 C C   . ARG B 1 70  ? -10.21200 14.74400  -31.73700 1.000 17.18524 ? 70  ARG B C   1 
ATOM   1457 O O   . ARG B 1 70  ? -10.53500 15.93500  -31.73000 1.000 15.92078 ? 70  ARG B O   1 
ATOM   1458 C CB  . ARG B 1 70  ? -12.04500 13.30200  -30.76800 1.000 21.47985 ? 70  ARG B CB  1 
ATOM   1459 C CG  . ARG B 1 70  ? -12.35700 12.63500  -32.07600 1.000 30.77238 ? 70  ARG B CG  1 
ATOM   1460 C CD  . ARG B 1 70  ? -13.84800 12.29700  -32.13900 1.000 32.49575 ? 70  ARG B CD  1 
ATOM   1461 N NE  . ARG B 1 70  ? -14.65600 13.39600  -32.65700 1.000 44.59227 ? 70  ARG B NE  1 
ATOM   1462 C CZ  . ARG B 1 70  ? -15.96400 13.51600  -32.47100 1.000 49.79167 ? 70  ARG B CZ  1 
ATOM   1463 N NH1 . ARG B 1 70  ? -16.64100 12.63900  -31.74500 1.000 49.00451 ? 70  ARG B NH1 1 
ATOM   1464 N NH2 . ARG B 1 70  ? -16.60700 14.54800  -33.01600 1.000 50.34422 ? 70  ARG B NH2 1 
ATOM   1465 N N   . GLU B 1 71  ? -9.46200  14.20600  -32.69500 1.000 15.70356 ? 71  GLU B N   1 
ATOM   1466 C CA  . GLU B 1 71  ? -9.16400  14.92500  -33.92500 1.000 17.69099 ? 71  GLU B CA  1 
ATOM   1467 C C   . GLU B 1 71  ? -10.44700 15.21600  -34.69500 1.000 16.10979 ? 71  GLU B C   1 
ATOM   1468 O O   . GLU B 1 71  ? -11.46400 14.53500  -34.54600 1.000 18.88336 ? 71  GLU B O   1 
ATOM   1469 C CB  . GLU B 1 71  ? -8.23600  14.10900  -34.82400 1.000 16.24373 ? 71  GLU B CB  1 
ATOM   1470 C CG  . GLU B 1 71  ? -6.80000  14.11100  -34.38200 1.000 22.79990 ? 71  GLU B CG  1 
ATOM   1471 C CD  . GLU B 1 71  ? -5.94400  13.12200  -35.15800 1.000 30.75269 ? 71  GLU B CD  1 
ATOM   1472 O OE1 . GLU B 1 71  ? -6.44900  12.49200  -36.12200 1.000 26.01750 ? 71  GLU B OE1 1 
ATOM   1473 O OE2 . GLU B 1 71  ? -4.75700  12.98300  -34.78200 1.000 28.49532 ? 71  GLU B OE2 1 
ATOM   1474 N N   . GLY B 1 72  ? -10.38600 16.22700  -35.55300 1.000 17.98433 ? 72  GLY B N   1 
ATOM   1475 C CA  . GLY B 1 72  ? -11.46300 16.48600  -36.49200 1.000 18.13295 ? 72  GLY B CA  1 
ATOM   1476 C C   . GLY B 1 72  ? -12.10100 17.85000  -36.38700 1.000 19.97650 ? 72  GLY B C   1 
ATOM   1477 O O   . GLY B 1 72  ? -12.90900 18.20100  -37.25900 1.000 19.73348 ? 72  GLY B O   1 
ATOM   1478 N N   . ARG B 1 73  ? -11.79300 18.64900  -35.37200 1.000 19.22994 ? 73  ARG B N   1 
ATOM   1479 C CA  . ARG B 1 73  ? -12.40800 19.96200  -35.29900 1.000 19.70219 ? 73  ARG B CA  1 
ATOM   1480 C C   . ARG B 1 73  ? -11.56900 20.98800  -36.05100 1.000 17.37633 ? 73  ARG B C   1 
ATOM   1481 O O   . ARG B 1 73  ? -10.36900 20.80900  -36.27300 1.000 14.02801 ? 73  ARG B O   1 
ATOM   1482 C CB  . ARG B 1 73  ? -12.62400 20.39100  -33.83800 1.000 19.90432 ? 73  ARG B CB  1 
ATOM   1483 C CG  . ARG B 1 73  ? -13.85000 19.70500  -33.17200 1.000 29.75476 ? 73  ARG B CG  1 
ATOM   1484 C CD  . ARG B 1 73  ? -15.07800 19.79400  -34.10100 1.000 37.29054 ? 73  ARG B CD  1 
ATOM   1485 N NE  . ARG B 1 73  ? -15.06900 21.08100  -34.79100 1.000 43.84412 ? 73  ARG B NE  1 
ATOM   1486 C CZ  . ARG B 1 73  ? -15.75100 21.37900  -35.88500 1.000 37.69791 ? 73  ARG B CZ  1 
ATOM   1487 N NH1 . ARG B 1 73  ? -16.62300 20.52800  -36.41000 1.000 38.18916 ? 73  ARG B NH1 1 
ATOM   1488 N NH2 . ARG B 1 73  ? -15.55400 22.56400  -36.46300 1.000 26.47567 ? 73  ARG B NH2 1 
ATOM   1489 N N   . SER B 1 74  ? -12.22200 22.07400  -36.45500 1.000 18.71424 ? 74  SER B N   1 
ATOM   1490 C CA  . SER B 1 74  ? -11.52700 23.11200  -37.20800 1.000 17.78882 ? 74  SER B CA  1 
ATOM   1491 C C   . SER B 1 74  ? -10.59200 23.90100  -36.29900 1.000 19.32011 ? 74  SER B C   1 
ATOM   1492 O O   . SER B 1 74  ? -10.80600 24.00000  -35.08500 1.000 14.97539 ? 74  SER B O   1 
ATOM   1493 C CB  . SER B 1 74  ? -12.53000 24.06200  -37.85100 1.000 19.97170 ? 74  SER B CB  1 
ATOM   1494 O OG  . SER B 1 74  ? -13.06600 24.93300  -36.86900 1.000 18.82882 ? 74  SER B OG  1 
ATOM   1495 N N   . ALA B 1 75  ? -9.54600  24.47500  -36.90200 1.000 16.59396 ? 75  ALA B N   1 
ATOM   1496 C CA  . ALA B 1 75  ? -8.64800  25.33800  -36.14000 1.000 17.36823 ? 75  ALA B CA  1 
ATOM   1497 C C   . ALA B 1 75  ? -9.41000  26.49200  -35.49400 1.000 20.89759 ? 75  ALA B C   1 
ATOM   1498 O O   . ALA B 1 75  ? -9.09900  26.90500  -34.36900 1.000 20.48404 ? 75  ALA B O   1 
ATOM   1499 C CB  . ALA B 1 75  ? -7.53500  25.86500  -37.04100 1.000 24.61754 ? 75  ALA B CB  1 
ATOM   1500 N N   . ASP B 1 76  ? -10.43000 27.01000  -36.18000 1.000 19.00967 ? 76  ASP B N   1 
ATOM   1501 C CA  . ASP B 1 76  ? -11.20400 28.11300  -35.61600 1.000 23.46841 ? 76  ASP B CA  1 
ATOM   1502 C C   . ASP B 1 76  ? -11.97400 27.67500  -34.37200 1.000 17.46506 ? 76  ASP B C   1 
ATOM   1503 O O   . ASP B 1 76  ? -11.98000 28.37700  -33.35500 1.000 22.35386 ? 76  ASP B O   1 
ATOM   1504 C CB  . ASP B 1 76  ? -12.15400 28.68300  -36.67000 1.000 27.84624 ? 76  ASP B CB  1 
ATOM   1505 C CG  . ASP B 1 76  ? -11.44400 29.61100  -37.65100 1.000 40.94504 ? 76  ASP B CG  1 
ATOM   1506 O OD1 . ASP B 1 76  ? -10.22300 29.84900  -37.48100 1.000 41.93630 ? 76  ASP B OD1 1 
ATOM   1507 O OD2 . ASP B 1 76  ? -12.10700 30.10500  -38.59000 1.000 51.13672 ? 76  ASP B OD2 1 
ATOM   1508 N N   . LEU B 1 77  ? -12.64300 26.52800  -34.43300 1.000 18.20702 ? 77  LEU B N   1 
ATOM   1509 C CA  . LEU B 1 77  ? -13.37100 26.07000  -33.25300 1.000 19.87358 ? 77  LEU B CA  1 
ATOM   1510 C C   . LEU B 1 77  ? -12.41800 25.81000  -32.08700 1.000 23.08003 ? 77  LEU B C   1 
ATOM   1511 O O   . LEU B 1 77  ? -12.69400 26.21000  -30.94700 1.000 21.79891 ? 77  LEU B O   1 
ATOM   1512 C CB  . LEU B 1 77  ? -14.18700 24.82200  -33.58500 1.000 18.82149 ? 77  LEU B CB  1 
ATOM   1513 C CG  . LEU B 1 77  ? -15.02000 24.18900  -32.46100 1.000 27.83697 ? 77  LEU B CG  1 
ATOM   1514 C CD1 . LEU B 1 77  ? -15.60500 25.22500  -31.50400 1.000 37.13550 ? 77  LEU B CD1 1 
ATOM   1515 C CD2 . LEU B 1 77  ? -16.13900 23.36100  -33.04800 1.000 35.02928 ? 77  LEU B CD2 1 
ATOM   1516 N N   . LYS B 1 78  ? -11.28400 25.15600  -32.34900 1.000 16.80524 ? 78  LYS B N   1 
ATOM   1517 C CA  . LYS B 1 78  ? -10.34700 24.88100  -31.26400 1.000 15.85933 ? 78  LYS B CA  1 
ATOM   1518 C C   . LYS B 1 78  ? -9.81400  26.16700  -30.64900 1.000 19.54908 ? 78  LYS B C   1 
ATOM   1519 O O   . LYS B 1 78  ? -9.65700  26.25900  -29.42500 1.000 18.57411 ? 78  LYS B O   1 
ATOM   1520 C CB  . LYS B 1 78  ? -9.20600  23.99500  -31.77200 1.000 17.49805 ? 78  LYS B CB  1 
ATOM   1521 C CG  . LYS B 1 78  ? -9.70400  22.60900  -32.16900 1.000 17.97530 ? 78  LYS B CG  1 
ATOM   1522 C CD  . LYS B 1 78  ? -8.59300  21.68700  -32.68200 1.000 21.88709 ? 78  LYS B CD  1 
ATOM   1523 C CE  . LYS B 1 78  ? -8.04600  22.13200  -34.03200 1.000 20.47977 ? 78  LYS B CE  1 
ATOM   1524 N NZ  . LYS B 1 78  ? -7.01600  21.16100  -34.52500 1.000 20.61639 ? 78  LYS B NZ  1 
ATOM   1525 N N   . GLY B 1 79  ? -9.51100  27.16800  -31.47600 1.000 17.80439 ? 79  GLY B N   1 
ATOM   1526 C CA  . GLY B 1 79  ? -9.04400  28.43500  -30.93700 1.000 19.10250 ? 79  GLY B CA  1 
ATOM   1527 C C   . GLY B 1 79  ? -10.11200 29.13900  -30.12000 1.000 18.49058 ? 79  GLY B C   1 
ATOM   1528 O O   . GLY B 1 79  ? -9.82700  29.68400  -29.04900 1.000 21.41869 ? 79  GLY B O   1 
ATOM   1529 N N   . GLN B 1 80  ? -11.35500 29.12300  -30.60600 1.000 18.88025 ? 80  GLN B N   1 
ATOM   1530 C CA  . GLN B 1 80  ? -12.46200 29.69200  -29.84400 1.000 20.32429 ? 80  GLN B CA  1 
ATOM   1531 C C   . GLN B 1 80  ? -12.63300 28.98500  -28.50500 1.000 22.15943 ? 80  GLN B C   1 
ATOM   1532 O O   . GLN B 1 80  ? -12.90200 29.62700  -27.48100 1.000 19.76211 ? 80  GLN B O   1 
ATOM   1533 C CB  . GLN B 1 80  ? -13.75700 29.58400  -30.64100 1.000 24.41576 ? 80  GLN B CB  1 
ATOM   1534 C CG  . GLN B 1 80  ? -13.93900 30.60200  -31.74400 1.000 28.92504 ? 80  GLN B CG  1 
ATOM   1535 C CD  . GLN B 1 80  ? -15.39600 30.71600  -32.13400 1.000 39.32904 ? 80  GLN B CD  1 
ATOM   1536 O OE1 . GLN B 1 80  ? -16.23000 31.15600  -31.33700 1.000 44.53194 ? 80  GLN B OE1 1 
ATOM   1537 N NE2 . GLN B 1 80  ? -15.71900 30.29300  -33.35000 1.000 45.85793 ? 80  GLN B NE2 1 
ATOM   1538 N N   . LEU B 1 81  ? -12.53700 27.65500  -28.50600 1.000 18.55873 ? 81  LEU B N   1 
ATOM   1539 C CA  . LEU B 1 81  ? -12.72500 26.90000  -27.27400 1.000 18.11357 ? 81  LEU B CA  1 
ATOM   1540 C C   . LEU B 1 81  ? -11.60000 27.17200  -26.28300 1.000 19.84235 ? 81  LEU B C   1 
ATOM   1541 O O   . LEU B 1 81  ? -11.85000 27.31100  -25.07900 1.000 17.25075 ? 81  LEU B O   1 
ATOM   1542 C CB  . LEU B 1 81  ? -12.83400 25.41200  -27.60400 1.000 17.52637 ? 81  LEU B CB  1 
ATOM   1543 C CG  . LEU B 1 81  ? -12.93100 24.45200  -26.41500 1.000 21.50092 ? 81  LEU B CG  1 
ATOM   1544 C CD1 . LEU B 1 81  ? -14.10300 24.83600  -25.53900 1.000 23.62379 ? 81  LEU B CD1 1 
ATOM   1545 C CD2 . LEU B 1 81  ? -13.08300 23.01000  -26.91100 1.000 22.40521 ? 81  LEU B CD2 1 
ATOM   1546 N N   . ALA B 1 82  ? -10.35500 27.26300  -26.76000 1.000 16.25689 ? 82  ALA B N   1 
ATOM   1547 C CA  . ALA B 1 82  ? -9.25900  27.57500  -25.85000 1.000 17.36402 ? 82  ALA B CA  1 
ATOM   1548 C C   . ALA B 1 82  ? -9.44200  28.95900  -25.23700 1.000 21.60397 ? 82  ALA B C   1 
ATOM   1549 O O   . ALA B 1 82  ? -9.27700  29.14400  -24.02300 1.000 21.34007 ? 82  ALA B O   1 
ATOM   1550 C CB  . ALA B 1 82  ? -7.91600  27.46900  -26.57400 1.000 19.66597 ? 82  ALA B CB  1 
ATOM   1551 N N   . GLN B 1 83  ? -9.80900  29.93900  -26.06600 1.000 19.40731 ? 83  GLN B N   1 
ATOM   1552 C CA  . GLN B 1 83  ? -10.01900 31.29900  -25.57700 1.000 21.70327 ? 83  GLN B CA  1 
ATOM   1553 C C   . GLN B 1 83  ? -11.16600 31.35600  -24.57100 1.000 20.85808 ? 83  GLN B C   1 
ATOM   1554 O O   . GLN B 1 83  ? -11.08100 32.05600  -23.55300 1.000 22.60971 ? 83  GLN B O   1 
ATOM   1555 C CB  . GLN B 1 83  ? -10.28500 32.22900  -26.76900 1.000 26.94665 ? 83  GLN B CB  1 
ATOM   1556 C CG  . GLN B 1 83  ? -10.17500 33.70500  -26.45600 1.000 40.12045 ? 83  GLN B CG  1 
ATOM   1557 C CD  . GLN B 1 83  ? -9.03700  34.01300  -25.49000 1.000 47.07323 ? 83  GLN B CD  1 
ATOM   1558 O OE1 . GLN B 1 83  ? -9.25100  34.09200  -24.27400 1.000 44.63845 ? 83  GLN B OE1 1 
ATOM   1559 N NE2 . GLN B 1 83  ? -7.82500  34.19200  -26.02300 1.000 45.06689 ? 83  GLN B NE2 1 
ATOM   1560 N N   . ARG B 1 84  ? -12.24800 30.62600  -24.84200 1.000 19.54679 ? 84  ARG B N   1 
ATOM   1561 C CA  . ARG B 1 84  ? -13.36800 30.56800  -23.90800 1.000 23.50852 ? 84  ARG B CA  1 
ATOM   1562 C C   . ARG B 1 84  ? -12.96100 29.96600  -22.56700 1.000 21.31972 ? 84  ARG B C   1 
ATOM   1563 O O   . ARG B 1 84  ? -13.42000 30.42100  -21.51200 1.000 20.19031 ? 84  ARG B O   1 
ATOM   1564 C CB  . ARG B 1 84  ? -14.51500 29.76400  -24.51100 1.000 23.49742 ? 84  ARG B CB  1 
ATOM   1565 C CG  . ARG B 1 84  ? -15.62600 29.51700  -23.51100 1.000 30.25892 ? 84  ARG B CG  1 
ATOM   1566 C CD  . ARG B 1 84  ? -16.98800 29.40100  -24.16100 1.000 41.51472 ? 84  ARG B CD  1 
ATOM   1567 N NE  . ARG B 1 84  ? -17.17300 30.32200  -25.27800 1.000 48.06288 ? 84  ARG B NE  1 
ATOM   1568 C CZ  . ARG B 1 84  ? -17.07600 31.64300  -25.20300 1.000 47.27592 ? 84  ARG B CZ  1 
ATOM   1569 N NH1 . ARG B 1 84  ? -16.69400 32.25100  -24.09000 1.000 48.52162 ? 84  ARG B NH1 1 
ATOM   1570 N NH2 . ARG B 1 84  ? -17.34900 32.37200  -26.28100 1.000 54.25922 ? 84  ARG B NH2 1 
ATOM   1571 N N   . ILE B 1 85  ? -12.13300 28.91700  -22.58300 1.000 17.45314 ? 85  ILE B N   1 
ATOM   1572 C CA  . ILE B 1 85  ? -11.67700 28.31900  -21.32600 1.000 17.49505 ? 85  ILE B CA  1 
ATOM   1573 C C   . ILE B 1 85  ? -10.83400 29.31000  -20.52600 1.000 18.79782 ? 85  ILE B C   1 
ATOM   1574 O O   . ILE B 1 85  ? -10.98500 29.42600  -19.30500 1.000 17.61932 ? 85  ILE B O   1 
ATOM   1575 C CB  . ILE B 1 85  ? -10.91600 27.00700  -21.59800 1.000 15.67538 ? 85  ILE B CB  1 
ATOM   1576 C CG1 . ILE B 1 85  ? -11.88600 25.94400  -22.13000 1.000 16.18435 ? 85  ILE B CG1 1 
ATOM   1577 C CG2 . ILE B 1 85  ? -10.20800 26.55000  -20.32700 1.000 16.49554 ? 85  ILE B CG2 1 
ATOM   1578 C CD1 . ILE B 1 85  ? -11.22100 24.63200  -22.59600 1.000 19.87430 ? 85  ILE B CD1 1 
ATOM   1579 N N   . VAL B 1 86  ? -9.94500  30.05100  -21.19200 1.000 15.21054 ? 86  VAL B N   1 
ATOM   1580 C CA  . VAL B 1 86  ? -9.18600  31.08500  -20.49000 1.000 20.72485 ? 86  VAL B CA  1 
ATOM   1581 C C   . VAL B 1 86  ? -10.13400 32.06700  -19.80500 1.000 23.79404 ? 86  VAL B C   1 
ATOM   1582 O O   . VAL B 1 86  ? -10.01200 32.33500  -18.60500 1.000 20.90431 ? 86  VAL B O   1 
ATOM   1583 C CB  . VAL B 1 86  ? -8.23400  31.81000  -21.45400 1.000 24.77365 ? 86  VAL B CB  1 
ATOM   1584 C CG1 . VAL B 1 86  ? -7.61100  33.01100  -20.75900 1.000 25.89148 ? 86  VAL B CG1 1 
ATOM   1585 C CG2 . VAL B 1 86  ? -7.15200  30.85500  -21.94900 1.000 19.96452 ? 86  VAL B CG2 1 
ATOM   1586 N N   . ASP B 1 87  ? -11.10500 32.59800  -20.55600 1.000 23.14932 ? 87  ASP B N   1 
ATOM   1587 C CA  . ASP B 1 87  ? -12.01000 33.60800  -20.00400 1.000 28.82477 ? 87  ASP B CA  1 
ATOM   1588 C C   . ASP B 1 87  ? -12.84100 33.04500  -18.85700 1.000 23.90275 ? 87  ASP B C   1 
ATOM   1589 O O   . ASP B 1 87  ? -12.89300 33.62100  -17.76800 1.000 25.21297 ? 87  ASP B O   1 
ATOM   1590 C CB  . ASP B 1 87  ? -12.92800 34.15900  -21.09900 1.000 28.45134 ? 87  ASP B CB  1 
ATOM   1591 C CG  . ASP B 1 87  ? -12.18500 35.00400  -22.12800 1.000 39.85118 ? 87  ASP B CG  1 
ATOM   1592 O OD1 . ASP B 1 87  ? -11.11400 35.55700  -21.79400 1.000 39.92349 ? 87  ASP B OD1 1 
ATOM   1593 O OD2 . ASP B 1 87  ? -12.66400 35.11100  -23.27800 1.000 45.02715 ? 87  ASP B OD2 1 
ATOM   1594 N N   . ASP B 1 88  ? -13.49800 31.91000  -19.08400 1.000 23.78021 ? 88  ASP B N   1 
ATOM   1595 C CA  . ASP B 1 88  ? -14.41500 31.39000  -18.08100 1.000 27.24711 ? 88  ASP B CA  1 
ATOM   1596 C C   . ASP B 1 88  ? -13.68100 30.79800  -16.87600 1.000 26.15233 ? 88  ASP B C   1 
ATOM   1597 O O   . ASP B 1 88  ? -14.18700 30.88300  -15.74900 1.000 22.33701 ? 88  ASP B O   1 
ATOM   1598 C CB  . ASP B 1 88  ? -15.36100 30.38300  -18.73300 1.000 24.15103 ? 88  ASP B CB  1 
ATOM   1599 C CG  . ASP B 1 88  ? -16.28700 31.04300  -19.73900 1.000 33.74172 ? 88  ASP B CG  1 
ATOM   1600 O OD1 . ASP B 1 88  ? -16.32500 32.29100  -19.75500 1.000 36.07073 ? 88  ASP B OD1 1 
ATOM   1601 O OD2 . ASP B 1 88  ? -16.95200 30.33900  -20.52900 1.000 29.54278 ? 88  ASP B OD2 1 
ATOM   1602 N N   . VAL B 1 89  ? -12.48700 30.22900  -17.06900 1.000 20.14173 ? 89  VAL B N   1 
ATOM   1603 C CA  . VAL B 1 89  ? -11.72100 29.77400  -15.91200 1.000 18.15283 ? 89  VAL B CA  1 
ATOM   1604 C C   . VAL B 1 89  ? -11.19800 30.96800  -15.12200 1.000 22.03512 ? 89  VAL B C   1 
ATOM   1605 O O   . VAL B 1 89  ? -11.12500 30.93100  -13.88600 1.000 24.20881 ? 89  VAL B O   1 
ATOM   1606 C CB  . VAL B 1 89  ? -10.58400 28.83300  -16.35000 1.000 19.07945 ? 89  VAL B CB  1 
ATOM   1607 C CG1 . VAL B 1 89  ? -9.61700  28.58700  -15.20600 1.000 18.63720 ? 89  VAL B CG1 1 
ATOM   1608 C CG2 . VAL B 1 89  ? -11.16900 27.51300  -16.84800 1.000 16.28358 ? 89  VAL B CG2 1 
ATOM   1609 N N   . SER B 1 90  ? -10.83200 32.04500  -15.82000 1.000 19.34325 ? 90  SER B N   1 
ATOM   1610 C CA  . SER B 1 90  ? -10.43000 33.27500  -15.14300 1.000 28.15668 ? 90  SER B CA  1 
ATOM   1611 C C   . SER B 1 90  ? -11.51700 33.76200  -14.19200 1.000 26.76733 ? 90  SER B C   1 
ATOM   1612 O O   . SER B 1 90  ? -11.23300 34.14200  -13.05000 1.000 26.79520 ? 90  SER B O   1 
ATOM   1613 C CB  . SER B 1 90  ? -10.11900 34.35200  -16.17700 1.000 27.24235 ? 90  SER B CB  1 
ATOM   1614 O OG  . SER B 1 90  ? -9.77300  35.56800  -15.55700 1.000 31.58464 ? 90  SER B OG  1 
ATOM   1615 N N   . VAL B 1 91  ? -12.76700 33.75700  -14.65500 1.000 24.80184 ? 91  VAL B N   1 
ATOM   1616 C CA  . VAL B 1 91  ? -13.89200 34.19100  -13.82700 1.000 28.32513 ? 91  VAL B CA  1 
ATOM   1617 C C   . VAL B 1 91  ? -14.15200 33.19700  -12.70500 1.000 29.90805 ? 91  VAL B C   1 
ATOM   1618 O O   . VAL B 1 91  ? -14.20900 33.57000  -11.52900 1.000 34.37764 ? 91  VAL B O   1 
ATOM   1619 C CB  . VAL B 1 91  ? -15.14700 34.38700  -14.69600 1.000 26.59516 ? 91  VAL B CB  1 
ATOM   1620 C CG1 . VAL B 1 91  ? -16.39100 34.45800  -13.82300 1.000 35.81988 ? 91  VAL B CG1 1 
ATOM   1621 C CG2 . VAL B 1 91  ? -15.00000 35.63300  -15.57800 1.000 26.73717 ? 91  VAL B CG2 1 
ATOM   1622 N N   . ALA B 1 92  ? -14.31300 31.91200  -13.05000 1.000 26.83698 ? 92  ALA B N   1 
ATOM   1623 C CA  . ALA B 1 92  ? -14.71200 30.91800  -12.05700 1.000 26.18155 ? 92  ALA B CA  1 
ATOM   1624 C C   . ALA B 1 92  ? -13.68700 30.77600  -10.93700 1.000 31.20588 ? 92  ALA B C   1 
ATOM   1625 O O   . ALA B 1 92  ? -14.04700 30.43600  -9.80400  1.000 31.61596 ? 92  ALA B O   1 
ATOM   1626 C CB  . ALA B 1 92  ? -14.94700 29.56500  -12.73200 1.000 23.74857 ? 92  ALA B CB  1 
ATOM   1627 N N   . ALA B 1 93  ? -12.41200 31.00100  -11.22700 1.000 24.74357 ? 93  ALA B N   1 
ATOM   1628 C CA  . ALA B 1 93  ? -11.37100 30.89500  -10.22000 1.000 26.58913 ? 93  ALA B CA  1 
ATOM   1629 C C   . ALA B 1 93  ? -10.92500 32.25100  -9.70000  1.000 25.68891 ? 93  ALA B C   1 
ATOM   1630 O O   . ALA B 1 93  ? -10.06400 32.30300  -8.81800  1.000 33.61293 ? 93  ALA B O   1 
ATOM   1631 C CB  . ALA B 1 93  ? -10.16500 30.13000  -10.77700 1.000 24.54325 ? 93  ALA B CB  1 
ATOM   1632 N N   . GLU B 1 94  ? -11.49500 33.33800  -10.22000 1.000 30.52635 ? 94  GLU B N   1 
ATOM   1633 C CA  . GLU B 1 94  ? -11.11500 34.70100  -9.85500  1.000 34.26495 ? 94  GLU B CA  1 
ATOM   1634 C C   . GLU B 1 94  ? -9.59300  34.83600  -9.85400  1.000 34.31799 ? 94  GLU B C   1 
ATOM   1635 O O   . GLU B 1 94  ? -8.93600  35.04900  -8.83700  1.000 35.75960 ? 94  GLU B O   1 
ATOM   1636 C CB  . GLU B 1 94  ? -11.72700 35.08600  -8.50600  1.000 37.46318 ? 94  GLU B CB  1 
ATOM   1637 C CG  . GLU B 1 94  ? -13.24500 35.10600  -8.54800  1.000 39.33491 ? 94  GLU B CG  1 
ATOM   1638 C CD  . GLU B 1 94  ? -13.82600 36.37200  -7.95800  1.000 45.13526 ? 94  GLU B CD  1 
ATOM   1639 O OE1 . GLU B 1 94  ? -13.06500 37.34100  -7.72500  1.000 46.32120 ? 94  GLU B OE1 1 
ATOM   1640 O OE2 . GLU B 1 94  ? -15.05000 36.39700  -7.73000  1.000 46.79843 ? 94  GLU B OE2 1 
ATOM   1641 N N   . ILE B 1 95  ? -9.04700  34.66500  -11.04700 1.000 32.36182 ? 95  ILE B N   1 
ATOM   1642 C CA  . ILE B 1 95  ? -7.60700  34.63600  -11.21600 1.000 27.49403 ? 95  ILE B CA  1 
ATOM   1643 C C   . ILE B 1 95  ? -7.27700  35.30900  -12.53400 1.000 29.12712 ? 95  ILE B C   1 
