data_9FOV
# 
_entry.id   9FOV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FOV         pdb_00009fov 10.2210/pdb9fov/pdb 
WWPDB D_1292139323 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FOV 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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              hermann.schindelin@uni-wuerzburg.de 
_pdbx_contact_author.name_first         Hermann 
_pdbx_contact_author.name_last          Schindelin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2067-3187 
# 
_audit_author.name               'Schindelin, H.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-2067-3187 
# 
_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 Tryparedoxin from Trypanosoma cruzi' 
_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               'Schindelin, H.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-2067-3187 
# 
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 'Tryparedoxin, putative' 16237.395 2   ? ? ? ? 
2 non-polymer syn GLYCEROL                 92.094    1   ? ? ? ? 
3 water       nat water                    18.015    387 ? ? ? ? 
# 
_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       
;GAMGSGLAKYLPSTIKLVSKSGTVSPISLAGKTVFFYFSASWCPPCRGFTPTLVEFYEKFRESKNFEVVLVTWDDEEEAY
NGYFAKMPWLAIPFSSRAELEALRSTFGVETIPTVIAVNADTGAVVSTKGRERLLTDPEGKNFPWSD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMGSGLAKYLPSTIKLVSKSGTVSPISLAGKTVFFYFSASWCPPCRGFTPTLVEFYEKFRESKNFEVVLVTWDDEEEAY
NGYFAKMPWLAIPFSSRAELEALRSTFGVETIPTVIAVNADTGAVVSTKGRERLLTDPEGKNFPWSD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   GLY n 
1 7   LEU n 
1 8   ALA n 
1 9   LYS n 
1 10  TYR n 
1 11  LEU n 
1 12  PRO n 
1 13  SER n 
1 14  THR n 
1 15  ILE n 
1 16  LYS n 
1 17  LEU n 
1 18  VAL n 
1 19  SER n 
1 20  LYS n 
1 21  SER n 
1 22  GLY n 
1 23  THR n 
1 24  VAL n 
1 25  SER n 
1 26  PRO n 
1 27  ILE n 
1 28  SER n 
1 29  LEU n 
1 30  ALA n 
1 31  GLY n 
1 32  LYS n 
1 33  THR n 
1 34  VAL n 
1 35  PHE n 
1 36  PHE n 
1 37  TYR n 
1 38  PHE n 
1 39  SER n 
1 40  ALA n 
1 41  SER n 
1 42  TRP n 
1 43  CYS n 
1 44  PRO n 
1 45  PRO n 
1 46  CYS n 
1 47  ARG n 
1 48  GLY n 
1 49  PHE n 
1 50  THR n 
1 51  PRO n 
1 52  THR n 
1 53  LEU n 
1 54  VAL n 
1 55  GLU n 
1 56  PHE n 
1 57  TYR n 
1 58  GLU n 
1 59  LYS n 
1 60  PHE n 
1 61  ARG n 
1 62  GLU n 
1 63  SER n 
1 64  LYS n 
1 65  ASN n 
1 66  PHE n 
1 67  GLU n 
1 68  VAL n 
1 69  VAL n 
1 70  LEU n 
1 71  VAL n 
1 72  THR n 
1 73  TRP n 
1 74  ASP n 
1 75  ASP n 
1 76  GLU n 
1 77  GLU n 
1 78  GLU n 
1 79  ALA n 
1 80  TYR n 
1 81  ASN n 
1 82  GLY n 
1 83  TYR n 
1 84  PHE n 
1 85  ALA n 
1 86  LYS n 
1 87  MET n 
1 88  PRO n 
1 89  TRP n 
1 90  LEU n 
1 91  ALA n 
1 92  ILE n 
1 93  PRO n 
1 94  PHE n 
1 95  SER n 
1 96  SER n 
1 97  ARG n 
1 98  ALA n 
1 99  GLU n 
1 100 LEU n 
1 101 GLU n 
1 102 ALA n 
1 103 LEU n 
1 104 ARG n 
1 105 SER n 
1 106 THR n 
1 107 PHE n 
1 108 GLY n 
1 109 VAL n 
1 110 GLU n 
1 111 THR n 
1 112 ILE n 
1 113 PRO n 
1 114 THR n 
1 115 VAL n 
1 116 ILE n 
1 117 ALA n 
1 118 VAL n 
1 119 ASN n 
1 120 ALA n 
1 121 ASP n 
1 122 THR n 
1 123 GLY n 
1 124 ALA n 
1 125 VAL n 
1 126 VAL n 
1 127 SER n 
1 128 THR n 
1 129 LYS n 
1 130 GLY n 
1 131 ARG n 
1 132 GLU n 
1 133 ARG n 
1 134 LEU n 
1 135 LEU n 
1 136 THR n 
1 137 ASP n 
1 138 PRO n 
1 139 GLU n 
1 140 GLY n 
1 141 LYS n 
1 142 ASN n 
1 143 PHE n 
1 144 PRO n 
1 145 TRP n 
1 146 SER n 
1 147 ASP 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                   147 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Tc00.1047053509997.30 
_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      'Trypanosoma cruzi' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5693 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   ALA 2   -1  -1  ALA ALA A . n 
A 1 3   MET 3   0   0   MET MET A . n 
A 1 4   GLY 4   1   1   GLY GLY A . n 
A 1 5   SER 5   2   2   SER SER A . n 
A 1 6   GLY 6   3   3   GLY GLY A . n 
A 1 7   LEU 7   4   4   LEU LEU A . n 
A 1 8   ALA 8   5   5   ALA ALA A . n 
A 1 9   LYS 9   6   6   LYS LYS A . n 
A 1 10  TYR 10  7   7   TYR TYR A . n 
A 1 11  LEU 11  8   8   LEU LEU A . n 
A 1 12  PRO 12  9   9   PRO PRO A . n 
A 1 13  SER 13  10  10  SER SER A . n 
A 1 14  THR 14  11  11  THR THR A . n 
A 1 15  ILE 15  12  12  ILE ILE A . n 
A 1 16  LYS 16  13  13  LYS LYS A . n 
A 1 17  LEU 17  14  14  LEU LEU A . n 
A 1 18  VAL 18  15  15  VAL VAL A . n 
A 1 19  SER 19  16  16  SER SER A . n 
A 1 20  LYS 20  17  17  LYS LYS A . n 
A 1 21  SER 21  18  18  SER SER A . n 
A 1 22  GLY 22  19  19  GLY GLY A . n 
A 1 23  THR 23  20  20  THR THR A . n 
A 1 24  VAL 24  21  21  VAL VAL A . n 
A 1 25  SER 25  22  22  SER SER A . n 
A 1 26  PRO 26  23  23  PRO PRO A . n 
A 1 27  ILE 27  24  24  ILE ILE A . n 
A 1 28  SER 28  25  25  SER SER A . n 
A 1 29  LEU 29  26  26  LEU LEU A . n 
A 1 30  ALA 30  27  27  ALA ALA A . n 
A 1 31  GLY 31  28  28  GLY GLY A . n 
A 1 32  LYS 32  29  29  LYS LYS A . n 
A 1 33  THR 33  30  30  THR THR A . n 
A 1 34  VAL 34  31  31  VAL VAL A . n 
A 1 35  PHE 35  32  32  PHE PHE A . n 
A 1 36  PHE 36  33  33  PHE PHE A . n 
A 1 37  TYR 37  34  34  TYR TYR A . n 
A 1 38  PHE 38  35  35  PHE PHE A . n 
A 1 39  SER 39  36  36  SER SER A . n 
A 1 40  ALA 40  37  37  ALA ALA A . n 
A 1 41  SER 41  38  38  SER SER A . n 
A 1 42  TRP 42  39  39  TRP TRP A . n 
A 1 43  CYS 43  40  40  CYS CYS A . n 
A 1 44  PRO 44  41  41  PRO PRO A . n 
A 1 45  PRO 45  42  42  PRO PRO A . n 
A 1 46  CYS 46  43  43  CYS CYS A . n 
A 1 47  ARG 47  44  44  ARG ARG A . n 
A 1 48  GLY 48  45  45  GLY GLY A . n 
A 1 49  PHE 49  46  46  PHE PHE A . n 
A 1 50  THR 50  47  47  THR THR A . n 
A 1 51  PRO 51  48  48  PRO PRO A . n 
A 1 52  THR 52  49  49  THR THR A . n 
A 1 53  LEU 53  50  50  LEU LEU A . n 
A 1 54  VAL 54  51  51  VAL VAL A . n 
A 1 55  GLU 55  52  52  GLU GLU A . n 
A 1 56  PHE 56  53  53  PHE PHE A . n 
A 1 57  TYR 57  54  54  TYR TYR A . n 
A 1 58  GLU 58  55  55  GLU GLU A . n 
A 1 59  LYS 59  56  56  LYS LYS A . n 
A 1 60  PHE 60  57  57  PHE PHE A . n 
A 1 61  ARG 61  58  58  ARG ARG A . n 
A 1 62  GLU 62  59  59  GLU GLU A . n 
A 1 63  SER 63  60  60  SER SER A . n 
A 1 64  LYS 64  61  61  LYS LYS A . n 
A 1 65  ASN 65  62  62  ASN ASN A . n 
A 1 66  PHE 66  63  63  PHE PHE A . n 
A 1 67  GLU 67  64  64  GLU GLU A . n 
A 1 68  VAL 68  65  65  VAL VAL A . n 
A 1 69  VAL 69  66  66  VAL VAL A . n 
A 1 70  LEU 70  67  67  LEU LEU A . n 
A 1 71  VAL 71  68  68  VAL VAL A . n 
A 1 72  THR 72  69  69  THR THR A . n 
A 1 73  TRP 73  70  70  TRP TRP A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  ASP 75  72  72  ASP ASP A . n 
A 1 76  GLU 76  73  73  GLU GLU A . n 
A 1 77  GLU 77  74  74  GLU GLU A . n 
A 1 78  GLU 78  75  75  GLU GLU A . n 
A 1 79  ALA 79  76  76  ALA ALA A . n 
A 1 80  TYR 80  77  77  TYR TYR A . n 
A 1 81  ASN 81  78  78  ASN ASN A . n 
A 1 82  GLY 82  79  79  GLY GLY A . n 
A 1 83  TYR 83  80  80  TYR TYR A . n 
A 1 84  PHE 84  81  81  PHE PHE A . n 
A 1 85  ALA 85  82  82  ALA ALA A . n 
A 1 86  LYS 86  83  83  LYS LYS A . n 
A 1 87  MET 87  84  84  MET MET A . n 
A 1 88  PRO 88  85  85  PRO PRO A . n 
A 1 89  TRP 89  86  86  TRP TRP A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  ALA 91  88  88  ALA ALA A . n 
A 1 92  ILE 92  89  89  ILE ILE A . n 
A 1 93  PRO 93  90  90  PRO PRO A . n 
A 1 94  PHE 94  91  91  PHE PHE A . n 
A 1 95  SER 95  92  92  SER SER A . n 
A 1 96  SER 96  93  93  SER SER A . n 
A 1 97  ARG 97  94  94  ARG ARG A . n 
A 1 98  ALA 98  95  95  ALA ALA A . n 
A 1 99  GLU 99  96  96  GLU GLU A . n 
A 1 100 LEU 100 97  97  LEU LEU A . n 
A 1 101 GLU 101 98  98  GLU GLU A . n 
A 1 102 ALA 102 99  99  ALA ALA A . n 
A 1 103 LEU 103 100 100 LEU LEU A . n 
A 1 104 ARG 104 101 101 ARG ARG A . n 
A 1 105 SER 105 102 102 SER SER A . n 
A 1 106 THR 106 103 103 THR THR A . n 
A 1 107 PHE 107 104 104 PHE PHE A . n 
A 1 108 GLY 108 105 105 GLY GLY A . n 
A 1 109 VAL 109 106 106 VAL VAL A . n 
A 1 110 GLU 110 107 107 GLU GLU A . n 
A 1 111 THR 111 108 108 THR THR A . n 
A 1 112 ILE 112 109 109 ILE ILE A . n 
A 1 113 PRO 113 110 110 PRO PRO A . n 
A 1 114 THR 114 111 111 THR THR A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 ILE 116 113 113 ILE ILE A . n 
A 1 117 ALA 117 114 114 ALA ALA A . n 
A 1 118 VAL 118 115 115 VAL VAL A . n 
A 1 119 ASN 119 116 116 ASN ASN A . n 
A 1 120 ALA 120 117 117 ALA ALA A . n 
A 1 121 ASP 121 118 118 ASP ASP A . n 
A 1 122 THR 122 119 119 THR THR A . n 
A 1 123 GLY 123 120 120 GLY GLY A . n 
