data_9KBQ
# 
_entry.id   9KBQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9KBQ         pdb_00009kbq 10.2210/pdb9kbq/pdb 
WWPDB D_1300053241 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        9KBQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              fenhu@fjmu.edu.cn 
_pdbx_contact_author.name_first         fen 
_pdbx_contact_author.name_last          hu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2349-5336 
# 
_audit_author.name               'Hu, F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2349-5336 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of PHAb10, a peptidoglycan hydrolase with thermal stability and broad-spectrum' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Hu, F.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0003-2349-5336 
# 
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 Lysozyme 16539.961 2   3.2.1.17 ? ? ? 
2 water   nat water    18.015    260 ?        ? ? ? 
# 
_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       
;MSKTTSNAGLNLIKGFEGKRLNAYDDGVGVWTIGFGTIKYPNGVRVKKGDTCTEQQAETYLKNDLTKFEVAINKLVKVSL
TQNQFDALASFTYNLGETNLANSTLLKKLNKGDYQGAADQFLVWNKAGGKVMKGLVRRREAERALFLKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKTTSNAGLNLIKGFEGKRLNAYDDGVGVWTIGFGTIKYPNGVRVKKGDTCTEQQAETYLKNDLTKFEVAINKLVKVSL
TQNQFDALASFTYNLGETNLANSTLLKKLNKGDYQGAADQFLVWNKAGGKVMKGLVRRREAERALFLKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   THR n 
1 5   THR n 
1 6   SER n 
1 7   ASN n 
1 8   ALA n 
1 9   GLY n 
1 10  LEU n 
1 11  ASN n 
1 12  LEU n 
1 13  ILE n 
1 14  LYS n 
1 15  GLY n 
1 16  PHE n 
1 17  GLU n 
1 18  GLY n 
1 19  LYS n 
1 20  ARG n 
1 21  LEU n 
1 22  ASN n 
1 23  ALA n 
1 24  TYR n 
1 25  ASP n 
1 26  ASP n 
1 27  GLY n 
1 28  VAL n 
1 29  GLY n 
1 30  VAL n 
1 31  TRP n 
1 32  THR n 
1 33  ILE n 
1 34  GLY n 
1 35  PHE n 
1 36  GLY n 
1 37  THR n 
1 38  ILE n 
1 39  LYS n 
1 40  TYR n 
1 41  PRO n 
1 42  ASN n 
1 43  GLY n 
1 44  VAL n 
1 45  ARG n 
1 46  VAL n 
1 47  LYS n 
1 48  LYS n 
1 49  GLY n 
1 50  ASP n 
1 51  THR n 
1 52  CYS n 
1 53  THR n 
1 54  GLU n 
1 55  GLN n 
1 56  GLN n 
1 57  ALA n 
1 58  GLU n 
1 59  THR n 
1 60  TYR n 
1 61  LEU n 
1 62  LYS n 
1 63  ASN n 
1 64  ASP n 
1 65  LEU n 
1 66  THR n 
1 67  LYS n 
1 68  PHE n 
1 69  GLU n 
1 70  VAL n 
1 71  ALA n 
1 72  ILE n 
1 73  ASN n 
1 74  LYS n 
1 75  LEU n 
1 76  VAL n 
1 77  LYS n 
1 78  VAL n 
1 79  SER n 
1 80  LEU n 
1 81  THR n 
1 82  GLN n 
1 83  ASN n 
1 84  GLN n 
1 85  PHE n 
1 86  ASP n 
1 87  ALA n 
1 88  LEU n 
1 89  ALA n 
1 90  SER n 
1 91  PHE n 
1 92  THR n 
1 93  TYR n 
1 94  ASN n 
1 95  LEU n 
1 96  GLY n 
1 97  GLU n 
1 98  THR n 
1 99  ASN n 
1 100 LEU n 
1 101 ALA n 
1 102 ASN n 
1 103 SER n 
1 104 THR n 
1 105 LEU n 
1 106 LEU n 
1 107 LYS n 
1 108 LYS n 
1 109 LEU n 
1 110 ASN n 
1 111 LYS n 
1 112 GLY n 
1 113 ASP n 
1 114 TYR n 
1 115 GLN n 
1 116 GLY n 
1 117 ALA n 
1 118 ALA n 
1 119 ASP n 
1 120 GLN n 
1 121 PHE n 
1 122 LEU n 
1 123 VAL n 
1 124 TRP n 
1 125 ASN n 
1 126 LYS n 
1 127 ALA n 
1 128 GLY n 
1 129 GLY n 
1 130 LYS n 
1 131 VAL n 
1 132 MET n 
1 133 LYS n 
1 134 GLY n 
1 135 LEU n 
1 136 VAL n 
1 137 ARG n 
1 138 ARG n 
1 139 ARG n 
1 140 GLU n 
1 141 ALA n 
1 142 GLU n 
1 143 ARG n 
1 144 ALA n 
1 145 LEU n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 LYS 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                   149 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FJU42_09780 
_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      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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   MET 1   21  ?   ?   ?   A . n 
A 1 2   SER 2   22  22  SER SER A . n 
A 1 3   LYS 3   23  23  LYS LYS A . n 
A 1 4   THR 4   24  24  THR THR A . n 
A 1 5   THR 5   25  25  THR THR A . n 
A 1 6   SER 6   26  26  SER SER A . n 
A 1 7   ASN 7   27  27  ASN ASN A . n 
A 1 8   ALA 8   28  28  ALA ALA A . n 
A 1 9   GLY 9   29  29  GLY GLY A . n 
A 1 10  LEU 10  30  30  LEU LEU A . n 
A 1 11  ASN 11  31  31  ASN ASN A . n 
A 1 12  LEU 12  32  32  LEU LEU A . n 
A 1 13  ILE 13  33  33  ILE ILE A . n 
A 1 14  LYS 14  34  34  LYS LYS A . n 
A 1 15  GLY 15  35  35  GLY GLY A . n 
A 1 16  PHE 16  36  36  PHE PHE A . n 
A 1 17  GLU 17  37  37  GLU GLU A . n 
A 1 18  GLY 18  38  38  GLY GLY A . n 
A 1 19  LYS 19  39  39  LYS LYS A . n 
A 1 20  ARG 20  40  40  ARG ARG A . n 
A 1 21  LEU 21  41  41  LEU LEU A . n 
A 1 22  ASN 22  42  42  ASN ASN A . n 
A 1 23  ALA 23  43  43  ALA ALA A . n 
A 1 24  TYR 24  44  44  TYR TYR A . n 
A 1 25  ASP 25  45  45  ASP ASP A . n 
A 1 26  ASP 26  46  46  ASP ASP A . n 
A 1 27  GLY 27  47  47  GLY GLY A . n 
A 1 28  VAL 28  48  48  VAL VAL A . n 
A 1 29  GLY 29  49  49  GLY GLY A . n 
A 1 30  VAL 30  50  50  VAL VAL A . n 
A 1 31  TRP 31  51  51  TRP TRP A . n 
A 1 32  THR 32  52  52  THR THR A . n 
A 1 33  ILE 33  53  53  ILE ILE A . n 
A 1 34  GLY 34  54  54  GLY GLY A . n 
A 1 35  PHE 35  55  55  PHE PHE A . n 
A 1 36  GLY 36  56  56  GLY GLY A . n 
A 1 37  THR 37  57  57  THR THR A . n 
A 1 38  ILE 38  58  58  ILE ILE A . n 
A 1 39  LYS 39  59  59  LYS LYS A . n 
A 1 40  TYR 40  60  60  TYR TYR A . n 
A 1 41  PRO 41  61  61  PRO PRO A . n 
A 1 42  ASN 42  62  62  ASN ASN A . n 
A 1 43  GLY 43  63  63  GLY GLY A . n 
A 1 44  VAL 44  64  64  VAL VAL A . n 
A 1 45  ARG 45  65  65  ARG ARG A . n 
A 1 46  VAL 46  66  66  VAL VAL A . n 
A 1 47  LYS 47  67  67  LYS LYS A . n 
A 1 48  LYS 48  68  68  LYS LYS A . n 
A 1 49  GLY 49  69  69  GLY GLY A . n 
A 1 50  ASP 50  70  70  ASP ASP A . n 
A 1 51  THR 51  71  71  THR THR A . n 
A 1 52  CYS 52  72  72  CYS CYS A . n 
A 1 53  THR 53  73  73  THR THR A . n 
A 1 54  GLU 54  74  74  GLU GLU A . n 
A 1 55  GLN 55  75  75  GLN GLN A . n 
A 1 56  GLN 56  76  76  GLN GLN A . n 
A 1 57  ALA 57  77  77  ALA ALA A . n 
A 1 58  GLU 58  78  78  GLU GLU A . n 
A 1 59  THR 59  79  79  THR THR A . n 
A 1 60  TYR 60  80  80  TYR TYR A . n 
A 1 61  LEU 61  81  81  LEU LEU A . n 
A 1 62  LYS 62  82  82  LYS LYS A . n 
A 1 63  ASN 63  83  83  ASN ASN A . n 
A 1 64  ASP 64  84  84  ASP ASP A . n 
A 1 65  LEU 65  85  85  LEU LEU A . n 
A 1 66  THR 66  86  86  THR THR A . n 
A 1 67  LYS 67  87  87  LYS LYS A . n 
A 1 68  PHE 68  88  88  PHE PHE A . n 
A 1 69  GLU 69  89  89  GLU GLU A . n 
A 1 70  VAL 70  90  90  VAL VAL A . n 
A 1 71  ALA 71  91  91  ALA ALA A . n 
A 1 72  ILE 72  92  92  ILE ILE A . n 
A 1 73  ASN 73  93  93  ASN ASN A . n 
A 1 74  LYS 74  94  94  LYS LYS A . n 
A 1 75  LEU 75  95  95  LEU LEU A . n 
A 1 76  VAL 76  96  96  VAL VAL A . n 
A 1 77  LYS 77  97  97  LYS LYS A . n 
A 1 78  VAL 78  98  98  VAL VAL A . n 
A 1 79  SER 79  99  99  SER SER A . n 
A 1 80  LEU 80  100 100 LEU LEU A . n 
A 1 81  THR 81  101 101 THR THR A . n 
A 1 82  GLN 82  102 102 GLN GLN A . n 
A 1 83  ASN 83  103 103 ASN ASN A . n 
A 1 84  GLN 84  104 104 GLN GLN A . n 
A 1 85  PHE 85  105 105 PHE PHE A . n 
A 1 86  ASP 86  106 106 ASP ASP A . n 
A 1 87  ALA 87  107 107 ALA ALA A . n 
A 1 88  LEU 88  108 108 LEU LEU A . n 
A 1 89  ALA 89  109 109 ALA ALA A . n 
A 1 90  SER 90  110 110 SER SER A . n 
A 1 91  PHE 91  111 111 PHE PHE A . n 
A 1 92  THR 92  112 112 THR THR A . n 
A 1 93  TYR 93  113 113 TYR TYR A . n 
A 1 94  ASN 94  114 114 ASN ASN A . n 
A 1 95  LEU 95  115 115 LEU LEU A . n 
A 1 96  GLY 96  116 116 GLY GLY A . n 
A 1 97  GLU 97  117 117 GLU GLU A . n 
A 1 98  THR 98  118 118 THR THR A . n 
A 1 99  ASN 99  119 119 ASN ASN A . n 
A 1 100 LEU 100 120 120 LEU LEU A . n 
A 1 101 ALA 101 121 121 ALA ALA A . n 
A 1 102 ASN 102 122 122 ASN ASN A . n 
A 1 103 SER 103 123 123 SER SER A . n 
A 1 104 THR 104 124 124 THR THR A . n 
A 1 105 LEU 105 125 125 LEU LEU A . n 
A 1 106 LEU 106 126 126 LEU LEU A . n 
A 1 107 LYS 107 127 127 LYS LYS A . n 
A 1 108 LYS 108 128 128 LYS LYS A . n 
A 1 109 LEU 109 129 129 LEU LEU A . n 
A 1 110 ASN 110 130 130 ASN ASN A . n 
A 1 111 LYS 111 131 131 LYS LYS A . n 
A 1 112 GLY 112 132 132 GLY GLY A . n 
A 1 113 ASP 113 133 133 ASP ASP A . n 
A 1 114 TYR 114 134 134 TYR TYR A . n 
A 1 115 GLN 115 135 135 GLN GLN A . n 
A 1 116 GLY 116 136 136 GLY GLY A . n 
A 1 117 ALA 117 137 137 ALA ALA A . n 
A 1 118 ALA 118 138 138 ALA ALA A . n 
A 1 119 ASP 119 139 139 ASP ASP A . n 
A 1 120 GLN 120 140 140 GLN GLN A . n 
A 1 121 PHE 121 141 141 PHE PHE A . n 
A 1 122 LEU 122 142 142 LEU LEU A . n 
A 1 123 VAL 123 143 143 VAL VAL A . n 
A 1 124 TRP 124 144 144 TRP TRP A . n 
A 1 125 ASN 125 145 145 ASN ASN A . n 
A 1 126 LYS 126 146 146 LYS LYS A . n 
A 1 127 ALA 127 147 147 ALA ALA A . n 
A 1 128 GLY 128 148 148 GLY GLY A . n 
A 1 129 GLY 129 149 149 GLY GLY A . n 
A 1 130 LYS 130 150 150 LYS LYS A . n 
A 1 131 VAL 131 151 151 VAL VAL A . n 
A 1 132 MET 132 152 152 MET MET A . n 
A 1 133 LYS 133 153 153 LYS LYS A . n 
A 1 134 GLY 134 154 154 GLY GLY A . n 
A 1 135 LEU 135 155 155 LEU LEU A . n 
A 1 136 VAL 136 156 156 VAL VAL A . n 
A 1 137 ARG 137 157 157 ARG ARG A . n 
A 1 138 ARG 138 158 158 ARG ARG A . n 
A 1 139 ARG 139 159 159 ARG ARG A . n 
A 1 140 GLU 140 160 160 GLU GLU A . n 
A 1 141 ALA 141 161 161 ALA ALA A . n 
A 1 142 GLU 142 162 162 GLU GLU A . n 
A 1 143 ARG 143 163 163 ARG ARG A . n 
A 1 144 ALA 144 164 164 ALA ALA A . n 
A 1 145 LEU 145 165 165 LEU LEU A . n 
A 1 146 PHE 146 166 166 PHE PHE A . n 
A 1 147 LEU 147 167 167 LEU LEU A . n 
A 1 148 LYS 148 168 168 LYS LYS A . n 
A 1 149 LYS 149 169 ?   ?   ?   A . n 
B 1 1   MET 1   21  ?   ?   ?   B . n 
B 1 2   SER 2   22  22  SER SER B . n 
B 1 3   LYS 3   23  23  LYS LYS B . n 
B 1 4   THR 4   24  24  THR THR B . n 
B 1 5   THR 5   25  25  THR THR B . n 
B 1 6   SER 6   26  26  SER SER B . n 
B 1 7   ASN 7   27  27  ASN ASN B . n 
B 1 8   ALA 8   28  28  ALA ALA B . n 
B 1 9   GLY 9   29  29  GLY GLY B . n 
B 1 10  LEU 10  30  30  LEU LEU B . n 
B 1 11  ASN 11  31  31  ASN ASN B . n 
B 1 12  LEU 12  32  32  LEU LEU B . n 
B 1 13  ILE 13  33  33  ILE ILE B . n 
B 1 14  LYS 14  34  34  LYS LYS B . n 
B 1 15  GLY 15  35  35  GLY GLY B . n 
B 1 16  PHE 16  36  36  PHE PHE B . n 
B 1 17  GLU 17  37  37  GLU GLU B . n 
B 1 18  GLY 18  38  38  GLY GLY B . n 
B 1 19  LYS 19  39  39  LYS LYS B . n 
B 1 20  ARG 20  40  40  ARG ARG B . n 
B 1 21  LEU 21  41  41  LEU LEU B . n 
B 1 22  ASN 22  42  42  ASN ASN B . n 
B 1 23  ALA 23  43  43  ALA ALA B . n 
B 1 24  TYR 24  44  44  TYR TYR B . n 
B 1 25  ASP 25  45  45  ASP ASP B . n 
B 1 26  ASP 26  46  46  ASP ASP B . n 
B 1 27  GLY 27  47  47  GLY GLY B . n 
B 1 28  VAL 28  48  48  VAL VAL B . n 
B 1 29  GLY 29  49  49  GLY GLY B . n 
B 1 30  VAL 30  50  50  VAL VAL B . n 
B 1 31  TRP 31  51  51  TRP TRP B . n 
B 1 32  THR 32  52  52  THR THR B . n 
B 1 33  ILE 33  53  53  ILE ILE B . n 
B 1 34  GLY 34  54  54  GLY GLY B . n 
B 1 35  PHE 35  55  55  PHE PHE B . n 
B 1 36  GLY 36  56  56  GLY GLY B . n 
B 1 37  THR 37  57  57  THR THR B . n 
B 1 38  ILE 38  58  58  ILE ILE B . n 
B 1 39  LYS 39  59  59  LYS LYS B . n 
B 1 40  TYR 40  60  60  TYR TYR B . n 
B 1 41  PRO 41  61  61  PRO PRO B . n 
B 1 42  ASN 42  62  62  ASN ASN B . n 
B 1 43  GLY 43  63  63  GLY GLY B . n 
B 1 44  VAL 44  64  64  VAL VAL B . n 
B 1 45  ARG 45  65  65  ARG ARG B . n 
B 1 46  VAL 46  66  66  VAL VAL B . n 
B 1 47  LYS 47  67  67  LYS LYS B . n 
B 1 48  LYS 48  68  68  LYS LYS B . n 
B 1 49  GLY 49  69  69  GLY GLY B . n 
B 1 50  ASP 50  70  70  ASP ASP B . n 
B 1 51  THR 51  71  71  THR THR B . n 
B 1 52  CYS 52  72  72  CYS CYS B . n 
B 1 53  THR 53  73  73  THR THR B . n 
B 1 54  GLU 54  74  74  GLU GLU B . n 
B 1 55  GLN 55  75  75  GLN GLN B . n 
B 1 56  GLN 56  76  76  GLN GLN B . n 
B 1 57  ALA 57  77  77  ALA ALA B . n 
B 1 58  GLU 58  78  78  GLU GLU B . n 
B 1 59  THR 59  79  79  THR THR B . n 
B 1 60  TYR 60  80  80  TYR TYR B . n 
B 1 61  LEU 61  81  81  LEU LEU B . n 
B 1 62  LYS 62  82  82  LYS LYS B . n 
B 1 63  ASN 63  83  83  ASN ASN B . n 
B 1 64  ASP 64  84  84  ASP ASP B . n 
B 1 65  LEU 65  85  85  LEU LEU B . n 
B 1 66  THR 66  86  86  THR THR B . n 
B 1 67  LYS 67  87  87  LYS LYS B . n 
B 1 68  PHE 68  88  88  PHE PHE B . n 
B 1 69  GLU 69  89  89  GLU GLU B . n 
B 1 70  VAL 70  90  90  VAL VAL B . n 
B 1 71  ALA 71  91  91  ALA ALA B . n 
B 1 72  ILE 72  92  92  ILE ILE B . n 
B 1 73  ASN 73  93  93  ASN ASN B . n 
B 1 74  LYS 74  94  94  LYS LYS B . n 
B 1 75  LEU 75  95  95  LEU LEU B . n 
B 1 76  VAL 76  96  96  VAL VAL B . n 
B 1 77  LYS 77  97  97  LYS LYS B . n 
B 1 78  VAL 78  98  98  VAL VAL B . n 
B 1 79  SER 79  99  99  SER SER B . n 
B 1 80  LEU 80  100 100 LEU LEU B . n 
B 1 81  THR 81  101 101 THR THR B . n 
B 1 82  GLN 82  102 102 GLN GLN B . n 
B 1 83  ASN 83  103 103 ASN ASN B . n 
B 1 84  GLN 84  104 104 GLN GLN B . n 
B 1 85  PHE 85  105 105 PHE PHE B . n 
B 1 86  ASP 86  106 106 ASP ASP B . n 
B 1 87  ALA 87  107 107 ALA ALA B . n 
B 1 88  LEU 88  108 108 LEU LEU B . n 
B 1 89  ALA 89  109 109 ALA ALA B . n 
B 1 90  SER 90  110 110 SER SER B . n 
B 1 91  PHE 91  111 111 PHE PHE B . n 
B 1 92  THR 92  112 112 THR THR B . n 
B 1 93  TYR 93  113 113 TYR TYR B . n 
B 1 94  ASN 94  114 114 ASN ASN B . n 
B 1 95  LEU 95  115 115 LEU LEU B . n 
B 1 96  GLY 96  116 116 GLY GLY B . n 
B 1 97  GLU 97  117 117 GLU GLU B . n 
B 1 98  THR 98  118 118 THR THR B . n 
B 1 99  ASN 99  119 119 ASN ASN B . n 
B 1 100 LEU 100 120 120 LEU LEU B . n 
B 1 101 ALA 101 121 121 ALA ALA B . n 
B 1 102 ASN 102 122 122 ASN ASN B . n 
B 1 103 SER 103 123 123 SER SER B . n 
B 1 104 THR 104 124 124 THR THR B . n 
B 1 105 LEU 105 125 125 LEU LEU B . n 
B 1 106 LEU 106 126 126 LEU LEU B . n 
B 1 107 LYS 107 127 127 LYS LYS B . n 
B 1 108 LYS 108 128 128 LYS LYS B . n 
B 1 109 LEU 109 129 129 LEU LEU B . n 
B 1 110 ASN 110 130 130 ASN ASN B . n 
B 1 111 LYS 111 131 131 LYS LYS B . n 
B 1 112 GLY 112 132 132 GLY GLY B . n 
B 1 113 ASP 113 133 133 ASP ASP B . n 
B 1 114 TYR 114 134 134 TYR TYR B . n 
B 1 115 GLN 115 135 135 GLN GLN B . n 
B 1 116 GLY 116 136 136 GLY GLY B . n 
B 1 117 ALA 117 137 137 ALA ALA B . n 
B 1 118 ALA 118 138 138 ALA ALA B . n 
B 1 119 ASP 119 139 139 ASP ASP B . n 
B 1 120 GLN 120 140 140 GLN GLN B . n 
B 1 121 PHE 121 141 141 PHE PHE B . n 
B 1 122 LEU 122 142 142 LEU LEU B . n 
B 1 123 VAL 123 143 143 VAL VAL B . n 
B 1 124 TRP 124 144 144 TRP TRP B . n 
B 1 125 ASN 125 145 145 ASN ASN B . n 
B 1 126 LYS 126 146 146 LYS LYS B . n 
B 1 127 ALA 127 147 147 ALA ALA B . n 
B 1 128 GLY 128 148 148 GLY GLY B . n 
B 1 129 GLY 129 149 149 GLY GLY B . n 
B 1 130 LYS 130 150 150 LYS LYS B . n 
B 1 131 VAL 131 151 151 VAL VAL B . n 
B 1 132 MET 132 152 152 MET MET B . n 
B 1 133 LYS 133 153 153 LYS LYS B . n 
B 1 134 GLY 134 154 154 GLY GLY B . n 
B 1 135 LEU 135 155 155 LEU LEU B . n 
B 1 136 VAL 136 156 156 VAL VAL B . n 
B 1 137 ARG 137 157 157 ARG ARG B . n 
B 1 138 ARG 138 158 158 ARG ARG B . n 
B 1 139 ARG 139 159 159 ARG ARG B . n 
B 1 140 GLU 140 160 160 GLU GLU B . n 
B 1 141 ALA 141 161 161 ALA ALA B . n 
B 1 142 GLU 142 162 162 GLU GLU B . n 
B 1 143 ARG 143 163 163 ARG ARG B . n 
B 1 144 ALA 144 164 164 ALA ALA B . n 
B 1 145 LEU 145 165 165 LEU LEU B . n 
B 1 146 PHE 146 166 166 PHE PHE B . n 
B 1 147 LEU 147 167 167 LEU LEU B . n 
B 1 148 LYS 148 168 168 LYS LYS B . n 
B 1 149 LYS 149 169 ?   ?   ?   B . 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 
C 2 HOH 1   201 11  HOH HOH A . 
C 2 HOH 2   202 121 HOH HOH A . 
C 2 HOH 3   203 142 HOH HOH A . 
C 2 HOH 4   204 250 HOH HOH A . 
C 2 HOH 5   205 145 HOH HOH A . 
C 2 HOH 6   206 254 HOH HOH A . 
C 2 HOH 7   207 70  HOH HOH A . 
C 2 HOH 8   208 68  HOH HOH A . 
C 2 HOH 9   209 152 HOH HOH A . 
C 2 HOH 10  210 15  HOH HOH A . 
C 2 HOH 11  211 69  HOH HOH A . 
C 2 HOH 12  212 51  HOH HOH A . 
C 2 HOH 13  213 52  HOH HOH A . 
C 2 HOH 14  214 93  HOH HOH A . 
C 2 HOH 15  215 3   HOH HOH A . 
C 2 HOH 16  216 46  HOH HOH A . 
C 2 HOH 17  217 190 HOH HOH A . 
C 2 HOH 18  218 5   HOH HOH A . 
C 2 HOH 19  219 4   HOH HOH A . 
C 2 HOH 20  220 140 HOH HOH A . 
C 2 HOH 21  221 130 HOH HOH A . 
C 2 HOH 22  222 16  HOH HOH A . 
C 2 HOH 23  223 114 HOH HOH A . 
C 2 HOH 24  224 235 HOH HOH A . 
C 2 HOH 25  225 17  HOH HOH A . 
C 2 HOH 26  226 61  HOH HOH A . 
C 2 HOH 27  227 243 HOH HOH A . 
C 2 HOH 28  228 63  HOH HOH A . 
C 2 HOH 29  229 74  HOH HOH A . 
C 2 HOH 30  230 49  HOH HOH A . 
C 2 HOH 31  231 2   HOH HOH A . 
C 2 HOH 32  232 33  HOH HOH A . 
C 2 HOH 33  233 30  HOH HOH A . 
C 2 HOH 34  234 126 HOH HOH A . 
C 2 HOH 35  235 24  HOH HOH A . 
C 2 HOH 36  236 60  HOH HOH A . 
C 2 HOH 37  237 27  HOH HOH A . 
C 2 HOH 38  238 29  HOH HOH A . 
C 2 HOH 39  239 80  HOH HOH A . 
C 2 HOH 40  240 54  HOH HOH A . 
C 2 HOH 41  241 182 HOH HOH A . 
C 2 HOH 42  242 178 HOH HOH A . 
C 2 HOH 43  243 198 HOH HOH A . 
C 2 HOH 44  244 84  HOH HOH A . 
C 2 HOH 45  245 100 HOH HOH A . 
C 2 HOH 46  246 242 HOH HOH A . 
C 2 HOH 47  247 66  HOH HOH A . 
C 2 HOH 48  248 171 HOH HOH A . 
C 2 HOH 49  249 88  HOH HOH A . 
C 2 HOH 50  250 101 HOH HOH A . 
C 2 HOH 51  251 210 HOH HOH A . 
C 2 HOH 52  252 65  HOH HOH A . 
C 2 HOH 53  253 118 HOH HOH A . 
C 2 HOH 54  254 18  HOH HOH A . 
C 2 HOH 55  255 113 HOH HOH A . 
C 2 HOH 56  256 143 HOH HOH A . 
C 2 HOH 57  257 90  HOH HOH A . 
C 2 HOH 58  258 6   HOH HOH A . 
C 2 HOH 59  259 96  HOH HOH A . 
C 2 HOH 60  260 141 HOH HOH A . 
C 2 HOH 61  261 119 HOH HOH A . 
C 2 HOH 62  262 155 HOH HOH A . 
C 2 HOH 63  263 123 HOH HOH A . 
C 2 HOH 64  264 99  HOH HOH A . 
C 2 HOH 65  265 120 HOH HOH A . 
C 2 HOH 66  266 127 HOH HOH A . 
C 2 HOH 67  267 13  HOH HOH A . 
C 2 HOH 68  268 168 HOH HOH A . 
C 2 HOH 69  269 122 HOH HOH A . 
C 2 HOH 70  270 26  HOH HOH A . 
C 2 HOH 71  271 111 HOH HOH A . 
C 2 HOH 72  272 137 HOH HOH A . 
C 2 HOH 73  273 50  HOH HOH A . 
C 2 HOH 74  274 44  HOH HOH A . 
C 2 HOH 75  275 222 HOH HOH A . 
C 2 HOH 76  276 14  HOH HOH A . 
C 2 HOH 77  277 34  HOH HOH A . 
C 2 HOH 78  278 57  HOH HOH A . 
C 2 HOH 79  279 45  HOH HOH A . 
C 2 HOH 80  280 92  HOH HOH A . 
C 2 HOH 81  281 205 HOH HOH A . 
C 2 HOH 82  282 55  HOH HOH A . 
C 2 HOH 83  283 234 HOH HOH A . 
C 2 HOH 84  284 208 HOH HOH A . 
C 2 HOH 85  285 9   HOH HOH A . 
C 2 HOH 86  286 37  HOH HOH A . 
C 2 HOH 87  287 267 HOH HOH A . 
C 2 HOH 88  288 85  HOH HOH A . 
C 2 HOH 89  289 244 HOH HOH A . 
C 2 HOH 90  290 135 HOH HOH A . 
C 2 HOH 91  291 95  HOH HOH A . 
C 2 HOH 92  292 236 HOH HOH A . 
C 2 HOH 93  293 270 HOH HOH A . 
C 2 HOH 94  294 149 HOH HOH A . 
C 2 HOH 95  295 220 HOH HOH A . 
C 2 HOH 96  296 224 HOH HOH A . 
C 2 HOH 97  297 184 HOH HOH A . 
C 2 HOH 98  298 251 HOH HOH A . 
C 2 HOH 99  299 173 HOH HOH A . 
C 2 HOH 100 300 229 HOH HOH A . 
C 2 HOH 101 301 105 HOH HOH A . 
C 2 HOH 102 302 116 HOH HOH A . 
C 2 HOH 103 303 150 HOH HOH A . 
C 2 HOH 104 304 203 HOH HOH A . 
C 2 HOH 105 305 72  HOH HOH A . 
C 2 HOH 106 306 239 HOH HOH A . 
C 2 HOH 107 307 188 HOH HOH A . 
C 2 HOH 108 308 217 HOH HOH A . 
C 2 HOH 109 309 261 HOH HOH A . 
C 2 HOH 110 310 199 HOH HOH A . 
C 2 HOH 111 311 266 HOH HOH A . 
C 2 HOH 112 312 157 HOH HOH A . 
C 2 HOH 113 313 172 HOH HOH A . 
C 2 HOH 114 314 76  HOH HOH A . 
C 2 HOH 115 315 102 HOH HOH A . 
C 2 HOH 116 316 89  HOH HOH A . 
C 2 HOH 117 317 259 HOH HOH A . 
C 2 HOH 118 318 82  HOH HOH A . 
C 2 HOH 119 319 240 HOH HOH A . 
C 2 HOH 120 320 249 HOH HOH A . 
C 2 HOH 121 321 138 HOH HOH A . 
C 2 HOH 122 322 257 HOH HOH A . 
C 2 HOH 123 323 59  HOH HOH A . 
C 2 HOH 124 324 158 HOH HOH A . 
C 2 HOH 125 325 98  HOH HOH A . 
C 2 HOH 126 326 196 HOH HOH A . 
C 2 HOH 127 327 253 HOH HOH A . 
C 2 HOH 128 328 128 HOH HOH A . 
C 2 HOH 129 329 204 HOH HOH A . 
C 2 HOH 130 330 148 HOH HOH A . 
C 2 HOH 131 331 218 HOH HOH A . 
C 2 HOH 132 332 156 HOH HOH A . 
C 2 HOH 133 333 151 HOH HOH A . 
C 2 HOH 134 334 212 HOH HOH A . 
C 2 HOH 135 335 237 HOH HOH A . 
C 2 HOH 136 336 207 HOH HOH A . 
C 2 HOH 137 337 233 HOH HOH A . 
C 2 HOH 138 338 245 HOH HOH A . 
C 2 HOH 139 339 227 HOH HOH A . 
C 2 HOH 140 340 269 HOH HOH A . 
D 2 HOH 1   201 248 HOH HOH B . 
D 2 HOH 2   202 175 HOH HOH B . 
D 2 HOH 3   203 83  HOH HOH B . 
D 2 HOH 4   204 226 HOH HOH B . 
D 2 HOH 5   205 163 HOH HOH B . 
D 2 HOH 6   206 73  HOH HOH B . 
D 2 HOH 7   207 35  HOH HOH B . 
D 2 HOH 8   208 58  HOH HOH B . 
D 2 HOH 9   209 7   HOH HOH B . 
D 2 HOH 10  210 112 HOH HOH B . 
D 2 HOH 11  211 215 HOH HOH B . 
D 2 HOH 12  212 20  HOH HOH B . 
D 2 HOH 13  213 10  HOH HOH B . 
D 2 HOH 14  214 183 HOH HOH B . 
D 2 HOH 15  215 106 HOH HOH B . 
D 2 HOH 16  216 147 HOH HOH B . 
D 2 HOH 17  217 97  HOH HOH B . 
D 2 HOH 18  218 8   HOH HOH B . 
D 2 HOH 19  219 41  HOH HOH B . 
D 2 HOH 20  220 139 HOH HOH B . 
D 2 HOH 21  221 136 HOH HOH B . 
D 2 HOH 22  222 21  HOH HOH B . 
D 2 HOH 23  223 28  HOH HOH B . 
D 2 HOH 24  224 117 HOH HOH B . 
D 2 HOH 25  225 109 HOH HOH B . 
D 2 HOH 26  226 67  HOH HOH B . 
D 2 HOH 27  227 75  HOH HOH B . 
D 2 HOH 28  228 47  HOH HOH B . 
D 2 HOH 29  229 189 HOH HOH B . 
D 2 HOH 30  230 132 HOH HOH B . 
D 2 HOH 31  231 87  HOH HOH B . 
D 2 HOH 32  232 22  HOH HOH B . 
D 2 HOH 33  233 197 HOH HOH B . 
D 2 HOH 34  234 25  HOH HOH B . 
D 2 HOH 35  235 144 HOH HOH B . 
D 2 HOH 36  236 39  HOH HOH B . 
D 2 HOH 37  237 31  HOH HOH B . 
D 2 HOH 38  238 164 HOH HOH B . 
D 2 HOH 39  239 103 HOH HOH B . 
D 2 HOH 40  240 23  HOH HOH B . 
D 2 HOH 41  241 107 HOH HOH B . 
D 2 HOH 42  242 134 HOH HOH B . 
D 2 HOH 43  243 81  HOH HOH B . 
D 2 HOH 44  244 202 HOH HOH B . 
D 2 HOH 45  245 241 HOH HOH B . 
D 2 HOH 46  246 94  HOH HOH B . 
D 2 HOH 47  247 1   HOH HOH B . 
D 2 HOH 48  248 162 HOH HOH B . 
D 2 HOH 49  249 165 HOH HOH B . 
D 2 HOH 50  250 186 HOH HOH B . 
D 2 HOH 51  251 260 HOH HOH B . 
D 2 HOH 52  252 79  HOH HOH B . 
D 2 HOH 53  253 160 HOH HOH B . 
D 2 HOH 54  254 38  HOH HOH B . 
D 2 HOH 55  255 48  HOH HOH B . 
D 2 HOH 56  256 124 HOH HOH B . 
D 2 HOH 57  257 32  HOH HOH B . 
D 2 HOH 58  258 225 HOH HOH B . 
D 2 HOH 59  259 179 HOH HOH B . 
D 2 HOH 60  260 264 HOH HOH B . 
D 2 HOH 61  261 12  HOH HOH B . 
D 2 HOH 62  262 104 HOH HOH B . 
D 2 HOH 63  263 64  HOH HOH B . 
D 2 HOH 64  264 214 HOH HOH B . 
D 2 HOH 65  265 181 HOH HOH B . 
D 2 HOH 66  266 108 HOH HOH B . 
D 2 HOH 67  267 131 HOH HOH B . 
D 2 HOH 68  268 258 HOH HOH B . 
D 2 HOH 69  269 36  HOH HOH B . 
D 2 HOH 70  270 77  HOH HOH B . 
D 2 HOH 71  271 161 HOH HOH B . 
D 2 HOH 72  272 43  HOH HOH B . 
D 2 HOH 73  273 56  HOH HOH B . 
D 2 HOH 74  274 86  HOH HOH B . 
D 2 HOH 75  275 185 HOH HOH B . 
D 2 HOH 76  276 180 HOH HOH B . 
D 2 HOH 77  277 53  HOH HOH B . 
D 2 HOH 78  278 71  HOH HOH B . 
D 2 HOH 79  279 192 HOH HOH B . 
D 2 HOH 80  280 193 HOH HOH B . 
D 2 HOH 81  281 19  HOH HOH B . 
D 2 HOH 82  282 169 HOH HOH B . 
D 2 HOH 83  283 252 HOH HOH B . 
D 2 HOH 84  284 154 HOH HOH B . 
D 2 HOH 85  285 238 HOH HOH B . 
D 2 HOH 86  286 166 HOH HOH B . 
D 2 HOH 87  287 78  HOH HOH B . 
D 2 HOH 88  288 91  HOH HOH B . 
D 2 HOH 89  289 42  HOH HOH B . 
D 2 HOH 90  290 265 HOH HOH B . 
D 2 HOH 91  291 211 HOH HOH B . 
D 2 HOH 92  292 110 HOH HOH B . 
D 2 HOH 93  293 219 HOH HOH B . 
D 2 HOH 94  294 256 HOH HOH B . 
D 2 HOH 95  295 255 HOH HOH B . 
D 2 HOH 96  296 167 HOH HOH B . 
D 2 HOH 97  297 194 HOH HOH B . 
D 2 HOH 98  298 174 HOH HOH B . 
D 2 HOH 99  299 115 HOH HOH B . 
D 2 HOH 100 300 176 HOH HOH B . 
D 2 HOH 101 301 62  HOH HOH B . 
D 2 HOH 102 302 231 HOH HOH B . 
D 2 HOH 103 303 247 HOH HOH B . 
D 2 HOH 104 304 187 HOH HOH B . 
D 2 HOH 105 305 262 HOH HOH B . 
D 2 HOH 106 306 129 HOH HOH B . 
D 2 HOH 107 307 216 HOH HOH B . 
D 2 HOH 108 308 125 HOH HOH B . 
D 2 HOH 109 309 146 HOH HOH B . 
D 2 HOH 110 310 133 HOH HOH B . 
D 2 HOH 111 311 213 HOH HOH B . 
D 2 HOH 112 312 170 HOH HOH B . 
D 2 HOH 113 313 191 HOH HOH B . 
D 2 HOH 114 314 268 HOH HOH B . 
D 2 HOH 115 315 177 HOH HOH B . 
D 2 HOH 116 316 153 HOH HOH B . 
D 2 HOH 117 317 209 HOH HOH B . 
D 2 HOH 118 318 232 HOH HOH B . 
D 2 HOH 119 319 246 HOH HOH B . 
D 2 HOH 120 320 230 HOH HOH B . 
# 
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      ? ? ? 1.20.1_4487 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASES      ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.020 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KBQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     31.860 
_cell.length_a_esd                 ? 
_cell.length_b                     73.770 
_cell.length_b_esd                 ? 