ATOM   1644 O O   . ILE B 1 95  ? -7.98500  35.12500  -13.53100 1.000 29.22830 ? 95  ILE B O   1 
ATOM   1645 C CB  . ILE B 1 95  ? -7.08400  33.19300  -11.16200 1.000 33.15143 ? 95  ILE B CB  1 
ATOM   1646 C CG1 . ILE B 1 95  ? -5.58600  33.16600  -11.39400 1.000 32.29969 ? 95  ILE B CG1 1 
ATOM   1647 C CG2 . ILE B 1 95  ? -7.79600  32.32500  -12.18800 1.000 31.93824 ? 95  ILE B CG2 1 
ATOM   1648 C CD1 . ILE B 1 95  ? -5.07900  31.81700  -11.26700 1.000 35.67720 ? 95  ILE B CD1 1 
ATOM   1649 N N   . ASP B 1 96  ? -6.20700  36.09900  -12.52600 1.000 25.41277 ? 96  ASP B N   1 
ATOM   1650 C CA  . ASP B 1 96  ? -5.82600  36.87100  -13.69700 1.000 28.82195 ? 96  ASP B CA  1 
ATOM   1651 C C   . ASP B 1 96  ? -5.58500  35.94100  -14.87700 1.000 32.89539 ? 96  ASP B C   1 
ATOM   1652 O O   . ASP B 1 96  ? -4.92200  34.90800  -14.73800 1.000 31.11865 ? 96  ASP B O   1 
ATOM   1653 C CB  . ASP B 1 96  ? -4.56900  37.68600  -13.39600 1.000 35.60652 ? 96  ASP B CB  1 
ATOM   1654 C CG  . ASP B 1 96  ? -4.32000  38.78300  -14.41900 1.000 44.38375 ? 96  ASP B CG  1 
ATOM   1655 O OD1 . ASP B 1 96  ? -4.29600  38.49100  -15.63700 1.000 39.23016 ? 96  ASP B OD1 1 
ATOM   1656 O OD2 . ASP B 1 96  ? -4.14300  39.94900  -14.00000 1.000 55.62983 ? 96  ASP B OD2 1 
ATOM   1657 N N   . ARG B 1 97  ? -6.13500  36.31700  -16.03800 1.000 28.75896 ? 97  ARG B N   1 
ATOM   1658 C CA  . ARG B 1 97  ? -5.95400  35.53100  -17.25800 1.000 30.83207 ? 97  ARG B CA  1 
ATOM   1659 C C   . ARG B 1 97  ? -4.48600  35.28400  -17.57300 1.000 26.72768 ? 97  ARG B C   1 
ATOM   1660 O O   . ARG B 1 97  ? -4.15500  34.28500  -18.22000 1.000 30.77521 ? 97  ARG B O   1 
ATOM   1661 C CB  . ARG B 1 97  ? -6.62300  36.23000  -18.43600 1.000 32.75088 ? 97  ARG B CB  1 
ATOM   1662 C CG  . ARG B 1 97  ? -8.14200  36.10400  -18.47900 1.000 38.55313 ? 97  ARG B CG  1 
ATOM   1663 C CD  . ARG B 1 97  ? -8.75200  37.04400  -19.53400 1.000 43.70453 ? 97  ARG B CD  1 
ATOM   1664 N NE  . ARG B 1 97  ? -8.74400  36.48000  -20.88100 1.000 44.99071 ? 97  ARG B NE  1 
ATOM   1665 C CZ  . ARG B 1 97  ? -7.76500  36.62900  -21.76500 1.000 49.09594 ? 97  ARG B CZ  1 
ATOM   1666 N NH1 . ARG B 1 97  ? -6.66700  37.30900  -21.47500 1.000 51.58450 ? 97  ARG B NH1 1 
ATOM   1667 N NH2 . ARG B 1 97  ? -7.89100  36.07900  -22.97100 1.000 48.55092 ? 97  ARG B NH2 1 
ATOM   1668 N N   . LYS B 1 98  ? -3.59100  36.16600  -17.12000 1.000 29.44246 ? 98  LYS B N   1 
ATOM   1669 C CA  . LYS B 1 98  ? -2.16800  35.98700  -17.38100 1.000 33.18222 ? 98  LYS B CA  1 
ATOM   1670 C C   . LYS B 1 98  ? -1.58600  34.77700  -16.66400 1.000 32.90379 ? 98  LYS B C   1 
ATOM   1671 O O   . LYS B 1 98  ? -0.47300  34.35800  -16.99700 1.000 28.92034 ? 98  LYS B O   1 
ATOM   1672 C CB  . LYS B 1 98  ? -1.38500  37.23200  -16.96600 1.000 35.82849 ? 98  LYS B CB  1 
ATOM   1673 C CG  . LYS B 1 98  ? -1.18500  37.36700  -15.45600 1.000 40.63429 ? 98  LYS B CG  1 
ATOM   1674 C CD  . LYS B 1 98  ? -0.45800  38.65800  -15.10300 1.000 45.91379 ? 98  LYS B CD  1 
ATOM   1675 C CE  . LYS B 1 98  ? -0.41200  38.87000  -13.60000 1.000 45.96723 ? 98  LYS B CE  1 
ATOM   1676 N NZ  . LYS B 1 98  ? -0.41400  40.32100  -13.25800 1.000 51.37207 ? 98  LYS B NZ  1 
ATOM   1677 N N   . HIS B 1 99  ? -2.29300  34.22400  -15.67600 1.000 27.97817 ? 99  HIS B N   1 
ATOM   1678 C CA  . HIS B 1 99  ? -1.84000  33.03000  -14.97700 1.000 25.97288 ? 99  HIS B CA  1 
ATOM   1679 C C   . HIS B 1 99  ? -2.31600  31.74600  -15.63800 1.000 21.96771 ? 99  HIS B C   1 
ATOM   1680 O O   . HIS B 1 99  ? -2.01100  30.66400  -15.13400 1.000 22.46920 ? 99  HIS B O   1 
ATOM   1681 C CB  . HIS B 1 99  ? -2.32700  33.03800  -13.52300 1.000 27.10331 ? 99  HIS B CB  1 
ATOM   1682 C CG  . HIS B 1 99  ? -1.71800  34.11500  -12.67600 1.000 32.99423 ? 99  HIS B CG  1 
ATOM   1683 N ND1 . HIS B 1 99  ? -0.39400  34.10300  -12.29300 1.000 35.64252 ? 99  HIS B ND1 1 
ATOM   1684 C CD2 . HIS B 1 99  ? -2.26300  35.21900  -12.11100 1.000 34.01127 ? 99  HIS B CD2 1 
ATOM   1685 C CE1 . HIS B 1 99  ? -0.14600  35.16300  -11.54300 1.000 38.81752 ? 99  HIS B CE1 1 
ATOM   1686 N NE2 . HIS B 1 99  ? -1.26300  35.85700  -11.41900 1.000 35.92422 ? 99  HIS B NE2 1 
ATOM   1687 N N   . ILE B 1 100 ? -3.08100  31.83400  -16.72000 1.000 19.92276 ? 100 ILE B N   1 
ATOM   1688 C CA  . ILE B 1 100 ? -3.79600  30.68500  -17.26700 1.000 20.49549 ? 100 ILE B CA  1 
ATOM   1689 C C   . ILE B 1 100 ? -3.15300  30.27400  -18.58600 1.000 24.43059 ? 100 ILE B C   1 
ATOM   1690 O O   . ILE B 1 100 ? -3.04100  31.08500  -19.51300 1.000 23.38175 ? 100 ILE B O   1 
ATOM   1691 C CB  . ILE B 1 100 ? -5.28800  30.98700  -17.45500 1.000 22.62426 ? 100 ILE B CB  1 
ATOM   1692 C CG1 . ILE B 1 100 ? -5.90400  31.41800  -16.11500 1.000 23.08878 ? 100 ILE B CG1 1 
ATOM   1693 C CG2 . ILE B 1 100 ? -6.00900  29.77000  -18.01300 1.000 21.95338 ? 100 ILE B CG2 1 
ATOM   1694 C CD1 . ILE B 1 100 ? -7.39100  31.57000  -16.17200 1.000 22.19354 ? 100 ILE B CD1 1 
ATOM   1695 N N   . TRP B 1 101 ? -2.74200  29.00600  -18.66500 1.000 16.08265 ? 101 TRP B N   1 
ATOM   1696 C CA  . TRP B 1 101 ? -2.20300  28.39900  -19.87600 1.000 16.09531 ? 101 TRP B CA  1 
ATOM   1697 C C   . TRP B 1 101 ? -3.14000  27.28500  -20.31200 1.000 16.18080 ? 101 TRP B C   1 
ATOM   1698 O O   . TRP B 1 101 ? -3.65600  26.53800  -19.47500 1.000 12.14967 ? 101 TRP B O   1 
ATOM   1699 C CB  . TRP B 1 101 ? -0.80100  27.81700  -19.64000 1.000 18.56343 ? 101 TRP B CB  1 
ATOM   1700 C CG  . TRP B 1 101 ? 0.26700   28.79400  -19.24300 1.000 21.25722 ? 101 TRP B CG  1 
ATOM   1701 C CD1 . TRP B 1 101 ? 0.14100   29.88900  -18.42500 1.000 26.77518 ? 101 TRP B CD1 1 
ATOM   1702 C CD2 . TRP B 1 101 ? 1.64100   28.74400  -19.63500 1.000 20.21457 ? 101 TRP B CD2 1 
ATOM   1703 N NE1 . TRP B 1 101 ? 1.35400   30.52300  -18.29900 1.000 29.37809 ? 101 TRP B NE1 1 
ATOM   1704 C CE2 . TRP B 1 101 ? 2.29100   29.83900  -19.03300 1.000 25.79308 ? 101 TRP B CE2 1 
ATOM   1705 C CE3 . TRP B 1 101 ? 2.38200   27.87700  -20.44400 1.000 17.39455 ? 101 TRP B CE3 1 
ATOM   1706 C CZ2 . TRP B 1 101 ? 3.65000   30.08500  -19.20300 1.000 23.51141 ? 101 TRP B CZ2 1 
ATOM   1707 C CZ3 . TRP B 1 101 ? 3.72800   28.11900  -20.61700 1.000 19.50722 ? 101 TRP B CZ3 1 
ATOM   1708 C CH2 . TRP B 1 101 ? 4.35000   29.22300  -20.00400 1.000 27.14168 ? 101 TRP B CH2 1 
ATOM   1709 N N   . VAL B 1 102 ? -3.37500  27.16800  -21.61900 1.000 11.93518 ? 102 VAL B N   1 
ATOM   1710 C CA  . VAL B 1 102 ? -4.29300  26.16000  -22.14400 1.000 12.67237 ? 102 VAL B CA  1 
ATOM   1711 C C   . VAL B 1 102 ? -3.68800  25.59300  -23.42200 1.000 12.82678 ? 102 VAL B C   1 
ATOM   1712 O O   . VAL B 1 102 ? -3.48400  26.33400  -24.38900 1.000 12.12601 ? 102 VAL B O   1 
ATOM   1713 C CB  . VAL B 1 102 ? -5.69400  26.73300  -22.43300 1.000 14.60029 ? 102 VAL B CB  1 
ATOM   1714 C CG1 . VAL B 1 102 ? -6.60700  25.65300  -22.98200 1.000 12.87285 ? 102 VAL B CG1 1 
ATOM   1715 C CG2 . VAL B 1 102 ? -6.30800  27.38300  -21.17200 1.000 15.99287 ? 102 VAL B CG2 1 
ATOM   1716 N N   . TYR B 1 103 ? -3.39000  24.29300  -23.42300 1.000 9.86643  ? 103 TYR B N   1 
ATOM   1717 C CA  . TYR B 1 103 ? -2.94000  23.56700  -24.61200 1.000 12.00947 ? 103 TYR B CA  1 
ATOM   1718 C C   . TYR B 1 103 ? -3.94700  22.48300  -24.96100 1.000 12.47865 ? 103 TYR B C   1 
ATOM   1719 O O   . TYR B 1 103 ? -4.38400  21.74700  -24.08000 1.000 9.28109  ? 103 TYR B O   1 
ATOM   1720 C CB  . TYR B 1 103 ? -1.60700  22.84900  -24.38100 1.000 10.53429 ? 103 TYR B CB  1 
ATOM   1721 C CG  . TYR B 1 103 ? -0.36800  23.68500  -24.18300 1.000 11.84623 ? 103 TYR B CG  1 
ATOM   1722 C CD1 . TYR B 1 103 ? -0.40500  25.07900  -24.19700 1.000 10.96349 ? 103 TYR B CD1 1 
ATOM   1723 C CD2 . TYR B 1 103 ? 0.84700   23.05700  -23.97500 1.000 11.72482 ? 103 TYR B CD2 1 
ATOM   1724 C CE1 . TYR B 1 103 ? 0.74500   25.81800  -24.00400 1.000 13.92093 ? 103 TYR B CE1 1 
ATOM   1725 C CE2 . TYR B 1 103 ? 2.00100   23.77500  -23.78100 1.000 14.22085 ? 103 TYR B CE2 1 
ATOM   1726 C CZ  . TYR B 1 103 ? 1.94800   25.15300  -23.81100 1.000 15.21517 ? 103 TYR B CZ  1 
ATOM   1727 O OH  . TYR B 1 103 ? 3.12000   25.82900  -23.62600 1.000 17.59544 ? 103 TYR B OH  1 
ATOM   1728 N N   . PHE B 1 104 ? -4.26100  22.33300  -26.24900 1.000 12.96762 ? 104 PHE B N   1 
ATOM   1729 C CA  . PHE B 1 104 ? -5.09800  21.23700  -26.72800 1.000 13.00512 ? 104 PHE B CA  1 
ATOM   1730 C C   . PHE B 1 104 ? -4.26500  20.23500  -27.51100 1.000 14.52446 ? 104 PHE B C   1 
ATOM   1731 O O   . PHE B 1 104 ? -3.60300  20.60800  -28.48300 1.000 13.55384 ? 104 PHE B O   1 
ATOM   1732 C CB  . PHE B 1 104 ? -6.22100  21.73900  -27.63500 1.000 15.00861 ? 104 PHE B CB  1 
ATOM   1733 C CG  . PHE B 1 104 ? -7.29400  22.47300  -26.91800 1.000 18.68762 ? 104 PHE B CG  1 
ATOM   1734 C CD1 . PHE B 1 104 ? -7.33400  22.50200  -25.53300 1.000 17.78969 ? 104 PHE B CD1 1 
ATOM   1735 C CD2 . PHE B 1 104 ? -8.28600  23.12500  -27.63600 1.000 22.14161 ? 104 PHE B CD2 1 
ATOM   1736 C CE1 . PHE B 1 104 ? -8.33900  23.18900  -24.86300 1.000 19.59328 ? 104 PHE B CE1 1 
ATOM   1737 C CE2 . PHE B 1 104 ? -9.29400  23.81600  -26.97200 1.000 22.88115 ? 104 PHE B CE2 1 
ATOM   1738 C CZ  . PHE B 1 104 ? -9.31300  23.85300  -25.58200 1.000 20.71249 ? 104 PHE B CZ  1 
ATOM   1739 N N   . GLY B 1 105 ? -4.32300  18.96700  -27.10700 1.000 13.01308 ? 105 GLY B N   1 
ATOM   1740 C CA  . GLY B 1 105 ? -3.79800  17.86600  -27.89200 1.000 16.52545 ? 105 GLY B CA  1 
ATOM   1741 C C   . GLY B 1 105 ? -4.93700  17.07600  -28.50900 1.000 16.19323 ? 105 GLY B C   1 
ATOM   1742 O O   . GLY B 1 105 ? -6.05100  17.03300  -27.96900 1.000 17.41279 ? 105 GLY B O   1 
ATOM   1743 N N   . GLU B 1 106 ? -4.67000  16.46100  -29.65200 1.000 12.97737 ? 106 GLU B N   1 
ATOM   1744 C CA  . GLU B 1 106 ? -5.68600  15.69800  -30.36300 1.000 15.26887 ? 106 GLU B CA  1 
ATOM   1745 C C   . GLU B 1 106 ? -5.16400  14.32000  -30.74000 1.000 17.39456 ? 106 GLU B C   1 
ATOM   1746 O O   . GLU B 1 106 ? -3.97400  14.13600  -31.01500 1.000 14.54353 ? 106 GLU B O   1 
ATOM   1747 C CB  . GLU B 1 106 ? -6.13300  16.38300  -31.64700 1.000 21.17545 ? 106 GLU B CB  1 
ATOM   1748 C CG  . GLU B 1 106 ? -6.64500  17.78000  -31.50700 1.000 19.30140 ? 106 GLU B CG  1 
ATOM   1749 C CD  . GLU B 1 106 ? -6.52100  18.50000  -32.81800 1.000 20.71248 ? 106 GLU B CD  1 
ATOM   1750 O OE1 . GLU B 1 106 ? -5.41900  19.01600  -33.11500 1.000 22.22252 ? 106 GLU B OE1 1 
ATOM   1751 O OE2 . GLU B 1 106 ? -7.51200  18.51500  -33.56400 1.000 21.49079 ? 106 GLU B OE2 1 
ATOM   1752 N N   . MET B 1 107 ? -6.08500  13.37000  -30.81800 1.000 13.48779 ? 107 MET B N   1 
ATOM   1753 C CA  . MET B 1 107 ? -5.79400  11.99100  -31.17400 1.000 17.15046 ? 107 MET B CA  1 
ATOM   1754 C C   . MET B 1 107 ? -6.92900  11.44800  -32.02400 1.000 17.65500 ? 107 MET B C   1 
ATOM   1755 O O   . MET B 1 107 ? -8.06900  11.92000  -31.92000 1.000 15.15297 ? 107 MET B O   1 
ATOM   1756 C CB  . MET B 1 107 ? -5.65200  11.08800  -29.93900 1.000 16.64858 ? 107 MET B CB  1 
ATOM   1757 C CG  . MET B 1 107 ? -4.54700  11.45100  -29.00300 1.000 19.43722 ? 107 MET B CG  1 
ATOM   1758 S SD  . MET B 1 107 ? -5.13200  11.14600  -27.32100 1.000 19.65513 ? 107 MET B SD  1 
ATOM   1759 C CE  . MET B 1 107 ? -6.10600  12.66700  -27.11400 1.000 15.36385 ? 107 MET B CE  1 
ATOM   1760 N N   . PRO B 1 108 ? -6.64800  10.45600  -32.86900 1.000 15.59410 ? 108 PRO B N   1 
ATOM   1761 C CA  . PRO B 1 108 ? -7.72900  9.77600   -33.59000 1.000 15.96705 ? 108 PRO B CA  1 
ATOM   1762 C C   . PRO B 1 108 ? -8.71400  9.15800   -32.61400 1.000 17.38187 ? 108 PRO B C   1 
ATOM   1763 O O   . PRO B 1 108 ? -8.32400  8.57100   -31.60000 1.000 14.53113 ? 108 PRO B O   1 
ATOM   1764 C CB  . PRO B 1 108 ? -6.99300  8.70300   -34.40400 1.000 19.33995 ? 108 PRO B CB  1 
ATOM   1765 C CG  . PRO B 1 108 ? -5.60100  9.24300   -34.56200 1.000 19.85709 ? 108 PRO B CG  1 
ATOM   1766 C CD  . PRO B 1 108 ? -5.31200  9.98900   -33.29300 1.000 19.60236 ? 108 PRO B CD  1 
ATOM   1767 N N   . ALA B 1 109 ? -10.00500 9.29700   -32.92900 1.000 16.49014 ? 109 ALA B N   1 
ATOM   1768 C CA  . ALA B 1 109 ? -11.03600 8.70100   -32.08500 1.000 20.65448 ? 109 ALA B CA  1 
ATOM   1769 C C   . ALA B 1 109 ? -10.82500 7.20400   -31.92400 1.000 19.17020 ? 109 ALA B C   1 
ATOM   1770 O O   . ALA B 1 109 ? -11.24300 6.62200   -30.91500 1.000 20.72083 ? 109 ALA B O   1 
ATOM   1771 C CB  . ALA B 1 109 ? -12.42100 8.97800   -32.67100 1.000 22.69761 ? 109 ALA B CB  1 
ATOM   1772 N N   . GLN B 1 110 ? -10.16200 6.57200   -32.89300 1.000 17.58115 ? 110 GLN B N   1 
ATOM   1773 C CA  . GLN B 1 110 ? -9.99900  5.12400   -32.91500 1.000 22.44833 ? 110 GLN B CA  1 
ATOM   1774 C C   . GLN B 1 110 ? -9.02600  4.61400   -31.85900 1.000 25.08107 ? 110 GLN B C   1 
ATOM   1775 O O   . GLN B 1 110 ? -8.96000  3.39800   -31.64400 1.000 24.14382 ? 110 GLN B O   1 
ATOM   1776 C CB  . GLN B 1 110 ? -9.53600  4.67000   -34.30900 1.000 27.41040 ? 110 GLN B CB  1 
ATOM   1777 C CG  . GLN B 1 110 ? -10.57500 4.89200   -35.41800 1.000 33.27683 ? 110 GLN B CG  1 
ATOM   1778 C CD  . GLN B 1 110 ? -10.56500 6.30500   -36.00000 1.000 39.82957 ? 110 GLN B CD  1 
ATOM   1779 O OE1 . GLN B 1 110 ? -9.69900  7.12700   -35.67100 1.000 32.68501 ? 110 GLN B OE1 1 
ATOM   1780 N NE2 . GLN B 1 110 ? -11.53200 6.59200   -36.87900 1.000 43.00086 ? 110 GLN B NE2 1 
ATOM   1781 N N   . GLN B 1 111 ? -8.27300  5.49600   -31.20000 1.000 17.82381 ? 111 GLN B N   1 
ATOM   1782 C CA  . GLN B 1 111 ? -7.40700  5.11300   -30.09200 1.000 18.55098 ? 111 GLN B CA  1 
ATOM   1783 C C   . GLN B 1 111 ? -7.79500  5.86400   -28.82200 1.000 18.35321 ? 111 GLN B C   1 
ATOM   1784 O O   . GLN B 1 111 ? -6.94300  6.20100   -27.99200 1.000 16.65157 ? 111 GLN B O   1 
ATOM   1785 C CB  . GLN B 1 111 ? -5.93700  5.33800   -30.45500 1.000 19.66388 ? 111 GLN B CB  1 
ATOM   1786 C CG  . GLN B 1 111 ? -5.57600  6.77100   -30.82300 1.000 15.69008 ? 111 GLN B CG  1 
ATOM   1787 C CD  . GLN B 1 111 ? -4.34800  6.85600   -31.70700 1.000 17.35892 ? 111 GLN B CD  1 
ATOM   1788 O OE1 . GLN B 1 111 ? -4.31600  6.27400   -32.79600 1.000 20.50295 ? 111 GLN B OE1 1 
ATOM   1789 N NE2 . GLN B 1 111 ? -3.33200  7.59200   -31.25600 1.000 14.87592 ? 111 GLN B NE2 1 
ATOM   1790 N N   . MET B 1 112 ? -9.08700  6.15200   -28.67200 1.000 17.23146 ? 112 MET B N   1 
ATOM   1791 C CA  . MET B 1 112 ? -9.62000  6.84000   -27.50800 1.000 15.40866 ? 112 MET B CA  1 
ATOM   1792 C C   . MET B 1 112 ? -10.81800 6.06400   -26.98700 1.000 20.82514 ? 112 MET B C   1 
ATOM   1793 O O   . MET B 1 112 ? -11.74200 5.74900   -27.74900 1.000 19.36713 ? 112 MET B O   1 
ATOM   1794 C CB  . MET B 1 112 ? -10.02900 8.27500   -27.83600 1.000 14.95512 ? 112 MET B CB  1 
ATOM   1795 C CG  . MET B 1 112 ? -8.88100  9.14000   -28.30200 1.000 14.93639 ? 112 MET B CG  1 
ATOM   1796 S SD  . MET B 1 112 ? -9.41500  10.80100  -28.73800 1.000 16.79877 ? 112 MET B SD  1 
ATOM   1797 C CE  . MET B 1 112 ? -9.91800  11.49000  -27.18300 1.000 19.64815 ? 112 MET B CE  1 
ATOM   1798 N N   . VAL B 1 113 ? -10.80800 5.77500   -25.68700 1.000 18.17360 ? 113 VAL B N   1 
ATOM   1799 C CA  . VAL B 1 113 ? -11.85400 4.98700   -25.04200 1.000 21.44189 ? 113 VAL B CA  1 
ATOM   1800 C C   . VAL B 1 113 ? -12.37800 5.78100   -23.85700 1.000 22.85523 ? 113 VAL B C   1 
ATOM   1801 O O   . VAL B 1 113 ? -11.59700 6.23800   -23.01500 1.000 20.48441 ? 113 VAL B O   1 
ATOM   1802 C CB  . VAL B 1 113 ? -11.34200 3.60300   -24.59500 1.000 23.33489 ? 113 VAL B CB  1 
ATOM   1803 C CG1 . VAL B 1 113 ? -12.40000 2.88300   -23.76900 1.000 26.87898 ? 113 VAL B CG1 1 
ATOM   1804 C CG2 . VAL B 1 113 ? -10.94900 2.75500   -25.80200 1.000 22.24106 ? 113 VAL B CG2 1 
ATOM   1805 N N   . GLU B 1 114 ? -13.69200 5.97800   -23.80800 1.000 24.74704 ? 114 GLU B N   1 
ATOM   1806 C CA  . GLU B 1 114 ? -14.34200 6.63400   -22.68600 1.000 24.18130 ? 114 GLU B CA  1 
ATOM   1807 C C   . GLU B 1 114 ? -15.46200 5.74100   -22.18200 1.000 31.20494 ? 114 GLU B C   1 
ATOM   1808 O O   . GLU B 1 114 ? -16.14900 5.09600   -22.97900 1.000 31.35626 ? 114 GLU B O   1 
ATOM   1809 C CB  . GLU B 1 114 ? -14.89700 8.00100   -23.08400 1.000 25.79614 ? 114 GLU B CB  1 
ATOM   1810 C CG  . GLU B 1 114 ? -13.84000 8.98800   -23.53500 1.000 24.72486 ? 114 GLU B CG  1 
ATOM   1811 C CD  . GLU B 1 114 ? -14.46100 10.29500  -23.94400 1.000 33.99734 ? 114 GLU B CD  1 
ATOM   1812 O OE1 . GLU B 1 114 ? -15.70100 10.36600  -23.97500 1.000 46.21858 ? 114 GLU B OE1 1 
ATOM   1813 O OE2 . GLU B 1 114 ? -13.71300 11.25500  -24.24100 1.000 34.19371 ? 114 GLU B OE2 1 
ATOM   1814 N N   . TYR B 1 115 ? -15.64300 5.71400   -20.85900 1.000 35.35044 ? 115 TYR B N   1 
ATOM   1815 C CA  . TYR B 1 115 ? -16.61400 4.82100   -20.22500 1.000 34.12870 ? 115 TYR B CA  1 
ATOM   1816 C C   . TYR B 1 115 ? -16.45700 3.39200   -20.72600 1.000 34.90498 ? 115 TYR B C   1 
ATOM   1817 O O   . TYR B 1 115 ? -17.43600 2.67200   -20.90900 1.000 36.51140 ? 115 TYR B O   1 
ATOM   1818 C CB  . TYR B 1 115 ? -18.04300 5.30700   -20.45200 1.000 36.73976 ? 115 TYR B CB  1 
ATOM   1819 C CG  . TYR B 1 115 ? -18.30900 6.63900   -19.82000 1.000 35.38981 ? 115 TYR B CG  1 
ATOM   1820 C CD1 . TYR B 1 115 ? -18.55600 6.73300   -18.45800 1.000 36.89515 ? 115 TYR B CD1 1 
ATOM   1821 C CD2 . TYR B 1 115 ? -18.29600 7.80600   -20.57400 1.000 37.59317 ? 115 TYR B CD2 1 
ATOM   1822 C CE1 . TYR B 1 115 ? -18.79500 7.93800   -17.86800 1.000 35.73600 ? 115 TYR B CE1 1 
ATOM   1823 C CE2 . TYR B 1 115 ? -18.53600 9.02800   -19.98700 1.000 36.46689 ? 115 TYR B CE2 1 
ATOM   1824 C CZ  . TYR B 1 115 ? -18.78700 9.08600   -18.63000 1.000 38.20146 ? 115 TYR B CZ  1 
ATOM   1825 O OH  . TYR B 1 115 ? -19.02700 10.29100  -18.01100 1.000 37.76807 ? 115 TYR B OH  1 
ATOM   1826 N N   . GLY B 1 116 ? -15.21200 2.99000   -20.97500 1.000 34.35980 ? 116 GLY B N   1 
ATOM   1827 C CA  . GLY B 1 116 ? -14.93800 1.67700   -21.52900 1.000 34.83205 ? 116 GLY B CA  1 
ATOM   1828 C C   . GLY B 1 116 ? -15.43700 1.43700   -22.94200 1.000 35.58093 ? 116 GLY B C   1 
ATOM   1829 O O   . GLY B 1 116 ? -15.51400 0.28100   -23.36100 1.000 40.47502 ? 116 GLY B O   1 
ATOM   1830 N N   . ARG B 1 117 ? -15.74800 2.49400   -23.70800 1.000 37.08121 ? 117 ARG B N   1 
ATOM   1831 C CA  . ARG B 1 117 ? -16.20600 2.36700   -25.09200 1.000 36.11901 ? 117 ARG B CA  1 
ATOM   1832 C C   . ARG B 1 117 ? -15.38000 3.25900   -26.01800 1.000 33.03607 ? 117 ARG B C   1 