A 1 124 ALA 124 121 121 ALA ALA A . n 
A 1 125 VAL 125 122 122 VAL VAL A . n 
A 1 126 VAL 126 123 123 VAL VAL A . n 
A 1 127 SER 127 124 124 SER SER A . n 
A 1 128 THR 128 125 125 THR THR A . n 
A 1 129 LYS 129 126 126 LYS LYS A . n 
A 1 130 GLY 130 127 127 GLY GLY A . n 
A 1 131 ARG 131 128 128 ARG ARG A . n 
A 1 132 GLU 132 129 129 GLU GLU A . n 
A 1 133 ARG 133 130 130 ARG ARG A . n 
A 1 134 LEU 134 131 131 LEU LEU A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 THR 136 133 133 THR THR A . n 
A 1 137 ASP 137 134 134 ASP ASP A . n 
A 1 138 PRO 138 135 135 PRO PRO A . n 
A 1 139 GLU 139 136 136 GLU GLU A . n 
A 1 140 GLY 140 137 137 GLY GLY A . n 
A 1 141 LYS 141 138 138 LYS LYS A . n 
A 1 142 ASN 142 139 139 ASN ASN A . n 
A 1 143 PHE 143 140 140 PHE PHE A . n 
A 1 144 PRO 144 141 141 PRO PRO A . n 
A 1 145 TRP 145 142 142 TRP TRP A . n 
A 1 146 SER 146 143 143 SER SER A . n 
A 1 147 ASP 147 144 144 ASP ASP A . n 
B 1 1   GLY 1   -2  ?   ?   ?   B . n 
B 1 2   ALA 2   -1  ?   ?   ?   B . n 
B 1 3   MET 3   0   0   MET MET B . n 
B 1 4   GLY 4   1   1   GLY GLY B . n 
B 1 5   SER 5   2   2   SER SER B . n 
B 1 6   GLY 6   3   3   GLY GLY B . n 
B 1 7   LEU 7   4   4   LEU LEU B . n 
B 1 8   ALA 8   5   5   ALA ALA B . n 
B 1 9   LYS 9   6   6   LYS LYS B . n 
B 1 10  TYR 10  7   7   TYR TYR B . n 
B 1 11  LEU 11  8   8   LEU LEU B . n 
B 1 12  PRO 12  9   9   PRO PRO B . n 
B 1 13  SER 13  10  10  SER SER B . n 
B 1 14  THR 14  11  11  THR THR B . n 
B 1 15  ILE 15  12  12  ILE ILE B . n 
B 1 16  LYS 16  13  13  LYS LYS B . n 
B 1 17  LEU 17  14  14  LEU LEU B . n 
B 1 18  VAL 18  15  15  VAL VAL B . n 
B 1 19  SER 19  16  16  SER SER B . n 
B 1 20  LYS 20  17  17  LYS LYS B . n 
B 1 21  SER 21  18  18  SER SER B . n 
B 1 22  GLY 22  19  19  GLY GLY B . n 
B 1 23  THR 23  20  20  THR THR B . n 
B 1 24  VAL 24  21  21  VAL VAL B . n 
B 1 25  SER 25  22  22  SER SER B . n 
B 1 26  PRO 26  23  23  PRO PRO B . n 
B 1 27  ILE 27  24  24  ILE ILE B . n 
B 1 28  SER 28  25  25  SER SER B . n 
B 1 29  LEU 29  26  26  LEU LEU B . n 
B 1 30  ALA 30  27  27  ALA ALA B . n 
B 1 31  GLY 31  28  28  GLY GLY B . n 
B 1 32  LYS 32  29  29  LYS LYS B . n 
B 1 33  THR 33  30  30  THR THR B . n 
B 1 34  VAL 34  31  31  VAL VAL B . n 
B 1 35  PHE 35  32  32  PHE PHE B . n 
B 1 36  PHE 36  33  33  PHE PHE B . n 
B 1 37  TYR 37  34  34  TYR TYR B . n 
B 1 38  PHE 38  35  35  PHE PHE B . n 
B 1 39  SER 39  36  36  SER SER B . n 
B 1 40  ALA 40  37  37  ALA ALA B . n 
B 1 41  SER 41  38  38  SER SER B . n 
B 1 42  TRP 42  39  39  TRP TRP B . n 
B 1 43  CYS 43  40  40  CYS CYS B . n 
B 1 44  PRO 44  41  41  PRO PRO B . n 
B 1 45  PRO 45  42  42  PRO PRO B . n 
B 1 46  CYS 46  43  43  CYS CYS B . n 
B 1 47  ARG 47  44  44  ARG ARG B . n 
B 1 48  GLY 48  45  45  GLY GLY B . n 
B 1 49  PHE 49  46  46  PHE PHE B . n 
B 1 50  THR 50  47  47  THR THR B . n 
B 1 51  PRO 51  48  48  PRO PRO B . n 
B 1 52  THR 52  49  49  THR THR B . n 
B 1 53  LEU 53  50  50  LEU LEU B . n 
B 1 54  VAL 54  51  51  VAL VAL B . n 
B 1 55  GLU 55  52  52  GLU GLU B . n 
B 1 56  PHE 56  53  53  PHE PHE B . n 
B 1 57  TYR 57  54  54  TYR TYR B . n 
B 1 58  GLU 58  55  55  GLU GLU B . n 
B 1 59  LYS 59  56  56  LYS LYS B . n 
B 1 60  PHE 60  57  57  PHE PHE B . n 
B 1 61  ARG 61  58  58  ARG ARG B . n 
B 1 62  GLU 62  59  59  GLU GLU B . n 
B 1 63  SER 63  60  60  SER SER B . n 
B 1 64  LYS 64  61  61  LYS LYS B . n 
B 1 65  ASN 65  62  62  ASN ASN B . n 
B 1 66  PHE 66  63  63  PHE PHE B . n 
B 1 67  GLU 67  64  64  GLU GLU B . n 
B 1 68  VAL 68  65  65  VAL VAL B . n 
B 1 69  VAL 69  66  66  VAL VAL B . n 
B 1 70  LEU 70  67  67  LEU LEU B . n 
B 1 71  VAL 71  68  68  VAL VAL B . n 
B 1 72  THR 72  69  69  THR THR B . n 
B 1 73  TRP 73  70  70  TRP TRP B . n 
B 1 74  ASP 74  71  71  ASP ASP B . n 
B 1 75  ASP 75  72  72  ASP ASP B . n 
B 1 76  GLU 76  73  73  GLU GLU B . n 
B 1 77  GLU 77  74  74  GLU GLU B . n 
B 1 78  GLU 78  75  75  GLU GLU B . n 
B 1 79  ALA 79  76  76  ALA ALA B . n 
B 1 80  TYR 80  77  77  TYR TYR B . n 
B 1 81  ASN 81  78  78  ASN ASN B . n 
B 1 82  GLY 82  79  79  GLY GLY B . n 
B 1 83  TYR 83  80  80  TYR TYR B . n 
B 1 84  PHE 84  81  81  PHE PHE B . n 
B 1 85  ALA 85  82  82  ALA ALA B . n 
B 1 86  LYS 86  83  83  LYS LYS B . n 
B 1 87  MET 87  84  84  MET MET B . n 
B 1 88  PRO 88  85  85  PRO PRO B . n 
B 1 89  TRP 89  86  86  TRP TRP B . n 
B 1 90  LEU 90  87  87  LEU LEU B . n 
B 1 91  ALA 91  88  88  ALA ALA B . n 
B 1 92  ILE 92  89  89  ILE ILE B . n 
B 1 93  PRO 93  90  90  PRO PRO B . n 
B 1 94  PHE 94  91  91  PHE PHE B . n 
B 1 95  SER 95  92  92  SER SER B . n 
B 1 96  SER 96  93  93  SER SER B . n 
B 1 97  ARG 97  94  94  ARG ARG B . n 
B 1 98  ALA 98  95  95  ALA ALA B . n 
B 1 99  GLU 99  96  96  GLU GLU B . n 
B 1 100 LEU 100 97  97  LEU LEU B . n 
B 1 101 GLU 101 98  98  GLU GLU B . n 
B 1 102 ALA 102 99  99  ALA ALA B . n 
B 1 103 LEU 103 100 100 LEU LEU B . n 
B 1 104 ARG 104 101 101 ARG ARG B . n 
B 1 105 SER 105 102 102 SER SER B . n 
B 1 106 THR 106 103 103 THR THR B . n 
B 1 107 PHE 107 104 104 PHE PHE B . n 
B 1 108 GLY 108 105 105 GLY GLY B . n 
B 1 109 VAL 109 106 106 VAL VAL B . n 
B 1 110 GLU 110 107 107 GLU GLU B . n 
B 1 111 THR 111 108 108 THR THR B . n 
B 1 112 ILE 112 109 109 ILE ILE B . n 
B 1 113 PRO 113 110 110 PRO PRO B . n 
B 1 114 THR 114 111 111 THR THR B . n 
B 1 115 VAL 115 112 112 VAL VAL B . n 
B 1 116 ILE 116 113 113 ILE ILE B . n 
B 1 117 ALA 117 114 114 ALA ALA B . n 
B 1 118 VAL 118 115 115 VAL VAL B . n 
B 1 119 ASN 119 116 116 ASN ASN B . n 
B 1 120 ALA 120 117 117 ALA ALA B . n 
B 1 121 ASP 121 118 118 ASP ASP B . n 
B 1 122 THR 122 119 119 THR THR B . n 
B 1 123 GLY 123 120 120 GLY GLY B . n 
B 1 124 ALA 124 121 121 ALA ALA B . n 
B 1 125 VAL 125 122 122 VAL VAL B . n 
B 1 126 VAL 126 123 123 VAL VAL B . n 
B 1 127 SER 127 124 124 SER SER B . n 
B 1 128 THR 128 125 125 THR THR B . n 
B 1 129 LYS 129 126 126 LYS LYS B . n 
B 1 130 GLY 130 127 127 GLY GLY B . n 
B 1 131 ARG 131 128 128 ARG ARG B . n 
B 1 132 GLU 132 129 129 GLU GLU B . n 
B 1 133 ARG 133 130 130 ARG ARG B . n 
B 1 134 LEU 134 131 131 LEU LEU B . n 
B 1 135 LEU 135 132 132 LEU LEU B . n 
B 1 136 THR 136 133 133 THR THR B . n 
B 1 137 ASP 137 134 134 ASP ASP B . n 
B 1 138 PRO 138 135 135 PRO PRO B . n 
B 1 139 GLU 139 136 136 GLU GLU B . n 
B 1 140 GLY 140 137 137 GLY GLY B . n 
B 1 141 LYS 141 138 138 LYS LYS B . n 
B 1 142 ASN 142 139 139 ASN ASN B . n 
B 1 143 PHE 143 140 140 PHE PHE B . n 
B 1 144 PRO 144 141 141 PRO PRO B . n 
B 1 145 TRP 145 142 142 TRP TRP B . n 
B 1 146 SER 146 143 143 SER SER B . n 
B 1 147 ASP 147 144 144 ASP ASP 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 GOL 1   201 201 GOL GOL A . 
D 3 HOH 1   301 243 HOH HOH A . 
D 3 HOH 2   302 271 HOH HOH A . 
D 3 HOH 3   303 261 HOH HOH A . 
D 3 HOH 4   304 338 HOH HOH A . 
D 3 HOH 5   305 228 HOH HOH A . 
D 3 HOH 6   306 68  HOH HOH A . 
D 3 HOH 7   307 364 HOH HOH A . 
D 3 HOH 8   308 349 HOH HOH A . 
D 3 HOH 9   309 205 HOH HOH A . 
D 3 HOH 10  310 195 HOH HOH A . 
D 3 HOH 11  311 191 HOH HOH A . 
D 3 HOH 12  312 135 HOH HOH A . 
D 3 HOH 13  313 145 HOH HOH A . 
D 3 HOH 14  314 100 HOH HOH A . 
D 3 HOH 15  315 249 HOH HOH A . 
D 3 HOH 16  316 15  HOH HOH A . 
D 3 HOH 17  317 203 HOH HOH A . 
D 3 HOH 18  318 172 HOH HOH A . 
D 3 HOH 19  319 290 HOH HOH A . 
D 3 HOH 20  320 50  HOH HOH A . 
D 3 HOH 21  321 186 HOH HOH A . 
D 3 HOH 22  322 81  HOH HOH A . 
D 3 HOH 23  323 88  HOH HOH A . 
D 3 HOH 24  324 192 HOH HOH A . 
D 3 HOH 25  325 390 HOH HOH A . 
D 3 HOH 26  326 127 HOH HOH A . 
D 3 HOH 27  327 118 HOH HOH A . 
D 3 HOH 28  328 379 HOH HOH A . 
D 3 HOH 29  329 65  HOH HOH A . 
D 3 HOH 30  330 30  HOH HOH A . 
D 3 HOH 31  331 293 HOH HOH A . 
D 3 HOH 32  332 8   HOH HOH A . 
D 3 HOH 33  333 238 HOH HOH A . 
D 3 HOH 34  334 236 HOH HOH A . 
D 3 HOH 35  335 112 HOH HOH A . 
D 3 HOH 36  336 14  HOH HOH A . 
D 3 HOH 37  337 69  HOH HOH A . 
D 3 HOH 38  338 107 HOH HOH A . 
D 3 HOH 39  339 174 HOH HOH A . 
D 3 HOH 40  340 229 HOH HOH A . 
D 3 HOH 41  341 288 HOH HOH A . 
D 3 HOH 42  342 190 HOH HOH A . 
D 3 HOH 43  343 295 HOH HOH A . 
D 3 HOH 44  344 110 HOH HOH A . 
D 3 HOH 45  345 5   HOH HOH A . 
D 3 HOH 46  346 72  HOH HOH A . 
D 3 HOH 47  347 51  HOH HOH A . 
D 3 HOH 48  348 66  HOH HOH A . 
D 3 HOH 49  349 148 HOH HOH A . 
D 3 HOH 50  350 196 HOH HOH A . 
D 3 HOH 51  351 67  HOH HOH A . 
D 3 HOH 52  352 130 HOH HOH A . 
D 3 HOH 53  353 62  HOH HOH A . 
D 3 HOH 54  354 150 HOH HOH A . 