_cell.length_c                     78.620 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KBQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KBQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.79 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.91 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Citric acid pH 3.5, 25% w/v Polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     81 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          24.270 
_reflns.entry_id                                       9KBQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               34.65 
_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                                     55245 
_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                           99.86 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.36 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.574 
_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                             5468 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.788 
_reflns_shell.pdbx_CC_star                                  0.939 
_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                                78.120 
_refine.B_iso_mean                               32.1047 
_refine.B_iso_min                                18.150 
_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                                 9KBQ 
_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                            1.5200 
_refine.ls_d_res_low                             34.6500 
_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                     55215 
_refine.ls_number_reflns_R_free                  2547 
_refine.ls_number_reflns_R_work                  52668 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.8700 
_refine.ls_percent_reflns_R_free                 4.6100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1932 
_refine.ls_R_factor_R_free                       0.2149 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1921 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1M38 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_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                 27.8200 
_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                            0.2100 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.5200 
_refine_hist.d_res_low                        34.6500 
_refine_hist.number_atoms_solvent             260 
_refine_hist.number_atoms_total               2552 
_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       294 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          42.25 
_refine_hist.pdbx_number_atoms_protein        2292 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.5200 1.5500  . . 137 2878 98.0000  . . . 0.0000 0.3339 . . . . . . . . . . . 0.3749 
'X-RAY DIFFRACTION' 1.5500 1.5800  . . 154 2844 98.0000  . . . 0.0000 0.3289 . . . . . . . . . . . 0.3640 
'X-RAY DIFFRACTION' 1.5800 1.6200  . . 132 2926 99.0000  . . . 0.0000 0.2882 . . . . . . . . . . . 0.3581 
'X-RAY DIFFRACTION' 1.6200 1.6500  . . 143 2945 99.0000  . . . 0.0000 0.2664 . . . . . . . . . . . 0.2874 
'X-RAY DIFFRACTION' 1.6500 1.6900  . . 131 2942 99.0000  . . . 0.0000 0.2451 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 1.6900 1.7400  . . 138 2938 99.0000  . . . 0.0000 .      . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 1.7400 1.7900  . . 133 2929 99.0000  . . . 0.0000 0.2387 . . . . . . . . . . . 0.2925 
'X-RAY DIFFRACTION' 1.7900 1.8500  . . 123 2908 98.0000  . . . 0.0000 0.2540 . . . . . . . . . . . 0.3100 
'X-RAY DIFFRACTION' 1.8500 1.9200  . . 152 2903 98.0000  . . . 0.0000 0.2388 . . . . . . . . . . . 0.2980 
'X-RAY DIFFRACTION' 1.9200 1.9900  . . 145 2979 100.0000 . . . 0.0000 0.2124 . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 1.9900 2.0800  . . 159 2862 99.0000  . . . 0.0000 0.1983 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 2.0800 2.1900  . . 144 2956 99.0000  . . . 0.0000 0.1966 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 2.1900 2.3300  . . 165 2864 98.0000  . . . 0.0000 0.1927 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 2.3300 2.5100  . . 123 2932 98.0000  . . . 0.0000 0.1910 . . . . . . . . . . . 0.1961 
'X-RAY DIFFRACTION' 2.5100 2.7600  . . 136 2966 100.0000 . . . 0.0000 0.1897 . . . . . . . . . . . 0.2310 
'X-RAY DIFFRACTION' 2.7600 3.1600  . . 151 2957 99.0000  . . . 0.0000 0.1882 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 3.1600 3.9800  . . 129 2969 98.0000  . . . 0.0000 0.1636 . . . . . . . . . . . 0.1771 
'X-RAY DIFFRACTION' 3.9800 34.6500 . . 152 2970 99.0000  . . . 0.0000 0.1672 . . . . . . . . . . . 0.1789 
# 
_struct.entry_id                     9KBQ 
_struct.title                        
'Crystal structure of PHAb10, a peptidoglycan hydrolase with thermal stability and broad-spectrum' 
_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        9KBQ 
_struct_keywords.text            'peptidoglycan dydrolase, cationic peptides, dimer, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A8B4M5Z7_ACIBA 
_struct_ref.pdbx_db_accession          A0A8B4M5Z7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSKTTSNAGLNLIKGFEGKRLNAYDDGVGVWTIGFGTIKYPNGVRVKKGDTCTEQQAETYLKNDLTKFEVAINKLVKVPL
TQNQFDALASFTYNLGETNLANSTLLKKLNKSDYQGAADQFLVWNKAGGKVMKGLVRRREAERALFLKK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9KBQ A 1 ? 149 ? A0A8B4M5Z7 1 ? 149 ? 21 169 
2 1 9KBQ B 1 ? 149 ? A0A8B4M5Z7 1 ? 149 ? 21 169 
# 
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 9KBQ SER A 79  ? UNP A0A8B4M5Z7 PRO 79  conflict 99  1 
1 9KBQ GLY A 112 ? UNP A0A8B4M5Z7 SER 112 conflict 132 2 
2 9KBQ SER B 79  ? UNP A0A8B4M5Z7 PRO 79  conflict 99  3 
2 9KBQ GLY B 112 ? UNP A0A8B4M5Z7 SER 112 conflict 132 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 6   ? GLY A 18  ? SER A 26  GLY A 38  1 ? 13 
HELX_P HELX_P2  AA2 THR A 53  ? LEU A 65  ? THR A 73  LEU A 85  1 ? 13 
HELX_P HELX_P3  AA3 LEU A 65  ? VAL A 76  ? LEU A 85  VAL A 96  1 ? 12 
HELX_P HELX_P4  AA4 THR A 81  ? GLY A 96  ? THR A 101 GLY A 116 1 ? 16 
HELX_P HELX_P5  AA5 GLY A 96  ? ASN A 102 ? GLY A 116 ASN A 122 1 ? 7  
HELX_P HELX_P6  AA6 SER A 103 ? LYS A 111 ? SER A 123 LYS A 131 1 ? 9  
HELX_P HELX_P7  AA7 ASP A 113 ? PHE A 121 ? ASP A 133 PHE A 141 1 ? 9  
HELX_P HELX_P8  AA8 LEU A 122 ? TRP A 124 ? LEU A 142 TRP A 144 5 ? 3  
HELX_P HELX_P9  AA9 MET A 132 ? LYS A 148 ? MET A 152 LYS A 168 1 ? 17 
HELX_P HELX_P10 AB1 SER B 6   ? GLY B 18  ? SER B 26  GLY B 38  1 ? 13 
HELX_P HELX_P11 AB2 THR B 53  ? VAL B 76  ? THR B 73  VAL B 96  1 ? 24 
HELX_P HELX_P12 AB3 THR B 81  ? GLY B 96  ? THR B 101 GLY B 116 1 ? 16 
HELX_P HELX_P13 AB4 GLY B 96  ? SER B 103 ? GLY B 116 SER B 123 1 ? 8  
HELX_P HELX_P14 AB5 SER B 103 ? LYS B 111 ? SER B 123 LYS B 131 1 ? 9  
HELX_P HELX_P15 AB6 ASP B 113 ? PHE B 121 ? ASP B 133 PHE B 141 1 ? 9  
HELX_P HELX_P16 AB7 LEU B 122 ? TRP B 124 ? LEU B 142 TRP B 144 5 ? 3  
HELX_P HELX_P17 AB8 MET B 132 ? LYS B 148 ? MET B 152 LYS B 168 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 20  ? ASP A 25  ? ARG A 40  ASP A 45  
AA1 2 TRP A 31  ? GLY A 34  ? TRP A 51  GLY A 54  
AA2 1 LYS A 126 ? ALA A 127 ? LYS A 146 ALA A 147 
AA2 2 LYS A 130 ? VAL A 131 ? LYS A 150 VAL A 151 
AA3 1 ARG B 20  ? ASP B 25  ? ARG B 40  ASP B 45  
AA3 2 TRP B 31  ? GLY B 34  ? TRP B 51  GLY B 54  
AA4 1 LYS B 126 ? ALA B 127 ? LYS B 146 ALA B 147 
AA4 2 LYS B 130 ? VAL B 131 ? LYS B 150 VAL B 151 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 20  ? N ARG A 40  O GLY A 34  ? O GLY A 54  
AA2 1 2 N ALA A 127 ? N ALA A 147 O LYS A 130 ? O LYS A 150 
AA3 1 2 N ARG B 20  ? N ARG B 40  O GLY B 34  ? O GLY B 54  
AA4 1 2 N ALA B 127 ? N ALA B 147 O LYS B 130 ? O LYS B 150 
# 
_pdbx_entry_details.entry_id                   9KBQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASN 
_pdbx_validate_symm_contact.auth_seq_id_1     122 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     157 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_655 
_pdbx_validate_symm_contact.dist              2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 55 ? ? -107.34 61.69 
2 1 PHE B 55 ? ? -111.22 65.57 
# 
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 MET 21  ? A MET 1   
2 1 Y 1 A LYS 169 ? A LYS 149 
3 1 Y 1 B MET 21  ? B MET 1   
4 1 Y 1 B LYS 169 ? B LYS 149 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HOH O    O N N 137 
HOH H1   H N N 138 
HOH H2   H N N 139 
ILE N    N N N 140 
ILE CA   C N S 141 
ILE C    C N N 142 
ILE O    O N N 143 
ILE CB   C N S 144 
ILE CG1  C N N 145 
ILE CG2  C N N 146 
ILE CD1  C N N 147 
ILE OXT  O N N 148 
ILE H    H N N 149 
ILE H2   H N N 150 
ILE HA   H N N 151 
ILE HB   H N N 152 
ILE HG12 H N N 153 
ILE HG13 H N N 154 
ILE HG21 H N N 155 
ILE HG22 H N N 156 
ILE HG23 H N N 157 
ILE HD11 H N N 158 
ILE HD12 H N N 159 
ILE HD13 H N N 160 
ILE HXT  H N N 161 
LEU N    N N N 162 
LEU CA   C N S 163 
LEU C    C N N 164 
LEU O    O N N 165 
LEU CB   C N N 166 
LEU CG   C N N 167 
LEU CD1  C N N 168 
LEU CD2  C N N 169 
LEU OXT  O N N 170 
LEU H    H N N 171 
LEU H2   H N N 172 
LEU HA   H N N 173 
LEU HB2  H N N 174 
LEU HB3  H N N 175 
LEU HG   H N N 176 
LEU HD11 H N N 177 
LEU HD12 H N N 178 
LEU HD13 H N N 179 
LEU HD21 H N N 180 
LEU HD22 H N N 181 
LEU HD23 H N N 182 
LEU HXT  H N N 183 
LYS N    N N N 184 
LYS CA   C N S 185 
LYS C    C N N 186 
LYS O    O N N 187 
LYS CB   C N N 188 
LYS CG   C N N 189 
LYS CD   C N N 190 
LYS CE   C N N 191 
LYS NZ   N N N 192 
LYS OXT  O N N 193 
LYS H    H N N 194 
LYS H2   H N N 195 
LYS HA   H N N 196 
LYS HB2  H N N 197 
LYS HB3  H N N 198 
LYS HG2  H N N 199 
LYS HG3  H N N 200 
LYS HD2  H N N 201 
LYS HD3  H N N 202 
LYS HE2  H N N 203 
LYS HE3  H N N 204 
LYS HZ1  H N N 205 
LYS HZ2  H N N 206 
LYS HZ3  H N N 207 
LYS HXT  H N N 208 
MET N    N N N 209 
MET CA   C N S 210 
MET C    C N N 211 
MET O    O N N 212 
MET CB   C N N 213 
MET CG   C N N 214 
MET SD   S N N 215 
MET CE   C N N 216 
MET OXT  O N N 217 
MET H    H N N 218 
MET H2   H N N 219 
MET HA   H N N 220 
MET HB2  H N N 221 
MET HB3  H N N 222 
MET HG2  H N N 223 
MET HG3  H N N 224 
MET HE1  H N N 225 
MET HE2  H N N 226 
MET HE3  H N N 227 
MET HXT  H N N 228 
PHE N    N N N 229 
PHE CA   C N S 230 
PHE C    C N N 231 
PHE O    O N N 232 
PHE CB   C N N 233 
PHE CG   C Y N 234 
PHE CD1  C Y N 235 
PHE CD2  C Y N 236 
PHE CE1  C Y N 237 
PHE CE2  C Y N 238 
PHE CZ   C Y N 239 
PHE OXT  O N N 240 
PHE H    H N N 241 
PHE H2   H N N 242 
PHE HA   H N N 243 
PHE HB2  H N N 244 
PHE HB3  H N N 245 
PHE HD1  H N N 246 
PHE HD2  H N N 247 
PHE HE1  H N N 248 
PHE HE2  H N N 249 
PHE HZ   H N N 250 
PHE HXT  H N N 251 
PRO N    N N N 252 
PRO CA   C N S 253 
PRO C    C N N 254 
PRO O    O N N 255 
PRO CB   C N N 256 
PRO CG   C N N 257 
PRO CD   C N N 258 
PRO OXT  O N N 259 
PRO H    H N N 260 
PRO HA   H N N 261 
PRO HB2  H N N 262 
PRO HB3  H N N 263 
PRO HG2  H N N 264 
PRO HG3  H N N 265 
PRO HD2  H N N 266 
PRO HD3  H N N 267 
PRO HXT  H N N 268 
SER N    N N N 269 
SER CA   C N S 270 
SER C    C N N 271 
SER O    O N N 272 
SER CB   C N N 273 
SER OG   O N N 274 
SER OXT  O N N 275 
SER H    H N N 276 
SER H2   H N N 277 
SER HA   H N N 278 
SER HB2  H N N 279 
SER HB3  H N N 280 
SER HG   H N N 281 
SER HXT  H N N 282 
THR N    N N N 283 
THR CA   C N S 284 
THR C    C N N 285 
THR O    O N N 286 
THR CB   C N R 287 
THR OG1  O N N 288 
THR CG2  C N N 289 
THR OXT  O N N 290 
THR H    H N N 291 
THR H2   H N N 292 
THR HA   H N N 293 
THR HB   H N N 294 
THR HG1  H N N 295 
THR HG21 H N N 296 
THR HG22 H N N 297 
THR HG23 H N N 298 
THR HXT  H N N 299 
TRP N    N N N 300 
TRP CA   C N S 301 
TRP C    C N N 302 
TRP O    O N N 303 
TRP CB   C N N 304 
TRP CG   C Y N 305 
TRP CD1  C Y N 306 
TRP CD2  C Y N 307 
TRP NE1  N Y N 308 
TRP CE2  C Y N 309 
TRP CE3  C Y N 310 
TRP CZ2  C Y N 311 
TRP CZ3  C Y N 312 
TRP CH2  C Y N 313 
TRP OXT  O N N 314 
TRP H    H N N 315 
TRP H2   H N N 316 
TRP HA   H N N 317 
TRP HB2  H N N 318 
TRP HB3  H N N 319 
TRP HD1  H N N 320 
TRP HE1  H N N 321 
TRP HE3  H N N 322 
TRP HZ2  H N N 323 
TRP HZ3  H N N 324 
TRP HH2  H N N 325 
TRP HXT  H N N 326 
TYR N    N N N 327 
TYR CA   C N S 328 
TYR C    C N N 329 
TYR O    O N N 330 
TYR CB   C N N 331 
TYR CG   C Y N 332 
TYR CD1  C Y N 333 
TYR CD2  C Y N 334 
TYR CE1  C Y N 335 
TYR CE2  C Y N 336 
TYR CZ   C Y N 337 
TYR OH   O N N 338 
TYR OXT  O N N 339 
TYR H    H N N 340 
TYR H2   H N N 341 
TYR HA   H N N 342 
TYR HB2  H N N 343 
TYR HB3  H N N 344 
TYR HD1  H N N 345 
TYR HD2  H N N 346 
TYR HE1  H N N 347 
TYR HE2  H N N 348 
TYR HH   H N N 349 
TYR HXT  H N N 350 
VAL N    N N N 351 
VAL CA   C N S 352 
VAL C    C N N 353 
VAL O    O N N 354 
VAL CB   C N N 355 
VAL CG1  C N N 356 
VAL CG2  C N N 357 
VAL OXT  O N N 358 
VAL H    H N N 359 
VAL H2   H N N 360 
VAL HA   H N N 361 
VAL HB   H N N 362 
VAL HG11 H N N 363 
VAL HG12 H N N 364 
VAL HG13 H N N 365 
VAL HG21 H N N 366 
VAL HG22 H N N 367 
VAL HG23 H N N 368 
VAL HXT  H N N 369 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HOH O   H1   sing N N 129 
HOH O   H2   sing N N 130 
ILE N   CA   sing N N 131 
ILE N   H    sing N N 132 
ILE N   H2   sing N N 133 
ILE CA  C    sing N N 134 
ILE CA  CB   sing N N 135 
ILE CA  HA   sing N N 136 
ILE C   O    doub N N 137 
ILE C   OXT  sing N N 138 
ILE CB  CG1  sing N N 139 
ILE CB  CG2  sing N N 140 
ILE CB  HB   sing N N 141 
ILE CG1 CD1  sing N N 142 
ILE CG1 HG12 sing N N 143 
ILE CG1 HG13 sing N N 144 
ILE CG2 HG21 sing N N 145 
ILE CG2 HG22 sing N N 146 
ILE CG2 HG23 sing N N 147 
ILE CD1 HD11 sing N N 148 
ILE CD1 HD12 sing N N 149 
ILE CD1 HD13 sing N N 150 
ILE OXT HXT  sing N N 151 
LEU N   CA   sing N N 152 
LEU N   H    sing N N 153 
LEU N   H2   sing N N 154 
LEU CA  C    sing N N 155 
LEU CA  CB   sing N N 156 
LEU CA  HA   sing N N 157 
LEU C   O    doub N N 158 
LEU C   OXT  sing N N 159 
LEU CB  CG   sing N N 160 
LEU CB  HB2  sing N N 161 
LEU CB  HB3  sing N N 162 
LEU CG  CD1  sing N N 163 
LEU CG  CD2  sing N N 164 
LEU CG  HG   sing N N 165 
LEU CD1 HD11 sing N N 166 
LEU CD1 HD12 sing N N 167 
LEU CD1 HD13 sing N N 168 
LEU CD2 HD21 sing N N 169 
LEU CD2 HD22 sing N N 170 
LEU CD2 HD23 sing N N 171 
LEU OXT HXT  sing N N 172 
LYS N   CA   sing N N 173 
LYS N   H    sing N N 174 
LYS N   H2   sing N N 175 
LYS CA  C    sing N N 176 
LYS CA  CB   sing N N 177 
LYS CA  HA   sing N N 178 
LYS C   O    doub N N 179 
LYS C   OXT  sing N N 180 
LYS CB  CG   sing N N 181 
LYS CB  HB2  sing N N 182 
LYS CB  HB3  sing N N 183 
LYS CG  CD   sing N N 184 
LYS CG  HG2  sing N N 185 
LYS CG  HG3  sing N N 186 
LYS CD  CE   sing N N 187 
LYS CD  HD2  sing N N 188 
LYS CD  HD3  sing N N 189 
LYS CE  NZ   sing N N 190 
LYS CE  HE2  sing N N 191 
LYS CE  HE3  sing N N 192 
LYS NZ  HZ1  sing N N 193 
LYS NZ  HZ2  sing N N 194 
LYS NZ  HZ3  sing N N 195 
LYS OXT HXT  sing N N 196 
MET N   CA   sing N N 197 
MET N   H    sing N N 198 
MET N   H2   sing N N 199 
MET CA  C    sing N N 200 
MET CA  CB   sing N N 201 
MET CA  HA   sing N N 202 
MET C   O    doub N N 203 
MET C   OXT  sing N N 204 
MET CB  CG   sing N N 205 
MET CB  HB2  sing N N 206 
MET CB  HB3  sing N N 207 
MET CG  SD   sing N N 208 
MET CG  HG2  sing N N 209 
MET CG  HG3  sing N N 210 
MET SD  CE   sing N N 211 
MET CE  HE1  sing N N 212 
MET CE  HE2  sing N N 213 
MET CE  HE3  sing N N 214 
MET OXT HXT  sing N N 215 
PHE N   CA   sing N N 216 
PHE N   H    sing N N 217 
PHE N   H2   sing N N 218 
PHE CA  C    sing N N 219 
PHE CA  CB   sing N N 220 
PHE CA  HA   sing N N 221 
PHE C   O    doub N N 222 
PHE C   OXT  sing N N 223 
PHE CB  CG   sing N N 224 
PHE CB  HB2  sing N N 225 
PHE CB  HB3  sing N N 226 
PHE CG  CD1  doub Y N 227 
PHE CG  CD2  sing Y N 228 
PHE CD1 CE1  sing Y N 229 
PHE CD1 HD1  sing N N 230 
PHE CD2 CE2  doub Y N 231 
PHE CD2 HD2  sing N N 232 
PHE CE1 CZ   doub Y N 233 
PHE CE1 HE1  sing N N 234 
PHE CE2 CZ   sing Y N 235 
PHE CE2 HE2  sing N N 236 
PHE CZ  HZ   sing N N 237 
PHE OXT HXT  sing N N 238 
PRO N   CA   sing N N 239 
PRO N   CD   sing N N 240 
PRO N   H    sing N N 241 
PRO CA  C    sing N N 242 
PRO CA  CB   sing N N 243 
PRO CA  HA   sing N N 244 
PRO C   O    doub N N 245 
PRO C   OXT  sing N N 246 
PRO CB  CG   sing N N 247 
PRO CB  HB2  sing N N 248 
PRO CB  HB3  sing N N 249 
PRO CG  CD   sing N N 250 
PRO CG  HG2  sing N N 251 
PRO CG  HG3  sing N N 252 
PRO CD  HD2  sing N N 253 
PRO CD  HD3  sing N N 254 
PRO OXT HXT  sing N N 255 
SER N   CA   sing N N 256 
SER N   H    sing N N 257 
SER N   H2   sing N N 258 
SER CA  C    sing N N 259 
SER CA  CB   sing N N 260 
SER CA  HA   sing N N 261 
SER C   O    doub N N 262 
SER C   OXT  sing N N 263 
SER CB  OG   sing N N 264 
SER CB  HB2  sing N N 265 
SER CB  HB3  sing N N 266 
SER OG  HG   sing N N 267 
SER OXT HXT  sing N N 268 
THR N   CA   sing N N 269 
THR N   H    sing N N 270 
THR N   H2   sing N N 271 
THR CA  C    sing N N 272 
THR CA  CB   sing N N 273 
THR CA  HA   sing N N 274 
THR C   O    doub N N 275 
THR C   OXT  sing N N 276 
THR CB  OG1  sing N N 277 
THR CB  CG2  sing N N 278 
THR CB  HB   sing N N 279 
THR OG1 HG1  sing N N 280 
THR CG2 HG21 sing N N 281 
THR CG2 HG22 sing N N 282 
THR CG2 HG23 sing N N 283 
THR OXT HXT  sing N N 284 
TRP N   CA   sing N N 285 
TRP N   H    sing N N 286 
TRP N   H2   sing N N 287 
TRP CA  C    sing N N 288 
TRP CA  CB   sing N N 289 
TRP CA  HA   sing N N 290 
TRP C   O    doub N N 291 
TRP C   OXT  sing N N 292 
TRP CB  CG   sing N N 293 
TRP CB  HB2  sing N N 294 
TRP CB  HB3  sing N N 295 
TRP CG  CD1  doub Y N 296 
TRP CG  CD2  sing Y N 297 
TRP CD1 NE1  sing Y N 298 
TRP CD1 HD1  sing N N 299 
TRP CD2 CE2  doub Y N 300 
TRP CD2 CE3  sing Y N 301 
TRP NE1 CE2  sing Y N 302 
TRP NE1 HE1  sing N N 303 
TRP CE2 CZ2  sing Y N 304 
TRP CE3 CZ3  doub Y N 305 
TRP CE3 HE3  sing N N 306 
TRP CZ2 CH2  doub Y N 307 
TRP CZ2 HZ2  sing N N 308 
TRP CZ3 CH2  sing Y N 309 
TRP CZ3 HZ3  sing N N 310 
TRP CH2 HH2  sing N N 311 
TRP OXT HXT  sing N N 312 
TYR N   CA   sing N N 313 
TYR N   H    sing N N 314 
TYR N   H2   sing N N 315 
TYR CA  C    sing N N 316 
TYR CA  CB   sing N N 317 
TYR CA  HA   sing N N 318 
TYR C   O    doub N N 319 
TYR C   OXT  sing N N 320 
TYR CB  CG   sing N N 321 
TYR CB  HB2  sing N N 322 
TYR CB  HB3  sing N N 323 
TYR CG  CD1  doub Y N 324 
TYR CG  CD2  sing Y N 325 
TYR CD1 CE1  sing Y N 326 
TYR CD1 HD1  sing N N 327 
TYR CD2 CE2  doub Y N 328 
TYR CD2 HD2  sing N N 329 
TYR CE1 CZ   doub Y N 330 
TYR CE1 HE1  sing N N 331 
TYR CE2 CZ   sing Y N 332 
TYR CE2 HE2  sing N N 333 
TYR CZ  OH   sing N N 334 
TYR OH  HH   sing N N 335 
TYR OXT HXT  sing N N 336 
VAL N   CA   sing N N 337 
VAL N   H    sing N N 338 
VAL N   H2   sing N N 339 
VAL CA  C    sing N N 340 
VAL CA  CB   sing N N 341 
VAL CA  HA   sing N N 342 
VAL C   O    doub N N 343 
VAL C   OXT  sing N N 344 
VAL CB  CG1  sing N N 345 
VAL CB  CG2  sing N N 346 
VAL CB  HB   sing N N 347 
VAL CG1 HG11 sing N N 348 
VAL CG1 HG12 sing N N 349 
VAL CG1 HG13 sing N N 350 
VAL CG2 HG21 sing N N 351 
VAL CG2 HG22 sing N N 352 
VAL CG2 HG23 sing N N 353 
VAL OXT HXT  sing N N 354 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           81802001 
_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   6ET6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KBQ 
_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]   0.031387 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001656 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013556 
_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]   0.012737 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 2   ? 19.853  13.274  46.941 1.00 57.10 ? 22  SER A N   1 
ATOM   2    C CA  . SER A 1 2   ? 19.358  13.508  45.589 1.00 46.62 ? 22  SER A CA  1 
ATOM   3    C C   . SER A 1 2   ? 17.955  12.928  45.425 1.00 45.20 ? 22  SER A C   1 
ATOM   4    O O   . SER A 1 2   ? 17.591  11.955  46.083 1.00 52.40 ? 22  SER A O   1 
ATOM   5    C CB  . SER A 1 2   ? 20.317  12.916  44.557 1.00 42.16 ? 22  SER A CB  1 
ATOM   6    O OG  . SER A 1 2   ? 20.128  11.520  44.428 1.00 52.76 ? 22  SER A OG  1 
ATOM   7    N N   . LYS A 1 3   ? 17.178  13.526  44.529 1.00 41.33 ? 23  LYS A N   1 
ATOM   8    C CA  . LYS A 1 3   ? 15.741  13.308  44.476 1.00 34.93 ? 23  LYS A CA  1 
ATOM   9    C C   . LYS A 1 3   ? 15.370  12.088  43.640 1.00 33.16 ? 23  LYS A C   1 
ATOM   10   O O   . LYS A 1 3   ? 16.122  11.632  42.774 1.00 33.67 ? 23  LYS A O   1 
ATOM   11   C CB  . LYS A 1 3   ? 15.039  14.535  43.897 1.00 30.79 ? 23  LYS A CB  1 
ATOM   12   C CG  . LYS A 1 3   ? 15.017  15.738  44.817 1.00 32.15 ? 23  LYS A CG  1 
ATOM   13   C CD  . LYS A 1 3   ? 14.288  16.896  44.158 1.00 29.80 ? 23  LYS A CD  1 
ATOM   14   C CE  . LYS A 1 3   ? 14.084  18.039  45.130 1.00 38.13 ? 23  LYS A CE  1 
ATOM   15   N NZ  . LYS A 1 3   ? 15.382  18.697  45.436 1.00 37.97 ? 23  LYS A NZ  1 
ATOM   16   N N   . THR A 1 4   ? 14.176  11.571  43.913 1.00 27.83 ? 24  THR A N   1 
ATOM   17   C CA  . THR A 1 4   ? 13.500  10.608  43.061 1.00 30.35 ? 24  THR A CA  1 
ATOM   18   C C   . THR A 1 4   ? 12.097  11.127  42.774 1.00 28.69 ? 24  THR A C   1 
ATOM   19   O O   . THR A 1 4   ? 11.611  12.055  43.425 1.00 29.35 ? 24  THR A O   1 
ATOM   20   C CB  . THR A 1 4   ? 13.437  9.221   43.711 1.00 35.58 ? 24  THR A CB  1 
ATOM   21   O OG1 . THR A 1 4   ? 12.783  9.327   44.979 1.00 35.27 ? 24  THR A OG1 1 
ATOM   22   C CG2 . THR A 1 4   ? 14.838  8.664   43.912 1.00 35.42 ? 24  THR A CG2 1 
ATOM   23   N N   . THR A 1 5   ? 11.442  10.525  41.783 1.00 27.77 ? 25  THR A N   1 
ATOM   24   C CA  . THR A 1 5   ? 10.107  10.971  41.406 1.00 26.56 ? 25  THR A CA  1 
ATOM   25   C C   . THR A 1 5   ? 9.101   10.691  42.518 1.00 27.97 ? 25  THR A C   1 
ATOM   26   O O   . THR A 1 5   ? 9.003   9.563   43.015 1.00 29.38 ? 25  THR A O   1 
ATOM   27   C CB  . THR A 1 5   ? 9.672   10.287  40.113 1.00 25.99 ? 25  THR A CB  1 
ATOM   28   O OG1 . THR A 1 5   ? 10.746  10.342  39.165 1.00 27.18 ? 25  THR A OG1 1 
ATOM   29   C CG2 . THR A 1 5   ? 8.446   10.970  39.539 1.00 28.19 ? 25  THR A CG2 1 
ATOM   30   N N   . SER A 1 6   ? 8.358   11.723  42.914 1.00 28.97 ? 26  SER A N   1 
ATOM   31   C CA  . SER A 1 6   ? 7.321   11.572  43.920 1.00 30.18 ? 26  SER A CA  1 
ATOM   32   C C   . SER A 1 6   ? 5.994   11.212  43.254 1.00 34.24 ? 26  SER A C   1 
ATOM   33   O O   . SER A 1 6   ? 5.902   11.046  42.034 1.00 33.97 ? 26  SER A O   1 
ATOM   34   C CB  . SER A 1 6   ? 7.194   12.847  44.753 1.00 30.74 ? 26  SER A CB  1 
ATOM   35   O OG  . SER A 1 6   ? 6.316   13.766  44.125 1.00 40.50 ? 26  SER A OG  1 
ATOM   36   N N   . ASN A 1 7   ? 4.944   11.108  44.073 1.00 41.01 ? 27  ASN A N   1 
ATOM   37   C CA  . ASN A 1 7   ? 3.628   10.734  43.567 1.00 42.84 ? 27  ASN A CA  1 
ATOM   38   C C   . ASN A 1 7   ? 3.116   11.702  42.507 1.00 46.80 ? 27  ASN A C   1 
ATOM   39   O O   . ASN A 1 7   ? 2.363   11.299  41.617 1.00 42.77 ? 27  ASN A O   1 
ATOM   40   C CB  . ASN A 1 7   ? 2.626   10.653  44.720 1.00 45.42 ? 27  ASN A CB  1 
ATOM   41   C CG  . ASN A 1 7   ? 2.692   9.334   45.461 1.00 52.69 ? 27  ASN A CG  1 
ATOM   42   O OD1 . ASN A 1 7   ? 3.459   8.442   45.099 1.00 52.44 ? 27  ASN A OD1 1 
ATOM   43   N ND2 . ASN A 1 7   ? 1.882   9.202   46.504 1.00 58.32 ? 27  ASN A ND2 1 
ATOM   44   N N   . ALA A 1 8   ? 3.507   12.977  42.577 1.00 37.58 ? 28  ALA A N   1 
ATOM   45   C CA  . ALA A 1 8   ? 3.020   13.946  41.597 1.00 38.64 ? 28  ALA A CA  1 
ATOM   46   C C   . ALA A 1 8   ? 3.527   13.620  40.196 1.00 39.21 ? 28  ALA A C   1 
ATOM   47   O O   . ALA A 1 8   ? 2.750   13.576  39.230 1.00 38.46 ? 28  ALA A O   1 
ATOM   48   C CB  . ALA A 1 8   ? 3.434   15.360  42.005 1.00 35.00 ? 28  ALA A CB  1 
ATOM   49   N N   . GLY A 1 9   ? 4.834   13.390  40.062 1.00 34.95 ? 29  GLY A N   1 
ATOM   50   C CA  . GLY A 1 9   ? 5.371   13.028  38.760 1.00 30.61 ? 29  GLY A CA  1 
ATOM   51   C C   . GLY A 1 9   ? 4.875   11.671  38.300 1.00 28.25 ? 29  GLY A C   1 
ATOM   52   O O   . GLY A 1 9   ? 4.602   11.468  37.110 1.00 31.85 ? 29  GLY A O   1 
ATOM   53   N N   . LEU A 1 10  ? 4.743   10.729  39.239 1.00 34.90 ? 30  LEU A N   1 
ATOM   54   C CA  . LEU A 1 10  ? 4.208   9.413   38.902 1.00 31.80 ? 30  LEU A CA  1 
ATOM   55   C C   . LEU A 1 10  ? 2.791   9.517   38.362 1.00 37.89 ? 30  LEU A C   1 
ATOM   56   O O   . LEU A 1 10  ? 2.432   8.814   37.414 1.00 36.53 ? 30  LEU A O   1 
ATOM   57   C CB  . LEU A 1 10  ? 4.244   8.491   40.122 1.00 36.08 ? 30  LEU A CB  1 
ATOM   58   C CG  . LEU A 1 10  ? 5.620   8.038   40.611 1.00 33.08 ? 30  LEU A CG  1 
ATOM   59   C CD1 . LEU A 1 10  ? 5.507   7.267   41.915 1.00 36.54 ? 30  LEU A CD1 1 
ATOM   60   C CD2 . LEU A 1 10  ? 6.291   7.188   39.564 1.00 32.43 ? 30  LEU A CD2 1 
ATOM   61   N N   . ASN A 1 11  ? 1.970   10.389  38.951 1.00 36.08 ? 31  ASN A N   1 
ATOM   62   C CA  . ASN A 1 11  ? 0.613   10.582  38.453 1.00 37.91 ? 31  ASN A CA  1 
ATOM   63   C C   . ASN A 1 11  ? 0.616   11.254  37.090 1.00 42.60 ? 31  ASN A C   1 
ATOM   64   O O   . ASN A 1 11  ? -0.182  10.898  36.216 1.00 42.26 ? 31  ASN A O   1 
ATOM   65   C CB  . ASN A 1 11  ? -0.209  11.400  39.449 1.00 41.03 ? 31  ASN A CB  1 
ATOM   66   C CG  . ASN A 1 11  ? -0.464  10.657  40.746 1.00 44.81 ? 31  ASN A CG  1 
ATOM   67   O OD1 . ASN A 1 11  ? -0.360  9.430   40.806 1.00 54.08 ? 31  ASN A OD1 1 
ATOM   68   N ND2 . ASN A 1 11  ? -0.816  11.396  41.789 1.00 52.51 ? 31  ASN A ND2 1 
ATOM   69   N N   . LEU A 1 12  ? 1.502   12.233  36.884 1.00 40.01 ? 32  LEU A N   1 
ATOM   70   C CA  . LEU A 1 12  ? 1.624   12.823  35.554 1.00 40.98 ? 32  LEU A CA  1 
ATOM   71   C C   . LEU A 1 12  ? 1.910   11.752  34.508 1.00 39.80 ? 32  LEU A C   1 
ATOM   72   O O   . LEU A 1 12  ? 1.285   11.724  33.442 1.00 40.69 ? 32  LEU A O   1 
ATOM   73   C CB  . LEU A 1 12  ? 2.719   13.891  35.528 1.00 38.98 ? 32  LEU A CB  1 
ATOM   74   C CG  . LEU A 1 12  ? 2.316   15.295  35.976 1.00 34.06 ? 32  LEU A CG  1 
ATOM   75   C CD1 . LEU A 1 12  ? 3.491   16.244  35.832 1.00 35.22 ? 32  LEU A CD1 1 
ATOM   76   C CD2 . LEU A 1 12  ? 1.112   15.787  35.188 1.00 37.84 ? 32  LEU A CD2 1 
ATOM   77   N N   . ILE A 1 13  ? 2.846   10.850  34.806 1.00 34.59 ? 33  ILE A N   1 
ATOM   78   C CA  . ILE A 1 13  ? 3.240   9.854   33.812 1.00 34.23 ? 33  ILE A CA  1 
ATOM   79   C C   . ILE A 1 13  ? 2.159   8.791   33.648 1.00 27.85 ? 33  ILE A C   1 
ATOM   80   O O   . ILE A 1 13  ? 1.878   8.344   32.529 1.00 37.08 ? 33  ILE A O   1 
ATOM   81   C CB  . ILE A 1 13  ? 4.603   9.244   34.181 1.00 34.17 ? 33  ILE A CB  1 
ATOM   82   C CG1 . ILE A 1 13  ? 5.678   10.333  34.120 1.00 33.51 ? 33  ILE A CG1 1 
ATOM   83   C CG2 . ILE A 1 13  ? 4.949   8.092   33.256 1.00 30.40 ? 33  ILE A CG2 1 
ATOM   84   C CD1 . ILE A 1 13  ? 6.971   9.954   34.781 1.00 33.78 ? 33  ILE A CD1 1 
ATOM   85   N N   . LYS A 1 14  ? 1.530   8.377   34.752 1.00 34.54 ? 34  LYS A N   1 
ATOM   86   C CA  . LYS A 1 14  ? 0.401   7.457   34.673 1.00 34.80 ? 34  LYS A CA  1 
ATOM   87   C C   . LYS A 1 14  ? -0.729  8.045   33.844 1.00 48.23 ? 34  LYS A C   1 
ATOM   88   O O   . LYS A 1 14  ? -1.480  7.302   33.200 1.00 41.11 ? 34  LYS A O   1 
ATOM   89   C CB  . LYS A 1 14  ? -0.106  7.126   36.078 1.00 36.65 ? 34  LYS A CB  1 
ATOM   90   C CG  . LYS A 1 14  ? 0.730   6.133   36.852 1.00 32.42 ? 34  LYS A CG  1 
ATOM   91   C CD  . LYS A 1 14  ? 0.283   6.080   38.304 1.00 40.02 ? 34  LYS A CD  1 
ATOM   92   C CE  . LYS A 1 14  ? 1.189   5.201   39.135 1.00 40.06 ? 34  LYS A CE  1 
ATOM   93   N NZ  . LYS A 1 14  ? 0.528   4.774   40.404 1.00 45.39 ? 34  LYS A NZ  1 
ATOM   94   N N   . GLY A 1 15  ? -0.858  9.374   33.849 1.00 43.25 ? 35  GLY A N   1 
ATOM   95   C CA  . GLY A 1 15  ? -1.911  10.014  33.080 1.00 42.48 ? 35  GLY A CA  1 
ATOM   96   C C   . GLY A 1 15  ? -1.820  9.728   31.595 1.00 45.03 ? 35  GLY A C   1 
ATOM   97   O O   . GLY A 1 15  ? -2.822  9.401   30.954 1.00 53.20 ? 35  GLY A O   1 
ATOM   98   N N   . PHE A 1 16  ? -0.622  9.843   31.021 1.00 35.88 ? 36  PHE A N   1 
ATOM   99   C CA  . PHE A 1 16  ? -0.487  9.666   29.582 1.00 40.99 ? 36  PHE A CA  1 
ATOM   100  C C   . PHE A 1 16  ? 0.123   8.328   29.172 1.00 38.34 ? 36  PHE A C   1 
ATOM   101  O O   . PHE A 1 16  ? 0.226   8.059   27.971 1.00 41.56 ? 36  PHE A O   1 
ATOM   102  C CB  . PHE A 1 16  ? 0.295   10.836  28.953 1.00 49.70 ? 36  PHE A CB  1 
ATOM   103  C CG  . PHE A 1 16  ? 1.732   10.973  29.404 1.00 46.66 ? 36  PHE A CG  1 
ATOM   104  C CD1 . PHE A 1 16  ? 2.745   10.271  28.767 1.00 43.42 ? 36  PHE A CD1 1 
ATOM   105  C CD2 . PHE A 1 16  ? 2.081   11.888  30.389 1.00 43.26 ? 36  PHE A CD2 1 
ATOM   106  C CE1 . PHE A 1 16  ? 4.071   10.425  29.149 1.00 37.15 ? 36  PHE A CE1 1 
ATOM   107  C CE2 . PHE A 1 16  ? 3.407   12.051  30.775 1.00 44.06 ? 36  PHE A CE2 1 
ATOM   108  C CZ  . PHE A 1 16  ? 4.403   11.319  30.155 1.00 35.58 ? 36  PHE A CZ  1 
ATOM   109  N N   . GLU A 1 17  ? 0.499   7.466   30.118 1.00 36.98 ? 37  GLU A N   1 
ATOM   110  C CA  . GLU A 1 17  ? 0.822   6.099   29.728 1.00 33.84 ? 37  GLU A CA  1 
ATOM   111  C C   . GLU A 1 17  ? -0.367  5.162   29.865 1.00 34.60 ? 37  GLU A C   1 
ATOM   112  O O   . GLU A 1 17  ? -0.435  4.153   29.155 1.00 36.25 ? 37  GLU A O   1 
ATOM   113  C CB  . GLU A 1 17  ? 1.992   5.553   30.552 1.00 33.94 ? 37  GLU A CB  1 
ATOM   114  C CG  . GLU A 1 17  ? 3.331   6.193   30.229 1.00 41.05 ? 37  GLU A CG  1 
ATOM   115  C CD  . GLU A 1 17  ? 3.743   5.979   28.783 1.00 44.87 ? 37  GLU A CD  1 
ATOM   116  O OE1 . GLU A 1 17  ? 3.530   4.865   28.255 1.00 41.07 ? 37  GLU A OE1 1 
ATOM   117  O OE2 . GLU A 1 17  ? 4.281   6.926   28.174 1.00 48.78 ? 37  GLU A OE2 1 
ATOM   118  N N   . GLY A 1 18  ? -1.307  5.478   30.748 1.00 32.94 ? 38  GLY A N   1 
ATOM   119  C CA  . GLY A 1 18  ? -2.421  4.591   31.011 1.00 32.55 ? 38  GLY A CA  1 
ATOM   120  C C   . GLY A 1 18  ? -1.970  3.373   31.796 1.00 36.63 ? 38  GLY A C   1 
ATOM   121  O O   . GLY A 1 18  ? -0.797  3.194   32.117 1.00 35.17 ? 38  GLY A O   1 
ATOM   122  N N   . LYS A 1 19  ? -2.941  2.521   32.110 1.00 30.54 ? 39  LYS A N   1 
ATOM   123  C CA  . LYS A 1 19  ? -2.704  1.291   32.856 1.00 30.94 ? 39  LYS A CA  1 
ATOM   124  C C   . LYS A 1 19  ? -3.255  0.123   32.052 1.00 28.90 ? 39  LYS A C   1 
ATOM   125  O O   . LYS A 1 19  ? -4.442  0.107   31.708 1.00 34.52 ? 39  LYS A O   1 
ATOM   126  C CB  . LYS A 1 19  ? -3.351  1.365   34.241 1.00 31.62 ? 39  LYS A CB  1 
ATOM   127  C CG  . LYS A 1 19  ? -2.957  0.239   35.184 1.00 39.16 ? 39  LYS A CG  1 
ATOM   128  C CD  . LYS A 1 19  ? -3.950  0.132   36.335 1.00 43.47 ? 39  LYS A CD  1 
ATOM   129  C CE  . LYS A 1 19  ? -4.954  -0.982  36.118 1.00 52.88 ? 39  LYS A CE  1 
ATOM   130  N NZ  . LYS A 1 19  ? -5.467  -1.515  37.412 1.00 63.02 ? 39  LYS A NZ  1 
ATOM   131  N N   . ARG A 1 20  ? -2.388  -0.837  31.733 1.00 29.12 ? 40  ARG A N   1 
ATOM   132  C CA  . ARG A 1 20  ? -2.776  -2.019  30.969 1.00 30.50 ? 40  ARG A CA  1 
ATOM   133  C C   . ARG A 1 20  ? -2.067  -3.207  31.605 1.00 31.31 ? 40  ARG A C   1 
ATOM   134  O O   . ARG A 1 20  ? -0.844  -3.329  31.494 1.00 34.86 ? 40  ARG A O   1 
ATOM   135  C CB  . ARG A 1 20  ? -2.396  -1.867  29.494 1.00 36.82 ? 40  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 20  ? -3.273  -0.874  28.713 1.00 35.44 ? 40  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 20  ? -3.470  -1.285  27.252 1.00 46.32 ? 40  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 20  ? -4.668  -2.084  27.020 1.00 49.47 ? 40  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 20  ? -5.889  -1.579  26.891 1.00 51.64 ? 40  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 20  ? -6.115  -0.279  26.995 1.00 45.42 ? 40  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 20  ? -6.908  -2.399  26.644 1.00 46.47 ? 40  ARG A NH2 1 
ATOM   142  N N   . LEU A 1 21  ? -2.823  -4.072  32.276 1.00 32.41 ? 41  LEU A N   1 
ATOM   143  C CA  . LEU A 1 21  ? -2.254  -5.208  32.987 1.00 29.67 ? 41  LEU A CA  1 
ATOM   144  C C   . LEU A 1 21  ? -2.017  -6.415  32.086 1.00 35.67 ? 41  LEU A C   1 
ATOM   145  O O   . LEU A 1 21  ? -1.422  -7.398  32.537 1.00 31.80 ? 41  LEU A O   1 
ATOM   146  C CB  . LEU A 1 21  ? -3.161  -5.588  34.163 1.00 27.16 ? 41  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 21  ? -3.391  -4.456  35.165 1.00 29.69 ? 41  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 21  ? -4.133  -4.961  36.396 1.00 32.10 ? 41  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 21  ? -2.065  -3.814  35.568 1.00 31.03 ? 41  LEU A CD2 1 
ATOM   150  N N   . ASN A 1 22  ? -2.465  -6.366  30.834 1.00 30.67 ? 42  ASN A N   1 
ATOM   151  C CA  . ASN A 1 22  ? -2.085  -7.337  29.817 1.00 29.85 ? 42  ASN A CA  1 
ATOM   152  C C   . ASN A 1 22  ? -1.159  -6.660  28.816 1.00 29.59 ? 42  ASN A C   1 
ATOM   153  O O   . ASN A 1 22  ? -1.393  -5.512  28.423 1.00 31.53 ? 42  ASN A O   1 
ATOM   154  C CB  . ASN A 1 22  ? -3.308  -7.911  29.091 1.00 38.20 ? 42  ASN A CB  1 
ATOM   155  C CG  . ASN A 1 22  ? -4.290  -8.585  30.032 1.00 41.05 ? 42  ASN A CG  1 
ATOM   156  O OD1 . ASN A 1 22  ? -3.993  -9.628  30.617 1.00 43.28 ? 42  ASN A OD1 1 
ATOM   157  N ND2 . ASN A 1 22  ? -5.473  -8.000  30.171 1.00 49.09 ? 42  ASN A ND2 1 
ATOM   158  N N   . ALA A 1 23  ? -0.109  -7.369  28.409 1.00 29.20 ? 43  ALA A N   1 
ATOM   159  C CA  . ALA A 1 23  ? 0.859   -6.797  27.484 1.00 27.70 ? 43  ALA A CA  1 
ATOM   160  C C   . ALA A 1 23  ? 0.208   -6.497  26.139 1.00 23.60 ? 43  ALA A C   1 
ATOM   161  O O   . ALA A 1 23  ? -0.668  -7.235  25.674 1.00 29.64 ? 43  ALA A O   1 
ATOM   162  C CB  . ALA A 1 23  ? 2.042   -7.742  27.289 1.00 28.07 ? 43  ALA A CB  1 
ATOM   163  N N   . TYR A 1 24  ? 0.638   -5.399  25.520 1.00 26.48 ? 44  TYR A N   1 
ATOM   164  C CA  . TYR A 1 24  ? 0.097   -4.964  24.239 1.00 30.11 ? 44  TYR A CA  1 
ATOM   165  C C   . TYR A 1 24  ? 1.219   -4.480  23.335 1.00 30.01 ? 44  TYR A C   1 
ATOM   166  O O   . TYR A 1 24  ? 2.267   -4.025  23.799 1.00 23.99 ? 44  TYR A O   1 
ATOM   167  C CB  . TYR A 1 24  ? -0.954  -3.851  24.409 1.00 28.66 ? 44  TYR A CB  1 
ATOM   168  C CG  . TYR A 1 24  ? -0.428  -2.560  25.010 1.00 36.27 ? 44  TYR A CG  1 
ATOM   169  C CD1 . TYR A 1 24  ? -0.257  -2.431  26.384 1.00 36.70 ? 44  TYR A CD1 1 