ATOM   1833 O O   . ARG B 1 117 ? -14.93800 4.33800   -25.62200 1.000 29.64654 ? 117 ARG B O   1 
ATOM   1834 C CB  . ARG B 1 117 ? -17.69600 2.74600   -25.22100 1.000 40.19938 ? 117 ARG B CB  1 
ATOM   1835 C CG  . ARG B 1 117 ? -18.64900 1.56700   -25.33800 1.000 52.23642 ? 117 ARG B CG  1 
ATOM   1836 C CD  . ARG B 1 117 ? -18.53400 0.90000   -26.70800 1.000 56.45688 ? 117 ARG B CD  1 
ATOM   1837 N NE  . ARG B 1 117 ? -19.69400 0.06900   -27.01100 1.000 57.69950 ? 117 ARG B NE  1 
ATOM   1838 C CZ  . ARG B 1 117 ? -19.85100 -0.61300  -28.13700 1.000 61.06979 ? 117 ARG B CZ  1 
ATOM   1839 N NH1 . ARG B 1 117 ? -18.93100 -0.59900  -29.08700 1.000 60.16952 ? 117 ARG B NH1 1 
ATOM   1840 N NH2 . ARG B 1 117 ? -20.96100 -1.32300  -28.31500 1.000 63.72085 ? 117 ARG B NH2 1 
ATOM   1841 N N   . PHE B 1 118 ? -15.20300 2.81600   -27.26700 1.000 29.43747 ? 118 PHE B N   1 
ATOM   1842 C CA  . PHE B 1 118 ? -14.50700 3.61600   -28.27500 1.000 32.01975 ? 118 PHE B CA  1 
ATOM   1843 C C   . PHE B 1 118 ? -15.31500 4.84000   -28.68900 1.000 36.80536 ? 118 PHE B C   1 
ATOM   1844 O O   . PHE B 1 118 ? -16.54800 4.82500   -28.70900 1.000 34.04304 ? 118 PHE B O   1 
ATOM   1845 C CB  . PHE B 1 118 ? -14.20600 2.78700   -29.52500 1.000 29.93042 ? 118 PHE B CB  1 
ATOM   1846 C CG  . PHE B 1 118 ? -12.96600 1.96100   -29.41500 1.000 38.37299 ? 118 PHE B CG  1 
ATOM   1847 C CD1 . PHE B 1 118 ? -11.71500 2.56100   -29.46700 1.000 31.18624 ? 118 PHE B CD1 1 
ATOM   1848 C CD2 . PHE B 1 118 ? -13.04400 0.58800   -29.24200 1.000 39.82990 ? 118 PHE B CD2 1 
ATOM   1849 C CE1 . PHE B 1 118 ? -10.56200 1.80400   -29.35100 1.000 31.31645 ? 118 PHE B CE1 1 
ATOM   1850 C CE2 . PHE B 1 118 ? -11.89400 -0.17600  -29.13000 1.000 38.48973 ? 118 PHE B CE2 1 
ATOM   1851 C CZ  . PHE B 1 118 ? -10.65000 0.43500   -29.18500 1.000 34.39708 ? 118 PHE B CZ  1 
ATOM   1852 N N   . LEU B 1 119 ? -14.58500 5.91900   -29.06900 1.000 30.03770 ? 119 LEU B N   1 
ATOM   1853 C CA  . LEU B 1 119 ? -15.24000 7.17600   -29.39900 1.000 30.32836 ? 119 LEU B CA  1 
ATOM   1854 C C   . LEU B 1 119 ? -15.64500 7.21500   -30.87100 1.000 30.63434 ? 119 LEU B C   1 
ATOM   1855 O O   . LEU B 1 119 ? -14.99100 6.60300   -31.71800 1.000 29.76173 ? 119 LEU B O   1 
ATOM   1856 C CB  . LEU B 1 119 ? -14.31500 8.35200   -29.09300 1.000 27.36292 ? 119 LEU B CB  1 
ATOM   1857 C CG  . LEU B 1 119 ? -14.45600 8.94900   -27.69700 1.000 32.87416 ? 119 LEU B CG  1 
ATOM   1858 C CD1 . LEU B 1 119 ? -14.68400 7.86300   -26.66000 1.000 31.44310 ? 119 LEU B CD1 1 
ATOM   1859 C CD2 . LEU B 1 119 ? -13.22900 9.77600   -27.35500 1.000 29.76960 ? 119 LEU B CD2 1 
ATOM   1860 N N   . PRO B 1 120 ? -16.73000 7.93300   -31.20400 1.000 34.98075 ? 120 PRO B N   1 
ATOM   1861 C CA  . PRO B 1 120 ? -17.11900 8.08900   -32.61300 1.000 36.17912 ? 120 PRO B CA  1 
ATOM   1862 C C   . PRO B 1 120 ? -16.22000 9.08600   -33.34100 1.000 35.37075 ? 120 PRO B C   1 
ATOM   1863 O O   . PRO B 1 120 ? -15.77900 10.02400  -32.67300 1.000 30.92205 ? 120 PRO B O   1 
ATOM   1864 C CB  . PRO B 1 120 ? -18.55200 8.60600   -32.52200 1.000 39.63013 ? 120 PRO B CB  1 
ATOM   1865 C CG  . PRO B 1 120 ? -18.59100 9.35800   -31.22900 1.000 39.67153 ? 120 PRO B CG  1 
ATOM   1866 C CD  . PRO B 1 120 ? -17.68000 8.59300   -30.28800 1.000 36.66828 ? 120 PRO B CD  1 
ATOM   1867 N N   . PRO C 1 1   ? 7.22500   2.74400   -24.10900 1.000 24.14714 ? 1   PRO C N   1 
ATOM   1868 C CA  . PRO C 1 1   ? 6.06500   3.59900   -23.82900 1.000 19.98053 ? 1   PRO C CA  1 
ATOM   1869 C C   . PRO C 1 1   ? 5.90900   3.93700   -22.35000 1.000 16.96328 ? 1   PRO C C   1 
ATOM   1870 O O   . PRO C 1 1   ? 6.43100   3.23800   -21.47500 1.000 17.10800 ? 1   PRO C O   1 
ATOM   1871 C CB  . PRO C 1 1   ? 4.88500   2.75200   -24.29500 1.000 15.75979 ? 1   PRO C CB  1 
ATOM   1872 C CG  . PRO C 1 1   ? 5.34400   1.34600   -24.05500 1.000 24.06820 ? 1   PRO C CG  1 
ATOM   1873 C CD  . PRO C 1 1   ? 6.82700   1.34500   -24.34900 1.000 30.05478 ? 1   PRO C CD  1 
ATOM   1874 N N   . VAL C 1 2   ? 5.17800   5.01100   -22.09400 1.000 11.88987 ? 2   VAL C N   1 
ATOM   1875 C CA  . VAL C 1 2   ? 4.85000   5.44700   -20.74900 1.000 12.28351 ? 2   VAL C CA  1 
ATOM   1876 C C   . VAL C 1 2   ? 3.33900   5.48900   -20.63600 1.000 12.15635 ? 2   VAL C C   1 
ATOM   1877 O O   . VAL C 1 2   ? 2.67300   6.13100   -21.45600 1.000 11.49963 ? 2   VAL C O   1 
ATOM   1878 C CB  . VAL C 1 2   ? 5.44200   6.83200   -20.42500 1.000 13.56106 ? 2   VAL C CB  1 
ATOM   1879 C CG1 . VAL C 1 2   ? 4.91400   7.32100   -19.06300 1.000 13.68619 ? 2   VAL C CG1 1 
ATOM   1880 C CG2 . VAL C 1 2   ? 6.96400   6.79200   -20.45300 1.000 13.99369 ? 2   VAL C CG2 1 
ATOM   1881 N N   . TYR C 1 3   ? 2.80200   4.81700   -19.62800 1.000 9.63104  ? 3   TYR C N   1 
ATOM   1882 C CA  . TYR C 1 3   ? 1.38200   4.87300   -19.31200 1.000 8.81373  ? 3   TYR C CA  1 
ATOM   1883 C C   . TYR C 1 3   ? 1.22300   5.68400   -18.03600 1.000 11.17088 ? 3   TYR C C   1 
ATOM   1884 O O   . TYR C 1 3   ? 1.61400   5.22700   -16.95600 1.000 11.04695 ? 3   TYR C O   1 
ATOM   1885 C CB  . TYR C 1 3   ? 0.78800   3.47500   -19.15700 1.000 11.87277 ? 3   TYR C CB  1 
ATOM   1886 C CG  . TYR C 1 3   ? 0.82900   2.70200   -20.44500 1.000 11.35169 ? 3   TYR C CG  1 
ATOM   1887 C CD1 . TYR C 1 3   ? -0.20300  2.79800   -21.37300 1.000 13.69630 ? 3   TYR C CD1 1 
ATOM   1888 C CD2 . TYR C 1 3   ? 1.92300   1.90000   -20.74800 1.000 13.61204 ? 3   TYR C CD2 1 
ATOM   1889 C CE1 . TYR C 1 3   ? -0.14600  2.08500   -22.57100 1.000 14.59825 ? 3   TYR C CE1 1 
ATOM   1890 C CE2 . TYR C 1 3   ? 1.99100   1.19900   -21.93100 1.000 15.04982 ? 3   TYR C CE2 1 
ATOM   1891 C CZ  . TYR C 1 3   ? 0.95800   1.29300   -22.83100 1.000 18.63964 ? 3   TYR C CZ  1 
ATOM   1892 O OH  . TYR C 1 3   ? 1.05700   0.57800   -23.99600 1.000 24.79548 ? 3   TYR C OH  1 
ATOM   1893 N N   . MET C 1 4   ? 0.68500   6.89500   -18.16700 1.000 9.58877  ? 4   MET C N   1 
ATOM   1894 C CA  . MET C 1 4   ? 0.30600   7.70000   -17.01300 1.000 8.92114  ? 4   MET C CA  1 
ATOM   1895 C C   . MET C 1 4   ? -1.06900  7.23300   -16.54700 1.000 10.79078 ? 4   MET C C   1 
ATOM   1896 O O   . MET C 1 4   ? -2.02800  7.27500   -17.32500 1.000 11.12607 ? 4   MET C O   1 
ATOM   1897 C CB  . MET C 1 4   ? 0.28100   9.18400   -17.39000 1.000 10.44253 ? 4   MET C CB  1 
ATOM   1898 C CG  . MET C 1 4   ? 1.51700   9.68400   -18.12200 1.000 11.74967 ? 4   MET C CG  1 
ATOM   1899 S SD  . MET C 1 4   ? 3.00000   9.51700   -17.07100 1.000 14.21055 ? 4   MET C SD  1 
ATOM   1900 C CE  . MET C 1 4   ? 2.48100   10.38500  -15.60300 1.000 10.28555 ? 4   MET C CE  1 
ATOM   1901 N N   . VAL C 1 5   ? -1.18600  6.81400   -15.28500 1.000 9.32995  ? 5   VAL C N   1 
ATOM   1902 C CA  . VAL C 1 5   ? -2.42400  6.22800   -14.77100 1.000 8.50890  ? 5   VAL C CA  1 
ATOM   1903 C C   . VAL C 1 5   ? -2.95900  7.12300   -13.66200 1.000 10.06065 ? 5   VAL C C   1 
ATOM   1904 O O   . VAL C 1 5   ? -2.39900  7.17200   -12.55600 1.000 10.29773 ? 5   VAL C O   1 
ATOM   1905 C CB  . VAL C 1 5   ? -2.22600  4.78100   -14.28500 1.000 11.81522 ? 5   VAL C CB  1 
ATOM   1906 C CG1 . VAL C 1 5   ? -3.55900  4.19400   -13.82400 1.000 10.92236 ? 5   VAL C CG1 1 
ATOM   1907 C CG2 . VAL C 1 5   ? -1.63600  3.91800   -15.42900 1.000 9.51828  ? 5   VAL C CG2 1 
ATOM   1908 N N   . TYR C 1 6   ? -4.05600  7.81800   -13.94600 1.000 8.97032  ? 6   TYR C N   1 
ATOM   1909 C CA  . TYR C 1 6   ? -4.63000  8.79200   -13.01900 1.000 10.54133 ? 6   TYR C CA  1 
ATOM   1910 C C   . TYR C 1 6   ? -5.72900  8.12600   -12.19800 1.000 11.43214 ? 6   TYR C C   1 
ATOM   1911 O O   . TYR C 1 6   ? -6.76700  7.73200   -12.73800 1.000 11.40306 ? 6   TYR C O   1 
ATOM   1912 C CB  . TYR C 1 6   ? -5.16600  9.99100   -13.79200 1.000 10.17983 ? 6   TYR C CB  1 
ATOM   1913 C CG  . TYR C 1 6   ? -4.06900  10.64600  -14.58700 1.000 8.20534  ? 6   TYR C CG  1 
ATOM   1914 C CD1 . TYR C 1 6   ? -3.22000  11.57400  -13.99000 1.000 9.97015  ? 6   TYR C CD1 1 
ATOM   1915 C CD2 . TYR C 1 6   ? -3.86600  10.31800  -15.92600 1.000 8.62408  ? 6   TYR C CD2 1 
ATOM   1916 C CE1 . TYR C 1 6   ? -2.19000  12.17700  -14.72400 1.000 9.24172  ? 6   TYR C CE1 1 
ATOM   1917 C CE2 . TYR C 1 6   ? -2.84500  10.91200  -16.66900 1.000 8.31636  ? 6   TYR C CE2 1 
ATOM   1918 C CZ  . TYR C 1 6   ? -2.02200  11.84000  -16.05500 1.000 8.40493  ? 6   TYR C CZ  1 
ATOM   1919 O OH  . TYR C 1 6   ? -1.00600  12.42900  -16.77300 1.000 8.35849  ? 6   TYR C OH  1 
ATOM   1920 N N   . VAL C 1 7   ? -5.49600  8.01300   -10.89200 1.000 11.25304 ? 7   VAL C N   1 
ATOM   1921 C CA  . VAL C 1 7   ? -6.37400  7.29300   -9.97800  1.000 14.33379 ? 7   VAL C CA  1 
ATOM   1922 C C   . VAL C 1 7   ? -6.51100  8.12500   -8.71500  1.000 12.76425 ? 7   VAL C C   1 
ATOM   1923 O O   . VAL C 1 7   ? -5.70800  9.01900   -8.44600  1.000 11.03312 ? 7   VAL C O   1 
ATOM   1924 C CB  . VAL C 1 7   ? -5.83000  5.87800   -9.62800  1.000 15.50722 ? 7   VAL C CB  1 
ATOM   1925 C CG1 . VAL C 1 7   ? -5.86900  4.96100   -10.83600 1.000 17.88735 ? 7   VAL C CG1 1 
ATOM   1926 C CG2 . VAL C 1 7   ? -4.39500  5.96500   -9.08000  1.000 11.68112 ? 7   VAL C CG2 1 
ATOM   1927 N N   . SER C 1 8   ? -7.53900  7.81900   -7.92300  1.000 13.24050 ? 8   SER C N   1 
ATOM   1928 C CA  . SER C 1 8   ? -7.67800  8.47800   -6.62900  1.000 15.19910 ? 8   SER C CA  1 
ATOM   1929 C C   . SER C 1 8   ? -6.75900  7.83200   -5.59500  1.000 16.73904 ? 8   SER C C   1 
ATOM   1930 O O   . SER C 1 8   ? -6.47900  6.63300   -5.64900  1.000 16.63709 ? 8   SER C O   1 
ATOM   1931 C CB  . SER C 1 8   ? -9.12500  8.42800   -6.14500  1.000 17.28539 ? 8   SER C CB  1 
ATOM   1932 O OG  . SER C 1 8   ? -9.96100  9.16500   -7.02300  1.000 20.71890 ? 8   SER C OG  1 
ATOM   1933 N N   . GLN C 1 9   ? -6.27200  8.65400   -4.66200  1.000 15.64056 ? 9   GLN C N   1 
ATOM   1934 C CA  . GLN C 1 9   ? -5.38500  8.18200   -3.60300  1.000 20.30484 ? 9   GLN C CA  1 
ATOM   1935 C C   . GLN C 1 9   ? -6.02000  7.02500   -2.83600  1.000 21.66460 ? 9   GLN C C   1 
ATOM   1936 O O   . GLN C 1 9   ? -7.20100  7.06500   -2.49300  1.000 19.74417 ? 9   GLN C O   1 
ATOM   1937 C CB  . GLN C 1 9   ? -5.06200  9.33400   -2.64600  1.000 18.35615 ? 9   GLN C CB  1 
ATOM   1938 C CG  . GLN C 1 9   ? -4.07400  10.33900  -3.22800  1.000 26.94498 ? 9   GLN C CG  1 
ATOM   1939 C CD  . GLN C 1 9   ? -3.91500  11.59600  -2.37500  1.000 32.05727 ? 9   GLN C CD  1 
ATOM   1940 O OE1 . GLN C 1 9   ? -4.65500  11.81200  -1.40700  1.000 29.47282 ? 9   GLN C OE1 1 
ATOM   1941 N NE2 . GLN C 1 9   ? -2.95200  12.44000  -2.74100  1.000 33.53108 ? 9   GLN C NE2 1 
ATOM   1942 N N   . ASP C 1 10  ? -5.23200  5.97600   -2.60100  1.000 27.31489 ? 10  ASP C N   1 
ATOM   1943 C CA  . ASP C 1 10  ? -5.62100  4.79200   -1.83800  1.000 28.04358 ? 10  ASP C CA  1 
ATOM   1944 C C   . ASP C 1 10  ? -6.71900  3.96800   -2.50600  1.000 26.11402 ? 10  ASP C C   1 
ATOM   1945 O O   . ASP C 1 10  ? -7.19300  3.00900   -1.89800  1.000 29.99610 ? 10  ASP C O   1 
ATOM   1946 C CB  . ASP C 1 10  ? -6.10200  5.12500   -0.41700  1.000 32.47210 ? 10  ASP C CB  1 
ATOM   1947 C CG  . ASP C 1 10  ? -5.06200  5.85800   0.41600   1.000 38.83577 ? 10  ASP C CG  1 
ATOM   1948 O OD1 . ASP C 1 10  ? -3.91200  5.36600   0.51900   1.000 41.74136 ? 10  ASP C OD1 1 
ATOM   1949 O OD2 . ASP C 1 10  ? -5.40600  6.92700   0.98000   1.000 41.07121 ? 10  ASP C OD2 1 
ATOM   1950 N N   . ARG C 1 11  ? -7.17100  4.31800   -3.71500  1.000 22.25701 ? 11  ARG C N   1 
ATOM   1951 C CA  . ARG C 1 11  ? -8.10800  3.44000   -4.41000  1.000 23.83535 ? 11  ARG C CA  1 
ATOM   1952 C C   . ARG C 1 11  ? -7.45100  2.11100   -4.77800  1.000 24.06023 ? 11  ARG C C   1 
ATOM   1953 O O   . ARG C 1 11  ? -8.12100  1.07200   -4.81600  1.000 26.56332 ? 11  ARG C O   1 
ATOM   1954 C CB  . ARG C 1 11  ? -8.65300  4.13300   -5.66500  1.000 25.41223 ? 11  ARG C CB  1 
ATOM   1955 C CG  . ARG C 1 11  ? -9.61800  3.28700   -6.48400  1.000 27.24023 ? 11  ARG C CG  1 
ATOM   1956 C CD  . ARG C 1 11  ? -10.84400 2.92400   -5.65300  1.000 30.84559 ? 11  ARG C CD  1 
ATOM   1957 N NE  . ARG C 1 11  ? -11.76700 2.04300   -6.36200  1.000 34.39288 ? 11  ARG C NE  1 
ATOM   1958 C CZ  . ARG C 1 11  ? -11.64500 0.72300   -6.41300  1.000 38.54731 ? 11  ARG C CZ  1 
ATOM   1959 N NH1 . ARG C 1 11  ? -10.60100 0.10400   -5.88700  1.000 29.96998 ? 11  ARG C NH1 1 
ATOM   1960 N NH2 . ARG C 1 11  ? -12.60000 0.00400   -7.00000  1.000 43.37460 ? 11  ARG C NH2 1 
ATOM   1961 N N   . LEU C 1 12  ? -6.15200  2.12200   -5.05900  1.000 22.25127 ? 12  LEU C N   1 
ATOM   1962 C CA  . LEU C 1 12  ? -5.41400  0.91700   -5.42600  1.000 23.72187 ? 12  LEU C CA  1 
ATOM   1963 C C   . LEU C 1 12  ? -4.39000  0.61500   -4.33900  1.000 22.41231 ? 12  LEU C C   1 
ATOM   1964 O O   . LEU C 1 12  ? -3.53800  1.45500   -4.02800  1.000 23.30325 ? 12  LEU C O   1 
ATOM   1965 C CB  . LEU C 1 12  ? -4.72400  1.07700   -6.78100  1.000 20.93165 ? 12  LEU C CB  1 
ATOM   1966 C CG  . LEU C 1 12  ? -5.53400  1.37700   -8.04700  1.000 17.38047 ? 12  LEU C CG  1 
ATOM   1967 C CD1 . LEU C 1 12  ? -4.56800  1.58400   -9.21900  1.000 17.82831 ? 12  LEU C CD1 1 
ATOM   1968 C CD2 . LEU C 1 12  ? -6.53000  0.28200   -8.38600  1.000 23.09453 ? 12  LEU C CD2 1 
ATOM   1969 N N   . THR C 1 13  ? -4.48200  -0.58000  -3.75600  1.000 28.05282 ? 13  THR C N   1 
ATOM   1970 C CA  . THR C 1 13  ? -3.46800  -1.03000  -2.81700  1.000 23.59847 ? 13  THR C CA  1 
ATOM   1971 C C   . THR C 1 13  ? -2.16900  -1.30500  -3.56100  1.000 25.55610 ? 13  THR C C   1 
ATOM   1972 O O   . THR C 1 13  ? -2.17600  -1.45500  -4.78500  1.000 22.49922 ? 13  THR C O   1 
ATOM   1973 C CB  . THR C 1 13  ? -3.93400  -2.29800  -2.11200  1.000 27.97149 ? 13  THR C CB  1 
ATOM   1974 O OG1 . THR C 1 13  ? -4.41100  -3.22400  -3.09300  1.000 24.44660 ? 13  THR C OG1 1 
ATOM   1975 C CG2 . THR C 1 13  ? -5.04400  -1.97600  -1.14600  1.000 28.98887 ? 13  THR C CG2 1 
ATOM   1976 N N   . PRO C 1 14  ? -1.03700  -1.38000  -2.84700  1.000 26.08147 ? 14  PRO C N   1 
ATOM   1977 C CA  . PRO C 1 14  ? 0.21600   -1.78600  -3.51100  1.000 23.55824 ? 14  PRO C CA  1 
ATOM   1978 C C   . PRO C 1 14  ? 0.07800   -3.01800  -4.39500  1.000 24.68810 ? 14  PRO C C   1 
ATOM   1979 O O   . PRO C 1 14  ? 0.65300   -3.04700  -5.49500  1.000 23.29548 ? 14  PRO C O   1 
ATOM   1980 C CB  . PRO C 1 14  ? 1.16000   -2.04000  -2.33000  1.000 29.31235 ? 14  PRO C CB  1 
ATOM   1981 C CG  . PRO C 1 14  ? 0.68100   -1.09900  -1.29700  1.000 25.86553 ? 14  PRO C CG  1 
ATOM   1982 C CD  . PRO C 1 14  ? -0.81300  -1.04800  -1.42800  1.000 29.91364 ? 14  PRO C CD  1 
ATOM   1983 N N   . SER C 1 15  ? -0.68100  -4.03100  -3.96500  1.000 24.35654 ? 15  SER C N   1 
ATOM   1984 C CA  . SER C 1 15  ? -0.82900  -5.21500  -4.80400  1.000 22.27278 ? 15  SER C CA  1 
ATOM   1985 C C   . SER C 1 15  ? -1.74700  -4.94300  -5.99000  1.000 23.57252 ? 15  SER C C   1 
ATOM   1986 O O   . SER C 1 15  ? -1.54600  -5.51600  -7.06800  1.000 19.40735 ? 15  SER C O   1 
ATOM   1987 C CB  . SER C 1 15  ? -1.34000  -6.40200  -3.97500  1.000 35.30238 ? 15  SER C CB  1 
ATOM   1988 O OG  . SER C 1 15  ? -2.74800  -6.37500  -3.81500  1.000 37.92878 ? 15  SER C OG  1 
ATOM   1989 N N   . ALA C 1 16  ? -2.74800  -4.07200  -5.82200  1.000 20.75384 ? 16  ALA C N   1 
ATOM   1990 C CA  . ALA C 1 16  ? -3.58000  -3.68500  -6.95800  1.000 21.58917 ? 16  ALA C CA  1 
ATOM   1991 C C   . ALA C 1 16  ? -2.79300  -2.84000  -7.95900  1.000 22.86530 ? 16  ALA C C   1 
ATOM   1992 O O   . ALA C 1 16  ? -2.99000  -2.97500  -9.17300  1.000 18.89888 ? 16  ALA C O   1 
ATOM   1993 C CB  . ALA C 1 16  ? -4.81900  -2.93100  -6.47800  1.000 24.41922 ? 16  ALA C CB  1 
ATOM   1994 N N   . LYS C 1 17  ? -1.92000  -1.94400  -7.47200  1.000 16.81299 ? 17  LYS C N   1 
ATOM   1995 C CA  . LYS C 1 17  ? -1.04900  -1.19600  -8.37700  1.000 17.35415 ? 17  LYS C CA  1 
ATOM   1996 C C   . LYS C 1 17  ? -0.15100  -2.13400  -9.15700  1.000 18.76093 ? 17  LYS C C   1 
ATOM   1997 O O   . LYS C 1 17  ? 0.02300   -1.97300  -10.37400 1.000 16.34499 ? 17  LYS C O   1 
ATOM   1998 C CB  . LYS C 1 17  ? -0.19300  -0.18500  -7.61100  1.000 17.73316 ? 17  LYS C CB  1 
ATOM   1999 C CG  . LYS C 1 17  ? -0.99300  0.96200   -7.04100  1.000 18.91698 ? 17  LYS C CG  1 
ATOM   2000 C CD  . LYS C 1 17  ? -0.10900  1.96500   -6.30600  1.000 21.59694 ? 17  LYS C CD  1 
ATOM   2001 C CE  . LYS C 1 17  ? -0.97300  3.04400   -5.66400  1.000 22.66117 ? 17  LYS C CE  1 
ATOM   2002 N NZ  . LYS C 1 17  ? -0.18500  3.94400   -4.78800  1.000 25.59196 ? 17  LYS C NZ  1 
ATOM   2003 N N   . HIS C 1 18  ? 0.44200   -3.11500  -8.47000  1.000 18.11475 ? 18  HIS C N   1 
ATOM   2004 C CA  . HIS C 1 18  ? 1.30000   -4.06200  -9.16800  1.000 18.32250 ? 18  HIS C CA  1 
ATOM   2005 C C   . HIS C 1 18  ? 0.51200   -4.84600  -10.21000 1.000 17.15246 ? 18  HIS C C   1 
ATOM   2006 O O   . HIS C 1 18  ? 0.98100   -5.03500  -11.34200 1.000 18.59380 ? 18  HIS C O   1 
ATOM   2007 C CB  . HIS C 1 18  ? 1.97300   -5.02100  -8.18300  1.000 19.35104 ? 18  HIS C CB  1 
ATOM   2008 C CG  . HIS C 1 18  ? 2.75000   -6.09500  -8.86700  1.000 24.96784 ? 18  HIS C CG  1 
ATOM   2009 N ND1 . HIS C 1 18  ? 2.21900   -7.33900  -9.13900  1.000 37.02937 ? 18  HIS C ND1 1 
ATOM   2010 C CD2 . HIS C 1 18  ? 3.98700   -6.08300  -9.41900  1.000 32.08538 ? 18  HIS C CD2 1 
ATOM   2011 C CE1 . HIS C 1 18  ? 3.11300   -8.06200  -9.79300  1.000 41.17067 ? 18  HIS C CE1 1 
ATOM   2012 N NE2 . HIS C 1 18  ? 4.19500   -7.32200  -9.97600  1.000 33.42215 ? 18  HIS C NE2 1 
ATOM   2013 N N   . ALA C 1 19  ? -0.69100  -5.29700  -9.84900  1.000 16.34012 ? 19  ALA C N   1 
ATOM   2014 C CA  . ALA C 1 19  ? -1.53700  -6.01600  -10.79700 1.000 19.34532 ? 19  ALA C CA  1 
ATOM   2015 C C   . ALA C 1 19  ? -1.87800  -5.14700  -12.00500 1.000 18.61114 ? 19  ALA C C   1 
ATOM   2016 O O   . ALA C 1 19  ? -1.81500  -5.61400  -13.14800 1.000 17.19873 ? 19  ALA C O   1 
ATOM   2017 C CB  . ALA C 1 19  ? -2.80900  -6.49400  -10.10000 1.000 16.87822 ? 19  ALA C CB  1 
ATOM   2018 N N   . VAL C 1 20  ? -2.24100  -3.88000  -11.77000 1.000 17.55806 ? 20  VAL C N   1 
ATOM   2019 C CA  . VAL C 1 20  ? -2.57500  -2.97900  -12.87700 1.000 16.28576 ? 20  VAL C CA  1 
ATOM   2020 C C   . VAL C 1 20  ? -1.36200  -2.75100  -13.76400 1.000 14.90776 ? 20  VAL C C   1 