D 3 HOH 55  355 85  HOH HOH A . 
D 3 HOH 56  356 250 HOH HOH A . 
D 3 HOH 57  357 347 HOH HOH A . 
D 3 HOH 58  358 61  HOH HOH A . 
D 3 HOH 59  359 1   HOH HOH A . 
D 3 HOH 60  360 90  HOH HOH A . 
D 3 HOH 61  361 111 HOH HOH A . 
D 3 HOH 62  362 83  HOH HOH A . 
D 3 HOH 63  363 339 HOH HOH A . 
D 3 HOH 64  364 59  HOH HOH A . 
D 3 HOH 65  365 39  HOH HOH A . 
D 3 HOH 66  366 208 HOH HOH A . 
D 3 HOH 67  367 32  HOH HOH A . 
D 3 HOH 68  368 117 HOH HOH A . 
D 3 HOH 69  369 206 HOH HOH A . 
D 3 HOH 70  370 368 HOH HOH A . 
D 3 HOH 71  371 216 HOH HOH A . 
D 3 HOH 72  372 129 HOH HOH A . 
D 3 HOH 73  373 9   HOH HOH A . 
D 3 HOH 74  374 185 HOH HOH A . 
D 3 HOH 75  375 29  HOH HOH A . 
D 3 HOH 76  376 245 HOH HOH A . 
D 3 HOH 77  377 386 HOH HOH A . 
D 3 HOH 78  378 340 HOH HOH A . 
D 3 HOH 79  379 119 HOH HOH A . 
D 3 HOH 80  380 2   HOH HOH A . 
D 3 HOH 81  381 64  HOH HOH A . 
D 3 HOH 82  382 21  HOH HOH A . 
D 3 HOH 83  383 44  HOH HOH A . 
D 3 HOH 84  384 266 HOH HOH A . 
D 3 HOH 85  385 89  HOH HOH A . 
D 3 HOH 86  386 10  HOH HOH A . 
D 3 HOH 87  387 87  HOH HOH A . 
D 3 HOH 88  388 335 HOH HOH A . 
D 3 HOH 89  389 268 HOH HOH A . 
D 3 HOH 90  390 104 HOH HOH A . 
D 3 HOH 91  391 311 HOH HOH A . 
D 3 HOH 92  392 209 HOH HOH A . 
D 3 HOH 93  393 40  HOH HOH A . 
D 3 HOH 94  394 276 HOH HOH A . 
D 3 HOH 95  395 116 HOH HOH A . 
D 3 HOH 96  396 310 HOH HOH A . 
D 3 HOH 97  397 11  HOH HOH A . 
D 3 HOH 98  398 17  HOH HOH A . 
D 3 HOH 99  399 343 HOH HOH A . 
D 3 HOH 100 400 97  HOH HOH A . 
D 3 HOH 101 401 84  HOH HOH A . 
D 3 HOH 102 402 375 HOH HOH A . 
D 3 HOH 103 403 92  HOH HOH A . 
D 3 HOH 104 404 285 HOH HOH A . 
D 3 HOH 105 405 56  HOH HOH A . 
D 3 HOH 106 406 388 HOH HOH A . 
D 3 HOH 107 407 133 HOH HOH A . 
D 3 HOH 108 408 385 HOH HOH A . 
D 3 HOH 109 409 63  HOH HOH A . 
D 3 HOH 110 410 102 HOH HOH A . 
D 3 HOH 111 411 214 HOH HOH A . 
D 3 HOH 112 412 48  HOH HOH A . 
D 3 HOH 113 413 42  HOH HOH A . 
D 3 HOH 114 414 143 HOH HOH A . 
D 3 HOH 115 415 120 HOH HOH A . 
D 3 HOH 116 416 26  HOH HOH A . 
D 3 HOH 117 417 76  HOH HOH A . 
D 3 HOH 118 418 160 HOH HOH A . 
D 3 HOH 119 419 36  HOH HOH A . 
D 3 HOH 120 420 336 HOH HOH A . 
D 3 HOH 121 421 141 HOH HOH A . 
D 3 HOH 122 422 370 HOH HOH A . 
D 3 HOH 123 423 71  HOH HOH A . 
D 3 HOH 124 424 220 HOH HOH A . 
D 3 HOH 125 425 12  HOH HOH A . 
D 3 HOH 126 426 313 HOH HOH A . 
D 3 HOH 127 427 376 HOH HOH A . 
D 3 HOH 128 428 381 HOH HOH A . 
D 3 HOH 129 429 262 HOH HOH A . 
D 3 HOH 130 430 106 HOH HOH A . 
D 3 HOH 131 431 294 HOH HOH A . 
D 3 HOH 132 432 162 HOH HOH A . 
D 3 HOH 133 433 232 HOH HOH A . 
D 3 HOH 134 434 47  HOH HOH A . 
D 3 HOH 135 435 222 HOH HOH A . 
D 3 HOH 136 436 201 HOH HOH A . 
D 3 HOH 137 437 257 HOH HOH A . 
D 3 HOH 138 438 4   HOH HOH A . 
D 3 HOH 139 439 79  HOH HOH A . 
D 3 HOH 140 440 94  HOH HOH A . 
D 3 HOH 141 441 280 HOH HOH A . 
D 3 HOH 142 442 279 HOH HOH A . 
D 3 HOH 143 443 96  HOH HOH A . 
D 3 HOH 144 444 247 HOH HOH A . 
D 3 HOH 145 445 325 HOH HOH A . 
D 3 HOH 146 446 307 HOH HOH A . 
D 3 HOH 147 447 360 HOH HOH A . 
D 3 HOH 148 448 391 HOH HOH A . 
D 3 HOH 149 449 221 HOH HOH A . 
D 3 HOH 150 450 152 HOH HOH A . 
D 3 HOH 151 451 383 HOH HOH A . 
D 3 HOH 152 452 259 HOH HOH A . 
D 3 HOH 153 453 123 HOH HOH A . 
D 3 HOH 154 454 377 HOH HOH A . 
D 3 HOH 155 455 164 HOH HOH A . 
D 3 HOH 156 456 382 HOH HOH A . 
D 3 HOH 157 457 240 HOH HOH A . 
D 3 HOH 158 458 363 HOH HOH A . 
D 3 HOH 159 459 374 HOH HOH A . 
D 3 HOH 160 460 86  HOH HOH A . 
D 3 HOH 161 461 357 HOH HOH A . 
D 3 HOH 162 462 297 HOH HOH A . 
D 3 HOH 163 463 289 HOH HOH A . 
D 3 HOH 164 464 274 HOH HOH A . 
D 3 HOH 165 465 255 HOH HOH A . 
D 3 HOH 166 466 180 HOH HOH A . 
D 3 HOH 167 467 330 HOH HOH A . 
D 3 HOH 168 468 303 HOH HOH A . 
D 3 HOH 169 469 329 HOH HOH A . 
D 3 HOH 170 470 281 HOH HOH A . 
D 3 HOH 171 471 169 HOH HOH A . 
D 3 HOH 172 472 314 HOH HOH A . 
D 3 HOH 173 473 345 HOH HOH A . 
D 3 HOH 174 474 354 HOH HOH A . 
D 3 HOH 175 475 269 HOH HOH A . 
D 3 HOH 176 476 258 HOH HOH A . 
D 3 HOH 177 477 125 HOH HOH A . 
D 3 HOH 178 478 331 HOH HOH A . 
D 3 HOH 179 479 212 HOH HOH A . 
D 3 HOH 180 480 155 HOH HOH A . 
D 3 HOH 181 481 193 HOH HOH A . 
D 3 HOH 182 482 283 HOH HOH A . 
D 3 HOH 183 483 278 HOH HOH A . 
D 3 HOH 184 484 302 HOH HOH A . 
D 3 HOH 185 485 358 HOH HOH A . 
D 3 HOH 186 486 306 HOH HOH A . 
D 3 HOH 187 487 170 HOH HOH A . 
D 3 HOH 188 488 299 HOH HOH A . 
D 3 HOH 189 489 7   HOH HOH A . 
D 3 HOH 190 490 158 HOH HOH A . 
D 3 HOH 191 491 326 HOH HOH A . 
D 3 HOH 192 492 138 HOH HOH A . 
D 3 HOH 193 493 270 HOH HOH A . 
D 3 HOH 194 494 342 HOH HOH A . 
D 3 HOH 195 495 284 HOH HOH A . 
D 3 HOH 196 496 353 HOH HOH A . 
D 3 HOH 197 497 323 HOH HOH A . 
D 3 HOH 198 498 286 HOH HOH A . 
D 3 HOH 199 499 239 HOH HOH A . 
D 3 HOH 200 500 324 HOH HOH A . 
D 3 HOH 201 501 309 HOH HOH A . 
D 3 HOH 202 502 264 HOH HOH A . 
D 3 HOH 203 503 321 HOH HOH A . 
D 3 HOH 204 504 287 HOH HOH A . 
D 3 HOH 205 505 231 HOH HOH A . 
D 3 HOH 206 506 256 HOH HOH A . 
D 3 HOH 207 507 367 HOH HOH A . 
D 3 HOH 208 508 131 HOH HOH A . 
D 3 HOH 209 509 384 HOH HOH A . 
E 3 HOH 1   201 362 HOH HOH B . 
E 3 HOH 2   202 177 HOH HOH B . 
E 3 HOH 3   203 175 HOH HOH B . 
E 3 HOH 4   204 183 HOH HOH B . 
E 3 HOH 5   205 144 HOH HOH B . 
E 3 HOH 6   206 105 HOH HOH B . 
E 3 HOH 7   207 98  HOH HOH B . 
E 3 HOH 8   208 80  HOH HOH B . 
E 3 HOH 9   209 207 HOH HOH B . 
E 3 HOH 10  210 166 HOH HOH B . 
E 3 HOH 11  211 215 HOH HOH B . 
E 3 HOH 12  212 304 HOH HOH B . 
E 3 HOH 13  213 327 HOH HOH B . 
E 3 HOH 14  214 157 HOH HOH B . 
E 3 HOH 15  215 121 HOH HOH B . 
E 3 HOH 16  216 233 HOH HOH B . 
E 3 HOH 17  217 197 HOH HOH B . 
E 3 HOH 18  218 28  HOH HOH B . 
E 3 HOH 19  219 46  HOH HOH B . 
E 3 HOH 20  220 91  HOH HOH B . 
E 3 HOH 21  221 27  HOH HOH B . 
E 3 HOH 22  222 234 HOH HOH B . 
E 3 HOH 23  223 113 HOH HOH B . 
E 3 HOH 24  224 312 HOH HOH B . 
E 3 HOH 25  225 260 HOH HOH B . 
E 3 HOH 26  226 200 HOH HOH B . 
E 3 HOH 27  227 142 HOH HOH B . 
E 3 HOH 28  228 387 HOH HOH B . 
E 3 HOH 29  229 156 HOH HOH B . 
E 3 HOH 30  230 19  HOH HOH B . 
E 3 HOH 31  231 380 HOH HOH B . 
E 3 HOH 32  232 73  HOH HOH B . 
E 3 HOH 33  233 317 HOH HOH B . 
E 3 HOH 34  234 341 HOH HOH B . 
E 3 HOH 35  235 251 HOH HOH B . 
E 3 HOH 36  236 202 HOH HOH B . 
E 3 HOH 37  237 33  HOH HOH B . 
E 3 HOH 38  238 93  HOH HOH B . 
E 3 HOH 39  239 57  HOH HOH B . 
E 3 HOH 40  240 227 HOH HOH B . 
E 3 HOH 41  241 198 HOH HOH B . 
E 3 HOH 42  242 356 HOH HOH B . 
E 3 HOH 43  243 124 HOH HOH B . 
E 3 HOH 44  244 308 HOH HOH B . 
E 3 HOH 45  245 173 HOH HOH B . 
E 3 HOH 46  246 153 HOH HOH B . 
E 3 HOH 47  247 58  HOH HOH B . 
E 3 HOH 48  248 146 HOH HOH B . 
E 3 HOH 49  249 230 HOH HOH B . 
E 3 HOH 50  250 151 HOH HOH B . 
E 3 HOH 51  251 77  HOH HOH B . 
E 3 HOH 52  252 22  HOH HOH B . 
E 3 HOH 53  253 31  HOH HOH B . 
E 3 HOH 54  254 78  HOH HOH B . 
E 3 HOH 55  255 184 HOH HOH B . 
E 3 HOH 56  256 38  HOH HOH B . 
E 3 HOH 57  257 223 HOH HOH B . 
E 3 HOH 58  258 147 HOH HOH B . 
E 3 HOH 59  259 3   HOH HOH B . 
E 3 HOH 60  260 6   HOH HOH B . 
E 3 HOH 61  261 252 HOH HOH B . 
E 3 HOH 62  262 126 HOH HOH B . 
E 3 HOH 63  263 82  HOH HOH B . 
E 3 HOH 64  264 35  HOH HOH B . 
E 3 HOH 65  265 128 HOH HOH B . 
E 3 HOH 66  266 45  HOH HOH B . 
E 3 HOH 67  267 95  HOH HOH B . 
E 3 HOH 68  268 346 HOH HOH B . 
E 3 HOH 69  269 34  HOH HOH B . 
E 3 HOH 70  270 366 HOH HOH B . 
E 3 HOH 71  271 20  HOH HOH B . 
E 3 HOH 72  272 115 HOH HOH B . 
E 3 HOH 73  273 70  HOH HOH B . 