ATOM   170  C CD2 . TYR A 1 24  ? -0.107  -1.474  24.207 1.00 41.91 ? 44  TYR A CD2 1 
ATOM   171  C CE1 . TYR A 1 24  ? 0.218   -1.258  26.942 1.00 41.12 ? 44  TYR A CE1 1 
ATOM   172  C CE2 . TYR A 1 24  ? 0.371   -0.292  24.758 1.00 37.88 ? 44  TYR A CE2 1 
ATOM   173  C CZ  . TYR A 1 24  ? 0.531   -0.194  26.124 1.00 37.98 ? 44  TYR A CZ  1 
ATOM   174  O OH  . TYR A 1 24  ? 1.005   0.974   26.681 1.00 47.36 ? 44  TYR A OH  1 
ATOM   175  N N   . ASP A 1 25  ? 0.986   -4.601  22.025 1.00 25.97 ? 45  ASP A N   1 
ATOM   176  C CA  . ASP A 1 25  ? 1.867   -4.035  21.008 1.00 24.69 ? 45  ASP A CA  1 
ATOM   177  C C   . ASP A 1 25  ? 1.637   -2.536  20.875 1.00 30.51 ? 45  ASP A C   1 
ATOM   178  O O   . ASP A 1 25  ? 0.500   -2.093  20.693 1.00 28.48 ? 45  ASP A O   1 
ATOM   179  C CB  . ASP A 1 25  ? 1.617   -4.700  19.652 1.00 26.32 ? 45  ASP A CB  1 
ATOM   180  C CG  . ASP A 1 25  ? 2.773   -4.516  18.676 1.00 30.30 ? 45  ASP A CG  1 
ATOM   181  O OD1 . ASP A 1 25  ? 3.511   -3.521  18.802 1.00 29.73 ? 45  ASP A OD1 1 
ATOM   182  O OD2 . ASP A 1 25  ? 2.948   -5.375  17.778 1.00 30.90 ? 45  ASP A OD2 1 
ATOM   183  N N   . ASP A 1 26  ? 2.716   -1.759  20.938 1.00 26.55 ? 46  ASP A N   1 
ATOM   184  C CA  . ASP A 1 26  ? 2.606   -0.310  20.809 1.00 26.30 ? 46  ASP A CA  1 
ATOM   185  C C   . ASP A 1 26  ? 2.604   0.163   19.360 1.00 25.45 ? 46  ASP A C   1 
ATOM   186  O O   . ASP A 1 26  ? 2.491   1.373   19.119 1.00 27.29 ? 46  ASP A O   1 
ATOM   187  C CB  . ASP A 1 26  ? 3.728   0.386   21.594 1.00 30.08 ? 46  ASP A CB  1 
ATOM   188  C CG  . ASP A 1 26  ? 5.101   0.165   20.993 1.00 29.21 ? 46  ASP A CG  1 
ATOM   189  O OD1 . ASP A 1 26  ? 5.233   -0.621  20.030 1.00 28.05 ? 46  ASP A OD1 1 
ATOM   190  O OD2 . ASP A 1 26  ? 6.062   0.796   21.489 1.00 31.65 ? 46  ASP A OD2 1 
ATOM   191  N N   . GLY A 1 27  ? 2.724   -0.747  18.394 1.00 24.96 ? 47  GLY A N   1 
ATOM   192  C CA  . GLY A 1 27  ? 2.686   -0.393  16.988 1.00 24.56 ? 47  GLY A CA  1 
ATOM   193  C C   . GLY A 1 27  ? 4.038   -0.395  16.311 1.00 24.71 ? 47  GLY A C   1 
ATOM   194  O O   . GLY A 1 27  ? 4.097   -0.404  15.070 1.00 24.53 ? 47  GLY A O   1 
ATOM   195  N N   . VAL A 1 28  ? 5.124   -0.356  17.076 1.00 25.80 ? 48  VAL A N   1 
ATOM   196  C CA  . VAL A 1 28  ? 6.466   -0.494  16.532 1.00 29.20 ? 48  VAL A CA  1 
ATOM   197  C C   . VAL A 1 28  ? 7.067   -1.845  16.916 1.00 25.86 ? 48  VAL A C   1 
ATOM   198  O O   . VAL A 1 28  ? 8.276   -2.048  16.811 1.00 31.63 ? 48  VAL A O   1 
ATOM   199  C CB  . VAL A 1 28  ? 7.372   0.681   16.945 1.00 27.34 ? 48  VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 28  ? 6.725   2.010   16.576 1.00 32.21 ? 48  VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 28  ? 7.673   0.646   18.437 1.00 29.41 ? 48  VAL A CG2 1 
ATOM   202  N N   . GLY A 1 29  ? 6.223   -2.777  17.342 1.00 24.84 ? 49  GLY A N   1 
ATOM   203  C CA  . GLY A 1 29  ? 6.653   -4.119  17.661 1.00 26.93 ? 49  GLY A CA  1 
ATOM   204  C C   . GLY A 1 29  ? 7.181   -4.290  19.062 1.00 26.57 ? 49  GLY A C   1 
ATOM   205  O O   . GLY A 1 29  ? 7.755   -5.341  19.366 1.00 30.65 ? 49  GLY A O   1 
ATOM   206  N N   . VAL A 1 30  ? 6.995   -3.301  19.924 1.00 25.29 ? 50  VAL A N   1 
ATOM   207  C CA  . VAL A 1 30  ? 7.535   -3.323  21.276 1.00 28.11 ? 50  VAL A CA  1 
ATOM   208  C C   . VAL A 1 30  ? 6.385   -3.618  22.226 1.00 26.42 ? 50  VAL A C   1 
ATOM   209  O O   . VAL A 1 30  ? 5.474   -2.803  22.399 1.00 25.48 ? 50  VAL A O   1 
ATOM   210  C CB  . VAL A 1 30  ? 8.230   -2.001  21.621 1.00 29.26 ? 50  VAL A CB  1 
ATOM   211  C CG1 . VAL A 1 30  ? 8.651   -1.984  23.088 1.00 30.74 ? 50  VAL A CG1 1 
ATOM   212  C CG2 . VAL A 1 30  ? 9.426   -1.794  20.702 1.00 33.40 ? 50  VAL A CG2 1 
ATOM   213  N N   . TRP A 1 31  ? 6.424   -4.782  22.862 1.00 29.38 ? 51  TRP A N   1 
ATOM   214  C CA  . TRP A 1 31  ? 5.351   -5.155  23.764 1.00 25.52 ? 51  TRP A CA  1 
ATOM   215  C C   . TRP A 1 31  ? 5.507   -4.408  25.080 1.00 24.59 ? 51  TRP A C   1 
ATOM   216  O O   . TRP A 1 31  ? 6.619   -4.232  25.584 1.00 26.61 ? 51  TRP A O   1 
ATOM   217  C CB  . TRP A 1 31  ? 5.331   -6.668  23.960 1.00 24.95 ? 51  TRP A CB  1 
ATOM   218  C CG  . TRP A 1 31  ? 4.804   -7.305  22.713 1.00 27.90 ? 51  TRP A CG  1 
ATOM   219  C CD1 . TRP A 1 31  ? 5.511   -7.596  21.583 1.00 32.96 ? 51  TRP A CD1 1 
ATOM   220  C CD2 . TRP A 1 31  ? 3.446   -7.664  22.441 1.00 27.01 ? 51  TRP A CD2 1 
ATOM   221  N NE1 . TRP A 1 31  ? 4.681   -8.139  20.632 1.00 35.25 ? 51  TRP A NE1 1 
ATOM   222  C CE2 . TRP A 1 31  ? 3.407   -8.189  21.134 1.00 30.53 ? 51  TRP A CE2 1 
ATOM   223  C CE3 . TRP A 1 31  ? 2.261   -7.600  23.178 1.00 28.20 ? 51  TRP A CE3 1 
ATOM   224  C CZ2 . TRP A 1 31  ? 2.231   -8.651  20.552 1.00 33.33 ? 51  TRP A CZ2 1 
ATOM   225  C CZ3 . TRP A 1 31  ? 1.094   -8.060  22.598 1.00 28.95 ? 51  TRP A CZ3 1 
ATOM   226  C CH2 . TRP A 1 31  ? 1.087   -8.576  21.296 1.00 34.06 ? 51  TRP A CH2 1 
ATOM   227  N N   . THR A 1 32  ? 4.379   -3.937  25.605 1.00 21.88 ? 52  THR A N   1 
ATOM   228  C CA  . THR A 1 32  ? 4.330   -2.930  26.654 1.00 25.14 ? 52  THR A CA  1 
ATOM   229  C C   . THR A 1 32  ? 3.295   -3.360  27.682 1.00 23.17 ? 52  THR A C   1 
ATOM   230  O O   . THR A 1 32  ? 2.293   -3.989  27.333 1.00 26.44 ? 52  THR A O   1 
ATOM   231  C CB  . THR A 1 32  ? 3.971   -1.558  26.058 1.00 28.06 ? 52  THR A CB  1 
ATOM   232  O OG1 . THR A 1 32  ? 4.828   -1.289  24.939 1.00 27.51 ? 52  THR A OG1 1 
ATOM   233  C CG2 . THR A 1 32  ? 4.138   -0.445  27.082 1.00 26.54 ? 52  THR A CG2 1 
ATOM   234  N N   . ILE A 1 33  ? 3.541   -3.045  28.956 1.00 23.55 ? 53  ILE A N   1 
ATOM   235  C CA  . ILE A 1 33  ? 2.658   -3.494  30.024 1.00 23.83 ? 53  ILE A CA  1 
ATOM   236  C C   . ILE A 1 33  ? 2.719   -2.500  31.174 1.00 25.63 ? 53  ILE A C   1 
ATOM   237  O O   . ILE A 1 33  ? 3.662   -1.719  31.299 1.00 25.34 ? 53  ILE A O   1 
ATOM   238  C CB  . ILE A 1 33  ? 3.028   -4.923  30.498 1.00 24.73 ? 53  ILE A CB  1 
ATOM   239  C CG1 . ILE A 1 33  ? 1.837   -5.597  31.173 1.00 23.55 ? 53  ILE A CG1 1 
ATOM   240  C CG2 . ILE A 1 33  ? 4.251   -4.889  31.411 1.00 26.27 ? 53  ILE A CG2 1 
ATOM   241  C CD1 . ILE A 1 33  ? 2.028   -7.097  31.382 1.00 24.93 ? 53  ILE A CD1 1 
ATOM   242  N N   . GLY A 1 34  ? 1.687   -2.532  32.014 1.00 25.85 ? 54  GLY A N   1 
ATOM   243  C CA  . GLY A 1 34  ? 1.608   -1.674  33.180 1.00 23.30 ? 54  GLY A CA  1 
ATOM   244  C C   . GLY A 1 34  ? 1.468   -0.212  32.808 1.00 25.20 ? 54  GLY A C   1 
ATOM   245  O O   . GLY A 1 34  ? 0.531   0.168   32.097 1.00 30.56 ? 54  GLY A O   1 
ATOM   246  N N   . PHE A 1 35  ? 2.402   0.613   33.275 1.00 25.99 ? 55  PHE A N   1 
ATOM   247  C CA  . PHE A 1 35  ? 2.411   2.035   32.949 1.00 26.31 ? 55  PHE A CA  1 
ATOM   248  C C   . PHE A 1 35  ? 3.541   2.334   31.973 1.00 25.98 ? 55  PHE A C   1 
ATOM   249  O O   . PHE A 1 35  ? 4.463   3.087   32.299 1.00 31.67 ? 55  PHE A O   1 
ATOM   250  C CB  . PHE A 1 35  ? 2.572   2.885   34.216 1.00 28.77 ? 55  PHE A CB  1 
ATOM   251  C CG  . PHE A 1 35  ? 1.518   2.638   35.255 1.00 28.98 ? 55  PHE A CG  1 
ATOM   252  C CD1 . PHE A 1 35  ? 0.227   3.107   35.085 1.00 28.99 ? 55  PHE A CD1 1 
ATOM   253  C CD2 . PHE A 1 35  ? 1.826   1.939   36.412 1.00 26.39 ? 55  PHE A CD2 1 
ATOM   254  C CE1 . PHE A 1 35  ? -0.742  2.879   36.052 1.00 27.63 ? 55  PHE A CE1 1 
ATOM   255  C CE2 . PHE A 1 35  ? 0.864   1.710   37.381 1.00 30.61 ? 55  PHE A CE2 1 
ATOM   256  C CZ  . PHE A 1 35  ? -0.422  2.174   37.199 1.00 33.95 ? 55  PHE A CZ  1 
ATOM   257  N N   . GLY A 1 36  ? 3.492   1.730   30.787 1.00 24.13 ? 56  GLY A N   1 
ATOM   258  C CA  . GLY A 1 36  ? 4.476   1.987   29.757 1.00 26.50 ? 56  GLY A CA  1 
ATOM   259  C C   . GLY A 1 36  ? 5.755   1.187   29.845 1.00 27.07 ? 56  GLY A C   1 
ATOM   260  O O   . GLY A 1 36  ? 6.724   1.526   29.156 1.00 28.71 ? 56  GLY A O   1 
ATOM   261  N N   . THR A 1 37  ? 5.797   0.135   30.661 1.00 24.71 ? 57  THR A N   1 
ATOM   262  C CA  . THR A 1 37  ? 7.010   -0.657  30.817 1.00 23.53 ? 57  THR A CA  1 
ATOM   263  C C   . THR A 1 37  ? 7.220   -1.590  29.627 1.00 20.28 ? 57  THR A C   1 
ATOM   264  O O   . THR A 1 37  ? 6.285   -2.247  29.158 1.00 23.83 ? 57  THR A O   1 
ATOM   265  C CB  . THR A 1 37  ? 6.938   -1.469  32.111 1.00 23.08 ? 57  THR A CB  1 
ATOM   266  O OG1 . THR A 1 37  ? 6.923   -0.579  33.235 1.00 22.94 ? 57  THR A OG1 1 
ATOM   267  C CG2 . THR A 1 37  ? 8.129   -2.423  32.229 1.00 25.19 ? 57  THR A CG2 1 
ATOM   268  N N   . ILE A 1 38  ? 8.454   -1.632  29.129 1.00 22.88 ? 58  ILE A N   1 
ATOM   269  C CA  . ILE A 1 38  ? 8.834   -2.539  28.054 1.00 22.38 ? 58  ILE A CA  1 
ATOM   270  C C   . ILE A 1 38  ? 9.928   -3.509  28.465 1.00 24.99 ? 58  ILE A C   1 
ATOM   271  O O   . ILE A 1 38  ? 10.172  -4.486  27.742 1.00 25.72 ? 58  ILE A O   1 
ATOM   272  C CB  . ILE A 1 38  ? 9.269   -1.769  26.786 1.00 25.89 ? 58  ILE A CB  1 
ATOM   273  C CG1 . ILE A 1 38  ? 10.596  -1.049  27.038 1.00 26.30 ? 58  ILE A CG1 1 
ATOM   274  C CG2 . ILE A 1 38  ? 8.199   -0.772  26.387 1.00 27.60 ? 58  ILE A CG2 1 
ATOM   275  C CD1 . ILE A 1 38  ? 11.154  -0.364  25.800 1.00 34.13 ? 58  ILE A CD1 1 
ATOM   276  N N   . LYS A 1 39  ? 10.588  -3.283  29.601 1.00 25.59 ? 59  LYS A N   1 
ATOM   277  C CA  . LYS A 1 39  ? 11.632  -4.170  30.098 1.00 26.15 ? 59  LYS A CA  1 
ATOM   278  C C   . LYS A 1 39  ? 11.487  -4.239  31.607 1.00 22.67 ? 59  LYS A C   1 
ATOM   279  O O   . LYS A 1 39  ? 11.413  -3.202  32.268 1.00 24.50 ? 59  LYS A O   1 
ATOM   280  C CB  . LYS A 1 39  ? 13.032  -3.663  29.732 1.00 30.24 ? 59  LYS A CB  1 
ATOM   281  C CG  . LYS A 1 39  ? 14.166  -4.584  30.152 1.00 35.15 ? 59  LYS A CG  1 
ATOM   282  C CD  . LYS A 1 39  ? 15.430  -4.326  29.347 1.00 40.52 ? 59  LYS A CD  1 
ATOM   283  C CE  . LYS A 1 39  ? 15.170  -4.373  27.855 1.00 48.20 ? 59  LYS A CE  1 
ATOM   284  N NZ  . LYS A 1 39  ? 16.417  -4.668  27.097 1.00 66.29 ? 59  LYS A NZ  1 
ATOM   285  N N   . TYR A 1 40  ? 11.446  -5.452  32.144 1.00 23.68 ? 60  TYR A N   1 
ATOM   286  C CA  . TYR A 1 40  ? 11.352  -5.640  33.580 1.00 23.57 ? 60  TYR A CA  1 
ATOM   287  C C   . TYR A 1 40  ? 12.684  -5.277  34.229 1.00 23.83 ? 60  TYR A C   1 
ATOM   288  O O   . TYR A 1 40  ? 13.714  -5.216  33.559 1.00 25.24 ? 60  TYR A O   1 
ATOM   289  C CB  . TYR A 1 40  ? 10.945  -7.081  33.874 1.00 23.04 ? 60  TYR A CB  1 
ATOM   290  C CG  . TYR A 1 40  ? 9.612   -7.452  33.267 1.00 20.38 ? 60  TYR A CG  1 
ATOM   291  C CD1 . TYR A 1 40  ? 8.459   -6.752  33.602 1.00 21.90 ? 60  TYR A CD1 1 
ATOM   292  C CD2 . TYR A 1 40  ? 9.508   -8.483  32.342 1.00 21.79 ? 60  TYR A CD2 1 
ATOM   293  C CE1 . TYR A 1 40  ? 7.235   -7.085  33.050 1.00 25.00 ? 60  TYR A CE1 1 
ATOM   294  C CE2 . TYR A 1 40  ? 8.288   -8.826  31.784 1.00 23.08 ? 60  TYR A CE2 1 
ATOM   295  C CZ  . TYR A 1 40  ? 7.154   -8.118  32.136 1.00 24.30 ? 60  TYR A CZ  1 
ATOM   296  O OH  . TYR A 1 40  ? 5.937   -8.445  31.579 1.00 26.00 ? 60  TYR A OH  1 
ATOM   297  N N   . PRO A 1 41  ? 12.701  -5.038  35.547 1.00 23.55 ? 61  PRO A N   1 
ATOM   298  C CA  . PRO A 1 41  ? 13.949  -4.589  36.187 1.00 26.99 ? 61  PRO A CA  1 
ATOM   299  C C   . PRO A 1 41  ? 15.069  -5.612  36.140 1.00 27.61 ? 61  PRO A C   1 
ATOM   300  O O   . PRO A 1 41  ? 16.223  -5.244  36.393 1.00 29.27 ? 61  PRO A O   1 
ATOM   301  C CB  . PRO A 1 41  ? 13.522  -4.291  37.629 1.00 26.99 ? 61  PRO A CB  1 
ATOM   302  C CG  . PRO A 1 41  ? 12.040  -4.127  37.574 1.00 23.21 ? 61  PRO A CG  1 
ATOM   303  C CD  . PRO A 1 41  ? 11.557  -4.999  36.474 1.00 22.12 ? 61  PRO A CD  1 
ATOM   304  N N   . ASN A 1 42  ? 14.777  -6.869  35.819 1.00 23.91 ? 62  ASN A N   1 
ATOM   305  C CA  . ASN A 1 42  ? 15.807  -7.881  35.649 1.00 27.06 ? 62  ASN A CA  1 
ATOM   306  C C   . ASN A 1 42  ? 16.359  -7.918  34.231 1.00 29.51 ? 62  ASN A C   1 
ATOM   307  O O   . ASN A 1 42  ? 17.160  -8.802  33.913 1.00 27.98 ? 62  ASN A O   1 
ATOM   308  C CB  . ASN A 1 42  ? 15.265  -9.261  36.051 1.00 23.91 ? 62  ASN A CB  1 
ATOM   309  C CG  . ASN A 1 42  ? 14.088  -9.704  35.197 1.00 32.06 ? 62  ASN A CG  1 
ATOM   310  O OD1 . ASN A 1 42  ? 13.609  -8.962  34.338 1.00 26.70 ? 62  ASN A OD1 1 
ATOM   311  N ND2 . ASN A 1 42  ? 13.624  -10.927 35.421 1.00 24.88 ? 62  ASN A ND2 1 
ATOM   312  N N   . GLY A 1 43  ? 15.954  -6.977  33.378 1.00 27.99 ? 63  GLY A N   1 
ATOM   313  C CA  . GLY A 1 43  ? 16.416  -6.923  32.007 1.00 27.61 ? 63  GLY A CA  1 
ATOM   314  C C   . GLY A 1 43  ? 15.620  -7.743  31.015 1.00 33.11 ? 63  GLY A C   1 
ATOM   315  O O   . GLY A 1 43  ? 15.937  -7.715  29.818 1.00 34.66 ? 63  GLY A O   1 
ATOM   316  N N   . VAL A 1 44  ? 14.599  -8.465  31.462 1.00 26.41 ? 64  VAL A N   1 
ATOM   317  C CA  . VAL A 1 44  ? 13.806  -9.308  30.575 1.00 27.71 ? 64  VAL A CA  1 
ATOM   318  C C   . VAL A 1 44  ? 12.777  -8.447  29.855 1.00 26.95 ? 64  VAL A C   1 
ATOM   319  O O   . VAL A 1 44  ? 12.044  -7.678  30.484 1.00 24.80 ? 64  VAL A O   1 
ATOM   320  C CB  . VAL A 1 44  ? 13.130  -10.436 31.370 1.00 26.89 ? 64  VAL A CB  1 
ATOM   321  C CG1 . VAL A 1 44  ? 12.158  -11.204 30.490 1.00 28.28 ? 64  VAL A CG1 1 
ATOM   322  C CG2 . VAL A 1 44  ? 14.185  -11.365 31.962 1.00 28.49 ? 64  VAL A CG2 1 
ATOM   323  N N   . ARG A 1 45  ? 12.719  -8.570  28.531 1.00 26.46 ? 65  ARG A N   1 
ATOM   324  C CA  . ARG A 1 45  ? 11.767  -7.783  27.762 1.00 28.19 ? 65  ARG A CA  1 
ATOM   325  C C   . ARG A 1 45  ? 10.342  -8.285  27.961 1.00 24.63 ? 65  ARG A C   1 
ATOM   326  O O   . ARG A 1 45  ? 10.092  -9.492  28.039 1.00 25.79 ? 65  ARG A O   1 
ATOM   327  C CB  . ARG A 1 45  ? 12.130  -7.805  26.275 1.00 33.11 ? 65  ARG A CB  1 
ATOM   328  C CG  . ARG A 1 45  ? 13.548  -7.348  25.985 1.00 41.94 ? 65  ARG A CG  1 
ATOM   329  C CD  . ARG A 1 45  ? 13.946  -7.637  24.548 1.00 61.98 ? 65  ARG A CD  1 
ATOM   330  N NE  . ARG A 1 45  ? 15.372  -7.424  24.339 1.00 72.14 ? 65  ARG A NE  1 
ATOM   331  C CZ  . ARG A 1 45  ? 15.889  -6.329  23.799 1.00 75.58 ? 65  ARG A CZ  1 
ATOM   332  N NH1 . ARG A 1 45  ? 15.121  -5.336  23.382 1.00 74.92 ? 65  ARG A NH1 1 
ATOM   333  N NH2 . ARG A 1 45  ? 17.210  -6.226  23.677 1.00 77.27 ? 65  ARG A NH2 1 
ATOM   334  N N   . VAL A 1 46  ? 9.407   -7.337  28.058 1.00 23.54 ? 66  VAL A N   1 
ATOM   335  C CA  . VAL A 1 46  ? 7.986   -7.660  28.041 1.00 22.59 ? 66  VAL A CA  1 
ATOM   336  C C   . VAL A 1 46  ? 7.653   -8.383  26.741 1.00 24.70 ? 66  VAL A C   1 
ATOM   337  O O   . VAL A 1 46  ? 8.182   -8.049  25.672 1.00 28.81 ? 66  VAL A O   1 
ATOM   338  C CB  . VAL A 1 46  ? 7.160   -6.369  28.189 1.00 25.51 ? 66  VAL A CB  1 
ATOM   339  C CG1 . VAL A 1 46  ? 5.666   -6.641  28.023 1.00 26.01 ? 66  VAL A CG1 1 
ATOM   340  C CG2 . VAL A 1 46  ? 7.460   -5.684  29.533 1.00 21.10 ? 66  VAL A CG2 1 
ATOM   341  N N   . LYS A 1 47  ? 6.778   -9.387  26.821 1.00 27.47 ? 67  LYS A N   1 
ATOM   342  C CA  . LYS A 1 47  ? 6.389   -10.133 25.632 1.00 28.95 ? 67  LYS A CA  1 
ATOM   343  C C   . LYS A 1 47  ? 4.884   -10.360 25.614 1.00 30.05 ? 67  LYS A C   1 
ATOM   344  O O   . LYS A 1 47  ? 4.197   -10.227 26.630 1.00 27.91 ? 67  LYS A O   1 
ATOM   345  C CB  . LYS A 1 47  ? 7.125   -11.478 25.533 1.00 32.91 ? 67  LYS A CB  1 
ATOM   346  C CG  . LYS A 1 47  ? 6.811   -12.462 26.639 1.00 33.90 ? 67  LYS A CG  1 
ATOM   347  C CD  . LYS A 1 47  ? 7.801   -13.618 26.623 1.00 44.26 ? 67  LYS A CD  1 
ATOM   348  C CE  . LYS A 1 47  ? 7.344   -14.757 27.521 1.00 43.09 ? 67  LYS A CE  1 
ATOM   349  N NZ  . LYS A 1 47  ? 7.393   -14.382 28.961 1.00 51.77 ? 67  LYS A NZ  1 
ATOM   350  N N   . LYS A 1 48  ? 4.385   -10.720 24.430 1.00 30.77 ? 68  LYS A N   1 
ATOM   351  C CA  . LYS A 1 48  ? 2.972   -11.027 24.260 1.00 26.92 ? 68  LYS A CA  1 
ATOM   352  C C   . LYS A 1 48  ? 2.557   -12.146 25.207 1.00 28.87 ? 68  LYS A C   1 
ATOM   353  O O   . LYS A 1 48  ? 3.271   -13.139 25.373 1.00 32.77 ? 68  LYS A O   1 
ATOM   354  C CB  . LYS A 1 48  ? 2.696   -11.428 22.807 1.00 32.86 ? 68  LYS A CB  1 
ATOM   355  C CG  . LYS A 1 48  ? 1.357   -12.114 22.567 1.00 35.85 ? 68  LYS A CG  1 
ATOM   356  C CD  . LYS A 1 48  ? 0.991   -12.125 21.082 1.00 38.88 ? 68  LYS A CD  1 
ATOM   357  C CE  . LYS A 1 48  ? -0.518  -12.103 20.875 1.00 44.67 ? 68  LYS A CE  1 
ATOM   358  N NZ  . LYS A 1 48  ? -0.896  -12.465 19.477 1.00 60.28 ? 68  LYS A NZ  1 
ATOM   359  N N   . GLY A 1 49  ? 1.393   -11.978 25.832 1.00 29.45 ? 69  GLY A N   1 
ATOM   360  C CA  . GLY A 1 49  ? 0.891   -12.928 26.795 1.00 32.44 ? 69  GLY A CA  1 
ATOM   361  C C   . GLY A 1 49  ? 1.219   -12.599 28.236 1.00 29.75 ? 69  GLY A C   1 
ATOM   362  O O   . GLY A 1 49  ? 0.625   -13.193 29.142 1.00 34.45 ? 69  GLY A O   1 
ATOM   363  N N   . ASP A 1 50  ? 2.142   -11.668 28.472 1.00 27.24 ? 70  ASP A N   1 
ATOM   364  C CA  . ASP A 1 50  ? 2.491   -11.288 29.834 1.00 26.53 ? 70  ASP A CA  1 
ATOM   365  C C   . ASP A 1 50  ? 1.315   -10.611 30.525 1.00 29.38 ? 70  ASP A C   1 
ATOM   366  O O   . ASP A 1 50  ? 0.506   -9.917  29.899 1.00 30.79 ? 70  ASP A O   1 
ATOM   367  C CB  . ASP A 1 50  ? 3.697   -10.345 29.848 1.00 24.99 ? 70  ASP A CB  1 
ATOM   368  C CG  . ASP A 1 50  ? 5.011   -11.065 29.619 1.00 30.02 ? 70  ASP A CG  1 
ATOM   369  O OD1 . ASP A 1 50  ? 5.005   -12.313 29.495 1.00 29.56 ? 70  ASP A OD1 1 
ATOM   370  O OD2 . ASP A 1 50  ? 6.055   -10.379 29.564 1.00 27.65 ? 70  ASP A OD2 1 
ATOM   371  N N   . THR A 1 51  ? 1.224   -10.827 31.834 1.00 27.10 ? 71  THR A N   1 
ATOM   372  C CA  . THR A 1 51  ? 0.263   -10.143 32.683 1.00 26.18 ? 71  THR A CA  1 
ATOM   373  C C   . THR A 1 51  ? 0.988   -9.680  33.937 1.00 30.21 ? 71  THR A C   1 
ATOM   374  O O   . THR A 1 51  ? 1.996   -10.268 34.333 1.00 29.53 ? 71  THR A O   1 
ATOM   375  C CB  . THR A 1 51  ? -0.917  -11.048 33.071 1.00 34.57 ? 71  THR A CB  1 
ATOM   376  O OG1 . THR A 1 51  ? -0.439  -12.142 33.869 1.00 39.54 ? 71  THR A OG1 1 
ATOM   377  C CG2 . THR A 1 51  ? -1.617  -11.589 31.831 1.00 30.61 ? 71  THR A CG2 1 
ATOM   378  N N   . CYS A 1 52  ? 0.486   -8.612  34.554 1.00 28.69 ? 72  CYS A N   1 
ATOM   379  C CA  . CYS A 1 52  ? 1.036   -8.179  35.830 1.00 26.72 ? 72  CYS A CA  1 
ATOM   380  C C   . CYS A 1 52  ? -0.077  -7.618  36.702 1.00 30.26 ? 72  CYS A C   1 
ATOM   381  O O   . CYS A 1 52  ? -1.184  -7.331  36.239 1.00 31.45 ? 72  CYS A O   1 
ATOM   382  C CB  . CYS A 1 52  ? 2.152   -7.138  35.654 1.00 25.02 ? 72  CYS A CB  1 
ATOM   383  S SG  . CYS A 1 52  ? 1.623   -5.516  35.026 1.00 29.19 ? 72  CYS A SG  1 
ATOM   384  N N   . THR A 1 53  ? 0.227   -7.482  37.987 1.00 26.45 ? 73  THR A N   1 
ATOM   385  C CA  . THR A 1 53  ? -0.662  -6.814  38.922 1.00 31.35 ? 73  THR A CA  1 
ATOM   386  C C   . THR A 1 53  ? -0.371  -5.317  38.939 1.00 30.13 ? 73  THR A C   1 
ATOM   387  O O   . THR A 1 53  ? 0.673   -4.855  38.471 1.00 27.97 ? 73  THR A O   1 
ATOM   388  C CB  . THR A 1 53  ? -0.496  -7.384  40.328 1.00 29.38 ? 73  THR A CB  1 
ATOM   389  O OG1 . THR A 1 53  ? 0.810   -7.052  40.811 1.00 29.97 ? 73  THR A OG1 1 
ATOM   390  C CG2 . THR A 1 53  ? -0.650  -8.900  40.309 1.00 33.24 ? 73  THR A CG2 1 
ATOM   391  N N   . GLU A 1 54  ? -1.313  -4.556  39.498 1.00 34.56 ? 74  GLU A N   1 
ATOM   392  C CA  . GLU A 1 54  ? -1.119  -3.114  39.598 1.00 36.61 ? 74  GLU A CA  1 
ATOM   393  C C   . GLU A 1 54  ? 0.102   -2.784  40.452 1.00 27.52 ? 74  GLU A C   1 
ATOM   394  O O   . GLU A 1 54  ? 0.848   -1.846  40.150 1.00 32.60 ? 74  GLU A O   1 
ATOM   395  C CB  . GLU A 1 54  ? -2.378  -2.458  40.165 1.00 41.64 ? 74  GLU A CB  1 
ATOM   396  C CG  . GLU A 1 54  ? -2.270  -0.957  40.349 1.00 50.46 ? 74  GLU A CG  1 
ATOM   397  C CD  . GLU A 1 54  ? -3.590  -0.326  40.742 1.00 70.68 ? 74  GLU A CD  1 
ATOM   398  O OE1 . GLU A 1 54  ? -4.536  -1.075  41.067 1.00 73.67 ? 74  GLU A OE1 1 
ATOM   399  O OE2 . GLU A 1 54  ? -3.683  0.920   40.726 1.00 78.12 ? 74  GLU A OE2 1 
ATOM   400  N N   . GLN A 1 55  ? 0.329   -3.556  41.515 1.00 30.23 ? 75  GLN A N   1 
ATOM   401  C CA  . GLN A 1 55  ? 1.489   -3.336  42.377 1.00 29.83 ? 75  GLN A CA  1 
ATOM   402  C C   . GLN A 1 55  ? 2.791   -3.550  41.614 1.00 27.32 ? 75  GLN A C   1 
ATOM   403  O O   . GLN A 1 55  ? 3.737   -2.748  41.717 1.00 27.74 ? 75  GLN A O   1 
ATOM   404  C CB  . GLN A 1 55  ? 1.403   -4.274  43.584 1.00 33.91 ? 75  GLN A CB  1 
ATOM   405  C CG  . GLN A 1 55  ? 2.462   -4.068  44.640 1.00 40.33 ? 75  GLN A CG  1 
ATOM   406  C CD  . GLN A 1 55  ? 2.388   -5.125  45.730 1.00 51.58 ? 75  GLN A CD  1 
ATOM   407  O OE1 . GLN A 1 55  ? 2.141   -4.818  46.897 1.00 58.44 ? 75  GLN A OE1 1 
ATOM   408  N NE2 . GLN A 1 55  ? 2.588   -6.382  45.348 1.00 50.42 ? 75  GLN A NE2 1 
ATOM   409  N N   . GLN A 1 56  ? 2.859   -4.642  40.844 1.00 26.61 ? 76  GLN A N   1 
ATOM   410  C CA  . GLN A 1 56  ? 4.022   -4.887  40.004 1.00 23.91 ? 76  GLN A CA  1 
ATOM   411  C C   . GLN A 1 56  ? 4.220   -3.755  39.004 1.00 25.24 ? 76  GLN A C   1 
ATOM   412  O O   . GLN A 1 56  ? 5.348   -3.304  38.786 1.00 25.82 ? 76  GLN A O   1 
ATOM   413  C CB  . GLN A 1 56  ? 3.874   -6.222  39.276 1.00 23.34 ? 76  GLN A CB  1 
ATOM   414  C CG  . GLN A 1 56  ? 4.166   -7.427  40.165 1.00 25.22 ? 76  GLN A CG  1 
ATOM   415  C CD  . GLN A 1 56  ? 3.427   -8.681  39.732 1.00 32.06 ? 76  GLN A CD  1 
ATOM   416  O OE1 . GLN A 1 56  ? 2.827   -8.735  38.657 1.00 27.29 ? 76  GLN A OE1 1 
ATOM   417  N NE2 . GLN A 1 56  ? 3.478   -9.709  40.574 1.00 27.42 ? 76  GLN A NE2 1 
ATOM   418  N N   . ALA A 1 57  ? 3.133   -3.290  38.385 1.00 26.51 ? 77  ALA A N   1 
ATOM   419  C CA  . ALA A 1 57  ? 3.243   -2.197  37.423 1.00 25.01 ? 77  ALA A CA  1 
ATOM   420  C C   . ALA A 1 57  ? 3.791   -0.937  38.079 1.00 26.44 ? 77  ALA A C   1 
ATOM   421  O O   . ALA A 1 57  ? 4.598   -0.216  37.479 1.00 24.65 ? 77  ALA A O   1 
ATOM   422  C CB  . ALA A 1 57  ? 1.883   -1.924  36.780 1.00 27.29 ? 77  ALA A CB  1 
ATOM   423  N N   . GLU A 1 58  ? 3.381   -0.661  39.317 1.00 27.94 ? 78  GLU A N   1 
ATOM   424  C CA  . GLU A 1 58  ? 3.918   0.507   40.009 1.00 25.88 ? 78  GLU A CA  1 
ATOM   425  C C   . GLU A 1 58  ? 5.417   0.353   40.247 1.00 25.24 ? 78  GLU A C   1 
ATOM   426  O O   . GLU A 1 58  ? 6.204   1.279   39.999 1.00 25.96 ? 78  GLU A O   1 
ATOM   427  C CB  . GLU A 1 58  ? 3.179   0.722   41.328 1.00 29.65 ? 78  GLU A CB  1 
ATOM   428  C CG  . GLU A 1 58  ? 3.737   1.876   42.132 1.00 40.76 ? 78  GLU A CG  1 
ATOM   429  C CD  . GLU A 1 58  ? 2.902   3.125   41.966 1.00 58.31 ? 78  GLU A CD  1 
ATOM   430  O OE1 . GLU A 1 58  ? 1.832   3.032   41.325 1.00 51.75 ? 78  GLU A OE1 1 
ATOM   431  O OE2 . GLU A 1 58  ? 3.313   4.195   42.463 1.00 51.55 ? 78  GLU A OE2 1 
ATOM   432  N N   . THR A 1 59  ? 5.833   -0.825  40.725 1.00 23.41 ? 79  THR A N   1 
ATOM   433  C CA  . THR A 1 59  ? 7.264   -1.065  40.907 1.00 23.70 ? 79  THR A CA  1 
ATOM   434  C C   . THR A 1 59  ? 8.029   -0.906  39.599 1.00 24.78 ? 79  THR A C   1 
ATOM   435  O O   . THR A 1 59  ? 9.124   -0.325  39.573 1.00 24.57 ? 79  THR A O   1 
ATOM   436  C CB  . THR A 1 59  ? 7.492   -2.464  41.474 1.00 24.31 ? 79  THR A CB  1 
ATOM   437  O OG1 . THR A 1 59  ? 6.745   -2.606  42.684 1.00 29.83 ? 79  THR A OG1 1 
ATOM   438  C CG2 . THR A 1 59  ? 8.972   -2.701  41.756 1.00 26.27 ? 79  THR A CG2 1 
ATOM   439  N N   . TYR A 1 60  ? 7.469   -1.427  38.504 1.00 25.15 ? 80  TYR A N   1 
ATOM   440  C CA  . TYR A 1 60  ? 8.155   -1.371  37.216 1.00 21.94 ? 80  TYR A CA  1 
ATOM   441  C C   . TYR A 1 60  ? 8.292   0.066   36.736 1.00 24.60 ? 80  TYR A C   1 
ATOM   442  O O   . TYR A 1 60  ? 9.341   0.448   36.212 1.00 24.09 ? 80  TYR A O   1 
ATOM   443  C CB  . TYR A 1 60  ? 7.415   -2.211  36.173 1.00 20.61 ? 80  TYR A CB  1 
ATOM   444  C CG  . TYR A 1 60  ? 7.328   -3.690  36.487 1.00 23.53 ? 80  TYR A CG  1 
ATOM   445  C CD1 . TYR A 1 60  ? 8.251   -4.298  37.320 1.00 25.40 ? 80  TYR A CD1 1 
ATOM   446  C CD2 . TYR A 1 60  ? 6.316   -4.472  35.944 1.00 25.20 ? 80  TYR A CD2 1 
ATOM   447  C CE1 . TYR A 1 60  ? 8.172   -5.659  37.602 1.00 24.56 ? 80  TYR A CE1 1 
ATOM   448  C CE2 . TYR A 1 60  ? 6.230   -5.828  36.217 1.00 25.79 ? 80  TYR A CE2 1 
ATOM   449  C CZ  . TYR A 1 60  ? 7.159   -6.406  37.053 1.00 25.75 ? 80  TYR A CZ  1 
ATOM   450  O OH  . TYR A 1 60  ? 7.064   -7.754  37.325 1.00 29.96 ? 80  TYR A OH  1 
ATOM   451  N N   . LEU A 1 61  ? 7.245   0.874   36.908 1.00 23.21 ? 81  LEU A N   1 
ATOM   452  C CA  . LEU A 1 61  ? 7.322   2.280   36.515 1.00 24.52 ? 81  LEU A CA  1 
ATOM   453  C C   . LEU A 1 61  ? 8.373   3.021   37.331 1.00 27.36 ? 81  LEU A C   1 
ATOM   454  O O   . LEU A 1 61  ? 9.171   3.801   36.786 1.00 26.31 ? 81  LEU A O   1 
ATOM   455  C CB  . LEU A 1 61  ? 5.955   2.940   36.681 1.00 24.64 ? 81  LEU A CB  1 
ATOM   456  C CG  . LEU A 1 61  ? 5.933   4.467   36.569 1.00 23.90 ? 81  LEU A CG  1 
ATOM   457  C CD1 . LEU A 1 61  ? 6.379   4.903   35.184 1.00 26.34 ? 81  LEU A CD1 1 
ATOM   458  C CD2 . LEU A 1 61  ? 4.548   5.000   36.892 1.00 30.27 ? 81  LEU A CD2 1 
ATOM   459  N N   . LYS A 1 62  ? 8.391   2.792   38.646 1.00 26.33 ? 82  LYS A N   1 
ATOM   460  C CA  . LYS A 1 62  ? 9.407   3.434   39.471 1.00 26.01 ? 82  LYS A CA  1 
ATOM   461  C C   . LYS A 1 62  ? 10.802  3.028   39.019 1.00 27.70 ? 82  LYS A C   1 
ATOM   462  O O   . LYS A 1 62  ? 11.724  3.852   39.010 1.00 26.31 ? 82  LYS A O   1 
ATOM   463  C CB  . LYS A 1 62  ? 9.187   3.094   40.948 1.00 26.98 ? 82  LYS A CB  1 
ATOM   464  C CG  . LYS A 1 62  ? 7.898   3.672   41.514 1.00 32.06 ? 82  LYS A CG  1 
ATOM   465  C CD  . LYS A 1 62  ? 7.702   3.297   42.978 1.00 32.31 ? 82  LYS A CD  1 
ATOM   466  C CE  . LYS A 1 62  ? 8.634   4.094   43.875 1.00 47.12 ? 82  LYS A CE  1 
ATOM   467  N NZ  . LYS A 1 62  ? 7.880   4.965   44.822 1.00 57.21 ? 82  LYS A NZ  1 
ATOM   468  N N   . ASN A 1 63  ? 10.972  1.767   38.610 1.00 23.99 ? 83  ASN A N   1 
ATOM   469  C CA  . ASN A 1 63  ? 12.266  1.346   38.077 1.00 23.33 ? 83  ASN A CA  1 
ATOM   470  C C   . ASN A 1 63  ? 12.568  2.025   36.745 1.00 26.42 ? 83  ASN A C   1 
ATOM   471  O O   . ASN A 1 63  ? 13.709  2.425   36.493 1.00 29.38 ? 83  ASN A O   1 
ATOM   472  C CB  . ASN A 1 63  ? 12.315  -0.176  37.917 1.00 26.44 ? 83  ASN A CB  1 
ATOM   473  C CG  . ASN A 1 63  ? 13.666  -0.657  37.425 1.00 27.50 ? 83  ASN A CG  1 
ATOM   474  O OD1 . ASN A 1 63  ? 14.664  -0.565  38.143 1.00 35.24 ? 83  ASN A OD1 1 
ATOM   475  N ND2 . ASN A 1 63  ? 13.712  -1.145  36.189 1.00 27.18 ? 83  ASN A ND2 1 
ATOM   476  N N   . ASP A 1 64  ? 11.562  2.155   35.877 1.00 26.63 ? 84  ASP A N   1 
ATOM   477  C CA  . ASP A 1 64  ? 11.780  2.773   34.573 1.00 25.63 ? 84  ASP A CA  1 
ATOM   478  C C   . ASP A 1 64  ? 12.267  4.199   34.733 1.00 28.49 ? 84  ASP A C   1 
ATOM   479  O O   . ASP A 1 64  ? 13.038  4.696   33.902 1.00 26.84 ? 84  ASP A O   1 
ATOM   480  C CB  . ASP A 1 64  ? 10.495  2.795   33.739 1.00 25.96 ? 84  ASP A CB  1 
ATOM   481  C CG  . ASP A 1 64  ? 10.070  1.425   33.249 1.00 31.17 ? 84  ASP A CG  1 
ATOM   482  O OD1 . ASP A 1 64  ? 10.930  0.528   33.133 1.00 29.45 ? 84  ASP A OD1 1 
ATOM   483  O OD2 . ASP A 1 64  ? 8.852   1.244   33.041 1.00 28.96 ? 84  ASP A OD2 1 
ATOM   484  N N   . LEU A 1 65  ? 11.807  4.870   35.790 1.00 25.27 ? 85  LEU A N   1 
ATOM   485  C CA  . LEU A 1 65  ? 12.146  6.276   35.986 1.00 24.97 ? 85  LEU A CA  1 
ATOM   486  C C   . LEU A 1 65  ? 13.574  6.504   36.460 1.00 28.12 ? 85  LEU A C   1 
ATOM   487  O O   . LEU A 1 65  ? 14.048  7.643   36.381 1.00 27.64 ? 85  LEU A O   1 
ATOM   488  C CB  . LEU A 1 65  ? 11.185  6.917   36.982 1.00 24.80 ? 85  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 65  ? 9.953   7.512   36.316 1.00 30.34 ? 85  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 65  ? 8.843   7.628   37.310 1.00 32.15 ? 85  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 65  ? 10.300  8.876   35.727 1.00 26.13 ? 85  LEU A CD2 1 
ATOM   492  N N   . THR A 1 66  ? 14.259  5.470   36.960 1.00 29.15 ? 86  THR A N   1 
ATOM   493  C CA  . THR A 1 66  ? 15.565  5.668   37.583 1.00 27.51 ? 86  THR A CA  1 
ATOM   494  C C   . THR A 1 66  ? 16.587  6.267   36.619 1.00 33.63 ? 86  THR A C   1 
ATOM   495  O O   . THR A 1 66  ? 17.341  7.171   36.996 1.00 30.73 ? 86  THR A O   1 
ATOM   496  C CB  . THR A 1 66  ? 16.081  4.343   38.153 1.00 31.36 ? 86  THR A CB  1 
ATOM   497  O OG1 . THR A 1 66  ? 15.178  3.878   39.163 1.00 32.50 ? 86  THR A OG1 1 
ATOM   498  C CG2 . THR A 1 66  ? 17.460  4.531   38.767 1.00 33.68 ? 86  THR A CG2 1 
ATOM   499  N N   . LYS A 1 67  ? 16.637  5.774   35.375 1.00 30.76 ? 87  LYS A N   1 
ATOM   500  C CA  . LYS A 1 67  ? 17.600  6.314   34.417 1.00 25.21 ? 87  LYS A CA  1 
ATOM   501  C C   . LYS A 1 67  ? 17.350  7.796   34.158 1.00 28.10 ? 87  LYS A C   1 
ATOM   502  O O   . LYS A 1 67  ? 18.300  8.582   34.049 1.00 31.95 ? 87  LYS A O   1 
ATOM   503  C CB  . LYS A 1 67  ? 17.563  5.514   33.108 1.00 30.55 ? 87  LYS A CB  1 
ATOM   504  C CG  . LYS A 1 67  ? 16.224  5.486   32.368 1.00 27.84 ? 87  LYS A CG  1 
ATOM   505  C CD  . LYS A 1 67  ? 16.308  4.594   31.128 1.00 31.70 ? 87  LYS A CD  1 
ATOM   506  C CE  . LYS A 1 67  ? 15.603  3.254   31.321 1.00 42.87 ? 87  LYS A CE  1 
ATOM   507  N NZ  . LYS A 1 67  ? 14.132  3.415   31.524 1.00 43.04 ? 87  LYS A NZ  1 
ATOM   508  N N   . PHE A 1 68  ? 16.083  8.204   34.123 1.00 25.93 ? 88  PHE A N   1 
ATOM   509  C CA  . PHE A 1 68  ? 15.765  9.607   33.872 1.00 26.14 ? 88  PHE A CA  1 
ATOM   510  C C   . PHE A 1 68  ? 16.052  10.462  35.097 1.00 26.41 ? 88  PHE A C   1 
ATOM   511  O O   . PHE A 1 68  ? 16.489  11.613  34.973 1.00 26.45 ? 88  PHE A O   1 
ATOM   512  C CB  . PHE A 1 68  ? 14.303  9.729   33.458 1.00 24.48 ? 88  PHE A CB  1 
ATOM   513  C CG  . PHE A 1 68  ? 13.959  8.908   32.248 1.00 22.32 ? 88  PHE A CG  1 
ATOM   514  C CD1 . PHE A 1 68  ? 14.539  9.176   31.017 1.00 24.73 ? 88  PHE A CD1 1 
ATOM   515  C CD2 . PHE A 1 68  ? 13.076  7.846   32.351 1.00 23.76 ? 88  PHE A CD2 1 
ATOM   516  C CE1 . PHE A 1 68  ? 14.229  8.413   29.907 1.00 29.39 ? 88  PHE A CE1 1 
ATOM   517  C CE2 . PHE A 1 68  ? 12.757  7.081   31.239 1.00 23.78 ? 88  PHE A CE2 1 
ATOM   518  C CZ  . PHE A 1 68  ? 13.338  7.362   30.018 1.00 30.73 ? 88  PHE A CZ  1 
ATOM   519  N N   . GLU A 1 69  ? 15.810  9.910   36.289 1.00 24.99 ? 89  GLU A N   1 
ATOM   520  C CA  . GLU A 1 69  ? 16.168  10.608  37.518 1.00 26.10 ? 89  GLU A CA  1 
ATOM   521  C C   . GLU A 1 69  ? 17.671  10.844  37.579 1.00 29.62 ? 89  GLU A C   1 
ATOM   522  O O   . GLU A 1 69  ? 18.127  11.938  37.941 1.00 29.83 ? 89  GLU A O   1 
ATOM   523  C CB  . GLU A 1 69  ? 15.701  9.802   38.734 1.00 26.41 ? 89  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 69  ? 14.189  9.729   38.905 1.00 28.05 ? 89  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 69  ? 13.768  8.639   39.878 1.00 30.65 ? 89  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 69  ? 14.658  7.924   40.374 1.00 35.17 ? 89  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 69  ? 12.557  8.512   40.149 1.00 28.15 ? 89  GLU A OE2 1 
ATOM   528  N N   . VAL A 1 70  ? 18.453  9.826   37.215 1.00 30.96 ? 90  VAL A N   1 
ATOM   529  C CA  . VAL A 1 70  ? 19.906  9.964   37.174 1.00 37.30 ? 90  VAL A CA  1 
ATOM   530  C C   . VAL A 1 70  ? 20.303  11.057  36.191 1.00 30.74 ? 90  VAL A C   1 
ATOM   531  O O   . VAL A 1 70  ? 21.154  11.907  36.488 1.00 33.45 ? 90  VAL A O   1 
ATOM   532  C CB  . VAL A 1 70  ? 20.559  8.617   36.817 1.00 32.21 ? 90  VAL A CB  1 
ATOM   533  C CG1 . VAL A 1 70  ? 22.035  8.796   36.507 1.00 33.53 ? 90  VAL A CG1 1 
ATOM   534  C CG2 . VAL A 1 70  ? 20.361  7.628   37.943 1.00 32.06 ? 90  VAL A CG2 1 
ATOM   535  N N   . ALA A 1 71  ? 19.690  11.049  35.003 1.00 25.98 ? 91  ALA A N   1 
ATOM   536  C CA  . ALA A 1 71  ? 19.993  12.085  34.017 1.00 25.14 ? 91  ALA A CA  1 
ATOM   537  C C   . ALA A 1 71  ? 19.694  13.481  34.557 1.00 28.40 ? 91  ALA A C   1 
ATOM   538  O O   . ALA A 1 71  ? 20.500  14.402  34.382 1.00 29.87 ? 91  ALA A O   1 
ATOM   539  C CB  . ALA A 1 71  ? 19.210  11.838  32.725 1.00 26.95 ? 91  ALA A CB  1 
ATOM   540  N N   . ILE A 1 72  ? 18.539  13.664  35.206 1.00 25.95 ? 92  ILE A N   1 
ATOM   541  C CA  . ILE A 1 72  ? 18.182  14.991  35.714 1.00 24.54 ? 92  ILE A CA  1 
ATOM   542  C C   . ILE A 1 72  ? 19.155  15.429  36.795 1.00 29.68 ? 92  ILE A C   1 
ATOM   543  O O   . ILE A 1 72  ? 19.599  16.584  36.824 1.00 27.88 ? 92  ILE A O   1 
ATOM   544  C CB  . ILE A 1 72  ? 16.729  15.014  36.230 1.00 24.09 ? 92  ILE A CB  1 
ATOM   545  C CG1 . ILE A 1 72  ? 15.742  14.792  35.079 1.00 25.88 ? 92  ILE A CG1 1 
ATOM   546  C CG2 . ILE A 1 72  ? 16.430  16.312  36.975 1.00 26.97 ? 92  ILE A CG2 1 
ATOM   547  C CD1 . ILE A 1 72  ? 14.381  14.312  35.538 1.00 26.11 ? 92  ILE A CD1 1 
ATOM   548  N N   . ASN A 1 73  ? 19.507  14.520  37.701 1.00 29.19 ? 93  ASN A N   1 
ATOM   549  C CA  . ASN A 1 73  ? 20.400  14.896  38.790 1.00 29.46 ? 93  ASN A CA  1 
ATOM   550  C C   . ASN A 1 73  ? 21.804  15.200  38.287 1.00 33.75 ? 93  ASN A C   1 
ATOM   551  O O   . ASN A 1 73  ? 22.525  15.990  38.908 1.00 39.11 ? 93  ASN A O   1 
ATOM   552  C CB  . ASN A 1 73  ? 20.428  13.789  39.842 1.00 26.76 ? 93  ASN A CB  1 
ATOM   553  C CG  . ASN A 1 73  ? 19.198  13.807  40.724 1.00 34.13 ? 93  ASN A CG  1 
ATOM   554  O OD1 . ASN A 1 73  ? 18.748  14.868  41.163 1.00 39.97 ? 93  ASN A OD1 1 
ATOM   555  N ND2 . ASN A 1 73  ? 18.636  12.632  40.980 1.00 34.61 ? 93  ASN A ND2 1 
ATOM   556  N N   . LYS A 1 74  ? 22.209  14.592  37.172 1.00 30.32 ? 94  LYS A N   1 
ATOM   557  C CA  . LYS A 1 74  ? 23.503  14.919  36.584 1.00 30.02 ? 94  LYS A CA  1 
ATOM   558  C C   . LYS A 1 74  ? 23.460  16.240  35.822 1.00 35.80 ? 94  LYS A C   1 
ATOM   559  O O   . LYS A 1 74  ? 24.401  17.038  35.900 1.00 36.49 ? 94  LYS A O   1 
ATOM   560  C CB  . LYS A 1 74  ? 23.948  13.788  35.657 1.00 39.07 ? 94  LYS A CB  1 
ATOM   561  C CG  . LYS A 1 74  ? 25.242  14.052  34.914 1.00 39.73 ? 94  LYS A CG  1 
ATOM   562  C CD  . LYS A 1 74  ? 25.566  12.902  33.976 1.00 53.59 ? 94  LYS A CD  1 
ATOM   563  C CE  . LYS A 1 74  ? 25.171  13.243  32.549 1.00 52.18 ? 94  LYS A CE  1 
ATOM   564  N NZ  . LYS A 1 74  ? 24.504  12.091  31.883 1.00 58.69 ? 94  LYS A NZ  1 
ATOM   565  N N   . LEU A 1 75  ? 22.377  16.490  35.092 1.00 29.01 ? 95  LEU A N   1 