ATOM   2021 O O   . VAL C 1 20  ? -1.45900  -2.79400  -15.00000 1.000 15.43944 ? 20  VAL C O   1 
ATOM   2022 C CB  . VAL C 1 20  ? -3.13900  -1.64800  -12.34000 1.000 17.61173 ? 20  VAL C CB  1 
ATOM   2023 C CG1 . VAL C 1 20  ? -3.18600  -0.58700  -13.45600 1.000 14.51867 ? 20  VAL C CG1 1 
ATOM   2024 C CG2 . VAL C 1 20  ? -4.53800  -1.86400  -11.73700 1.000 16.50859 ? 20  VAL C CG2 1 
ATOM   2025 N N   . ALA C 1 21  ? -0.20200  -2.49400  -13.15800 1.000 14.96542 ? 21  ALA C N   1 
ATOM   2026 C CA  . ALA C 1 21  ? 1.00100   -2.25400  -13.95100 1.000 16.05918 ? 21  ALA C CA  1 
ATOM   2027 C C   . ALA C 1 21  ? 1.37600   -3.48400  -14.76400 1.000 17.18647 ? 21  ALA C C   1 
ATOM   2028 O O   . ALA C 1 21  ? 1.76300   -3.36800  -15.93300 1.000 16.76065 ? 21  ALA C O   1 
ATOM   2029 C CB  . ALA C 1 21  ? 2.16400   -1.83900  -13.04300 1.000 17.27287 ? 21  ALA C CB  1 
ATOM   2030 N N   . LYS C 1 22  ? 1.28100   -4.67400  -14.15700 1.000 16.12778 ? 22  LYS C N   1 
ATOM   2031 C CA  . LYS C 1 22  ? 1.55700   -5.90300  -14.89400 1.000 15.90418 ? 22  LYS C CA  1 
ATOM   2032 C C   . LYS C 1 22  ? 0.56300   -6.09200  -16.03200 1.000 18.33387 ? 22  LYS C C   1 
ATOM   2033 O O   . LYS C 1 22  ? 0.94200   -6.50400  -17.13600 1.000 22.08648 ? 22  LYS C O   1 
ATOM   2034 C CB  . LYS C 1 22  ? 1.52800   -7.09900  -13.93600 1.000 21.88994 ? 22  LYS C CB  1 
ATOM   2035 C CG  . LYS C 1 22  ? 1.67700   -8.46600  -14.60000 1.000 27.64555 ? 22  LYS C CG  1 
ATOM   2036 C CD  . LYS C 1 22  ? 1.98700   -9.56100  -13.56300 1.000 32.84319 ? 22  LYS C CD  1 
ATOM   2037 C CE  . LYS C 1 22  ? 1.67800   -10.96200 -14.10500 1.000 36.85641 ? 22  LYS C CE  1 
ATOM   2038 N NZ  . LYS C 1 22  ? 2.41000   -11.27100 -15.36400 1.000 33.20947 ? 22  LYS C NZ  1 
ATOM   2039 N N   . ALA C 1 23  ? -0.71400  -5.79800  -15.78600 1.000 18.93096 ? 23  ALA C N   1 
ATOM   2040 C CA  . ALA C 1 23  ? -1.72500  -5.97800  -16.82600 1.000 18.67360 ? 23  ALA C CA  1 
ATOM   2041 C C   . ALA C 1 23  ? -1.47600  -5.04700  -18.00800 1.000 17.44678 ? 23  ALA C C   1 
ATOM   2042 O O   . ALA C 1 23  ? -1.62200  -5.45500  -19.16300 1.000 18.52773 ? 23  ALA C O   1 
ATOM   2043 C CB  . ALA C 1 23  ? -3.12200  -5.75200  -16.24800 1.000 18.97594 ? 23  ALA C CB  1 
ATOM   2044 N N   . ILE C 1 24  ? -1.09800  -3.79600  -17.74100 1.000 16.12709 ? 24  ILE C N   1 
ATOM   2045 C CA  . ILE C 1 24  ? -0.79200  -2.86800  -18.82800 1.000 15.98601 ? 24  ILE C CA  1 
ATOM   2046 C C   . ILE C 1 24  ? 0.47900   -3.29600  -19.54600 1.000 19.13394 ? 24  ILE C C   1 
ATOM   2047 O O   . ILE C 1 24  ? 0.55500   -3.26100  -20.78100 1.000 16.31007 ? 24  ILE C O   1 
ATOM   2048 C CB  . ILE C 1 24  ? -0.67100  -1.43400  -18.28400 1.000 14.79094 ? 24  ILE C CB  1 
ATOM   2049 C CG1 . ILE C 1 24  ? -2.02300  -0.92700  -17.79900 1.000 14.21041 ? 24  ILE C CG1 1 
ATOM   2050 C CG2 . ILE C 1 24  ? -0.10700  -0.50200  -19.35100 1.000 14.76968 ? 24  ILE C CG2 1 
ATOM   2051 C CD1 . ILE C 1 24  ? -1.93000  0.38800   -17.02300 1.000 15.79008 ? 24  ILE C CD1 1 
ATOM   2052 N N   . THR C 1 25  ? 1.50400   -3.69200  -18.77900 1.000 16.11266 ? 25  THR C N   1 
ATOM   2053 C CA  . THR C 1 25  ? 2.77300   -4.11100  -19.36100 1.000 17.75213 ? 25  THR C CA  1 
ATOM   2054 C C   . THR C 1 25  ? 2.59000   -5.33600  -20.24700 1.000 19.79905 ? 25  THR C C   1 
ATOM   2055 O O   . THR C 1 25  ? 3.15000   -5.40800  -21.35000 1.000 22.41090 ? 25  THR C O   1 
ATOM   2056 C CB  . THR C 1 25  ? 3.78000   -4.40200  -18.24300 1.000 23.32780 ? 25  THR C CB  1 
ATOM   2057 O OG1 . THR C 1 25  ? 3.97900   -3.22200  -17.45000 1.000 24.39181 ? 25  THR C OG1 1 
ATOM   2058 C CG2 . THR C 1 25  ? 5.11700   -4.85600  -18.81700 1.000 23.65120 ? 25  THR C CG2 1 
ATOM   2059 N N   . ASP C 1 26  ? 1.80800   -6.31100  -19.77200 1.000 20.43275 ? 26  ASP C N   1 
ATOM   2060 C CA  . ASP C 1 26  ? 1.59700   -7.54400  -20.51900 1.000 19.77985 ? 26  ASP C CA  1 
ATOM   2061 C C   . ASP C 1 26  ? 0.73300   -7.32000  -21.75000 1.000 25.67923 ? 26  ASP C C   1 
ATOM   2062 O O   . ASP C 1 26  ? 0.89900   -8.02500  -22.75100 1.000 27.24991 ? 26  ASP C O   1 
ATOM   2063 C CB  . ASP C 1 26  ? 0.94300   -8.59700  -19.63800 1.000 22.56202 ? 26  ASP C CB  1 
ATOM   2064 C CG  . ASP C 1 26  ? 1.87800   -9.14100  -18.56600 1.000 29.09075 ? 26  ASP C CG  1 
ATOM   2065 O OD1 . ASP C 1 26  ? 3.11300   -8.97300  -18.67900 1.000 30.61501 ? 26  ASP C OD1 1 
ATOM   2066 O OD2 . ASP C 1 26  ? 1.35300   -9.75400  -17.61400 1.000 29.51060 ? 26  ASP C OD2 1 
ATOM   2067 N N   . ALA C 1 27  ? -0.22900  -6.39500  -21.67700 1.000 20.29468 ? 27  ALA C N   1 
ATOM   2068 C CA  . ALA C 1 27  ? -0.98200  -6.02100  -22.86800 1.000 23.11463 ? 27  ALA C CA  1 
ATOM   2069 C C   . ALA C 1 27  ? -0.05000  -5.44100  -23.92000 1.000 31.65488 ? 27  ALA C C   1 
ATOM   2070 O O   . ALA C 1 27  ? -0.09400  -5.82900  -25.09000 1.000 32.85227 ? 27  ALA C O   1 
ATOM   2071 C CB  . ALA C 1 27  ? -2.07500  -5.01300  -22.50300 1.000 22.55978 ? 27  ALA C CB  1 
ATOM   2072 N N   . ALA C 1 28  ? 0.82200   -4.51800  -23.49800 1.000 31.00957 ? 28  ALA C N   1 
ATOM   2073 C CA  . ALA C 1 28  ? 1.75500   -3.80500  -24.35500 1.000 34.97033 ? 28  ALA C CA  1 
ATOM   2074 C C   . ALA C 1 28  ? 2.88300   -4.68600  -24.87700 1.000 41.16255 ? 28  ALA C C   1 
ATOM   2075 O O   . ALA C 1 28  ? 3.59300   -4.25800  -25.79300 1.000 46.39832 ? 28  ALA C O   1 
ATOM   2076 C CB  . ALA C 1 28  ? 2.34300   -2.61100  -23.60000 1.000 27.57889 ? 28  ALA C CB  1 
ATOM   2077 N N   . ARG C 1 29  ? 3.05700   -5.90300  -24.35500 1.000 36.57018 ? 29  ARG C N   1 
ATOM   2078 C CA  . ARG C 1 29  ? 4.02200   -6.82100  -24.95700 1.000 42.51245 ? 29  ARG C CA  1 
ATOM   2079 C C   . ARG C 1 29  ? 3.36700   -7.91700  -25.79500 1.000 41.37710 ? 29  ARG C C   1 
ATOM   2080 O O   . ARG C 1 29  ? 3.91000   -8.28500  -26.84100 1.000 46.68861 ? 29  ARG C O   1 
ATOM   2081 C CB  . ARG C 1 29  ? 4.92100   -7.45100  -23.88200 1.000 45.60432 ? 29  ARG C CB  1 
ATOM   2082 C CG  . ARG C 1 29  ? 4.26100   -8.47600  -22.96400 1.000 40.80690 ? 29  ARG C CG  1 
ATOM   2083 C CD  . ARG C 1 29  ? 5.04600   -8.61300  -21.65500 1.000 47.45444 ? 29  ARG C CD  1 
ATOM   2084 N NE  . ARG C 1 29  ? 4.95100   -9.94800  -21.07000 1.000 53.55326 ? 29  ARG C NE  1 
ATOM   2085 C CZ  . ARG C 1 29  ? 5.81700   -10.92700 -21.30400 1.000 49.21532 ? 29  ARG C CZ  1 
ATOM   2086 N NH1 . ARG C 1 29  ? 6.84500   -10.75900 -22.11800 1.000 47.24882 ? 29  ARG C NH1 1 
ATOM   2087 N NH2 . ARG C 1 29  ? 5.64900   -12.10200 -20.70500 1.000 50.58561 ? 29  ARG C NH2 1 
ATOM   2088 N N   . GLY C 1 30  ? 2.19900   -8.42300  -25.38400 1.000 35.69960 ? 30  GLY C N   1 
ATOM   2089 C CA  . GLY C 1 30  ? 1.58600   -9.52600  -26.11000 1.000 40.37627 ? 30  GLY C CA  1 
ATOM   2090 C C   . GLY C 1 30  ? 1.20900   -9.16400  -27.53600 1.000 52.76515 ? 30  GLY C C   1 
ATOM   2091 O O   . GLY C 1 30  ? 1.32400   -9.99000  -28.44600 1.000 57.93911 ? 30  GLY C O   1 
ATOM   2092 N N   . LEU C 1 31  ? 0.77900   -7.91800  -27.75500 1.000 45.92802 ? 31  LEU C N   1 
ATOM   2093 C CA  . LEU C 1 31  ? 0.24000   -7.49800  -29.04600 1.000 50.34034 ? 31  LEU C CA  1 
ATOM   2094 C C   . LEU C 1 31  ? 1.27100   -6.86900  -29.97400 1.000 49.93603 ? 31  LEU C C   1 
ATOM   2095 O O   . LEU C 1 31  ? 1.14200   -6.99700  -31.19700 1.000 52.96591 ? 31  LEU C O   1 
ATOM   2096 C CB  . LEU C 1 31  ? -0.90600  -6.50700  -28.83500 1.000 45.41700 ? 31  LEU C CB  1 
ATOM   2097 C CG  . LEU C 1 31  ? -2.21000  -7.15600  -28.39400 1.000 49.20466 ? 31  LEU C CG  1 
ATOM   2098 C CD1 . LEU C 1 31  ? -3.24000  -6.09600  -28.06900 1.000 34.69389 ? 31  LEU C CD1 1 
ATOM   2099 C CD2 . LEU C 1 31  ? -2.70600  -8.09400  -29.48900 1.000 41.27856 ? 31  LEU C CD2 1 
ATOM   2100 N N   . THR C 1 32  ? 2.28200   -6.18600  -29.43500 1.000 48.99948 ? 32  THR C N   1 
ATOM   2101 C CA  . THR C 1 32  ? 3.26700   -5.47600  -30.24500 1.000 54.07168 ? 32  THR C CA  1 
ATOM   2102 C C   . THR C 1 32  ? 4.64500   -6.11400  -30.23500 1.000 57.99028 ? 32  THR C C   1 
ATOM   2103 O O   . THR C 1 32  ? 5.40300   -5.92900  -31.19000 1.000 59.62200 ? 32  THR C O   1 
ATOM   2104 C CB  . THR C 1 32  ? 3.42200   -4.02400  -29.76600 1.000 55.46347 ? 32  THR C CB  1 
ATOM   2105 O OG1 . THR C 1 32  ? 4.36700   -3.97800  -28.68900 1.000 55.82157 ? 32  THR C OG1 1 
ATOM   2106 C CG2 . THR C 1 32  ? 2.09400   -3.45400  -29.28200 1.000 49.62626 ? 32  THR C CG2 1 
ATOM   2107 N N   . GLY C 1 33  ? 4.99200   -6.84400  -29.17900 1.000 56.79638 ? 33  GLY C N   1 
ATOM   2108 C CA  . GLY C 1 33  ? 6.34500   -7.32300  -28.99600 1.000 56.52023 ? 33  GLY C CA  1 
ATOM   2109 C C   . GLY C 1 33  ? 7.26200   -6.36600  -28.26900 1.000 55.68537 ? 33  GLY C C   1 
ATOM   2110 O O   . GLY C 1 33  ? 8.47400   -6.61100  -28.22200 1.000 55.33802 ? 33  GLY C O   1 
ATOM   2111 N N   . THR C 1 34  ? 6.72900   -5.27600  -27.71900 1.000 55.71091 ? 34  THR C N   1 
ATOM   2112 C CA  . THR C 1 34  ? 7.53600   -4.35000  -26.93200 1.000 58.99820 ? 34  THR C CA  1 
ATOM   2113 C C   . THR C 1 34  ? 8.06400   -5.05600  -25.69100 1.000 55.97908 ? 34  THR C C   1 
ATOM   2114 O O   . THR C 1 34  ? 7.28200   -5.53400  -24.86200 1.000 53.59300 ? 34  THR C O   1 
ATOM   2115 C CB  . THR C 1 34  ? 6.70700   -3.12400  -26.54200 1.000 58.30772 ? 34  THR C CB  1 
ATOM   2116 O OG1 . THR C 1 34  ? 6.44000   -2.32900  -27.70900 1.000 55.87871 ? 34  THR C OG1 1 
ATOM   2117 C CG2 . THR C 1 34  ? 7.44400   -2.28400  -25.49400 1.000 50.18296 ? 34  THR C CG2 1 
ATOM   2118 N N   . GLN C 1 35  ? 9.39200   -5.12600  -25.57300 1.000 52.67552 ? 35  GLN C N   1 
ATOM   2119 C CA  . GLN C 1 35  ? 10.02100  -5.89300  -24.50400 1.000 55.82774 ? 35  GLN C CA  1 
ATOM   2120 C C   . GLN C 1 35  ? 9.52200   -5.43400  -23.13700 1.000 56.00008 ? 35  GLN C C   1 
ATOM   2121 O O   . GLN C 1 35  ? 9.07600   -4.29400  -22.96100 1.000 55.27118 ? 35  GLN C O   1 
ATOM   2122 C CB  . GLN C 1 35  ? 11.54700  -5.75700  -24.57500 1.000 55.11838 ? 35  GLN C CB  1 
ATOM   2123 C CG  . GLN C 1 35  ? 12.16500  -6.14400  -25.91600 1.000 59.77279 ? 35  GLN C CG  1 
ATOM   2124 C CD  . GLN C 1 35  ? 13.09900  -5.06200  -26.45600 1.000 69.60078 ? 35  GLN C CD  1 
ATOM   2125 O OE1 . GLN C 1 35  ? 12.67600  -3.93100  -26.71500 1.000 67.77267 ? 35  GLN C OE1 1 
ATOM   2126 N NE2 . GLN C 1 35  ? 14.37800  -5.40300  -26.61200 1.000 66.61322 ? 35  GLN C NE2 1 
ATOM   2127 N N   . HIS C 1 36  ? 9.60300   -6.34300  -22.16200 1.000 50.38203 ? 36  HIS C N   1 
ATOM   2128 C CA  . HIS C 1 36  ? 9.10600   -6.06700  -20.81500 1.000 52.89394 ? 36  HIS C CA  1 
ATOM   2129 C C   . HIS C 1 36  ? 9.68300   -4.76700  -20.25900 1.000 53.04602 ? 36  HIS C C   1 
ATOM   2130 O O   . HIS C 1 36  ? 8.93800   -3.85000  -19.88400 1.000 48.68828 ? 36  HIS C O   1 
ATOM   2131 C CB  . HIS C 1 36  ? 9.44700   -7.24000  -19.88900 1.000 49.11324 ? 36  HIS C CB  1 
ATOM   2132 C CG  . HIS C 1 36  ? 8.28200   -7.74600  -19.09900 1.000 49.60514 ? 36  HIS C CG  1 
ATOM   2133 N ND1 . HIS C 1 36  ? 7.67400   -7.00400  -18.11000 1.000 46.84357 ? 36  HIS C ND1 1 
ATOM   2134 C CD2 . HIS C 1 36  ? 7.61300   -8.92200  -19.15000 1.000 51.74504 ? 36  HIS C CD2 1 
ATOM   2135 C CE1 . HIS C 1 36  ? 6.67900   -7.69700  -17.58500 1.000 47.15501 ? 36  HIS C CE1 1 
ATOM   2136 N NE2 . HIS C 1 36  ? 6.62000   -8.86500  -18.19900 1.000 56.04943 ? 36  HIS C NE2 1 
ATOM   2137 N N   . PHE C 1 37  ? 11.01700  -4.65700  -20.23000 1.000 49.25709 ? 37  PHE C N   1 
ATOM   2138 C CA  . PHE C 1 37  ? 11.70500  -3.53800  -19.59000 1.000 50.70615 ? 37  PHE C CA  1 
ATOM   2139 C C   . PHE C 1 37  ? 11.42200  -2.18600  -20.25000 1.000 49.91001 ? 37  PHE C C   1 
ATOM   2140 O O   . PHE C 1 37  ? 11.88200  -1.16100  -19.73800 1.000 48.00891 ? 37  PHE C O   1 
ATOM   2141 C CB  . PHE C 1 37  ? 13.21900  -3.80900  -19.55700 1.000 53.34146 ? 37  PHE C CB  1 
ATOM   2142 C CG  . PHE C 1 37  ? 13.88600  -3.75000  -20.91200 1.000 54.92010 ? 37  PHE C CG  1 
ATOM   2143 C CD1 . PHE C 1 37  ? 13.87200  -4.85000  -21.75900 1.000 55.34916 ? 37  PHE C CD1 1 
ATOM   2144 C CD2 . PHE C 1 37  ? 14.53800  -2.59800  -21.33300 1.000 56.71542 ? 37  PHE C CD2 1 
ATOM   2145 C CE1 . PHE C 1 37  ? 14.48100  -4.79700  -23.00500 1.000 54.07822 ? 37  PHE C CE1 1 
ATOM   2146 C CE2 . PHE C 1 37  ? 15.14500  -2.53900  -22.57700 1.000 57.91808 ? 37  PHE C CE2 1 
ATOM   2147 C CZ  . PHE C 1 37  ? 15.11500  -3.63800  -23.41300 1.000 57.31162 ? 37  PHE C CZ  1 
ATOM   2148 N N   . LEU C 1 38  ? 10.67600  -2.13000  -21.34900 1.000 50.96816 ? 38  LEU C N   1 
ATOM   2149 C CA  . LEU C 1 38  ? 10.42600  -0.85300  -22.00400 1.000 50.62505 ? 38  LEU C CA  1 
ATOM   2150 C C   . LEU C 1 38  ? 9.15800   -0.15500  -21.52700 1.000 45.27115 ? 38  LEU C C   1 
ATOM   2151 O O   . LEU C 1 38  ? 8.93400   1.00300   -21.91100 1.000 41.72532 ? 38  LEU C O   1 
ATOM   2152 C CB  . LEU C 1 38  ? 10.34500  -1.03500  -23.52500 1.000 46.16009 ? 38  LEU C CB  1 
ATOM   2153 C CG  . LEU C 1 38  ? 11.67800  -1.06400  -24.27500 1.000 54.43699 ? 38  LEU C CG  1 
ATOM   2154 C CD1 . LEU C 1 38  ? 11.47100  -0.75700  -25.76000 1.000 55.68364 ? 38  LEU C CD1 1 
ATOM   2155 C CD2 . LEU C 1 38  ? 12.67500  -0.09200  -23.64800 1.000 50.19983 ? 38  LEU C CD2 1 
ATOM   2156 N N   . ALA C 1 39  ? 8.31400   -0.82400  -20.73100 1.000 29.44120 ? 39  ALA C N   1 
ATOM   2157 C CA  . ALA C 1 39  ? 6.98700   -0.31100  -20.40200 1.000 24.40877 ? 39  ALA C CA  1 
ATOM   2158 C C   . ALA C 1 39  ? 7.03600   0.34600   -19.02700 1.000 19.27088 ? 39  ALA C C   1 
ATOM   2159 O O   . ALA C 1 39  ? 7.27000   -0.32600  -18.01600 1.000 18.58389 ? 39  ALA C O   1 
ATOM   2160 C CB  . ALA C 1 39  ? 5.93900   -1.41900  -20.44300 1.000 28.67438 ? 39  ALA C CB  1 
ATOM   2161 N N   . GLN C 1 40  ? 6.82600   1.66000   -18.99500 1.000 13.51143 ? 40  GLN C N   1 
ATOM   2162 C CA  . GLN C 1 40  ? 6.74000   2.40500   -17.74600 1.000 14.61334 ? 40  GLN C CA  1 
ATOM   2163 C C   . GLN C 1 40  ? 5.27200   2.65000   -17.42300 1.000 14.39722 ? 40  GLN C C   1 
ATOM   2164 O O   . GLN C 1 40  ? 4.52100   3.15000   -18.26900 1.000 12.99831 ? 40  GLN C O   1 
ATOM   2165 C CB  . GLN C 1 40  ? 7.48700   3.74600   -17.83100 1.000 12.54516 ? 40  GLN C CB  1 
ATOM   2166 C CG  . GLN C 1 40  ? 7.23400   4.60400   -16.55900 1.000 13.24825 ? 40  GLN C CG  1 
ATOM   2167 C CD  . GLN C 1 40  ? 8.07100   5.87600   -16.43400 1.000 15.73980 ? 40  GLN C CD  1 
ATOM   2168 O OE1 . GLN C 1 40  ? 7.72100   6.74700   -15.64900 1.000 15.01759 ? 40  GLN C OE1 1 
ATOM   2169 N NE2 . GLN C 1 40  ? 9.18100   5.97200   -17.16600 1.000 14.08457 ? 40  GLN C NE2 1 
ATOM   2170 N N   . VAL C 1 41  ? 4.86200   2.28600   -16.21400 1.000 10.83224 ? 41  VAL C N   1 
ATOM   2171 C CA  . VAL C 1 41  ? 3.54800   2.63700   -15.68900 1.000 10.24928 ? 41  VAL C CA  1 
ATOM   2172 C C   . VAL C 1 41  ? 3.76700   3.58500   -14.51900 1.000 12.57685 ? 41  VAL C C   1 
ATOM   2173 O O   . VAL C 1 41  ? 4.46600   3.25400   -13.55200 1.000 14.04895 ? 41  VAL C O   1 
ATOM   2174 C CB  . VAL C 1 41  ? 2.75400   1.39200   -15.26700 1.000 12.26423 ? 41  VAL C CB  1 
ATOM   2175 C CG1 . VAL C 1 41  ? 1.42700   1.79400   -14.63000 1.000 11.22057 ? 41  VAL C CG1 1 
ATOM   2176 C CG2 . VAL C 1 41  ? 2.52100   0.49300   -16.47700 1.000 14.35743 ? 41  VAL C CG2 1 
ATOM   2177 N N   . ASN C 1 42  ? 3.16700   4.76400   -14.60100 1.000 11.43290 ? 42  ASN C N   1 
ATOM   2178 C CA  . ASN C 1 42  ? 3.46300   5.85200   -13.68000 1.000 12.94792 ? 42  ASN C CA  1 
ATOM   2179 C C   . ASN C 1 42  ? 2.13000   6.26900   -13.04800 1.000 10.10233 ? 42  ASN C C   1 
ATOM   2180 O O   . ASN C 1 42  ? 1.28700   6.89100   -13.70800 1.000 10.20359 ? 42  ASN C O   1 
ATOM   2181 C CB  . ASN C 1 42  ? 4.16400   6.97400   -14.45700 1.000 12.71857 ? 42  ASN C CB  1 
ATOM   2182 C CG  . ASN C 1 42  ? 4.85700   7.98500   -13.55100 1.000 16.30439 ? 42  ASN C CG  1 
ATOM   2183 O OD1 . ASN C 1 42  ? 4.27900   8.42600   -12.57100 1.000 17.29647 ? 42  ASN C OD1 1 
ATOM   2184 N ND2 . ASN C 1 42  ? 6.11200   8.32400   -13.86200 1.000 12.75189 ? 42  ASN C ND2 1 
ATOM   2185 N N   . PHE C 1 43  ? 1.90700   5.88400   -11.79000 1.000 9.87195  ? 43  PHE C N   1 
ATOM   2186 C CA  . PHE C 1 43  ? 0.63400   6.16600   -11.14100 1.000 11.26091 ? 43  PHE C CA  1 
ATOM   2187 C C   . PHE C 1 43  ? 0.63500   7.58700   -10.59900 1.000 11.34905 ? 43  PHE C C   1 
ATOM   2188 O O   . PHE C 1 43  ? 1.53200   7.97500   -9.84900  1.000 10.35740 ? 43  PHE C O   1 
ATOM   2189 C CB  . PHE C 1 43  ? 0.34700   5.18400   -10.00700 1.000 10.60791 ? 43  PHE C CB  1 
ATOM   2190 C CG  . PHE C 1 43  ? 0.03000   3.80100   -10.47600 1.000 11.22194 ? 43  PHE C CG  1 
ATOM   2191 C CD1 . PHE C 1 43  ? -1.24800  3.48000   -10.90300 1.000 12.17463 ? 43  PHE C CD1 1 
ATOM   2192 C CD2 . PHE C 1 43  ? 1.01200   2.82100   -10.50100 1.000 13.72353 ? 43  PHE C CD2 1 
ATOM   2193 C CE1 . PHE C 1 43  ? -1.55700  2.18800   -11.34700 1.000 14.01439 ? 43  PHE C CE1 1 
ATOM   2194 C CE2 . PHE C 1 43  ? 0.71200   1.52500   -10.94900 1.000 14.65167 ? 43  PHE C CE2 1 
ATOM   2195 C CZ  . PHE C 1 43  ? -0.57200  1.21400   -11.37100 1.000 11.11587 ? 43  PHE C CZ  1 
ATOM   2196 N N   . GLN C 1 44  ? -0.38300  8.35000   -10.97000 1.000 9.40908  ? 44  GLN C N   1 
ATOM   2197 C CA  . GLN C 1 44  ? -0.58400  9.71400   -10.49100 1.000 10.42854 ? 44  GLN C CA  1 
ATOM   2198 C C   . GLN C 1 44  ? -1.82800  9.70600   -9.60900  1.000 12.48872 ? 44  GLN C C   1 
ATOM   2199 O O   . GLN C 1 44  ? -2.95100  9.65800   -10.12000 1.000 9.46518  ? 44  GLN C O   1 
ATOM   2200 C CB  . GLN C 1 44  ? -0.75000  10.65800  -11.67400 1.000 12.36988 ? 44  GLN C CB  1 
ATOM   2201 C CG  . GLN C 1 44  ? 0.45900   10.60800  -12.59300 1.000 9.67026  ? 44  GLN C CG  1 
ATOM   2202 C CD  . GLN C 1 44  ? 1.63800   11.35700  -12.00100 1.000 13.47871 ? 44  GLN C CD  1 
ATOM   2203 O OE1 . GLN C 1 44  ? 1.50700   12.53000  -11.65900 1.000 15.19318 ? 44  GLN C OE1 1 
ATOM   2204 N NE2 . GLN C 1 44  ? 2.78600   10.69000  -11.86700 1.000 12.29049 ? 44  GLN C NE2 1 
ATOM   2205 N N   . GLU C 1 45  ? -1.62300  9.75000   -8.28300  1.000 10.97975 ? 45  GLU C N   1 
ATOM   2206 C CA  . GLU C 1 45  ? -2.72400  9.75000   -7.32600  1.000 11.00992 ? 45  GLU C CA  1 
ATOM   2207 C C   . GLU C 1 45  ? -3.10900  11.16800  -6.93200  1.000 12.10780 ? 45  GLU C C   1 
ATOM   2208 O O   . GLU C 1 45  ? -2.24400  12.02200  -6.71100  1.000 12.44041 ? 45  GLU C O   1 
ATOM   2209 C CB  . GLU C 1 45  ? -2.34000  8.95700   -6.06900  1.000 14.45408 ? 45  GLU C CB  1 