E 3 HOH 74  274 305 HOH HOH B . 
E 3 HOH 75  275 16  HOH HOH B . 
E 3 HOH 76  276 194 HOH HOH B . 
E 3 HOH 77  277 337 HOH HOH B . 
E 3 HOH 78  278 49  HOH HOH B . 
E 3 HOH 79  279 13  HOH HOH B . 
E 3 HOH 80  280 41  HOH HOH B . 
E 3 HOH 81  281 218 HOH HOH B . 
E 3 HOH 82  282 189 HOH HOH B . 
E 3 HOH 83  283 134 HOH HOH B . 
E 3 HOH 84  284 296 HOH HOH B . 
E 3 HOH 85  285 149 HOH HOH B . 
E 3 HOH 86  286 163 HOH HOH B . 
E 3 HOH 87  287 24  HOH HOH B . 
E 3 HOH 88  288 23  HOH HOH B . 
E 3 HOH 89  289 210 HOH HOH B . 
E 3 HOH 90  290 43  HOH HOH B . 
E 3 HOH 91  291 265 HOH HOH B . 
E 3 HOH 92  292 171 HOH HOH B . 
E 3 HOH 93  293 154 HOH HOH B . 
E 3 HOH 94  294 355 HOH HOH B . 
E 3 HOH 95  295 322 HOH HOH B . 
E 3 HOH 96  296 99  HOH HOH B . 
E 3 HOH 97  297 272 HOH HOH B . 
E 3 HOH 98  298 75  HOH HOH B . 
E 3 HOH 99  299 204 HOH HOH B . 
E 3 HOH 100 300 140 HOH HOH B . 
E 3 HOH 101 301 334 HOH HOH B . 
E 3 HOH 102 302 52  HOH HOH B . 
E 3 HOH 103 303 320 HOH HOH B . 
E 3 HOH 104 304 109 HOH HOH B . 
E 3 HOH 105 305 235 HOH HOH B . 
E 3 HOH 106 306 18  HOH HOH B . 
E 3 HOH 107 307 292 HOH HOH B . 
E 3 HOH 108 308 365 HOH HOH B . 
E 3 HOH 109 309 179 HOH HOH B . 
E 3 HOH 110 310 344 HOH HOH B . 
E 3 HOH 111 311 101 HOH HOH B . 
E 3 HOH 112 312 25  HOH HOH B . 
E 3 HOH 113 313 263 HOH HOH B . 
E 3 HOH 114 314 159 HOH HOH B . 
E 3 HOH 115 315 275 HOH HOH B . 
E 3 HOH 116 316 178 HOH HOH B . 
E 3 HOH 117 317 37  HOH HOH B . 
E 3 HOH 118 318 199 HOH HOH B . 
E 3 HOH 119 319 359 HOH HOH B . 
E 3 HOH 120 320 53  HOH HOH B . 
E 3 HOH 121 321 181 HOH HOH B . 
E 3 HOH 122 322 74  HOH HOH B . 
E 3 HOH 123 323 165 HOH HOH B . 
E 3 HOH 124 324 226 HOH HOH B . 
E 3 HOH 125 325 213 HOH HOH B . 
E 3 HOH 126 326 60  HOH HOH B . 
E 3 HOH 127 327 219 HOH HOH B . 
E 3 HOH 128 328 122 HOH HOH B . 
E 3 HOH 129 329 225 HOH HOH B . 
E 3 HOH 130 330 54  HOH HOH B . 
E 3 HOH 131 331 132 HOH HOH B . 
E 3 HOH 132 332 378 HOH HOH B . 
E 3 HOH 133 333 217 HOH HOH B . 
E 3 HOH 134 334 254 HOH HOH B . 
E 3 HOH 135 335 176 HOH HOH B . 
E 3 HOH 136 336 298 HOH HOH B . 
E 3 HOH 137 337 373 HOH HOH B . 
E 3 HOH 138 338 114 HOH HOH B . 
E 3 HOH 139 339 348 HOH HOH B . 
E 3 HOH 140 340 301 HOH HOH B . 
E 3 HOH 141 341 352 HOH HOH B . 
E 3 HOH 142 342 369 HOH HOH B . 
E 3 HOH 143 343 332 HOH HOH B . 
E 3 HOH 144 344 182 HOH HOH B . 
E 3 HOH 145 345 103 HOH HOH B . 
E 3 HOH 146 346 372 HOH HOH B . 
E 3 HOH 147 347 188 HOH HOH B . 
E 3 HOH 148 348 371 HOH HOH B . 
E 3 HOH 149 349 137 HOH HOH B . 
E 3 HOH 150 350 351 HOH HOH B . 
E 3 HOH 151 351 161 HOH HOH B . 
E 3 HOH 152 352 224 HOH HOH B . 
E 3 HOH 153 353 328 HOH HOH B . 
E 3 HOH 154 354 187 HOH HOH B . 
E 3 HOH 155 355 246 HOH HOH B . 
E 3 HOH 156 356 167 HOH HOH B . 
E 3 HOH 157 357 242 HOH HOH B . 
E 3 HOH 158 358 108 HOH HOH B . 
E 3 HOH 159 359 55  HOH HOH B . 
E 3 HOH 160 360 244 HOH HOH B . 
E 3 HOH 161 361 350 HOH HOH B . 
E 3 HOH 162 362 316 HOH HOH B . 
E 3 HOH 163 363 277 HOH HOH B . 
E 3 HOH 164 364 300 HOH HOH B . 
E 3 HOH 165 365 253 HOH HOH B . 
E 3 HOH 166 366 319 HOH HOH B . 
E 3 HOH 167 367 136 HOH HOH B . 
E 3 HOH 168 368 267 HOH HOH B . 
E 3 HOH 169 369 211 HOH HOH B . 
E 3 HOH 170 370 389 HOH HOH B . 
E 3 HOH 171 371 291 HOH HOH B . 
E 3 HOH 172 372 273 HOH HOH B . 
E 3 HOH 173 373 168 HOH HOH B . 
E 3 HOH 174 374 318 HOH HOH B . 
E 3 HOH 175 375 241 HOH HOH B . 
E 3 HOH 176 376 139 HOH HOH B . 
E 3 HOH 177 377 237 HOH HOH B . 
E 3 HOH 178 378 282 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A LEU 4 ? N   B A LEU 7  N   
2  1 Y 0 A LEU 4 ? CA  B A LEU 7  CA  
3  1 Y 0 A LEU 4 ? C   B A LEU 7  C   
4  1 Y 0 A LEU 4 ? O   B A LEU 7  O   
5  1 Y 0 A LEU 4 ? CB  B A LEU 7  CB  
6  1 Y 0 A LEU 4 ? CG  B A LEU 7  CG  
7  1 Y 0 A LEU 4 ? CD1 B A LEU 7  CD1 
8  1 Y 0 A LEU 4 ? CD2 B A LEU 7  CD2 
9  1 Y 0 A ALA 5 ? N   B A ALA 8  N   
10 1 Y 0 A ALA 5 ? CA  B A ALA 8  CA  
11 1 Y 0 A ALA 5 ? C   B A ALA 8  C   
12 1 Y 0 A ALA 5 ? O   B A ALA 8  O   
13 1 Y 0 A ALA 5 ? CB  B A ALA 8  CB  
14 1 Y 0 A LYS 6 ? N   B A LYS 9  N   
15 1 Y 0 A LYS 6 ? CA  B A LYS 9  CA  
16 1 Y 0 A LYS 6 ? C   B A LYS 9  C   
17 1 Y 0 A LYS 6 ? O   B A LYS 9  O   
18 1 Y 0 A LYS 6 ? CB  B A LYS 9  CB  
19 1 Y 0 A LYS 6 ? CG  B A LYS 9  CG  
20 1 Y 0 A LYS 6 ? CD  B A LYS 9  CD  
21 1 Y 0 A LYS 6 ? CE  B A LYS 9  CE  
22 1 Y 0 A LYS 6 ? NZ  B A LYS 9  NZ  
23 1 Y 0 A TYR 7 ? N   B A TYR 10 N   
24 1 Y 0 A TYR 7 ? CA  B A TYR 10 CA  
25 1 Y 0 A TYR 7 ? C   B A TYR 10 C   
26 1 Y 0 A TYR 7 ? O   B A TYR 10 O   
27 1 Y 0 A TYR 7 ? CB  B A TYR 10 CB  
28 1 Y 0 A TYR 7 ? CG  B A TYR 10 CG  
29 1 Y 0 A TYR 7 ? CD1 B A TYR 10 CD1 
30 1 Y 0 A TYR 7 ? CD2 B A TYR 10 CD2 
31 1 Y 0 A TYR 7 ? CE1 B A TYR 10 CE1 
32 1 Y 0 A TYR 7 ? CE2 B A TYR 10 CE2 
33 1 Y 0 A TYR 7 ? CZ  B A TYR 10 CZ  
34 1 Y 0 A TYR 7 ? OH  B A TYR 10 OH  
35 1 Y 0 A LEU 8 ? N   B A LEU 11 N   
36 1 Y 0 A LEU 8 ? CA  B A LEU 11 CA  
37 1 Y 0 A LEU 8 ? C   B A LEU 11 C   
38 1 Y 0 A LEU 8 ? O   B A LEU 11 O   
39 1 Y 0 A LEU 8 ? CB  B A LEU 11 CB  
40 1 Y 0 A LEU 8 ? CG  B A LEU 11 CG  
41 1 Y 0 A LEU 8 ? CD1 B A LEU 11 CD1 
42 1 Y 0 A LEU 8 ? CD2 B A LEU 11 CD2 
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.820 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FOV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.463 
_cell.length_a_esd                 ? 
_cell.length_b                     30.403 
_cell.length_b_esd                 ? 
_cell.length_c                     74.910 
_cell.length_c_esd                 ? 