ATOM   566  C CA  . LEU A 1 75  ? 22.332  17.603  34.153 1.00 25.74 ? 95  LEU A CA  1 
ATOM   567  C C   . LEU A 1 75  ? 21.926  18.923  34.788 1.00 27.80 ? 95  LEU A C   1 
ATOM   568  O O   . LEU A 1 75  ? 22.354  19.980  34.306 1.00 28.16 ? 95  LEU A O   1 
ATOM   569  C CB  . LEU A 1 75  ? 21.367  17.285  33.010 1.00 26.43 ? 95  LEU A CB  1 
ATOM   570  C CG  . LEU A 1 75  ? 21.822  16.228  32.001 1.00 29.25 ? 95  LEU A CG  1 
ATOM   571  C CD1 . LEU A 1 75  ? 20.647  15.768  31.152 1.00 26.06 ? 95  LEU A CD1 1 
ATOM   572  C CD2 . LEU A 1 75  ? 22.940  16.776  31.123 1.00 28.33 ? 95  LEU A CD2 1 
ATOM   573  N N   . VAL A 1 76  ? 21.099  18.900  35.832 1.00 26.80 ? 96  VAL A N   1 
ATOM   574  C CA  . VAL A 1 76  ? 20.601  20.127  36.453 1.00 22.67 ? 96  VAL A CA  1 
ATOM   575  C C   . VAL A 1 76  ? 21.578  20.571  37.532 1.00 25.21 ? 96  VAL A C   1 
ATOM   576  O O   . VAL A 1 76  ? 21.971  19.780  38.398 1.00 29.35 ? 96  VAL A O   1 
ATOM   577  C CB  . VAL A 1 76  ? 19.187  19.927  37.025 1.00 27.65 ? 96  VAL A CB  1 
ATOM   578  C CG1 . VAL A 1 76  ? 18.738  21.165  37.803 1.00 28.12 ? 96  VAL A CG1 1 
ATOM   579  C CG2 . VAL A 1 76  ? 18.198  19.643  35.891 1.00 24.38 ? 96  VAL A CG2 1 
ATOM   580  N N   . LYS A 1 77  ? 21.971  21.843  37.471 1.00 27.74 ? 97  LYS A N   1 
ATOM   581  C CA  . LYS A 1 77  ? 22.991  22.403  38.349 1.00 33.32 ? 97  LYS A CA  1 
ATOM   582  C C   . LYS A 1 77  ? 22.441  23.471  39.283 1.00 32.40 ? 97  LYS A C   1 
ATOM   583  O O   . LYS A 1 77  ? 23.224  24.234  39.862 1.00 35.59 ? 97  LYS A O   1 
ATOM   584  C CB  . LYS A 1 77  ? 24.140  22.984  37.520 1.00 30.62 ? 97  LYS A CB  1 
ATOM   585  C CG  . LYS A 1 77  ? 24.655  22.043  36.445 1.00 34.82 ? 97  LYS A CG  1 
ATOM   586  C CD  . LYS A 1 77  ? 25.600  21.038  37.068 1.00 36.59 ? 97  LYS A CD  1 
ATOM   587  C CE  . LYS A 1 77  ? 25.963  19.925  36.104 1.00 45.17 ? 97  LYS A CE  1 
ATOM   588  N NZ  . LYS A 1 77  ? 26.782  18.886  36.787 1.00 51.02 ? 97  LYS A NZ  1 
ATOM   589  N N   . VAL A 1 78  ? 21.122  23.555  39.438 1.00 26.41 ? 98  VAL A N   1 
ATOM   590  C CA  . VAL A 1 78  ? 20.491  24.521  40.326 1.00 26.53 ? 98  VAL A CA  1 
ATOM   591  C C   . VAL A 1 78  ? 19.525  23.767  41.229 1.00 26.20 ? 98  VAL A C   1 
ATOM   592  O O   . VAL A 1 78  ? 19.250  22.584  41.031 1.00 26.31 ? 98  VAL A O   1 
ATOM   593  C CB  . VAL A 1 78  ? 19.755  25.633  39.552 1.00 24.67 ? 98  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 78  ? 20.751  26.537  38.849 1.00 27.07 ? 98  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 78  ? 18.781  25.016  38.553 1.00 24.83 ? 98  VAL A CG2 1 
ATOM   596  N N   . SER A 1 79  ? 19.014  24.469  42.241 1.00 27.94 ? 99  SER A N   1 
ATOM   597  C CA  . SER A 1 79  ? 18.040  23.858  43.132 1.00 26.65 ? 99  SER A CA  1 
ATOM   598  C C   . SER A 1 79  ? 16.741  23.557  42.388 1.00 28.85 ? 99  SER A C   1 
ATOM   599  O O   . SER A 1 79  ? 16.377  24.227  41.417 1.00 25.50 ? 99  SER A O   1 
ATOM   600  C CB  . SER A 1 79  ? 17.770  24.764  44.341 1.00 31.15 ? 99  SER A CB  1 
ATOM   601  O OG  . SER A 1 79  ? 16.907  25.836  44.012 1.00 35.29 ? 99  SER A OG  1 
ATOM   602  N N   . LEU A 1 80  ? 16.058  22.510  42.837 1.00 25.96 ? 100 LEU A N   1 
ATOM   603  C CA  . LEU A 1 80  ? 14.743  22.142  42.333 1.00 27.89 ? 100 LEU A CA  1 
ATOM   604  C C   . LEU A 1 80  ? 13.824  21.880  43.513 1.00 24.41 ? 100 LEU A C   1 
ATOM   605  O O   . LEU A 1 80  ? 14.198  21.149  44.435 1.00 28.67 ? 100 LEU A O   1 
ATOM   606  C CB  . LEU A 1 80  ? 14.804  20.882  41.456 1.00 27.03 ? 100 LEU A CB  1 
ATOM   607  C CG  . LEU A 1 80  ? 15.568  20.912  40.132 1.00 25.68 ? 100 LEU A CG  1 
ATOM   608  C CD1 . LEU A 1 80  ? 15.625  19.498  39.555 1.00 24.07 ? 100 LEU A CD1 1 
ATOM   609  C CD2 . LEU A 1 80  ? 14.914  21.861  39.138 1.00 23.75 ? 100 LEU A CD2 1 
ATOM   610  N N   . THR A 1 81  ? 12.630  22.467  43.489 1.00 24.42 ? 101 THR A N   1 
ATOM   611  C CA  . THR A 1 81  ? 11.585  21.941  44.351 1.00 27.49 ? 101 THR A CA  1 
ATOM   612  C C   . THR A 1 81  ? 11.241  20.527  43.896 1.00 28.68 ? 101 THR A C   1 
ATOM   613  O O   . THR A 1 81  ? 11.570  20.114  42.780 1.00 26.36 ? 101 THR A O   1 
ATOM   614  C CB  . THR A 1 81  ? 10.331  22.813  44.306 1.00 24.65 ? 101 THR A CB  1 
ATOM   615  O OG1 . THR A 1 81  ? 9.730   22.715  43.006 1.00 25.57 ? 101 THR A OG1 1 
ATOM   616  C CG2 . THR A 1 81  ? 10.663  24.278  44.584 1.00 24.53 ? 101 THR A CG2 1 
ATOM   617  N N   . GLN A 1 82  ? 10.575  19.769  44.773 1.00 28.22 ? 102 GLN A N   1 
ATOM   618  C CA  . GLN A 1 82  ? 10.130  18.440  44.368 1.00 25.66 ? 102 GLN A CA  1 
ATOM   619  C C   . GLN A 1 82  ? 9.158   18.524  43.196 1.00 26.82 ? 102 GLN A C   1 
ATOM   620  O O   . GLN A 1 82  ? 9.173   17.666  42.305 1.00 26.20 ? 102 GLN A O   1 
ATOM   621  C CB  . GLN A 1 82  ? 9.502   17.696  45.550 1.00 26.51 ? 102 GLN A CB  1 
ATOM   622  C CG  . GLN A 1 82  ? 9.127   16.248  45.219 1.00 29.74 ? 102 GLN A CG  1 
ATOM   623  C CD  . GLN A 1 82  ? 10.338  15.395  44.901 1.00 28.26 ? 102 GLN A CD  1 
ATOM   624  O OE1 . GLN A 1 82  ? 11.293  15.343  45.674 1.00 33.28 ? 102 GLN A OE1 1 
ATOM   625  N NE2 . GLN A 1 82  ? 10.307  14.720  43.754 1.00 27.69 ? 102 GLN A NE2 1 
ATOM   626  N N   . ASN A 1 83  ? 8.314   19.560  43.169 1.00 26.02 ? 103 ASN A N   1 
ATOM   627  C CA  . ASN A 1 83  ? 7.400   19.738  42.042 1.00 25.20 ? 103 ASN A CA  1 
ATOM   628  C C   . ASN A 1 83  ? 8.169   19.916  40.740 1.00 26.63 ? 103 ASN A C   1 
ATOM   629  O O   . ASN A 1 83  ? 7.800   19.344  39.705 1.00 24.81 ? 103 ASN A O   1 
ATOM   630  C CB  . ASN A 1 83  ? 6.491   20.945  42.284 1.00 25.38 ? 103 ASN A CB  1 
ATOM   631  C CG  . ASN A 1 83  ? 5.408   20.666  43.310 1.00 26.28 ? 103 ASN A CG  1 
ATOM   632  O OD1 . ASN A 1 83  ? 5.142   19.516  43.654 1.00 31.70 ? 103 ASN A OD1 1 
ATOM   633  N ND2 . ASN A 1 83  ? 4.766   21.725  43.791 1.00 30.65 ? 103 ASN A ND2 1 
ATOM   634  N N   . GLN A 1 84  ? 9.241   20.711  40.772 1.00 25.66 ? 104 GLN A N   1 
ATOM   635  C CA  . GLN A 1 84  ? 10.031  20.952  39.567 1.00 21.66 ? 104 GLN A CA  1 
ATOM   636  C C   . GLN A 1 84  ? 10.744  19.683  39.119 1.00 26.84 ? 104 GLN A C   1 
ATOM   637  O O   . GLN A 1 84  ? 10.796  19.379  37.915 1.00 22.50 ? 104 GLN A O   1 
ATOM   638  C CB  . GLN A 1 84  ? 11.028  22.084  39.825 1.00 25.01 ? 104 GLN A CB  1 
ATOM   639  C CG  . GLN A 1 84  ? 10.345  23.431  39.925 1.00 24.53 ? 104 GLN A CG  1 
ATOM   640  C CD  . GLN A 1 84  ? 11.254  24.554  40.388 1.00 23.59 ? 104 GLN A CD  1 
ATOM   641  O OE1 . GLN A 1 84  ? 12.224  24.336  41.116 1.00 24.55 ? 104 GLN A OE1 1 
ATOM   642  N NE2 . GLN A 1 84  ? 10.938  25.765  39.959 1.00 23.26 ? 104 GLN A NE2 1 
ATOM   643  N N   . PHE A 1 85  ? 11.280  18.919  40.073 1.00 25.02 ? 105 PHE A N   1 
ATOM   644  C CA  . PHE A 1 85  ? 11.897  17.642  39.737 1.00 24.40 ? 105 PHE A CA  1 
ATOM   645  C C   . PHE A 1 85  ? 10.885  16.704  39.093 1.00 24.81 ? 105 PHE A C   1 
ATOM   646  O O   . PHE A 1 85  ? 11.190  16.049  38.092 1.00 24.10 ? 105 PHE A O   1 
ATOM   647  C CB  . PHE A 1 85  ? 12.515  16.995  40.983 1.00 24.04 ? 105 PHE A CB  1 
ATOM   648  C CG  . PHE A 1 85  ? 13.254  15.715  40.685 1.00 24.43 ? 105 PHE A CG  1 
ATOM   649  C CD1 . PHE A 1 85  ? 12.586  14.495  40.677 1.00 25.37 ? 105 PHE A CD1 1 
ATOM   650  C CD2 . PHE A 1 85  ? 14.602  15.736  40.362 1.00 26.30 ? 105 PHE A CD2 1 
ATOM   651  C CE1 . PHE A 1 85  ? 13.253  13.326  40.375 1.00 25.20 ? 105 PHE A CE1 1 
ATOM   652  C CE2 . PHE A 1 85  ? 15.279  14.559  40.063 1.00 26.41 ? 105 PHE A CE2 1 
ATOM   653  C CZ  . PHE A 1 85  ? 14.600  13.354  40.066 1.00 26.62 ? 105 PHE A CZ  1 
ATOM   654  N N   . ASP A 1 86  ? 9.674   16.626  39.660 1.00 26.01 ? 106 ASP A N   1 
ATOM   655  C CA  . ASP A 1 86  ? 8.636   15.745  39.123 1.00 27.81 ? 106 ASP A CA  1 
ATOM   656  C C   . ASP A 1 86  ? 8.233   16.161  37.713 1.00 24.89 ? 106 ASP A C   1 
ATOM   657  O O   . ASP A 1 86  ? 8.019   15.310  36.837 1.00 24.52 ? 106 ASP A O   1 
ATOM   658  C CB  . ASP A 1 86  ? 7.415   15.758  40.045 1.00 26.09 ? 106 ASP A CB  1 
ATOM   659  C CG  . ASP A 1 86  ? 7.622   14.946  41.319 1.00 29.28 ? 106 ASP A CG  1 
ATOM   660  O OD1 . ASP A 1 86  ? 8.650   14.254  41.437 1.00 27.05 ? 106 ASP A OD1 1 
ATOM   661  O OD2 . ASP A 1 86  ? 6.754   15.034  42.210 1.00 34.54 ? 106 ASP A OD2 1 
ATOM   662  N N   . ALA A 1 87  ? 8.106   17.468  37.480 1.00 23.47 ? 107 ALA A N   1 
ATOM   663  C CA  . ALA A 1 87  ? 7.804   17.950  36.137 1.00 22.40 ? 107 ALA A CA  1 
ATOM   664  C C   . ALA A 1 87  ? 8.894   17.539  35.154 1.00 23.75 ? 107 ALA A C   1 
ATOM   665  O O   . ALA A 1 87  ? 8.607   17.092  34.030 1.00 22.23 ? 107 ALA A O   1 
ATOM   666  C CB  . ALA A 1 87  ? 7.633   19.470  36.163 1.00 20.78 ? 107 ALA A CB  1 
ATOM   667  N N   . LEU A 1 88  ? 10.160  17.682  35.560 1.00 22.95 ? 108 LEU A N   1 
ATOM   668  C CA  . LEU A 1 88  ? 11.255  17.289  34.680 1.00 19.84 ? 108 LEU A CA  1 
ATOM   669  C C   . LEU A 1 88  ? 11.294  15.780  34.488 1.00 23.25 ? 108 LEU A C   1 
ATOM   670  O O   . LEU A 1 88  ? 11.673  15.299  33.417 1.00 22.36 ? 108 LEU A O   1 
ATOM   671  C CB  . LEU A 1 88  ? 12.582  17.793  35.234 1.00 19.98 ? 108 LEU A CB  1 
ATOM   672  C CG  . LEU A 1 88  ? 12.770  19.313  35.150 1.00 19.81 ? 108 LEU A CG  1 
ATOM   673  C CD1 . LEU A 1 88  ? 13.922  19.744  36.031 1.00 23.29 ? 108 LEU A CD1 1 
ATOM   674  C CD2 . LEU A 1 88  ? 13.020  19.702  33.714 1.00 22.97 ? 108 LEU A CD2 1 
ATOM   675  N N   . ALA A 1 89  ? 10.888  15.020  35.503 1.00 22.25 ? 109 ALA A N   1 
ATOM   676  C CA  . ALA A 1 89  ? 10.852  13.570  35.373 1.00 19.97 ? 109 ALA A CA  1 
ATOM   677  C C   . ALA A 1 89  ? 9.847   13.151  34.313 1.00 23.24 ? 109 ALA A C   1 
ATOM   678  O O   . ALA A 1 89  ? 10.149  12.315  33.453 1.00 23.66 ? 109 ALA A O   1 
ATOM   679  C CB  . ALA A 1 89  ? 10.530  12.933  36.730 1.00 21.03 ? 109 ALA A CB  1 
ATOM   680  N N   . SER A 1 90  ? 8.652   13.746  34.340 1.00 21.98 ? 110 SER A N   1 
ATOM   681  C CA  . SER A 1 90  ? 7.655   13.465  33.306 1.00 23.07 ? 110 SER A CA  1 
ATOM   682  C C   . SER A 1 90  ? 8.168   13.865  31.921 1.00 27.46 ? 110 SER A C   1 
ATOM   683  O O   . SER A 1 90  ? 8.110   13.083  30.955 1.00 25.38 ? 110 SER A O   1 
ATOM   684  C CB  . SER A 1 90  ? 6.354   14.195  33.646 1.00 25.32 ? 110 SER A CB  1 
ATOM   685  O OG  . SER A 1 90  ? 5.413   14.130  32.587 1.00 28.31 ? 110 SER A OG  1 
ATOM   686  N N   . PHE A 1 91  ? 8.691   15.086  31.816 1.00 22.20 ? 111 PHE A N   1 
ATOM   687  C CA  . PHE A 1 91  ? 9.214   15.592  30.547 1.00 22.01 ? 111 PHE A CA  1 
ATOM   688  C C   . PHE A 1 91  ? 10.290  14.672  29.973 1.00 22.86 ? 111 PHE A C   1 
ATOM   689  O O   . PHE A 1 91  ? 10.262  14.327  28.784 1.00 22.97 ? 111 PHE A O   1 
ATOM   690  C CB  . PHE A 1 91  ? 9.757   17.003  30.789 1.00 19.10 ? 111 PHE A CB  1 
ATOM   691  C CG  . PHE A 1 91  ? 10.409  17.642  29.600 1.00 21.45 ? 111 PHE A CG  1 
ATOM   692  C CD1 . PHE A 1 91  ? 11.760  17.463  29.351 1.00 21.26 ? 111 PHE A CD1 1 
ATOM   693  C CD2 . PHE A 1 91  ? 9.681   18.468  28.764 1.00 22.15 ? 111 PHE A CD2 1 
ATOM   694  C CE1 . PHE A 1 91  ? 12.367  18.058  28.263 1.00 24.90 ? 111 PHE A CE1 1 
ATOM   695  C CE2 . PHE A 1 91  ? 10.285  19.083  27.685 1.00 24.90 ? 111 PHE A CE2 1 
ATOM   696  C CZ  . PHE A 1 91  ? 11.627  18.877  27.431 1.00 23.78 ? 111 PHE A CZ  1 
ATOM   697  N N   . THR A 1 92  ? 11.243  14.256  30.810 1.00 22.28 ? 112 THR A N   1 
ATOM   698  C CA  . THR A 1 92  ? 12.401  13.495  30.363 1.00 22.31 ? 112 THR A CA  1 
ATOM   699  C C   . THR A 1 92  ? 12.048  12.036  30.106 1.00 24.07 ? 112 THR A C   1 
ATOM   700  O O   . THR A 1 92  ? 12.589  11.425  29.172 1.00 24.64 ? 112 THR A O   1 
ATOM   701  C CB  . THR A 1 92  ? 13.519  13.594  31.411 1.00 25.04 ? 112 THR A CB  1 
ATOM   702  O OG1 . THR A 1 92  ? 13.818  14.979  31.667 1.00 23.30 ? 112 THR A OG1 1 
ATOM   703  C CG2 . THR A 1 92  ? 14.783  12.911  30.918 1.00 29.09 ? 112 THR A CG2 1 
ATOM   704  N N   . TYR A 1 93  ? 11.148  11.470  30.915 1.00 22.68 ? 113 TYR A N   1 
ATOM   705  C CA  . TYR A 1 93  ? 10.580  10.159  30.610 1.00 24.20 ? 113 TYR A CA  1 
ATOM   706  C C   . TYR A 1 93  ? 10.006  10.137  29.207 1.00 26.07 ? 113 TYR A C   1 
ATOM   707  O O   . TYR A 1 93  ? 10.198  9.170   28.455 1.00 24.60 ? 113 TYR A O   1 
ATOM   708  C CB  . TYR A 1 93  ? 9.479   9.827   31.619 1.00 24.34 ? 113 TYR A CB  1 
ATOM   709  C CG  . TYR A 1 93  ? 8.763   8.522   31.349 1.00 25.05 ? 113 TYR A CG  1 
ATOM   710  C CD1 . TYR A 1 93  ? 7.664   8.473   30.491 1.00 27.50 ? 113 TYR A CD1 1 
ATOM   711  C CD2 . TYR A 1 93  ? 9.157   7.353   31.978 1.00 26.36 ? 113 TYR A CD2 1 
ATOM   712  C CE1 . TYR A 1 93  ? 7.007   7.286   30.238 1.00 29.52 ? 113 TYR A CE1 1 
ATOM   713  C CE2 . TYR A 1 93  ? 8.498   6.155   31.731 1.00 28.48 ? 113 TYR A CE2 1 
ATOM   714  C CZ  . TYR A 1 93  ? 7.425   6.135   30.865 1.00 33.88 ? 113 TYR A CZ  1 
ATOM   715  O OH  . TYR A 1 93  ? 6.764   4.955   30.615 1.00 33.56 ? 113 TYR A OH  1 
ATOM   716  N N   . ASN A 1 94  ? 9.285   11.200  28.842 1.00 23.18 ? 114 ASN A N   1 
ATOM   717  C CA  . ASN A 1 94  ? 8.622   11.250  27.543 1.00 23.64 ? 114 ASN A CA  1 
ATOM   718  C C   . ASN A 1 94  ? 9.597   11.543  26.404 1.00 27.78 ? 114 ASN A C   1 
ATOM   719  O O   . ASN A 1 94  ? 9.497   10.939  25.326 1.00 26.41 ? 114 ASN A O   1 
ATOM   720  C CB  . ASN A 1 94  ? 7.510   12.300  27.606 1.00 24.76 ? 114 ASN A CB  1 
ATOM   721  C CG  . ASN A 1 94  ? 6.672   12.351  26.361 1.00 30.59 ? 114 ASN A CG  1 
ATOM   722  O OD1 . ASN A 1 94  ? 6.258   13.426  25.938 1.00 29.02 ? 114 ASN A OD1 1 
ATOM   723  N ND2 . ASN A 1 94  ? 6.424   11.193  25.755 1.00 38.34 ? 114 ASN A ND2 1 
ATOM   724  N N   . LEU A 1 95  ? 10.558  12.443  26.622 1.00 23.76 ? 115 LEU A N   1 
ATOM   725  C CA  . LEU A 1 95  ? 11.372  12.966  25.531 1.00 23.77 ? 115 LEU A CA  1 
ATOM   726  C C   . LEU A 1 95  ? 12.809  12.459  25.512 1.00 23.67 ? 115 LEU A C   1 
ATOM   727  O O   . LEU A 1 95  ? 13.464  12.573  24.468 1.00 26.82 ? 115 LEU A O   1 
ATOM   728  C CB  . LEU A 1 95  ? 11.378  14.499  25.580 1.00 24.42 ? 115 LEU A CB  1 
ATOM   729  C CG  . LEU A 1 95  ? 10.027  15.093  25.164 1.00 27.56 ? 115 LEU A CG  1 
ATOM   730  C CD1 . LEU A 1 95  ? 9.938   16.528  25.565 1.00 31.75 ? 115 LEU A CD1 1 
ATOM   731  C CD2 . LEU A 1 95  ? 9.818   14.956  23.662 1.00 30.27 ? 115 LEU A CD2 1 
ATOM   732  N N   . GLY A 1 96  ? 13.316  11.913  26.615 1.00 24.65 ? 116 GLY A N   1 
ATOM   733  C CA  . GLY A 1 96  ? 14.633  11.311  26.632 1.00 28.11 ? 116 GLY A CA  1 
ATOM   734  C C   . GLY A 1 96  ? 15.731  12.255  27.098 1.00 26.11 ? 116 GLY A C   1 
ATOM   735  O O   . GLY A 1 96  ? 15.598  13.480  27.083 1.00 24.93 ? 116 GLY A O   1 
ATOM   736  N N   . GLU A 1 97  ? 16.856  11.646  27.493 1.00 27.80 ? 117 GLU A N   1 
ATOM   737  C CA  . GLU A 1 97  ? 17.960  12.392  28.092 1.00 28.99 ? 117 GLU A CA  1 
ATOM   738  C C   . GLU A 1 97  ? 18.633  13.322  27.090 1.00 27.95 ? 117 GLU A C   1 
ATOM   739  O O   . GLU A 1 97  ? 19.006  14.447  27.442 1.00 26.89 ? 117 GLU A O   1 
ATOM   740  C CB  . GLU A 1 97  ? 18.991  11.428  28.686 1.00 31.01 ? 117 GLU A CB  1 
ATOM   741  C CG  . GLU A 1 97  ? 20.267  12.121  29.160 1.00 36.76 ? 117 GLU A CG  1 
ATOM   742  C CD  . GLU A 1 97  ? 21.279  11.161  29.756 1.00 47.99 ? 117 GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 97  ? 20.991  9.946   29.806 1.00 52.08 ? 117 GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 97  ? 22.362  11.625  30.176 1.00 47.12 ? 117 GLU A OE2 1 
ATOM   745  N N   . THR A 1 98  ? 18.814  12.875  25.843 1.00 28.18 ? 118 THR A N   1 
ATOM   746  C CA  . THR A 1 98  ? 19.488  13.720  24.860 1.00 26.49 ? 118 THR A CA  1 
ATOM   747  C C   . THR A 1 98  ? 18.699  14.995  24.591 1.00 28.07 ? 118 THR A C   1 
ATOM   748  O O   . THR A 1 98  ? 19.279  16.089  24.515 1.00 27.12 ? 118 THR A O   1 
ATOM   749  C CB  . THR A 1 98  ? 19.713  12.950  23.557 1.00 29.96 ? 118 THR A CB  1 
ATOM   750  O OG1 . THR A 1 98  ? 20.546  11.815  23.818 1.00 36.93 ? 118 THR A OG1 1 
ATOM   751  C CG2 . THR A 1 98  ? 20.389  13.844  22.513 1.00 36.07 ? 118 THR A CG2 1 
ATOM   752  N N   . ASN A 1 99  ? 17.375  14.879  24.447 1.00 26.93 ? 119 ASN A N   1 
ATOM   753  C CA  . ASN A 1 99  ? 16.560  16.070  24.231 1.00 21.82 ? 119 ASN A CA  1 
ATOM   754  C C   . ASN A 1 99  ? 16.648  17.024  25.414 1.00 21.58 ? 119 ASN A C   1 
ATOM   755  O O   . ASN A 1 99  ? 16.729  18.244  25.224 1.00 23.07 ? 119 ASN A O   1 
ATOM   756  C CB  . ASN A 1 99  ? 15.110  15.686  23.959 1.00 23.29 ? 119 ASN A CB  1 
ATOM   757  C CG  . ASN A 1 99  ? 14.880  15.282  22.513 1.00 24.26 ? 119 ASN A CG  1 
ATOM   758  O OD1 . ASN A 1 99  ? 15.489  15.845  21.596 1.00 26.76 ? 119 ASN A OD1 1 
ATOM   759  N ND2 . ASN A 1 99  ? 13.998  14.311  22.301 1.00 28.81 ? 119 ASN A ND2 1 
ATOM   760  N N   . LEU A 1 100 ? 16.643  16.495  26.640 1.00 23.05 ? 120 LEU A N   1 
ATOM   761  C CA  . LEU A 1 100 ? 16.785  17.382  27.794 1.00 22.79 ? 120 LEU A CA  1 
ATOM   762  C C   . LEU A 1 100 ? 18.150  18.059  27.783 1.00 23.43 ? 120 LEU A C   1 
ATOM   763  O O   . LEU A 1 100 ? 18.258  19.277  27.984 1.00 21.06 ? 120 LEU A O   1 
ATOM   764  C CB  . LEU A 1 100 ? 16.570  16.609  29.098 1.00 21.36 ? 120 LEU A CB  1 
ATOM   765  C CG  . LEU A 1 100 ? 16.862  17.409  30.376 1.00 22.45 ? 120 LEU A CG  1 
ATOM   766  C CD1 . LEU A 1 100 ? 15.801  18.488  30.533 1.00 25.21 ? 120 LEU A CD1 1 
ATOM   767  C CD2 . LEU A 1 100 ? 16.911  16.496  31.595 1.00 27.22 ? 120 LEU A CD2 1 
ATOM   768  N N   . ALA A 1 101 ? 19.205  17.285  27.519 1.00 24.19 ? 121 ALA A N   1 
ATOM   769  C CA  . ALA A 1 101 ? 20.568  17.799  27.598 1.00 25.05 ? 121 ALA A CA  1 
ATOM   770  C C   . ALA A 1 101 ? 20.801  18.936  26.612 1.00 26.96 ? 121 ALA A C   1 
ATOM   771  O O   . ALA A 1 101 ? 21.530  19.884  26.914 1.00 28.47 ? 121 ALA A O   1 
ATOM   772  C CB  . ALA A 1 101 ? 21.567  16.669  27.351 1.00 27.90 ? 121 ALA A CB  1 
ATOM   773  N N   . ASN A 1 102 ? 20.202  18.858  25.428 1.00 22.58 ? 122 ASN A N   1 
ATOM   774  C CA  . ASN A 1 102 ? 20.400  19.871  24.401 1.00 24.15 ? 122 ASN A CA  1 
ATOM   775  C C   . ASN A 1 102 ? 19.361  20.985  24.441 1.00 23.13 ? 122 ASN A C   1 
ATOM   776  O O   . ASN A 1 102 ? 19.402  21.877  23.588 1.00 24.73 ? 122 ASN A O   1 
ATOM   777  C CB  . ASN A 1 102 ? 20.399  19.221  23.014 1.00 25.95 ? 122 ASN A CB  1 
ATOM   778  C CG  . ASN A 1 102 ? 21.551  18.258  22.820 1.00 34.28 ? 122 ASN A CG  1 
ATOM   779  O OD1 . ASN A 1 102 ? 22.597  18.391  23.451 1.00 38.48 ? 122 ASN A OD1 1 
ATOM   780  N ND2 . ASN A 1 102 ? 21.369  17.290  21.935 1.00 38.76 ? 122 ASN A ND2 1 
ATOM   781  N N   . SER A 1 103 ? 18.458  20.977  25.417 1.00 24.13 ? 123 SER A N   1 
ATOM   782  C CA  . SER A 1 103 ? 17.298  21.853  25.361 1.00 21.95 ? 123 SER A CA  1 
ATOM   783  C C   . SER A 1 103 ? 17.626  23.266  25.837 1.00 23.13 ? 123 SER A C   1 
ATOM   784  O O   . SER A 1 103 ? 18.462  23.474  26.721 1.00 23.54 ? 123 SER A O   1 
ATOM   785  C CB  . SER A 1 103 ? 16.155  21.284  26.203 1.00 20.94 ? 123 SER A CB  1 
ATOM   786  O OG  . SER A 1 103 ? 16.495  21.229  27.584 1.00 22.22 ? 123 SER A OG  1 
ATOM   787  N N   . THR A 1 104 ? 16.954  24.244  25.226 1.00 22.32 ? 124 THR A N   1 
ATOM   788  C CA  . THR A 1 104 ? 16.956  25.595  25.780 1.00 21.88 ? 124 THR A CA  1 
ATOM   789  C C   . THR A 1 104 ? 16.363  25.598  27.183 1.00 23.09 ? 124 THR A C   1 
ATOM   790  O O   . THR A 1 104 ? 16.751  26.420  28.025 1.00 21.89 ? 124 THR A O   1 
ATOM   791  C CB  . THR A 1 104 ? 16.174  26.527  24.850 1.00 24.22 ? 124 THR A CB  1 
ATOM   792  O OG1 . THR A 1 104 ? 16.801  26.539  23.559 1.00 26.83 ? 124 THR A OG1 1 
ATOM   793  C CG2 . THR A 1 104 ? 16.114  27.957  25.393 1.00 22.01 ? 124 THR A CG2 1 
ATOM   794  N N   . LEU A 1 105 ? 15.436  24.675  27.455 1.00 22.77 ? 125 LEU A N   1 
ATOM   795  C CA  . LEU A 1 105 ? 14.885  24.508  28.796 1.00 20.58 ? 125 LEU A CA  1 
ATOM   796  C C   . LEU A 1 105 ? 15.998  24.377  29.831 1.00 22.20 ? 125 LEU A C   1 
ATOM   797  O O   . LEU A 1 105 ? 16.066  25.148  30.802 1.00 20.57 ? 125 LEU A O   1 
ATOM   798  C CB  . LEU A 1 105 ? 13.963  23.275  28.820 1.00 22.11 ? 125 LEU A CB  1 
ATOM   799  C CG  . LEU A 1 105 ? 13.000  23.068  30.005 1.00 21.93 ? 125 LEU A CG  1 
ATOM   800  C CD1 . LEU A 1 105 ? 11.919  22.062  29.626 1.00 27.04 ? 125 LEU A CD1 1 
ATOM   801  C CD2 . LEU A 1 105 ? 13.720  22.582  31.248 1.00 24.00 ? 125 LEU A CD2 1 
ATOM   802  N N   . LEU A 1 106 ? 16.880  23.395  29.635 1.00 20.95 ? 126 LEU A N   1 
ATOM   803  C CA  . LEU A 1 106 ? 17.958  23.148  30.585 1.00 20.04 ? 126 LEU A CA  1 
ATOM   804  C C   . LEU A 1 106 ? 18.953  24.300  30.616 1.00 22.86 ? 126 LEU A C   1 
ATOM   805  O O   . LEU A 1 106 ? 19.472  24.643  31.682 1.00 23.04 ? 126 LEU A O   1 
ATOM   806  C CB  . LEU A 1 106 ? 18.668  21.836  30.246 1.00 20.84 ? 126 LEU A CB  1 
ATOM   807  C CG  . LEU A 1 106 ? 19.837  21.455  31.155 1.00 21.68 ? 126 LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 106 ? 19.345  21.158  32.569 1.00 23.77 ? 126 LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 106 ? 20.586  20.254  30.582 1.00 23.37 ? 126 LEU A CD2 1 
ATOM   810  N N   . LYS A 1 107 ? 19.243  24.902  29.463 1.00 21.52 ? 127 LYS A N   1 
ATOM   811  C CA  . LYS A 1 107 ? 20.167  26.036  29.433 1.00 22.24 ? 127 LYS A CA  1 
ATOM   812  C C   . LYS A 1 107 ? 19.667  27.178  30.318 1.00 22.71 ? 127 LYS A C   1 
ATOM   813  O O   . LYS A 1 107 ? 20.404  27.702  31.176 1.00 26.43 ? 127 LYS A O   1 
ATOM   814  C CB  . LYS A 1 107 ? 20.355  26.498  27.986 1.00 24.37 ? 127 LYS A CB  1 
ATOM   815  C CG  . LYS A 1 107 ? 21.277  27.688  27.811 1.00 29.03 ? 127 LYS A CG  1 
ATOM   816  C CD  . LYS A 1 107 ? 21.272  28.160  26.360 1.00 28.91 ? 127 LYS A CD  1 
ATOM   817  C CE  . LYS A 1 107 ? 22.313  29.244  26.134 1.00 38.78 ? 127 LYS A CE  1 
ATOM   818  N NZ  . LYS A 1 107 ? 22.399  29.641  24.698 1.00 34.18 ? 127 LYS A NZ  1 
ATOM   819  N N   . LYS A 1 108 ? 18.396  27.554  30.148 1.00 22.12 ? 128 LYS A N   1 
ATOM   820  C CA  . LYS A 1 108 ? 17.847  28.626  30.976 1.00 22.80 ? 128 LYS A CA  1 
ATOM   821  C C   . LYS A 1 108 ? 17.770  28.208  32.435 1.00 25.42 ? 128 LYS A C   1 
ATOM   822  O O   . LYS A 1 108 ? 18.085  29.002  33.331 1.00 22.99 ? 128 LYS A O   1 
ATOM   823  C CB  . LYS A 1 108 ? 16.467  29.035  30.473 1.00 20.38 ? 128 LYS A CB  1 
ATOM   824  C CG  . LYS A 1 108 ? 16.501  29.674  29.095 1.00 23.36 ? 128 LYS A CG  1 
ATOM   825  C CD  . LYS A 1 108 ? 15.178  30.314  28.742 1.00 23.37 ? 128 LYS A CD  1 
ATOM   826  C CE  . LYS A 1 108 ? 15.280  31.056  27.413 1.00 30.52 ? 128 LYS A CE  1 
ATOM   827  N NZ  . LYS A 1 108 ? 14.111  31.943  27.174 1.00 37.62 ? 128 LYS A NZ  1 
ATOM   828  N N   . LEU A 1 109 ? 17.358  26.967  32.696 1.00 21.50 ? 129 LEU A N   1 
ATOM   829  C CA  . LEU A 1 109 ? 17.249  26.510  34.076 1.00 21.47 ? 129 LEU A CA  1 
ATOM   830  C C   . LEU A 1 109 ? 18.592  26.612  34.791 1.00 24.40 ? 129 LEU A C   1 
ATOM   831  O O   . LEU A 1 109 ? 18.674  27.122  35.919 1.00 23.37 ? 129 LEU A O   1 
ATOM   832  C CB  . LEU A 1 109 ? 16.716  25.072  34.093 1.00 19.93 ? 129 LEU A CB  1 
ATOM   833  C CG  . LEU A 1 109 ? 16.621  24.362  35.435 1.00 21.21 ? 129 LEU A CG  1 
ATOM   834  C CD1 . LEU A 1 109 ? 15.738  25.145  36.395 1.00 23.94 ? 129 LEU A CD1 1 
ATOM   835  C CD2 . LEU A 1 109 ? 16.079  22.931  35.254 1.00 22.47 ? 129 LEU A CD2 1 
ATOM   836  N N   . ASN A 1 110 ? 19.667  26.177  34.129 1.00 22.07 ? 130 ASN A N   1 
ATOM   837  C CA  . ASN A 1 110 ? 20.982  26.159  34.747 1.00 21.99 ? 130 ASN A CA  1 
ATOM   838  C C   . ASN A 1 110 ? 21.598  27.544  34.842 1.00 24.39 ? 130 ASN A C   1 
ATOM   839  O O   . ASN A 1 110 ? 22.591  27.707  35.562 1.00 25.70 ? 130 ASN A O   1 
ATOM   840  C CB  . ASN A 1 110 ? 21.921  25.222  33.984 1.00 24.62 ? 130 ASN A CB  1 
ATOM   841  C CG  . ASN A 1 110 ? 21.724  23.774  34.373 1.00 23.59 ? 130 ASN A CG  1 
ATOM   842  O OD1 . ASN A 1 110 ? 21.135  23.477  35.408 1.00 25.13 ? 130 ASN A OD1 1 
ATOM   843  N ND2 . ASN A 1 110 ? 22.218  22.862  33.542 1.00 24.65 ? 130 ASN A ND2 1 
ATOM   844  N N   . LYS A 1 111 ? 21.048  28.529  34.130 1.00 22.20 ? 131 LYS A N   1 
ATOM   845  C CA  . LYS A 1 111 ? 21.405  29.914  34.427 1.00 22.60 ? 131 LYS A CA  1 
ATOM   846  C C   . LYS A 1 111 ? 20.692  30.456  35.659 1.00 27.57 ? 131 LYS A C   1 
ATOM   847  O O   . LYS A 1 111 ? 21.021  31.565  36.100 1.00 29.13 ? 131 LYS A O   1 
ATOM   848  C CB  . LYS A 1 111 ? 21.096  30.819  33.236 1.00 25.07 ? 131 LYS A CB  1 
ATOM   849  C CG  . LYS A 1 111 ? 22.015  30.593  32.053 1.00 30.09 ? 131 LYS A CG  1 
ATOM   850  C CD  . LYS A 1 111 ? 21.644  31.494  30.890 1.00 33.08 ? 131 LYS A CD  1 
ATOM   851  C CE  . LYS A 1 111 ? 22.313  31.032  29.610 1.00 43.13 ? 131 LYS A CE  1 
ATOM   852  N NZ  . LYS A 1 111 ? 23.793  31.155  29.692 1.00 53.35 ? 131 LYS A NZ  1 
ATOM   853  N N   . GLY A 1 112 ? 19.749  29.707  36.232 1.00 25.76 ? 132 GLY A N   1 
ATOM   854  C CA  . GLY A 1 112 ? 18.895  30.220  37.292 1.00 22.17 ? 132 GLY A CA  1 
ATOM   855  C C   . GLY A 1 112 ? 17.623  30.881  36.809 1.00 28.37 ? 132 GLY A C   1 
ATOM   856  O O   . GLY A 1 112 ? 16.932  31.522  37.610 1.00 28.60 ? 132 GLY A O   1 
ATOM   857  N N   . ASP A 1 113 ? 17.288  30.744  35.525 1.00 26.76 ? 133 ASP A N   1 
ATOM   858  C CA  . ASP A 1 113 ? 16.111  31.378  34.929 1.00 22.88 ? 133 ASP A CA  1 
ATOM   859  C C   . ASP A 1 113 ? 14.963  30.369  34.942 1.00 26.63 ? 133 ASP A C   1 
ATOM   860  O O   . ASP A 1 113 ? 14.661  29.699  33.953 1.00 25.27 ? 133 ASP A O   1 
ATOM   861  C CB  . ASP A 1 113 ? 16.442  31.875  33.523 1.00 24.26 ? 133 ASP A CB  1 
ATOM   862  C CG  . ASP A 1 113 ? 15.248  32.481  32.804 1.00 24.73 ? 133 ASP A CG  1 
ATOM   863  O OD1 . ASP A 1 113 ? 14.233  32.811  33.458 1.00 30.06 ? 133 ASP A OD1 1 
ATOM   864  O OD2 . ASP A 1 113 ? 15.334  32.636  31.568 1.00 28.29 ? 133 ASP A OD2 1 
ATOM   865  N N   . TYR A 1 114 ? 14.308  30.267  36.104 1.00 23.77 ? 134 TYR A N   1 
ATOM   866  C CA  . TYR A 1 114 ? 13.252  29.272  36.282 1.00 23.69 ? 134 TYR A CA  1 
ATOM   867  C C   . TYR A 1 114 ? 12.021  29.585  35.436 1.00 26.47 ? 134 TYR A C   1 
ATOM   868  O O   . TYR A 1 114 ? 11.389  28.674  34.893 1.00 25.89 ? 134 TYR A O   1 
ATOM   869  C CB  . TYR A 1 114 ? 12.874  29.166  37.761 1.00 24.20 ? 134 TYR A CB  1 
ATOM   870  C CG  . TYR A 1 114 ? 13.940  28.525  38.610 1.00 23.66 ? 134 TYR A CG  1 
ATOM   871  C CD1 . TYR A 1 114 ? 14.961  29.279  39.177 1.00 27.17 ? 134 TYR A CD1 1 
ATOM   872  C CD2 . TYR A 1 114 ? 13.925  27.155  38.855 1.00 23.64 ? 134 TYR A CD2 1 
ATOM   873  C CE1 . TYR A 1 114 ? 15.938  28.684  39.956 1.00 25.01 ? 134 TYR A CE1 1 
ATOM   874  C CE2 . TYR A 1 114 ? 14.892  26.556  39.633 1.00 23.77 ? 134 TYR A CE2 1 
ATOM   875  C CZ  . TYR A 1 114 ? 15.899  27.322  40.187 1.00 23.64 ? 134 TYR A CZ  1 
ATOM   876  O OH  . TYR A 1 114 ? 16.861  26.719  40.951 1.00 27.48 ? 134 TYR A OH  1 
ATOM   877  N N   . GLN A 1 115 ? 11.658  30.861  35.307 1.00 26.03 ? 135 GLN A N   1 
ATOM   878  C CA  . GLN A 1 115 ? 10.473  31.199  34.522 1.00 25.49 ? 135 GLN A CA  1 
ATOM   879  C C   . GLN A 1 115 ? 10.688  30.903  33.040 1.00 24.50 ? 135 GLN A C   1 
ATOM   880  O O   . GLN A 1 115 ? 9.791   30.372  32.362 1.00 28.71 ? 135 GLN A O   1 
ATOM   881  C CB  . GLN A 1 115 ? 10.106  32.670  34.742 1.00 28.28 ? 135 GLN A CB  1 
ATOM   882  C CG  . GLN A 1 115 ? 8.884   33.115  33.964 1.00 37.30 ? 135 GLN A CG  1 
ATOM   883  C CD  . GLN A 1 115 ? 7.622   32.417  34.427 1.00 41.09 ? 135 GLN A CD  1 
ATOM   884  O OE1 . GLN A 1 115 ? 7.260   32.471  35.602 1.00 45.59 ? 135 GLN A OE1 1 
ATOM   885  N NE2 . GLN A 1 115 ? 6.935   31.763  33.495 1.00 46.79 ? 135 GLN A NE2 1 
ATOM   886  N N   . GLY A 1 116 ? 11.877  31.228  32.525 1.00 24.87 ? 136 GLY A N   1 
ATOM   887  C CA  . GLY A 1 116 ? 12.191  30.890  31.146 1.00 23.95 ? 136 GLY A CA  1 
ATOM   888  C C   . GLY A 1 116 ? 12.152  29.394  30.891 1.00 24.96 ? 136 GLY A C   1 
ATOM   889  O O   . GLY A 1 116 ? 11.613  28.941  29.876 1.00 24.98 ? 136 GLY A O   1 
ATOM   890  N N   . ALA A 1 117 ? 12.712  28.607  31.815 1.00 25.47 ? 137 ALA A N   1 
ATOM   891  C CA  . ALA A 1 117 ? 12.668  27.150  31.673 1.00 20.04 ? 137 ALA A CA  1 
ATOM   892  C C   . ALA A 1 117 ? 11.227  26.638  31.666 1.00 25.76 ? 137 ALA A C   1 
ATOM   893  O O   . ALA A 1 117 ? 10.843  25.779  30.844 1.00 24.08 ? 137 ALA A O   1 
ATOM   894  C CB  . ALA A 1 117 ? 13.468  26.502  32.807 1.00 23.11 ? 137 ALA A CB  1 
ATOM   895  N N   . ALA A 1 118 ? 10.415  27.151  32.594 1.00 22.62 ? 138 ALA A N   1 
ATOM   896  C CA  . ALA A 1 118 ? 9.016   26.753  32.656 1.00 22.68 ? 138 ALA A CA  1 
ATOM   897  C C   . ALA A 1 118 ? 8.333   26.985  31.320 1.00 24.73 ? 138 ALA A C   1 
ATOM   898  O O   . ALA A 1 118 ? 7.590   26.122  30.836 1.00 25.41 ? 138 ALA A O   1 
ATOM   899  C CB  . ALA A 1 118 ? 8.301   27.520  33.769 1.00 24.06 ? 138 ALA A CB  1 
ATOM   900  N N   . ASP A 1 119 ? 8.604   28.132  30.694 1.00 25.15 ? 139 ASP A N   1 
ATOM   901  C CA  . ASP A 1 119 ? 7.989   28.402  29.399 1.00 25.40 ? 139 ASP A CA  1 
ATOM   902  C C   . ASP A 1 119 ? 8.550   27.500  28.298 1.00 25.09 ? 139 ASP A C   1 
ATOM   903  O O   . ASP A 1 119 ? 7.834   27.189  27.338 1.00 26.13 ? 139 ASP A O   1 
ATOM   904  C CB  . ASP A 1 119 ? 8.154   29.879  29.044 1.00 28.66 ? 139 ASP A CB  1 
ATOM   905  C CG  . ASP A 1 119 ? 7.299   30.777  29.917 1.00 37.14 ? 139 ASP A CG  1 
ATOM   906  O OD1 . ASP A 1 119 ? 6.340   30.262  30.529 1.00 35.93 ? 139 ASP A OD1 1 
ATOM   907  O OD2 . ASP A 1 119 ? 7.574   31.995  29.984 1.00 36.27 ? 139 ASP A OD2 1 
ATOM   908  N N   . GLN A 1 120 ? 9.809   27.061  28.420 1.00 22.09 ? 140 GLN A N   1 
ATOM   909  C CA  . GLN A 1 120 ? 10.365  26.144  27.419 1.00 22.65 ? 140 GLN A CA  1 
ATOM   910  C C   . GLN A 1 120 ? 9.707   24.773  27.419 1.00 25.07 ? 140 GLN A C   1 
ATOM   911  O O   . GLN A 1 120 ? 9.800   24.061  26.407 1.00 23.34 ? 140 GLN A O   1 
ATOM   912  C CB  . GLN A 1 120 ? 11.869  25.966  27.612 1.00 23.46 ? 140 GLN A CB  1 
ATOM   913  C CG  . GLN A 1 120 ? 12.665  27.165  27.152 1.00 21.62 ? 140 GLN A CG  1 
ATOM   914  C CD  . GLN A 1 120 ? 12.483  27.423  25.675 1.00 25.57 ? 140 GLN A CD  1 
ATOM   915  O OE1 . GLN A 1 120 ? 12.650  26.523  24.850 1.00 28.31 ? 140 GLN A OE1 1 
ATOM   916  N NE2 . GLN A 1 120 ? 12.116  28.647  25.333 1.00 28.10 ? 140 GLN A NE2 1 
ATOM   917  N N   . PHE A 1 121 ? 9.088   24.356  28.526 1.00 22.49 ? 141 PHE A N   1 
ATOM   918  C CA  . PHE A 1 121 ? 8.329   23.094  28.445 1.00 23.28 ? 141 PHE A CA  1 
ATOM   919  C C   . PHE A 1 121 ? 7.382   23.073  27.242 1.00 24.23 ? 141 PHE A C   1 
ATOM   920  O O   . PHE A 1 121 ? 7.239   22.040  26.571 1.00 22.41 ? 141 PHE A O   1 
ATOM   921  C CB  . PHE A 1 121 ? 7.498   22.838  29.710 1.00 22.38 ? 141 PHE A CB  1 
ATOM   922  C CG  . PHE A 1 121 ? 8.282   22.293  30.872 1.00 20.93 ? 141 PHE A CG  1 
ATOM   923  C CD1 . PHE A 1 121 ? 8.958   23.146  31.725 1.00 24.62 ? 141 PHE A CD1 1 
ATOM   924  C CD2 . PHE A 1 121 ? 8.323   20.928  31.125 1.00 21.15 ? 141 PHE A CD2 1 
ATOM   925  C CE1 . PHE A 1 121 ? 9.669   22.649  32.816 1.00 24.52 ? 141 PHE A CE1 1 
ATOM   926  C CE2 . PHE A 1 121 ? 9.038   20.426  32.203 1.00 23.58 ? 141 PHE A CE2 1 
ATOM   927  C CZ  . PHE A 1 121 ? 9.709   21.291  33.053 1.00 26.65 ? 141 PHE A CZ  1 
ATOM   928  N N   . LEU A 1 122 ? 6.752   24.209  26.932 1.00 25.58 ? 142 LEU A N   1 
ATOM   929  C CA  . LEU A 1 122 ? 5.650   24.253  25.980 1.00 22.43 ? 142 LEU A CA  1 
ATOM   930  C C   . LEU A 1 122 ? 6.085   24.083  24.533 1.00 25.88 ? 142 LEU A C   1 
ATOM   931  O O   . LEU A 1 122 ? 5.229   23.847  23.672 1.00 27.89 ? 142 LEU A O   1 
ATOM   932  C CB  . LEU A 1 122 ? 4.898   25.579  26.125 1.00 23.74 ? 142 LEU A CB  1 
ATOM   933  C CG  . LEU A 1 122 ? 4.309   25.865  27.508 1.00 25.09 ? 142 LEU A CG  1 
ATOM   934  C CD1 . LEU A 1 122 ? 3.654   27.240  27.505 1.00 27.60 ? 142 LEU A CD1 1 
ATOM   935  C CD2 . LEU A 1 122 ? 3.316   24.777  27.882 1.00 28.87 ? 142 LEU A CD2 1 
ATOM   936  N N   . VAL A 1 123 ? 7.378   24.213  24.226 1.00 21.73 ? 143 VAL A N   1 
ATOM   937  C CA  . VAL A 1 123 ? 7.774   24.101  22.822 1.00 23.61 ? 143 VAL A CA  1 
ATOM   938  C C   . VAL A 1 123 ? 7.907   22.656  22.375 1.00 23.33 ? 143 VAL A C   1 
ATOM   939  O O   . VAL A 1 123 ? 8.029   22.397  21.170 1.00 25.02 ? 143 VAL A O   1 
ATOM   940  C CB  . VAL A 1 123 ? 9.091   24.850  22.543 1.00 30.59 ? 143 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 123 ? 9.021   26.274  23.080 1.00 25.36 ? 143 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 123 ? 10.265  24.113  23.134 1.00 32.36 ? 143 VAL A CG2 1 
ATOM   943  N N   . TRP A 1 124 ? 7.854   21.701  23.301 1.00 22.03 ? 144 TRP A N   1 
ATOM   944  C CA  . TRP A 1 124 ? 8.034   20.284  22.975 1.00 21.52 ? 144 TRP A CA  1 
ATOM   945  C C   . TRP A 1 124 ? 6.681   19.594  22.792 1.00 24.72 ? 144 TRP A C   1 
ATOM   946  O O   . TRP A 1 124 ? 6.322   18.654  23.501 1.00 24.94 ? 144 TRP A O   1 
ATOM   947  C CB  . TRP A 1 124 ? 8.853   19.598  24.064 1.00 20.38 ? 144 TRP A CB  1 
ATOM   948  C CG  . TRP A 1 124 ? 10.238  20.109  24.134 1.00 23.26 ? 144 TRP A CG  1 
ATOM   949  C CD1 . TRP A 1 124 ? 10.670  21.218  24.813 1.00 22.35 ? 144 TRP A CD1 1 
ATOM   950  C CD2 . TRP A 1 124 ? 11.381  19.570  23.479 1.00 23.50 ? 144 TRP A CD2 1 
ATOM   951  N NE1 . TRP A 1 124 ? 12.019  21.387  24.630 1.00 22.24 ? 144 TRP A NE1 1 
ATOM   952  C CE2 . TRP A 1 124 ? 12.479  20.385  23.809 1.00 22.63 ? 144 TRP A CE2 1 
ATOM   953  C CE3 . TRP A 1 124 ? 11.588  18.465  22.642 1.00 23.84 ? 144 TRP A CE3 1 
ATOM   954  C CZ2 . TRP A 1 124 ? 13.764  20.136  23.337 1.00 26.15 ? 144 TRP A CZ2 1 
ATOM   955  C CZ3 . TRP A 1 124 ? 12.863  18.213  22.181 1.00 23.31 ? 144 TRP A CZ3 1 
ATOM   956  C CH2 . TRP A 1 124 ? 13.937  19.045  22.528 1.00 29.64 ? 144 TRP A CH2 1 
ATOM   957  N N   . ASN A 1 125 ? 5.927   20.069  21.799 1.00 26.28 ? 145 ASN A N   1 
ATOM   958  C CA  . ASN A 1 125 ? 4.567   19.593  21.586 1.00 22.45 ? 145 ASN A CA  1 
ATOM   959  C C   . ASN A 1 125 ? 4.402   18.867  20.251 1.00 26.91 ? 145 ASN A C   1 
ATOM   960  O O   . ASN A 1 125 ? 3.271   18.662  19.809 1.00 27.45 ? 145 ASN A O   1 
ATOM   961  C CB  . ASN A 1 125 ? 3.575   20.753  21.682 1.00 25.81 ? 145 ASN A CB  1 
ATOM   962  C CG  . ASN A 1 125 ? 3.854   21.853  20.674 1.00 32.69 ? 145 ASN A CG  1 