ATOM   2210 C CG  . GLU C 1 45  ? -2.15100  7.49100   -6.33900  1.000 15.38413 ? 45  GLU C CG  1 
ATOM   2211 C CD  . GLU C 1 45  ? -1.62700  6.74600   -5.13500  1.000 19.28742 ? 45  GLU C CD  1 
ATOM   2212 O OE1 . GLU C 1 45  ? -0.49300  7.03100   -4.72200  1.000 20.88644 ? 45  GLU C OE1 1 
ATOM   2213 O OE2 . GLU C 1 45  ? -2.35700  5.88100   -4.61200  1.000 22.47335 ? 45  GLU C OE2 1 
ATOM   2214 N N   . GLN C 1 46  ? -4.41200  11.40400  -6.82600  1.000 10.63980 ? 46  GLN C N   1 
ATOM   2215 C CA  . GLN C 1 46  ? -4.98200  12.65200  -6.34100  1.000 12.24042 ? 46  GLN C CA  1 
ATOM   2216 C C   . GLN C 1 46  ? -6.10200  12.33200  -5.35500  1.000 13.21249 ? 46  GLN C C   1 
ATOM   2217 O O   . GLN C 1 46  ? -6.71600  11.26800  -5.43700  1.000 14.35980 ? 46  GLN C O   1 
ATOM   2218 C CB  . GLN C 1 46  ? -5.54300  13.49500  -7.50200  1.000 12.86249 ? 46  GLN C CB  1 
ATOM   2219 C CG  . GLN C 1 46  ? -4.47000  14.10300  -8.39000  1.000 11.73399 ? 46  GLN C CG  1 
ATOM   2220 C CD  . GLN C 1 46  ? -3.71900  15.21700  -7.68500  1.000 13.32118 ? 46  GLN C CD  1 
ATOM   2221 O OE1 . GLN C 1 46  ? -4.31600  16.01300  -6.96100  1.000 16.41524 ? 46  GLN C OE1 1 
ATOM   2222 N NE2 . GLN C 1 46  ? -2.40400  15.27800  -7.88700  1.000 12.95604 ? 46  GLN C NE2 1 
ATOM   2223 N N   . PRO C 1 47  ? -6.41000  13.25000  -4.44000  1.000 13.89491 ? 47  PRO C N   1 
ATOM   2224 C CA  . PRO C 1 47  ? -7.53600  13.00500  -3.52200  1.000 17.87658 ? 47  PRO C CA  1 
ATOM   2225 C C   . PRO C 1 47  ? -8.84400  12.76000  -4.26700  1.000 19.57966 ? 47  PRO C C   1 
ATOM   2226 O O   . PRO C 1 47  ? -9.11900  13.36500  -5.30600  1.000 15.39527 ? 47  PRO C O   1 
ATOM   2227 C CB  . PRO C 1 47  ? -7.59700  14.28600  -2.68100  1.000 20.27983 ? 47  PRO C CB  1 
ATOM   2228 C CG  . PRO C 1 47  ? -6.83500  15.30400  -3.44600  1.000 24.68698 ? 47  PRO C CG  1 
ATOM   2229 C CD  . PRO C 1 47  ? -5.76800  14.55100  -4.19400  1.000 18.28346 ? 47  PRO C CD  1 
ATOM   2230 N N   . ALA C 1 48  ? -9.64600  11.83700  -3.73400  1.000 15.54828 ? 48  ALA C N   1 
ATOM   2231 C CA  . ALA C 1 48  ? -10.98000 11.62300  -4.27700  1.000 17.40688 ? 48  ALA C CA  1 
ATOM   2232 C C   . ALA C 1 48  ? -11.76400 12.92700  -4.20700  1.000 18.27651 ? 48  ALA C C   1 
ATOM   2233 O O   . ALA C 1 48  ? -11.64500 13.69400  -3.24800  1.000 18.18933 ? 48  ALA C O   1 
ATOM   2234 C CB  . ALA C 1 48  ? -11.70300 10.51800  -3.50300  1.000 19.56340 ? 48  ALA C CB  1 
ATOM   2235 N N   . GLY C 1 49  ? -12.54700 13.19100  -5.24600  1.000 16.82234 ? 49  GLY C N   1 
ATOM   2236 C CA  . GLY C 1 49  ? -13.22900 14.45100  -5.40100  1.000 14.23718 ? 49  GLY C CA  1 
ATOM   2237 C C   . GLY C 1 49  ? -12.57300 15.39600  -6.38700  1.000 17.94453 ? 49  GLY C C   1 
ATOM   2238 O O   . GLY C 1 49  ? -13.14000 16.45800  -6.66400  1.000 15.39917 ? 49  GLY C O   1 
ATOM   2239 N N   . ASN C 1 50  ? -11.38300 15.06100  -6.90000  1.000 16.75146 ? 50  ASN C N   1 
ATOM   2240 C CA  . ASN C 1 50  ? -10.70300 15.90900  -7.87600  1.000 16.06668 ? 50  ASN C CA  1 
ATOM   2241 C C   . ASN C 1 50  ? -11.11100 15.61000  -9.31500  1.000 13.26034 ? 50  ASN C C   1 
ATOM   2242 O O   . ASN C 1 50  ? -10.69100 16.34300  -10.21700 1.000 13.00679 ? 50  ASN C O   1 
ATOM   2243 C CB  . ASN C 1 50  ? -9.16800  15.78200  -7.72300  1.000 13.67986 ? 50  ASN C CB  1 
ATOM   2244 C CG  . ASN C 1 50  ? -8.59500  16.79700  -6.73000  1.000 16.88322 ? 50  ASN C CG  1 
ATOM   2245 O OD1 . ASN C 1 50  ? -9.33600  17.39900  -5.94900  1.000 19.99140 ? 50  ASN C OD1 1 
ATOM   2246 N ND2 . ASN C 1 50  ? -7.27600  17.00100  -6.76400  1.000 14.77174 ? 50  ASN C ND2 1 
ATOM   2247 N N   . VAL C 1 51  ? -11.91100 14.56400  -9.55600  1.000 11.57307 ? 51  VAL C N   1 
ATOM   2248 C CA  . VAL C 1 51  ? -12.44300 14.24300  -10.88300 1.000 13.78558 ? 51  VAL C CA  1 
ATOM   2249 C C   . VAL C 1 51  ? -13.88500 14.73200  -10.98300 1.000 13.46941 ? 51  VAL C C   1 
ATOM   2250 O O   . VAL C 1 51  ? -14.69800 14.47800  -10.08300 1.000 13.48565 ? 51  VAL C O   1 
ATOM   2251 C CB  . VAL C 1 51  ? -12.36500 12.73200  -11.16300 1.000 15.83524 ? 51  VAL C CB  1 
ATOM   2252 C CG1 . VAL C 1 51  ? -12.96900 12.40900  -12.51900 1.000 16.60893 ? 51  VAL C CG1 1 
ATOM   2253 C CG2 . VAL C 1 51  ? -10.91300 12.23000  -11.09400 1.000 14.31404 ? 51  VAL C CG2 1 
ATOM   2254 N N   . PHE C 1 52  ? -14.20500 15.43800  -12.07200 1.000 12.15658 ? 52  PHE C N   1 
ATOM   2255 C CA  . PHE C 1 52  ? -15.56900 15.86000  -12.38600 1.000 13.29447 ? 52  PHE C CA  1 
ATOM   2256 C C   . PHE C 1 52  ? -15.96100 15.28400  -13.74200 1.000 15.51654 ? 52  PHE C C   1 
ATOM   2257 O O   . PHE C 1 52  ? -15.16300 15.29000  -14.68100 1.000 14.33065 ? 52  PHE C O   1 
ATOM   2258 C CB  . PHE C 1 52  ? -15.70500 17.39900  -12.40500 1.000 12.99924 ? 52  PHE C CB  1 
ATOM   2259 C CG  . PHE C 1 52  ? -15.53900 18.04100  -11.04200 1.000 15.68532 ? 52  PHE C CG  1 
ATOM   2260 C CD1 . PHE C 1 52  ? -14.29800 18.10600  -10.44000 1.000 16.65807 ? 52  PHE C CD1 1 
ATOM   2261 C CD2 . PHE C 1 52  ? -16.63300 18.55400  -10.35700 1.000 14.88144 ? 52  PHE C CD2 1 
ATOM   2262 C CE1 . PHE C 1 52  ? -14.13300 18.66200  -9.17700  1.000 15.01366 ? 52  PHE C CE1 1 
ATOM   2263 C CE2 . PHE C 1 52  ? -16.47600 19.13100  -9.09200  1.000 18.23757 ? 52  PHE C CE2 1 
ATOM   2264 C CZ  . PHE C 1 52  ? -15.22800 19.18300  -8.50100  1.000 17.42932 ? 52  PHE C CZ  1 
ATOM   2265 N N   . LEU C 1 53  ? -17.18500 14.77300  -13.85200 1.000 15.09404 ? 53  LEU C N   1 
ATOM   2266 C CA  . LEU C 1 53  ? -17.70600 14.31900  -15.13600 1.000 16.00298 ? 53  LEU C CA  1 
ATOM   2267 C C   . LEU C 1 53  ? -18.97200 15.11200  -15.40600 1.000 22.87204 ? 53  LEU C C   1 
ATOM   2268 O O   . LEU C 1 53  ? -19.88000 15.12800  -14.56900 1.000 17.55006 ? 53  LEU C O   1 
ATOM   2269 C CB  . LEU C 1 53  ? -17.97900 12.81300  -15.13500 1.000 17.85053 ? 53  LEU C CB  1 
ATOM   2270 C CG  . LEU C 1 53  ? -16.76500 11.91700  -14.85300 1.000 22.35399 ? 53  LEU C CG  1 
ATOM   2271 C CD1 . LEU C 1 53  ? -17.14200 10.44800  -14.69700 1.000 20.21757 ? 53  LEU C CD1 1 
ATOM   2272 C CD2 . LEU C 1 53  ? -15.71300 12.06800  -15.95300 1.000 18.36384 ? 53  LEU C CD2 1 
ATOM   2273 N N   . GLY C 1 54  ? -19.01300 15.80700  -16.54100 1.000 21.43622 ? 54  GLY C N   1 
ATOM   2274 C CA  . GLY C 1 54  ? -20.12700 16.69200  -16.82100 1.000 25.06126 ? 54  GLY C CA  1 
ATOM   2275 C C   . GLY C 1 54  ? -20.37400 17.69900  -15.72000 1.000 26.60674 ? 54  GLY C C   1 
ATOM   2276 O O   . GLY C 1 54  ? -21.51400 18.10100  -15.48000 1.000 25.01723 ? 54  GLY C O   1 
ATOM   2277 N N   . GLY C 1 55  ? -19.31600 18.11300  -15.03100 1.000 20.31336 ? 55  GLY C N   1 
ATOM   2278 C CA  . GLY C 1 55  ? -19.45500 19.05700  -13.94500 1.000 19.35506 ? 55  GLY C CA  1 
ATOM   2279 C C   . GLY C 1 55  ? -19.87300 18.45400  -12.62200 1.000 21.69272 ? 55  GLY C C   1 
ATOM   2280 O O   . GLY C 1 55  ? -20.02500 19.20000  -11.64300 1.000 23.76091 ? 55  GLY C O   1 
ATOM   2281 N N   . VAL C 1 56  ? -20.06400 17.13700  -12.56000 1.000 20.61210 ? 56  VAL C N   1 
ATOM   2282 C CA  . VAL C 1 56  ? -20.47400 16.44600  -11.34300 1.000 19.27273 ? 56  VAL C CA  1 
ATOM   2283 C C   . VAL C 1 56  ? -19.25600 15.81200  -10.68800 1.000 17.50636 ? 56  VAL C C   1 
ATOM   2284 O O   . VAL C 1 56  ? -18.55400 15.00500  -11.30900 1.000 16.77434 ? 56  VAL C O   1 
ATOM   2285 C CB  . VAL C 1 56  ? -21.54500 15.38300  -11.63800 1.000 21.65943 ? 56  VAL C CB  1 
ATOM   2286 C CG1 . VAL C 1 56  ? -21.97300 14.69200  -10.33000 1.000 21.98694 ? 56  VAL C CG1 1 
ATOM   2287 C CG2 . VAL C 1 56  ? -22.74800 16.03200  -12.34500 1.000 22.10073 ? 56  VAL C CG2 1 
ATOM   2288 N N   . GLN C 1 57  ? -19.03900 16.13800  -9.41700  1.000 18.98766 ? 57  GLN C N   1 
ATOM   2289 C CA  . GLN C 1 57  ? -17.89600 15.61000  -8.69100  1.000 18.58938 ? 57  GLN C CA  1 
ATOM   2290 C C   . GLN C 1 57  ? -18.02800 14.11000  -8.48300  1.000 20.22018 ? 57  GLN C C   1 
ATOM   2291 O O   . GLN C 1 57  ? -19.07800 13.61700  -8.06800  1.000 23.82718 ? 57  GLN C O   1 
ATOM   2292 C CB  . GLN C 1 57  ? -17.76400 16.31400  -7.35000  1.000 21.04038 ? 57  GLN C CB  1 
ATOM   2293 C CG  . GLN C 1 57  ? -16.51600 15.92400  -6.58400  1.000 18.34743 ? 57  GLN C CG  1 
ATOM   2294 C CD  . GLN C 1 57  ? -16.43700 16.63700  -5.26300  1.000 24.57384 ? 57  GLN C CD  1 
ATOM   2295 O OE1 . GLN C 1 57  ? -17.41300 16.69200  -4.51700  1.000 24.03927 ? 57  GLN C OE1 1 
ATOM   2296 N NE2 . GLN C 1 57  ? -15.27900 17.20600  -4.96900  1.000 20.85101 ? 57  GLN C NE2 1 
ATOM   2297 N N   . GLN C 1 58  ? -16.95600 13.38000  -8.76500  1.000 17.41227 ? 58  GLN C N   1 
ATOM   2298 C CA  . GLN C 1 58  ? -16.94900 11.92800  -8.68300  1.000 19.03930 ? 58  GLN C CA  1 
ATOM   2299 C C   . GLN C 1 58  ? -16.33600 11.45800  -7.37300  1.000 18.28400 ? 58  GLN C C   1 
ATOM   2300 O O   . GLN C 1 58  ? -15.67300 12.21500  -6.65700  1.000 19.57310 ? 58  GLN C O   1 
ATOM   2301 C CB  . GLN C 1 58  ? -16.18200 11.33400  -9.86300  1.000 22.13220 ? 58  GLN C CB  1 
ATOM   2302 C CG  . GLN C 1 58  ? -16.79300 11.72100  -11.20300 1.000 19.47509 ? 58  GLN C CG  1 
ATOM   2303 C CD  . GLN C 1 58  ? -18.21800 11.21800  -11.32500 1.000 25.17139 ? 58  GLN C CD  1 
ATOM   2304 O OE1 . GLN C 1 58  ? -18.45800 10.02000  -11.23500 1.000 27.71599 ? 58  GLN C OE1 1 
ATOM   2305 N NE2 . GLN C 1 58  ? -19.17200 12.13500  -11.49500 1.000 24.32818 ? 58  GLN C NE2 1 
ATOM   2306 N N   . GLY C 1 59  ? -16.57900 10.18300  -7.06400  1.000 21.68387 ? 59  GLY C N   1 
ATOM   2307 C CA  . GLY C 1 59  ? -15.92800 9.53200   -5.94200  1.000 25.00543 ? 59  GLY C CA  1 
ATOM   2308 C C   . GLY C 1 59  ? -14.52200 9.13800   -6.33500  1.000 28.90073 ? 59  GLY C C   1 
ATOM   2309 O O   . GLY C 1 59  ? -13.84600 9.88300   -7.04700  1.000 30.61223 ? 59  GLY C O   1 
ATOM   2310 N N   . GLY C 1 60  ? -14.06900 7.96900   -5.92000  1.000 29.10578 ? 60  GLY C N   1 
ATOM   2311 C CA  . GLY C 1 60  ? -12.69700 7.60100   -6.21300  1.000 26.89614 ? 60  GLY C CA  1 
ATOM   2312 C C   . GLY C 1 60  ? -12.53100 6.48100   -7.21000  1.000 25.59591 ? 60  GLY C C   1 
ATOM   2313 O O   . GLY C 1 60  ? -11.46300 5.87600   -7.26900  1.000 24.48781 ? 60  GLY C O   1 
ATOM   2314 N N   . ASP C 1 61  ? -13.55500 6.19100   -8.01300  1.000 25.42417 ? 61  ASP C N   1 
ATOM   2315 C CA  . ASP C 1 61  ? -13.49200 5.00400   -8.85400  1.000 25.73502 ? 61  ASP C CA  1 
ATOM   2316 C C   . ASP C 1 61  ? -12.94400 5.25600   -10.25500 1.000 26.40900 ? 61  ASP C C   1 
ATOM   2317 O O   . ASP C 1 61  ? -12.58200 4.29000   -10.93700 1.000 27.80779 ? 61  ASP C O   1 
ATOM   2318 C CB  . ASP C 1 61  ? -14.87700 4.35600   -8.96000  1.000 31.58661 ? 61  ASP C CB  1 
ATOM   2319 C CG  . ASP C 1 61  ? -15.02100 3.14600   -8.04800  1.000 39.83873 ? 61  ASP C CG  1 
ATOM   2320 O OD1 . ASP C 1 61  ? -14.48700 3.18500   -6.91500  1.000 33.49674 ? 61  ASP C OD1 1 
ATOM   2321 O OD2 . ASP C 1 61  ? -15.65900 2.15200   -8.46800  1.000 48.47782 ? 61  ASP C OD2 1 
ATOM   2322 N N   . THR C 1 62  ? -12.85500 6.50200   -10.71200 1.000 22.50765 ? 62  THR C N   1 
ATOM   2323 C CA  . THR C 1 62  ? -12.42300 6.71000   -12.08900 1.000 20.88845 ? 62  THR C CA  1 
ATOM   2324 C C   . THR C 1 62  ? -10.94600 6.36500   -12.24800 1.000 17.19465 ? 62  THR C C   1 
ATOM   2325 O O   . THR C 1 62  ? -10.13300 6.59200   -11.34400 1.000 16.36106 ? 62  THR C O   1 
ATOM   2326 C CB  . THR C 1 62  ? -12.67400 8.15200   -12.53900 1.000 24.18149 ? 62  THR C CB  1 
ATOM   2327 O OG1 . THR C 1 62  ? -14.01900 8.53600   -12.21600 1.000 28.32368 ? 62  THR C OG1 1 
ATOM   2328 C CG2 . THR C 1 62  ? -12.47700 8.26200   -14.05700 1.000 21.90937 ? 62  THR C CG2 1 
ATOM   2329 N N   . ILE C 1 63  ? -10.61500 5.76800   -13.39200 1.000 14.04399 ? 63  ILE C N   1 
ATOM   2330 C CA  . ILE C 1 63  ? -9.24100  5.54700   -13.82100 1.000 16.78183 ? 63  ILE C CA  1 
ATOM   2331 C C   . ILE C 1 63  ? -9.11000  6.10900   -15.22700 1.000 15.77564 ? 63  ILE C C   1 
ATOM   2332 O O   . ILE C 1 63  ? -9.89900  5.75800   -16.11100 1.000 15.94930 ? 63  ILE C O   1 
ATOM   2333 C CB  . ILE C 1 63  ? -8.85500  4.05500   -13.82300 1.000 15.17917 ? 63  ILE C CB  1 
ATOM   2334 C CG1 . ILE C 1 63  ? -8.96100  3.47300   -12.42100 1.000 20.33763 ? 63  ILE C CG1 1 
ATOM   2335 C CG2 . ILE C 1 63  ? -7.44900  3.87100   -14.31800 1.000 15.27391 ? 63  ILE C CG2 1 
ATOM   2336 C CD1 . ILE C 1 63  ? -8.80200  1.96100   -12.41200 1.000 25.36665 ? 63  ILE C CD1 1 
ATOM   2337 N N   . PHE C 1 64  ? -8.11600  6.96800   -15.43500 1.000 13.66235 ? 64  PHE C N   1 
ATOM   2338 C CA  . PHE C 1 64  ? -7.77800  7.46300   -16.76500 1.000 8.61100  ? 64  PHE C CA  1 
ATOM   2339 C C   . PHE C 1 64  ? -6.35600  7.03700   -17.08000 1.000 9.92764  ? 64  PHE C C   1 
ATOM   2340 O O   . PHE C 1 64  ? -5.43000  7.35500   -16.33000 1.000 9.95319  ? 64  PHE C O   1 
ATOM   2341 C CB  . PHE C 1 64  ? -7.93100  8.98400   -16.84500 1.000 11.09782 ? 64  PHE C CB  1 
ATOM   2342 C CG  . PHE C 1 64  ? -7.39100  9.59100   -18.12100 1.000 12.18147 ? 64  PHE C CG  1 
ATOM   2343 C CD1 . PHE C 1 64  ? -7.71600  9.04400   -19.35300 1.000 10.79129 ? 64  PHE C CD1 1 
ATOM   2344 C CD2 . PHE C 1 64  ? -6.57400  10.72900  -18.08200 1.000 11.70837 ? 64  PHE C CD2 1 
ATOM   2345 C CE1 . PHE C 1 64  ? -7.22400  9.59100   -20.54500 1.000 10.90299 ? 64  PHE C CE1 1 
ATOM   2346 C CE2 . PHE C 1 64  ? -6.07800  11.30100  -19.28400 1.000 10.98483 ? 64  PHE C CE2 1 
ATOM   2347 C CZ  . PHE C 1 64  ? -6.40700  10.72000  -20.50900 1.000 11.60653 ? 64  PHE C CZ  1 
ATOM   2348 N N   . VAL C 1 65  ? -6.18300  6.33300   -18.19200 1.000 9.77956  ? 65  VAL C N   1 
ATOM   2349 C CA  . VAL C 1 65  ? -4.88200  5.86800   -18.65000 1.000 12.35230 ? 65  VAL C CA  1 
ATOM   2350 C C   . VAL C 1 65  ? -4.51300  6.67800   -19.88700 1.000 12.49861 ? 65  VAL C C   1 
ATOM   2351 O O   . VAL C 1 65  ? -5.21200  6.61700   -20.90300 1.000 9.86481  ? 65  VAL C O   1 
ATOM   2352 C CB  . VAL C 1 65  ? -4.89600  4.36500   -18.97400 1.000 10.14778 ? 65  VAL C CB  1 
ATOM   2353 C CG1 . VAL C 1 65  ? -3.52500  3.90800   -19.45500 1.000 9.98153  ? 65  VAL C CG1 1 
ATOM   2354 C CG2 . VAL C 1 65  ? -5.37900  3.52400   -17.77800 1.000 12.08504 ? 65  VAL C CG2 1 
ATOM   2355 N N   . HIS C 1 66  ? -3.41500  7.42200   -19.81400 1.000 9.17348  ? 66  HIS C N   1 
ATOM   2356 C CA  . HIS C 1 66  ? -2.90000  8.16200   -20.96700 1.000 10.40230 ? 66  HIS C CA  1 
ATOM   2357 C C   . HIS C 1 66  ? -1.60900  7.47000   -21.39400 1.000 10.69791 ? 66  HIS C C   1 
ATOM   2358 O O   . HIS C 1 66  ? -0.58300  7.59000   -20.71400 1.000 9.55224  ? 66  HIS C O   1 
ATOM   2359 C CB  . HIS C 1 66  ? -2.67400  9.63200   -20.62000 1.000 12.27653 ? 66  HIS C CB  1 
ATOM   2360 C CG  . HIS C 1 66  ? -2.37700  10.49500  -21.80600 1.000 13.54308 ? 66  HIS C CG  1 
ATOM   2361 N ND1 . HIS C 1 66  ? -1.81100  11.74900  -21.69100 1.000 12.87171 ? 66  HIS C ND1 1 
ATOM   2362 C CD2 . HIS C 1 66  ? -2.58000  10.29000  -23.12900 1.000 11.36724 ? 66  HIS C CD2 1 
ATOM   2363 C CE1 . HIS C 1 66  ? -1.66800  12.27500  -22.89700 1.000 13.37343 ? 66  HIS C CE1 1 
ATOM   2364 N NE2 . HIS C 1 66  ? -2.12500  11.41200  -23.78500 1.000 12.33975 ? 66  HIS C NE2 1 
ATOM   2365 N N   . GLY C 1 67  ? -1.67300  6.72700   -22.49500 1.000 9.26969  ? 67  GLY C N   1 
ATOM   2366 C CA  . GLY C 1 67  ? -0.51400  6.01300   -23.00400 1.000 12.41492 ? 67  GLY C CA  1 
ATOM   2367 C C   . GLY C 1 67  ? 0.22700   6.86200   -24.01000 1.000 13.32544 ? 67  GLY C C   1 
ATOM   2368 O O   . GLY C 1 67  ? -0.38100  7.43200   -24.91500 1.000 14.48344 ? 67  GLY C O   1 
ATOM   2369 N N   . LEU C 1 68  ? 1.55000   6.94500   -23.85000 1.000 10.26694 ? 68  LEU C N   1 
ATOM   2370 C CA  . LEU C 1 68  ? 2.40300   7.77100   -24.70500 1.000 9.44943  ? 68  LEU C CA  1 
ATOM   2371 C C   . LEU C 1 68  ? 3.30400   6.83400   -25.49600 1.000 13.16328 ? 68  LEU C C   1 
ATOM   2372 O O   . LEU C 1 68  ? 4.18500   6.17900   -24.92600 1.000 11.42125 ? 68  LEU C O   1 
ATOM   2373 C CB  . LEU C 1 68  ? 3.20700   8.76400   -23.87000 1.000 9.41838  ? 68  LEU C CB  1 
ATOM   2374 C CG  . LEU C 1 68  ? 2.28200   9.66600   -23.04100 1.000 13.45442 ? 68  LEU C CG  1 
ATOM   2375 C CD1 . LEU C 1 68  ? 3.07800   10.47400  -22.01600 1.000 13.84477 ? 68  LEU C CD1 1 
ATOM   2376 C CD2 . LEU C 1 68  ? 1.45300   10.57700  -23.95500 1.000 13.08769 ? 68  LEU C CD2 1 
ATOM   2377 N N   . HIS C 1 69  ? 3.07700   6.77400   -26.80400 1.000 11.49806 ? 69  HIS C N   1 
ATOM   2378 C CA  . HIS C 1 69  ? 3.64700   5.75700   -27.66500 1.000 16.23754 ? 69  HIS C CA  1 
ATOM   2379 C C   . HIS C 1 69  ? 4.47800   6.38200   -28.77300 1.000 14.35672 ? 69  HIS C C   1 
ATOM   2380 O O   . HIS C 1 69  ? 4.31600   7.55400   -29.12700 1.000 13.96329 ? 69  HIS C O   1 
ATOM   2381 C CB  . HIS C 1 69  ? 2.54300   4.90300   -28.30800 1.000 15.18582 ? 69  HIS C CB  1 
ATOM   2382 C CG  . HIS C 1 69  ? 1.79400   4.05200   -27.32900 1.000 18.56251 ? 69  HIS C CG  1 
ATOM   2383 N ND1 . HIS C 1 69  ? 0.60500   4.44600   -26.75500 1.000 23.74675 ? 69  HIS C ND1 1 
ATOM   2384 C CD2 . HIS C 1 69  ? 2.07500   2.83200   -26.81100 1.000 21.52147 ? 69  HIS C CD2 1 
ATOM   2385 C CE1 . HIS C 1 69  ? 0.17600   3.49600   -25.93700 1.000 20.22243 ? 69  HIS C CE1 1 
ATOM   2386 N NE2 . HIS C 1 69  ? 1.04900   2.50500   -25.95700 1.000 21.65758 ? 69  HIS C NE2 1 
ATOM   2387 N N   . ARG C 1 70  ? 5.33200   5.56700   -29.37300 1.000 16.32564 ? 70  ARG C N   1 
ATOM   2388 C CA  . ARG C 1 70  ? 5.94700   6.00900   -30.60800 1.000 17.01634 ? 70  ARG C CA  1 
ATOM   2389 C C   . ARG C 1 70  ? 5.00100   5.75000   -31.78000 1.000 16.84258 ? 70  ARG C C   1 
ATOM   2390 O O   . ARG C 1 70  ? 4.21500   4.79500   -31.77400 1.000 16.47440 ? 70  ARG C O   1 
ATOM   2391 C CB  . ARG C 1 70  ? 7.30900   5.34700   -30.80400 1.000 24.21893 ? 70  ARG C CB  1 
ATOM   2392 C CG  . ARG C 1 70  ? 7.31200   3.91700   -31.14700 1.000 31.74524 ? 70  ARG C CG  1 
ATOM   2393 C CD  . ARG C 1 70  ? 8.75700   3.49600   -31.19000 1.000 37.28971 ? 70  ARG C CD  1 
ATOM   2394 N NE  . ARG C 1 70  ? 9.07000   2.63900   -32.32500 1.000 48.50767 ? 70  ARG C NE  1 
ATOM   2395 C CZ  . ARG C 1 70  ? 10.30500  2.38900   -32.74100 1.000 54.68017 ? 70  ARG C CZ  1 
ATOM   2396 N NH1 . ARG C 1 70  ? 11.35300  2.97500   -32.17800 1.000 38.77528 ? 70  ARG C NH1 1 
ATOM   2397 N NH2 . ARG C 1 70  ? 10.49200  1.53500   -33.74800 1.000 48.02576 ? 70  ARG C NH2 1 