_cell.volume                       136172.741 
_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                         9FOV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            'P 2y' 
_symmetry.space_group_name_H-M             'P 1 2 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                   9FOV 
_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             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.1 
_exptl_crystal.description                  Plate 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.8 M Ammoniumcitrate
Protein concentration: 6.8 mg/ml
25 mM Na-phosphate buffer, pH 7.5, 150 mM NaCl
1 microliter of protein plus 1 microliter of reservoir
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-24 
_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   0.97626 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97626 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          11.04 
_reflns.entry_id                                       9FOV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.25 
_reflns.d_resolution_low                               40.52 
_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                                     73970 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.120 
_reflns.pdbx_Rpim_I_all                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.108 
_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                                    1.25 
_reflns_shell.d_res_low                                     1.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3604 
_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                               4.0 
_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                               1.405 
_reflns_shell.pdbx_Rpim_I_all                               0.648 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.517 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.239 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.36 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FOV 
_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                            1.25 
_refine.ls_d_res_low                             35.85 
_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                     73847 
_refine.ls_number_reflns_R_free                  1809 
_refine.ls_number_reflns_R_work                  72038 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.06 
_refine.ls_percent_reflns_R_free                 2.45 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1682 
_refine.ls_R_factor_R_free                       0.1958 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1675 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.5756 
_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                            0.1757 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.25 
_refine_hist.d_res_low                        35.85 
_refine_hist.number_atoms_solvent             387 
_refine_hist.number_atoms_total               2674 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2281 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0038  ? 2689 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7435  ? 3717 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0705  ? 417  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0069  ? 473  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.2364 ? 1028 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.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' 1.25 1.28  . . 134 5424 96.28 . . . . 0.3179 . . . . . . . . . . . 0.3547 
'X-RAY DIFFRACTION' 1.28 1.32  . . 131 5444 97.19 . . . . 0.2799 . . . . . . . . . . . 0.3407 
'X-RAY DIFFRACTION' 1.32 1.36  . . 138 5406 96.64 . . . . 0.2545 . . . . . . . . . . . 0.3075 
'X-RAY DIFFRACTION' 1.36 1.41  . . 127 5472 97.61 . . . . 0.2233 . . . . . . . . . . . 0.2621 
'X-RAY DIFFRACTION' 1.41 1.47  . . 136 5597 99.15 . . . . 0.2080 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 1.47 1.54  . . 128 5522 98.62 . . . . 0.1862 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 1.54 1.62  . . 138 5557 98.39 . . . . 0.1565 . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 1.62 1.72  . . 128 5508 98.39 . . . . 0.1500 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 1.72 1.85  . . 152 5502 97.90 . . . . 0.1471 . . . . . . . . . . . 0.1784 
'X-RAY DIFFRACTION' 1.85 2.04  . . 137 5539 97.46 . . . . 0.1473 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 2.04 2.33  . . 155 5622 99.16 . . . . 0.1440 . . . . . . . . . . . 0.1798 
'X-RAY DIFFRACTION' 2.33 2.94  . . 146 5645 99.16 . . . . 0.1532 . . . . . . . . . . . 0.1557 
'X-RAY DIFFRACTION' 2.94 35.85 . . 159 5800 98.81 . . . . 0.1529 . . . . . . . . . . . 0.1702 
# 
_struct.entry_id                     9FOV 
_struct.title                        'Crystal structure of Tryparedoxin from Trypanosoma cruzi' 
_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        9FOV 
_struct_keywords.text            'Thioredoxin superfamily Trypanothione Electron transport, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q4D1B8_TRYCC 
_struct_ref.pdbx_db_accession          Q4D1B8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGLAKYLPSTIKLVSKSGTVSPISLAGKTVFFYFSASWCPPCRGFTPTLVEFYEKFRESKNFEVVLVTWDDEEEAYNGYF
AKMPWLAIPFSSRAELEALRSTFGVETIPTVIAVNADTGAVVSTKGRERLLTDPEGKNFPWSD
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FOV A 5 ? 147 ? Q4D1B8 2 ? 144 ? 2 144 
2 1 9FOV B 5 ? 147 ? Q4D1B8 2 ? 144 ? 2 144 
# 
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 9FOV GLY A 1 ? UNP Q4D1B8 ? ? 'expression tag' -2 1 
1 9FOV ALA A 2 ? UNP Q4D1B8 ? ? 'expression tag' -1 2 
1 9FOV MET A 3 ? UNP Q4D1B8 ? ? 'expression tag' 0  3 
1 9FOV GLY A 4 ? UNP Q4D1B8 ? ? 'expression tag' 1  4 
2 9FOV GLY B 1 ? UNP Q4D1B8 ? ? 'expression tag' -2 5 
2 9FOV ALA B 2 ? UNP Q4D1B8 ? ? 'expression tag' -1 6 
2 9FOV MET B 3 ? UNP Q4D1B8 ? ? 'expression tag' 0  7 
2 9FOV GLY B 4 ? UNP Q4D1B8 ? ? 'expression tag' 1  8 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1600  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  12980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 4   ? ALA A 8   ? GLY A 1   ALA A 5   5 ? 5  
HELX_P HELX_P2  AA2 SER A 25  ? ALA A 30  ? SER A 22  ALA A 27  5 ? 6  
HELX_P HELX_P3  AA3 CYS A 43  ? ARG A 61  ? CYS A 40  ARG A 58  1 ? 19 
HELX_P HELX_P4  AA4 GLU A 76  ? ALA A 85  ? GLU A 73  ALA A 82  1 ? 10 
HELX_P HELX_P5  AA5 SER A 96  ? GLY A 108 ? SER A 93  GLY A 105 1 ? 13 
HELX_P HELX_P6  AA6 LYS A 129 ? LEU A 134 ? LYS A 126 LEU A 131 1 ? 6  
HELX_P HELX_P7  AA7 LEU A 135 ? ASP A 137 ? LEU A 132 ASP A 134 5 ? 3  
HELX_P HELX_P8  AA8 GLY B 4   ? LYS B 9   ? GLY B 1   LYS B 6   1 ? 6  
HELX_P HELX_P9  AA9 SER B 25  ? ALA B 30  ? SER B 22  ALA B 27  5 ? 6  
HELX_P HELX_P10 AB1 CYS B 43  ? ARG B 61  ? CYS B 40  ARG B 58  1 ? 19 
HELX_P HELX_P11 AB2 GLU B 76  ? ALA B 85  ? GLU B 73  ALA B 82  1 ? 10 
HELX_P HELX_P12 AB3 SER B 96  ? GLY B 108 ? SER B 93  GLY B 105 1 ? 13 
HELX_P HELX_P13 AB4 LYS B 129 ? LEU B 134 ? LYS B 126 LEU B 131 1 ? 6  
HELX_P HELX_P14 AB5 LEU B 135 ? ASP B 137 ? LEU B 132 ASP B 134 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 112 A . ? ILE 109 A PRO 113 A ? PRO 110 A 1 -2.21 
2 PHE 143 A . ? PHE 140 A PRO 144 A ? PRO 141 A 1 4.42  
3 ILE 112 B . ? ILE 109 B PRO 113 B ? PRO 110 B 1 -2.50 
4 PHE 143 B . ? PHE 140 B PRO 144 B ? PRO 141 B 1 3.14  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
# 
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 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? 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 LEU A 17  ? VAL A 18  ? LEU A 14  VAL A 15  
AA1 2 THR A 23  ? VAL A 24  ? THR A 20  VAL A 21  
AA2 1 LEU A 90  ? ALA A 91  ? LEU A 87  ALA A 88  
AA2 2 PHE A 66  ? THR A 72  ? PHE A 63  THR A 69  
AA2 3 THR A 33  ? SER A 39  ? THR A 30  SER A 36  
AA2 4 THR A 114 ? ASN A 119 ? THR A 111 ASN A 116 
AA2 5 VAL A 125 ? SER A 127 ? VAL A 122 SER A 124 
AA3 1 LEU B 17  ? VAL B 18  ? LEU B 14  VAL B 15  
AA3 2 THR B 23  ? VAL B 24  ? THR B 20  VAL B 21  
AA4 1 LEU B 90  ? ALA B 91  ? LEU B 87  ALA B 88  
AA4 2 PHE B 66  ? THR B 72  ? PHE B 63  THR B 69  
AA4 3 THR B 33  ? SER B 39  ? THR B 30  SER B 36  
AA4 4 THR B 114 ? ASN B 119 ? THR B 111 ASN B 116 
AA4 5 VAL B 125 ? SER B 127 ? VAL B 122 SER B 124 
# 
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 LEU A 17  ? N LEU A 14  O VAL A 24  ? O VAL A 21  
AA2 1 2 O LEU A 90  ? O LEU A 87  N LEU A 70  ? N LEU A 67  
AA2 2 3 O VAL A 71  ? O VAL A 68  N TYR A 37  ? N TYR A 34  
AA2 3 4 N PHE A 36  ? N PHE A 33  O ILE A 116 ? O ILE A 113 
AA2 4 5 N ALA A 117 ? N ALA A 114 O VAL A 126 ? O VAL A 123 
AA3 1 2 N LEU B 17  ? N LEU B 14  O VAL B 24  ? O VAL B 21  
AA4 1 2 O LEU B 90  ? O LEU B 87  N LEU B 70  ? N LEU B 67  
AA4 2 3 O VAL B 71  ? O VAL B 68  N TYR B 37  ? N TYR B 34  
AA4 3 4 N PHE B 36  ? N PHE B 33  O ILE B 116 ? O ILE B 113 
AA4 4 5 N ALA B 117 ? N ALA B 114 O VAL B 126 ? O VAL B 123 
# 
_pdbx_entry_details.entry_id                   9FOV 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 HZ1 B LYS 56  ? ? O B HOH 203 ? ? 1.58 
2  1 OE2 B GLU 73  ? B O B HOH 201 ? ? 1.88 
3  1 O   B HOH 343 ? ? O B HOH 374 ? ? 1.96 
4  1 O   B HOH 312 ? ? O B HOH 350 ? ? 1.99 
5  1 O   B HOH 225 ? ? O B HOH 236 ? ? 2.03 
6  1 O   A HOH 458 ? ? O A HOH 496 ? ? 2.04 
7  1 O   A HOH 467 ? ? O A HOH 478 ? ? 2.08 
8  1 N   A ALA -1  ? ? O A HOH 301 ? ? 2.14 
9  1 O   A HOH 391 ? ? O A HOH 501 ? ? 2.14 
10 1 O   B HOH 335 ? ? O B HOH 362 ? ? 2.14 
11 1 O   B HOH 247 ? ? O B HOH 352 ? ? 2.15 
12 1 O   A HOH 403 ? ? O A HOH 479 ? ? 2.17 
13 1 O   B HOH 332 ? ? O B HOH 348 ? ? 2.17 
14 1 OG  A SER 18  ? ? O A HOH 302 ? ? 2.17 
15 1 O   B HOH 289 ? ? O B HOH 295 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     277 
_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    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     342 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_545 