ATOM   963  O OD1 . ASN A 1 125 ? 4.649   21.687  19.742 1.00 31.25 ? 145 ASN A OD1 1 
ATOM   964  N ND2 . ASN A 1 125 ? 3.198   22.995  20.859 1.00 34.97 ? 145 ASN A ND2 1 
ATOM   965  N N   . LYS A 1 126 ? 5.501   18.470  19.614 1.00 25.84 ? 146 LYS A N   1 
ATOM   966  C CA  . LYS A 1 126 ? 5.481   17.888  18.278 1.00 26.25 ? 146 LYS A CA  1 
ATOM   967  C C   . LYS A 1 126 ? 5.955   16.438  18.299 1.00 30.79 ? 146 LYS A C   1 
ATOM   968  O O   . LYS A 1 126 ? 6.786   16.042  19.121 1.00 31.78 ? 146 LYS A O   1 
ATOM   969  C CB  . LYS A 1 126 ? 6.364   18.702  17.324 1.00 30.23 ? 146 LYS A CB  1 
ATOM   970  C CG  . LYS A 1 126 ? 5.672   19.909  16.713 1.00 37.13 ? 146 LYS A CG  1 
ATOM   971  C CD  . LYS A 1 126 ? 6.669   20.853  16.045 1.00 44.23 ? 146 LYS A CD  1 
ATOM   972  C CE  . LYS A 1 126 ? 6.261   22.316  16.190 1.00 51.88 ? 146 LYS A CE  1 
ATOM   973  N NZ  . LYS A 1 126 ? 5.998   22.712  17.601 1.00 48.90 ? 146 LYS A NZ  1 
ATOM   974  N N   . ALA A 1 127 ? 5.415   15.645  17.376 1.00 27.41 ? 147 ALA A N   1 
ATOM   975  C CA  . ALA A 1 127 ? 5.874   14.280  17.154 1.00 31.17 ? 147 ALA A CA  1 
ATOM   976  C C   . ALA A 1 127 ? 5.768   14.010  15.666 1.00 27.69 ? 147 ALA A C   1 
ATOM   977  O O   . ALA A 1 127 ? 4.691   14.183  15.087 1.00 31.01 ? 147 ALA A O   1 
ATOM   978  C CB  . ALA A 1 127 ? 5.049   13.262  17.946 1.00 35.57 ? 147 ALA A CB  1 
ATOM   979  N N   . GLY A 1 128 ? 6.881   13.618  15.051 1.00 29.37 ? 148 GLY A N   1 
ATOM   980  C CA  . GLY A 1 128 ? 6.884   13.324  13.625 1.00 28.68 ? 148 GLY A CA  1 
ATOM   981  C C   . GLY A 1 128 ? 6.396   14.462  12.759 1.00 29.41 ? 148 GLY A C   1 
ATOM   982  O O   . GLY A 1 128 ? 5.693   14.225  11.770 1.00 28.93 ? 148 GLY A O   1 
ATOM   983  N N   . GLY A 1 129 ? 6.742   15.702  13.109 1.00 33.50 ? 149 GLY A N   1 
ATOM   984  C CA  . GLY A 1 129 ? 6.319   16.863  12.354 1.00 32.26 ? 149 GLY A CA  1 
ATOM   985  C C   . GLY A 1 129 ? 4.914   17.350  12.640 1.00 29.05 ? 149 GLY A C   1 
ATOM   986  O O   . GLY A 1 129 ? 4.450   18.276  11.962 1.00 36.22 ? 149 GLY A O   1 
ATOM   987  N N   . LYS A 1 130 ? 4.230   16.768  13.621 1.00 26.87 ? 150 LYS A N   1 
ATOM   988  C CA  . LYS A 1 130 ? 2.812   17.003  13.862 1.00 30.76 ? 150 LYS A CA  1 
ATOM   989  C C   . LYS A 1 130 ? 2.641   17.534  15.280 1.00 29.21 ? 150 LYS A C   1 
ATOM   990  O O   . LYS A 1 130 ? 3.018   16.860  16.244 1.00 30.68 ? 150 LYS A O   1 
ATOM   991  C CB  . LYS A 1 130 ? 2.019   15.703  13.667 1.00 28.18 ? 150 LYS A CB  1 
ATOM   992  C CG  . LYS A 1 130 ? 0.510   15.802  13.860 1.00 29.06 ? 150 LYS A CG  1 
ATOM   993  C CD  . LYS A 1 130 ? -0.141  16.570  12.716 1.00 38.65 ? 150 LYS A CD  1 
ATOM   994  C CE  . LYS A 1 130 ? -1.569  16.964  13.039 1.00 43.31 ? 150 LYS A CE  1 
ATOM   995  N NZ  . LYS A 1 130 ? -2.523  15.858  12.753 1.00 46.46 ? 150 LYS A NZ  1 
ATOM   996  N N   . VAL A 1 131 ? 2.075   18.734  15.408 1.00 27.06 ? 151 VAL A N   1 
ATOM   997  C CA  . VAL A 1 131 ? 1.694   19.220  16.731 1.00 25.86 ? 151 VAL A CA  1 
ATOM   998  C C   . VAL A 1 131 ? 0.581   18.335  17.270 1.00 29.47 ? 151 VAL A C   1 
ATOM   999  O O   . VAL A 1 131 ? -0.459  18.152  16.621 1.00 32.17 ? 151 VAL A O   1 
ATOM   1000 C CB  . VAL A 1 131 ? 1.261   20.691  16.676 1.00 29.01 ? 151 VAL A CB  1 
ATOM   1001 C CG1 . VAL A 1 131 ? 0.663   21.106  18.013 1.00 30.52 ? 151 VAL A CG1 1 
ATOM   1002 C CG2 . VAL A 1 131 ? 2.448   21.578  16.343 1.00 31.70 ? 151 VAL A CG2 1 
ATOM   1003 N N   . MET A 1 132 ? 0.803   17.764  18.451 1.00 25.93 ? 152 MET A N   1 
ATOM   1004 C CA  . MET A 1 132 ? -0.103  16.797  19.053 1.00 29.44 ? 152 MET A CA  1 
ATOM   1005 C C   . MET A 1 132 ? -0.810  17.438  20.239 1.00 34.32 ? 152 MET A C   1 
ATOM   1006 O O   . MET A 1 132 ? -0.154  17.986  21.129 1.00 32.37 ? 152 MET A O   1 
ATOM   1007 C CB  . MET A 1 132 ? 0.665   15.554  19.510 1.00 32.19 ? 152 MET A CB  1 
ATOM   1008 C CG  . MET A 1 132 ? 1.439   14.860  18.406 1.00 42.70 ? 152 MET A CG  1 
ATOM   1009 S SD  . MET A 1 132 ? 0.453   13.609  17.574 1.00 60.07 ? 152 MET A SD  1 
ATOM   1010 C CE  . MET A 1 132 ? 1.655   12.947  16.419 1.00 39.21 ? 152 MET A CE  1 
ATOM   1011 N N   . LYS A 1 133 ? -2.145  17.365  20.250 1.00 33.35 ? 153 LYS A N   1 
ATOM   1012 C CA  . LYS A 1 133 ? -2.908  17.898  21.378 1.00 47.26 ? 153 LYS A CA  1 
ATOM   1013 C C   . LYS A 1 133 ? -2.489  17.245  22.689 1.00 34.75 ? 153 LYS A C   1 
ATOM   1014 O O   . LYS A 1 133 ? -2.340  17.928  23.711 1.00 37.56 ? 153 LYS A O   1 
ATOM   1015 C CB  . LYS A 1 133 ? -4.405  17.695  21.145 1.00 48.09 ? 153 LYS A CB  1 
ATOM   1016 C CG  . LYS A 1 133 ? -5.053  18.718  20.230 1.00 49.24 ? 153 LYS A CG  1 
ATOM   1017 C CD  . LYS A 1 133 ? -6.570  18.557  20.243 1.00 48.67 ? 153 LYS A CD  1 
ATOM   1018 C CE  . LYS A 1 133 ? -7.077  17.918  18.959 1.00 54.88 ? 153 LYS A CE  1 
ATOM   1019 N NZ  . LYS A 1 133 ? -8.506  18.264  18.707 1.00 62.83 ? 153 LYS A NZ  1 
ATOM   1020 N N   . GLY A 1 134 ? -2.300  15.923  22.680 1.00 36.71 ? 154 GLY A N   1 
ATOM   1021 C CA  . GLY A 1 134 ? -1.893  15.233  23.894 1.00 33.30 ? 154 GLY A CA  1 
ATOM   1022 C C   . GLY A 1 134 ? -0.554  15.711  24.419 1.00 38.27 ? 154 GLY A C   1 
ATOM   1023 O O   . GLY A 1 134 ? -0.356  15.828  25.633 1.00 33.38 ? 154 GLY A O   1 
ATOM   1024 N N   . LEU A 1 135 ? 0.383   16.006  23.515 1.00 30.51 ? 155 LEU A N   1 
ATOM   1025 C CA  . LEU A 1 135 ? 1.678   16.511  23.951 1.00 28.62 ? 155 LEU A CA  1 
ATOM   1026 C C   . LEU A 1 135 ? 1.552   17.918  24.517 1.00 28.15 ? 155 LEU A C   1 
ATOM   1027 O O   . LEU A 1 135 ? 2.215   18.248  25.504 1.00 28.22 ? 155 LEU A O   1 
ATOM   1028 C CB  . LEU A 1 135 ? 2.682   16.487  22.799 1.00 26.75 ? 155 LEU A CB  1 
ATOM   1029 C CG  . LEU A 1 135 ? 3.056   15.109  22.248 1.00 30.16 ? 155 LEU A CG  1 
ATOM   1030 C CD1 . LEU A 1 135 ? 4.129   15.246  21.176 1.00 30.33 ? 155 LEU A CD1 1 
ATOM   1031 C CD2 . LEU A 1 135 ? 3.517   14.188  23.373 1.00 29.75 ? 155 LEU A CD2 1 
ATOM   1032 N N   . VAL A 1 136 ? 0.714   18.763  23.906 1.00 26.81 ? 156 VAL A N   1 
ATOM   1033 C CA  . VAL A 1 136 ? 0.462   20.086  24.480 1.00 28.22 ? 156 VAL A CA  1 
ATOM   1034 C C   . VAL A 1 136 ? -0.082  19.942  25.895 1.00 27.22 ? 156 VAL A C   1 
ATOM   1035 O O   . VAL A 1 136 ? 0.332   20.658  26.817 1.00 26.46 ? 156 VAL A O   1 
ATOM   1036 C CB  . VAL A 1 136 ? -0.501  20.900  23.596 1.00 32.67 ? 156 VAL A CB  1 
ATOM   1037 C CG1 . VAL A 1 136 ? -0.775  22.263  24.235 1.00 32.80 ? 156 VAL A CG1 1 
ATOM   1038 C CG2 . VAL A 1 136 ? 0.063   21.079  22.206 1.00 28.54 ? 156 VAL A CG2 1 
ATOM   1039 N N   . ARG A 1 137 ? -1.016  19.007  26.088 1.00 29.80 ? 157 ARG A N   1 
ATOM   1040 C CA  . ARG A 1 137 ? -1.583  18.780  27.415 1.00 36.50 ? 157 ARG A CA  1 
ATOM   1041 C C   . ARG A 1 137 ? -0.511  18.352  28.411 1.00 28.25 ? 157 ARG A C   1 
ATOM   1042 O O   . ARG A 1 137 ? -0.447  18.868  29.539 1.00 32.76 ? 157 ARG A O   1 
ATOM   1043 C CB  . ARG A 1 137 ? -2.693  17.733  27.332 1.00 41.24 ? 157 ARG A CB  1 
ATOM   1044 C CG  . ARG A 1 137 ? -4.076  18.299  27.582 1.00 48.99 ? 157 ARG A CG  1 
ATOM   1045 C CD  . ARG A 1 137 ? -5.164  17.300  27.238 1.00 44.70 ? 157 ARG A CD  1 
ATOM   1046 N NE  . ARG A 1 137 ? -6.303  17.979  26.635 1.00 54.55 ? 157 ARG A NE  1 
ATOM   1047 C CZ  . ARG A 1 137 ? -6.776  17.722  25.425 1.00 53.74 ? 157 ARG A CZ  1 
ATOM   1048 N NH1 . ARG A 1 137 ? -6.244  16.786  24.657 1.00 51.52 ? 157 ARG A NH1 1 
ATOM   1049 N NH2 . ARG A 1 137 ? -7.801  18.434  24.968 1.00 51.96 ? 157 ARG A NH2 1 
ATOM   1050 N N   . ARG A 1 138 ? 0.339   17.404  28.015 1.00 28.92 ? 158 ARG A N   1 
ATOM   1051 C CA  . ARG A 1 138 ? 1.422   16.963  28.890 1.00 27.36 ? 158 ARG A CA  1 
ATOM   1052 C C   . ARG A 1 138 ? 2.337   18.120  29.263 1.00 26.97 ? 158 ARG A C   1 
ATOM   1053 O O   . ARG A 1 138 ? 2.691   18.295  30.437 1.00 26.60 ? 158 ARG A O   1 
ATOM   1054 C CB  . ARG A 1 138 ? 2.230   15.850  28.225 1.00 31.11 ? 158 ARG A CB  1 
ATOM   1055 C CG  . ARG A 1 138 ? 1.464   14.579  27.955 1.00 39.40 ? 158 ARG A CG  1 
ATOM   1056 C CD  . ARG A 1 138 ? 2.349   13.586  27.224 1.00 44.07 ? 158 ARG A CD  1 
ATOM   1057 N NE  . ARG A 1 138 ? 1.581   12.678  26.382 1.00 45.28 ? 158 ARG A NE  1 
ATOM   1058 C CZ  . ARG A 1 138 ? 2.115   11.712  25.649 1.00 41.64 ? 158 ARG A CZ  1 
ATOM   1059 N NH1 . ARG A 1 138 ? 3.425   11.534  25.591 1.00 39.60 ? 158 ARG A NH1 1 
ATOM   1060 N NH2 . ARG A 1 138 ? 1.317   10.908  24.953 1.00 48.89 ? 158 ARG A NH2 1 
ATOM   1061 N N   . ARG A 1 139 ? 2.726   18.926  28.269 1.00 25.11 ? 159 ARG A N   1 
ATOM   1062 C CA  . ARG A 1 139 ? 3.668   20.011  28.520 1.00 24.16 ? 159 ARG A CA  1 
ATOM   1063 C C   . ARG A 1 139 ? 3.050   21.079  29.411 1.00 26.64 ? 159 ARG A C   1 
ATOM   1064 O O   . ARG A 1 139 ? 3.728   21.630  30.284 1.00 25.91 ? 159 ARG A O   1 
ATOM   1065 C CB  . ARG A 1 139 ? 4.137   20.626  27.202 1.00 20.43 ? 159 ARG A CB  1 
ATOM   1066 C CG  . ARG A 1 139 ? 4.867   19.648  26.267 1.00 24.55 ? 159 ARG A CG  1 
ATOM   1067 C CD  . ARG A 1 139 ? 6.189   19.144  26.835 1.00 24.39 ? 159 ARG A CD  1 
ATOM   1068 N NE  . ARG A 1 139 ? 6.067   17.907  27.600 1.00 24.78 ? 159 ARG A NE  1 
ATOM   1069 C CZ  . ARG A 1 139 ? 6.071   16.688  27.073 1.00 24.00 ? 159 ARG A CZ  1 
ATOM   1070 N NH1 . ARG A 1 139 ? 6.111   16.497  25.763 1.00 26.46 ? 159 ARG A NH1 1 
ATOM   1071 N NH2 . ARG A 1 139 ? 6.040   15.634  27.883 1.00 24.28 ? 159 ARG A NH2 1 
ATOM   1072 N N   . GLU A 1 140 ? 1.766   21.383  29.211 1.00 24.65 ? 160 GLU A N   1 
ATOM   1073 C CA  . GLU A 1 140 ? 1.118   22.384  30.054 1.00 24.99 ? 160 GLU A CA  1 
ATOM   1074 C C   . GLU A 1 140 ? 0.987   21.887  31.489 1.00 23.55 ? 160 GLU A C   1 
ATOM   1075 O O   . GLU A 1 140 ? 1.178   22.661  32.437 1.00 28.33 ? 160 GLU A O   1 
ATOM   1076 C CB  . GLU A 1 140 ? -0.241  22.768  29.467 1.00 27.00 ? 160 GLU A CB  1 
ATOM   1077 C CG  . GLU A 1 140 ? -0.120  23.468  28.101 1.00 33.12 ? 160 GLU A CG  1 
ATOM   1078 C CD  . GLU A 1 140 ? -1.456  23.895  27.508 1.00 54.08 ? 160 GLU A CD  1 
ATOM   1079 O OE1 . GLU A 1 140 ? -2.446  23.150  27.666 1.00 50.58 ? 160 GLU A OE1 1 
ATOM   1080 O OE2 . GLU A 1 140 ? -1.512  24.963  26.858 1.00 52.83 ? 160 GLU A OE2 1 
ATOM   1081 N N   . ALA A 1 141 ? 0.694   20.595  31.673 1.00 25.17 ? 161 ALA A N   1 
ATOM   1082 C CA  . ALA A 1 141 ? 0.645   20.038  33.023 1.00 24.75 ? 161 ALA A CA  1 
ATOM   1083 C C   . ALA A 1 141 ? 2.015   20.080  33.688 1.00 27.77 ? 161 ALA A C   1 
ATOM   1084 O O   . ALA A 1 141 ? 2.127   20.397  34.885 1.00 26.91 ? 161 ALA A O   1 
ATOM   1085 C CB  . ALA A 1 141 ? 0.113   18.605  32.982 1.00 25.96 ? 161 ALA A CB  1 
ATOM   1086 N N   . GLU A 1 142 ? 3.070   19.770  32.929 1.00 25.27 ? 162 GLU A N   1 
ATOM   1087 C CA  . GLU A 1 142 ? 4.415   19.793  33.495 1.00 25.93 ? 162 GLU A CA  1 
ATOM   1088 C C   . GLU A 1 142 ? 4.813   21.212  33.875 1.00 24.15 ? 162 GLU A C   1 
ATOM   1089 O O   . GLU A 1 142 ? 5.395   21.436  34.942 1.00 26.71 ? 162 GLU A O   1 
ATOM   1090 C CB  . GLU A 1 142 ? 5.434   19.208  32.512 1.00 24.10 ? 162 GLU A CB  1 
ATOM   1091 C CG  . GLU A 1 142 ? 5.349   17.699  32.369 1.00 23.10 ? 162 GLU A CG  1 
ATOM   1092 C CD  . GLU A 1 142 ? 5.891   17.226  31.034 1.00 23.80 ? 162 GLU A CD  1 
ATOM   1093 O OE1 . GLU A 1 142 ? 6.314   18.084  30.242 1.00 26.46 ? 162 GLU A OE1 1 
ATOM   1094 O OE2 . GLU A 1 142 ? 5.833   16.009  30.768 1.00 26.63 ? 162 GLU A OE2 1 
ATOM   1095 N N   . ARG A 1 143 ? 4.514   22.185  33.004 1.00 23.60 ? 163 ARG A N   1 
ATOM   1096 C CA  . ARG A 1 143 ? 4.803   23.585  33.303 1.00 22.94 ? 163 ARG A CA  1 
ATOM   1097 C C   . ARG A 1 143 ? 4.066   24.039  34.557 1.00 26.59 ? 163 ARG A C   1 
ATOM   1098 O O   . ARG A 1 143 ? 4.644   24.713  35.421 1.00 25.67 ? 163 ARG A O   1 
ATOM   1099 C CB  . ARG A 1 143 ? 4.426   24.463  32.108 1.00 23.41 ? 163 ARG A CB  1 
ATOM   1100 C CG  . ARG A 1 143 ? 4.607   25.958  32.342 1.00 24.42 ? 163 ARG A CG  1 
ATOM   1101 C CD  . ARG A 1 143 ? 4.192   26.765  31.125 1.00 25.77 ? 163 ARG A CD  1 
ATOM   1102 N NE  . ARG A 1 143 ? 4.458   28.187  31.323 1.00 30.22 ? 163 ARG A NE  1 
ATOM   1103 C CZ  . ARG A 1 143 ? 3.680   29.000  32.023 1.00 40.22 ? 163 ARG A CZ  1 
ATOM   1104 N NH1 . ARG A 1 143 ? 2.586   28.561  32.623 1.00 43.41 ? 163 ARG A NH1 1 
ATOM   1105 N NH2 . ARG A 1 143 ? 4.013   30.283  32.130 1.00 34.17 ? 163 ARG A NH2 1 
ATOM   1106 N N   . ALA A 1 144 ? 2.781   23.679  34.669 1.00 27.20 ? 164 ALA A N   1 
ATOM   1107 C CA  . ALA A 1 144 ? 1.996   24.103  35.825 1.00 27.75 ? 164 ALA A CA  1 
ATOM   1108 C C   . ALA A 1 144 ? 2.551   23.515  37.114 1.00 30.66 ? 164 ALA A C   1 
ATOM   1109 O O   . ALA A 1 144 ? 2.629   24.212  38.137 1.00 28.74 ? 164 ALA A O   1 
ATOM   1110 C CB  . ALA A 1 144 ? 0.533   23.707  35.643 1.00 29.78 ? 164 ALA A CB  1 
ATOM   1111 N N   . LEU A 1 145 ? 2.937   22.235  37.091 1.00 28.14 ? 165 LEU A N   1 
ATOM   1112 C CA  . LEU A 1 145 ? 3.541   21.643  38.283 1.00 26.81 ? 165 LEU A CA  1 
ATOM   1113 C C   . LEU A 1 145 ? 4.884   22.293  38.604 1.00 27.29 ? 165 LEU A C   1 
ATOM   1114 O O   . LEU A 1 145 ? 5.194   22.556  39.775 1.00 25.71 ? 165 LEU A O   1 
ATOM   1115 C CB  . LEU A 1 145 ? 3.704   20.136  38.095 1.00 26.88 ? 165 LEU A CB  1 
ATOM   1116 C CG  . LEU A 1 145 ? 4.327   19.381  39.270 1.00 25.91 ? 165 LEU A CG  1 
ATOM   1117 C CD1 . LEU A 1 145 ? 3.496   19.590  40.529 1.00 31.08 ? 165 LEU A CD1 1 
ATOM   1118 C CD2 . LEU A 1 145 ? 4.463   17.898  38.949 1.00 28.53 ? 165 LEU A CD2 1 
ATOM   1119 N N   . PHE A 1 146 ? 5.685   22.559  37.572 1.00 26.33 ? 166 PHE A N   1 
ATOM   1120 C CA  . PHE A 1 146 ? 6.981   23.208  37.731 1.00 26.64 ? 166 PHE A CA  1 
ATOM   1121 C C   . PHE A 1 146 ? 6.836   24.570  38.397 1.00 28.94 ? 166 PHE A C   1 
ATOM   1122 O O   . PHE A 1 146 ? 7.689   24.975  39.196 1.00 25.94 ? 166 PHE A O   1 
ATOM   1123 C CB  . PHE A 1 146 ? 7.633   23.334  36.344 1.00 23.65 ? 166 PHE A CB  1 
ATOM   1124 C CG  . PHE A 1 146 ? 9.067   23.800  36.361 1.00 23.29 ? 166 PHE A CG  1 
ATOM   1125 C CD1 . PHE A 1 146 ? 9.368   25.158  36.333 1.00 26.06 ? 166 PHE A CD1 1 
ATOM   1126 C CD2 . PHE A 1 146 ? 10.109  22.889  36.365 1.00 22.07 ? 166 PHE A CD2 1 
ATOM   1127 C CE1 . PHE A 1 146 ? 10.683  25.593  36.331 1.00 26.09 ? 166 PHE A CE1 1 
ATOM   1128 C CE2 . PHE A 1 146 ? 11.426  23.318  36.357 1.00 26.21 ? 166 PHE A CE2 1 
ATOM   1129 C CZ  . PHE A 1 146 ? 11.712  24.677  36.336 1.00 25.57 ? 166 PHE A CZ  1 
ATOM   1130 N N   . LEU A 1 147 ? 5.763   25.290  38.081 1.00 26.25 ? 167 LEU A N   1 
ATOM   1131 C CA  . LEU A 1 147 ? 5.560   26.636  38.606 1.00 25.52 ? 167 LEU A CA  1 
ATOM   1132 C C   . LEU A 1 147 ? 4.853   26.654  39.953 1.00 33.65 ? 167 LEU A C   1 
ATOM   1133 O O   . LEU A 1 147 ? 4.745   27.724  40.567 1.00 35.87 ? 167 LEU A O   1 
ATOM   1134 C CB  . LEU A 1 147 ? 4.762   27.465  37.598 1.00 28.39 ? 167 LEU A CB  1 
ATOM   1135 C CG  . LEU A 1 147 ? 5.539   27.917  36.360 1.00 28.92 ? 167 LEU A CG  1 
ATOM   1136 C CD1 . LEU A 1 147 ? 4.626   28.579  35.337 1.00 29.16 ? 167 LEU A CD1 1 
ATOM   1137 C CD2 . LEU A 1 147 ? 6.683   28.847  36.756 1.00 34.17 ? 167 LEU A CD2 1 
ATOM   1138 N N   . LYS A 1 148 ? 4.382   25.508  40.426 1.00 29.63 ? 168 LYS A N   1 
ATOM   1139 C CA  . LYS A 1 148 ? 3.602   25.435  41.654 1.00 34.12 ? 168 LYS A CA  1 
ATOM   1140 C C   . LYS A 1 148 ? 4.497   25.472  42.893 1.00 33.89 ? 168 LYS A C   1 
ATOM   1141 O O   . LYS A 1 148 ? 5.300   24.566  43.126 1.00 31.33 ? 168 LYS A O   1 
ATOM   1142 C CB  . LYS A 1 148 ? 2.744   24.171  41.645 1.00 35.07 ? 168 LYS A CB  1 
ATOM   1143 C CG  . LYS A 1 148 ? 1.484   24.256  42.495 1.00 41.35 ? 168 LYS A CG  1 
ATOM   1144 C CD  . LYS A 1 148 ? 0.997   22.872  42.873 1.00 42.06 ? 168 LYS A CD  1 
ATOM   1145 C CE  . LYS A 1 148 ? 0.011   22.918  44.033 1.00 47.18 ? 168 LYS A CE  1 
ATOM   1146 N NZ  . LYS A 1 148 ? -1.141  22.001  43.807 1.00 53.55 ? 168 LYS A NZ  1 
ATOM   1147 N N   . SER B 1 2   ? 5.294   10.481  -8.266 1.00 59.03 ? 22  SER B N   1 
ATOM   1148 C CA  . SER B 1 2   ? 5.005   10.481  -6.837 1.00 49.75 ? 22  SER B CA  1 
ATOM   1149 C C   . SER B 1 2   ? 3.577   10.944  -6.576 1.00 48.05 ? 22  SER B C   1 
ATOM   1150 O O   . SER B 1 2   ? 3.088   11.884  -7.204 1.00 45.93 ? 22  SER B O   1 
ATOM   1151 C CB  . SER B 1 2   ? 5.998   11.366  -6.087 1.00 49.06 ? 22  SER B CB  1 
ATOM   1152 O OG  . SER B 1 2   ? 7.119   10.611  -5.660 1.00 59.96 ? 22  SER B OG  1 
ATOM   1153 N N   . LYS B 1 3   ? 2.917   10.285  -5.633 1.00 35.90 ? 23  LYS B N   1 
ATOM   1154 C CA  . LYS B 1 3   ? 1.499   10.487  -5.394 1.00 28.68 ? 23  LYS B CA  1 
ATOM   1155 C C   . LYS B 1 3   ? 1.256   11.665  -4.461 1.00 25.71 ? 23  LYS B C   1 
ATOM   1156 O O   . LYS B 1 3   ? 2.112   12.049  -3.660 1.00 30.90 ? 23  LYS B O   1 
ATOM   1157 C CB  . LYS B 1 3   ? 0.877   9.227   -4.792 1.00 26.67 ? 23  LYS B CB  1 
ATOM   1158 C CG  . LYS B 1 3   ? 0.701   8.085   -5.780 1.00 33.64 ? 23  LYS B CG  1 
ATOM   1159 C CD  . LYS B 1 3   ? -0.072  6.937   -5.156 1.00 29.14 ? 23  LYS B CD  1 
ATOM   1160 C CE  . LYS B 1 3   ? -0.339  5.850   -6.182 1.00 36.93 ? 23  LYS B CE  1 
ATOM   1161 N NZ  . LYS B 1 3   ? 0.932   5.202   -6.618 1.00 39.81 ? 23  LYS B NZ  1 
ATOM   1162 N N   . THR B 1 4   ? 0.061   12.234  -4.578 1.00 30.02 ? 24  THR B N   1 
ATOM   1163 C CA  . THR B 1 4   ? -0.479  13.163  -3.599 1.00 26.96 ? 24  THR B CA  1 
ATOM   1164 C C   . THR B 1 4   ? -1.817  12.616  -3.133 1.00 25.55 ? 24  THR B C   1 
ATOM   1165 O O   . THR B 1 4   ? -2.381  11.704  -3.744 1.00 29.36 ? 24  THR B O   1 
ATOM   1166 C CB  . THR B 1 4   ? -0.663  14.579  -4.167 1.00 34.12 ? 24  THR B CB  1 
ATOM   1167 O OG1 . THR B 1 4   ? -1.452  14.513  -5.357 1.00 34.48 ? 24  THR B OG1 1 
ATOM   1168 C CG2 . THR B 1 4   ? 0.684   15.198  -4.495 1.00 38.15 ? 24  THR B CG2 1 
ATOM   1169 N N   . THR B 1 5   ? -2.317  13.160  -2.026 1.00 25.91 ? 25  THR B N   1 
ATOM   1170 C CA  . THR B 1 5   ? -3.570  12.664  -1.479 1.00 25.36 ? 25  THR B CA  1 
ATOM   1171 C C   . THR B 1 5   ? -4.730  12.993  -2.409 1.00 27.82 ? 25  THR B C   1 
ATOM   1172 O O   . THR B 1 5   ? -4.928  14.151  -2.798 1.00 28.98 ? 25  THR B O   1 
ATOM   1173 C CB  . THR B 1 5   ? -3.811  13.242  -0.087 1.00 25.89 ? 25  THR B CB  1 
ATOM   1174 O OG1 . THR B 1 5   ? -2.629  13.065  0.699  1.00 24.75 ? 25  THR B OG1 1 
ATOM   1175 C CG2 . THR B 1 5   ? -4.968  12.525  0.588  1.00 25.02 ? 25  THR B CG2 1 
ATOM   1176 N N   . SER B 1 6   ? -5.479  11.963  -2.783 1.00 30.01 ? 26  SER B N   1 
ATOM   1177 C CA  . SER B 1 6   ? -6.630  12.116  -3.657 1.00 29.56 ? 26  SER B CA  1 
ATOM   1178 C C   . SER B 1 6   ? -7.871  12.403  -2.812 1.00 40.11 ? 26  SER B C   1 
ATOM   1179 O O   . SER B 1 6   ? -7.796  12.571  -1.592 1.00 34.97 ? 26  SER B O   1 
ATOM   1180 C CB  . SER B 1 6   ? -6.796  10.869  -4.517 1.00 27.97 ? 26  SER B CB  1 
ATOM   1181 O OG  . SER B 1 6   ? -7.744  9.999   -3.930 1.00 35.81 ? 26  SER B OG  1 
ATOM   1182 N N   . ASN B 1 7   ? -9.040  12.431  -3.456 1.00 43.57 ? 27  ASN B N   1 
ATOM   1183 C CA  . ASN B 1 7   ? -10.265 12.826  -2.768 1.00 42.18 ? 27  ASN B CA  1 
ATOM   1184 C C   . ASN B 1 7   ? -10.715 11.802  -1.734 1.00 46.64 ? 27  ASN B C   1 
ATOM   1185 O O   . ASN B 1 7   ? -11.383 12.170  -0.765 1.00 46.30 ? 27  ASN B O   1 
ATOM   1186 C CB  . ASN B 1 7   ? -11.373 13.078  -3.788 1.00 57.70 ? 27  ASN B CB  1 
ATOM   1187 C CG  . ASN B 1 7   ? -10.945 14.033  -4.880 1.00 51.74 ? 27  ASN B CG  1 
ATOM   1188 O OD1 . ASN B 1 7   ? -10.627 15.192  -4.611 1.00 61.07 ? 27  ASN B OD1 1 
ATOM   1189 N ND2 . ASN B 1 7   ? -10.918 13.552  -6.117 1.00 64.73 ? 27  ASN B ND2 1 
ATOM   1190 N N   . ALA B 1 8   ? -10.375 10.524  -1.907 1.00 38.52 ? 28  ALA B N   1 
ATOM   1191 C CA  . ALA B 1 8   ? -10.742 9.546   -0.887 1.00 41.84 ? 28  ALA B CA  1 
ATOM   1192 C C   . ALA B 1 8   ? -10.044 9.845   0.434  1.00 38.01 ? 28  ALA B C   1 
ATOM   1193 O O   . ALA B 1 8   ? -10.689 9.896   1.493  1.00 39.81 ? 28  ALA B O   1 
ATOM   1194 C CB  . ALA B 1 8   ? -10.412 8.130   -1.365 1.00 42.07 ? 28  ALA B CB  1 
ATOM   1195 N N   . GLY B 1 9   ? -8.728  10.067  0.389  1.00 34.10 ? 29  GLY B N   1 
ATOM   1196 C CA  . GLY B 1 9   ? -8.005  10.409  1.603  1.00 34.87 ? 29  GLY B CA  1 
ATOM   1197 C C   . GLY B 1 9   ? -8.417  11.756  2.161  1.00 26.67 ? 29  GLY B C   1 
ATOM   1198 O O   . GLY B 1 9   ? -8.527  11.924  3.380  1.00 33.09 ? 29  GLY B O   1 
ATOM   1199 N N   . LEU B 1 10  ? -8.647  12.735  1.279  1.00 34.73 ? 30  LEU B N   1 
ATOM   1200 C CA  . LEU B 1 10  ? -9.093  14.045  1.742  1.00 30.49 ? 30  LEU B CA  1 
ATOM   1201 C C   . LEU B 1 10  ? -10.436 13.949  2.447  1.00 36.63 ? 30  LEU B C   1 
ATOM   1202 O O   . LEU B 1 10  ? -10.631 14.568  3.492  1.00 33.64 ? 30  LEU B O   1 
ATOM   1203 C CB  . LEU B 1 10  ? -9.169  15.038  0.579  1.00 34.65 ? 30  LEU B CB  1 
ATOM   1204 C CG  . LEU B 1 10  ? -7.861  15.479  -0.078 1.00 30.32 ? 30  LEU B CG  1 
ATOM   1205 C CD1 . LEU B 1 10  ? -8.147  16.416  -1.242 1.00 36.64 ? 30  LEU B CD1 1 
ATOM   1206 C CD2 . LEU B 1 10  ? -6.958  16.151  0.944  1.00 30.04 ? 30  LEU B CD2 1 
ATOM   1207 N N   . ASN B 1 11  ? -11.372 13.166  1.906  1.00 40.37 ? 31  ASN B N   1 
ATOM   1208 C CA  . ASN B 1 11  ? -12.671 13.017  2.556  1.00 44.50 ? 31  ASN B CA  1 
ATOM   1209 C C   . ASN B 1 11  ? -12.545 12.291  3.888  1.00 39.93 ? 31  ASN B C   1 
ATOM   1210 O O   . ASN B 1 11  ? -13.199 12.664  4.869  1.00 41.26 ? 31  ASN B O   1 
ATOM   1211 C CB  . ASN B 1 11  ? -13.649 12.288  1.635  1.00 44.44 ? 31  ASN B CB  1 
ATOM   1212 C CG  . ASN B 1 11  ? -13.976 13.084  0.388  1.00 43.38 ? 31  ASN B CG  1 
ATOM   1213 O OD1 . ASN B 1 11  ? -13.798 14.303  0.349  1.00 48.73 ? 31  ASN B OD1 1 
ATOM   1214 N ND2 . ASN B 1 11  ? -14.465 12.398  -0.639 1.00 52.57 ? 31  ASN B ND2 1 
ATOM   1215 N N   . LEU B 1 12  ? -11.710 11.249  3.946  1.00 43.55 ? 32  LEU B N   1 
ATOM   1216 C CA  . LEU B 1 12  ? -11.443 10.582  5.218  1.00 37.79 ? 32  LEU B CA  1 
ATOM   1217 C C   . LEU B 1 12  ? -10.967 11.584  6.272  1.00 36.58 ? 32  LEU B C   1 
ATOM   1218 O O   . LEU B 1 12  ? -11.547 11.702  7.365  1.00 36.60 ? 32  LEU B O   1 
ATOM   1219 C CB  . LEU B 1 12  ? -10.399 9.484   4.996  1.00 46.89 ? 32  LEU B CB  1 
ATOM   1220 C CG  . LEU B 1 12  ? -10.443 8.172   5.783  1.00 42.74 ? 32  LEU B CG  1 
ATOM   1221 C CD1 . LEU B 1 12  ? -11.851 7.601   5.815  1.00 42.73 ? 32  LEU B CD1 1 
ATOM   1222 C CD2 . LEU B 1 12  ? -9.461  7.166   5.191  1.00 37.29 ? 32  LEU B CD2 1 
ATOM   1223 N N   . ILE B 1 13  ? -9.921  12.344  5.935  1.00 35.81 ? 33  ILE B N   1 
ATOM   1224 C CA  . ILE B 1 13  ? -9.326  13.266  6.896  1.00 35.71 ? 33  ILE B CA  1 
ATOM   1225 C C   . ILE B 1 13  ? -10.300 14.386  7.244  1.00 33.00 ? 33  ILE B C   1 
ATOM   1226 O O   . ILE B 1 13  ? -10.385 14.812  8.401  1.00 35.81 ? 33  ILE B O   1 
ATOM   1227 C CB  . ILE B 1 13  ? -7.995  13.815  6.351  1.00 31.64 ? 33  ILE B CB  1 
ATOM   1228 C CG1 . ILE B 1 13  ? -6.962  12.691  6.246  1.00 35.34 ? 33  ILE B CG1 1 
ATOM   1229 C CG2 . ILE B 1 13  ? -7.463  14.908  7.248  1.00 29.00 ? 33  ILE B CG2 1 
ATOM   1230 C CD1 . ILE B 1 13  ? -5.795  13.020  5.334  1.00 32.58 ? 33  ILE B CD1 1 
ATOM   1231 N N   . LYS B 1 14  ? -11.046 14.885  6.250  1.00 32.77 ? 34  LYS B N   1 
ATOM   1232 C CA  . LYS B 1 14  ? -12.025 15.937  6.502  1.00 31.54 ? 34  LYS B CA  1 
ATOM   1233 C C   . LYS B 1 14  ? -13.105 15.460  7.462  1.00 35.14 ? 34  LYS B C   1 
ATOM   1234 O O   . LYS B 1 14  ? -13.530 16.207  8.352  1.00 36.64 ? 34  LYS B O   1 
ATOM   1235 C CB  . LYS B 1 14  ? -12.641 16.402  5.180  1.00 30.25 ? 34  LYS B CB  1 
ATOM   1236 C CG  . LYS B 1 14  ? -11.743 17.327  4.366  1.00 31.72 ? 34  LYS B CG  1 
ATOM   1237 C CD  . LYS B 1 14  ? -12.049 17.280  2.872  1.00 46.48 ? 34  LYS B CD  1 
ATOM   1238 C CE  . LYS B 1 14  ? -13.279 18.087  2.508  1.00 46.53 ? 34  LYS B CE  1 
ATOM   1239 N NZ  . LYS B 1 14  ? -13.356 18.352  1.038  1.00 46.19 ? 34  LYS B NZ  1 
ATOM   1240 N N   . GLY B 1 15  ? -13.557 14.215  7.300  1.00 37.59 ? 35  GLY B N   1 
ATOM   1241 C CA  . GLY B 1 15  ? -14.498 13.657  8.253  1.00 40.53 ? 35  GLY B CA  1 
ATOM   1242 C C   . GLY B 1 15  ? -13.932 13.594  9.657  1.00 39.76 ? 35  GLY B C   1 
ATOM   1243 O O   . GLY B 1 15  ? -14.630 13.887  10.630 1.00 40.69 ? 35  GLY B O   1 
ATOM   1244 N N   . PHE B 1 16  ? -12.654 13.229  9.784  1.00 43.90 ? 36  PHE B N   1 
ATOM   1245 C CA  . PHE B 1 16  ? -12.094 13.100  11.132 1.00 33.09 ? 36  PHE B CA  1 
ATOM   1246 C C   . PHE B 1 16  ? -11.808 14.448  11.790 1.00 44.99 ? 36  PHE B C   1 
ATOM   1247 O O   . PHE B 1 16  ? -12.014 14.602  12.999 1.00 43.44 ? 36  PHE B O   1 
ATOM   1248 C CB  . PHE B 1 16  ? -10.834 12.244  11.101 1.00 42.13 ? 36  PHE B CB  1 
ATOM   1249 C CG  . PHE B 1 16  ? -11.055 10.887  10.521 1.00 41.21 ? 36  PHE B CG  1 
ATOM   1250 C CD1 . PHE B 1 16  ? -12.195 10.167  10.843 1.00 51.40 ? 36  PHE B CD1 1 
ATOM   1251 C CD2 . PHE B 1 16  ? -10.133 10.326  9.659  1.00 42.28 ? 36  PHE B CD2 1 
ATOM   1252 C CE1 . PHE B 1 16  ? -12.411 8.910   10.314 1.00 48.96 ? 36  PHE B CE1 1 
ATOM   1253 C CE2 . PHE B 1 16  ? -10.341 9.069   9.130  1.00 51.73 ? 36  PHE B CE2 1 
ATOM   1254 C CZ  . PHE B 1 16  ? -11.484 8.361   9.455  1.00 48.01 ? 36  PHE B CZ  1 
ATOM   1255 N N   . GLU B 1 17  ? -11.323 15.429  11.031 1.00 35.87 ? 37  GLU B N   1 
ATOM   1256 C CA  . GLU B 1 17  ? -10.994 16.731  11.601 1.00 36.82 ? 37  GLU B CA  1 
ATOM   1257 C C   . GLU B 1 17  ? -12.222 17.583  11.872 1.00 34.86 ? 37  GLU B C   1 
ATOM   1258 O O   . GLU B 1 17  ? -12.169 18.471  12.732 1.00 39.32 ? 37  GLU B O   1 
ATOM   1259 C CB  . GLU B 1 17  ? -10.056 17.504  10.670 1.00 31.65 ? 37  GLU B CB  1 
ATOM   1260 C CG  . GLU B 1 17  ? -8.670  16.915  10.530 1.00 36.78 ? 37  GLU B CG  1 
ATOM   1261 C CD  . GLU B 1 17  ? -7.977  16.748  11.866 1.00 44.45 ? 37  GLU B CD  1 
ATOM   1262 O OE1 . GLU B 1 17  ? -7.828  17.755  12.592 1.00 45.05 ? 37  GLU B OE1 1 
ATOM   1263 O OE2 . GLU B 1 17  ? -7.580  15.609  12.189 1.00 50.72 ? 37  GLU B OE2 1 
ATOM   1264 N N   . GLY B 1 18  ? -13.315 17.344  11.157 1.00 32.22 ? 38  GLY B N   1 
ATOM   1265 C CA  . GLY B 1 18  ? -14.454 18.233  11.213 1.00 35.32 ? 38  GLY B CA  1 
ATOM   1266 C C   . GLY B 1 18  ? -14.219 19.479  10.387 1.00 35.99 ? 38  GLY B C   1 
ATOM   1267 O O   . GLY B 1 18  ? -13.072 19.854  10.130 1.00 34.57 ? 38  GLY B O   1 
ATOM   1268 N N   . LYS B 1 19  ? -15.299 20.114  9.950  1.00 41.30 ? 39  LYS B N   1 
ATOM   1269 C CA  . LYS B 1 19  ? -15.246 21.384  9.238  1.00 34.44 ? 39  LYS B CA  1 
ATOM   1270 C C   . LYS B 1 19  ? -15.554 22.510  10.216 1.00 36.30 ? 39  LYS B C   1 
ATOM   1271 O O   . LYS B 1 19  ? -16.628 22.528  10.825 1.00 40.85 ? 39  LYS B O   1 
ATOM   1272 C CB  . LYS B 1 19  ? -16.254 21.405  8.094  1.00 35.12 ? 39  LYS B CB  1 
ATOM   1273 C CG  . LYS B 1 19  ? -16.328 22.731  7.365  1.00 39.25 ? 39  LYS B CG  1 
ATOM   1274 C CD  . LYS B 1 19  ? -16.751 22.532  5.936  1.00 50.16 ? 39  LYS B CD  1 
ATOM   1275 C CE  . LYS B 1 19  ? -18.167 23.052  5.778  1.00 53.92 ? 39  LYS B CE  1 
ATOM   1276 N NZ  . LYS B 1 19  ? -18.943 22.271  4.775  1.00 57.63 ? 39  LYS B NZ  1 
ATOM   1277 N N   . ARG B 1 20  ? -14.622 23.450  10.360 1.00 37.44 ? 40  ARG B N   1 
ATOM   1278 C CA  . ARG B 1 20  ? -14.831 24.629  11.194 1.00 32.98 ? 40  ARG B CA  1 
ATOM   1279 C C   . ARG B 1 20  ? -14.331 25.852  10.441 1.00 33.46 ? 40  ARG B C   1 
ATOM   1280 O O   . ARG B 1 20  ? -13.120 26.037  10.279 1.00 38.99 ? 40  ARG B O   1 
ATOM   1281 C CB  . ARG B 1 20  ? -14.124 24.495  12.543 1.00 45.36 ? 40  ARG B CB  1 
ATOM   1282 C CG  . ARG B 1 20  ? -14.614 23.341  13.399 1.00 44.22 ? 40  ARG B CG  1 
ATOM   1283 C CD  . ARG B 1 20  ? -15.393 23.862  14.594 1.00 44.97 ? 40  ARG B CD  1 
ATOM   1284 N NE  . ARG B 1 20  ? -15.087 23.133  15.819 1.00 52.44 ? 40  ARG B NE  1 
ATOM   1285 C CZ  . ARG B 1 20  ? -15.159 23.658  17.034 1.00 56.15 ? 40  ARG B CZ  1 
ATOM   1286 N NH1 . ARG B 1 20  ? -15.559 24.905  17.225 1.00 55.35 ? 40  ARG B NH1 1 
ATOM   1287 N NH2 . ARG B 1 20  ? -14.825 22.913  18.084 1.00 62.19 ? 40  ARG B NH2 1 
ATOM   1288 N N   . LEU B 1 21  ? -15.260 26.689  9.990  1.00 33.26 ? 41  LEU B N   1 
ATOM   1289 C CA  . LEU B 1 21  ? -14.915 27.881  9.230  1.00 31.05 ? 41  LEU B CA  1 
ATOM   1290 C C   . LEU B 1 21  ? -14.636 29.089  10.114 1.00 31.25 ? 41  LEU B C   1 
ATOM   1291 O O   . LEU B 1 21  ? -14.285 30.151  9.595  1.00 33.39 ? 41  LEU B O   1 
ATOM   1292 C CB  . LEU B 1 21  ? -16.029 28.203  8.234  1.00 30.24 ? 41  LEU B CB  1 
ATOM   1293 C CG  . LEU B 1 21  ? -16.305 27.066  7.244  1.00 32.47 ? 41  LEU B CG  1 
ATOM   1294 C CD1 . LEU B 1 21  ? -17.298 27.494  6.178  1.00 38.32 ? 41  LEU B CD1 1 
ATOM   1295 C CD2 . LEU B 1 21  ? -15.007 26.566  6.622  1.00 31.91 ? 41  LEU B CD2 1 
ATOM   1296 N N   . ASN B 1 22  ? -14.790 28.957  11.426 1.00 34.42 ? 42  ASN B N   1 
ATOM   1297 C CA  . ASN B 1 22  ? -14.335 29.958  12.378 1.00 35.32 ? 42  ASN B CA  1 
ATOM   1298 C C   . ASN B 1 22  ? -13.247 29.348  13.249 1.00 29.71 ? 42  ASN B C   1 
ATOM   1299 O O   . ASN B 1 22  ? -13.365 28.198  13.690 1.00 31.74 ? 42  ASN B O   1 
ATOM   1300 C CB  . ASN B 1 22  ? -15.485 30.481  13.248 1.00 40.57 ? 42  ASN B CB  1 
ATOM   1301 C CG  . ASN B 1 22  ? -16.606 31.085  12.427 1.00 42.24 ? 42  ASN B CG  1 
ATOM   1302 O OD1 . ASN B 1 22  ? -16.519 32.230  11.992 1.00 50.84 ? 42  ASN B OD1 1 
ATOM   1303 N ND2 . ASN B 1 22  ? -17.664 30.315  12.210 1.00 51.76 ? 42  ASN B ND2 1 
ATOM   1304 N N   . ALA B 1 23  ? -12.182 30.117  13.475 1.00 30.08 ? 43  ALA B N   1 
ATOM   1305 C CA  . ALA B 1 23  ? -11.067 29.636  14.276 1.00 31.85 ? 43  ALA B CA  1 
ATOM   1306 C C   . ALA B 1 23  ? -11.556 29.201  15.649 1.00 34.59 ? 43  ALA B C   1 
ATOM   1307 O O   . ALA B 1 23  ? -12.400 29.859  16.263 1.00 34.28 ? 43  ALA B O   1 
ATOM   1308 C CB  . ALA B 1 23  ? -10.002 30.722  14.417 1.00 34.44 ? 43  ALA B CB  1 
ATOM   1309 N N   . TYR B 1 24  ? -11.040 28.071  16.122 1.00 30.45 ? 44  TYR B N   1 
ATOM   1310 C CA  . TYR B 1 24  ? -11.467 27.522  17.397 1.00 34.14 ? 44  TYR B CA  1 
ATOM   1311 C C   . TYR B 1 24  ? -10.257 27.039  18.176 1.00 33.25 ? 44  TYR B C   1 
ATOM   1312 O O   . TYR B 1 24  ? -9.255  26.601  17.604 1.00 29.12 ? 44  TYR B O   1 
ATOM   1313 C CB  . TYR B 1 24  ? -12.468 26.368  17.224 1.00 32.37 ? 44  TYR B CB  1 
ATOM   1314 C CG  . TYR B 1 24  ? -11.914 25.151  16.519 1.00 33.26 ? 44  TYR B CG  1 
ATOM   1315 C CD1 . TYR B 1 24  ? -11.811 25.112  15.134 1.00 28.72 ? 44  TYR B CD1 1 
ATOM   1316 C CD2 . TYR B 1 24  ? -11.515 24.029  17.235 1.00 37.11 ? 44  TYR B CD2 1 
ATOM   1317 C CE1 . TYR B 1 24  ? -11.308 24.000  14.486 1.00 32.24 ? 44  TYR B CE1 1 
ATOM   1318 C CE2 . TYR B 1 24  ? -11.015 22.912  16.593 1.00 35.50 ? 44  TYR B CE2 1 
ATOM   1319 C CZ  . TYR B 1 24  ? -10.915 22.902  15.217 1.00 35.20 ? 44  TYR B CZ  1 
ATOM   1320 O OH  . TYR B 1 24  ? -10.424 21.799  14.557 1.00 38.22 ? 44  TYR B OH  1 
ATOM   1321 N N   . ASP B 1 25  ? -10.356 27.155  19.495 1.00 36.78 ? 45  ASP B N   1 
ATOM   1322 C CA  . ASP B 1 25  ? -9.404  26.513  20.386 1.00 30.08 ? 45  ASP B CA  1 
ATOM   1323 C C   . ASP B 1 25  ? -9.636  25.011  20.311 1.00 42.79 ? 45  ASP B C   1 
ATOM   1324 O O   . ASP B 1 25  ? -10.750 24.538  20.563 1.00 37.00 ? 45  ASP B O   1 
ATOM   1325 C CB  . ASP B 1 25  ? -9.594  27.040  21.811 1.00 30.68 ? 45  ASP B CB  1 
ATOM   1326 C CG  . ASP B 1 25  ? -8.494  26.616  22.754 1.00 35.74 ? 45  ASP B CG  1 
ATOM   1327 O OD1 . ASP B 1 25  ? -8.016  25.468  22.663 1.00 35.96 ? 45  ASP B OD1 1 
ATOM   1328 O OD2 . ASP B 1 25  ? -8.104  27.443  23.605 1.00 30.30 ? 45  ASP B OD2 1 
ATOM   1329 N N   . ASP B 1 26  ? -8.603  24.261  19.935 1.00 39.45 ? 46  ASP B N   1 
ATOM   1330 C CA  . ASP B 1 26  ? -8.767  22.827  19.723 1.00 40.16 ? 46  ASP B CA  1 
ATOM   1331 C C   . ASP B 1 26  ? -8.884  22.045  21.025 1.00 34.36 ? 46  ASP B C   1 
ATOM   1332 O O   . ASP B 1 26  ? -8.998  20.818  20.979 1.00 34.62 ? 46  ASP B O   1 
ATOM   1333 C CB  . ASP B 1 26  ? -7.609  22.271  18.887 1.00 38.78 ? 46  ASP B CB  1 
ATOM   1334 C CG  . ASP B 1 26  ? -6.253  22.459  19.550 1.00 40.50 ? 46  ASP B CG  1 
ATOM   1335 O OD1 . ASP B 1 26  ? -6.188  23.033  20.659 1.00 34.81 ? 46  ASP B OD1 1 
ATOM   1336 O OD2 . ASP B 1 26  ? -5.246  22.010  18.964 1.00 34.98 ? 46  ASP B OD2 1 
ATOM   1337 N N   . GLY B 1 27  ? -8.865  22.728  22.165 1.00 29.25 ? 47  GLY B N   1 
ATOM   1338 C CA  . GLY B 1 27  ? -8.916  22.106  23.476 1.00 24.58 ? 47  GLY B CA  1 
ATOM   1339 C C   . GLY B 1 27  ? -7.660  22.271  24.301 1.00 36.22 ? 47  GLY B C   1 
ATOM   1340 O O   . GLY B 1 27  ? -7.698  22.003  25.510 1.00 41.18 ? 47  GLY B O   1 
ATOM   1341 N N   . VAL B 1 28  ? -6.550  22.699  23.700 1.00 38.27 ? 48  VAL B N   1 
ATOM   1342 C CA  . VAL B 1 28  ? -5.291  22.851  24.426 1.00 32.18 ? 48  VAL B CA  1 
ATOM   1343 C C   . VAL B 1 28  ? -4.672  24.211  24.125 1.00 41.17 ? 48  VAL B C   1 
ATOM   1344 O O   . VAL B 1 28  ? -3.475  24.425  24.349 1.00 43.35 ? 48  VAL B O   1 
ATOM   1345 C CB  . VAL B 1 28  ? -4.310  21.716  24.080 1.00 35.62 ? 48  VAL B CB  1 
ATOM   1346 C CG1 . VAL B 1 28  ? -4.860  20.375  24.538 1.00 38.82 ? 48  VAL B CG1 1 
ATOM   1347 C CG2 . VAL B 1 28  ? -4.024  21.701  22.586 1.00 42.02 ? 48  VAL B CG2 1 
ATOM   1348 N N   . GLY B 1 29  ? -5.473  25.137  23.605 1.00 35.40 ? 49  GLY B N   1 
ATOM   1349 C CA  . GLY B 1 29  ? -5.007  26.490  23.379 1.00 26.41 ? 49  GLY B CA  1 
ATOM   1350 C C   . GLY B 1 29  ? -4.339  26.748  22.043 1.00 30.70 ? 49  GLY B C   1 
ATOM   1351 O O   . GLY B 1 29  ? -3.812  27.849  21.839 1.00 33.45 ? 49  GLY B O   1 
ATOM   1352 N N   . VAL B 1 30  ? -4.330  25.780  21.135 1.00 32.06 ? 50  VAL B N   1 
ATOM   1353 C CA  . VAL B 1 30  ? -3.763  25.956  19.802 1.00 29.07 ? 50  VAL B CA  1 
ATOM   1354 C C   . VAL B 1 30  ? -4.912  26.296  18.865 1.00 26.65 ? 50  VAL B C   1 
ATOM   1355 O O   . VAL B 1 30  ? -5.802  25.472  18.626 1.00 26.92 ? 50  VAL B O   1 
ATOM   1356 C CB  . VAL B 1 30  ? -3.008  24.707  19.331 1.00 32.13 ? 50  VAL B CB  1 
ATOM   1357 C CG1 . VAL B 1 30  ? -2.641  24.842  17.854 1.00 34.55 ? 50  VAL B CG1 1 
ATOM   1358 C CG2 . VAL B 1 30  ? -1.765  24.498  20.168 1.00 32.33 ? 50  VAL B CG2 1 
ATOM   1359 N N   . TRP B 1 31  ? -4.900  27.512  18.328 1.00 27.52 ? 51  TRP B N   1 