ATOM   2398 N N   . GLU C 1 71  ? 5.00900   6.67300   -32.73200 1.000 15.50405 ? 71  GLU C N   1 
ATOM   2399 C CA  . GLU C 1 71  ? 4.25000   6.52900   -33.96200 1.000 17.53414 ? 71  GLU C CA  1 
ATOM   2400 C C   . GLU C 1 71  ? 4.65100   5.25600   -34.68900 1.000 16.74843 ? 71  GLU C C   1 
ATOM   2401 O O   . GLU C 1 71  ? 5.75100   4.73500   -34.51300 1.000 19.29171 ? 71  GLU C O   1 
ATOM   2402 C CB  . GLU C 1 71  ? 4.49800   7.73000   -34.87600 1.000 16.53429 ? 71  GLU C CB  1 
ATOM   2403 C CG  . GLU C 1 71  ? 3.98200   9.04300   -34.34400 1.000 22.88570 ? 71  GLU C CG  1 
ATOM   2404 C CD  . GLU C 1 71  ? 4.37800   10.21800  -35.22100 1.000 29.40894 ? 71  GLU C CD  1 
ATOM   2405 O OE1 . GLU C 1 71  ? 5.21300   10.03300  -36.14000 1.000 27.36991 ? 71  GLU C OE1 1 
ATOM   2406 O OE2 . GLU C 1 71  ? 3.84400   11.32700  -34.98000 1.000 29.68551 ? 71  GLU C OE2 1 
ATOM   2407 N N   . GLY C 1 72  ? 3.75600   4.76400   -35.53800 1.000 17.88106 ? 72  GLY C N   1 
ATOM   2408 C CA  . GLY C 1 72  ? 4.09800   3.68600   -36.45300 1.000 16.67423 ? 72  GLY C CA  1 
ATOM   2409 C C   . GLY C 1 72  ? 3.22000   2.45800   -36.36500 1.000 17.63229 ? 72  GLY C C   1 
ATOM   2410 O O   . GLY C 1 72  ? 3.26700   1.62700   -37.28200 1.000 19.92352 ? 72  GLY C O   1 
ATOM   2411 N N   . ARG C 1 73  ? 2.41400   2.29100   -35.32100 1.000 18.94647 ? 73  ARG C N   1 
ATOM   2412 C CA  . ARG C 1 73  ? 1.54500   1.12800   -35.27300 1.000 19.02751 ? 73  ARG C CA  1 
ATOM   2413 C C   . ARG C 1 73  ? 0.27600   1.37000   -36.07900 1.000 18.17269 ? 73  ARG C C   1 
ATOM   2414 O O   . ARG C 1 73  ? -0.16200  2.50800   -36.28600 1.000 13.81350 ? 73  ARG C O   1 
ATOM   2415 C CB  . ARG C 1 73  ? 1.16300   0.79000   -33.83600 1.000 19.30474 ? 73  ARG C CB  1 
ATOM   2416 C CG  . ARG C 1 73  ? 2.34300   0.60700   -32.92200 1.000 30.93762 ? 73  ARG C CG  1 
ATOM   2417 C CD  . ARG C 1 73  ? 3.22100   -0.54600  -33.34600 1.000 34.68613 ? 73  ARG C CD  1 
ATOM   2418 N NE  . ARG C 1 73  ? 4.19900   -0.85800  -32.31100 1.000 44.47702 ? 73  ARG C NE  1 
ATOM   2419 C CZ  . ARG C 1 73  ? 4.86600   -2.00100  -32.23400 1.000 48.86650 ? 73  ARG C CZ  1 
ATOM   2420 N NH1 . ARG C 1 73  ? 4.68400   -2.96600  -33.12100 1.000 46.20102 ? 73  ARG C NH1 1 
ATOM   2421 N NH2 . ARG C 1 73  ? 5.73100   -2.18000  -31.23800 1.000 50.63596 ? 73  ARG C NH2 1 
ATOM   2422 N N   . SER C 1 74  ? -0.33800  0.27100   -36.50300 1.000 17.09433 ? 74  SER C N   1 
ATOM   2423 C CA  . SER C 1 74  ? -1.59400  0.36500   -37.22700 1.000 17.03412 ? 74  SER C CA  1 
ATOM   2424 C C   . SER C 1 74  ? -2.71600  0.79100   -36.28500 1.000 18.87826 ? 74  SER C C   1 
ATOM   2425 O O   . SER C 1 74  ? -2.65500  0.58000   -35.06800 1.000 15.69545 ? 74  SER C O   1 
ATOM   2426 C CB  . SER C 1 74  ? -1.93600  -0.97700  -37.86300 1.000 19.17906 ? 74  SER C CB  1 
ATOM   2427 O OG  . SER C 1 74  ? -2.41200  -1.87400  -36.87700 1.000 18.15544 ? 74  SER C OG  1 
ATOM   2428 N N   . ALA C 1 75  ? -3.76500  1.38500   -36.86300 1.000 15.01775 ? 75  ALA C N   1 
ATOM   2429 C CA  . ALA C 1 75  ? -4.93400  1.72300   -36.06000 1.000 17.17136 ? 75  ALA C CA  1 
ATOM   2430 C C   . ALA C 1 75  ? -5.56500  0.47700   -35.44000 1.000 18.57696 ? 75  ALA C C   1 
ATOM   2431 O O   . ALA C 1 75  ? -6.07700  0.53000   -34.31300 1.000 19.56314 ? 75  ALA C O   1 
ATOM   2432 C CB  . ALA C 1 75  ? -5.95200  2.47900   -36.91300 1.000 21.92439 ? 75  ALA C CB  1 
ATOM   2433 N N   . ASP C 1 76  ? -5.52000  -0.65300  -36.14900 1.000 18.23429 ? 76  ASP C N   1 
ATOM   2434 C CA  . ASP C 1 76  ? -6.07300  -1.89400  -35.60900 1.000 22.65364 ? 76  ASP C CA  1 
ATOM   2435 C C   . ASP C 1 76  ? -5.32200  -2.32600  -34.35300 1.000 18.36205 ? 76  ASP C C   1 
ATOM   2436 O O   . ASP C 1 76  ? -5.93000  -2.70400  -33.34500 1.000 22.65960 ? 76  ASP C O   1 
ATOM   2437 C CB  . ASP C 1 76  ? -6.01200  -2.98900  -36.67700 1.000 25.01513 ? 76  ASP C CB  1 
ATOM   2438 C CG  . ASP C 1 76  ? -6.77900  -4.25300  -36.28300 1.000 39.40050 ? 76  ASP C CG  1 
ATOM   2439 O OD1 . ASP C 1 76  ? -7.33400  -4.32600  -35.15900 1.000 41.39971 ? 76  ASP C OD1 1 
ATOM   2440 O OD2 . ASP C 1 76  ? -6.83600  -5.18500  -37.11500 1.000 51.11962 ? 76  ASP C OD2 1 
ATOM   2441 N N   . LEU C 1 77  ? -3.99500  -2.30200  -34.40600 1.000 18.94448 ? 77  LEU C N   1 
ATOM   2442 C CA  . LEU C 1 77  ? -3.21200  -2.70500  -33.24400 1.000 20.37912 ? 77  LEU C CA  1 
ATOM   2443 C C   . LEU C 1 77  ? -3.45500  -1.76400  -32.07000 1.000 22.36220 ? 77  LEU C C   1 
ATOM   2444 O O   . LEU C 1 77  ? -3.59500  -2.21000  -30.91900 1.000 19.90986 ? 77  LEU C O   1 
ATOM   2445 C CB  . LEU C 1 77  ? -1.73100  -2.75100  -33.61100 1.000 16.66086 ? 77  LEU C CB  1 
ATOM   2446 C CG  . LEU C 1 77  ? -0.76600  -3.41400  -32.62000 1.000 26.27258 ? 77  LEU C CG  1 
ATOM   2447 C CD1 . LEU C 1 77  ? 0.47400   -3.89800  -33.33600 1.000 34.74646 ? 77  LEU C CD1 1 
ATOM   2448 C CD2 . LEU C 1 77  ? -0.37200  -2.45700  -31.51100 1.000 36.43756 ? 77  LEU C CD2 1 
ATOM   2449 N N   . LYS C 1 78  ? -3.49900  -0.45700  -32.33500 1.000 15.94526 ? 78  LYS C N   1 
ATOM   2450 C CA  . LYS C 1 78  ? -3.72600  0.49600   -31.25000 1.000 15.75437 ? 78  LYS C CA  1 
ATOM   2451 C C   . LYS C 1 78  ? -5.10900  0.33200   -30.64100 1.000 19.26147 ? 78  LYS C C   1 
ATOM   2452 O O   . LYS C 1 78  ? -5.27900  0.47100   -29.42300 1.000 18.37000 ? 78  LYS C O   1 
ATOM   2453 C CB  . LYS C 1 78  ? -3.53200  1.92700   -31.75900 1.000 17.35142 ? 78  LYS C CB  1 
ATOM   2454 C CG  . LYS C 1 78  ? -2.09100  2.22700   -32.11700 1.000 18.56349 ? 78  LYS C CG  1 
ATOM   2455 C CD  . LYS C 1 78  ? -1.90000  3.65100   -32.63600 1.000 19.46286 ? 78  LYS C CD  1 
ATOM   2456 C CE  . LYS C 1 78  ? -2.56200  3.88200   -33.99300 1.000 17.72343 ? 78  LYS C CE  1 
ATOM   2457 N NZ  . LYS C 1 78  ? -2.14600  5.21700   -34.53600 1.000 19.34529 ? 78  LYS C NZ  1 
ATOM   2458 N N   . GLY C 1 79  ? -6.12100  0.07700   -31.47100 1.000 18.68503 ? 79  GLY C N   1 
ATOM   2459 C CA  . GLY C 1 79  ? -7.45500  -0.11900  -30.93400 1.000 19.46344 ? 79  GLY C CA  1 
ATOM   2460 C C   . GLY C 1 79  ? -7.54600  -1.38600  -30.11000 1.000 19.06923 ? 79  GLY C C   1 
ATOM   2461 O O   . GLY C 1 79  ? -8.19400  -1.40900  -29.05900 1.000 21.42023 ? 79  GLY C O   1 
ATOM   2462 N N   . GLN C 1 80  ? -6.88000  -2.45000  -30.56900 1.000 16.19495 ? 80  GLN C N   1 
ATOM   2463 C CA  . GLN C 1 80  ? -6.83000  -3.70400  -29.82000 1.000 21.78565 ? 80  GLN C CA  1 
ATOM   2464 C C   . GLN C 1 80  ? -6.09800  -3.53700  -28.49000 1.000 23.27833 ? 80  GLN C C   1 
ATOM   2465 O O   . GLN C 1 80  ? -6.48800  -4.13000  -27.47200 1.000 19.23246 ? 80  GLN C O   1 
ATOM   2466 C CB  . GLN C 1 80  ? -6.13300  -4.76900  -30.64700 1.000 23.61061 ? 80  GLN C CB  1 
ATOM   2467 C CG  . GLN C 1 80  ? -6.96100  -5.38900  -31.74700 1.000 28.23268 ? 80  GLN C CG  1 
ATOM   2468 C CD  . GLN C 1 80  ? -6.40000  -6.73500  -32.14700 1.000 40.67069 ? 80  GLN C CD  1 
ATOM   2469 O OE1 . GLN C 1 80  ? -6.36500  -7.66900  -31.34000 1.000 47.24971 ? 80  GLN C OE1 1 
ATOM   2470 N NE2 . GLN C 1 80  ? -5.92800  -6.83700  -33.38500 1.000 47.87149 ? 80  GLN C NE2 1 
ATOM   2471 N N   . LEU C 1 81  ? -4.99700  -2.78600  -28.49900 1.000 18.89429 ? 81  LEU C N   1 
ATOM   2472 C CA  . LEU C 1 81  ? -4.24700  -2.55600  -27.27100 1.000 18.41101 ? 81  LEU C CA  1 
ATOM   2473 C C   . LEU C 1 81  ? -5.05800  -1.72800  -26.28500 1.000 18.63359 ? 81  LEU C C   1 
ATOM   2474 O O   . LEU C 1 81  ? -5.08400  -2.03100  -25.08400 1.000 17.58752 ? 81  LEU C O   1 
ATOM   2475 C CB  . LEU C 1 81  ? -2.90900  -1.88400  -27.60500 1.000 19.08503 ? 81  LEU C CB  1 
ATOM   2476 C CG  . LEU C 1 81  ? -2.00000  -1.50800  -26.42500 1.000 22.17084 ? 81  LEU C CG  1 
ATOM   2477 C CD1 . LEU C 1 81  ? -1.71800  -2.73100  -25.56000 1.000 24.98564 ? 81  LEU C CD1 1 
ATOM   2478 C CD2 . LEU C 1 81  ? -0.68600  -0.87300  -26.90400 1.000 19.99904 ? 81  LEU C CD2 1 
ATOM   2479 N N   . ALA C 1 82  ? -5.74200  -0.68500  -26.76700 1.000 16.55000 ? 82  ALA C N   1 
ATOM   2480 C CA  . ALA C 1 82  ? -6.58300  0.10200   -25.87300 1.000 15.86056 ? 82  ALA C CA  1 
ATOM   2481 C C   . ALA C 1 82  ? -7.69600  -0.74700  -25.26000 1.000 20.91357 ? 82  ALA C C   1 
ATOM   2482 O O   . ALA C 1 82  ? -7.95500  -0.66300  -24.05200 1.000 20.63920 ? 82  ALA C O   1 
ATOM   2483 C CB  . ALA C 1 82  ? -7.17000  1.30500   -26.61300 1.000 17.94544 ? 82  ALA C CB  1 
ATOM   2484 N N   . GLN C 1 83  ? -8.36400  -1.57700  -26.06800 1.000 21.00175 ? 83  GLN C N   1 
ATOM   2485 C CA  . GLN C 1 83  ? -9.43000  -2.41300  -25.51400 1.000 22.22731 ? 83  GLN C CA  1 
ATOM   2486 C C   . GLN C 1 83  ? -8.88300  -3.44700  -24.53500 1.000 20.89348 ? 83  GLN C C   1 
ATOM   2487 O O   . GLN C 1 83  ? -9.52600  -3.74900  -23.52100 1.000 21.86689 ? 83  GLN C O   1 
ATOM   2488 C CB  . GLN C 1 83  ? -10.20900 -3.10300  -26.63500 1.000 29.01826 ? 83  GLN C CB  1 
ATOM   2489 C CG  . GLN C 1 83  ? -11.64100 -2.59700  -26.78500 1.000 40.20019 ? 83  GLN C CG  1 
ATOM   2490 C CD  . GLN C 1 83  ? -12.42100 -2.58800  -25.46800 1.000 45.58518 ? 83  GLN C CD  1 
ATOM   2491 O OE1 . GLN C 1 83  ? -12.38800 -3.55700  -24.69800 1.000 46.56338 ? 83  GLN C OE1 1 
ATOM   2492 N NE2 . GLN C 1 83  ? -13.12500 -1.48500  -25.20500 1.000 41.09285 ? 83  GLN C NE2 1 
ATOM   2493 N N   . ARG C 1 84  ? -7.71000  -4.01100  -24.82500 1.000 20.77471 ? 84  ARG C N   1 
ATOM   2494 C CA  . ARG C 1 84  ? -7.08800  -4.96000  -23.90400 1.000 21.58992 ? 84  ARG C CA  1 
ATOM   2495 C C   . ARG C 1 84  ? -6.75900  -4.31100  -22.56300 1.000 22.31790 ? 84  ARG C C   1 
ATOM   2496 O O   . ARG C 1 84  ? -6.90800  -4.94000  -21.50700 1.000 21.16491 ? 84  ARG C O   1 
ATOM   2497 C CB  . ARG C 1 84  ? -5.82500  -5.54100  -24.53400 1.000 22.26903 ? 84  ARG C CB  1 
ATOM   2498 C CG  . ARG C 1 84  ? -5.15800  -6.63100  -23.70800 1.000 29.34444 ? 84  ARG C CG  1 
ATOM   2499 C CD  . ARG C 1 84  ? -5.93600  -7.94300  -23.77600 1.000 41.67091 ? 84  ARG C CD  1 
ATOM   2500 N NE  . ARG C 1 84  ? -5.35400  -8.88000  -24.73200 1.000 50.40878 ? 84  ARG C NE  1 
ATOM   2501 C CZ  . ARG C 1 84  ? -5.86500  -9.16800  -25.92200 1.000 54.42250 ? 84  ARG C CZ  1 
ATOM   2502 N NH1 . ARG C 1 84  ? -6.98700  -8.60900  -26.34900 1.000 54.80658 ? 84  ARG C NH1 1 
ATOM   2503 N NH2 . ARG C 1 84  ? -5.23400  -10.04300 -26.70400 1.000 53.21675 ? 84  ARG C NH2 1 
ATOM   2504 N N   . ILE C 1 85  ? -6.28200  -3.06300  -22.58000 1.000 17.29287 ? 85  ILE C N   1 
ATOM   2505 C CA  . ILE C 1 85  ? -5.99900  -2.36600  -21.32400 1.000 16.15348 ? 85  ILE C CA  1 
ATOM   2506 C C   . ILE C 1 85  ? -7.28200  -2.14900  -20.52900 1.000 16.87328 ? 85  ILE C C   1 
ATOM   2507 O O   . ILE C 1 85  ? -7.30700  -2.34200  -19.31000 1.000 18.39742 ? 85  ILE C O   1 
ATOM   2508 C CB  . ILE C 1 85  ? -5.26500  -1.03400  -21.59700 1.000 15.53331 ? 85  ILE C CB  1 
ATOM   2509 C CG1 . ILE C 1 85  ? -3.81700  -1.29500  -22.03300 1.000 18.23587 ? 85  ILE C CG1 1 
ATOM   2510 C CG2 . ILE C 1 85  ? -5.31600  -0.15100  -20.35900 1.000 15.23663 ? 85  ILE C CG2 1 
ATOM   2511 C CD1 . ILE C 1 85  ? -3.06500  -0.03400  -22.54000 1.000 18.32111 ? 85  ILE C CD1 1 
ATOM   2512 N N   . VAL C 1 86  ? -8.36600  -1.73800  -21.19400 1.000 13.92652 ? 86  VAL C N   1 
ATOM   2513 C CA  . VAL C 1 86  ? -9.64200  -1.58300  -20.49900 1.000 19.93217 ? 86  VAL C CA  1 
ATOM   2514 C C   . VAL C 1 86  ? -10.02300 -2.88500  -19.80700 1.000 23.68840 ? 86  VAL C C   1 
ATOM   2515 O O   . VAL C 1 86  ? -10.34000 -2.90800  -18.61400 1.000 20.54819 ? 86  VAL C O   1 
ATOM   2516 C CB  . VAL C 1 86  ? -10.74100 -1.13900  -21.48000 1.000 24.66316 ? 86  VAL C CB  1 
ATOM   2517 C CG1 . VAL C 1 86  ? -12.09500 -1.10500  -20.77900 1.000 25.18610 ? 86  VAL C CG1 1 
ATOM   2518 C CG2 . VAL C 1 86  ? -10.40500 0.21700   -22.07500 1.000 19.02371 ? 86  VAL C CG2 1 
ATOM   2519 N N   . ASP C 1 87  ? -9.98200  -3.99100  -20.54700 1.000 22.43463 ? 87  ASP C N   1 
ATOM   2520 C CA  . ASP C 1 87  ? -10.44100 -5.26200  -19.99400 1.000 27.53256 ? 87  ASP C CA  1 
ATOM   2521 C C   . ASP C 1 87  ? -9.53400  -5.73500  -18.86100 1.000 24.09641 ? 87  ASP C C   1 
ATOM   2522 O O   . ASP C 1 87  ? -10.01000 -6.09200  -17.78100 1.000 25.51305 ? 87  ASP C O   1 
ATOM   2523 C CB  . ASP C 1 87  ? -10.52500 -6.30800  -21.10500 1.000 29.83027 ? 87  ASP C CB  1 
ATOM   2524 C CG  . ASP C 1 87  ? -11.59000 -5.98100  -22.14600 1.000 34.79182 ? 87  ASP C CG  1 
ATOM   2525 O OD1 . ASP C 1 87  ? -12.57500 -5.28100  -21.82100 1.000 36.33870 ? 87  ASP C OD1 1 
ATOM   2526 O OD2 . ASP C 1 87  ? -11.44900 -6.43000  -23.30100 1.000 46.78441 ? 87  ASP C OD2 1 
ATOM   2527 N N   . ASP C 1 88  ? -8.22100  -5.73200  -19.08300 1.000 23.25951 ? 88  ASP C N   1 
ATOM   2528 C CA  . ASP C 1 88  ? -7.31400  -6.27900  -18.08400 1.000 26.54071 ? 88  ASP C CA  1 
ATOM   2529 C C   . ASP C 1 88  ? -7.15000  -5.35200  -16.88100 1.000 25.39220 ? 88  ASP C C   1 
ATOM   2530 O O   . ASP C 1 88  ? -6.92700  -5.83400  -15.76500 1.000 21.40998 ? 88  ASP C O   1 
ATOM   2531 C CB  . ASP C 1 88  ? -5.96800  -6.59600  -18.73100 1.000 22.96200 ? 88  ASP C CB  1 
ATOM   2532 C CG  . ASP C 1 88  ? -6.07400  -7.69200  -19.77900 1.000 31.58629 ? 88  ASP C CG  1 
ATOM   2533 O OD1 . ASP C 1 88  ? -7.15800  -8.29900  -19.89900 1.000 32.63954 ? 88  ASP C OD1 1 
ATOM   2534 O OD2 . ASP C 1 88  ? -5.08800  -7.93600  -20.50200 1.000 28.34668 ? 88  ASP C OD2 1 
ATOM   2535 N N   . VAL C 1 89  ? -7.26600  -4.03100  -17.06500 1.000 19.95102 ? 89  VAL C N   1 
ATOM   2536 C CA  . VAL C 1 89  ? -7.23600  -3.14800  -15.90400 1.000 18.65543 ? 89  VAL C CA  1 
ATOM   2537 C C   . VAL C 1 89  ? -8.53100  -3.28600  -15.11100 1.000 23.36571 ? 89  VAL C C   1 
ATOM   2538 O O   . VAL C 1 89  ? -8.53300  -3.20400  -13.87600 1.000 23.83125 ? 89  VAL C O   1 
ATOM   2539 C CB  . VAL C 1 89  ? -6.96900  -1.69000  -16.33200 1.000 19.99631 ? 89  VAL C CB  1 
ATOM   2540 C CG1 . VAL C 1 89  ? -7.28800  -0.72000  -15.20700 1.000 19.00784 ? 89  VAL C CG1 1 
ATOM   2541 C CG2 . VAL C 1 89  ? -5.50900  -1.52600  -16.75000 1.000 18.14314 ? 89  VAL C CG2 1 
ATOM   2542 N N   . SER C 1 90  ? -9.64800  -3.51000  -15.80800 1.000 20.26222 ? 90  SER C N   1 
ATOM   2543 C CA  . SER C 1 90  ? -10.92000 -3.74800  -15.13000 1.000 29.68255 ? 90  SER C CA  1 
ATOM   2544 C C   . SER C 1 90  ? -10.81800 -4.92300  -14.16600 1.000 25.89805 ? 90  SER C C   1 
ATOM   2545 O O   . SER C 1 90  ? -11.31900 -4.85400  -13.03500 1.000 26.47715 ? 90  SER C O   1 
ATOM   2546 C CB  . SER C 1 90  ? -12.01600 -4.01200  -16.16300 1.000 26.90500 ? 90  SER C CB  1 
ATOM   2547 O OG  . SER C 1 90  ? -13.24000 -4.31200  -15.53800 1.000 32.65523 ? 90  SER C OG  1 
ATOM   2548 N N   . VAL C 1 91  ? -10.17100 -6.00600  -14.60600 1.000 24.12873 ? 91  VAL C N   1 
ATOM   2549 C CA  . VAL C 1 91  ? -10.00000 -7.19300  -13.77200 1.000 28.19656 ? 91  VAL C CA  1 
ATOM   2550 C C   . VAL C 1 91  ? -9.00800  -6.92200  -12.65300 1.000 29.39696 ? 91  VAL C C   1 
ATOM   2551 O O   . VAL C 1 91  ? -9.27900  -7.21500  -11.48600 1.000 32.88539 ? 91  VAL C O   1 
ATOM   2552 C CB  . VAL C 1 91  ? -9.55700  -8.38900  -14.63400 1.000 29.43452 ? 91  VAL C CB  1 
ATOM   2553 C CG1 . VAL C 1 91  ? -9.05300  -9.52500  -13.75500 1.000 32.22973 ? 91  VAL C CG1 1 
ATOM   2554 C CG2 . VAL C 1 91  ? -10.70000 -8.84600  -15.54300 1.000 30.31580 ? 91  VAL C CG2 1 
ATOM   2555 N N   . ALA C 1 92  ? -7.83900  -6.36200  -12.98800 1.000 25.94207 ? 92  ALA C N   1 
ATOM   2556 C CA  . ALA C 1 92  ? -6.78000  -6.22200  -11.99100 1.000 27.90190 ? 92  ALA C CA  1 
ATOM   2557 C C   . ALA C 1 92  ? -7.14100  -5.21300  -10.90700 1.000 31.60296 ? 92  ALA C C   1 
ATOM   2558 O O   . ALA C 1 92  ? -6.65100  -5.31700  -9.77600  1.000 28.97428 ? 92  ALA C O   1 
ATOM   2559 C CB  . ALA C 1 92  ? -5.47000  -5.82200  -12.67000 1.000 25.29240 ? 92  ALA C CB  1 
ATOM   2560 N N   . ALA C 1 93  ? -7.97600  -4.22900  -11.22400 1.000 27.06588 ? 93  ALA C N   1 
ATOM   2561 C CA  . ALA C 1 93  ? -8.35600  -3.19500  -10.27400 1.000 26.18639 ? 93  ALA C CA  1 
ATOM   2562 C C   . ALA C 1 93  ? -9.71500  -3.44400  -9.64500  1.000 29.05900 ? 93  ALA C C   1 
ATOM   2563 O O   . ALA C 1 93  ? -10.11500 -2.68700  -8.75700  1.000 36.58389 ? 93  ALA C O   1 
ATOM   2564 C CB  . ALA C 1 93  ? -8.35900  -1.82100  -10.94600 1.000 24.28274 ? 93  ALA C CB  1 
ATOM   2565 N N   . GLU C 1 94  ? -10.42700 -4.48200  -10.07500 1.000 29.93305 ? 94  GLU C N   1 
ATOM   2566 C CA  . GLU C 1 94  ? -11.77700 -4.75800  -9.58600  1.000 38.47828 ? 94  GLU C CA  1 
ATOM   2567 C C   . GLU C 1 94  ? -12.66500 -3.52500  -9.75100  1.000 36.48958 ? 94  GLU C C   1 
ATOM   2568 O O   . GLU C 1 94  ? -13.33100 -3.07300  -8.81700  1.000 34.65761 ? 94  GLU C O   1 
ATOM   2569 C CB  . GLU C 1 94  ? -11.74100 -5.22100  -8.12200  1.000 41.41025 ? 94  GLU C CB  1 
ATOM   2570 C CG  . GLU C 1 94  ? -10.43500 -5.91200  -7.69800  1.000 43.80126 ? 94  GLU C CG  1 
ATOM   2571 C CD  . GLU C 1 94  ? -10.17500 -5.83200  -6.19700  1.000 51.70712 ? 94  GLU C CD  1 
ATOM   2572 O OE1 . GLU C 1 94  ? -11.14500 -5.65400  -5.42400  1.000 55.50521 ? 94  GLU C OE1 1 
ATOM   2573 O OE2 . GLU C 1 94  ? -8.99400  -5.94000  -5.79500  1.000 51.93780 ? 94  GLU C OE2 1 
ATOM   2574 N N   . ILE C 1 95  ? -12.63000 -2.93600  -10.94500 1.000 31.78354 ? 95  ILE C N   1 
ATOM   2575 C CA  . ILE C 1 95  ? -13.38200 -1.72000  -11.22500 1.000 27.05724 ? 95  ILE C CA  1 
ATOM   2576 C C   . ILE C 1 95  ? -14.16600 -1.93400  -12.51000 1.000 28.67618 ? 95  ILE C C   1 
ATOM   2577 O O   . ILE C 1 95  ? -13.66000 -2.53100  -13.46700 1.000 27.85624 ? 95  ILE C O   1 
ATOM   2578 C CB  . ILE C 1 95  ? -12.46700 -0.47500  -11.32300 1.000 33.21312 ? 95  ILE C CB  1 
ATOM   2579 C CG1 . ILE C 1 95  ? -11.83900 -0.17100  -9.96500  1.000 37.50714 ? 95  ILE C CG1 1 
ATOM   2580 C CG2 . ILE C 1 95  ? -13.24300 0.75300   -11.78200 1.000 30.69673 ? 95  ILE C CG2 1 
ATOM   2581 C CD1 . ILE C 1 95  ? -11.33600 1.26100   -9.81400  1.000 33.71797 ? 95  ILE C CD1 1 
ATOM   2582 N N   . ASP C 1 96  ? -15.41300 -1.46600  -12.51500 1.000 26.95855 ? 96  ASP C N   1 
ATOM   2583 C CA  . ASP C 1 96  ? -16.27000 -1.60500  -13.68100 1.000 30.09118 ? 96  ASP C CA  1 
ATOM   2584 C C   . ASP C 1 96  ? -15.65200 -0.89100  -14.87300 1.000 31.37118 ? 96  ASP C C   1 
ATOM   2585 O O   . ASP C 1 96  ? -15.16300 0.23600   -14.75000 1.000 29.46551 ? 96  ASP C O   1 