_pdbx_validate_symm_contact.dist              2.02 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 4   ? B -106.47 50.76   
2 1 TRP A 86  ? ? -105.00 -152.10 
3 1 TRP B 86  ? ? -106.42 -152.96 
4 1 TRP B 142 ? ? 70.38   41.57   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 388 ? D HOH . 
2 1 A HOH 444 ? D HOH . 
3 1 B HOH 357 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z   
2 -x,y,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -2 ? A GLY 1 
2 1 Y 1 B GLY -2 ? B GLY 1 
3 1 Y 1 B ALA -1 ? B ALA 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLU N    N N N 88  
GLU CA   C N S 89  
GLU C    C N N 90  
GLU O    O N N 91  
GLU CB   C N N 92  
GLU CG   C N N 93  
GLU CD   C N N 94  
GLU OE1  O N N 95  
GLU OE2  O N N 96  
GLU OXT  O N N 97  
GLU H    H N N 98  
GLU H2   H N N 99  
GLU HA   H N N 100 
GLU HB2  H N N 101 
GLU HB3  H N N 102 
GLU HG2  H N N 103 
GLU HG3  H N N 104 
GLU HE2  H N N 105 
GLU HXT  H N N 106 
GLY N    N N N 107 
GLY CA   C N N 108 
GLY C    C N N 109 
GLY O    O N N 110 
GLY OXT  O N N 111 
GLY H    H N N 112 
GLY H2   H N N 113 
GLY HA2  H N N 114 
GLY HA3  H N N 115 
GLY HXT  H N N 116 
GOL C1   C N N 117 
GOL O1   O N N 118 
GOL C2   C N N 119 
GOL O2   O N N 120 
GOL C3   C N N 121 
GOL O3   O N N 122 
GOL H11  H N N 123 
GOL H12  H N N 124 
GOL HO1  H N N 125 
GOL H2   H N N 126 
GOL HO2  H N N 127 
GOL H31  H N N 128 
GOL H32  H N N 129 
GOL HO3  H N N 130 
HOH O    O N N 131 
HOH H1   H N N 132 
HOH H2   H N N 133 
ILE N    N N N 134 
ILE CA   C N S 135 
ILE C    C N N 136 
ILE O    O N N 137 
ILE CB   C N S 138 
ILE CG1  C N N 139 
ILE CG2  C N N 140 
ILE CD1  C N N 141 
ILE OXT  O N N 142 
ILE H    H N N 143 
ILE H2   H N N 144 
ILE HA   H N N 145 
ILE HB   H N N 146 
ILE HG12 H N N 147 
ILE HG13 H N N 148 
ILE HG21 H N N 149 
ILE HG22 H N N 150 
ILE HG23 H N N 151 
ILE HD11 H N N 152 
ILE HD12 H N N 153 
ILE HD13 H N N 154 
ILE HXT  H N N 155 
LEU N    N N N 156 
LEU CA   C N S 157 
LEU C    C N N 158 
LEU O    O N N 159 
LEU CB   C N N 160 
LEU CG   C N N 161 
LEU CD1  C N N 162 
LEU CD2  C N N 163 
LEU OXT  O N N 164 
LEU H    H N N 165 
LEU H2   H N N 166 
LEU HA   H N N 167 
LEU HB2  H N N 168 
LEU HB3  H N N 169 
LEU HG   H N N 170 
LEU HD11 H N N 171 
LEU HD12 H N N 172 
LEU HD13 H N N 173 
LEU HD21 H N N 174 
LEU HD22 H N N 175 
LEU HD23 H N N 176 
LEU HXT  H N N 177 
LYS N    N N N 178 
LYS CA   C N S 179 
LYS C    C N N 180 
LYS O    O N N 181 
LYS CB   C N N 182 
LYS CG   C N N 183 
LYS CD   C N N 184 
LYS CE   C N N 185 
LYS NZ   N N N 186 
LYS OXT  O N N 187 
LYS H    H N N 188 
LYS H2   H N N 189 
LYS HA   H N N 190 
LYS HB2  H N N 191 
LYS HB3  H N N 192 
LYS HG2  H N N 193 
LYS HG3  H N N 194 
LYS HD2  H N N 195 
LYS HD3  H N N 196 
LYS HE2  H N N 197 
LYS HE3  H N N 198 
LYS HZ1  H N N 199 
LYS HZ2  H N N 200 
LYS HZ3  H N N 201 
LYS HXT  H N N 202 
MET N    N N N 203 
MET CA   C N S 204 
MET C    C N N 205 
MET O    O N N 206 
MET CB   C N N 207 
MET CG   C N N 208 
MET SD   S N N 209 
MET CE   C N N 210 
MET OXT  O N N 211 
MET H    H N N 212 
MET H2   H N N 213 
MET HA   H N N 214 
MET HB2  H N N 215 
MET HB3  H N N 216 
MET HG2  H N N 217 
MET HG3  H N N 218 
MET HE1  H N N 219 
MET HE2  H N N 220 
MET HE3  H N N 221 
MET HXT  H N N 222 
PHE N    N N N 223 
PHE CA   C N S 224 
PHE C    C N N 225 
PHE O    O N N 226 
PHE CB   C N N 227 
PHE CG   C Y N 228 
PHE CD1  C Y N 229 
PHE CD2  C Y N 230 
PHE CE1  C Y N 231 
PHE CE2  C Y N 232 
PHE CZ   C Y N 233 
PHE OXT  O N N 234 
PHE H    H N N 235 
PHE H2   H N N 236 
PHE HA   H N N 237 
PHE HB2  H N N 238 
PHE HB3  H N N 239 
PHE HD1  H N N 240 
PHE HD2  H N N 241 
PHE HE1  H N N 242 
PHE HE2  H N N 243 
PHE HZ   H N N 244 
PHE HXT  H N N 245 
PRO N    N N N 246 
PRO CA   C N S 247 
PRO C    C N N 248 
PRO O    O N N 249 
PRO CB   C N N 250 
PRO CG   C N N 251 
PRO CD   C N N 252 
PRO OXT  O N N 253 
PRO H    H N N 254 
PRO HA   H N N 255 
PRO HB2  H N N 256 
PRO HB3  H N N 257 
PRO HG2  H N N 258 
PRO HG3  H N N 259 
PRO HD2  H N N 260 
PRO HD3  H N N 261 
PRO HXT  H N N 262 
SER N    N N N 263 
SER CA   C N S 264 
SER C    C N N 265 
SER O    O N N 266 
SER CB   C N N 267 
SER OG   O N N 268 
SER OXT  O N N 269 
SER H    H N N 270 
SER H2   H N N 271 
SER HA   H N N 272 
SER HB2  H N N 273 
SER HB3  H N N 274 
SER HG   H N N 275 
SER HXT  H N N 276 
THR N    N N N 277 
THR CA   C N S 278 
THR C    C N N 279 
THR O    O N N 280 
THR CB   C N R 281 
THR OG1  O N N 282 
THR CG2  C N N 283 
THR OXT  O N N 284 
THR H    H N N 285 
THR H2   H N N 286 
THR HA   H N N 287 
THR HB   H N N 288 
THR HG1  H N N 289 
THR HG21 H N N 290 
THR HG22 H N N 291 
THR HG23 H N N 292 
THR HXT  H N N 293 
TRP N    N N N 294 
TRP CA   C N S 295 
TRP C    C N N 296 
TRP O    O N N 297 
TRP CB   C N N 298 
TRP CG   C Y N 299 
TRP CD1  C Y N 300 
TRP CD2  C Y N 301 
TRP NE1  N Y N 302 
TRP CE2  C Y N 303 
TRP CE3  C Y N 304 
TRP CZ2  C Y N 305 
TRP CZ3  C Y N 306 
TRP CH2  C Y N 307 
TRP OXT  O N N 308 
TRP H    H N N 309 
TRP H2   H N N 310 
TRP HA   H N N 311 
TRP HB2  H N N 312 
TRP HB3  H N N 313 
TRP HD1  H N N 314 
TRP HE1  H N N 315 
TRP HE3  H N N 316 
TRP HZ2  H N N 317 
TRP HZ3  H N N 318 
TRP HH2  H N N 319 
TRP HXT  H N N 320 
TYR N    N N N 321 
TYR CA   C N S 322 
TYR C    C N N 323 
TYR O    O N N 324 
TYR CB   C N N 325 
TYR CG   C Y N 326 
TYR CD1  C Y N 327 
TYR CD2  C Y N 328 
TYR CE1  C Y N 329 
TYR CE2  C Y N 330 
TYR CZ   C Y N 331 
TYR OH   O N N 332 
TYR OXT  O N N 333 
TYR H    H N N 334 
TYR H2   H N N 335 
TYR HA   H N N 336 
TYR HB2  H N N 337 
TYR HB3  H N N 338 
TYR HD1  H N N 339 
TYR HD2  H N N 340 
TYR HE1  H N N 341 
TYR HE2  H N N 342 
TYR HH   H N N 343 
TYR HXT  H N N 344 
VAL N    N N N 345 
VAL CA   C N S 346 
VAL C    C N N 347 
VAL O    O N N 348 
VAL CB   C N N 349 
VAL CG1  C N N 350 
VAL CG2  C N N 351 
VAL OXT  O N N 352 
VAL H    H N N 353 
VAL H2   H N N 354 
VAL HA   H N N 355 
VAL HB   H N N 356 
VAL HG11 H N N 357 
VAL HG12 H N N 358 
VAL HG13 H N N 359 
VAL HG21 H N N 360 
VAL HG22 H N N 361 
VAL HG23 H N N 362 
VAL HXT  H N N 363 
# 
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  
GLU N   CA   sing N N 83  
GLU N   H    sing N N 84  
GLU N   H2   sing N N 85  
GLU CA  C    sing N N 86  
GLU CA  CB   sing N N 87  
GLU CA  HA   sing N N 88  
GLU C   O    doub N N 89  
GLU C   OXT  sing N N 90  
GLU CB  CG   sing N N 91  
GLU CB  HB2  sing N N 92  
GLU CB  HB3  sing N N 93  
GLU CG  CD   sing N N 94  
GLU CG  HG2  sing N N 95  
GLU CG  HG3  sing N N 96  
GLU CD  OE1  doub N N 97  
GLU CD  OE2  sing N N 98  
GLU OE2 HE2  sing N N 99  
GLU OXT HXT  sing N N 100 
GLY N   CA   sing N N 101 
GLY N   H    sing N N 102 
GLY N   H2   sing N N 103 
GLY CA  C    sing N N 104 
GLY CA  HA2  sing N N 105 
GLY CA  HA3  sing N N 106 
GLY C   O    doub N N 107 
GLY C   OXT  sing N N 108 
GLY OXT HXT  sing N N 109 
GOL C1  O1   sing N N 110 
GOL C1  C2   sing N N 111 
GOL C1  H11  sing N N 112 
GOL C1  H12  sing N N 113 
GOL O1  HO1  sing N N 114 
GOL C2  O2   sing N N 115 
GOL C2  C3   sing N N 116 
GOL C2  H2   sing N N 117 
GOL O2  HO2  sing N N 118 
GOL C3  O3   sing N N 119 
GOL C3  H31  sing N N 120 
GOL C3  H32  sing N N 121 
GOL O3  HO3  sing N N 122 
HOH O   H1   sing N N 123 
HOH O   H2   sing N N 124 
ILE N   CA   sing N N 125 
ILE N   H    sing N N 126 
ILE N   H2   sing N N 127 
ILE CA  C    sing N N 128 
ILE CA  CB   sing N N 129 
ILE CA  HA   sing N N 130 
ILE C   O    doub N N 131 
ILE C   OXT  sing N N 132 
ILE CB  CG1  sing N N 133 
ILE CB  CG2  sing N N 134 
ILE CB  HB   sing N N 135 
ILE CG1 CD1  sing N N 136 
ILE CG1 HG12 sing N N 137 
ILE CG1 HG13 sing N N 138 
ILE CG2 HG21 sing N N 139 
ILE CG2 HG22 sing N N 140 
ILE CG2 HG23 sing N N 141 
ILE CD1 HD11 sing N N 142 
ILE CD1 HD12 sing N N 143 
ILE CD1 HD13 sing N N 144 
ILE OXT HXT  sing N N 145 
LEU N   CA   sing N N 146 
LEU N   H    sing N N 147 
LEU N   H2   sing N N 148 
LEU CA  C    sing N N 149 
LEU CA  CB   sing N N 150 
LEU CA  HA   sing N N 151 
LEU C   O    doub N N 152 
LEU C   OXT  sing N N 153 
LEU CB  CG   sing N N 154 
LEU CB  HB2  sing N N 155 
LEU CB  HB3  sing N N 156 
LEU CG  CD1  sing N N 157 
LEU CG  CD2  sing N N 158 
LEU CG  HG   sing N N 159 
LEU CD1 HD11 sing N N 160 
LEU CD1 HD12 sing N N 161 
LEU CD1 HD13 sing N N 162 
LEU CD2 HD21 sing N N 163 
LEU CD2 HD22 sing N N 164 
LEU CD2 HD23 sing N N 165 
LEU OXT HXT  sing N N 166 
LYS N   CA   sing N N 167 
LYS N   H    sing N N 168 
LYS N   H2   sing N N 169 
LYS CA  C    sing N N 170 
LYS CA  CB   sing N N 171 
LYS CA  HA   sing N N 172 
LYS C   O    doub N N 173 
LYS C   OXT  sing N N 174 
LYS CB  CG   sing N N 175 
LYS CB  HB2  sing N N 176 
LYS CB  HB3  sing N N 177 
LYS CG  CD   sing N N 178 
LYS CG  HG2  sing N N 179 
LYS CG  HG3  sing N N 180 
LYS CD  CE   sing N N 181 
LYS CD  HD2  sing N N 182 
LYS CD  HD3  sing N N 183 
LYS CE  NZ   sing N N 184 
LYS CE  HE2  sing N N 185 
LYS CE  HE3  sing N N 186 
LYS NZ  HZ1  sing N N 187 
LYS NZ  HZ2  sing N N 188 
LYS NZ  HZ3  sing N N 189 
LYS OXT HXT  sing N N 190 
MET N   CA   sing N N 191 
MET N   H    sing N N 192 
MET N   H2   sing N N 193 
MET CA  C    sing N N 194 
MET CA  CB   sing N N 195 
MET CA  HA   sing N N 196 
MET C   O    doub N N 197 
MET C   OXT  sing N N 198 
MET CB  CG   sing N N 199 
MET CB  HB2  sing N N 200 
MET CB  HB3  sing N N 201 
MET CG  SD   sing N N 202 
MET CG  HG2  sing N N 203 
MET CG  HG3  sing N N 204 
MET SD  CE   sing N N 205 
MET CE  HE1  sing N N 206 
MET CE  HE2  sing N N 207 
MET CE  HE3  sing N N 208 
MET OXT HXT  sing N N 209 
PHE N   CA   sing N N 210 
PHE N   H    sing N N 211 
PHE N   H2   sing N N 212 
PHE CA  C    sing N N 213 
PHE CA  CB   sing N N 214 
PHE CA  HA   sing N N 215 
PHE C   O    doub N N 216 
PHE C   OXT  sing N N 217 
PHE CB  CG   sing N N 218 
PHE CB  HB2  sing N N 219 
PHE CB  HB3  sing N N 220 
PHE CG  CD1  doub Y N 221 
PHE CG  CD2  sing Y N 222 
PHE CD1 CE1  sing Y N 223 
PHE CD1 HD1  sing N N 224 
PHE CD2 CE2  doub Y N 225 
PHE CD2 HD2  sing N N 226 