ATOM   1360 C CA  . TRP B 1 31  ? -6.012  27.953  17.504 1.00 25.51 ? 51  TRP B CA  1 
ATOM   1361 C C   . TRP B 1 31  ? -5.957  27.285  16.135 1.00 23.27 ? 51  TRP B C   1 
ATOM   1362 O O   . TRP B 1 31  ? -4.899  27.211  15.503 1.00 26.35 ? 51  TRP B O   1 
ATOM   1363 C CB  . TRP B 1 31  ? -6.015  29.476  17.401 1.00 25.74 ? 51  TRP B CB  1 
ATOM   1364 C CG  . TRP B 1 31  ? -6.466  30.039  18.708 1.00 25.44 ? 51  TRP B CG  1 
ATOM   1365 C CD1 . TRP B 1 31  ? -5.682  30.386  19.769 1.00 30.19 ? 51  TRP B CD1 1 
ATOM   1366 C CD2 . TRP B 1 31  ? -7.819  30.219  19.132 1.00 28.53 ? 51  TRP B CD2 1 
ATOM   1367 N NE1 . TRP B 1 31  ? -6.465  30.817  20.813 1.00 33.09 ? 51  TRP B NE1 1 
ATOM   1368 C CE2 . TRP B 1 31  ? -7.782  30.722  20.446 1.00 28.71 ? 51  TRP B CE2 1 
ATOM   1369 C CE3 . TRP B 1 31  ? -9.059  30.036  18.514 1.00 36.15 ? 51  TRP B CE3 1 
ATOM   1370 C CZ2 . TRP B 1 31  ? -8.937  31.037  21.156 1.00 38.48 ? 51  TRP B CZ2 1 
ATOM   1371 C CZ3 . TRP B 1 31  ? -10.205 30.348  19.219 1.00 42.06 ? 51  TRP B CZ3 1 
ATOM   1372 C CH2 . TRP B 1 31  ? -10.136 30.846  20.527 1.00 37.03 ? 51  TRP B CH2 1 
ATOM   1373 N N   . THR B 1 32  ? -7.113  26.793  15.693 1.00 24.02 ? 52  THR B N   1 
ATOM   1374 C CA  . THR B 1 32  ? -7.238  25.890  14.561 1.00 24.67 ? 52  THR B CA  1 
ATOM   1375 C C   . THR B 1 32  ? -8.406  26.344  13.698 1.00 26.08 ? 52  THR B C   1 
ATOM   1376 O O   . THR B 1 32  ? -9.344  26.971  14.193 1.00 27.46 ? 52  THR B O   1 
ATOM   1377 C CB  . THR B 1 32  ? -7.458  24.459  15.072 1.00 27.16 ? 52  THR B CB  1 
ATOM   1378 O OG1 . THR B 1 32  ? -6.493  24.182  16.096 1.00 27.22 ? 52  THR B OG1 1 
ATOM   1379 C CG2 . THR B 1 32  ? -7.309  23.442  13.956 1.00 25.67 ? 52  THR B CG2 1 
ATOM   1380 N N   . ILE B 1 33  ? -8.351  26.035  12.399 1.00 23.35 ? 53  ILE B N   1 
ATOM   1381 C CA  . ILE B 1 33  ? -9.418  26.418  11.485 1.00 24.10 ? 53  ILE B CA  1 
ATOM   1382 C C   . ILE B 1 33  ? -9.474  25.427  10.329 1.00 23.52 ? 53  ILE B C   1 
ATOM   1383 O O   . ILE B 1 33  ? -8.525  24.685  10.068 1.00 26.15 ? 53  ILE B O   1 
ATOM   1384 C CB  . ILE B 1 33  ? -9.220  27.869  10.979 1.00 24.64 ? 53  ILE B CB  1 
ATOM   1385 C CG1 . ILE B 1 33  ? -10.553 28.476  10.540 1.00 26.95 ? 53  ILE B CG1 1 
ATOM   1386 C CG2 . ILE B 1 33  ? -8.180  27.910  9.852  1.00 25.92 ? 53  ILE B CG2 1 
ATOM   1387 C CD1 . ILE B 1 33  ? -10.471 29.966  10.228 1.00 27.41 ? 53  ILE B CD1 1 
ATOM   1388 N N   . GLY B 1 34  ? -10.610 25.415  9.638  1.00 26.28 ? 54  GLY B N   1 
ATOM   1389 C CA  . GLY B 1 34  ? -10.741 24.565  8.463  1.00 25.59 ? 54  GLY B CA  1 
ATOM   1390 C C   . GLY B 1 34  ? -10.822 23.108  8.873  1.00 26.38 ? 54  GLY B C   1 
ATOM   1391 O O   . GLY B 1 34  ? -11.663 22.722  9.694  1.00 31.77 ? 54  GLY B O   1 
ATOM   1392 N N   . PHE B 1 35  ? -9.944  22.290  8.296  1.00 26.91 ? 55  PHE B N   1 
ATOM   1393 C CA  . PHE B 1 35  ? -9.841  20.868  8.615  1.00 27.85 ? 55  PHE B CA  1 
ATOM   1394 C C   . PHE B 1 35  ? -8.522  20.614  9.342  1.00 27.09 ? 55  PHE B C   1 
ATOM   1395 O O   . PHE B 1 35  ? -7.623  19.949  8.825  1.00 32.44 ? 55  PHE B O   1 
ATOM   1396 C CB  . PHE B 1 35  ? -9.933  20.021  7.334  1.00 27.45 ? 55  PHE B CB  1 
ATOM   1397 C CG  . PHE B 1 35  ? -11.154 20.285  6.503  1.00 27.44 ? 55  PHE B CG  1 
ATOM   1398 C CD1 . PHE B 1 35  ? -12.390 19.783  6.879  1.00 31.44 ? 55  PHE B CD1 1 
ATOM   1399 C CD2 . PHE B 1 35  ? -11.062 21.019  5.327  1.00 27.13 ? 55  PHE B CD2 1 
ATOM   1400 C CE1 . PHE B 1 35  ? -13.515 20.017  6.102  1.00 35.02 ? 55  PHE B CE1 1 
ATOM   1401 C CE2 . PHE B 1 35  ? -12.182 21.253  4.545  1.00 31.78 ? 55  PHE B CE2 1 
ATOM   1402 C CZ  . PHE B 1 35  ? -13.411 20.753  4.932  1.00 38.14 ? 55  PHE B CZ  1 
ATOM   1403 N N   . GLY B 1 36  ? -8.397  21.177  10.545 1.00 25.08 ? 56  GLY B N   1 
ATOM   1404 C CA  . GLY B 1 36  ? -7.231  20.957  11.382 1.00 27.07 ? 56  GLY B CA  1 
ATOM   1405 C C   . GLY B 1 36  ? -6.041  21.863  11.143 1.00 26.86 ? 56  GLY B C   1 
ATOM   1406 O O   . GLY B 1 36  ? -4.950  21.569  11.648 1.00 26.86 ? 56  GLY B O   1 
ATOM   1407 N N   . THR B 1 37  ? -6.209  22.961  10.408 1.00 22.89 ? 57  THR B N   1 
ATOM   1408 C CA  . THR B 1 37  ? -5.086  23.826  10.073 1.00 26.63 ? 57  THR B CA  1 
ATOM   1409 C C   . THR B 1 37  ? -4.740  24.739  11.242 1.00 21.87 ? 57  THR B C   1 
ATOM   1410 O O   . THR B 1 37  ? -5.623  25.364  11.838 1.00 24.73 ? 57  THR B O   1 
ATOM   1411 C CB  . THR B 1 37  ? -5.428  24.654  8.836  1.00 23.08 ? 57  THR B CB  1 
ATOM   1412 O OG1 . THR B 1 37  ? -5.592  23.774  7.719  1.00 22.89 ? 57  THR B OG1 1 
ATOM   1413 C CG2 . THR B 1 37  ? -4.326  25.679  8.523  1.00 22.93 ? 57  THR B CG2 1 
ATOM   1414 N N   . ILE B 1 38  ? -3.451  24.823  11.572 1.00 21.90 ? 58  ILE B N   1 
ATOM   1415 C CA  . ILE B 1 38  ? -2.979  25.752  12.588 1.00 22.69 ? 58  ILE B CA  1 
ATOM   1416 C C   . ILE B 1 38  ? -2.017  26.791  12.038 1.00 22.62 ? 58  ILE B C   1 
ATOM   1417 O O   . ILE B 1 38  ? -1.700  27.758  12.749 1.00 23.99 ? 58  ILE B O   1 
ATOM   1418 C CB  . ILE B 1 38  ? -2.330  25.020  13.785 1.00 28.68 ? 58  ILE B CB  1 
ATOM   1419 C CG1 . ILE B 1 38  ? -1.018  24.345  13.369 1.00 23.45 ? 58  ILE B CG1 1 
ATOM   1420 C CG2 . ILE B 1 38  ? -3.294  23.997  14.344 1.00 29.85 ? 58  ILE B CG2 1 
ATOM   1421 C CD1 . ILE B 1 38  ? -0.221  23.811  14.556 1.00 28.22 ? 58  ILE B CD1 1 
ATOM   1422 N N   . LYS B 1 39  ? -1.545  26.631  10.805 1.00 23.08 ? 59  LYS B N   1 
ATOM   1423 C CA  . LYS B 1 39  ? -0.660  27.598  10.176 1.00 25.88 ? 59  LYS B CA  1 
ATOM   1424 C C   . LYS B 1 39  ? -0.990  27.662  8.693  1.00 21.18 ? 59  LYS B C   1 
ATOM   1425 O O   . LYS B 1 39  ? -1.059  26.628  8.023  1.00 23.00 ? 59  LYS B O   1 
ATOM   1426 C CB  . LYS B 1 39  ? 0.809   27.219  10.386 1.00 28.49 ? 59  LYS B CB  1 
ATOM   1427 C CG  . LYS B 1 39  ? 1.813   28.207  9.822  1.00 31.39 ? 59  LYS B CG  1 
ATOM   1428 C CD  . LYS B 1 39  ? 3.174   28.033  10.477 1.00 43.86 ? 59  LYS B CD  1 
ATOM   1429 C CE  . LYS B 1 39  ? 3.743   26.653  10.197 1.00 52.96 ? 59  LYS B CE  1 
ATOM   1430 N NZ  . LYS B 1 39  ? 3.736   26.342  8.741  1.00 54.38 ? 59  LYS B NZ  1 
ATOM   1431 N N   . TYR B 1 40  ? -1.213  28.873  8.190  1.00 22.19 ? 60  TYR B N   1 
ATOM   1432 C CA  . TYR B 1 40  ? -1.505  29.046  6.779  1.00 22.12 ? 60  TYR B CA  1 
ATOM   1433 C C   . TYR B 1 40  ? -0.248  28.788  5.946  1.00 22.71 ? 60  TYR B C   1 
ATOM   1434 O O   . TYR B 1 40  ? 0.869   28.798  6.469  1.00 23.31 ? 60  TYR B O   1 
ATOM   1435 C CB  . TYR B 1 40  ? -2.052  30.453  6.539  1.00 22.90 ? 60  TYR B CB  1 
ATOM   1436 C CG  . TYR B 1 40  ? -3.280  30.751  7.365  1.00 19.98 ? 60  TYR B CG  1 
ATOM   1437 C CD1 . TYR B 1 40  ? -4.432  29.980  7.236  1.00 24.55 ? 60  TYR B CD1 1 
ATOM   1438 C CD2 . TYR B 1 40  ? -3.287  31.786  8.293  1.00 21.54 ? 60  TYR B CD2 1 
ATOM   1439 C CE1 . TYR B 1 40  ? -5.560  30.239  7.995  1.00 22.80 ? 60  TYR B CE1 1 
ATOM   1440 C CE2 . TYR B 1 40  ? -4.407  32.052  9.063  1.00 25.19 ? 60  TYR B CE2 1 
ATOM   1441 C CZ  . TYR B 1 40  ? -5.541  31.281  8.913  1.00 23.90 ? 60  TYR B CZ  1 
ATOM   1442 O OH  . TYR B 1 40  ? -6.652  31.541  9.689  1.00 25.69 ? 60  TYR B OH  1 
ATOM   1443 N N   . PRO B 1 41  ? -0.404  28.542  4.640  1.00 21.77 ? 61  PRO B N   1 
ATOM   1444 C CA  . PRO B 1 41  ? 0.774   28.214  3.819  1.00 23.69 ? 61  PRO B CA  1 
ATOM   1445 C C   . PRO B 1 41  ? 1.786   29.344  3.708  1.00 23.14 ? 61  PRO B C   1 
ATOM   1446 O O   . PRO B 1 41  ? 2.925   29.088  3.297  1.00 27.01 ? 61  PRO B O   1 
ATOM   1447 C CB  . PRO B 1 41  ? 0.170   27.864  2.449  1.00 23.14 ? 61  PRO B CB  1 
ATOM   1448 C CG  . PRO B 1 41  ? -1.269  27.533  2.724  1.00 23.32 ? 61  PRO B CG  1 
ATOM   1449 C CD  . PRO B 1 41  ? -1.662  28.399  3.890  1.00 21.22 ? 61  PRO B CD  1 
ATOM   1450 N N   . ASN B 1 42  ? 1.425   30.578  4.055  1.00 24.58 ? 62  ASN B N   1 
ATOM   1451 C CA  . ASN B 1 42  ? 2.379   31.677  4.053  1.00 27.00 ? 62  ASN B CA  1 
ATOM   1452 C C   . ASN B 1 42  ? 3.143   31.789  5.365  1.00 26.21 ? 62  ASN B C   1 
ATOM   1453 O O   . ASN B 1 42  ? 3.912   32.740  5.546  1.00 27.16 ? 62  ASN B O   1 
ATOM   1454 C CB  . ASN B 1 42  ? 1.670   33.004  3.737  1.00 24.96 ? 62  ASN B CB  1 
ATOM   1455 C CG  . ASN B 1 42  ? 0.625   33.370  4.766  1.00 25.01 ? 62  ASN B CG  1 
ATOM   1456 O OD1 . ASN B 1 42  ? 0.356   32.606  5.699  1.00 22.85 ? 62  ASN B OD1 1 
ATOM   1457 N ND2 . ASN B 1 42  ? 0.041   34.558  4.622  1.00 24.18 ? 62  ASN B ND2 1 
ATOM   1458 N N   . GLY B 1 43  ? 2.944   30.844  6.285  1.00 24.50 ? 63  GLY B N   1 
ATOM   1459 C CA  . GLY B 1 43  ? 3.623   30.860  7.564  1.00 25.41 ? 63  GLY B CA  1 
ATOM   1460 C C   . GLY B 1 43  ? 2.882   31.551  8.690  1.00 27.52 ? 63  GLY B C   1 
ATOM   1461 O O   . GLY B 1 43  ? 3.324   31.465  9.846  1.00 30.48 ? 63  GLY B O   1 
ATOM   1462 N N   . VAL B 1 44  ? 1.775   32.225  8.403  1.00 24.35 ? 64  VAL B N   1 
ATOM   1463 C CA  . VAL B 1 44  ? 1.041   32.966  9.425  1.00 26.07 ? 64  VAL B CA  1 
ATOM   1464 C C   . VAL B 1 44  ? 0.251   31.980  10.278 1.00 23.23 ? 64  VAL B C   1 
ATOM   1465 O O   . VAL B 1 44  ? -0.442  31.103  9.754  1.00 23.37 ? 64  VAL B O   1 
ATOM   1466 C CB  . VAL B 1 44  ? 0.119   34.009  8.771  1.00 25.67 ? 64  VAL B CB  1 
ATOM   1467 C CG1 . VAL B 1 44  ? -0.796  34.661  9.811  1.00 27.61 ? 64  VAL B CG1 1 
ATOM   1468 C CG2 . VAL B 1 44  ? 0.948   35.058  8.044  1.00 26.97 ? 64  VAL B CG2 1 
ATOM   1469 N N   . ARG B 1 45  ? 0.355   32.111  11.597 1.00 25.47 ? 65  ARG B N   1 
ATOM   1470 C CA  . ARG B 1 45  ? -0.371  31.204  12.473 1.00 24.37 ? 65  ARG B CA  1 
ATOM   1471 C C   . ARG B 1 45  ? -1.842  31.588  12.562 1.00 26.06 ? 65  ARG B C   1 
ATOM   1472 O O   . ARG B 1 45  ? -2.194  32.772  12.590 1.00 26.54 ? 65  ARG B O   1 
ATOM   1473 C CB  . ARG B 1 45  ? 0.243   31.186  13.874 1.00 30.39 ? 65  ARG B CB  1 
ATOM   1474 C CG  . ARG B 1 45  ? 1.678   30.685  13.920 1.00 36.63 ? 65  ARG B CG  1 
ATOM   1475 C CD  . ARG B 1 45  ? 1.747   29.158  14.000 1.00 46.01 ? 65  ARG B CD  1 
ATOM   1476 N NE  . ARG B 1 45  ? 0.777   28.589  14.932 1.00 52.11 ? 65  ARG B NE  1 
ATOM   1477 C CZ  . ARG B 1 45  ? 1.094   27.881  16.008 1.00 54.74 ? 65  ARG B CZ  1 
ATOM   1478 N NH1 . ARG B 1 45  ? 2.354   27.627  16.323 1.00 57.11 ? 65  ARG B NH1 1 
ATOM   1479 N NH2 . ARG B 1 45  ? 0.122   27.419  16.791 1.00 55.14 ? 65  ARG B NH2 1 
ATOM   1480 N N   . VAL B 1 46  ? -2.699  30.566  12.598 1.00 23.80 ? 66  VAL B N   1 
ATOM   1481 C CA  . VAL B 1 46  ? -4.120  30.765  12.858 1.00 22.79 ? 66  VAL B CA  1 
ATOM   1482 C C   . VAL B 1 46  ? -4.298  31.418  14.221 1.00 24.93 ? 66  VAL B C   1 
ATOM   1483 O O   . VAL B 1 46  ? -3.574  31.113  15.181 1.00 25.38 ? 66  VAL B O   1 
ATOM   1484 C CB  . VAL B 1 46  ? -4.858  29.415  12.785 1.00 22.34 ? 66  VAL B CB  1 
ATOM   1485 C CG1 . VAL B 1 46  ? -6.335  29.564  13.144 1.00 26.41 ? 66  VAL B CG1 1 
ATOM   1486 C CG2 . VAL B 1 46  ? -4.722  28.807  11.390 1.00 22.45 ? 66  VAL B CG2 1 
ATOM   1487 N N   . LYS B 1 47  ? -5.251  32.345  14.311 1.00 27.86 ? 67  LYS B N   1 
ATOM   1488 C CA  . LYS B 1 47  ? -5.515  33.025  15.571 1.00 26.27 ? 67  LYS B CA  1 
ATOM   1489 C C   . LYS B 1 47  ? -7.015  33.175  15.782 1.00 25.86 ? 67  LYS B C   1 
ATOM   1490 O O   . LYS B 1 47  ? -7.815  33.056  14.850 1.00 29.52 ? 67  LYS B O   1 
ATOM   1491 C CB  . LYS B 1 47  ? -4.835  34.400  15.625 1.00 31.43 ? 67  LYS B CB  1 
ATOM   1492 C CG  . LYS B 1 47  ? -5.372  35.375  14.617 1.00 35.46 ? 67  LYS B CG  1 
ATOM   1493 C CD  . LYS B 1 47  ? -4.586  36.672  14.634 1.00 40.41 ? 67  LYS B CD  1 
ATOM   1494 C CE  . LYS B 1 47  ? -5.365  37.772  13.947 1.00 45.59 ? 67  LYS B CE  1 
ATOM   1495 N NZ  . LYS B 1 47  ? -5.336  37.592  12.465 1.00 41.20 ? 67  LYS B NZ  1 
ATOM   1496 N N   . LYS B 1 48  ? -7.378  33.455  17.035 1.00 27.62 ? 68  LYS B N   1 
ATOM   1497 C CA  . LYS B 1 48  ? -8.769  33.684  17.398 1.00 28.91 ? 68  LYS B CA  1 
ATOM   1498 C C   . LYS B 1 48  ? -9.377  34.798  16.553 1.00 32.35 ? 68  LYS B C   1 
ATOM   1499 O O   . LYS B 1 48  ? -8.757  35.844  16.332 1.00 33.05 ? 68  LYS B O   1 
ATOM   1500 C CB  . LYS B 1 48  ? -8.861  34.044  18.882 1.00 30.18 ? 68  LYS B CB  1 
ATOM   1501 C CG  . LYS B 1 48  ? -10.239 34.491  19.333 1.00 36.25 ? 68  LYS B CG  1 
ATOM   1502 C CD  . LYS B 1 48  ? -10.285 34.694  20.844 1.00 41.54 ? 68  LYS B CD  1 
ATOM   1503 C CE  . LYS B 1 48  ? -11.653 35.184  21.294 1.00 48.85 ? 68  LYS B CE  1 
ATOM   1504 N NZ  . LYS B 1 48  ? -11.999 34.706  22.659 1.00 58.00 ? 68  LYS B NZ  1 
ATOM   1505 N N   . GLY B 1 49  ? -10.602 34.570  16.078 1.00 34.69 ? 69  GLY B N   1 
ATOM   1506 C CA  . GLY B 1 49  ? -11.284 35.522  15.230 1.00 34.26 ? 69  GLY B CA  1 
ATOM   1507 C C   . GLY B 1 49  ? -11.098 35.300  13.745 1.00 34.97 ? 69  GLY B C   1 
ATOM   1508 O O   . GLY B 1 49  ? -11.791 35.945  12.945 1.00 37.34 ? 69  GLY B O   1 
ATOM   1509 N N   . ASP B 1 50  ? -10.185 34.417  13.350 1.00 31.25 ? 70  ASP B N   1 
ATOM   1510 C CA  . ASP B 1 50  ? -10.006 34.113  11.940 1.00 28.85 ? 70  ASP B CA  1 
ATOM   1511 C C   . ASP B 1 50  ? -11.238 33.399  11.392 1.00 27.66 ? 70  ASP B C   1 
ATOM   1512 O O   . ASP B 1 50  ? -11.904 32.633  12.091 1.00 32.14 ? 70  ASP B O   1 
ATOM   1513 C CB  . ASP B 1 50  ? -8.770  33.236  11.730 1.00 29.44 ? 70  ASP B CB  1 
ATOM   1514 C CG  . ASP B 1 50  ? -7.472  34.010  11.828 1.00 31.68 ? 70  ASP B CG  1 
ATOM   1515 O OD1 . ASP B 1 50  ? -7.510  35.250  12.014 1.00 29.93 ? 70  ASP B OD1 1 
ATOM   1516 O OD2 . ASP B 1 50  ? -6.402  33.373  11.703 1.00 27.59 ? 70  ASP B OD2 1 
ATOM   1517 N N   . THR B 1 51  ? -11.546 33.671  10.128 1.00 28.97 ? 71  THR B N   1 
ATOM   1518 C CA  . THR B 1 51  ? -12.574 32.946  9.399  1.00 29.59 ? 71  THR B CA  1 
ATOM   1519 C C   . THR B 1 51  ? -11.995 32.523  8.059  1.00 28.73 ? 71  THR B C   1 
ATOM   1520 O O   . THR B 1 51  ? -11.052 33.137  7.555  1.00 31.32 ? 71  THR B O   1 
ATOM   1521 C CB  . THR B 1 51  ? -13.838 33.790  9.171  1.00 35.88 ? 71  THR B CB  1 
ATOM   1522 O OG1 . THR B 1 51  ? -13.539 34.863  8.269  1.00 39.53 ? 71  THR B OG1 1 
ATOM   1523 C CG2 . THR B 1 51  ? -14.358 34.358  10.484 1.00 35.59 ? 71  THR B CG2 1 
ATOM   1524 N N   . CYS B 1 52  ? -12.565 31.466  7.479  1.00 31.12 ? 72  CYS B N   1 
ATOM   1525 C CA  . CYS B 1 52  ? -12.149 31.042  6.149  1.00 29.52 ? 72  CYS B CA  1 
ATOM   1526 C C   . CYS B 1 52  ? -13.334 30.446  5.400  1.00 33.75 ? 72  CYS B C   1 
ATOM   1527 O O   . CYS B 1 52  ? -14.378 30.139  5.978  1.00 33.04 ? 72  CYS B O   1 
ATOM   1528 C CB  . CYS B 1 52  ? -10.992 30.037  6.209  1.00 26.72 ? 72  CYS B CB  1 
ATOM   1529 S SG  . CYS B 1 52  ? -11.422 28.378  6.814  1.00 30.31 ? 72  CYS B SG  1 
ATOM   1530 N N   . THR B 1 53  ? -13.160 30.295  4.091  1.00 29.70 ? 73  THR B N   1 
ATOM   1531 C CA  . THR B 1 53  ? -14.144 29.642  3.243  1.00 32.97 ? 73  THR B CA  1 
ATOM   1532 C C   . THR B 1 53  ? -13.853 28.146  3.166  1.00 30.48 ? 73  THR B C   1 
ATOM   1533 O O   . THR B 1 53  ? -12.785 27.676  3.561  1.00 28.69 ? 73  THR B O   1 
ATOM   1534 C CB  . THR B 1 53  ? -14.136 30.243  1.838  1.00 29.81 ? 73  THR B CB  1 
ATOM   1535 O OG1 . THR B 1 53  ? -12.880 29.961  1.213  1.00 31.47 ? 73  THR B OG1 1 
ATOM   1536 C CG2 . THR B 1 53  ? -14.349 31.756  1.892  1.00 29.29 ? 73  THR B CG2 1 
ATOM   1537 N N   . GLU B 1 54  ? -14.821 27.395  2.634  1.00 33.75 ? 74  GLU B N   1 
ATOM   1538 C CA  . GLU B 1 54  ? -14.620 25.962  2.432  1.00 35.57 ? 74  GLU B CA  1 
ATOM   1539 C C   . GLU B 1 54  ? -13.455 25.692  1.488  1.00 28.54 ? 74  GLU B C   1 
ATOM   1540 O O   . GLU B 1 54  ? -12.630 24.804  1.739  1.00 29.71 ? 74  GLU B O   1 
ATOM   1541 C CB  . GLU B 1 54  ? -15.893 25.321  1.879  1.00 42.75 ? 74  GLU B CB  1 
ATOM   1542 C CG  . GLU B 1 54  ? -15.794 23.811  1.745  1.00 54.81 ? 74  GLU B CG  1 
ATOM   1543 C CD  . GLU B 1 54  ? -17.014 23.095  2.281  1.00 62.53 ? 74  GLU B CD  1 
ATOM   1544 O OE1 . GLU B 1 54  ? -17.885 23.766  2.869  1.00 65.64 ? 74  GLU B OE1 1 
ATOM   1545 O OE2 . GLU B 1 54  ? -17.093 21.858  2.126  1.00 63.89 ? 74  GLU B OE2 1 
ATOM   1546 N N   . GLN B 1 55  ? -13.388 26.435  0.380  1.00 32.08 ? 75  GLN B N   1 
ATOM   1547 C CA  . GLN B 1 55  ? -12.305 26.238  -0.578 1.00 31.13 ? 75  GLN B CA  1 
ATOM   1548 C C   . GLN B 1 55  ? -10.955 26.529  0.065  1.00 29.22 ? 75  GLN B C   1 
ATOM   1549 O O   . GLN B 1 55  ? -9.982  25.793  -0.146 1.00 28.40 ? 75  GLN B O   1 
ATOM   1550 C CB  . GLN B 1 55  ? -12.520 27.137  -1.796 1.00 32.67 ? 75  GLN B CB  1 
ATOM   1551 C CG  . GLN B 1 55  ? -11.381 27.125  -2.807 1.00 40.94 ? 75  GLN B CG  1 
ATOM   1552 C CD  . GLN B 1 55  ? -11.018 25.727  -3.283 1.00 53.73 ? 75  GLN B CD  1 
ATOM   1553 O OE1 . GLN B 1 55  ? -9.996  25.160  -2.886 1.00 50.84 ? 75  GLN B OE1 1 
ATOM   1554 N NE2 . GLN B 1 55  ? -11.849 25.172  -4.157 1.00 56.75 ? 75  GLN B NE2 1 
ATOM   1555 N N   . GLN B 1 56  ? -10.881 27.602  0.856  1.00 26.55 ? 76  GLN B N   1 
ATOM   1556 C CA  . GLN B 1 56  ? -9.642  27.921  1.555  1.00 24.91 ? 76  GLN B CA  1 
ATOM   1557 C C   . GLN B 1 56  ? -9.256  26.797  2.507  1.00 28.50 ? 76  GLN B C   1 
ATOM   1558 O O   . GLN B 1 56  ? -8.090  26.394  2.565  1.00 24.04 ? 76  GLN B O   1 
ATOM   1559 C CB  . GLN B 1 56  ? -9.787  29.241  2.313  1.00 22.67 ? 76  GLN B CB  1 
ATOM   1560 C CG  . GLN B 1 56  ? -9.608  30.483  1.448  1.00 26.07 ? 76  GLN B CG  1 
ATOM   1561 C CD  . GLN B 1 56  ? -10.327 31.687  2.024  1.00 26.43 ? 76  GLN B CD  1 
ATOM   1562 O OE1 . GLN B 1 56  ? -10.696 31.700  3.195  1.00 28.01 ? 76  GLN B OE1 1 
ATOM   1563 N NE2 . GLN B 1 56  ? -10.517 32.717  1.203  1.00 28.20 ? 76  GLN B NE2 1 
ATOM   1564 N N   . ALA B 1 57  ? -10.231 26.278  3.258  1.00 26.38 ? 77  ALA B N   1 
ATOM   1565 C CA  . ALA B 1 57  ? -9.961  25.180  4.182  1.00 25.26 ? 77  ALA B CA  1 
ATOM   1566 C C   . ALA B 1 57  ? -9.414  23.959  3.451  1.00 26.59 ? 77  ALA B C   1 
ATOM   1567 O O   . ALA B 1 57  ? -8.474  23.311  3.927  1.00 25.38 ? 77  ALA B O   1 
ATOM   1568 C CB  . ALA B 1 57  ? -11.233 24.826  4.952  1.00 25.46 ? 77  ALA B CB  1 
ATOM   1569 N N   . GLU B 1 58  ? -9.981  23.629  2.291  1.00 26.75 ? 78  GLU B N   1 
ATOM   1570 C CA  . GLU B 1 58  ? -9.462  22.482  1.552  1.00 29.35 ? 78  GLU B CA  1 
ATOM   1571 C C   . GLU B 1 58  ? -8.048  22.747  1.047  1.00 24.40 ? 78  GLU B C   1 
ATOM   1572 O O   . GLU B 1 58  ? -7.187  21.862  1.101  1.00 24.87 ? 78  GLU B O   1 
ATOM   1573 C CB  . GLU B 1 58  ? -10.393 22.118  0.396  1.00 27.08 ? 78  GLU B CB  1 
ATOM   1574 C CG  . GLU B 1 58  ? -9.904  20.900  -0.382 1.00 35.57 ? 78  GLU B CG  1 
ATOM   1575 C CD  . GLU B 1 58  ? -10.752 20.587  -1.594 1.00 51.20 ? 78  GLU B CD  1 
ATOM   1576 O OE1 . GLU B 1 58  ? -11.806 19.935  -1.428 1.00 53.91 ? 78  GLU B OE1 1 
ATOM   1577 O OE2 . GLU B 1 58  ? -10.359 20.977  -2.713 1.00 64.10 ? 78  GLU B OE2 1 
ATOM   1578 N N   . THR B 1 59  ? -7.783  23.964  0.560  1.00 24.28 ? 79  THR B N   1 
ATOM   1579 C CA  . THR B 1 59  ? -6.426  24.289  0.130  1.00 22.41 ? 79  THR B CA  1 
ATOM   1580 C C   . THR B 1 59  ? -5.435  24.165  1.279  1.00 22.34 ? 79  THR B C   1 
ATOM   1581 O O   . THR B 1 59  ? -4.321  23.652  1.103  1.00 22.57 ? 79  THR B O   1 
ATOM   1582 C CB  . THR B 1 59  ? -6.385  25.703  -0.444 1.00 24.27 ? 79  THR B CB  1 
ATOM   1583 O OG1 . THR B 1 59  ? -7.314  25.795  -1.528 1.00 27.83 ? 79  THR B OG1 1 
ATOM   1584 C CG2 . THR B 1 59  ? -4.990  26.028  -0.940 1.00 24.22 ? 79  THR B CG2 1 
ATOM   1585 N N   . TYR B 1 60  ? -5.826  24.642  2.465  1.00 23.18 ? 80  TYR B N   1 
ATOM   1586 C CA  . TYR B 1 60  ? -4.951  24.591  3.630  1.00 22.68 ? 80  TYR B CA  1 
ATOM   1587 C C   . TYR B 1 60  ? -4.693  23.153  4.057  1.00 22.68 ? 80  TYR B C   1 
ATOM   1588 O O   . TYR B 1 60  ? -3.565  22.811  4.412  1.00 22.52 ? 80  TYR B O   1 
ATOM   1589 C CB  . TYR B 1 60  ? -5.551  25.392  4.787  1.00 22.75 ? 80  TYR B CB  1 
ATOM   1590 C CG  . TYR B 1 60  ? -5.758  26.862  4.493  1.00 22.80 ? 80  TYR B CG  1 
ATOM   1591 C CD1 . TYR B 1 60  ? -4.999  27.509  3.529  1.00 21.79 ? 80  TYR B CD1 1 
ATOM   1592 C CD2 . TYR B 1 60  ? -6.704  27.603  5.193  1.00 23.58 ? 80  TYR B CD2 1 
ATOM   1593 C CE1 . TYR B 1 60  ? -5.179  28.868  3.265  1.00 23.88 ? 80  TYR B CE1 1 
ATOM   1594 C CE2 . TYR B 1 60  ? -6.898  28.960  4.924  1.00 22.95 ? 80  TYR B CE2 1 
ATOM   1595 C CZ  . TYR B 1 60  ? -6.132  29.571  3.965  1.00 22.92 ? 80  TYR B CZ  1 
ATOM   1596 O OH  . TYR B 1 60  ? -6.331  30.920  3.712  1.00 25.31 ? 80  TYR B OH  1 
ATOM   1597 N N   . LEU B 1 61  ? -5.723  22.303  4.018  1.00 23.68 ? 81  LEU B N   1 
ATOM   1598 C CA  . LEU B 1 61  ? -5.538  20.884  4.315  1.00 25.61 ? 81  LEU B CA  1 
ATOM   1599 C C   . LEU B 1 61  ? -4.565  20.245  3.333  1.00 25.04 ? 81  LEU B C   1 
ATOM   1600 O O   . LEU B 1 61  ? -3.646  19.515  3.733  1.00 24.36 ? 81  LEU B O   1 
ATOM   1601 C CB  . LEU B 1 61  ? -6.885  20.166  4.272  1.00 23.53 ? 81  LEU B CB  1 
ATOM   1602 C CG  . LEU B 1 61  ? -6.837  18.630  4.367  1.00 24.20 ? 81  LEU B CG  1 
ATOM   1603 C CD1 . LEU B 1 61  ? -6.132  18.211  5.650  1.00 28.43 ? 81  LEU B CD1 1 
ATOM   1604 C CD2 . LEU B 1 61  ? -8.242  18.061  4.289  1.00 25.90 ? 81  LEU B CD2 1 
ATOM   1605 N N   . LYS B 1 62  ? -4.758  20.508  2.036  1.00 22.65 ? 82  LYS B N   1 
ATOM   1606 C CA  . LYS B 1 62  ? -3.853  19.960  1.032  1.00 22.13 ? 82  LYS B CA  1 
ATOM   1607 C C   . LYS B 1 62  ? -2.420  20.395  1.307  1.00 24.68 ? 82  LYS B C   1 
ATOM   1608 O O   . LYS B 1 62  ? -1.484  19.600  1.177  1.00 25.05 ? 82  LYS B O   1 
ATOM   1609 C CB  . LYS B 1 62  ? -4.294  20.393  -0.370 1.00 22.97 ? 82  LYS B CB  1 
ATOM   1610 C CG  . LYS B 1 62  ? -5.506  19.644  -0.898 1.00 26.39 ? 82  LYS B CG  1 
ATOM   1611 C CD  . LYS B 1 62  ? -5.989  20.208  -2.241 1.00 27.92 ? 82  LYS B CD  1 
ATOM   1612 C CE  . LYS B 1 62  ? -6.420  19.104  -3.189 1.00 49.11 ? 82  LYS B CE  1 
ATOM   1613 N NZ  . LYS B 1 62  ? -5.251  18.414  -3.802 1.00 44.88 ? 82  LYS B NZ  1 
ATOM   1614 N N   . ASN B 1 63  ? -2.231  21.653  1.715  1.00 21.03 ? 83  ASN B N   1 
ATOM   1615 C CA  . ASN B 1 63  ? -0.891  22.111  2.067  1.00 21.95 ? 83  ASN B CA  1 
ATOM   1616 C C   . ASN B 1 63  ? -0.362  21.394  3.306  1.00 25.43 ? 83  ASN B C   1 
ATOM   1617 O O   . ASN B 1 63  ? 0.817   21.030  3.357  1.00 26.59 ? 83  ASN B O   1 
ATOM   1618 C CB  . ASN B 1 63  ? -0.894  23.627  2.295  1.00 21.91 ? 83  ASN B CB  1 
ATOM   1619 C CG  . ASN B 1 63  ? 0.488   24.170  2.601  1.00 27.08 ? 83  ASN B CG  1 
ATOM   1620 O OD1 . ASN B 1 63  ? 0.724   24.718  3.681  1.00 32.99 ? 83  ASN B OD1 1 
ATOM   1621 N ND2 . ASN B 1 63  ? 1.407   24.027  1.655  1.00 27.57 ? 83  ASN B ND2 1 
ATOM   1622 N N   . ASP B 1 64  ? -1.210  21.209  4.323  1.00 23.02 ? 84  ASP B N   1 
ATOM   1623 C CA  . ASP B 1 64  ? -0.754  20.555  5.547  1.00 23.53 ? 84  ASP B CA  1 
ATOM   1624 C C   . ASP B 1 64  ? -0.306  19.131  5.269  1.00 25.82 ? 84  ASP B C   1 
ATOM   1625 O O   . ASP B 1 64  ? 0.568   18.605  5.967  1.00 25.19 ? 84  ASP B O   1 
ATOM   1626 C CB  . ASP B 1 64  ? -1.846  20.534  6.619  1.00 22.99 ? 84  ASP B CB  1 
ATOM   1627 C CG  . ASP B 1 64  ? -2.262  21.916  7.078  1.00 30.95 ? 84  ASP B CG  1 
ATOM   1628 O OD1 . ASP B 1 64  ? -1.379  22.782  7.201  1.00 28.23 ? 84  ASP B OD1 1 
ATOM   1629 O OD2 . ASP B 1 64  ? -3.444  22.083  7.453  1.00 26.48 ? 84  ASP B OD2 1 
ATOM   1630 N N   . LEU B 1 65  ? -0.897  18.495  4.260  1.00 24.48 ? 85  LEU B N   1 
ATOM   1631 C CA  . LEU B 1 65  ? -0.575  17.103  3.960  1.00 25.09 ? 85  LEU B CA  1 
ATOM   1632 C C   . LEU B 1 65  ? 0.770   16.918  3.263  1.00 29.59 ? 85  LEU B C   1 
ATOM   1633 O O   . LEU B 1 65  ? 1.310   15.808  3.297  1.00 26.80 ? 85  LEU B O   1 
ATOM   1634 C CB  . LEU B 1 65  ? -1.678  16.486  3.097  1.00 23.60 ? 85  LEU B CB  1 
ATOM   1635 C CG  . LEU B 1 65  ? -2.895  16.026  3.899  1.00 26.61 ? 85  LEU B CG  1 
ATOM   1636 C CD1 . LEU B 1 65  ? -4.088  15.827  3.000  1.00 24.04 ? 85  LEU B CD1 1 
ATOM   1637 C CD2 . LEU B 1 65  ? -2.567  14.728  4.638  1.00 29.55 ? 85  LEU B CD2 1 
ATOM   1638 N N   . THR B 1 66  ? 1.327   17.970  2.655  1.00 24.58 ? 86  THR B N   1 
ATOM   1639 C CA  . THR B 1 66  ? 2.464   17.812  1.750  1.00 27.17 ? 86  THR B CA  1 
ATOM   1640 C C   . THR B 1 66  ? 3.671   17.150  2.419  1.00 28.60 ? 86  THR B C   1 
ATOM   1641 O O   . THR B 1 66  ? 4.308   16.271  1.828  1.00 27.63 ? 86  THR B O   1 
ATOM   1642 C CB  . THR B 1 66  ? 2.847   19.174  1.165  1.00 28.84 ? 86  THR B CB  1 
ATOM   1643 O OG1 . THR B 1 66  ? 1.735   19.692  0.424  1.00 31.89 ? 86  THR B OG1 1 
ATOM   1644 C CG2 . THR B 1 66  ? 4.042   19.037  0.236  1.00 34.26 ? 86  THR B CG2 1 
ATOM   1645 N N   . LYS B 1 67  ? 4.013   17.562  3.646  1.00 26.55 ? 87  LYS B N   1 
ATOM   1646 C CA  . LYS B 1 67  ? 5.187   16.980  4.297  1.00 26.57 ? 87  LYS B CA  1 
ATOM   1647 C C   . LYS B 1 67  ? 4.990   15.493  4.575  1.00 27.39 ? 87  LYS B C   1 
ATOM   1648 O O   . LYS B 1 67  ? 5.934   14.703  4.449  1.00 29.94 ? 87  LYS B O   1 
ATOM   1649 C CB  . LYS B 1 67  ? 5.515   17.727  5.594  1.00 29.35 ? 87  LYS B CB  1 
ATOM   1650 C CG  . LYS B 1 67  ? 4.447   17.640  6.674  1.00 26.87 ? 87  LYS B CG  1 
ATOM   1651 C CD  . LYS B 1 67  ? 4.641   18.701  7.760  1.00 38.64 ? 87  LYS B CD  1 
ATOM   1652 C CE  . LYS B 1 67  ? 5.830   18.425  8.661  1.00 43.26 ? 87  LYS B CE  1 
ATOM   1653 N NZ  . LYS B 1 67  ? 5.913   19.462  9.737  1.00 46.11 ? 87  LYS B NZ  1 
ATOM   1654 N N   . PHE B 1 68  ? 3.764   15.088  4.908  1.00 24.85 ? 88  PHE B N   1 
ATOM   1655 C CA  . PHE B 1 68  ? 3.494   13.679  5.166  1.00 25.19 ? 88  PHE B CA  1 
ATOM   1656 C C   . PHE B 1 68  ? 3.450   12.876  3.874  1.00 24.49 ? 88  PHE B C   1 
ATOM   1657 O O   . PHE B 1 68  ? 3.855   11.707  3.860  1.00 25.08 ? 88  PHE B O   1 
ATOM   1658 C CB  . PHE B 1 68  ? 2.183   13.541  5.936  1.00 25.24 ? 88  PHE B CB  1 
ATOM   1659 C CG  . PHE B 1 68  ? 2.146   14.356  7.193  1.00 28.40 ? 88  PHE B CG  1 
ATOM   1660 C CD1 . PHE B 1 68  ? 3.008   14.074  8.242  1.00 28.53 ? 88  PHE B CD1 1 
ATOM   1661 C CD2 . PHE B 1 68  ? 1.268   15.415  7.319  1.00 30.27 ? 88  PHE B CD2 1 
ATOM   1662 C CE1 . PHE B 1 68  ? 2.989   14.831  9.402  1.00 28.37 ? 88  PHE B CE1 1 
ATOM   1663 C CE2 . PHE B 1 68  ? 1.240   16.180  8.473  1.00 26.42 ? 88  PHE B CE2 1 
ATOM   1664 C CZ  . PHE B 1 68  ? 2.102   15.888  9.523  1.00 31.57 ? 88  PHE B CZ  1 
ATOM   1665 N N   . GLU B 1 69  ? 2.970   13.484  2.787  1.00 25.17 ? 89  GLU B N   1 
ATOM   1666 C CA  . GLU B 1 69  ? 3.040   12.829  1.482  1.00 25.82 ? 89  GLU B CA  1 
ATOM   1667 C C   . GLU B 1 69  ? 4.488   12.604  1.064  1.00 25.15 ? 89  GLU B C   1 
ATOM   1668 O O   . GLU B 1 69  ? 4.835   11.536  0.541  1.00 28.16 ? 89  GLU B O   1 
ATOM   1669 C CB  . GLU B 1 69  ? 2.310   13.663  0.428  1.00 27.02 ? 89  GLU B CB  1 
ATOM   1670 C CG  . GLU B 1 69  ? 0.828   13.850  0.676  1.00 24.96 ? 89  GLU B CG  1 
ATOM   1671 C CD  . GLU B 1 69  ? 0.226   14.940  -0.197 1.00 27.80 ? 89  GLU B CD  1 
ATOM   1672 O OE1 . GLU B 1 69  ? 0.997   15.667  -0.860 1.00 31.95 ? 89  GLU B OE1 1 
ATOM   1673 O OE2 . GLU B 1 69  ? -1.015  15.055  -0.220 1.00 28.63 ? 89  GLU B OE2 1 
ATOM   1674 N N   . VAL B 1 70  ? 5.342   13.609  1.272  1.00 28.61 ? 90  VAL B N   1 
ATOM   1675 C CA  . VAL B 1 70  ? 6.766   13.457  0.991  1.00 30.67 ? 90  VAL B CA  1 
ATOM   1676 C C   . VAL B 1 70  ? 7.340   12.299  1.798  1.00 27.43 ? 90  VAL B C   1 
ATOM   1677 O O   . VAL B 1 70  ? 8.075   11.452  1.269  1.00 32.39 ? 90  VAL B O   1 
ATOM   1678 C CB  . VAL B 1 70  ? 7.509   14.773  1.284  1.00 32.64 ? 90  VAL B CB  1 
ATOM   1679 C CG1 . VAL B 1 70  ? 9.013   14.559  1.238  1.00 36.50 ? 90  VAL B CG1 1 
ATOM   1680 C CG2 . VAL B 1 70  ? 7.084   15.849  0.296  1.00 33.12 ? 90  VAL B CG2 1 
ATOM   1681 N N   . ALA B 1 71  ? 7.003   12.247  3.093  1.00 28.44 ? 91  ALA B N   1 
ATOM   1682 C CA  . ALA B 1 71  ? 7.468   11.153  3.942  1.00 26.53 ? 91  ALA B CA  1 
ATOM   1683 C C   . ALA B 1 71  ? 7.020   9.794   3.404  1.00 30.96 ? 91  ALA B C   1 
ATOM   1684 O O   . ALA B 1 71  ? 7.809   8.845   3.361  1.00 28.71 ? 91  ALA B O   1 
ATOM   1685 C CB  . ALA B 1 71  ? 6.973   11.357  5.374  1.00 29.13 ? 91  ALA B CB  1 
ATOM   1686 N N   . ILE B 1 72  ? 5.754   9.678   2.995  1.00 25.65 ? 92  ILE B N   1 
ATOM   1687 C CA  . ILE B 1 72  ? 5.249   8.389   2.514  1.00 26.43 ? 92  ILE B CA  1 
ATOM   1688 C C   . ILE B 1 72  ? 5.965   7.974   1.236  1.00 27.94 ? 92  ILE B C   1 
ATOM   1689 O O   . ILE B 1 72  ? 6.358   6.807   1.073  1.00 25.13 ? 92  ILE B O   1 
ATOM   1690 C CB  . ILE B 1 72  ? 3.726   8.445   2.300  1.00 22.94 ? 92  ILE B CB  1 
ATOM   1691 C CG1 . ILE B 1 72  ? 2.997   8.602   3.633  1.00 27.38 ? 92  ILE B CG1 1 
ATOM   1692 C CG2 . ILE B 1 72  ? 3.244   7.181   1.597  1.00 24.31 ? 92  ILE B CG2 1 
ATOM   1693 C CD1 . ILE B 1 72  ? 1.567   9.061   3.476  1.00 26.56 ? 92  ILE B CD1 1 
ATOM   1694 N N   . ASN B 1 73  ? 6.137   8.915   0.305  1.00 28.52 ? 93  ASN B N   1 
ATOM   1695 C CA  . ASN B 1 73  ? 6.810   8.580   -0.944 1.00 30.78 ? 93  ASN B CA  1 
ATOM   1696 C C   . ASN B 1 73  ? 8.266   8.197   -0.707 1.00 31.21 ? 93  ASN B C   1 
ATOM   1697 O O   . ASN B 1 73  ? 8.814   7.367   -1.444 1.00 35.39 ? 93  ASN B O   1 
ATOM   1698 C CB  . ASN B 1 73  ? 6.706   9.745   -1.920 1.00 31.03 ? 93  ASN B CB  1 
ATOM   1699 C CG  . ASN B 1 73  ? 5.331   9.851   -2.551 1.00 37.79 ? 93  ASN B CG  1 
ATOM   1700 O OD1 . ASN B 1 73  ? 4.795   8.871   -3.068 1.00 38.40 ? 93  ASN B OD1 1 
ATOM   1701 N ND2 . ASN B 1 73  ? 4.752   11.046  -2.513 1.00 32.66 ? 93  ASN B ND2 1 
ATOM   1702 N N   . LYS B 1 74  ? 8.900   8.770   0.319  1.00 29.43 ? 94  LYS B N   1 
ATOM   1703 C CA  . LYS B 1 74  ? 10.279  8.397   0.629  1.00 33.81 ? 94  LYS B CA  1 
ATOM   1704 C C   . LYS B 1 74  ? 10.357  7.043   1.329  1.00 30.92 ? 94  LYS B C   1 
ATOM   1705 O O   . LYS B 1 74  ? 11.267  6.250   1.058  1.00 39.84 ? 94  LYS B O   1 
ATOM   1706 C CB  . LYS B 1 74  ? 10.934  9.473   1.495  1.00 34.93 ? 94  LYS B CB  1 
ATOM   1707 C CG  . LYS B 1 74  ? 11.690  10.532  0.704  1.00 51.68 ? 94  LYS B CG  1 
ATOM   1708 C CD  . LYS B 1 74  ? 11.519  11.907  1.334  1.00 54.02 ? 94  LYS B CD  1 
ATOM   1709 C CE  . LYS B 1 74  ? 12.687  12.826  1.006  1.00 60.75 ? 94  LYS B CE  1 
ATOM   1710 N NZ  . LYS B 1 74  ? 12.938  12.896  -0.459 1.00 54.94 ? 94  LYS B NZ  1 
ATOM   1711 N N   . LEU B 1 75  ? 9.416   6.760   2.233  1.00 26.31 ? 95  LEU B N   1 
ATOM   1712 C CA  . LEU B 1 75  ? 9.542   5.607   3.119  1.00 23.17 ? 95  LEU B CA  1 
ATOM   1713 C C   . LEU B 1 75  ? 9.031   4.314   2.500  1.00 27.86 ? 95  LEU B C   1 
ATOM   1714 O O   . LEU B 1 75  ? 9.557   3.242   2.818  1.00 26.67 ? 95  LEU B O   1 
ATOM   1715 C CB  . LEU B 1 75  ? 8.794   5.865   4.425  1.00 25.27 ? 95  LEU B CB  1 
ATOM   1716 C CG  . LEU B 1 75  ? 9.414   6.922   5.347  1.00 26.11 ? 95  LEU B CG  1 
ATOM   1717 C CD1 . LEU B 1 75  ? 8.430   7.333   6.430  1.00 26.91 ? 95  LEU B CD1 1 
ATOM   1718 C CD2 . LEU B 1 75  ? 10.684  6.364   5.965  1.00 29.02 ? 95  LEU B CD2 1 
ATOM   1719 N N   . VAL B 1 76  ? 8.008   4.378   1.653  1.00 27.12 ? 96  VAL B N   1 
ATOM   1720 C CA  . VAL B 1 76  ? 7.413   3.175   1.080  1.00 23.16 ? 96  VAL B CA  1 
ATOM   1721 C C   . VAL B 1 76  ? 8.206   2.781   -0.157 1.00 23.87 ? 96  VAL B C   1 
ATOM   1722 O O   . VAL B 1 76  ? 8.444   3.608   -1.046 1.00 26.54 ? 96  VAL B O   1 
ATOM   1723 C CB  . VAL B 1 76  ? 5.928   3.398   0.747  1.00 24.68 ? 96  VAL B CB  1 
ATOM   1724 C CG1 . VAL B 1 76  ? 5.351   2.173   0.034  1.00 24.25 ? 96  VAL B CG1 1 
ATOM   1725 C CG2 . VAL B 1 76  ? 5.142   3.687   2.017  1.00 25.52 ? 96  VAL B CG2 1 
ATOM   1726 N N   . LYS B 1 77  ? 8.602   1.508   -0.219 1.00 25.40 ? 97  LYS B N   1 
ATOM   1727 C CA  . LYS B 1 77  ? 9.493   1.004   -1.258 1.00 28.39 ? 97  LYS B CA  1 
ATOM   1728 C C   . LYS B 1 77  ? 8.822   -0.032  -2.149 1.00 31.58 ? 97  LYS B C   1 
ATOM   1729 O O   . LYS B 1 77  ? 9.510   -0.713  -2.919 1.00 36.25 ? 97  LYS B O   1 
ATOM   1730 C CB  . LYS B 1 77  ? 10.758  0.410   -0.627 1.00 35.33 ? 97  LYS B CB  1 
ATOM   1731 C CG  . LYS B 1 77  ? 11.520  1.407   0.235  1.00 34.09 ? 97  LYS B CG  1 
ATOM   1732 C CD  . LYS B 1 77  ? 11.970  2.588   -0.598 1.00 31.55 ? 97  LYS B CD  1 
ATOM   1733 C CE  . LYS B 1 77  ? 12.767  3.584   0.226  1.00 38.77 ? 97  LYS B CE  1 
ATOM   1734 N NZ  . LYS B 1 77  ? 13.162  4.765   -0.594 1.00 48.70 ? 97  LYS B NZ  1 
ATOM   1735 N N   . VAL B 1 78  ? 7.501   -0.176  -2.054 1.00 29.25 ? 98  VAL B N   1 
ATOM   1736 C CA  . VAL B 1 78  ? 6.723   -1.069  -2.901 1.00 25.68 ? 98  VAL B CA  1 
ATOM   1737 C C   . VAL B 1 78  ? 5.628   -0.245  -3.566 1.00 23.46 ? 98  VAL B C   1 
ATOM   1738 O O   . VAL B 1 78  ? 5.407   0.921   -3.235 1.00 25.73 ? 98  VAL B O   1 
ATOM   1739 C CB  . VAL B 1 78  ? 6.120   -2.247  -2.113 1.00 26.38 ? 98  VAL B CB  1 
ATOM   1740 C CG1 . VAL B 1 78  ? 7.230   -3.134  -1.562 1.00 26.41 ? 98  VAL B CG1 1 
ATOM   1741 C CG2 . VAL B 1 78  ? 5.238   -1.726  -0.980 1.00 24.57 ? 98  VAL B CG2 1 
ATOM   1742 N N   . SER B 1 79  ? 4.936   -0.865  -4.516 1.00 25.81 ? 99  SER B N   1 
ATOM   1743 C CA  . SER B 1 79  ? 3.876   -0.154  -5.211 1.00 25.68 ? 99  SER B CA  1 
ATOM   1744 C C   . SER B 1 79  ? 2.701   0.103   -4.270 1.00 26.92 ? 99  SER B C   1 
ATOM   1745 O O   . SER B 1 79  ? 2.442   -0.658  -3.331 1.00 24.59 ? 99  SER B O   1 
ATOM   1746 C CB  . SER B 1 79  ? 3.420   -0.938  -6.444 1.00 30.10 ? 99  SER B CB  1 
ATOM   1747 O OG  . SER B 1 79  ? 2.432   -1.890  -6.112 1.00 33.62 ? 99  SER B OG  1 
ATOM   1748 N N   . LEU B 1 80  ? 2.027   1.227   -4.497 1.00 26.43 ? 100 LEU B N   1 
ATOM   1749 C CA  . LEU B 1 80  ? 0.809   1.581   -3.785 1.00 22.81 ? 100 LEU B CA  1 
ATOM   1750 C C   . LEU B 1 80  ? -0.276  1.918   -4.794 1.00 22.28 ? 100 LEU B C   1 
ATOM   1751 O O   . LEU B 1 80  ? -0.038  2.666   -5.747 1.00 27.24 ? 100 LEU B O   1 
ATOM   1752 C CB  . LEU B 1 80  ? 1.018   2.791   -2.853 1.00 23.18 ? 100 LEU B CB  1 
ATOM   1753 C CG  . LEU B 1 80  ? 1.975   2.659   -1.667 1.00 22.55 ? 100 LEU B CG  1 
ATOM   1754 C CD1 . LEU B 1 80  ? 2.085   4.007   -0.958 1.00 25.32 ? 100 LEU B CD1 1 
ATOM   1755 C CD2 . LEU B 1 80  ? 1.505   1.609   -0.682 1.00 24.22 ? 100 LEU B CD2 1 
ATOM   1756 N N   . THR B 1 81  ? -1.466  1.374   -4.575 1.00 22.57 ? 101 THR B N   1 
ATOM   1757 C CA  . THR B 1 81  ? -2.634  1.927   -5.231 1.00 25.53 ? 101 THR B CA  1 