ATOM   2586 C CB  . ASP C 1 96  ? -17.65400 -1.03000  -13.38700 1.000 34.02922 ? 96  ASP C CB  1 
ATOM   2587 C CG  . ASP C 1 96  ? -18.68000 -1.42500  -14.42700 1.000 42.75038 ? 96  ASP C CG  1 
ATOM   2588 O OD1 . ASP C 1 96  ? -18.56200 -0.98400  -15.58800 1.000 38.89275 ? 96  ASP C OD1 1 
ATOM   2589 O OD2 . ASP C 1 96  ? -19.60100 -2.19800  -14.08600 1.000 53.78117 ? 96  ASP C OD2 1 
ATOM   2590 N N   . ARG C 1 97  ? -15.68800 -1.56200  -16.03300 1.000 27.56677 ? 97  ARG C N   1 
ATOM   2591 C CA  . ARG C 1 97  ? -15.13500 -1.00900  -17.26900 1.000 29.96913 ? 97  ARG C CA  1 
ATOM   2592 C C   . ARG C 1 97  ? -15.63900 0.39700   -17.56000 1.000 28.05533 ? 97  ARG C C   1 
ATOM   2593 O O   . ARG C 1 97  ? -14.92800 1.19200   -18.18100 1.000 32.26959 ? 97  ARG C O   1 
ATOM   2594 C CB  . ARG C 1 97  ? -15.47600 -1.91300  -18.45200 1.000 30.43061 ? 97  ARG C CB  1 
ATOM   2595 C CG  . ARG C 1 97  ? -14.79400 -3.27300  -18.45800 1.000 38.08003 ? 97  ARG C CG  1 
ATOM   2596 C CD  . ARG C 1 97  ? -15.36700 -4.16000  -19.57700 1.000 40.64890 ? 97  ARG C CD  1 
ATOM   2597 N NE  . ARG C 1 97  ? -14.74500 -3.89700  -20.87000 1.000 44.52290 ? 97  ARG C NE  1 
ATOM   2598 C CZ  . ARG C 1 97  ? -15.25200 -3.12000  -21.81900 1.000 47.85253 ? 97  ARG C CZ  1 
ATOM   2599 N NH1 . ARG C 1 97  ? -16.41500 -2.50600  -21.66500 1.000 50.86521 ? 97  ARG C NH1 1 
ATOM   2600 N NH2 . ARG C 1 97  ? -14.57500 -2.95700  -22.95300 1.000 47.57558 ? 97  ARG C NH2 1 
ATOM   2601 N N   . LYS C 1 98  ? -16.85600 0.72600   -17.13300 1.000 29.09361 ? 98  LYS C N   1 
ATOM   2602 C CA  . LYS C 1 98  ? -17.42000 2.04300   -17.39800 1.000 33.30758 ? 98  LYS C CA  1 
ATOM   2603 C C   . LYS C 1 98  ? -16.67500 3.16200   -16.67700 1.000 32.87995 ? 98  LYS C C   1 
ATOM   2604 O O   . LYS C 1 98  ? -16.89500 4.33500   -16.99600 1.000 29.09850 ? 98  LYS C O   1 
ATOM   2605 C CB  . LYS C 1 98  ? -18.89600 2.06900   -16.99900 1.000 35.68823 ? 98  LYS C CB  1 
ATOM   2606 C CG  . LYS C 1 98  ? -19.13400 2.41500   -15.53100 1.000 40.66227 ? 98  LYS C CG  1 
ATOM   2607 C CD  . LYS C 1 98  ? -20.47100 1.88900   -15.02900 1.000 44.23817 ? 98  LYS C CD  1 
ATOM   2608 C CE  . LYS C 1 98  ? -20.88900 2.60600   -13.75600 1.000 42.11668 ? 98  LYS C CE  1 
ATOM   2609 N NZ  . LYS C 1 98  ? -21.54300 1.67400   -12.80200 1.000 50.78159 ? 98  LYS C NZ  1 
ATOM   2610 N N   . HIS C 1 99  ? -15.82000 2.83200   -15.70800 1.000 26.94528 ? 99  HIS C N   1 
ATOM   2611 C CA  . HIS C 1 99  ? -15.02200 3.82600   -15.00300 1.000 25.27130 ? 99  HIS C CA  1 
ATOM   2612 C C   . HIS C 1 99  ? -13.65100 4.03900   -15.63100 1.000 20.74860 ? 99  HIS C C   1 
ATOM   2613 O O   . HIS C 1 99  ? -12.86300 4.82900   -15.10500 1.000 20.58522 ? 99  HIS C O   1 
ATOM   2614 C CB  . HIS C 1 99  ? -14.83400 3.41300   -13.53900 1.000 28.58215 ? 99  HIS C CB  1 
ATOM   2615 C CG  . HIS C 1 99  ? -16.09100 3.46200   -12.72700 1.000 32.38073 ? 99  HIS C CG  1 
ATOM   2616 N ND1 . HIS C 1 99  ? -16.65100 2.34100   -12.15100 1.000 36.58644 ? 99  HIS C ND1 1 
ATOM   2617 C CD2 . HIS C 1 99  ? -16.89300 4.49900   -12.38700 1.000 32.92468 ? 99  HIS C CD2 1 
ATOM   2618 C CE1 . HIS C 1 99  ? -17.74700 2.68300   -11.49800 1.000 32.44332 ? 99  HIS C CE1 1 
ATOM   2619 N NE2 . HIS C 1 99  ? -17.91600 3.98700   -11.62400 1.000 40.98812 ? 99  HIS C NE2 1 
ATOM   2620 N N   . ILE C 1 100 ? -13.33500 3.34300   -16.71600 1.000 18.92793 ? 100 ILE C N   1 
ATOM   2621 C CA  . ILE C 1 100 ? -11.98200 3.30700   -17.25800 1.000 20.26233 ? 100 ILE C CA  1 
ATOM   2622 C C   . ILE C 1 100 ? -11.96400 4.06400   -18.58000 1.000 23.22061 ? 100 ILE C C   1 
ATOM   2623 O O   . ILE C 1 100 ? -12.74400 3.75800   -19.49000 1.000 23.58724 ? 100 ILE C O   1 
ATOM   2624 C CB  . ILE C 1 100 ? -11.48900 1.86900   -17.44100 1.000 22.16427 ? 100 ILE C CB  1 
ATOM   2625 C CG1 . ILE C 1 100 ? -11.55000 1.11800   -16.10400 1.000 25.26583 ? 100 ILE C CG1 1 
ATOM   2626 C CG2 . ILE C 1 100 ? -10.07500 1.85800   -17.99100 1.000 22.50595 ? 100 ILE C CG2 1 
ATOM   2627 C CD1 . ILE C 1 100 ? -11.04500 -0.28400  -16.19800 1.000 23.28074 ? 100 ILE C CD1 1 
ATOM   2628 N N   . TRP C 1 101 ? -11.07800 5.05500   -18.67800 1.000 17.44872 ? 101 TRP C N   1 
ATOM   2629 C CA  . TRP C 1 101 ? -10.83300 5.80100   -19.90700 1.000 15.26235 ? 101 TRP C CA  1 
ATOM   2630 C C   . TRP C 1 101 ? -9.39200  5.55400   -20.33800 1.000 15.15467 ? 101 TRP C C   1 
ATOM   2631 O O   . TRP C 1 101 ? -8.48600  5.49700   -19.50000 1.000 12.55583 ? 101 TRP C O   1 
ATOM   2632 C CB  . TRP C 1 101 ? -11.06900 7.31400   -19.70800 1.000 18.64989 ? 101 TRP C CB  1 
ATOM   2633 C CG  . TRP C 1 101 ? -12.46600 7.74000   -19.31000 1.000 20.15528 ? 101 TRP C CG  1 
ATOM   2634 C CD1 . TRP C 1 101 ? -13.36400 7.04700   -18.53900 1.000 27.74266 ? 101 TRP C CD1 1 
ATOM   2635 C CD2 . TRP C 1 101 ? -13.10600 8.97300   -19.65400 1.000 19.99683 ? 101 TRP C CD2 1 
ATOM   2636 N NE1 . TRP C 1 101 ? -14.52000 7.77300   -18.39300 1.000 29.97899 ? 101 TRP C NE1 1 
ATOM   2637 C CE2 . TRP C 1 101 ? -14.38800 8.96000   -19.06800 1.000 25.95426 ? 101 TRP C CE2 1 
ATOM   2638 C CE3 . TRP C 1 101 ? -12.71600 10.09100  -20.40500 1.000 21.15180 ? 101 TRP C CE3 1 
ATOM   2639 C CZ2 . TRP C 1 101 ? -15.28400 10.01800  -19.20400 1.000 23.52701 ? 101 TRP C CZ2 1 
ATOM   2640 C CZ3 . TRP C 1 101 ? -13.60500 11.14200  -20.54300 1.000 20.54116 ? 101 TRP C CZ3 1 
ATOM   2641 C CH2 . TRP C 1 101 ? -14.88100 11.09500  -19.94800 1.000 25.94828 ? 101 TRP C CH2 1 
ATOM   2642 N N   . VAL C 1 102 ? -9.16800  5.39600   -21.64000 1.000 12.05933 ? 102 VAL C N   1 
ATOM   2643 C CA  . VAL C 1 102 ? -7.83500  5.09300   -22.15200 1.000 11.92496 ? 102 VAL C CA  1 
ATOM   2644 C C   . VAL C 1 102 ? -7.63500  5.90300   -23.42300 1.000 14.09120 ? 102 VAL C C   1 
ATOM   2645 O O   . VAL C 1 102 ? -8.36400  5.70500   -24.40000 1.000 12.54367 ? 102 VAL C O   1 
ATOM   2646 C CB  . VAL C 1 102 ? -7.63900  3.59400   -22.45400 1.000 13.46186 ? 102 VAL C CB  1 
ATOM   2647 C CG1 . VAL C 1 102 ? -6.24400  3.33700   -23.01200 1.000 13.78307 ? 102 VAL C CG1 1 
ATOM   2648 C CG2 . VAL C 1 102 ? -7.89000  2.73800   -21.20600 1.000 16.30966 ? 102 VAL C CG2 1 
ATOM   2649 N N   . TYR C 1 103 ? -6.66200  6.81200   -23.41300 1.000 10.30867 ? 103 TYR C N   1 
ATOM   2650 C CA  . TYR C 1 103 ? -6.26500  7.56400   -24.60300 1.000 11.78667 ? 103 TYR C CA  1 
ATOM   2651 C C   . TYR C 1 103 ? -4.82400  7.23900   -24.96400 1.000 13.54778 ? 103 TYR C C   1 
ATOM   2652 O O   . TYR C 1 103 ? -3.95600  7.23100   -24.09100 1.000 10.79581 ? 103 TYR C O   1 
ATOM   2653 C CB  . TYR C 1 103 ? -6.32600  9.07800   -24.37900 1.000 11.90718 ? 103 TYR C CB  1 
ATOM   2654 C CG  . TYR C 1 103 ? -7.67600  9.71900   -24.19000 1.000 11.52222 ? 103 TYR C CG  1 
ATOM   2655 C CD1 . TYR C 1 103 ? -8.85600  8.98700   -24.21400 1.000 12.71946 ? 103 TYR C CD1 1 
ATOM   2656 C CD2 . TYR C 1 103 ? -7.75100  11.08800  -23.97600 1.000 10.79429 ? 103 TYR C CD2 1 
ATOM   2657 C CE1 . TYR C 1 103 ? -10.08400 9.62000   -24.02500 1.000 14.04542 ? 103 TYR C CE1 1 
ATOM   2658 C CE2 . TYR C 1 103 ? -8.95200  11.72500  -23.78100 1.000 14.76471 ? 103 TYR C CE2 1 
ATOM   2659 C CZ  . TYR C 1 103 ? -10.11300 10.99500  -23.82300 1.000 17.35534 ? 103 TYR C CZ  1 
ATOM   2660 O OH  . TYR C 1 103 ? -11.27700 11.68500  -23.62700 1.000 17.38813 ? 103 TYR C OH  1 
ATOM   2661 N N   . PHE C 1 104 ? -4.55300  7.03900   -26.25500 1.000 14.09477 ? 104 PHE C N   1 
ATOM   2662 C CA  . PHE C 1 104 ? -3.18800  6.87300   -26.74500 1.000 13.37182 ? 104 PHE C CA  1 
ATOM   2663 C C   . PHE C 1 104 ? -2.74700  8.09900   -27.52900 1.000 14.46510 ? 104 PHE C C   1 
ATOM   2664 O O   . PHE C 1 104 ? -3.40800  8.48800   -28.49500 1.000 12.72311 ? 104 PHE C O   1 
ATOM   2665 C CB  . PHE C 1 104 ? -3.06900  5.64300   -27.63800 1.000 14.93969 ? 104 PHE C CB  1 
ATOM   2666 C CG  . PHE C 1 104 ? -3.17300  4.35600   -26.90400 1.000 18.07945 ? 104 PHE C CG  1 
ATOM   2667 C CD1 . PHE C 1 104 ? -3.09800  4.32100   -25.52000 1.000 19.52365 ? 104 PHE C CD1 1 
ATOM   2668 C CD2 . PHE C 1 104 ? -3.33300  3.16900   -27.59800 1.000 23.02632 ? 104 PHE C CD2 1 
ATOM   2669 C CE1 . PHE C 1 104 ? -3.19100  3.11200   -24.83200 1.000 20.19214 ? 104 PHE C CE1 1 
ATOM   2670 C CE2 . PHE C 1 104 ? -3.42900  1.96500   -26.92000 1.000 20.44528 ? 104 PHE C CE2 1 
ATOM   2671 C CZ  . PHE C 1 104 ? -3.36300  1.93800   -25.53700 1.000 19.94142 ? 104 PHE C CZ  1 
ATOM   2672 N N   . GLY C 1 105 ? -1.62100  8.69200   -27.12700 1.000 14.61794 ? 105 GLY C N   1 
ATOM   2673 C CA  . GLY C 1 105 ? -0.94300  9.70600   -27.91600 1.000 16.97327 ? 105 GLY C CA  1 
ATOM   2674 C C   . GLY C 1 105 ? 0.31500   9.11300   -28.52200 1.000 15.10756 ? 105 GLY C C   1 
ATOM   2675 O O   . GLY C 1 105 ? 0.89200   8.16600   -27.98000 1.000 17.10731 ? 105 GLY C O   1 
ATOM   2676 N N   . GLU C 1 106 ? 0.73100   9.65000   -29.66400 1.000 12.13634 ? 106 GLU C N   1 
ATOM   2677 C CA  . GLU C 1 106 ? 1.90700   9.14500   -30.35800 1.000 13.36407 ? 106 GLU C CA  1 
ATOM   2678 C C   . GLU C 1 106 ? 2.83200   10.29000  -30.73100 1.000 17.73795 ? 106 GLU C C   1 
ATOM   2679 O O   . GLU C 1 106 ? 2.38800   11.41100  -30.98300 1.000 15.26533 ? 106 GLU C O   1 
ATOM   2680 C CB  . GLU C 1 106 ? 1.55600   8.40400   -31.64500 1.000 19.70941 ? 106 GLU C CB  1 
ATOM   2681 C CG  . GLU C 1 106 ? 0.60000   7.26800   -31.51500 1.000 19.34576 ? 106 GLU C CG  1 
ATOM   2682 C CD  . GLU C 1 106 ? -0.11900  7.04400   -32.81900 1.000 20.53490 ? 106 GLU C CD  1 
ATOM   2683 O OE1 . GLU C 1 106 ? -1.12700  7.74300   -33.08500 1.000 21.89669 ? 106 GLU C OE1 1 
ATOM   2684 O OE2 . GLU C 1 106 ? 0.34300   6.19500   -33.59500 1.000 21.99020 ? 106 GLU C OE2 1 
ATOM   2685 N N   . MET C 1 107 ? 4.11700   9.97300   -30.82200 1.000 14.34096 ? 107 MET C N   1 
ATOM   2686 C CA  . MET C 1 107 ? 5.15400   10.91800  -31.19400 1.000 17.10135 ? 107 MET C CA  1 
ATOM   2687 C C   . MET C 1 107 ? 6.18600   10.20700  -32.05400 1.000 17.65156 ? 107 MET C C   1 
ATOM   2688 O O   . MET C 1 107 ? 6.34800   8.98300   -31.95500 1.000 15.07550 ? 107 MET C O   1 
ATOM   2689 C CB  . MET C 1 107 ? 5.86200   11.50300  -29.96300 1.000 15.90647 ? 107 MET C CB  1 
ATOM   2690 C CG  . MET C 1 107 ? 4.97400   12.27100  -29.04000 1.000 19.58218 ? 107 MET C CG  1 
ATOM   2691 S SD  . MET C 1 107 ? 5.54400   11.98900  -27.34400 1.000 20.80475 ? 107 MET C SD  1 
ATOM   2692 C CE  . MET C 1 107 ? 4.83700   10.40000  -27.00800 1.000 15.99028 ? 107 MET C CE  1 
ATOM   2693 N N   . PRO C 1 108 ? 6.89800   10.94800  -32.90100 1.000 15.19500 ? 108 PRO C N   1 
ATOM   2694 C CA  . PRO C 1 108 ? 8.03500   10.36300  -33.61600 1.000 16.57800 ? 108 PRO C CA  1 
ATOM   2695 C C   . PRO C 1 108 ? 9.06100   9.81000   -32.63700 1.000 19.03864 ? 108 PRO C C   1 
ATOM   2696 O O   . PRO C 1 108 ? 9.36000   10.42100  -31.60600 1.000 15.41251 ? 108 PRO C O   1 
ATOM   2697 C CB  . PRO C 1 108 ? 8.59700   11.54800  -34.41500 1.000 17.65066 ? 108 PRO C CB  1 
ATOM   2698 C CG  . PRO C 1 108 ? 7.45100   12.49500  -34.55200 1.000 18.90090 ? 108 PRO C CG  1 
ATOM   2699 C CD  . PRO C 1 108 ? 6.66700   12.35700  -33.27900 1.000 17.88323 ? 108 PRO C CD  1 
ATOM   2700 N N   . ALA C 1 109 ? 9.59800   8.63500   -32.96600 1.000 18.22656 ? 109 ALA C N   1 
ATOM   2701 C CA  . ALA C 1 109 ? 10.61800  8.03000   -32.11800 1.000 21.74642 ? 109 ALA C CA  1 
ATOM   2702 C C   . ALA C 1 109 ? 11.82000  8.95000   -31.94800 1.000 20.14639 ? 109 ALA C C   1 
ATOM   2703 O O   . ALA C 1 109 ? 12.51200  8.88200   -30.92300 1.000 21.74637 ? 109 ALA C O   1 
ATOM   2704 C CB  . ALA C 1 109 ? 11.05400  6.68200   -32.69700 1.000 24.31244 ? 109 ALA C CB  1 
ATOM   2705 N N   . GLN C 1 110 ? 12.06500  9.83200   -32.92200 1.000 16.64525 ? 110 GLN C N   1 
ATOM   2706 C CA  . GLN C 1 110 ? 13.24100  10.69200  -32.91100 1.000 24.36676 ? 110 GLN C CA  1 
ATOM   2707 C C   . GLN C 1 110 ? 13.19600  11.74900  -31.81700 1.000 23.14637 ? 110 GLN C C   1 
ATOM   2708 O O   . GLN C 1 110 ? 14.23500  12.35500  -31.52800 1.000 23.22800 ? 110 GLN C O   1 
ATOM   2709 C CB  . GLN C 1 110 ? 13.42000  11.37700  -34.27600 1.000 26.62895 ? 110 GLN C CB  1 
ATOM   2710 C CG  . GLN C 1 110 ? 13.24200  10.45100  -35.47400 1.000 33.00695 ? 110 GLN C CG  1 
ATOM   2711 C CD  . GLN C 1 110 ? 11.77600  10.27600  -35.87100 1.000 31.58730 ? 110 GLN C CD  1 
ATOM   2712 O OE1 . GLN C 1 110 ? 11.18200  9.21200   -35.66100 1.000 32.78672 ? 110 GLN C OE1 1 
ATOM   2713 N NE2 . GLN C 1 110 ? 11.19000  11.32200  -36.45000 1.000 36.25287 ? 110 GLN C NE2 1 
ATOM   2714 N N   . GLN C 1 111 ? 12.03000  11.99900  -31.21400 1.000 17.88551 ? 111 GLN C N   1 
ATOM   2715 C CA  . GLN C 1 111 ? 11.91500  12.93700  -30.10400 1.000 17.95323 ? 111 GLN C CA  1 
ATOM   2716 C C   . GLN C 1 111 ? 11.45200  12.22400  -28.83500 1.000 20.63549 ? 111 GLN C C   1 
ATOM   2717 O O   . GLN C 1 111 ? 10.71800  12.78900  -28.01500 1.000 18.54526 ? 111 GLN C O   1 
ATOM   2718 C CB  . GLN C 1 111 ? 10.98500  14.09500  -30.47500 1.000 18.84022 ? 111 GLN C CB  1 
ATOM   2719 C CG  . GLN C 1 111 ? 9.55000   13.68900  -30.82400 1.000 15.91986 ? 111 GLN C CG  1 
ATOM   2720 C CD  . GLN C 1 111 ? 8.84400   14.70100  -31.70800 1.000 17.52905 ? 111 GLN C CD  1 
ATOM   2721 O OE1 . GLN C 1 111 ? 9.33700   15.03700  -32.79200 1.000 21.64154 ? 111 GLN C OE1 1 
ATOM   2722 N NE2 . GLN C 1 111 ? 7.67800   15.18700  -31.26700 1.000 15.63330 ? 111 GLN C NE2 1 
ATOM   2723 N N   . MET C 1 112 ? 11.85200  10.96100  -28.67600 1.000 16.54981 ? 112 MET C N   1 
ATOM   2724 C CA  . MET C 1 112 ? 11.52400  10.16700  -27.50400 1.000 14.75388 ? 112 MET C CA  1 
ATOM   2725 C C   . MET C 1 112 ? 12.79100  9.50900   -26.98700 1.000 20.02287 ? 112 MET C C   1 
ATOM   2726 O O   . MET C 1 112 ? 13.50800  8.85200   -27.75000 1.000 17.89004 ? 112 MET C O   1 
ATOM   2727 C CB  . MET C 1 112 ? 10.47700  9.09600   -27.81300 1.000 15.22909 ? 112 MET C CB  1 
ATOM   2728 C CG  . MET C 1 112 ? 9.17200   9.64500   -28.33600 1.000 16.09048 ? 112 MET C CG  1 
ATOM   2729 S SD  . MET C 1 112 ? 8.01600   8.33400   -28.74100 1.000 15.65511 ? 112 MET C SD  1 
ATOM   2730 C CE  . MET C 1 112 ? 7.63700   7.57900   -27.15300 1.000 18.08359 ? 112 MET C CE  1 
ATOM   2731 N N   . VAL C 1 113 ? 13.04600  9.66900   -25.68800 1.000 17.97469 ? 113 VAL C N   1 
ATOM   2732 C CA  . VAL C 1 113 ? 14.24300  9.15200   -25.03600 1.000 20.98440 ? 113 VAL C CA  1 
ATOM   2733 C C   . VAL C 1 113 ? 13.79700  8.30300   -23.85600 1.000 23.25778 ? 113 VAL C C   1 
ATOM   2734 O O   . VAL C 1 113 ? 13.03100  8.77000   -23.00500 1.000 19.51176 ? 113 VAL C O   1 
ATOM   2735 C CB  . VAL C 1 113 ? 15.17900  10.28600  -24.58500 1.000 20.71779 ? 113 VAL C CB  1 
ATOM   2736 C CG1 . VAL C 1 113 ? 16.28700  9.74800   -23.70300 1.000 27.14436 ? 113 VAL C CG1 1 
ATOM   2737 C CG2 . VAL C 1 113 ? 15.76300  10.99300  -25.79500 1.000 21.87977 ? 113 VAL C CG2 1 
ATOM   2738 N N   . GLU C 1 114 ? 14.23600  7.04600   -23.82700 1.000 26.67661 ? 114 GLU C N   1 
ATOM   2739 C CA  . GLU C 1 114 ? 13.98400  6.14400   -22.71500 1.000 23.56305 ? 114 GLU C CA  1 
ATOM   2740 C C   . GLU C 1 114 ? 15.32100  5.63500   -22.20000 1.000 32.20021 ? 114 GLU C C   1 
ATOM   2741 O O   . GLU C 1 114 ? 16.23400  5.37600   -22.98900 1.000 32.22283 ? 114 GLU C O   1 
ATOM   2742 C CB  . GLU C 1 114 ? 13.10100  4.97100   -23.13400 1.000 24.86463 ? 114 GLU C CB  1 
ATOM   2743 C CG  . GLU C 1 114 ? 11.71500  5.37700   -23.59600 1.000 23.90391 ? 114 GLU C CG  1 
ATOM   2744 C CD  . GLU C 1 114 ? 10.86200  4.18600   -23.96300 1.000 35.69469 ? 114 GLU C CD  1 
ATOM   2745 O OE1 . GLU C 1 114 ? 11.35600  3.04700   -23.85500 1.000 46.40502 ? 114 GLU C OE1 1 
ATOM   2746 O OE2 . GLU C 1 114 ? 9.69500   4.37900   -24.36400 1.000 35.37175 ? 114 GLU C OE2 1 
ATOM   2747 N N   . TYR C 1 115 ? 15.44100  5.50500   -20.87800 1.000 35.19032 ? 115 TYR C N   1 
ATOM   2748 C CA  . TYR C 1 115 ? 16.70100  5.07800   -20.26300 1.000 33.01399 ? 115 TYR C CA  1 
ATOM   2749 C C   . TYR C 1 115 ? 17.86300  5.92700   -20.75700 1.000 36.37703 ? 115 TYR C C   1 
ATOM   2750 O O   . TYR C 1 115 ? 18.97300  5.43200   -20.97400 1.000 35.37626 ? 115 TYR C O   1 
ATOM   2751 C CB  . TYR C 1 115 ? 16.97500  3.59900   -20.53500 1.000 39.40432 ? 115 TYR C CB  1 
ATOM   2752 C CG  . TYR C 1 115 ? 15.98600  2.69000   -19.87700 1.000 33.99200 ? 115 TYR C CG  1 
ATOM   2753 C CD1 . TYR C 1 115 ? 16.06500  2.44000   -18.51600 1.000 38.77408 ? 115 TYR C CD1 1 
ATOM   2754 C CD2 . TYR C 1 115 ? 14.96500  2.09000   -20.60600 1.000 37.78720 ? 115 TYR C CD2 1 
ATOM   2755 C CE1 . TYR C 1 115 ? 15.16900  1.61900   -17.89400 1.000 37.34142 ? 115 TYR C CE1 1 
ATOM   2756 C CE2 . TYR C 1 115 ? 14.05200  1.25900   -19.99100 1.000 38.44944 ? 115 TYR C CE2 1 
ATOM   2757 C CZ  . TYR C 1 115 ? 14.16400  1.02700   -18.63000 1.000 40.79926 ? 115 TYR C CZ  1 
ATOM   2758 O OH  . TYR C 1 115 ? 13.27600  0.20500   -17.98200 1.000 40.16610 ? 115 TYR C OH  1 
ATOM   2759 N N   . GLY C 1 116 ? 17.59600  7.21500   -20.97000 1.000 35.07736 ? 116 GLY C N   1 
ATOM   2760 C CA  . GLY C 1 116 ? 18.60400  8.10300   -21.52400 1.000 36.81417 ? 116 GLY C CA  1 
ATOM   2761 C C   . GLY C 1 116 ? 19.09500  7.74800   -22.91600 1.000 34.91301 ? 116 GLY C C   1 
ATOM   2762 O O   . GLY C 1 116 ? 20.17500  8.20200   -23.30200 1.000 38.60643 ? 116 GLY C O   1 
ATOM   2763 N N   . ARG C 1 117 ? 18.32800  6.95600   -23.68900 1.000 36.86138 ? 117 ARG C N   1 
ATOM   2764 C CA  . ARG C 1 117 ? 18.65900  6.60800   -25.07400 1.000 35.30105 ? 117 ARG C CA  1 
ATOM   2765 C C   . ARG C 1 117 ? 17.47600  6.91600   -25.99100 1.000 32.40696 ? 117 ARG C C   1 
ATOM   2766 O O   . ARG C 1 117 ? 16.32100  6.78800   -25.58600 1.000 31.53132 ? 117 ARG C O   1 
ATOM   2767 C CB  . ARG C 1 117 ? 19.01700  5.10400   -25.23400 1.000 37.30264 ? 117 ARG C CB  1 
ATOM   2768 C CG  . ARG C 1 117 ? 19.90600  4.53400   -24.14300 1.000 47.13032 ? 117 ARG C CG  1 
ATOM   2769 C CD  . ARG C 1 117 ? 19.34600  3.21900   -23.57400 1.000 55.67265 ? 117 ARG C CD  1 
ATOM   2770 N NE  . ARG C 1 117 ? 19.78900  2.03400   -24.30500 1.000 61.46783 ? 117 ARG C NE  1 
ATOM   2771 C CZ  . ARG C 1 117 ? 19.65000  0.78700   -23.86800 1.000 68.65822 ? 117 ARG C CZ  1 
ATOM   2772 N NH1 . ARG C 1 117 ? 19.07500  0.51900   -22.70600 1.000 64.91471 ? 117 ARG C NH1 1 
ATOM   2773 N NH2 . ARG C 1 117 ? 20.10700  -0.21800  -24.61200 1.000 68.65168 ? 117 ARG C NH2 1 
ATOM   2774 N N   . PHE C 1 118 ? 17.77300  7.27500   -27.24300 1.000 30.94084 ? 118 PHE C N   1 