PHE CE1 CZ   doub Y N 227 
PHE CE1 HE1  sing N N 228 
PHE CE2 CZ   sing Y N 229 
PHE CE2 HE2  sing N N 230 
PHE CZ  HZ   sing N N 231 
PHE OXT HXT  sing N N 232 
PRO N   CA   sing N N 233 
PRO N   CD   sing N N 234 
PRO N   H    sing N N 235 
PRO CA  C    sing N N 236 
PRO CA  CB   sing N N 237 
PRO CA  HA   sing N N 238 
PRO C   O    doub N N 239 
PRO C   OXT  sing N N 240 
PRO CB  CG   sing N N 241 
PRO CB  HB2  sing N N 242 
PRO CB  HB3  sing N N 243 
PRO CG  CD   sing N N 244 
PRO CG  HG2  sing N N 245 
PRO CG  HG3  sing N N 246 
PRO CD  HD2  sing N N 247 
PRO CD  HD3  sing N N 248 
PRO OXT HXT  sing N N 249 
SER N   CA   sing N N 250 
SER N   H    sing N N 251 
SER N   H2   sing N N 252 
SER CA  C    sing N N 253 
SER CA  CB   sing N N 254 
SER CA  HA   sing N N 255 
SER C   O    doub N N 256 
SER C   OXT  sing N N 257 
SER CB  OG   sing N N 258 
SER CB  HB2  sing N N 259 
SER CB  HB3  sing N N 260 
SER OG  HG   sing N N 261 
SER OXT HXT  sing N N 262 
THR N   CA   sing N N 263 
THR N   H    sing N N 264 
THR N   H2   sing N N 265 
THR CA  C    sing N N 266 
THR CA  CB   sing N N 267 
THR CA  HA   sing N N 268 
THR C   O    doub N N 269 
THR C   OXT  sing N N 270 
THR CB  OG1  sing N N 271 
THR CB  CG2  sing N N 272 
THR CB  HB   sing N N 273 
THR OG1 HG1  sing N N 274 
THR CG2 HG21 sing N N 275 
THR CG2 HG22 sing N N 276 
THR CG2 HG23 sing N N 277 
THR OXT HXT  sing N N 278 
TRP N   CA   sing N N 279 
TRP N   H    sing N N 280 
TRP N   H2   sing N N 281 
TRP CA  C    sing N N 282 
TRP CA  CB   sing N N 283 
TRP CA  HA   sing N N 284 
TRP C   O    doub N N 285 
TRP C   OXT  sing N N 286 
TRP CB  CG   sing N N 287 
TRP CB  HB2  sing N N 288 
TRP CB  HB3  sing N N 289 
TRP CG  CD1  doub Y N 290 
TRP CG  CD2  sing Y N 291 
TRP CD1 NE1  sing Y N 292 
TRP CD1 HD1  sing N N 293 
TRP CD2 CE2  doub Y N 294 
TRP CD2 CE3  sing Y N 295 
TRP NE1 CE2  sing Y N 296 
TRP NE1 HE1  sing N N 297 
TRP CE2 CZ2  sing Y N 298 
TRP CE3 CZ3  doub Y N 299 
TRP CE3 HE3  sing N N 300 
TRP CZ2 CH2  doub Y N 301 
TRP CZ2 HZ2  sing N N 302 
TRP CZ3 CH2  sing Y N 303 
TRP CZ3 HZ3  sing N N 304 
TRP CH2 HH2  sing N N 305 
TRP OXT HXT  sing N N 306 
TYR N   CA   sing N N 307 
TYR N   H    sing N N 308 
TYR N   H2   sing N N 309 
TYR CA  C    sing N N 310 
TYR CA  CB   sing N N 311 
TYR CA  HA   sing N N 312 
TYR C   O    doub N N 313 
TYR C   OXT  sing N N 314 
TYR CB  CG   sing N N 315 
TYR CB  HB2  sing N N 316 
TYR CB  HB3  sing N N 317 
TYR CG  CD1  doub Y N 318 
TYR CG  CD2  sing Y N 319 
TYR CD1 CE1  sing Y N 320 
TYR CD1 HD1  sing N N 321 
TYR CD2 CE2  doub Y N 322 
TYR CD2 HD2  sing N N 323 
TYR CE1 CZ   doub Y N 324 
TYR CE1 HE1  sing N N 325 
TYR CE2 CZ   sing Y N 326 
TYR CE2 HE2  sing N N 327 
TYR CZ  OH   sing N N 328 
TYR OH  HH   sing N N 329 
TYR OXT HXT  sing N N 330 
VAL N   CA   sing N N 331 
VAL N   H    sing N N 332 
VAL N   H2   sing N N 333 
VAL CA  C    sing N N 334 
VAL CA  CB   sing N N 335 
VAL CA  HA   sing N N 336 
VAL C   O    doub N N 337 
VAL C   OXT  sing N N 338 
VAL CB  CG1  sing N N 339 
VAL CB  CG2  sing N N 340 
VAL CB  HB   sing N N 341 
VAL CG1 HG11 sing N N 342 
VAL CG1 HG12 sing N N 343 
VAL CG1 HG13 sing N N 344 
VAL CG2 HG21 sing N N 345 
VAL CG2 HG22 sing N N 346 
VAL CG2 HG23 sing N N 347 
VAL OXT HXT  sing N N 348 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6gxg 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 2 1' 
_space_group.name_Hall        'P 2y' 
_space_group.IT_number        3 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FOV 
_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]   0.016009 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004840 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.032891 
_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]   0.013946 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . ALA A 1 2   ? 26.91785  -0.67398 14.32250 1.000 30.32996  ? -1  ALA A N    1 
ATOM   2    C CA   . ALA A 1 2   ? 26.40180  0.70515  14.55468 1.000 28.87729  ? -1  ALA A CA   1 
ATOM   3    C C    . ALA A 1 2   ? 25.24763  0.67660  15.54994 1.000 28.68849  ? -1  ALA A C    1 
ATOM   4    O O    . ALA A 1 2   ? 24.39731  -0.21264 15.50939 1.000 28.39378  ? -1  ALA A O    1 
ATOM   5    C CB   . ALA A 1 2   ? 25.95390  1.32790  13.24538 1.000 28.88928  ? -1  ALA A CB   1 
ATOM   6    H H    . ALA A 1 2   ? 27.78225  -0.70644 14.53192 1.000 36.39595  ? -1  ALA A H    1 
ATOM   7    H HA   . ALA A 1 2   ? 27.11093  1.25713  14.91986 1.000 34.65275  ? -1  ALA A HA   1 
ATOM   8    H HB1  . ALA A 1 2   ? 25.60090  2.21404  13.42161 1.000 34.66714  ? -1  ALA A HB1  1 
ATOM   9    H HB2  . ALA A 1 2   ? 26.71535  1.38804  12.64749 1.000 34.66714  ? -1  ALA A HB2  1 
ATOM   10   H HB3  . ALA A 1 2   ? 25.26580  0.77042  12.84961 1.000 34.66714  ? -1  ALA A HB3  1 
ATOM   11   N N    . MET A 1 3   ? 25.22139  1.65379  16.44758 1.000 27.46374  ? 0   MET A N    1 
ATOM   12   C CA   . MET A 1 3   ? 24.16261  1.74995  17.43813 1.000 25.88566  ? 0   MET A CA   1 
ATOM   13   C C    . MET A 1 3   ? 22.98419  2.52252  16.84519 1.000 23.14795  ? 0   MET A C    1 
ATOM   14   O O    . MET A 1 3   ? 23.01126  2.95489  15.69106 1.000 22.73871  ? 0   MET A O    1 
ATOM   15   C CB   . MET A 1 3   ? 24.70814  2.38017  18.71635 1.000 27.78001  ? 0   MET A CB   1 
ATOM   16   C CG   . MET A 1 3   ? 25.92036  1.64533  19.29166 1.000 30.52859  ? 0   MET A CG   1 
ATOM   17   S SD   . MET A 1 3   ? 25.63367  -0.11523 19.58156 1.000 34.09459  ? 0   MET A SD   1 
ATOM   18   C CE   . MET A 1 3   ? 24.34650  -0.04866 20.82215 1.000 33.00318  ? 0   MET A CE   1 
ATOM   19   H H    . MET A 1 3   ? 25.81103  2.27741  16.50245 1.000 32.95648  ? 0   MET A H    1 
ATOM   20   H HA   . MET A 1 3   ? 23.84867  0.86368  17.67659 1.000 31.06279  ? 0   MET A HA   1 
ATOM   21   H HB2  . MET A 1 3   ? 24.97715  3.29226  18.52493 1.000 33.33601  ? 0   MET A HB2  1 
ATOM   22   H HB3  . MET A 1 3   ? 24.01028  2.37457  19.39004 1.000 33.33601  ? 0   MET A HB3  1 
ATOM   23   H HG2  . MET A 1 3   ? 26.65919  1.72599  18.66834 1.000 36.63430  ? 0   MET A HG2  1 
ATOM   24   H HG3  . MET A 1 3   ? 26.15695  2.05024  20.14076 1.000 36.63430  ? 0   MET A HG3  1 
ATOM   25   H HE1  . MET A 1 3   ? 24.15939  -0.94870 21.13169 1.000 39.60382  ? 0   MET A HE1  1 
ATOM   26   H HE2  . MET A 1 3   ? 24.64973  0.49949  21.56274 1.000 39.60382  ? 0   MET A HE2  1 
ATOM   27   H HE3  . MET A 1 3   ? 23.54871  0.33848  20.42902 1.000 39.60382  ? 0   MET A HE3  1 
ATOM   28   N N    . GLY A 1 4   ? 21.92321  2.68336  17.63214 1.000 21.59058  ? 1   GLY A N    1 
ATOM   29   C CA   . GLY A 1 4   ? 20.74833  3.39240  17.16559 1.000 21.85734  ? 1   GLY A CA   1 
ATOM   30   C C    . GLY A 1 4   ? 19.82364  2.60287  16.26629 1.000 22.99779  ? 1   GLY A C    1 
ATOM   31   O O    . GLY A 1 4   ? 18.91743  3.19197  15.66368 1.000 21.97278  ? 1   GLY A O    1 
ATOM   32   H H    . GLY A 1 4   ? 21.86424  2.38976  18.43831 1.000 25.90870  ? 1   GLY A H    1 
ATOM   33   H HA2  . GLY A 1 4   ? 20.23390  3.67674  17.93722 1.000 26.22881  ? 1   GLY A HA2  1 
ATOM   34   H HA3  . GLY A 1 4   ? 21.03747  4.17612  16.67256 1.000 26.22881  ? 1   GLY A HA3  1 
ATOM   35   N N    . SER A 1 5   ? 20.00984  1.28557  16.16183 1.000 25.41944  ? 2   SER A N    1 
ATOM   36   C CA   . SER A 1 5   ? 19.18981  0.49257  15.25345 1.000 30.71076  ? 2   SER A CA   1 
ATOM   37   C C    . SER A 1 5   ? 17.75964  0.33135  15.75090 1.000 25.39184  ? 2   SER A C    1 
ATOM   38   O O    . SER A 1 5   ? 16.87743  -0.01264 14.95691 1.000 23.47244  ? 2   SER A O    1 
ATOM   39   C CB   . SER A 1 5   ? 19.82542  -0.88076 15.03070 1.000 40.34443  ? 2   SER A CB   1 
ATOM   40   O OG   . SER A 1 5   ? 19.95078  -1.58798 16.25098 1.000 47.99413  ? 2   SER A OG   1 
ATOM   41   H H    . SER A 1 5   ? 20.59665  0.83540  16.60069 1.000 30.50333  ? 2   SER A H    1 
ATOM   42   H HA   . SER A 1 5   ? 19.15407  0.94542  14.39640 1.000 36.85291  ? 2   SER A HA   1 
ATOM   43   H HB2  . SER A 1 5   ? 19.26534  -1.39257 14.42634 1.000 48.41331  ? 2   SER A HB2  1 
ATOM   44   H HB3  . SER A 1 5   ? 20.70706  -0.76068 14.64444 1.000 48.41331  ? 2   SER A HB3  1 
ATOM   45   H HG   . SER A 1 5   ? 20.37046  -1.12303 16.81070 1.000 57.59295  ? 2   SER A HG   1 
ATOM   46   N N    . GLY A 1 6   ? 17.51041  0.57053  17.03941 1.000 20.46368  ? 3   GLY A N    1 
ATOM   47   C CA   . GLY A 1 6   ? 16.15637  0.50749  17.55646 1.000 19.38927  ? 3   GLY A CA   1 
ATOM   48   C C    . GLY A 1 6   ? 15.22240  1.52446  16.93799 1.000 19.63807  ? 3   GLY A C    1 
ATOM   49   O O    . GLY A 1 6   ? 14.00407  1.32697  16.96027 1.000 23.61014  ? 3   GLY A O    1 
ATOM   50   H H    . GLY A 1 6   ? 18.10712  0.76945  17.62591 1.000 24.55641  ? 3   GLY A H    1 
ATOM   51   H HA2  . GLY A 1 6   ? 15.79420  -0.37607 17.38601 1.000 23.26712  ? 3   GLY A HA2  1 
ATOM   52   H HA3  . GLY A 1 6   ? 16.17665  0.66115  18.51400 1.000 23.26712  ? 3   GLY A HA3  1 
ATOM   53   N N    A LEU A 1 7   ? 15.75060  2.63281  16.42578 1.000 20.02361  ? 4   LEU A N    1 
ATOM   54   N N    B LEU A 1 7   ? 15.77522  2.58063  16.34036 0.000 20.02361  ? 4   LEU A N    1 
ATOM   55   C CA   A LEU A 1 7   ? 14.90241  3.65645  15.83233 1.000 23.07361  ? 4   LEU A CA   1 
ATOM   56   C CA   B LEU A 1 7   ? 14.98872  3.60208  15.66576 0.000 23.07361  ? 4   LEU A CA   1 
ATOM   57   C C    A LEU A 1 7   ? 14.58388  3.39887  14.36513 1.000 26.38361  ? 4   LEU A C    1 
ATOM   58   C C    B LEU A 1 7   ? 15.12200  3.47313  14.15370 0.000 26.38361  ? 4   LEU A C    1 
ATOM   59   O O    A LEU A 1 7   ? 13.71219  4.07643  13.80986 1.000 26.14361  ? 4   LEU A O    1 
ATOM   60   O O    B LEU A 1 7   ? 15.42344  4.45386  13.46535 0.000 26.14361  ? 4   LEU A O    1 
ATOM   61   C CB   A LEU A 1 7   ? 15.56633  5.03180  15.93401 1.000 25.79361  ? 4   LEU A CB   1 
ATOM   62   C CB   B LEU A 1 7   ? 15.45505  4.98885  16.10752 0.000 25.79361  ? 4   LEU A CB   1 
ATOM   63   C CG   A LEU A 1 7   ? 15.77009  5.61401  17.32843 1.000 28.28361  ? 4   LEU A CG   1 