ATOM   1758 C C   . THR B 1 81  ? -2.922  3.298   -4.633 1.00 27.02 ? 101 THR B C   1 
ATOM   1759 O O   . THR B 1 81  ? -2.433  3.638   -3.551 1.00 23.94 ? 101 THR B O   1 
ATOM   1760 C CB  . THR B 1 81  ? -3.841  1.003   -5.061 1.00 26.78 ? 101 THR B CB  1 
ATOM   1761 O OG1 . THR B 1 81  ? -4.260  1.009   -3.691 1.00 25.68 ? 101 THR B OG1 1 
ATOM   1762 C CG2 . THR B 1 81  ? -3.484  -0.433  -5.453 1.00 27.65 ? 101 THR B CG2 1 
ATOM   1763 N N   . GLN B 1 82  ? -3.708  4.103   -5.350 1.00 24.55 ? 102 GLN B N   1 
ATOM   1764 C CA  . GLN B 1 82  ? -4.047  5.423   -4.819 1.00 22.14 ? 102 GLN B CA  1 
ATOM   1765 C C   . GLN B 1 82  ? -4.827  5.298   -3.514 1.00 26.18 ? 102 GLN B C   1 
ATOM   1766 O O   . GLN B 1 82  ? -4.648  6.105   -2.593 1.00 25.55 ? 102 GLN B O   1 
ATOM   1767 C CB  . GLN B 1 82  ? -4.841  6.229   -5.848 1.00 22.85 ? 102 GLN B CB  1 
ATOM   1768 C CG  . GLN B 1 82  ? -5.140  7.647   -5.396 1.00 25.30 ? 102 GLN B CG  1 
ATOM   1769 C CD  . GLN B 1 82  ? -3.885  8.492   -5.274 1.00 26.93 ? 102 GLN B CD  1 
ATOM   1770 O OE1 . GLN B 1 82  ? -3.073  8.553   -6.197 1.00 31.00 ? 102 GLN B OE1 1 
ATOM   1771 N NE2 . GLN B 1 82  ? -3.714  9.145   -4.120 1.00 23.88 ? 102 GLN B NE2 1 
ATOM   1772 N N   . ASN B 1 83  ? -5.681  4.278   -3.410 1.00 23.88 ? 103 ASN B N   1 
ATOM   1773 C CA  . ASN B 1 83  ? -6.391  4.012   -2.161 1.00 24.65 ? 103 ASN B CA  1 
ATOM   1774 C C   . ASN B 1 83  ? -5.417  3.763   -1.013 1.00 24.37 ? 103 ASN B C   1 
ATOM   1775 O O   . ASN B 1 83  ? -5.600  4.285   0.097  1.00 23.85 ? 103 ASN B O   1 
ATOM   1776 C CB  . ASN B 1 83  ? -7.315  2.806   -2.335 1.00 27.64 ? 103 ASN B CB  1 
ATOM   1777 C CG  . ASN B 1 83  ? -8.575  3.142   -3.108 1.00 28.18 ? 103 ASN B CG  1 
ATOM   1778 O OD1 . ASN B 1 83  ? -8.904  4.313   -3.305 1.00 33.39 ? 103 ASN B OD1 1 
ATOM   1779 N ND2 . ASN B 1 83  ? -9.285  2.110   -3.557 1.00 31.32 ? 103 ASN B ND2 1 
ATOM   1780 N N   . GLN B 1 84  ? -4.379  2.959   -1.263 1.00 22.89 ? 104 GLN B N   1 
ATOM   1781 C CA  . GLN B 1 84  ? -3.409  2.652   -0.213 1.00 22.20 ? 104 GLN B CA  1 
ATOM   1782 C C   . GLN B 1 84  ? -2.631  3.896   0.194  1.00 23.40 ? 104 GLN B C   1 
ATOM   1783 O O   . GLN B 1 84  ? -2.413  4.136   1.395  1.00 23.65 ? 104 GLN B O   1 
ATOM   1784 C CB  . GLN B 1 84  ? -2.468  1.544   -0.684 1.00 24.44 ? 104 GLN B CB  1 
ATOM   1785 C CG  . GLN B 1 84  ? -3.183  0.207   -0.796 1.00 24.51 ? 104 GLN B CG  1 
ATOM   1786 C CD  . GLN B 1 84  ? -2.351  -0.900  -1.423 1.00 23.74 ? 104 GLN B CD  1 
ATOM   1787 O OE1 . GLN B 1 84  ? -1.509  -0.661  -2.291 1.00 22.42 ? 104 GLN B OE1 1 
ATOM   1788 N NE2 . GLN B 1 84  ? -2.582  -2.119  -0.969 1.00 24.67 ? 104 GLN B NE2 1 
ATOM   1789 N N   . PHE B 1 85  ? -2.222  4.710   -0.787 1.00 23.52 ? 105 PHE B N   1 
ATOM   1790 C CA  . PHE B 1 85  ? -1.550  5.964   -0.468 1.00 21.98 ? 105 PHE B CA  1 
ATOM   1791 C C   . PHE B 1 85  ? -2.452  6.864   0.365  1.00 24.48 ? 105 PHE B C   1 
ATOM   1792 O O   . PHE B 1 85  ? -1.997  7.472   1.336  1.00 23.50 ? 105 PHE B O   1 
ATOM   1793 C CB  . PHE B 1 85  ? -1.113  6.689   -1.746 1.00 21.40 ? 105 PHE B CB  1 
ATOM   1794 C CG  . PHE B 1 85  ? -0.351  7.967   -1.477 1.00 22.10 ? 105 PHE B CG  1 
ATOM   1795 C CD1 . PHE B 1 85  ? -1.021  9.169   -1.285 1.00 25.92 ? 105 PHE B CD1 1 
ATOM   1796 C CD2 . PHE B 1 85  ? 1.031   7.956   -1.378 1.00 23.79 ? 105 PHE B CD2 1 
ATOM   1797 C CE1 . PHE B 1 85  ? -0.321  10.329  -1.012 1.00 24.08 ? 105 PHE B CE1 1 
ATOM   1798 C CE2 . PHE B 1 85  ? 1.735   9.117   -1.107 1.00 26.25 ? 105 PHE B CE2 1 
ATOM   1799 C CZ  . PHE B 1 85  ? 1.056   10.306  -0.928 1.00 24.76 ? 105 PHE B CZ  1 
ATOM   1800 N N   . ASP B 1 86  ? -3.735  6.952   0.006  1.00 22.38 ? 106 ASP B N   1 
ATOM   1801 C CA  . ASP B 1 86  ? -4.659  7.829   0.724  1.00 24.80 ? 106 ASP B CA  1 
ATOM   1802 C C   . ASP B 1 86  ? -4.846  7.366   2.166  1.00 24.66 ? 106 ASP B C   1 
ATOM   1803 O O   . ASP B 1 86  ? -4.880  8.187   3.096  1.00 24.43 ? 106 ASP B O   1 
ATOM   1804 C CB  . ASP B 1 86  ? -6.007  7.865   -0.001 1.00 24.47 ? 106 ASP B CB  1 
ATOM   1805 C CG  . ASP B 1 86  ? -5.987  8.722   -1.256 1.00 28.19 ? 106 ASP B CG  1 
ATOM   1806 O OD1 . ASP B 1 86  ? -4.961  9.371   -1.550 1.00 25.36 ? 106 ASP B OD1 1 
ATOM   1807 O OD2 . ASP B 1 86  ? -7.015  8.723   -1.964 1.00 34.23 ? 106 ASP B OD2 1 
ATOM   1808 N N   . ALA B 1 87  ? -4.973  6.051   2.366  1.00 22.53 ? 107 ALA B N   1 
ATOM   1809 C CA  . ALA B 1 87  ? -5.073  5.509   3.717  1.00 21.52 ? 107 ALA B CA  1 
ATOM   1810 C C   . ALA B 1 87  ? -3.821  5.825   4.526  1.00 21.64 ? 107 ALA B C   1 
ATOM   1811 O O   . ALA B 1 87  ? -3.910  6.202   5.706  1.00 21.49 ? 107 ALA B O   1 
ATOM   1812 C CB  . ALA B 1 87  ? -5.309  3.998   3.653  1.00 22.77 ? 107 ALA B CB  1 
ATOM   1813 N N   . LEU B 1 88  ? -2.642  5.684   3.909  1.00 21.49 ? 108 LEU B N   1 
ATOM   1814 C CA  . LEU B 1 88  ? -1.409  6.029   4.613  1.00 22.84 ? 108 LEU B CA  1 
ATOM   1815 C C   . LEU B 1 88  ? -1.321  7.523   4.895  1.00 22.26 ? 108 LEU B C   1 
ATOM   1816 O O   . LEU B 1 88  ? -0.752  7.921   5.912  1.00 21.14 ? 108 LEU B O   1 
ATOM   1817 C CB  . LEU B 1 88  ? -0.189  5.573   3.813  1.00 21.66 ? 108 LEU B CB  1 
ATOM   1818 C CG  . LEU B 1 88  ? 0.043   4.057   3.781  1.00 19.67 ? 108 LEU B CG  1 
ATOM   1819 C CD1 . LEU B 1 88  ? 1.102   3.726   2.752  1.00 24.55 ? 108 LEU B CD1 1 
ATOM   1820 C CD2 . LEU B 1 88  ? 0.451   3.559   5.162  1.00 25.18 ? 108 LEU B CD2 1 
ATOM   1821 N N   . ALA B 1 89  ? -1.871  8.358   4.011  1.00 21.18 ? 109 ALA B N   1 
ATOM   1822 C CA  . ALA B 1 89  ? -1.867  9.799   4.245  1.00 19.22 ? 109 ALA B CA  1 
ATOM   1823 C C   . ALA B 1 89  ? -2.708  10.154  5.457  1.00 23.67 ? 109 ALA B C   1 
ATOM   1824 O O   . ALA B 1 89  ? -2.304  10.985  6.279  1.00 23.09 ? 109 ALA B O   1 
ATOM   1825 C CB  . ALA B 1 89  ? -2.376  10.538  3.005  1.00 20.78 ? 109 ALA B CB  1 
ATOM   1826 N N   . SER B 1 90  ? -3.878  9.529   5.593  1.00 21.19 ? 110 SER B N   1 
ATOM   1827 C CA  . SER B 1 90  ? -4.694  9.763   6.784  1.00 22.06 ? 110 SER B CA  1 
ATOM   1828 C C   . SER B 1 90  ? -3.972  9.284   8.043  1.00 23.63 ? 110 SER B C   1 
ATOM   1829 O O   . SER B 1 90  ? -3.872  10.012  9.043  1.00 22.83 ? 110 SER B O   1 
ATOM   1830 C CB  . SER B 1 90  ? -6.047  9.069   6.631  1.00 23.60 ? 110 SER B CB  1 
ATOM   1831 O OG  . SER B 1 90  ? -6.803  9.141   7.821  1.00 29.79 ? 110 SER B OG  1 
ATOM   1832 N N   . PHE B 1 91  ? -3.441  8.063   7.993  1.00 21.46 ? 111 PHE B N   1 
ATOM   1833 C CA  . PHE B 1 91  ? -2.717  7.495   9.130  1.00 21.42 ? 111 PHE B CA  1 
ATOM   1834 C C   . PHE B 1 91  ? -1.559  8.396   9.556  1.00 21.94 ? 111 PHE B C   1 
ATOM   1835 O O   . PHE B 1 91  ? -1.380  8.689   10.749 1.00 21.79 ? 111 PHE B O   1 
ATOM   1836 C CB  . PHE B 1 91  ? -2.231  6.100   8.719  1.00 18.15 ? 111 PHE B CB  1 
ATOM   1837 C CG  . PHE B 1 91  ? -1.414  5.376   9.754  1.00 21.89 ? 111 PHE B CG  1 
ATOM   1838 C CD1 . PHE B 1 91  ? -0.034  5.522   9.799  1.00 22.08 ? 111 PHE B CD1 1 
ATOM   1839 C CD2 . PHE B 1 91  ? -2.020  4.484   10.623 1.00 23.78 ? 111 PHE B CD2 1 
ATOM   1840 C CE1 . PHE B 1 91  ? 0.721   4.825   10.742 1.00 26.75 ? 111 PHE B CE1 1 
ATOM   1841 C CE2 . PHE B 1 91  ? -1.274  3.778   11.558 1.00 25.61 ? 111 PHE B CE2 1 
ATOM   1842 C CZ  . PHE B 1 91  ? 0.097   3.954   11.614 1.00 25.49 ? 111 PHE B CZ  1 
ATOM   1843 N N   . THR B 1 92  ? -0.768  8.860   8.589  1.00 21.77 ? 112 THR B N   1 
ATOM   1844 C CA  . THR B 1 92  ? 0.444   9.613   8.873  1.00 21.16 ? 112 THR B CA  1 
ATOM   1845 C C   . THR B 1 92  ? 0.130   11.044  9.283  1.00 23.19 ? 112 THR B C   1 
ATOM   1846 O O   . THR B 1 92  ? 0.823   11.601  10.142 1.00 23.86 ? 112 THR B O   1 
ATOM   1847 C CB  . THR B 1 92  ? 1.354   9.591   7.642  1.00 23.29 ? 112 THR B CB  1 
ATOM   1848 O OG1 . THR B 1 92  ? 1.607   8.227   7.265  1.00 23.96 ? 112 THR B OG1 1 
ATOM   1849 C CG2 . THR B 1 92  ? 2.679   10.271  7.934  1.00 25.20 ? 112 THR B CG2 1 
ATOM   1850 N N   . TYR B 1 93  ? -0.907  11.643  8.691  1.00 22.95 ? 113 TYR B N   1 
ATOM   1851 C CA  . TYR B 1 93  ? -1.385  12.944  9.147  1.00 22.84 ? 113 TYR B CA  1 
ATOM   1852 C C   . TYR B 1 93  ? -1.825  12.883  10.598 1.00 26.14 ? 113 TYR B C   1 
ATOM   1853 O O   . TYR B 1 93  ? -1.637  13.850  11.349 1.00 26.51 ? 113 TYR B O   1 
ATOM   1854 C CB  . TYR B 1 93  ? -2.544  13.402  8.259  1.00 24.85 ? 113 TYR B CB  1 
ATOM   1855 C CG  . TYR B 1 93  ? -3.188  14.705  8.669  1.00 28.33 ? 113 TYR B CG  1 
ATOM   1856 C CD1 . TYR B 1 93  ? -2.654  15.919  8.269  1.00 38.30 ? 113 TYR B CD1 1 
ATOM   1857 C CD2 . TYR B 1 93  ? -4.333  14.717  9.452  1.00 32.25 ? 113 TYR B CD2 1 
ATOM   1858 C CE1 . TYR B 1 93  ? -3.244  17.116  8.646  1.00 30.87 ? 113 TYR B CE1 1 
ATOM   1859 C CE2 . TYR B 1 93  ? -4.926  15.903  9.837  1.00 40.18 ? 113 TYR B CE2 1 
ATOM   1860 C CZ  . TYR B 1 93  ? -4.379  17.098  9.426  1.00 33.62 ? 113 TYR B CZ  1 
ATOM   1861 O OH  . TYR B 1 93  ? -4.968  18.284  9.808  1.00 41.24 ? 113 TYR B OH  1 
ATOM   1862 N N   . ASN B 1 94  ? -2.405  11.753  11.012 1.00 23.33 ? 114 ASN B N   1 
ATOM   1863 C CA  . ASN B 1 94  ? -2.862  11.630  12.391 1.00 24.01 ? 114 ASN B CA  1 
ATOM   1864 C C   . ASN B 1 94  ? -1.710  11.340  13.353 1.00 27.23 ? 114 ASN B C   1 
ATOM   1865 O O   . ASN B 1 94  ? -1.642  11.935  14.439 1.00 26.65 ? 114 ASN B O   1 
ATOM   1866 C CB  . ASN B 1 94  ? -3.932  10.541  12.467 1.00 24.68 ? 114 ASN B CB  1 
ATOM   1867 C CG  . ASN B 1 94  ? -4.501  10.370  13.855 1.00 30.77 ? 114 ASN B CG  1 
ATOM   1868 O OD1 . ASN B 1 94  ? -4.630  9.250   14.350 1.00 32.30 ? 114 ASN B OD1 1 
ATOM   1869 N ND2 . ASN B 1 94  ? -4.852  11.479  14.493 1.00 34.22 ? 114 ASN B ND2 1 
ATOM   1870 N N   . LEU B 1 95  ? -0.786  10.449  12.975 1.00 24.15 ? 115 LEU B N   1 
ATOM   1871 C CA  . LEU B 1 95  ? 0.209   9.925   13.907 1.00 20.60 ? 115 LEU B CA  1 
ATOM   1872 C C   . LEU B 1 95  ? 1.615   10.478  13.710 1.00 22.60 ? 115 LEU B C   1 
ATOM   1873 O O   . LEU B 1 95  ? 2.474   10.245  14.567 1.00 25.63 ? 115 LEU B O   1 
ATOM   1874 C CB  . LEU B 1 95  ? 0.249   8.390   13.818 1.00 20.77 ? 115 LEU B CB  1 
ATOM   1875 C CG  . LEU B 1 95  ? -1.026  7.703   14.300 1.00 21.53 ? 115 LEU B CG  1 
ATOM   1876 C CD1 . LEU B 1 95  ? -1.082  6.274   13.803 1.00 25.25 ? 115 LEU B CD1 1 
ATOM   1877 C CD2 . LEU B 1 95  ? -1.093  7.711   15.818 1.00 27.54 ? 115 LEU B CD2 1 
ATOM   1878 N N   . GLY B 1 96  ? 1.877   11.205  12.632 1.00 22.26 ? 116 GLY B N   1 
ATOM   1879 C CA  . GLY B 1 96  ? 3.193   11.762  12.400 1.00 24.45 ? 116 GLY B CA  1 
ATOM   1880 C C   . GLY B 1 96  ? 4.110   10.825  11.628 1.00 24.53 ? 116 GLY B C   1 
ATOM   1881 O O   . GLY B 1 96  ? 3.907   9.612   11.559 1.00 24.64 ? 116 GLY B O   1 
ATOM   1882 N N   . GLU B 1 97  ? 5.166   11.417  11.064 1.00 24.91 ? 117 GLU B N   1 
ATOM   1883 C CA  . GLU B 1 97  ? 6.080   10.673  10.200 1.00 27.04 ? 117 GLU B CA  1 
ATOM   1884 C C   . GLU B 1 97  ? 6.960   9.700   10.970 1.00 29.24 ? 117 GLU B C   1 
ATOM   1885 O O   . GLU B 1 97  ? 7.345   8.664   10.424 1.00 26.02 ? 117 GLU B O   1 
ATOM   1886 C CB  . GLU B 1 97  ? 6.968   11.627  9.399  1.00 28.98 ? 117 GLU B CB  1 
ATOM   1887 C CG  . GLU B 1 97  ? 6.323   12.943  9.039  1.00 40.44 ? 117 GLU B CG  1 
ATOM   1888 C CD  . GLU B 1 97  ? 7.285   13.881  8.346  1.00 48.67 ? 117 GLU B CD  1 
ATOM   1889 O OE1 . GLU B 1 97  ? 8.389   13.429  7.968  1.00 48.86 ? 117 GLU B OE1 1 
ATOM   1890 O OE2 . GLU B 1 97  ? 6.944   15.072  8.190  1.00 51.24 ? 117 GLU B OE2 1 
ATOM   1891 N N   . THR B 1 98  ? 7.304   10.008  12.222 1.00 25.29 ? 118 THR B N   1 
ATOM   1892 C CA  . THR B 1 98  ? 8.158   9.100   12.984 1.00 25.53 ? 118 THR B CA  1 
ATOM   1893 C C   . THR B 1 98  ? 7.435   7.801   13.314 1.00 24.89 ? 118 THR B C   1 
ATOM   1894 O O   . THR B 1 98  ? 8.022   6.713   13.221 1.00 26.07 ? 118 THR B O   1 
ATOM   1895 C CB  . THR B 1 98  ? 8.640   9.789   14.261 1.00 25.40 ? 118 THR B CB  1 
ATOM   1896 O OG1 . THR B 1 98  ? 9.318   10.996  13.902 1.00 30.97 ? 118 THR B OG1 1 
ATOM   1897 C CG2 . THR B 1 98  ? 9.598   8.893   15.033 1.00 28.84 ? 118 THR B CG2 1 
ATOM   1898 N N   . ASN B 1 99  ? 6.160   7.892   13.696 1.00 25.73 ? 119 ASN B N   1 
ATOM   1899 C CA  . ASN B 1 99  ? 5.384   6.687   13.954 1.00 21.46 ? 119 ASN B CA  1 
ATOM   1900 C C   . ASN B 1 99  ? 5.262   5.826   12.701 1.00 21.82 ? 119 ASN B C   1 
ATOM   1901 O O   . ASN B 1 99  ? 5.375   4.598   12.781 1.00 23.71 ? 119 ASN B O   1 
ATOM   1902 C CB  . ASN B 1 99  ? 4.008   7.050   14.511 1.00 22.24 ? 119 ASN B CB  1 
ATOM   1903 C CG  . ASN B 1 99  ? 4.043   7.314   16.009 1.00 24.29 ? 119 ASN B CG  1 
ATOM   1904 O OD1 . ASN B 1 99  ? 4.811   6.684   16.746 1.00 27.38 ? 119 ASN B OD1 1 
ATOM   1905 N ND2 . ASN B 1 99  ? 3.215   8.248   16.465 1.00 27.81 ? 119 ASN B ND2 1 
ATOM   1906 N N   . LEU B 1 100 ? 5.042   6.445   11.536 1.00 22.61 ? 120 LEU B N   1 
ATOM   1907 C CA  . LEU B 1 100 ? 5.046   5.663   10.300 1.00 21.89 ? 120 LEU B CA  1 
ATOM   1908 C C   . LEU B 1 100 ? 6.406   5.018   10.069 1.00 24.42 ? 120 LEU B C   1 
ATOM   1909 O O   . LEU B 1 100 ? 6.496   3.818   9.777  1.00 23.85 ? 120 LEU B O   1 
ATOM   1910 C CB  . LEU B 1 100 ? 4.661   6.536   9.103  1.00 22.93 ? 120 LEU B CB  1 
ATOM   1911 C CG  . LEU B 1 100 ? 4.714   5.802   7.751  1.00 21.45 ? 120 LEU B CG  1 
ATOM   1912 C CD1 . LEU B 1 100 ? 3.637   4.734   7.669  1.00 25.74 ? 120 LEU B CD1 1 
ATOM   1913 C CD2 . LEU B 1 100 ? 4.576   6.789   6.608  1.00 23.15 ? 120 LEU B CD2 1 
ATOM   1914 N N   . ALA B 1 101 ? 7.480   5.799   10.215 1.00 23.04 ? 121 ALA B N   1 
ATOM   1915 C CA  . ALA B 1 101 ? 8.822   5.304   9.922  1.00 24.07 ? 121 ALA B CA  1 
ATOM   1916 C C   . ALA B 1 101 ? 9.199   4.116   10.803 1.00 25.03 ? 121 ALA B C   1 
ATOM   1917 O O   . ALA B 1 101 ? 9.856   3.178   10.336 1.00 28.18 ? 121 ALA B O   1 
ATOM   1918 C CB  . ALA B 1 101 ? 9.843   6.434   10.077 1.00 29.01 ? 121 ALA B CB  1 
ATOM   1919 N N   . ASN B 1 102 ? 8.792   4.126   12.073 1.00 25.37 ? 122 ASN B N   1 
ATOM   1920 C CA  . ASN B 1 102 ? 9.139   3.045   12.993 1.00 25.44 ? 122 ASN B CA  1 
ATOM   1921 C C   . ASN B 1 102 ? 8.115   1.917   13.022 1.00 24.74 ? 122 ASN B C   1 
ATOM   1922 O O   . ASN B 1 102 ? 8.350   0.908   13.698 1.00 26.01 ? 122 ASN B O   1 
ATOM   1923 C CB  . ASN B 1 102 ? 9.302   3.581   14.425 1.00 27.74 ? 122 ASN B CB  1 
ATOM   1924 C CG  . ASN B 1 102 ? 10.391  4.622   14.537 1.00 36.36 ? 122 ASN B CG  1 
ATOM   1925 O OD1 . ASN B 1 102 ? 11.354  4.617   13.769 1.00 37.63 ? 122 ASN B OD1 1 
ATOM   1926 N ND2 . ASN B 1 102 ? 10.252  5.517   15.511 1.00 33.67 ? 122 ASN B ND2 1 
ATOM   1927 N N   . SER B 1 103 ? 7.000   2.054   12.309 1.00 24.08 ? 123 SER B N   1 
ATOM   1928 C CA  . SER B 1 103 ? 5.874   1.150   12.497 1.00 24.22 ? 123 SER B CA  1 
ATOM   1929 C C   . SER B 1 103 ? 6.160   -0.238  11.936 1.00 21.74 ? 123 SER B C   1 
ATOM   1930 O O   . SER B 1 103 ? 6.849   -0.396  10.923 1.00 25.70 ? 123 SER B O   1 
ATOM   1931 C CB  . SER B 1 103 ? 4.618   1.705   11.824 1.00 20.86 ? 123 SER B CB  1 
ATOM   1932 O OG  . SER B 1 103 ? 4.777   1.805   10.413 1.00 20.76 ? 123 SER B OG  1 
ATOM   1933 N N   . THR B 1 104 ? 5.598   -1.247  12.610 1.00 23.01 ? 124 THR B N   1 
ATOM   1934 C CA  . THR B 1 104 ? 5.535   -2.588  12.031 1.00 22.55 ? 124 THR B CA  1 
ATOM   1935 C C   . THR B 1 104 ? 4.775   -2.567  10.711 1.00 24.40 ? 124 THR B C   1 
ATOM   1936 O O   . THR B 1 104 ? 5.096   -3.328  9.788  1.00 25.19 ? 124 THR B O   1 
ATOM   1937 C CB  . THR B 1 104 ? 4.863   -3.550  13.009 1.00 23.14 ? 124 THR B CB  1 
ATOM   1938 O OG1 . THR B 1 104 ? 5.540   -3.501  14.273 1.00 24.69 ? 124 THR B OG1 1 
ATOM   1939 C CG2 . THR B 1 104 ? 4.899   -4.983  12.478 1.00 22.98 ? 124 THR B CG2 1 
ATOM   1940 N N   . LEU B 1 105 ? 3.757   -1.705  10.612 1.00 22.74 ? 125 LEU B N   1 
ATOM   1941 C CA  . LEU B 1 105 ? 3.020   -1.491  9.370  1.00 23.22 ? 125 LEU B CA  1 
ATOM   1942 C C   . LEU B 1 105 ? 3.963   -1.310  8.184  1.00 24.18 ? 125 LEU B C   1 
ATOM   1943 O O   . LEU B 1 105 ? 3.865   -2.025  7.177  1.00 22.87 ? 125 LEU B O   1 
ATOM   1944 C CB  . LEU B 1 105 ? 2.103   -0.264  9.531  1.00 23.10 ? 125 LEU B CB  1 
ATOM   1945 C CG  . LEU B 1 105 ? 0.957   -0.050  8.526  1.00 21.59 ? 125 LEU B CG  1 
ATOM   1946 C CD1 . LEU B 1 105 ? -0.072  0.916   9.112  1.00 25.49 ? 125 LEU B CD1 1 
ATOM   1947 C CD2 . LEU B 1 105 ? 1.453   0.465   7.173  1.00 24.16 ? 125 LEU B CD2 1 
ATOM   1948 N N   . LEU B 1 106 ? 4.883   -0.347  8.294  1.00 21.37 ? 126 LEU B N   1 
ATOM   1949 C CA  . LEU B 1 106 ? 5.798   -0.044  7.197  1.00 22.05 ? 126 LEU B CA  1 
ATOM   1950 C C   . LEU B 1 106 ? 6.789   -1.176  6.956  1.00 24.31 ? 126 LEU B C   1 
ATOM   1951 O O   . LEU B 1 106 ? 7.123   -1.475  5.805  1.00 24.65 ? 126 LEU B O   1 
ATOM   1952 C CB  . LEU B 1 106 ? 6.542   1.258   7.481  1.00 22.77 ? 126 LEU B CB  1 
ATOM   1953 C CG  . LEU B 1 106 ? 7.541   1.698   6.417  1.00 23.23 ? 126 LEU B CG  1 
ATOM   1954 C CD1 . LEU B 1 106 ? 6.813   2.062   5.138  1.00 23.50 ? 126 LEU B CD1 1 
ATOM   1955 C CD2 . LEU B 1 106 ? 8.350   2.884   6.925  1.00 24.84 ? 126 LEU B CD2 1 
ATOM   1956 N N   . LYS B 1 107 ? 7.291   -1.802  8.023  1.00 23.40 ? 127 LYS B N   1 
ATOM   1957 C CA  . LYS B 1 107 ? 8.182   -2.949  7.858  1.00 22.18 ? 127 LYS B CA  1 
ATOM   1958 C C   . LYS B 1 107 ? 7.518   -4.034  7.010  1.00 23.59 ? 127 LYS B C   1 
ATOM   1959 O O   . LYS B 1 107 ? 8.081   -4.510  6.007  1.00 28.39 ? 127 LYS B O   1 
ATOM   1960 C CB  . LYS B 1 107 ? 8.564   -3.495  9.238  1.00 27.74 ? 127 LYS B CB  1 
ATOM   1961 C CG  . LYS B 1 107 ? 9.781   -4.400  9.263  1.00 40.72 ? 127 LYS B CG  1 
ATOM   1962 C CD  . LYS B 1 107 ? 10.512  -4.314  10.607 1.00 47.05 ? 127 LYS B CD  1 
ATOM   1963 C CE  . LYS B 1 107 ? 10.649  -2.877  11.096 1.00 52.02 ? 127 LYS B CE  1 
ATOM   1964 N NZ  . LYS B 1 107 ? 10.976  -2.809  12.549 1.00 60.62 ? 127 LYS B NZ  1 
ATOM   1965 N N   . LYS B 1 108 ? 6.295   -4.413  7.387  1.00 22.61 ? 128 LYS B N   1 
ATOM   1966 C CA  . LYS B 1 108 ? 5.582   -5.441  6.633  1.00 23.31 ? 128 LYS B CA  1 
ATOM   1967 C C   . LYS B 1 108 ? 5.269   -4.969  5.222  1.00 26.32 ? 128 LYS B C   1 
ATOM   1968 O O   . LYS B 1 108 ? 5.397   -5.738  4.263  1.00 24.04 ? 128 LYS B O   1 
ATOM   1969 C CB  . LYS B 1 108 ? 4.300   -5.835  7.363  1.00 20.52 ? 128 LYS B CB  1 
ATOM   1970 C CG  . LYS B 1 108 ? 4.542   -6.642  8.629  1.00 25.83 ? 128 LYS B CG  1 
ATOM   1971 C CD  . LYS B 1 108 ? 3.251   -7.171  9.208  1.00 23.31 ? 128 LYS B CD  1 
ATOM   1972 C CE  . LYS B 1 108 ? 3.541   -7.978  10.472 1.00 29.45 ? 128 LYS B CE  1 
ATOM   1973 N NZ  . LYS B 1 108 ? 2.451   -8.928  10.809 1.00 37.16 ? 128 LYS B NZ  1 
ATOM   1974 N N   . LEU B 1 109 ? 4.869   -3.706  5.071  1.00 21.82 ? 129 LEU B N   1 
ATOM   1975 C CA  . LEU B 1 109 ? 4.549   -3.180  3.749  1.00 23.04 ? 129 LEU B CA  1 
ATOM   1976 C C   . LEU B 1 109 ? 5.751   -3.282  2.816  1.00 24.58 ? 129 LEU B C   1 
ATOM   1977 O O   . LEU B 1 109 ? 5.631   -3.729  1.667  1.00 22.76 ? 129 LEU B O   1 
ATOM   1978 C CB  . LEU B 1 109 ? 4.069   -1.732  3.885  1.00 20.88 ? 129 LEU B CB  1 
ATOM   1979 C CG  . LEU B 1 109 ? 3.698   -0.990  2.603  1.00 22.18 ? 129 LEU B CG  1 
ATOM   1980 C CD1 . LEU B 1 109 ? 2.733   -1.835  1.795  1.00 25.44 ? 129 LEU B CD1 1 
ATOM   1981 C CD2 . LEU B 1 109 ? 3.093   0.368   2.928  1.00 23.11 ? 129 LEU B CD2 1 
ATOM   1982 N N   . ASN B 1 110 ? 6.928   -2.885  3.297  1.00 24.13 ? 130 ASN B N   1 
ATOM   1983 C CA  . ASN B 1 110 ? 8.121   -2.915  2.465  1.00 22.69 ? 130 ASN B CA  1 
ATOM   1984 C C   . ASN B 1 110 ? 8.662   -4.319  2.250  1.00 24.66 ? 130 ASN B C   1 
ATOM   1985 O O   . ASN B 1 110 ? 9.554   -4.484  1.413  1.00 26.24 ? 130 ASN B O   1 
ATOM   1986 C CB  . ASN B 1 110 ? 9.200   -2.004  3.052  1.00 26.60 ? 130 ASN B CB  1 
ATOM   1987 C CG  . ASN B 1 110 ? 8.904   -0.545  2.799  1.00 24.89 ? 130 ASN B CG  1 
ATOM   1988 O OD1 . ASN B 1 110 ? 8.135   -0.216  1.894  1.00 24.58 ? 130 ASN B OD1 1 
ATOM   1989 N ND2 . ASN B 1 110 ? 9.499   0.339   3.598  1.00 26.31 ? 130 ASN B ND2 1 
ATOM   1990 N N   . LYS B 1 111 ? 8.156   -5.317  2.973  1.00 21.60 ? 131 LYS B N   1 
ATOM   1991 C CA  . LYS B 1 111 ? 8.423   -6.704  2.602  1.00 23.96 ? 131 LYS B CA  1 
ATOM   1992 C C   . LYS B 1 111 ? 7.465   -7.228  1.538  1.00 26.97 ? 131 LYS B C   1 
ATOM   1993 O O   . LYS B 1 111 ? 7.588   -8.391  1.134  1.00 26.14 ? 131 LYS B O   1 
ATOM   1994 C CB  . LYS B 1 111 ? 8.368   -7.601  3.838  1.00 26.29 ? 131 LYS B CB  1 
ATOM   1995 C CG  . LYS B 1 111 ? 9.521   -7.360  4.793  1.00 29.24 ? 131 LYS B CG  1 
ATOM   1996 C CD  . LYS B 1 111 ? 9.333   -8.146  6.067  1.00 32.02 ? 131 LYS B CD  1 
ATOM   1997 C CE  . LYS B 1 111 ? 10.544  -8.007  6.969  1.00 39.99 ? 131 LYS B CE  1 
ATOM   1998 N NZ  . LYS B 1 111 ? 10.455  -8.936  8.125  1.00 51.31 ? 131 LYS B NZ  1 
ATOM   1999 N N   . GLY B 1 112 ? 6.532   -6.403  1.062  1.00 25.99 ? 132 GLY B N   1 
ATOM   2000 C CA  . GLY B 1 112 ? 5.507   -6.850  0.137  1.00 25.70 ? 132 GLY B CA  1 
ATOM   2001 C C   . GLY B 1 112 ? 4.283   -7.445  0.793  1.00 27.16 ? 132 GLY B C   1 
ATOM   2002 O O   . GLY B 1 112 ? 3.394   -7.939  0.085  1.00 27.45 ? 132 GLY B O   1 
ATOM   2003 N N   . ASP B 1 113 ? 4.209   -7.408  2.124  1.00 26.15 ? 133 ASP B N   1 
ATOM   2004 C CA  . ASP B 1 113 ? 3.136   -8.036  2.895  1.00 24.36 ? 133 ASP B CA  1 
ATOM   2005 C C   . ASP B 1 113 ? 2.004   -7.025  3.105  1.00 27.21 ? 133 ASP B C   1 
ATOM   2006 O O   . ASP B 1 113 ? 1.832   -6.435  4.172  1.00 24.80 ? 133 ASP B O   1 
ATOM   2007 C CB  . ASP B 1 113 ? 3.690   -8.559  4.217  1.00 24.94 ? 133 ASP B CB  1 
ATOM   2008 C CG  . ASP B 1 113 ? 2.645   -9.242  5.071  1.00 24.05 ? 133 ASP B CG  1 
ATOM   2009 O OD1 . ASP B 1 113 ? 1.544   -9.542  4.556  1.00 28.02 ? 133 ASP B OD1 1 
ATOM   2010 O OD2 . ASP B 1 113 ? 2.920   -9.463  6.275  1.00 28.60 ? 133 ASP B OD2 1 
ATOM   2011 N N   . TYR B 1 114 ? 1.217   -6.837  2.043  1.00 24.94 ? 134 TYR B N   1 
ATOM   2012 C CA  . TYR B 1 114 ? 0.144   -5.845  2.076  1.00 24.21 ? 134 TYR B CA  1 
ATOM   2013 C C   . TYR B 1 114 ? -0.935  -6.198  3.093  1.00 25.21 ? 134 TYR B C   1 
ATOM   2014 O O   . TYR B 1 114 ? -1.462  -5.314  3.774  1.00 25.40 ? 134 TYR B O   1 
ATOM   2015 C CB  . TYR B 1 114 ? -0.471  -5.684  0.686  1.00 24.67 ? 134 TYR B CB  1 
ATOM   2016 C CG  . TYR B 1 114 ? 0.439   -5.003  -0.306 1.00 24.80 ? 134 TYR B CG  1 
ATOM   2017 C CD1 . TYR B 1 114 ? 1.320   -5.738  -1.087 1.00 25.77 ? 134 TYR B CD1 1 
ATOM   2018 C CD2 . TYR B 1 114 ? 0.421   -3.615  -0.459 1.00 22.33 ? 134 TYR B CD2 1 
ATOM   2019 C CE1 . TYR B 1 114 ? 2.154   -5.121  -1.993 1.00 26.61 ? 134 TYR B CE1 1 
ATOM   2020 C CE2 . TYR B 1 114 ? 1.253   -2.987  -1.372 1.00 23.16 ? 134 TYR B CE2 1 
ATOM   2021 C CZ  . TYR B 1 114 ? 2.120   -3.751  -2.136 1.00 26.51 ? 134 TYR B CZ  1 
ATOM   2022 O OH  . TYR B 1 114 ? 2.957   -3.148  -3.038 1.00 26.14 ? 134 TYR B OH  1 
ATOM   2023 N N   . GLN B 1 115 ? -1.295  -7.478  3.206  1.00 24.64 ? 135 GLN B N   1 
ATOM   2024 C CA  . GLN B 1 115 ? -2.340  -7.847  4.159  1.00 25.96 ? 135 GLN B CA  1 
ATOM   2025 C C   . GLN B 1 115 ? -1.880  -7.640  5.596  1.00 24.27 ? 135 GLN B C   1 
ATOM   2026 O O   . GLN B 1 115 ? -2.642  -7.136  6.437  1.00 27.04 ? 135 GLN B O   1 
ATOM   2027 C CB  . GLN B 1 115 ? -2.776  -9.295  3.937  1.00 30.84 ? 135 GLN B CB  1 
ATOM   2028 C CG  . GLN B 1 115 ? -3.913  -9.715  4.851  1.00 34.81 ? 135 GLN B CG  1 
ATOM   2029 C CD  . GLN B 1 115 ? -5.190  -8.954  4.557  1.00 40.53 ? 135 GLN B CD  1 
ATOM   2030 O OE1 . GLN B 1 115 ? -5.605  -8.831  3.403  1.00 42.54 ? 135 GLN B OE1 1 
ATOM   2031 N NE2 . GLN B 1 115 ? -5.815  -8.422  5.603  1.00 44.85 ? 135 GLN B NE2 1 
ATOM   2032 N N   . GLY B 1 116 ? -0.633  -8.011  5.897  1.00 24.93 ? 136 GLY B N   1 
ATOM   2033 C CA  . GLY B 1 116 ? -0.101  -7.754  7.226  1.00 24.12 ? 136 GLY B CA  1 
ATOM   2034 C C   . GLY B 1 116 ? -0.037  -6.270  7.539  1.00 24.91 ? 136 GLY B C   1 
ATOM   2035 O O   . GLY B 1 116 ? -0.382  -5.840  8.648  1.00 25.89 ? 136 GLY B O   1 
ATOM   2036 N N   . ALA B 1 117 ? 0.390   -5.468  6.558  1.00 23.50 ? 137 ALA B N   1 
ATOM   2037 C CA  . ALA B 1 117 ? 0.408   -4.019  6.744  1.00 23.41 ? 137 ALA B CA  1 
ATOM   2038 C C   . ALA B 1 117 ? -0.995  -3.488  7.012  1.00 26.68 ? 137 ALA B C   1 
ATOM   2039 O O   . ALA B 1 117 ? -1.201  -2.681  7.922  1.00 23.66 ? 137 ALA B O   1 
ATOM   2040 C CB  . ALA B 1 117 ? 1.025   -3.340  5.517  1.00 24.14 ? 137 ALA B CB  1 
ATOM   2041 N N   . ALA B 1 118 ? -1.979  -3.941  6.232  1.00 24.63 ? 138 ALA B N   1 
ATOM   2042 C CA  . ALA B 1 118 ? -3.357  -3.509  6.440  1.00 23.83 ? 138 ALA B CA  1 
ATOM   2043 C C   . ALA B 1 118 ? -3.830  -3.840  7.849  1.00 26.22 ? 138 ALA B C   1 
ATOM   2044 O O   . ALA B 1 118 ? -4.508  -3.033  8.496  1.00 25.89 ? 138 ALA B O   1 
ATOM   2045 C CB  . ALA B 1 118 ? -4.268  -4.170  5.401  1.00 27.03 ? 138 ALA B CB  1 
ATOM   2046 N N   . ASP B 1 119 ? -3.472  -5.021  8.349  1.00 27.49 ? 139 ASP B N   1 
ATOM   2047 C CA  . ASP B 1 119 ? -3.899  -5.373  9.694  1.00 26.89 ? 139 ASP B CA  1 
ATOM   2048 C C   . ASP B 1 119 ? -3.178  -4.551  10.762 1.00 25.52 ? 139 ASP B C   1 
ATOM   2049 O O   . ASP B 1 119 ? -3.721  -4.372  11.859 1.00 28.78 ? 139 ASP B O   1 
ATOM   2050 C CB  . ASP B 1 119 ? -3.703  -6.874  9.908  1.00 27.24 ? 139 ASP B CB  1 
ATOM   2051 C CG  . ASP B 1 119 ? -4.690  -7.700  9.102  1.00 37.72 ? 139 ASP B CG  1 
ATOM   2052 O OD1 . ASP B 1 119 ? -5.731  -7.145  8.685  1.00 35.26 ? 139 ASP B OD1 1 
ATOM   2053 O OD2 . ASP B 1 119 ? -4.430  -8.902  8.877  1.00 35.43 ? 139 ASP B OD2 1 
ATOM   2054 N N   . GLN B 1 120 ? -1.984  -4.032  10.463 1.00 25.85 ? 140 GLN B N   1 
ATOM   2055 C CA  . GLN B 1 120 ? -1.289  -3.196  11.445 1.00 24.13 ? 140 GLN B CA  1 
ATOM   2056 C C   . GLN B 1 120 ? -1.963  -1.847  11.691 1.00 25.50 ? 140 GLN B C   1 
ATOM   2057 O O   . GLN B 1 120 ? -1.703  -1.227  12.728 1.00 25.10 ? 140 GLN B O   1 
ATOM   2058 C CB  . GLN B 1 120 ? 0.168   -2.971  11.042 1.00 22.88 ? 140 GLN B CB  1 
ATOM   2059 C CG  . GLN B 1 120 ? 1.063   -4.178  11.301 1.00 25.03 ? 140 GLN B CG  1 
ATOM   2060 C CD  . GLN B 1 120 ? 1.189   -4.474  12.779 1.00 26.53 ? 140 GLN B CD  1 
ATOM   2061 O OE1 . GLN B 1 120 ? 1.594   -3.615  13.559 1.00 24.43 ? 140 GLN B OE1 1 
ATOM   2062 N NE2 . GLN B 1 120 ? 0.862   -5.702  13.169 1.00 29.11 ? 140 GLN B NE2 1 
ATOM   2063 N N   . PHE B 1 121 ? -2.782  -1.342  10.757 1.00 22.97 ? 141 PHE B N   1 
ATOM   2064 C CA  . PHE B 1 121 ? -3.518  -0.107  11.038 1.00 23.37 ? 141 PHE B CA  1 
ATOM   2065 C C   . PHE B 1 121 ? -4.258  -0.213  12.366 1.00 26.83 ? 141 PHE B C   1 
ATOM   2066 O O   . PHE B 1 121 ? -4.260  0.729   13.168 1.00 25.63 ? 141 PHE B O   1 
ATOM   2067 C CB  . PHE B 1 121 ? -4.524  0.213   9.919  1.00 25.45 ? 141 PHE B CB  1 
ATOM   2068 C CG  . PHE B 1 121 ? -3.922  0.825   8.669  1.00 23.08 ? 141 PHE B CG  1 
ATOM   2069 C CD1 . PHE B 1 121 ? -3.409  0.024   7.654  1.00 25.43 ? 141 PHE B CD1 1 
ATOM   2070 C CD2 . PHE B 1 121 ? -3.913  2.202   8.494  1.00 22.96 ? 141 PHE B CD2 1 
ATOM   2071 C CE1 . PHE B 1 121 ? -2.877  0.588   6.503  1.00 24.01 ? 141 PHE B CE1 1 
ATOM   2072 C CE2 . PHE B 1 121 ? -3.383  2.771   7.343  1.00 25.16 ? 141 PHE B CE2 1 
ATOM   2073 C CZ  . PHE B 1 121 ? -2.869  1.961   6.341  1.00 23.31 ? 141 PHE B CZ  1 
ATOM   2074 N N   . LEU B 1 122 ? -4.866  -1.370  12.629 1.00 25.83 ? 142 LEU B N   1 
ATOM   2075 C CA  . LEU B 1 122 ? -5.712  -1.564  13.799 1.00 28.97 ? 142 LEU B CA  1 
ATOM   2076 C C   . LEU B 1 122 ? -4.941  -1.529  15.109 1.00 28.75 ? 142 LEU B C   1 
ATOM   2077 O O   . LEU B 1 122 ? -5.565  -1.363  16.162 1.00 32.55 ? 142 LEU B O   1 
ATOM   2078 C CB  . LEU B 1 122 ? -6.454  -2.896  13.688 1.00 27.67 ? 142 LEU B CB  1 
ATOM   2079 C CG  . LEU B 1 122 ? -7.157  -3.161  12.354 1.00 31.12 ? 142 LEU B CG  1 
ATOM   2080 C CD1 . LEU B 1 122 ? -7.762  -4.556  12.343 1.00 33.86 ? 142 LEU B CD1 1 
ATOM   2081 C CD2 . LEU B 1 122 ? -8.218  -2.104  12.086 1.00 34.35 ? 142 LEU B CD2 1 
ATOM   2082 N N   . VAL B 1 123 ? -3.616  -1.677  15.073 1.00 24.12 ? 143 VAL B N   1 
ATOM   2083 C CA  . VAL B 1 123 ? -2.837  -1.671  16.310 1.00 25.47 ? 143 VAL B CA  1 
ATOM   2084 C C   . VAL B 1 123 ? -2.813  -0.270  16.914 1.00 30.86 ? 143 VAL B C   1 
ATOM   2085 O O   . VAL B 1 123 ? -2.701  -0.108  18.137 1.00 31.33 ? 143 VAL B O   1 
ATOM   2086 C CB  . VAL B 1 123 ? -1.413  -2.200  16.040 1.00 28.54 ? 143 VAL B CB  1 
ATOM   2087 C CG1 . VAL B 1 123 ? -0.526  -2.069  17.280 1.00 32.04 ? 143 VAL B CG1 1 
ATOM   2088 C CG2 . VAL B 1 123 ? -1.461  -3.633  15.562 1.00 27.94 ? 143 VAL B CG2 1 
ATOM   2089 N N   . TRP B 1 124 ? -2.954  0.758   16.080 1.00 27.28 ? 144 TRP B N   1 
ATOM   2090 C CA  . TRP B 1 124 ? -2.760  2.148   16.493 1.00 28.69 ? 144 TRP B CA  1 
ATOM   2091 C C   . TRP B 1 124 ? -4.085  2.771   16.936 1.00 32.56 ? 144 TRP B C   1 
ATOM   2092 O O   . TRP B 1 124 ? -4.562  3.763   16.378 1.00 30.43 ? 144 TRP B O   1 
ATOM   2093 C CB  . TRP B 1 124 ? -2.137  2.950   15.355 1.00 26.14 ? 144 TRP B CB  1 
ATOM   2094 C CG  . TRP B 1 124 ? -0.746  2.539   14.998 1.00 24.16 ? 144 TRP B CG  1 
ATOM   2095 C CD1 . TRP B 1 124 ? -0.377  1.511   14.172 1.00 23.48 ? 144 TRP B CD1 1 
ATOM   2096 C CD2 . TRP B 1 124 ? 0.466   3.131   15.468 1.00 25.16 ? 144 TRP B CD2 1 
ATOM   2097 N NE1 . TRP B 1 124 ? 0.991   1.447   14.082 1.00 24.44 ? 144 TRP B NE1 1 
ATOM   2098 C CE2 . TRP B 1 124 ? 1.532   2.424   14.882 1.00 22.57 ? 144 TRP B CE2 1 
ATOM   2099 C CE3 . TRP B 1 124 ? 0.755   4.194   16.336 1.00 24.49 ? 144 TRP B CE3 1 
ATOM   2100 C CZ2 . TRP B 1 124 ? 2.863   2.758   15.112 1.00 22.98 ? 144 TRP B CZ2 1 
ATOM   2101 C CZ3 . TRP B 1 124 ? 2.074   4.517   16.572 1.00 23.80 ? 144 TRP B CZ3 1 
ATOM   2102 C CH2 . TRP B 1 124 ? 3.113   3.796   15.972 1.00 24.89 ? 144 TRP B CH2 1 
ATOM   2103 N N   . ASN B 1 125 ? -4.673  2.184   17.978 1.00 31.18 ? 145 ASN B N   1 
ATOM   2104 C CA  . ASN B 1 125 ? -5.986  2.600   18.453 1.00 30.46 ? 145 ASN B CA  1 
ATOM   2105 C C   . ASN B 1 125 ? -5.945  3.208   19.851 1.00 31.60 ? 145 ASN B C   1 
ATOM   2106 O O   . ASN B 1 125 ? -6.986  3.300   20.508 1.00 35.31 ? 145 ASN B O   1 
ATOM   2107 C CB  . ASN B 1 125 ? -6.957  1.420   18.435 1.00 32.90 ? 145 ASN B CB  1 
ATOM   2108 C CG  . ASN B 1 125 ? -6.498  0.265   19.311 1.00 36.64 ? 145 ASN B CG  1 
ATOM   2109 O OD1 . ASN B 1 125 ? -5.461  0.337   19.975 1.00 35.51 ? 145 ASN B OD1 1 
ATOM   2110 N ND2 . ASN B 1 125 ? -7.283  -0.806  19.327 1.00 36.25 ? 145 ASN B ND2 1 
ATOM   2111 N N   . LYS B 1 126 ? -4.775  3.621   20.323 1.00 29.26 ? 146 LYS B N   1 
ATOM   2112 C CA  . LYS B 1 126 ? -4.616  4.008   21.718 1.00 32.66 ? 146 LYS B CA  1 
ATOM   2113 C C   . LYS B 1 126 ? -4.164  5.453   21.847 1.00 43.31 ? 146 LYS B C   1 
ATOM   2114 O O   . LYS B 1 126 ? -3.346  5.938   21.058 1.00 37.02 ? 146 LYS B O   1 
ATOM   2115 C CB  . LYS B 1 126 ? -3.620  3.095   22.441 1.00 37.03 ? 146 LYS B CB  1 
ATOM   2116 C CG  . LYS B 1 126 ? -4.252  1.844   23.019 1.00 41.68 ? 146 LYS B CG  1 
ATOM   2117 C CD  . LYS B 1 126 ? -3.199  0.814   23.393 1.00 44.10 ? 146 LYS B CD  1 
ATOM   2118 C CE  . LYS B 1 126 ? -3.781  -0.585  23.384 1.00 40.03 ? 146 LYS B CE  1 
ATOM   2119 N NZ  . LYS B 1 126 ? -3.955  -1.100  21.996 1.00 35.60 ? 146 LYS B NZ  1 
ATOM   2120 N N   . ALA B 1 127 ? -4.712  6.124   22.859 1.00 44.13 ? 147 ALA B N   1 
ATOM   2121 C CA  . ALA B 1 127 ? -4.287  7.455   23.272 1.00 47.07 ? 147 ALA B CA  1 
ATOM   2122 C C   . ALA B 1 127 ? -4.169  7.432   24.786 1.00 51.82 ? 147 ALA B C   1 
ATOM   2123 O O   . ALA B 1 127 ? -5.137  7.100   25.477 1.00 45.53 ? 147 ALA B O   1 
ATOM   2124 C CB  . ALA B 1 127 ? -5.277  8.531   22.820 1.00 50.72 ? 147 ALA B CB  1 
ATOM   2125 N N   . GLY B 1 128 ? -2.989  7.768   25.295 1.00 57.99 ? 148 GLY B N   1 
ATOM   2126 C CA  . GLY B 1 128 ? -2.761  7.660   26.731 1.00 48.61 ? 148 GLY B CA  1 
ATOM   2127 C C   . GLY B 1 128 ? -2.978  6.261   27.259 1.00 54.04 ? 148 GLY B C   1 
ATOM   2128 O O   . GLY B 1 128 ? -3.508  6.085   28.365 1.00 48.29 ? 148 GLY B O   1 
ATOM   2129 N N   . GLY B 1 129 ? -2.600  5.250   26.477 1.00 52.63 ? 149 GLY B N   1 
ATOM   2130 C CA  . GLY B 1 129 ? -2.742  3.868   26.890 1.00 43.86 ? 149 GLY B CA  1 
ATOM   2131 C C   . GLY B 1 129 ? -4.152  3.323   26.877 1.00 44.00 ? 149 GLY B C   1 
ATOM   2132 O O   . GLY B 1 129 ? -4.331  2.120   27.095 1.00 53.14 ? 149 GLY B O   1 
ATOM   2133 N N   . LYS B 1 130 ? -5.158  4.159   26.635 1.00 42.29 ? 150 LYS B N   1 
ATOM   2134 C CA  . LYS B 1 130 ? -6.545  3.724   26.562 1.00 41.67 ? 150 LYS B CA  1 
ATOM   2135 C C   . LYS B 1 130 ? -6.931  3.524   25.104 1.00 44.90 ? 150 LYS B C   1 
ATOM   2136 O O   . LYS B 1 130 ? -6.603  4.358   24.254 1.00 40.59 ? 150 LYS B O   1 
ATOM   2137 C CB  . LYS B 1 130 ? -7.483  4.748   27.206 1.00 48.26 ? 150 LYS B CB  1 
ATOM   2138 C CG  . LYS B 1 130 ? -7.417  4.835   28.723 1.00 51.90 ? 150 LYS B CG  1 
ATOM   2139 C CD  . LYS B 1 130 ? -7.368  6.288   29.171 1.00 57.82 ? 150 LYS B CD  1 
ATOM   2140 C CE  . LYS B 1 130 ? -8.766  6.837   29.418 1.00 56.89 ? 150 LYS B CE  1 
ATOM   2141 N NZ  . LYS B 1 130 ? -8.748  8.280   29.790 1.00 59.92 ? 150 LYS B NZ  1 
ATOM   2142 N N   . VAL B 1 131 ? -7.625  2.424   24.817 1.00 42.69 ? 151 VAL B N   1 
ATOM   2143 C CA  . VAL B 1 131 ? -8.199  2.250   23.491 1.00 39.31 ? 151 VAL B CA  1 
ATOM   2144 C C   . VAL B 1 131 ? -9.376  3.201   23.333 1.00 50.14 ? 151 VAL B C   1 
ATOM   2145 O O   . VAL B 1 131 ? -10.311 3.201   24.146 1.00 45.99 ? 151 VAL B O   1 
ATOM   2146 C CB  . VAL B 1 131 ? -8.618  0.791   23.263 1.00 38.97 ? 151 VAL B CB  1 
ATOM   2147 C CG1 . VAL B 1 131 ? -9.325  0.651   21.926 1.00 42.08 ? 151 VAL B CG1 1 
ATOM   2148 C CG2 . VAL B 1 131 ? -7.398  -0.113  23.306 1.00 39.53 ? 151 VAL B CG2 1 
ATOM   2149 N N   . MET B 1 132 ? -9.325  4.031   22.296 1.00 38.84 ? 152 MET B N   1 
ATOM   2150 C CA  . MET B 1 132 ? -10.366 5.007   22.007 1.00 44.62 ? 152 MET B CA  1 
ATOM   2151 C C   . MET B 1 132 ? -11.259 4.492   20.887 1.00 51.56 ? 152 MET B C   1 
ATOM   2152 O O   . MET B 1 132 ? -10.764 4.058   19.842 1.00 44.88 ? 152 MET B O   1 
ATOM   2153 C CB  . MET B 1 132 ? -9.752  6.353   21.624 1.00 45.34 ? 152 MET B CB  1 
ATOM   2154 C CG  . MET B 1 132 ? -8.684  6.831   22.588 1.00 49.40 ? 152 MET B CG  1 