ATOM   2775 C CA  . PHE C 1 118 ? 16.73700  7.52500   -28.24400 1.000 32.38054 ? 118 PHE C CA  1 
ATOM   2776 C C   . PHE C 1 118 ? 16.06300  6.23500   -28.69900 1.000 36.51688 ? 118 PHE C C   1 
ATOM   2777 O O   . PHE C 1 118 ? 16.69700  5.18200   -28.81900 1.000 35.66275 ? 118 PHE C O   1 
ATOM   2778 C CB  . PHE C 1 118 ? 17.32000  8.23100   -29.46800 1.000 30.49744 ? 118 PHE C CB  1 
ATOM   2779 C CG  . PHE C 1 118 ? 17.44200  9.71100   -29.30500 1.000 38.61415 ? 118 PHE C CG  1 
ATOM   2780 C CD1 . PHE C 1 118 ? 16.36200  10.54100  -29.57200 1.000 31.94398 ? 118 PHE C CD1 1 
ATOM   2781 C CD2 . PHE C 1 118 ? 18.62900  10.28100  -28.86500 1.000 38.74781 ? 118 PHE C CD2 1 
ATOM   2782 C CE1 . PHE C 1 118 ? 16.46100  11.90900  -29.40900 1.000 28.48503 ? 118 PHE C CE1 1 
ATOM   2783 C CE2 . PHE C 1 118 ? 18.73900  11.65400  -28.70700 1.000 34.36476 ? 118 PHE C CE2 1 
ATOM   2784 C CZ  . PHE C 1 118 ? 17.64600  12.46700  -28.98100 1.000 33.48578 ? 118 PHE C CZ  1 
ATOM   2785 N N   . LEU C 1 119 ? 14.76200  6.33500   -28.99300 1.000 31.49893 ? 119 LEU C N   1 
ATOM   2786 C CA  . LEU C 1 119 ? 14.03500  5.13600   -29.39100 1.000 31.52460 ? 119 LEU C CA  1 
ATOM   2787 C C   . LEU C 1 119 ? 14.32800  4.80100   -30.85400 1.000 34.32756 ? 119 LEU C C   1 
ATOM   2788 O O   . LEU C 1 119 ? 14.50500  5.70800   -31.67100 1.000 34.06560 ? 119 LEU C O   1 
ATOM   2789 C CB  . LEU C 1 119 ? 12.53500  5.32500   -29.19000 1.000 26.97209 ? 119 LEU C CB  1 
ATOM   2790 C CG  . LEU C 1 119 ? 12.11500  5.67500   -27.76700 1.000 27.26071 ? 119 LEU C CG  1 
ATOM   2791 C CD1 . LEU C 1 119 ? 10.65600  5.30200   -27.53700 1.000 30.41079 ? 119 LEU C CD1 1 
ATOM   2792 C CD2 . LEU C 1 119 ? 13.02900  4.98500   -26.75900 1.000 33.62146 ? 119 LEU C CD2 1 
ATOM   2793 N N   . PRO C 1 120 ? 14.40100  3.50100   -31.20800 1.000 39.43430 ? 120 PRO C N   1 
ATOM   2794 C CA  . PRO C 1 120 ? 14.78900  3.01800   -32.54700 1.000 44.56621 ? 120 PRO C CA  1 
ATOM   2795 C C   . PRO C 1 120 ? 14.10000  3.74100   -33.71700 1.000 46.61457 ? 120 PRO C C   1 
ATOM   2796 O O   . PRO C 1 120 ? 13.03000  3.35600   -34.19900 1.000 45.78385 ? 120 PRO C O   1 
ATOM   2797 C CB  . PRO C 1 120 ? 14.39700  1.52900   -32.51100 1.000 43.73272 ? 120 PRO C CB  1 
ATOM   2798 C CG  . PRO C 1 120 ? 13.76500  1.28000   -31.15300 1.000 43.55318 ? 120 PRO C CG  1 
ATOM   2799 C CD  . PRO C 1 120 ? 14.22000  2.38700   -30.26200 1.000 36.31352 ? 120 PRO C CD  1 
HETATM 2800 C C   . ACT D 2 .   ? -13.51000 14.84100  -27.56800 1.000 36.56344 ? 201 ACT B C   1 
HETATM 2801 O O   . ACT D 2 .   ? -13.01600 15.88300  -27.05800 1.000 44.13027 ? 201 ACT B O   1 
HETATM 2802 O OXT . ACT D 2 .   ? -14.05600 14.88600  -28.68700 1.000 46.98867 ? 201 ACT B OXT 1 
HETATM 2803 C CH3 . ACT D 2 .   ? -13.47300 13.49200  -26.85300 1.000 33.91389 ? 201 ACT B CH3 1 
HETATM 2804 C C   . ACT E 2 .   ? 4.60200   1.49100   -29.84300 1.000 37.97859 ? 201 ACT C C   1 
HETATM 2805 O O   . ACT E 2 .   ? 3.60000   1.85700   -29.15800 1.000 47.03603 ? 201 ACT C O   1 
HETATM 2806 O OXT . ACT E 2 .   ? 4.77500   1.90300   -31.02400 1.000 37.38622 ? 201 ACT C OXT 1 
HETATM 2807 C CH3 . ACT E 2 .   ? 5.63300   0.54000   -29.24700 1.000 40.91633 ? 201 ACT C CH3 1 
HETATM 2808 O O   . HOH F 3 .   ? 3.55500   21.67600  -10.17200 1.000 23.10672 ? 201 HOH A O   1 
HETATM 2809 O O   . HOH F 3 .   ? 20.74200  23.70800  -20.06100 1.000 27.03830 ? 202 HOH A O   1 
HETATM 2810 O O   . HOH F 3 .   ? -0.35500  16.11600  -9.71200  1.000 24.76505 ? 203 HOH A O   1 
HETATM 2811 O O   . HOH F 3 .   ? 13.58900  14.56800  -33.29200 1.000 28.94515 ? 204 HOH A O   1 
HETATM 2812 O O   . HOH F 3 .   ? 11.05400  5.85300   -9.60500  1.000 29.04360 ? 205 HOH A O   1 
HETATM 2813 O O   . HOH F 3 .   ? 12.17500  10.90300  -8.91300  1.000 18.48436 ? 206 HOH A O   1 
HETATM 2814 O O   . HOH F 3 .   ? 1.75600   15.07000  -19.32700 1.000 23.31561 ? 207 HOH A O   1 
HETATM 2815 O O   . HOH F 3 .   ? 7.19100   7.99700   -7.72000  1.000 18.73324 ? 208 HOH A O   1 
HETATM 2816 O O   . HOH F 3 .   ? 8.28100   21.60400  -32.79100 1.000 18.04370 ? 209 HOH A O   1 
HETATM 2817 O O   . HOH F 3 .   ? 10.37800  8.43700   -9.73500  1.000 25.90608 ? 210 HOH A O   1 
HETATM 2818 O O   . HOH F 3 .   ? 8.48000   5.29400   -7.92100  1.000 19.14457 ? 211 HOH A O   1 
HETATM 2819 O O   . HOH F 3 .   ? 6.49500   16.34000  -35.74200 1.000 36.98567 ? 212 HOH A O   1 
HETATM 2820 O O   . HOH F 3 .   ? -3.75500  36.12100  -27.76900 1.000 44.13359 ? 213 HOH A O   1 
HETATM 2821 O O   . HOH F 3 .   ? 12.02300  18.73900  -1.59000  1.000 29.39090 ? 214 HOH A O   1 
HETATM 2822 O O   . HOH F 3 .   ? 8.13600   16.42100  -1.99200  1.000 37.80044 ? 215 HOH A O   1 
HETATM 2823 O O   . HOH F 3 .   ? 9.333     18.525    1.190     1.000 30.89657 ? 216 HOH A O   1 
HETATM 2824 O O   . HOH F 3 .   ? 11.02900  15.62400  -5.76900  1.000 20.67178 ? 217 HOH A O   1 
HETATM 2825 O O   . HOH F 3 .   ? 3.11600   13.79200  -26.43700 1.000 22.18509 ? 218 HOH A O   1 
HETATM 2826 O O   . HOH F 3 .   ? 10.68800  20.99000  -2.78600  1.000 29.56306 ? 219 HOH A O   1 
HETATM 2827 O O   . HOH F 3 .   ? -5.27200  24.55000  -34.61000 1.000 23.34995 ? 220 HOH A O   1 
HETATM 2828 O O   . HOH F 3 .   ? 10.46800  -3.92200  -6.69700  1.000 34.42342 ? 221 HOH A O   1 
HETATM 2829 O O   . HOH F 3 .   ? 12.495    26.486    -35.827   1.000 39.51581 ? 222 HOH A O   1 
HETATM 2830 O O   . HOH F 3 .   ? 20.97700  24.32500  -13.57300 1.000 26.67334 ? 223 HOH A O   1 
HETATM 2831 O O   . HOH F 3 .   ? 5.16800   11.78000  -10.63900 1.000 12.21873 ? 224 HOH A O   1 
HETATM 2832 O O   . HOH F 3 .   ? 11.03900  27.38000  -15.90200 1.000 16.26439 ? 225 HOH A O   1 
HETATM 2833 O O   . HOH F 3 .   ? 14.40400  1.25500   -8.27200  1.000 35.76676 ? 226 HOH A O   1 
HETATM 2834 O O   . HOH F 3 .   ? -5.97400  30.54700  -32.70700 1.000 37.27716 ? 227 HOH A O   1 
HETATM 2835 O O   . HOH F 3 .   ? 13.97500  23.98000  -36.12000 1.000 25.04256 ? 228 HOH A O   1 
HETATM 2836 O O   . HOH F 3 .   ? 8.43900   9.59000   -11.91800 1.000 17.13522 ? 229 HOH A O   1 
HETATM 2837 O O   . HOH F 3 .   ? 13.93300  -2.51900  -12.08200 1.000 31.64270 ? 230 HOH A O   1 
HETATM 2838 O O   . HOH F 3 .   ? 2.74200   25.64900  -34.68800 1.000 27.23329 ? 231 HOH A O   1 
HETATM 2839 O O   . HOH F 3 .   ? 22.97600  21.10300  -15.63000 1.000 31.45097 ? 232 HOH A O   1 
HETATM 2840 O O   . HOH F 3 .   ? 9.75900   16.49800  -37.26500 1.000 30.16214 ? 233 HOH A O   1 
HETATM 2841 O O   . HOH F 3 .   ? 3.69000   4.13200   -3.57400  1.000 26.80441 ? 234 HOH A O   1 
HETATM 2842 O O   . HOH F 3 .   ? 0.92700   13.35900  -4.36600  1.000 34.76977 ? 235 HOH A O   1 
HETATM 2843 O O   . HOH F 3 .   ? 14.56300  4.30300   -16.01700 1.000 32.32960 ? 236 HOH A O   1 
HETATM 2844 O O   . HOH F 3 .   ? 15.78300  17.60800  -39.13700 1.000 27.35228 ? 237 HOH A O   1 
HETATM 2845 O O   . HOH F 3 .   ? 8.40000   9.44000   -1.65000  1.000 30.83227 ? 238 HOH A O   1 
HETATM 2846 O O   . HOH F 3 .   ? 7.15900   25.71400  -28.18400 1.000 24.75439 ? 239 HOH A O   1 
HETATM 2847 O O   . HOH F 3 .   ? 20.20900  30.12900  -23.57600 1.000 46.30177 ? 240 HOH A O   1 
HETATM 2848 O O   . HOH F 3 .   ? 3.71600   15.23800  -31.34900 1.000 27.15414 ? 241 HOH A O   1 
HETATM 2849 O O   . HOH F 3 .   ? 2.49000   15.63000  -4.12500  1.000 37.76169 ? 242 HOH A O   1 
HETATM 2850 O O   . HOH F 3 .   ? 21.02200  7.72400   -9.92600  1.000 39.98068 ? 243 HOH A O   1 
HETATM 2851 O O   . HOH F 3 .   ? 19.69200  26.05200  -7.21800  1.000 38.69912 ? 244 HOH A O   1 
HETATM 2852 O O   . HOH F 3 .   ? 14.68400  4.03700   -8.39800  1.000 34.62302 ? 245 HOH A O   1 
HETATM 2853 O O   . HOH F 3 .   ? 16.43700  23.79900  -36.96800 1.000 35.26378 ? 246 HOH A O   1 
HETATM 2854 O O   . HOH F 3 .   ? 21.67200  17.04700  -6.10200  1.000 47.56490 ? 247 HOH A O   1 
HETATM 2855 O O   . HOH F 3 .   ? 1.28100   22.76200  -9.92600  1.000 16.59076 ? 248 HOH A O   1 
HETATM 2856 O O   . HOH F 3 .   ? 22.90700  22.27500  -13.11900 1.000 40.52708 ? 249 HOH A O   1 
HETATM 2857 O O   . HOH F 3 .   ? 22.01500  25.58500  -11.29000 1.000 37.46004 ? 250 HOH A O   1 
HETATM 2858 O O   . HOH G 3 .   ? -7.82800  14.13800  -10.11300 1.000 23.15866 ? 301 HOH B O   1 
HETATM 2859 O O   . HOH G 3 .   ? -11.33200 13.77400  -25.74200 1.000 30.19885 ? 302 HOH B O   1 
HETATM 2860 O O   . HOH G 3 .   ? -1.12900  13.40100  -9.72800  1.000 23.05067 ? 303 HOH B O   1 
HETATM 2861 O O   . HOH G 3 .   ? -18.18700 28.08400  -20.07400 1.000 27.79027 ? 304 HOH B O   1 
HETATM 2862 O O   . HOH G 3 .   ? -0.00300  14.61700  -15.66100 1.000 7.92307  ? 305 HOH B O   1 
HETATM 2863 O O   . HOH G 3 .   ? 2.20600   28.63000  -9.72100  1.000 30.62179 ? 306 HOH B O   1 
HETATM 2864 O O   . HOH G 3 .   ? -10.18700 18.32800  -32.88800 1.000 17.63037 ? 307 HOH B O   1 
HETATM 2865 O O   . HOH G 3 .   ? 1.76300   32.28900  -12.91200 1.000 36.33686 ? 308 HOH B O   1 
HETATM 2866 O O   . HOH G 3 .   ? 0.20500   26.72800  -9.81800  1.000 25.24386 ? 309 HOH B O   1 
HETATM 2867 O O   . HOH G 3 .   ? -2.93400  27.03600  -8.87100  1.000 20.41035 ? 310 HOH B O   1 
HETATM 2868 O O   . HOH G 3 .   ? -1.13500  15.88500  -19.36300 1.000 25.11498 ? 311 HOH B O   1 
HETATM 2869 O O   . HOH G 3 .   ? -7.56800  18.57800  -2.33600  1.000 35.75432 ? 312 HOH B O   1 
HETATM 2870 O O   . HOH G 3 .   ? -9.61000  22.97100  -1.62000  1.000 30.13676 ? 313 HOH B O   1 
HETATM 2871 O O   . HOH G 3 .   ? -0.91200  17.75500  -26.40500 1.000 24.82537 ? 314 HOH B O   1 
HETATM 2872 O O   . HOH G 3 .   ? -6.34500  23.65300  -5.75400  1.000 20.06519 ? 315 HOH B O   1 
HETATM 2873 O O   . HOH G 3 .   ? -8.01000  17.81800  -36.16200 1.000 29.86250 ? 316 HOH B O   1 
HETATM 2874 O O   . HOH G 3 .   ? 2.12900   24.11300  -7.72000  1.000 16.36886 ? 317 HOH B O   1 
HETATM 2875 O O   . HOH G 3 .   ? 3.80800   26.56500  -7.79000  1.000 18.49962 ? 318 HOH B O   1 
HETATM 2876 O O   . HOH G 3 .   ? 13.19600  31.07600  -8.15900  1.000 25.55030 ? 319 HOH B O   1 
HETATM 2877 O O   . HOH G 3 .   ? -6.01200  5.05800   -34.64800 1.000 23.70072 ? 320 HOH B O   1 
HETATM 2878 O O   . HOH G 3 .   ? -4.39900  19.51900  -35.66700 1.000 37.28026 ? 321 HOH B O   1 
HETATM 2879 O O   . HOH G 3 .   ? -22.80400 21.57600  -12.09400 1.000 41.54892 ? 322 HOH B O   1 
HETATM 2880 O O   . HOH G 3 .   ? -16.56100 17.86600  -15.88700 1.000 16.83261 ? 323 HOH B O   1 
HETATM 2881 O O   . HOH G 3 .   ? 7.98500   35.20100  -12.01500 1.000 32.39841 ? 324 HOH B O   1 
HETATM 2882 O O   . HOH G 3 .   ? -10.84000 20.50200  -2.73400  1.000 28.33794 ? 325 HOH B O   1 
HETATM 2883 O O   . HOH G 3 .   ? -7.777    20.725    1.310     1.000 27.86854 ? 326 HOH B O   1 
HETATM 2884 O O   . HOH G 3 .   ? -14.75600 34.11600  -24.94600 1.000 48.32107 ? 327 HOH B O   1 
HETATM 2885 O O   . HOH G 3 .   ? -18.84100 27.96300  -13.54800 1.000 26.23124 ? 328 HOH B O   1 
HETATM 2886 O O   . HOH G 3 .   ? -16.91100 14.39400  -29.53500 1.000 49.99914 ? 329 HOH B O   1 
HETATM 2887 O O   . HOH G 3 .   ? -2.30600  16.61100  -3.92600  1.000 35.40482 ? 330 HOH B O   1 
HETATM 2888 O O   . HOH G 3 .   ? 4.14200   24.84800  -0.57300  1.000 33.14429 ? 331 HOH B O   1 
HETATM 2889 O O   . HOH G 3 .   ? -0.15200  20.46000  -10.60600 1.000 12.26549 ? 332 HOH B O   1 
HETATM 2890 O O   . HOH G 3 .   ? -0.01900  14.60600  -12.95600 1.000 11.88157 ? 333 HOH B O   1 
HETATM 2891 O O   . HOH G 3 .   ? 0.15000   24.42600  -11.87100 1.000 17.80758 ? 334 HOH B O   1 
HETATM 2892 O O   . HOH G 3 .   ? 1.80600   32.16400  -15.95500 1.000 31.44075 ? 335 HOH B O   1 
HETATM 2893 O O   . HOH G 3 .   ? -6.66600  22.13200  -37.23400 1.000 25.95485 ? 336 HOH B O   1 
HETATM 2894 O O   . HOH G 3 .   ? 7.28600   23.11300  -3.66000  1.000 25.50777 ? 337 HOH B O   1 
HETATM 2895 O O   . HOH G 3 .   ? -7.88800  38.70100  -15.95600 1.000 34.55894 ? 338 HOH B O   1 
HETATM 2896 O O   . HOH G 3 .   ? -1.98700  17.08000  -30.74300 1.000 28.82447 ? 339 HOH B O   1 
HETATM 2897 O O   . HOH G 3 .   ? 16.47100  30.91400  -14.47800 1.000 33.76565 ? 340 HOH B O   1 
HETATM 2898 O O   . HOH G 3 .   ? 0.14900   24.63400  -1.82400  1.000 28.60785 ? 341 HOH B O   1 
HETATM 2899 O O   . HOH G 3 .   ? 4.33900   33.88700  -8.28400  1.000 37.23076 ? 342 HOH B O   1 
HETATM 2900 O O   . HOH G 3 .   ? -10.88500 11.49100  -34.73700 1.000 27.82560 ? 343 HOH B O   1 
HETATM 2901 O O   . HOH G 3 .   ? -10.50400 26.81300  -39.15000 1.000 27.38910 ? 344 HOH B O   1 
HETATM 2902 O O   . HOH G 3 .   ? 10.86500  32.82400  -6.45000  1.000 33.87547 ? 345 HOH B O   1 
HETATM 2903 O O   . HOH G 3 .   ? -10.56700 29.19000  -4.42400  1.000 37.82116 ? 346 HOH B O   1 
HETATM 2904 O O   . HOH G 3 .   ? -4.58100  36.40400  -9.98700  1.000 36.20660 ? 347 HOH B O   1 
HETATM 2905 O O   . HOH G 3 .   ? -19.69400 26.15700  -7.19300  1.000 37.02893 ? 348 HOH B O   1 
HETATM 2906 O O   . HOH G 3 .   ? 1.84500   32.60000  -8.51800  1.000 34.72383 ? 349 HOH B O   1 
HETATM 2907 O O   . HOH G 3 .   ? -17.32700 31.12500  -15.45500 1.000 32.59775 ? 350 HOH B O   1 
HETATM 2908 O O   . HOH G 3 .   ? -16.24900 12.38100  -26.79900 1.000 44.02415 ? 351 HOH B O   1 
HETATM 2909 O O   . HOH G 3 .   ? 1.83700   23.26700  -0.22600  1.000 38.56692 ? 352 HOH B O   1 
HETATM 2910 O O   . HOH G 3 .   ? -18.10600 30.54700  -12.88000 1.000 38.93808 ? 353 HOH B O   1 
HETATM 2911 O O   . HOH G 3 .   ? -20.19100 28.44400  -11.12400 1.000 37.13896 ? 354 HOH B O   1 
HETATM 2912 O O   . HOH H 3 .   ? 4.33100   8.03800   -10.08100 1.000 23.16827 ? 301 HOH C O   1 
HETATM 2913 O O   . HOH H 3 .   ? 1.51000   -5.46900  -27.03800 1.000 49.42282 ? 302 HOH C O   1 
HETATM 2914 O O   . HOH H 3 .   ? -2.62100  -7.90100  -19.84700 1.000 26.72069 ? 303 HOH C O   1 
HETATM 2915 O O   . HOH H 3 .   ? 1.52900   14.15500  -9.66900  1.000 23.84867 ? 304 HOH C O   1 
HETATM 2916 O O   . HOH H 3 .   ? -0.50400  12.79100  -19.31800 1.000 24.47595 ? 305 HOH C O   1 
HETATM 2917 O O   . HOH H 3 .   ? 8.28200   -8.96100  -27.05700 1.000 51.89376 ? 306 HOH C O   1 
HETATM 2918 O O   . HOH H 3 .   ? -9.29300  5.82300   -8.93400  1.000 21.08437 ? 307 HOH C O   1 
HETATM 2919 O O   . HOH H 3 .   ? -6.79700  2.89400   -33.27400 1.000 25.57756 ? 308 HOH C O   1 
HETATM 2920 O O   . HOH H 3 .   ? -1.74400  8.49200   -35.60300 1.000 38.60011 ? 309 HOH C O   1 
HETATM 2921 O O   . HOH H 3 .   ? 1.91400   3.91100   -32.87900 1.000 17.37125 ? 310 HOH C O   1 
HETATM 2922 O O   . HOH H 3 .   ? -9.34600  11.70500  -7.74800  1.000 17.21243 ? 311 HOH C O   1 
HETATM 2923 O O   . HOH H 3 .   ? -10.54400 8.77800   -9.79000  1.000 24.67184 ? 312 HOH C O   1 
HETATM 2924 O O   . HOH H 3 .   ? -13.22800 9.24100   -9.68500  1.000 29.99044 ? 313 HOH C O   1 
HETATM 2925 O O   . HOH H 3 .   ? -12.27500 12.01600  -7.78700  1.000 17.59413 ? 314 HOH C O   1 
HETATM 2926 O O   . HOH H 3 .   ? -2.10100  12.31500  -26.38900 1.000 22.83900 ? 315 HOH C O   1 
HETATM 2927 O O   . HOH H 3 .   ? -0.41500  5.94300   -2.18600  1.000 39.54918 ? 316 HOH C O   1 
HETATM 2928 O O   . HOH H 3 .   ? 0.63200   2.40200   -2.64600  1.000 25.86674 ? 317 HOH C O   1 
HETATM 2929 O O   . HOH H 3 .   ? -1.56200  14.12500  -4.44400  1.000 36.25912 ? 318 HOH C O   1 
HETATM 2930 O O   . HOH H 3 .   ? -4.65100  4.55200   -5.82500  1.000 19.51021 ? 319 HOH C O   1 
HETATM 2931 O O   . HOH H 3 .   ? 11.24800  14.21200  -34.63100 1.000 22.52277 ? 320 HOH C O   1 
HETATM 2932 O O   . HOH H 3 .   ? -2.26000  2.08600   -1.63800  1.000 29.33277 ? 321 HOH C O   1 
HETATM 2933 O O   . HOH H 3 .   ? -1.329    4.609     1.268     1.000 27.77333 ? 322 HOH C O   1 
HETATM 2934 O O   . HOH H 3 .   ? -20.84200 17.82400  -8.09400  1.000 25.93186 ? 323 HOH C O   1 
HETATM 2935 O O   . HOH H 3 .   ? -0.58900  -4.04600  -36.96300 1.000 33.91859 ? 324 HOH C O   1 
HETATM 2936 O O   . HOH H 3 .   ? -5.00600  11.55100  -10.64700 1.000 11.93680 ? 325 HOH C O   1 
HETATM 2937 O O   . HOH H 3 .   ? -3.16000  5.15400   -37.20000 1.000 30.69765 ? 326 HOH C O   1 
HETATM 2938 O O   . HOH H 3 .   ? 1.07100   -2.19000  -36.18100 1.000 25.14039 ? 327 HOH C O   1 
HETATM 2939 O O   . HOH H 3 .   ? 5.55100   -1.38000  -15.93100 1.000 16.57675 ? 328 HOH C O   1 
HETATM 2940 O O   . HOH H 3 .   ? -10.81000 16.65000  -3.61700  1.000 25.58939 ? 329 HOH C O   1 
HETATM 2941 O O   . HOH H 3 .   ? -10.97900 13.42800  -0.47000  1.000 36.03253 ? 330 HOH C O   1 
HETATM 2942 O O   . HOH H 3 .   ? -16.25300 -0.27400  -9.95100  1.000 37.56058 ? 331 HOH C O   1 
HETATM 2943 O O   . HOH H 3 .   ? -2.27300  -8.46500  -13.47100 1.000 26.70059 ? 332 HOH C O   1 
HETATM 2944 O O   . HOH H 3 .   ? -8.62300  9.83000   -11.87500 1.000 18.13751 ? 333 HOH C O   1 
HETATM 2945 O O   . HOH H 3 .   ? -21.83100 10.96800  -11.90600 1.000 32.30309 ? 334 HOH C O   1 
HETATM 2946 O O   . HOH H 3 .   ? -22.22300 20.79900  -14.57400 1.000 35.19881 ? 335 HOH C O   1 
HETATM 2947 O O   . HOH H 3 .   ? -5.85600  -8.57200  -15.74200 1.000 33.57888 ? 336 HOH C O   1 
HETATM 2948 O O   . HOH H 3 .   ? 5.26600   -0.46300  -37.82500 1.000 26.58066 ? 337 HOH C O   1 
HETATM 2949 O O   . HOH H 3 .   ? -16.27100 7.11100   -16.08500 1.000 30.65272 ? 338 HOH C O   1 
HETATM 2950 O O   . HOH H 3 .   ? 6.14800   2.97500   -28.10300 1.000 25.41788 ? 339 HOH C O   1 
HETATM 2951 O O   . HOH H 3 .   ? 3.92700   -2.25400  -35.93200 1.000 39.68436 ? 340 HOH C O   1 
HETATM 2952 O O   . HOH H 3 .   ? 8.09200   6.63500   -34.61400 1.000 25.53303 ? 341 HOH C O   1 
HETATM 2953 O O   . HOH H 3 .   ? -18.85300 8.69400   -8.35200  1.000 34.62963 ? 342 HOH C O   1 
HETATM 2954 O O   . HOH H 3 .   ? -21.18800 15.13300  -6.55200  1.000 34.27178 ? 343 HOH C O   1 
HETATM 2955 O O   . HOH H 3 .   ? -8.82300  10.21400  -1.33500  1.000 30.77919 ? 344 HOH C O   1 
HETATM 2956 O O   . HOH H 3 .   ? -16.50300 7.18400   -8.43900  1.000 34.66695 ? 345 HOH C O   1 
HETATM 2957 O O   . HOH H 3 .   ? 6.38300   9.47200   -9.95300  1.000 16.88542 ? 346 HOH C O   1 
HETATM 2958 O O   . HOH H 3 .   ? -7.67100  11.56600  -9.91400  1.000 17.28549 ? 347 HOH C O   1 
HETATM 2959 O O   . HOH H 3 .   ? 9.85100   1.79800   -26.80900 1.000 42.92611 ? 348 HOH C O   1 
HETATM 2960 O O   . HOH H 3 .   ? -5.05900  -9.04100  -13.14800 1.000 36.72483 ? 349 HOH C O   1 
HETATM 2961 O O   . HOH H 3 .   ? -3.55500  7.78300   -37.49000 1.000 47.42022 ? 350 HOH C O   1 
HETATM 2962 O O   . HOH H 3 .   ? -1.62100  -9.93300  -11.19500 1.000 38.53446 ? 351 HOH C O   1 
# 