ATOM   2155 S SD  . MET B 1 132 ? -9.370  7.026   24.243 1.00 48.60 ? 152 MET B SD  1 
ATOM   2156 C CE  . MET B 1 132 ? -10.570 8.322   23.929 1.00 52.63 ? 152 MET B CE  1 
ATOM   2157 N N   . LYS B 1 133 ? -12.574 4.538   21.113 1.00 52.16 ? 153 LYS B N   1 
ATOM   2158 C CA  . LYS B 1 133 ? -13.519 4.064   20.108 1.00 52.55 ? 153 LYS B CA  1 
ATOM   2159 C C   . LYS B 1 133 ? -13.398 4.855   18.813 1.00 51.37 ? 153 LYS B C   1 
ATOM   2160 O O   . LYS B 1 133 ? -13.525 4.286   17.721 1.00 48.28 ? 153 LYS B O   1 
ATOM   2161 C CB  . LYS B 1 133 ? -14.944 4.140   20.657 1.00 56.66 ? 153 LYS B CB  1 
ATOM   2162 C CG  . LYS B 1 133 ? -15.665 2.801   20.689 1.00 65.91 ? 153 LYS B CG  1 
ATOM   2163 C CD  . LYS B 1 133 ? -16.923 2.866   21.545 1.00 70.43 ? 153 LYS B CD  1 
ATOM   2164 C CE  . LYS B 1 133 ? -17.854 3.979   21.092 1.00 67.01 ? 153 LYS B CE  1 
ATOM   2165 N NZ  . LYS B 1 133 ? -19.053 4.095   21.970 1.00 61.83 ? 153 LYS B NZ  1 
ATOM   2166 N N   . GLY B 1 134 ? -13.137 6.160   18.914 1.00 49.07 ? 154 GLY B N   1 
ATOM   2167 C CA  . GLY B 1 134 ? -12.934 6.958   17.718 1.00 49.85 ? 154 GLY B CA  1 
ATOM   2168 C C   . GLY B 1 134 ? -11.702 6.538   16.940 1.00 48.13 ? 154 GLY B C   1 
ATOM   2169 O O   . GLY B 1 134 ? -11.724 6.484   15.707 1.00 43.70 ? 154 GLY B O   1 
ATOM   2170 N N   . LEU B 1 135 ? -10.613 6.224   17.646 1.00 47.38 ? 155 LEU B N   1 
ATOM   2171 C CA  . LEU B 1 135 ? -9.408  5.763   16.963 1.00 48.70 ? 155 LEU B CA  1 
ATOM   2172 C C   . LEU B 1 135 ? -9.619  4.387   16.347 1.00 45.39 ? 155 LEU B C   1 
ATOM   2173 O O   . LEU B 1 135 ? -9.084  4.098   15.272 1.00 38.38 ? 155 LEU B O   1 
ATOM   2174 C CB  . LEU B 1 135 ? -8.223  5.744   17.927 1.00 38.95 ? 155 LEU B CB  1 
ATOM   2175 C CG  . LEU B 1 135 ? -7.762  7.100   18.463 1.00 41.95 ? 155 LEU B CG  1 
ATOM   2176 C CD1 . LEU B 1 135 ? -6.608  6.917   19.440 1.00 41.21 ? 155 LEU B CD1 1 
ATOM   2177 C CD2 . LEU B 1 135 ? -7.379  8.047   17.332 1.00 39.87 ? 155 LEU B CD2 1 
ATOM   2178 N N   . VAL B 1 136 ? -10.397 3.527   17.010 1.00 34.72 ? 156 VAL B N   1 
ATOM   2179 C CA  . VAL B 1 136 ? -10.746 2.235   16.422 1.00 40.25 ? 156 VAL B CA  1 
ATOM   2180 C C   . VAL B 1 136 ? -11.503 2.440   15.117 1.00 45.35 ? 156 VAL B C   1 
ATOM   2181 O O   . VAL B 1 136 ? -11.179 1.833   14.087 1.00 38.69 ? 156 VAL B O   1 
ATOM   2182 C CB  . VAL B 1 136 ? -11.559 1.391   17.419 1.00 43.74 ? 156 VAL B CB  1 
ATOM   2183 C CG1 . VAL B 1 136 ? -12.174 0.189   16.725 1.00 41.92 ? 156 VAL B CG1 1 
ATOM   2184 C CG2 . VAL B 1 136 ? -10.675 0.939   18.569 1.00 44.13 ? 156 VAL B CG2 1 
ATOM   2185 N N   . ARG B 1 137 ? -12.519 3.307   15.142 1.00 38.66 ? 157 ARG B N   1 
ATOM   2186 C CA  . ARG B 1 137 ? -13.295 3.576   13.934 1.00 43.36 ? 157 ARG B CA  1 
ATOM   2187 C C   . ARG B 1 137 ? -12.411 4.153   12.833 1.00 45.37 ? 157 ARG B C   1 
ATOM   2188 O O   . ARG B 1 137 ? -12.534 3.775   11.659 1.00 40.47 ? 157 ARG B O   1 
ATOM   2189 C CB  . ARG B 1 137 ? -14.443 4.532   14.262 1.00 50.26 ? 157 ARG B CB  1 
ATOM   2190 C CG  . ARG B 1 137 ? -15.603 3.872   14.994 1.00 55.23 ? 157 ARG B CG  1 
ATOM   2191 C CD  . ARG B 1 137 ? -16.768 4.833   15.187 1.00 60.62 ? 157 ARG B CD  1 
ATOM   2192 N NE  . ARG B 1 137 ? -17.996 4.127   15.530 1.00 59.83 ? 157 ARG B NE  1 
ATOM   2193 C CZ  . ARG B 1 137 ? -18.298 3.697   16.748 1.00 62.20 ? 157 ARG B CZ  1 
ATOM   2194 N NH1 . ARG B 1 137 ? -17.498 3.918   17.778 1.00 64.83 ? 157 ARG B NH1 1 
ATOM   2195 N NH2 . ARG B 1 137 ? -19.433 3.029   16.937 1.00 65.36 ? 157 ARG B NH2 1 
ATOM   2196 N N   . ARG B 1 138 ? -11.496 5.052   13.201 1.00 33.42 ? 158 ARG B N   1 
ATOM   2197 C CA  . ARG B 1 138 ? -10.620 5.681   12.219 1.00 37.63 ? 158 ARG B CA  1 
ATOM   2198 C C   . ARG B 1 138 ? -9.671  4.671   11.586 1.00 35.34 ? 158 ARG B C   1 
ATOM   2199 O O   . ARG B 1 138 ? -9.517  4.629   10.357 1.00 32.07 ? 158 ARG B O   1 
ATOM   2200 C CB  . ARG B 1 138 ? -9.834  6.809   12.879 1.00 35.74 ? 158 ARG B CB  1 
ATOM   2201 C CG  . ARG B 1 138 ? -8.705  7.321   12.029 1.00 34.34 ? 158 ARG B CG  1 
ATOM   2202 C CD  . ARG B 1 138 ? -8.313  8.732   12.422 1.00 38.05 ? 158 ARG B CD  1 
ATOM   2203 N NE  . ARG B 1 138 ? -7.599  9.392   11.336 1.00 37.89 ? 158 ARG B NE  1 
ATOM   2204 C CZ  . ARG B 1 138 ? -7.335  10.690  11.292 1.00 39.75 ? 158 ARG B CZ  1 
ATOM   2205 N NH1 . ARG B 1 138 ? -7.695  11.502  12.274 1.00 45.55 ? 158 ARG B NH1 1 
ATOM   2206 N NH2 . ARG B 1 138 ? -6.701  11.187  10.234 1.00 35.05 ? 158 ARG B NH2 1 
ATOM   2207 N N   . ARG B 1 139 ? -9.005  3.863   12.413 1.00 33.70 ? 159 ARG B N   1 
ATOM   2208 C CA  . ARG B 1 139 ? -8.094  2.852   11.888 1.00 26.63 ? 159 ARG B CA  1 
ATOM   2209 C C   . ARG B 1 139 ? -8.834  1.829   11.040 1.00 31.74 ? 159 ARG B C   1 
ATOM   2210 O O   . ARG B 1 139 ? -8.286  1.321   10.055 1.00 30.14 ? 159 ARG B O   1 
ATOM   2211 C CB  . ARG B 1 139 ? -7.353  2.159   13.031 1.00 27.19 ? 159 ARG B CB  1 
ATOM   2212 C CG  . ARG B 1 139 ? -6.458  3.081   13.835 1.00 27.93 ? 159 ARG B CG  1 
ATOM   2213 C CD  . ARG B 1 139 ? -5.266  3.589   13.022 1.00 26.31 ? 159 ARG B CD  1 
ATOM   2214 N NE  . ARG B 1 139 ? -5.464  4.902   12.413 1.00 28.70 ? 159 ARG B NE  1 
ATOM   2215 C CZ  . ARG B 1 139 ? -5.254  6.057   13.034 1.00 24.63 ? 159 ARG B CZ  1 
ATOM   2216 N NH1 . ARG B 1 139 ? -4.906  6.106   14.311 1.00 31.47 ? 159 ARG B NH1 1 
ATOM   2217 N NH2 . ARG B 1 139 ? -5.393  7.192   12.356 1.00 32.00 ? 159 ARG B NH2 1 
ATOM   2218 N N   . GLU B 1 140 ? -10.081 1.510   11.404 1.00 30.89 ? 160 GLU B N   1 
ATOM   2219 C CA  . GLU B 1 140 ? -10.856 0.580   10.592 1.00 32.56 ? 160 GLU B CA  1 
ATOM   2220 C C   . GLU B 1 140 ? -11.195 1.183   9.233  1.00 27.76 ? 160 GLU B C   1 
ATOM   2221 O O   . GLU B 1 140 ? -11.115 0.492   8.210  1.00 32.73 ? 160 GLU B O   1 
ATOM   2222 C CB  . GLU B 1 140 ? -12.122 0.159   11.336 1.00 35.02 ? 160 GLU B CB  1 
ATOM   2223 C CG  . GLU B 1 140 ? -11.989 -1.179  12.048 1.00 47.73 ? 160 GLU B CG  1 
ATOM   2224 C CD  . GLU B 1 140 ? -12.822 -1.255  13.309 1.00 56.17 ? 160 GLU B CD  1 
ATOM   2225 O OE1 . GLU B 1 140 ? -13.767 -0.451  13.449 1.00 62.10 ? 160 GLU B OE1 1 
ATOM   2226 O OE2 . GLU B 1 140 ? -12.524 -2.115  14.164 1.00 57.43 ? 160 GLU B OE2 1 
ATOM   2227 N N   . ALA B 1 141 ? -11.560 2.470   9.201  1.00 31.50 ? 161 ALA B N   1 
ATOM   2228 C CA  . ALA B 1 141 ? -11.821 3.133   7.923  1.00 27.91 ? 161 ALA B CA  1 
ATOM   2229 C C   . ALA B 1 141 ? -10.565 3.183   7.059  1.00 32.76 ? 161 ALA B C   1 
ATOM   2230 O O   . ALA B 1 141 ? -10.622 2.966   5.838  1.00 31.17 ? 161 ALA B O   1 
ATOM   2231 C CB  . ALA B 1 141 ? -12.360 4.543   8.165  1.00 32.98 ? 161 ALA B CB  1 
ATOM   2232 N N   . GLU B 1 142 ? -9.417  3.462   7.681  1.00 29.58 ? 162 GLU B N   1 
ATOM   2233 C CA  . GLU B 1 142 ? -8.166  3.534   6.933  1.00 27.43 ? 162 GLU B CA  1 
ATOM   2234 C C   . GLU B 1 142 ? -7.785  2.166   6.375  1.00 28.34 ? 162 GLU B C   1 
ATOM   2235 O O   . GLU B 1 142 ? -7.378  2.055   5.213  1.00 27.85 ? 162 GLU B O   1 
ATOM   2236 C CB  . GLU B 1 142 ? -7.055  4.082   7.830  1.00 26.00 ? 162 GLU B CB  1 
ATOM   2237 C CG  . GLU B 1 142 ? -7.158  5.574   8.116  1.00 29.13 ? 162 GLU B CG  1 
ATOM   2238 C CD  . GLU B 1 142 ? -6.247  6.004   9.250  1.00 30.77 ? 162 GLU B CD  1 
ATOM   2239 O OE1 . GLU B 1 142 ? -6.176  7.219   9.538  1.00 26.60 ? 162 GLU B OE1 1 
ATOM   2240 O OE2 . GLU B 1 142 ? -5.588  5.123   9.839  1.00 28.77 ? 162 GLU B OE2 1 
ATOM   2241 N N   . ARG B 1 143 ? -7.918  1.114   7.188  1.00 28.90 ? 163 ARG B N   1 
ATOM   2242 C CA  . ARG B 1 143 ? -7.658  -0.240  6.712  1.00 25.39 ? 163 ARG B CA  1 
ATOM   2243 C C   . ARG B 1 143 ? -8.602  -0.612  5.576  1.00 27.50 ? 163 ARG B C   1 
ATOM   2244 O O   . ARG B 1 143 ? -8.180  -1.228  4.592  1.00 27.99 ? 163 ARG B O   1 
ATOM   2245 C CB  . ARG B 1 143 ? -7.790  -1.234  7.868  1.00 26.02 ? 163 ARG B CB  1 
ATOM   2246 C CG  . ARG B 1 143 ? -7.700  -2.697  7.452  1.00 27.94 ? 163 ARG B CG  1 
ATOM   2247 C CD  . ARG B 1 143 ? -7.918  -3.605  8.649  1.00 29.04 ? 163 ARG B CD  1 
ATOM   2248 N NE  . ARG B 1 143 ? -7.785  -5.009  8.287  1.00 33.89 ? 163 ARG B NE  1 
ATOM   2249 C CZ  . ARG B 1 143 ? -8.767  -5.746  7.786  1.00 42.82 ? 163 ARG B CZ  1 
ATOM   2250 N NH1 . ARG B 1 143 ? -9.966  -5.234  7.558  1.00 38.35 ? 163 ARG B NH1 1 
ATOM   2251 N NH2 . ARG B 1 143 ? -8.539  -7.025  7.503  1.00 37.69 ? 163 ARG B NH2 1 
ATOM   2252 N N   . ALA B 1 144 ? -9.882  -0.245  5.697  1.00 27.71 ? 164 ALA B N   1 
ATOM   2253 C CA  . ALA B 1 144 ? -10.848 -0.559  4.646  1.00 32.97 ? 164 ALA B CA  1 
ATOM   2254 C C   . ALA B 1 144 ? -10.469 0.108   3.332  1.00 33.93 ? 164 ALA B C   1 
ATOM   2255 O O   . ALA B 1 144 ? -10.566 -0.508  2.264  1.00 32.56 ? 164 ALA B O   1 
ATOM   2256 C CB  . ALA B 1 144 ? -12.251 -0.133  5.076  1.00 34.56 ? 164 ALA B CB  1 
ATOM   2257 N N   . LEU B 1 145 ? -10.039 1.369   3.386  1.00 28.70 ? 165 LEU B N   1 
ATOM   2258 C CA  . LEU B 1 145 ? -9.606  2.036   2.160  1.00 27.69 ? 165 LEU B CA  1 
ATOM   2259 C C   . LEU B 1 145 ? -8.331  1.402   1.610  1.00 29.66 ? 165 LEU B C   1 
ATOM   2260 O O   . LEU B 1 145 ? -8.197  1.216   0.394  1.00 30.02 ? 165 LEU B O   1 
ATOM   2261 C CB  . LEU B 1 145 ? -9.412  3.531   2.419  1.00 28.61 ? 165 LEU B CB  1 
ATOM   2262 C CG  . LEU B 1 145 ? -8.965  4.425   1.264  1.00 28.35 ? 165 LEU B CG  1 
ATOM   2263 C CD1 . LEU B 1 145 ? -9.930  4.299   0.095  1.00 29.42 ? 165 LEU B CD1 1 
ATOM   2264 C CD2 . LEU B 1 145 ? -8.874  5.867   1.725  1.00 27.79 ? 165 LEU B CD2 1 
ATOM   2265 N N   . PHE B 1 146 ? -7.397  1.042   2.496  1.00 26.21 ? 166 PHE B N   1 
ATOM   2266 C CA  . PHE B 1 146 ? -6.153  0.399   2.078  1.00 25.74 ? 166 PHE B CA  1 
ATOM   2267 C C   . PHE B 1 146 ? -6.422  -0.886  1.299  1.00 30.18 ? 166 PHE B C   1 
ATOM   2268 O O   . PHE B 1 146 ? -5.717  -1.195  0.330  1.00 28.06 ? 166 PHE B O   1 
ATOM   2269 C CB  . PHE B 1 146 ? -5.295  0.118   3.318  1.00 27.45 ? 166 PHE B CB  1 
ATOM   2270 C CG  . PHE B 1 146 ? -3.884  -0.333  3.018  1.00 24.53 ? 166 PHE B CG  1 
ATOM   2271 C CD1 . PHE B 1 146 ? -2.869  0.592   2.818  1.00 22.00 ? 166 PHE B CD1 1 
ATOM   2272 C CD2 . PHE B 1 146 ? -3.572  -1.686  2.956  1.00 25.63 ? 166 PHE B CD2 1 
ATOM   2273 C CE1 . PHE B 1 146 ? -1.570  0.183   2.563  1.00 23.89 ? 166 PHE B CE1 1 
ATOM   2274 C CE2 . PHE B 1 146 ? -2.277  -2.104  2.697  1.00 24.23 ? 166 PHE B CE2 1 
ATOM   2275 C CZ  . PHE B 1 146 ? -1.275  -1.170  2.498  1.00 24.28 ? 166 PHE B CZ  1 
ATOM   2276 N N   . LEU B 1 147 ? -7.440  -1.641  1.699  1.00 28.73 ? 167 LEU B N   1 
ATOM   2277 C CA  . LEU B 1 147 ? -7.742  -2.927  1.081  1.00 27.86 ? 167 LEU B CA  1 
ATOM   2278 C C   . LEU B 1 147 ? -8.722  -2.813  -0.077 1.00 32.24 ? 167 LEU B C   1 
ATOM   2279 O O   . LEU B 1 147 ? -9.004  -3.824  -0.732 1.00 37.41 ? 167 LEU B O   1 
ATOM   2280 C CB  . LEU B 1 147 ? -8.294  -3.895  2.131  1.00 31.72 ? 167 LEU B CB  1 
ATOM   2281 C CG  . LEU B 1 147 ? -7.276  -4.393  3.156  1.00 27.37 ? 167 LEU B CG  1 
ATOM   2282 C CD1 . LEU B 1 147 ? -7.960  -5.191  4.255  1.00 33.93 ? 167 LEU B CD1 1 
ATOM   2283 C CD2 . LEU B 1 147 ? -6.189  -5.210  2.472  1.00 32.01 ? 167 LEU B CD2 1 
ATOM   2284 N N   . LYS B 1 148 ? -9.234  -1.620  -0.349 1.00 31.58 ? 168 LYS B N   1 
ATOM   2285 C CA  . LYS B 1 148 ? -10.186 -1.406  -1.431 1.00 38.23 ? 168 LYS B CA  1 
ATOM   2286 C C   . LYS B 1 148 ? -9.524  -1.596  -2.791 1.00 36.99 ? 168 LYS B C   1 
ATOM   2287 O O   . LYS B 1 148 ? -8.657  -0.814  -3.181 1.00 33.63 ? 168 LYS B O   1 
ATOM   2288 C CB  . LYS B 1 148 ? -10.792 -0.005  -1.331 1.00 34.16 ? 168 LYS B CB  1 
ATOM   2289 C CG  . LYS B 1 148 ? -12.044 0.209   -2.167 1.00 37.32 ? 168 LYS B CG  1 
ATOM   2290 C CD  . LYS B 1 148 ? -12.491 1.659   -2.078 1.00 45.91 ? 168 LYS B CD  1 
ATOM   2291 C CE  . LYS B 1 148 ? -13.834 1.895   -2.753 1.00 49.49 ? 168 LYS B CE  1 
ATOM   2292 N NZ  . LYS B 1 148 ? -14.165 0.845   -3.754 1.00 58.02 ? 168 LYS B NZ  1 
HETATM 2293 O O   . HOH C 2 .   ? 7.150   3.213   32.114 1.00 31.79 ? 201 HOH A O   1 
HETATM 2294 O O   . HOH C 2 .   ? -4.115  22.063  29.052 1.00 48.97 ? 202 HOH A O   1 
HETATM 2295 O O   . HOH C 2 .   ? 0.541   7.526   42.067 1.00 53.22 ? 203 HOH A O   1 
HETATM 2296 O O   . HOH C 2 .   ? 2.129   -12.502 35.384 1.00 46.73 ? 204 HOH A O   1 
HETATM 2297 O O   . HOH C 2 .   ? 4.332   -7.417  17.174 1.00 47.13 ? 205 HOH A O   1 
HETATM 2298 O O   . HOH C 2 .   ? 9.770   33.064  29.191 1.00 58.43 ? 206 HOH A O   1 
HETATM 2299 O O   . HOH C 2 .   ? -1.349  -0.287  20.375 1.00 36.37 ? 207 HOH A O   1 
HETATM 2300 O O   . HOH C 2 .   ? 7.708   24.072  19.070 1.00 36.30 ? 208 HOH A O   1 
HETATM 2301 O O   . HOH C 2 .   ? -5.275  -11.272 32.233 1.00 45.19 ? 209 HOH A O   1 
HETATM 2302 O O   . HOH C 2 .   ? 14.099  33.760  29.523 1.00 34.44 ? 210 HOH A O   1 
HETATM 2303 O O   . HOH C 2 .   ? 14.876  5.494   41.401 1.00 39.81 ? 211 HOH A O   1 
HETATM 2304 O O   . HOH C 2 .   ? 2.631   23.346  23.858 1.00 34.93 ? 212 HOH A O   1 
HETATM 2305 O O   . HOH C 2 .   ? 5.037   -9.089  36.231 1.00 36.96 ? 213 HOH A O   1 
HETATM 2306 O O   . HOH C 2 .   ? 6.081   16.889  44.018 1.00 38.96 ? 214 HOH A O   1 
HETATM 2307 O O   . HOH C 2 .   ? 2.316   -0.968  13.152 1.00 23.62 ? 215 HOH A O   1 
HETATM 2308 O O   . HOH C 2 .   ? 11.492  6.121   40.752 1.00 31.40 ? 216 HOH A O   1 
HETATM 2309 O O   . HOH C 2 .   ? 12.745  34.929  32.724 1.00 43.07 ? 217 HOH A O   1 
HETATM 2310 O O   . HOH C 2 .   ? 20.942  22.585  27.286 1.00 27.41 ? 218 HOH A O   1 
HETATM 2311 O O   . HOH C 2 .   ? 4.533   -0.266  34.679 1.00 25.57 ? 219 HOH A O   1 
HETATM 2312 O O   . HOH C 2 .   ? -0.718  -9.941  25.719 1.00 34.69 ? 220 HOH A O   1 
HETATM 2313 O O   . HOH C 2 .   ? 15.603  1.317   39.948 1.00 40.37 ? 221 HOH A O   1 
HETATM 2314 O O   . HOH C 2 .   ? 8.524   -11.493 29.425 1.00 28.49 ? 222 HOH A O   1 
HETATM 2315 O O   . HOH C 2 .   ? 11.430  15.984  48.319 1.00 41.32 ? 223 HOH A O   1 
HETATM 2316 O O   . HOH C 2 .   ? 13.386  26.775  22.236 1.00 41.45 ? 224 HOH A O   1 
HETATM 2317 O O   . HOH C 2 .   ? 10.663  -0.296  30.543 1.00 27.04 ? 225 HOH A O   1 
HETATM 2318 O O   . HOH C 2 .   ? 12.650  13.065  46.337 1.00 32.97 ? 226 HOH A O   1 
HETATM 2319 O O   . HOH C 2 .   ? 9.003   -5.351  24.844 1.00 35.85 ? 227 HOH A O   1 
HETATM 2320 O O   . HOH C 2 .   ? 17.135  19.274  22.720 1.00 33.27 ? 228 HOH A O   1 
HETATM 2321 O O   . HOH C 2 .   ? 17.467  17.567  20.787 1.00 38.11 ? 229 HOH A O   1 
HETATM 2322 O O   . HOH C 2 .   ? 9.555   6.911   42.505 1.00 35.11 ? 230 HOH A O   1 
HETATM 2323 O O   . HOH C 2 .   ? 11.672  30.504  27.601 1.00 28.92 ? 231 HOH A O   1 
HETATM 2324 O O   . HOH C 2 .   ? 5.965   1.149   24.275 1.00 31.45 ? 232 HOH A O   1 
HETATM 2325 O O   . HOH C 2 .   ? 15.619  3.068   34.591 1.00 30.61 ? 233 HOH A O   1 
HETATM 2326 O O   . HOH C 2 .   ? 0.438   1.464   29.633 1.00 38.91 ? 234 HOH A O   1 
HETATM 2327 O O   . HOH C 2 .   ? 19.438  27.147  42.882 1.00 33.39 ? 235 HOH A O   1 
HETATM 2328 O O   . HOH C 2 .   ? 0.063   20.069  36.729 1.00 37.37 ? 236 HOH A O   1 
HETATM 2329 O O   . HOH C 2 .   ? 0.911   26.381  38.476 1.00 33.96 ? 237 HOH A O   1 
HETATM 2330 O O   . HOH C 2 .   ? 7.858   24.601  42.008 1.00 29.78 ? 238 HOH A O   1 
HETATM 2331 O O   . HOH C 2 .   ? -1.607  -10.764 28.280 1.00 32.89 ? 239 HOH A O   1 
HETATM 2332 O O   . HOH C 2 .   ? 18.799  20.045  42.121 1.00 42.10 ? 240 HOH A O   1 
HETATM 2333 O O   . HOH C 2 .   ? 5.026   -14.457 23.629 1.00 41.48 ? 241 HOH A O   1 
HETATM 2334 O O   . HOH C 2 .   ? 9.147   -8.988  23.200 1.00 42.04 ? 242 HOH A O   1 
HETATM 2335 O O   . HOH C 2 .   ? 8.117   -7.700  17.872 1.00 52.09 ? 243 HOH A O   1 
HETATM 2336 O O   . HOH C 2 .   ? 10.237  6.355   28.507 1.00 35.59 ? 244 HOH A O   1 
HETATM 2337 O O   . HOH C 2 .   ? 11.103  -0.191  41.574 1.00 35.16 ? 245 HOH A O   1 
HETATM 2338 O O   . HOH C 2 .   ? 25.070  17.972  38.831 1.00 54.65 ? 246 HOH A O   1 
HETATM 2339 O O   . HOH C 2 .   ? 4.109   -14.390 27.813 1.00 39.74 ? 247 HOH A O   1 
HETATM 2340 O O   . HOH C 2 .   ? 13.687  0.021   32.803 1.00 43.45 ? 248 HOH A O   1 
HETATM 2341 O O   . HOH C 2 .   ? 1.750   -8.177  43.333 1.00 40.47 ? 249 HOH A O   1 
HETATM 2342 O O   . HOH C 2 .   ? 22.988  11.438  38.587 1.00 40.94 ? 250 HOH A O   1 
HETATM 2343 O O   . HOH C 2 .   ? -3.016  13.918  20.818 1.00 46.31 ? 251 HOH A O   1 
HETATM 2344 O O   . HOH C 2 .   ? 0.867   25.447  31.973 1.00 37.68 ? 252 HOH A O   1 
HETATM 2345 O O   . HOH C 2 .   ? 0.058   2.561   19.999 1.00 46.48 ? 253 HOH A O   1 
HETATM 2346 O O   . HOH C 2 .   ? 23.190  27.071  31.229 1.00 31.22 ? 254 HOH A O   1 
HETATM 2347 O O   . HOH C 2 .   ? 20.784  7.737   32.903 1.00 42.73 ? 255 HOH A O   1 
HETATM 2348 O O   . HOH C 2 .   ? -8.771  0.794   27.063 1.00 48.00 ? 256 HOH A O   1 
HETATM 2349 O O   . HOH C 2 .   ? 0.825   -6.533  16.241 1.00 41.38 ? 257 HOH A O   1 
HETATM 2350 O O   . HOH C 2 .   ? 13.634  23.843  25.144 1.00 25.36 ? 258 HOH A O   1 
HETATM 2351 O O   . HOH C 2 .   ? 6.712   28.958  25.369 1.00 38.21 ? 259 HOH A O   1 
HETATM 2352 O O   . HOH C 2 .   ? -3.878  -4.851  27.088 1.00 39.02 ? 260 HOH A O   1 
HETATM 2353 O O   . HOH C 2 .   ? -5.683  -3.754  32.128 1.00 44.72 ? 261 HOH A O   1 
HETATM 2354 O O   . HOH C 2 .   ? 24.459  20.243  32.351 1.00 38.45 ? 262 HOH A O   1 
HETATM 2355 O O   . HOH C 2 .   ? 19.005  -9.712  35.951 1.00 42.03 ? 263 HOH A O   1 
HETATM 2356 O O   . HOH C 2 .   ? 2.858   -12.909 33.014 1.00 41.56 ? 264 HOH A O   1 
HETATM 2357 O O   . HOH C 2 .   ? 17.160  18.587  43.145 1.00 42.09 ? 265 HOH A O   1 
HETATM 2358 O O   . HOH C 2 .   ? 19.195  9.801   40.591 1.00 41.21 ? 266 HOH A O   1 
HETATM 2359 O O   . HOH C 2 .   ? 16.297  12.264  23.732 1.00 27.29 ? 267 HOH A O   1 
HETATM 2360 O O   . HOH C 2 .   ? 5.686   33.631  31.497 1.00 49.22 ? 268 HOH A O   1 
HETATM 2361 O O   . HOH C 2 .   ? -2.757  20.013  30.914 1.00 43.02 ? 269 HOH A O   1 
HETATM 2362 O O   . HOH C 2 .   ? -3.428  -9.205  36.246 1.00 43.98 ? 270 HOH A O   1 
HETATM 2363 O O   . HOH C 2 .   ? 11.418  -11.738 26.710 1.00 39.42 ? 271 HOH A O   1 
HETATM 2364 O O   . HOH C 2 .   ? 17.932  32.926  30.225 1.00 40.03 ? 272 HOH A O   1 
HETATM 2365 O O   . HOH C 2 .   ? 6.154   -10.943 22.089 1.00 38.66 ? 273 HOH A O   1 
HETATM 2366 O O   . HOH C 2 .   ? 7.782   20.949  45.712 1.00 30.80 ? 274 HOH A O   1 
HETATM 2367 O O   . HOH C 2 .   ? -0.297  -11.546 36.751 1.00 45.84 ? 275 HOH A O   1 
HETATM 2368 O O   . HOH C 2 .   ? 10.992  -1.860  34.862 1.00 26.07 ? 276 HOH A O   1 
HETATM 2369 O O   . HOH C 2 .   ? 8.426   18.124  20.423 1.00 35.17 ? 277 HOH A O   1 
HETATM 2370 O O   . HOH C 2 .   ? 9.594   2.140   29.502 1.00 39.08 ? 278 HOH A O   1 
HETATM 2371 O O   . HOH C 2 .   ? 17.069  8.694   27.591 1.00 40.85 ? 279 HOH A O   1 
HETATM 2372 O O   . HOH C 2 .   ? 0.886   20.074  13.036 1.00 39.08 ? 280 HOH A O   1 
HETATM 2373 O O   . HOH C 2 .   ? -1.651  -5.527  20.992 1.00 42.68 ? 281 HOH A O   1 
HETATM 2374 O O   . HOH C 2 .   ? 10.087  20.713  47.559 1.00 36.70 ? 282 HOH A O   1 
HETATM 2375 O O   . HOH C 2 .   ? 8.839   -6.487  22.455 1.00 42.07 ? 283 HOH A O   1 
HETATM 2376 O O   . HOH C 2 .   ? 10.673  11.375  46.208 1.00 50.11 ? 284 HOH A O   1 
HETATM 2377 O O   . HOH C 2 .   ? 15.247  23.587  22.828 1.00 28.41 ? 285 HOH A O   1 
HETATM 2378 O O   . HOH C 2 .   ? 23.574  24.163  31.157 1.00 30.48 ? 286 HOH A O   1 
HETATM 2379 O O   . HOH C 2 .   ? 17.538  8.318   41.254 1.00 61.36 ? 287 HOH A O   1 
HETATM 2380 O O   . HOH C 2 .   ? -5.062  14.400  13.616 1.00 44.12 ? 288 HOH A O   1 
HETATM 2381 O O   . HOH C 2 .   ? 12.472  13.939  19.666 1.00 51.28 ? 289 HOH A O   1 
HETATM 2382 O O   . HOH C 2 .   ? 8.844   16.614  15.162 1.00 40.61 ? 290 HOH A O   1 
HETATM 2383 O O   . HOH C 2 .   ? 17.983  10.092  24.804 1.00 38.28 ? 291 HOH A O   1 
HETATM 2384 O O   . HOH C 2 .   ? -5.638  2.618   30.357 1.00 54.76 ? 292 HOH A O   1 
HETATM 2385 O O   . HOH C 2 .   ? 0.624   -10.452 17.685 1.00 58.86 ? 293 HOH A O   1 
HETATM 2386 O O   . HOH C 2 .   ? 0.148   15.267  39.169 1.00 48.00 ? 294 HOH A O   1 
HETATM 2387 O O   . HOH C 2 .   ? 4.358   -1.139  44.312 1.00 43.82 ? 295 HOH A O   1 
HETATM 2388 O O   . HOH C 2 .   ? 22.658  9.697   32.662 1.00 54.65 ? 296 HOH A O   1 
HETATM 2389 O O   . HOH C 2 .   ? 17.674  20.988  45.039 1.00 35.85 ? 297 HOH A O   1 
HETATM 2390 O O   . HOH C 2 .   ? 23.408  32.597  24.908 1.00 55.80 ? 298 HOH A O   1 
HETATM 2391 O O   . HOH C 2 .   ? 14.980  33.979  37.445 1.00 40.33 ? 299 HOH A O   1 
HETATM 2392 O O   . HOH C 2 .   ? 16.453  -1.784  34.763 1.00 50.28 ? 300 HOH A O   1 
HETATM 2393 O O   . HOH C 2 .   ? -4.031  -6.087  40.047 1.00 39.56 ? 301 HOH A O   1 
HETATM 2394 O O   . HOH C 2 .   ? 9.890   28.758  39.875 1.00 30.95 ? 302 HOH A O   1 
HETATM 2395 O O   . HOH C 2 .   ? -1.791  -5.375  43.029 1.00 40.07 ? 303 HOH A O   1 
HETATM 2396 O O   . HOH C 2 .   ? 14.420  -10.829 27.080 1.00 40.47 ? 304 HOH A O   1 
HETATM 2397 O O   . HOH C 2 .   ? 12.944  32.984  37.328 1.00 36.09 ? 305 HOH A O   1 
HETATM 2398 O O   . HOH C 2 .   ? -0.741  14.594  41.595 1.00 55.68 ? 306 HOH A O   1 
HETATM 2399 O O   . HOH C 2 .   ? -5.195  -4.802  29.810 1.00 44.03 ? 307 HOH A O   1 
HETATM 2400 O O   . HOH C 2 .   ? -2.704  20.447  15.903 1.00 51.94 ? 308 HOH A O   1 
HETATM 2401 O O   . HOH C 2 .   ? 26.419  24.903  39.174 1.00 52.40 ? 309 HOH A O   1 
HETATM 2402 O O   . HOH C 2 .   ? 4.841   -11.220 19.352 1.00 50.69 ? 310 HOH A O   1 
HETATM 2403 O O   . HOH C 2 .   ? 11.552  -4.551  24.689 1.00 57.67 ? 311 HOH A O   1 
HETATM 2404 O O   . HOH C 2 .   ? 11.192  4.155   30.007 1.00 39.60 ? 312 HOH A O   1 
HETATM 2405 O O   . HOH C 2 .   ? 5.201   -11.380 34.632 1.00 56.74 ? 313 HOH A O   1 
HETATM 2406 O O   . HOH C 2 .   ? 1.031   25.766  24.574 1.00 40.89 ? 314 HOH A O   1 
HETATM 2407 O O   . HOH C 2 .   ? -4.870  -9.279  34.041 1.00 50.23 ? 315 HOH A O   1 
HETATM 2408 O O   . HOH C 2 .   ? 0.030   21.575  39.095 1.00 39.10 ? 316 HOH A O   1 
HETATM 2409 O O   . HOH C 2 .   ? -2.428  21.676  33.163 1.00 54.48 ? 317 HOH A O   1 
HETATM 2410 O O   . HOH C 2 .   ? 16.456  21.650  21.470 1.00 35.87 ? 318 HOH A O   1 
HETATM 2411 O O   . HOH C 2 .   ? 10.298  20.293  19.191 1.00 48.69 ? 319 HOH A O   1 
HETATM 2412 O O   . HOH C 2 .   ? 1.988   -11.332 43.554 1.00 55.15 ? 320 HOH A O   1 
HETATM 2413 O O   . HOH C 2 .   ? 12.861  1.907   41.984 1.00 45.78 ? 321 HOH A O   1 
HETATM 2414 O O   . HOH C 2 .   ? 16.855  12.433  20.753 1.00 42.73 ? 322 HOH A O   1 
HETATM 2415 O O   . HOH C 2 .   ? -1.004  24.533  39.208 1.00 41.64 ? 323 HOH A O   1 
HETATM 2416 O O   . HOH C 2 .   ? 21.434  24.069  45.168 1.00 50.21 ? 324 HOH A O   1 
HETATM 2417 O O   . HOH C 2 .   ? 13.379  0.276   29.349 1.00 40.08 ? 325 HOH A O   1 
HETATM 2418 O O   . HOH C 2 .   ? 29.462  21.624  35.822 1.00 53.06 ? 326 HOH A O   1 
HETATM 2419 O O   . HOH C 2 .   ? 17.768  1.920   35.181 1.00 47.37 ? 327 HOH A O   1 
HETATM 2420 O O   . HOH C 2 .   ? 0.860   28.550  39.890 1.00 42.73 ? 328 HOH A O   1 
HETATM 2421 O O   . HOH C 2 .   ? 12.665  4.511   42.882 1.00 43.92 ? 329 HOH A O   1 
HETATM 2422 O O   . HOH C 2 .   ? -0.849  -6.882  17.943 1.00 51.66 ? 330 HOH A O   1 
HETATM 2423 O O   . HOH C 2 .   ? 21.873  10.144  40.706 1.00 50.37 ? 331 HOH A O   1 
HETATM 2424 O O   . HOH C 2 .   ? 0.110   27.419  35.771 1.00 38.87 ? 332 HOH A O   1 
HETATM 2425 O O   . HOH C 2 .   ? 0.305   30.172  35.908 1.00 48.26 ? 333 HOH A O   1 
HETATM 2426 O O   . HOH C 2 .   ? 10.067  2.971   26.804 1.00 40.39 ? 334 HOH A O   1 
HETATM 2427 O O   . HOH C 2 .   ? 12.153  21.479  20.149 1.00 49.23 ? 335 HOH A O   1 
HETATM 2428 O O   . HOH C 2 .   ? -2.218  -10.792 23.602 1.00 51.60 ? 336 HOH A O   1 
HETATM 2429 O O   . HOH C 2 .   ? 16.621  5.203   43.250 1.00 54.65 ? 337 HOH A O   1 
HETATM 2430 O O   . HOH C 2 .   ? 11.581  16.188  19.017 1.00 53.53 ? 338 HOH A O   1 
HETATM 2431 O O   . HOH C 2 .   ? 14.757  -0.322  27.363 1.00 53.91 ? 339 HOH A O   1 
HETATM 2432 O O   . HOH C 2 .   ? 9.560   18.761  49.376 1.00 56.23 ? 340 HOH A O   1 
HETATM 2433 O O   . HOH D 2 .   ? -11.297 35.265  6.484  1.00 37.68 ? 201 HOH B O   1 
HETATM 2434 O O   . HOH D 2 .   ? -5.435  21.553  16.522 1.00 47.16 ? 202 HOH B O   1 
HETATM 2435 O O   . HOH D 2 .   ? 2.067   -10.682 8.276  1.00 35.93 ? 203 HOH B O   1 
HETATM 2436 O O   . HOH D 2 .   ? 7.743   -4.744  14.271 1.00 38.93 ? 204 HOH B O   1 
HETATM 2437 O O   . HOH D 2 .   ? 2.182   22.402  -0.135 1.00 44.35 ? 205 HOH B O   1 
HETATM 2438 O O   . HOH D 2 .   ? -4.215  16.650  -2.253 1.00 35.16 ? 206 HOH B O   1 
HETATM 2439 O O   . HOH D 2 .   ? -12.494 32.473  16.320 1.00 37.77 ? 207 HOH B O   1 
HETATM 2440 O O   . HOH D 2 .   ? -2.079  17.411  -0.648 1.00 29.81 ? 208 HOH B O   1 
HETATM 2441 O O   . HOH D 2 .   ? -4.096  34.617  11.539 1.00 27.27 ? 209 HOH B O   1 
HETATM 2442 O O   . HOH D 2 .   ? -2.281  32.122  17.236 1.00 39.71 ? 210 HOH B O   1 
HETATM 2443 O O   . HOH D 2 .   ? -14.815 2.940   10.580 1.00 55.60 ? 211 HOH B O   1 
HETATM 2444 O O   . HOH D 2 .   ? 9.413   0.548   10.148 1.00 26.71 ? 212 HOH B O   1 
HETATM 2445 O O   . HOH D 2 .   ? -1.444  23.649  9.736  1.00 26.21 ? 213 HOH B O   1 
HETATM 2446 O O   . HOH D 2 .   ? 5.752   30.586  10.564 1.00 52.92 ? 214 HOH B O   1 
HETATM 2447 O O   . HOH D 2 .   ? 1.016   18.158  -1.850 1.00 37.33 ? 215 HOH B O   1 
HETATM 2448 O O   . HOH D 2 .   ? -2.822  7.794   -8.756 1.00 43.88 ? 216 HOH B O   1 
HETATM 2449 O O   . HOH D 2 .   ? 5.550   -9.648  6.786  1.00 39.45 ? 217 HOH B O   1 
HETATM 2450 O O   . HOH D 2 .   ? -8.093  23.344  6.643  1.00 27.27 ? 218 HOH B O   1 
HETATM 2451 O O   . HOH D 2 .   ? -8.163  6.882   -3.723 1.00 39.23 ? 219 HOH B O   1 
HETATM 2452 O O   . HOH D 2 .   ? 3.170   -3.462  15.766 1.00 29.15 ? 220 HOH B O   1 
HETATM 2453 O O   . HOH D 2 .   ? -11.471 5.078   -3.823 1.00 49.96 ? 221 HOH B O   1 
HETATM 2454 O O   . HOH D 2 .   ? -11.324 21.325  12.024 1.00 36.25 ? 222 HOH B O   1 
HETATM 2455 O O   . HOH D 2 .   ? -6.020  -0.807  -2.475 1.00 32.99 ? 223 HOH B O   1 
HETATM 2456 O O   . HOH D 2 .   ? 9.887   -2.799  -4.641 1.00 38.32 ? 224 HOH B O   1 
HETATM 2457 O O   . HOH D 2 .   ? -12.097 -2.736  1.864  1.00 41.70 ? 225 HOH B O   1 
HETATM 2458 O O   . HOH D 2 .   ? 8.560   15.338  4.868  1.00 43.46 ? 226 HOH B O   1 
HETATM 2459 O O   . HOH D 2 .   ? -2.412  20.968  10.817 1.00 38.36 ? 227 HOH B O   1 
HETATM 2460 O O   . HOH D 2 .   ? 3.071   20.235  4.697  1.00 29.65 ? 228 HOH B O   1 
HETATM 2461 O O   . HOH D 2 .   ? 9.524   12.854  15.909 1.00 45.42 ? 229 HOH B O   1 
HETATM 2462 O O   . HOH D 2 .   ? 0.151   -11.591 5.736  1.00 42.22 ? 230 HOH B O   1 
HETATM 2463 O O   . HOH D 2 .   ? 11.972  2.977   4.096  1.00 39.53 ? 231 HOH B O   1 
HETATM 2464 O O   . HOH D 2 .   ? -2.556  28.608  15.984 1.00 31.06 ? 232 HOH B O   1 
HETATM 2465 O O   . HOH D 2 .   ? -6.749  -3.108  20.777 1.00 50.31 ? 233 HOH B O   1 
HETATM 2466 O O   . HOH D 2 .   ? -12.915 3.585   4.406  1.00 35.43 ? 234 HOH B O   1 
HETATM 2467 O O   . HOH D 2 .   ? 10.830  5.401   -1.959 1.00 45.01 ? 235 HOH B O   1 
HETATM 2468 O O   . HOH D 2 .   ? -12.482 30.928  -1.361 1.00 34.12 ? 236 HOH B O   1 
HETATM 2469 O O   . HOH D 2 .   ? 10.775  -3.897  5.696  1.00 30.46 ? 237 HOH B O   1 
HETATM 2470 O O   . HOH D 2 .   ? 5.108   3.600   -3.953 1.00 47.67 ? 238 HOH B O   1 
HETATM 2471 O O   . HOH D 2 .   ? -0.935  35.106  13.465 1.00 36.07 ? 239 HOH B O   1 
HETATM 2472 O O   . HOH D 2 .   ? 0.034   -7.458  10.892 1.00 30.24 ? 240 HOH B O   1 
HETATM 2473 O O   . HOH D 2 .   ? -12.803 27.824  20.690 1.00 38.12 ? 241 HOH B O   1 
HETATM 2474 O O   . HOH D 2 .   ? 7.469   5.846   17.093 1.00 41.99 ? 242 HOH B O   1 
HETATM 2475 O O   . HOH D 2 .   ? -6.751  37.172  17.796 1.00 42.47 ? 243 HOH B O   1 
HETATM 2476 O O   . HOH D 2 .   ? -8.561  37.201  13.864 1.00 46.21 ? 244 HOH B O   1 
HETATM 2477 O O   . HOH D 2 .   ? -15.818 13.695  4.576  1.00 55.62 ? 245 HOH B O   1 
HETATM 2478 O O   . HOH D 2 .   ? -9.992  35.692  8.894  1.00 37.20 ? 246 HOH B O   1 
HETATM 2479 O O   . HOH D 2 .   ? 5.305   10.424  14.704 1.00 24.69 ? 247 HOH B O   1 
HETATM 2480 O O   . HOH D 2 .   ? 5.327   33.435  3.180  1.00 42.22 ? 248 HOH B O   1 
HETATM 2481 O O   . HOH D 2 .   ? 9.434   11.999  -1.174 1.00 48.64 ? 249 HOH B O   1 
HETATM 2482 O O   . HOH D 2 .   ? 2.053   19.889  8.035  1.00 43.32 ? 250 HOH B O   1 
HETATM 2483 O O   . HOH D 2 .   ? -4.302  -6.322  13.857 1.00 43.57 ? 251 HOH B O   1 
HETATM 2484 O O   . HOH D 2 .   ? -8.092  32.327  5.461  1.00 39.21 ? 252 HOH B O   1 
HETATM 2485 O O   . HOH D 2 .   ? -13.858 33.367  14.064 1.00 38.86 ? 253 HOH B O   1 
HETATM 2486 O O   . HOH D 2 .   ? -2.703  23.632  -1.273 1.00 31.99 ? 254 HOH B O   1 
HETATM 2487 O O   . HOH D 2 .   ? -4.523  19.971  14.017 1.00 43.27 ? 255 HOH B O   1 
HETATM 2488 O O   . HOH D 2 .   ? 6.879   5.245   -2.848 1.00 40.25 ? 256 HOH B O   1 
HETATM 2489 O O   . HOH D 2 .   ? -1.440  10.887  -6.749 1.00 33.89 ? 257 HOH B O   1 
HETATM 2490 O O   . HOH D 2 .   ? 1.199   -11.228 2.214  1.00 40.73 ? 258 HOH B O   1 
HETATM 2491 O O   . HOH D 2 .   ? -12.436 16.515  -1.035 1.00 58.33 ? 259 HOH B O   1 
HETATM 2492 O O   . HOH D 2 .   ? 3.440   25.580  4.324  1.00 50.46 ? 260 HOH B O   1 
HETATM 2493 O O   . HOH D 2 .   ? -1.790  25.281  5.534  1.00 26.20 ? 261 HOH B O   1 
HETATM 2494 O O   . HOH D 2 .   ? -8.477  -1.174  16.383 1.00 44.92 ? 262 HOH B O   1 
HETATM 2495 O O   . HOH D 2 .   ? -2.573  29.263  18.680 1.00 38.63 ? 263 HOH B O   1 
HETATM 2496 O O   . HOH D 2 .   ? -8.260  -8.754  2.148  1.00 51.79 ? 264 HOH B O   1 
HETATM 2497 O O   . HOH D 2 .   ? -2.098  11.263  17.264 1.00 49.24 ? 265 HOH B O   1 
HETATM 2498 O O   . HOH D 2 .   ? -11.191 -2.440  8.453  1.00 40.86 ? 266 HOH B O   1 
HETATM 2499 O O   . HOH D 2 .   ? 3.127   5.325   -4.648 1.00 43.94 ? 267 HOH B O   1 
HETATM 2500 O O   . HOH D 2 .   ? -2.841  14.465  15.379 1.00 47.26 ? 268 HOH B O   1 
HETATM 2501 O O   . HOH D 2 .   ? -4.443  3.317   -8.106 1.00 31.61 ? 269 HOH B O   1 
HETATM 2502 O O   . HOH D 2 .   ? 4.913   -3.706  -5.343 1.00 34.82 ? 270 HOH B O   1 
HETATM 2503 O O   . HOH D 2 .   ? 12.134  -2.067  -2.624 1.00 37.65 ? 271 HOH B O   1 
HETATM 2504 O O   . HOH D 2 .   ? -6.666  2.977   -5.889 1.00 32.82 ? 272 HOH B O   1 
HETATM 2505 O O   . HOH D 2 .   ? -0.550  -9.361  1.036  1.00 31.19 ? 273 HOH B O   1 
HETATM 2506 O O   . HOH D 2 .   ? -5.179  33.810  19.005 1.00 35.81 ? 274 HOH B O   1 
HETATM 2507 O O   . HOH D 2 .   ? -6.547  15.750  -4.727 1.00 49.77 ? 275 HOH B O   1 
HETATM 2508 O O   . HOH D 2 .   ? -13.961 20.403  15.296 1.00 57.97 ? 276 HOH B O   1 
HETATM 2509 O O   . HOH D 2 .   ? 1.932   34.400  12.741 1.00 38.40 ? 277 HOH B O   1 
HETATM 2510 O O   . HOH D 2 .   ? -15.529 28.205  -0.772 1.00 43.49 ? 278 HOH B O   1 
HETATM 2511 O O   . HOH D 2 .   ? -13.107 8.163   1.949  1.00 45.96 ? 279 HOH B O   1 
HETATM 2512 O O   . HOH D 2 .   ? -14.173 10.273  7.811  1.00 45.26 ? 280 HOH B O   1 
HETATM 2513 O O   . HOH D 2 .   ? 11.230  -1.007  5.693  1.00 34.68 ? 281 HOH B O   1 
HETATM 2514 O O   . HOH D 2 .   ? 3.730   16.067  -2.125 1.00 45.44 ? 282 HOH B O   1 
HETATM 2515 O O   . HOH D 2 .   ? -17.506 28.801  2.149  1.00 47.14 ? 283 HOH B O   1 
HETATM 2516 O O   . HOH D 2 .   ? 5.460   34.061  7.844  1.00 46.13 ? 284 HOH B O   1 
HETATM 2517 O O   . HOH D 2 .   ? -7.493  25.813  26.145 1.00 47.92 ? 285 HOH B O   1 
HETATM 2518 O O   . HOH D 2 .   ? -3.812  12.713  -6.290 1.00 46.10 ? 286 HOH B O   1 
HETATM 2519 O O   . HOH D 2 .   ? -9.575  24.458  25.339 1.00 35.80 ? 287 HOH B O   1 
HETATM 2520 O O   . HOH D 2 .   ? 3.226   2.835   -6.860 1.00 35.84 ? 288 HOH B O   1 
HETATM 2521 O O   . HOH D 2 .   ? -1.824  4.054   19.082 1.00 37.68 ? 289 HOH B O   1 
HETATM 2522 O O   . HOH D 2 .   ? 12.304  7.618   16.585 1.00 57.09 ? 290 HOH B O   1 
HETATM 2523 O O   . HOH D 2 .   ? 2.639   26.490  0.046  1.00 45.51 ? 291 HOH B O   1 
HETATM 2524 O O   . HOH D 2 .   ? -11.800 25.132  23.605 1.00 41.40 ? 292 HOH B O   1 
HETATM 2525 O O   . HOH D 2 .   ? -13.529 33.989  5.028  1.00 44.99 ? 293 HOH B O   1 
HETATM 2526 O O   . HOH D 2 .   ? -5.628  -4.236  18.143 1.00 52.99 ? 294 HOH B O   1 
HETATM 2527 O O   . HOH D 2 .   ? -12.752 34.129  -1.244 1.00 57.39 ? 295 HOH B O   1 
HETATM 2528 O O   . HOH D 2 .   ? -1.670  37.547  12.620 1.00 46.26 ? 296 HOH B O   1 
HETATM 2529 O O   . HOH D 2 .   ? 13.168  0.169   3.740  1.00 50.79 ? 297 HOH B O   1 
HETATM 2530 O O   . HOH D 2 .   ? -4.799  15.441  -6.694 1.00 62.36 ? 298 HOH B O   1 
HETATM 2531 O O   . HOH D 2 .   ? -8.684  23.539  28.849 1.00 34.37 ? 299 HOH B O   1 
HETATM 2532 O O   . HOH D 2 .   ? -0.729  21.859  -1.828 1.00 39.98 ? 300 HOH B O   1 
HETATM 2533 O O   . HOH D 2 .   ? 6.485   10.136  17.184 1.00 32.59 ? 301 HOH B O   1 
HETATM 2534 O O   . HOH D 2 .   ? 7.118   19.170  2.022  1.00 51.26 ? 302 HOH B O   1 
HETATM 2535 O O   . HOH D 2 .   ? 13.176  -1.887  9.517  1.00 60.71 ? 303 HOH B O   1 
HETATM 2536 O O   . HOH D 2 .   ? 7.757   13.466  -2.996 1.00 50.89 ? 304 HOH B O   1 
HETATM 2537 O O   . HOH D 2 .   ? -7.596  35.228  7.489  1.00 59.63 ? 305 HOH B O   1 
HETATM 2538 O O   . HOH D 2 .   ? -0.978  19.010  -2.815 1.00 41.96 ? 306 HOH B O   1 
HETATM 2539 O O   . HOH D 2 .   ? -6.282  14.865  16.276 1.00 49.56 ? 307 HOH B O   1 
HETATM 2540 O O   . HOH D 2 .   ? 1.322   23.430  10.300 1.00 45.72 ? 308 HOH B O   1 
HETATM 2541 O O   . HOH D 2 .   ? 11.088  -0.074  8.073  1.00 41.79 ? 309 HOH B O   1 
HETATM 2542 O O   . HOH D 2 .   ? -1.128  -12.682 3.365  1.00 50.05 ? 310 HOH B O   1 
HETATM 2543 O O   . HOH D 2 .   ? -0.754  34.950  16.057 1.00 49.34 ? 311 HOH B O   1 
HETATM 2544 O O   . HOH D 2 .   ? 8.672   11.187  18.234 1.00 52.34 ? 312 HOH B O   1 
HETATM 2545 O O   . HOH D 2 .   ? -14.074 35.231  0.487  1.00 46.11 ? 313 HOH B O   1 
HETATM 2546 O O   . HOH D 2 .   ? -2.616  32.511  19.405 1.00 53.90 ? 314 HOH B O   1 
HETATM 2547 O O   . HOH D 2 .   ? -4.041  23.382  -3.412 1.00 46.70 ? 315 HOH B O   1 
HETATM 2548 O O   . HOH D 2 .   ? -14.179 33.488  18.557 1.00 50.72 ? 316 HOH B O   1 
HETATM 2549 O O   . HOH D 2 .   ? 3.298   24.776  12.954 1.00 64.38 ? 317 HOH B O   1 
HETATM 2550 O O   . HOH D 2 .   ? 8.894   18.057  3.497  1.00 55.54 ? 318 HOH B O   1 
HETATM 2551 O O   . HOH D 2 .   ? -15.342 2.586   5.961  1.00 52.23 ? 319 HOH B O   1 
HETATM 2552 O O   . HOH D 2 .   ? 12.963  -4.618  7.574  1.00 56.61 ? 320 HOH B O   1 
# 