ATOM   64   C CG   B LEU A 1 7   ? 15.56608  5.16538  17.62176 0.000 28.28361  ? 4   LEU A CG   1 
ATOM   65   C CD1  A LEU A 1 7   ? 16.44257  6.97479  17.22204 1.000 27.86361  ? 4   LEU A CD1  1 
ATOM   66   C CD1  B LEU A 1 7   ? 16.01280  6.57327  17.96771 0.000 27.86361  ? 4   LEU A CD1  1 
ATOM   67   C CD2  A LEU A 1 7   ? 14.44993  5.72543  18.07400 1.000 28.48361  ? 4   LEU A CD2  1 
ATOM   68   C CD2  B LEU A 1 7   ? 14.24200  4.83602  18.29378 0.000 28.48361  ? 4   LEU A CD2  1 
ATOM   69   H H    A LEU A 1 7   ? 16.59162  2.81191  16.41109 1.000 24.02833  ? 4   LEU A H    1 
ATOM   70   H H    B LEU A 1 7   ? 16.62203  2.72820  16.31313 0.000 24.02833  ? 4   LEU A H    1 
ATOM   71   H HA   A LEU A 1 7   ? 14.07183  3.67479  16.33303 1.000 27.68833  ? 4   LEU A HA   1 
ATOM   72   H HA   B LEU A 1 7   ? 14.05382  3.49348  15.90040 0.000 27.68833  ? 4   LEU A HA   1 
ATOM   73   H HB2  A LEU A 1 7   ? 16.44376  4.96838  15.52536 1.000 30.95233  ? 4   LEU A HB2  1 
ATOM   74   H HB2  B LEU A 1 7   ? 16.33164  5.15538  15.72706 0.000 30.95233  ? 4   LEU A HB2  1 
ATOM   75   H HB3  A LEU A 1 7   ? 15.01689  5.66320  15.44376 1.000 30.95233  ? 4   LEU A HB3  1 
ATOM   76   H HB3  B LEU A 1 7   ? 14.82115  5.64626  15.78058 0.000 30.95233  ? 4   LEU A HB3  1 
ATOM   77   H HG   A LEU A 1 7   ? 16.34189  5.02140  17.84103 1.000 33.94033  ? 4   LEU A HG   1 
ATOM   78   H HG   B LEU A 1 7   ? 16.23570  4.55207  17.96288 0.000 33.94033  ? 4   LEU A HG   1 
ATOM   79   H HD11 A LEU A 1 7   ? 16.60885  7.31553  18.11487 1.000 33.43633  ? 4   LEU A HD11 1 
ATOM   80   H HD11 B LEU A 1 7   ? 16.10237  6.64853  18.93063 0.000 33.43633  ? 4   LEU A HD11 1 
ATOM   81   H HD12 A LEU A 1 7   ? 17.28090  6.87625  16.74414 1.000 33.43633  ? 4   LEU A HD12 1 
ATOM   82   H HD12 B LEU A 1 7   ? 16.86656  6.74739  17.54147 0.000 33.43633  ? 4   LEU A HD12 1 
ATOM   83   H HD13 A LEU A 1 7   ? 15.85666  7.57984  16.74088 1.000 33.43633  ? 4   LEU A HD13 1 
ATOM   84   H HD13 B LEU A 1 7   ? 15.34845  7.20314  17.64707 0.000 33.43633  ? 4   LEU A HD13 1 
ATOM   85   H HD21 A LEU A 1 7   ? 14.59963  6.18672  18.91406 1.000 34.18033  ? 4   LEU A HD21 1 
ATOM   86   H HD21 B LEU A 1 7   ? 14.28583  5.10244  19.22544 0.000 34.18033  ? 4   LEU A HD21 1 
ATOM   87   H HD22 A LEU A 1 7   ? 13.82112  6.22486  17.52987 1.000 34.18033  ? 4   LEU A HD22 1 
ATOM   88   H HD22 B LEU A 1 7   ? 13.53103  5.31941  17.84460 0.000 34.18033  ? 4   LEU A HD22 1 
ATOM   89   H HD23 A LEU A 1 7   ? 14.10632  4.83416  18.24269 1.000 34.18033  ? 4   LEU A HD23 1 
ATOM   90   H HD23 B LEU A 1 7   ? 14.08436  3.88105  18.22989 0.000 34.18033  ? 4   LEU A HD23 1 
ATOM   91   N N    A ALA A 1 8   ? 15.25898  2.43738  13.73200 1.000 30.57361  ? 5   ALA A N    1 
ATOM   92   N N    B ALA A 1 8   ? 14.90990  2.26670  13.62995 0.000 30.57361  ? 5   ALA A N    1 
ATOM   93   C CA   A ALA A 1 8   ? 15.15508  2.28572  12.28460 1.000 34.48361  ? 5   ALA A CA   1 
ATOM   94   C CA   B ALA A 1 8   ? 14.91125  2.03569  12.19140 0.000 34.48361  ? 5   ALA A CA   1 
ATOM   95   C C    A ALA A 1 8   ? 13.71530  2.06245  11.84022 1.000 33.81361  ? 5   ALA A C    1 
ATOM   96   C C    B ALA A 1 8   ? 13.50974  1.93811  11.61022 0.000 33.81361  ? 5   ALA A C    1 
ATOM   97   O O    A ALA A 1 8   ? 13.29596  2.57862  10.79780 1.000 31.31361  ? 5   ALA A O    1 
ATOM   98   O O    B ALA A 1 8   ? 13.30976  2.27785  10.43944 0.000 31.31361  ? 5   ALA A O    1 
ATOM   99   C CB   A ALA A 1 8   ? 16.04380  1.13256  11.81894 1.000 37.43361  ? 5   ALA A CB   1 
ATOM   100  C CB   B ALA A 1 8   ? 15.67628  0.74995  11.85956 0.000 37.43361  ? 5   ALA A CB   1 
ATOM   101  H H    A ALA A 1 8   ? 15.77743  1.86739  14.11399 1.000 36.68833  ? 5   ALA A H    1 
ATOM   102  H H    B ALA A 1 8   ? 14.76120  1.55865  14.09488 0.000 36.68833  ? 5   ALA A H    1 
ATOM   103  H HA   A ALA A 1 8   ? 15.46753  3.10309  11.86606 1.000 41.38033  ? 5   ALA A HA   1 
ATOM   104  H HA   B ALA A 1 8   ? 15.36920  2.77164  11.75602 0.000 41.38033  ? 5   ALA A HA   1 
ATOM   105  H HB1  A ALA A 1 8   ? 15.97702  1.05190  10.85461 1.000 44.92033  ? 5   ALA A HB1  1 
ATOM   106  H HB1  B ALA A 1 8   ? 15.67513  0.62098  10.89817 0.000 44.92033  ? 5   ALA A HB1  1 
ATOM   107  H HB2  A ALA A 1 8   ? 16.96137  1.31870  12.07255 1.000 44.92033  ? 5   ALA A HB2  1 
ATOM   108  H HB2  B ALA A 1 8   ? 16.58768  0.83285  12.18109 0.000 44.92033  ? 5   ALA A HB2  1 
ATOM   109  H HB3  A ALA A 1 8   ? 15.74385  0.31234  12.24104 1.000 44.92033  ? 5   ALA A HB3  1 
ATOM   110  H HB3  B ALA A 1 8   ? 15.23898  0.00115  12.29427 0.000 44.92033  ? 5   ALA A HB3  1 
ATOM   111  N N    A LYS A 1 9   ? 12.94449  1.28696  12.60376 1.000 34.28361  ? 6   LYS A N    1 
ATOM   112  N N    B LYS A 1 9   ? 12.53957  1.48129  12.40184 0.000 34.28361  ? 6   LYS A N    1 
ATOM   113  C CA   A LYS A 1 9   ? 11.56343  1.03071  12.20902 1.000 42.45361  ? 6   LYS A CA   1 
ATOM   114  C CA   B LYS A 1 9   ? 11.14866  1.42602  11.97487 0.000 42.45361  ? 6   LYS A CA   1 
ATOM   115  C C    A LYS A 1 9   ? 10.67755  2.23785  12.47738 1.000 39.52361  ? 6   LYS A C    1 
ATOM   116  C C    B LYS A 1 9   ? 10.39172  2.68798  12.36803 0.000 39.52361  ? 6   LYS A C    1 
ATOM   117  O O    A LYS A 1 9   ? 9.78499   2.54855  11.68048 1.000 46.66361  ? 6   LYS A O    1 
ATOM   118  O O    B LYS A 1 9   ? 9.63334   3.23535  11.55992 0.000 46.66361  ? 6   LYS A O    1 
ATOM   119  C CB   A LYS A 1 9   ? 11.01912  -0.19065 12.94654 1.000 55.58361  ? 6   LYS A CB   1 
ATOM   120  C CB   B LYS A 1 9   ? 10.46188  0.20917  12.60012 0.000 55.58361  ? 6   LYS A CB   1 
ATOM   121  C CG   A LYS A 1 9   ? 11.11752  -1.47972 12.15710 1.000 62.05361  ? 6   LYS A CG   1 
ATOM   122  C CG   B LYS A 1 9   ? 11.25708  -1.08423 12.49175 0.000 62.05361  ? 6   LYS A CG   1 
ATOM   123  C CD   A LYS A 1 9   ? 10.09104  -1.51611 11.03686 1.000 66.99361  ? 6   LYS A CD   1 
ATOM   124  C CD   B LYS A 1 9   ? 11.48238  -1.48818 11.04365 0.000 66.99361  ? 6   LYS A CD   1 
ATOM   125  C CE   A LYS A 1 9   ? 10.75865  -1.57538 9.67506  1.000 73.71361  ? 6   LYS A CE   1 
ATOM   126  C CE   B LYS A 1 9   ? 12.36073  -2.72611 10.94698 0.000 73.71361  ? 6   LYS A CE   1 
ATOM   127  N NZ   A LYS A 1 9   ? 11.45526  -2.87274 9.45878  1.000 79.49361  ? 6   LYS A NZ   1 
ATOM   128  N NZ   B LYS A 1 9   ? 12.62850  -3.11027 9.53366  0.000 79.49361  ? 6   LYS A NZ   1 
ATOM   129  H H    A LYS A 1 9   ? 13.19166  0.90806  13.33515 1.000 41.14033  ? 6   LYS A H    1 
ATOM   130  H H    B LYS A 1 9   ? 12.66618  1.19388  13.20244 0.000 41.14033  ? 6   LYS A H    1 
ATOM   131  H HA   A LYS A 1 9   ? 11.54441  0.84042  11.25806 1.000 50.94433  ? 6   LYS A HA   1 
ATOM   132  H HA   B LYS A 1 9   ? 11.11511  1.33148  11.01007 0.000 50.94433  ? 6   LYS A HA   1 
ATOM   133  H HB2  A LYS A 1 9   ? 11.52213  -0.30798 13.76759 1.000 66.70033  ? 6   LYS A HB2  1 
ATOM   134  H HB2  B LYS A 1 9   ? 10.31617  0.38626  13.54262 0.000 66.70033  ? 6   LYS A HB2  1 
ATOM   135  H HB3  A LYS A 1 9   ? 10.08277  -0.03954 13.14983 1.000 66.70033  ? 6   LYS A HB3  1 
ATOM   136  H HB3  B LYS A 1 9   ? 9.61217   0.06981  12.15350 0.000 66.70033  ? 6   LYS A HB3  1 
ATOM   137  H HG2  A LYS A 1 9   ? 12.00178  -1.55118 11.76483 1.000 74.46433  ? 6   LYS A HG2  1 
ATOM   138  H HG2  B LYS A 1 9   ? 12.12314  -0.96383 12.91169 0.000 74.46433  ? 6   LYS A HG2  1 
ATOM   139  H HG3  A LYS A 1 9   ? 10.95434  -2.23246 12.74673 1.000 74.46433  ? 6   LYS A HG3  1 
ATOM   140  H HG3  B LYS A 1 9   ? 10.77033  -1.79740 12.93375 0.000 74.46433  ? 6   LYS A HG3  1 
ATOM   141  H HD2  A LYS A 1 9   ? 9.53281   -2.30295 11.13759 1.000 80.39233  ? 6   LYS A HD2  1 
ATOM   142  H HD2  B LYS A 1 9   ? 10.62866  -1.68558 10.62759 0.000 80.39233  ? 6   LYS A HD2  1 
ATOM   143  H HD3  A LYS A 1 9   ? 9.54528   -0.71510 11.07460 1.000 80.39233  ? 6   LYS A HD3  1 
ATOM   144  H HD3  B LYS A 1 9   ? 11.92185  -0.76365 10.57161 0.000 80.39233  ? 6   LYS A HD3  1 
ATOM   145  H HE2  A LYS A 1 9   ? 10.08591  -1.47256 8.98387  1.000 88.45633  ? 6   LYS A HE2  1 
ATOM   146  H HE2  B LYS A 1 9   ? 13.21088  -2.54896 11.37914 0.000 88.45633  ? 6   LYS A HE2  1 
ATOM   147  H HE3  A LYS A 1 9   ? 11.41417  -0.86350 9.60852  1.000 88.45633  ? 6   LYS A HE3  1 
ATOM   148  H HE3  B LYS A 1 9   ? 11.91499  -3.46878 11.38363 0.000 88.45633  ? 6   LYS A HE3  1 
ATOM   149  H HZ1  A LYS A 1 9   ? 11.86327  -2.87101 8.66781  1.000 95.39233  ? 6   LYS A HZ1  1 
ATOM   150  H HZ1  B LYS A 1 9   ? 13.15446  -3.82776 9.50766  0.000 95.39233  ? 6   LYS A HZ1  1 
ATOM   151  H HZ2  A LYS A 1 9   ? 12.06226  -3.00236 10.09661 1.000 95.39233  ? 6   LYS A HZ2  1 
ATOM   152  H HZ2  B LYS A 1 9   ? 11.86362  -3.29766 9.11900  0.000 95.39233  ? 6   LYS A HZ2  1 
ATOM   153  H HZ3  A LYS A 1 9   ? 10.86764  -3.54086 9.47919  1.000 95.39233  ? 6   LYS A HZ3  1 
ATOM   154  H HZ3  B LYS A 1 9   ? 13.03167  -2.44100 9.10746  0.000 95.39233  ? 6   LYS A HZ3  1 
ATOM   155  N N    A TYR A 1 10  ? 10.91645  2.93116  13.58905 1.000 23.98361  ? 7   TYR A N    1 
ATOM   156  N N    B TYR A 1 10  ? 10.58836  3.15818  13.60259 0.000 23.98361  ? 7   TYR A N    1 
ATOM   157  C CA   A TYR A 1 10  ? 10.07806  4.06318  13.94748 1.000 22.14361  ? 7   TYR A CA   1 
ATOM   158  C CA   B TYR A 1 10  ? 9.93117   4.38163  14.04529 0.000 22.14361  ? 7   TYR A CA   1 
ATOM   159  C C    A TYR A 1 10  ? 10.38598  5.28566  13.08604 1.000 28.42361  ? 7   TYR A C    1 
ATOM   160  C C    B TYR A 1 10  ? 10.30780  5.55868  13.15582 0.000 28.42361  ? 7   TYR A C    1 
ATOM   161  O O    A TYR A 1 10  ? 9.47156   6.01961  12.69340 1.000 23.85361  ? 7   TYR A O    1 
ATOM   162  O O    B TYR A 1 10  ? 9.44655   6.35930  12.77256 0.000 23.85361  ? 7   TYR A O    1 
ATOM   163  C CB   A TYR A 1 10  ? 10.30554  4.42134  15.41294 1.000 14.57361  ? 7   TYR A CB   1 
ATOM   164  C CB   B TYR A 1 10  ? 10.32284  4.67620  15.49294 0.000 14.57361  ? 7   TYR A CB   1 
ATOM   165  C CG   A TYR A 1 10  ? 10.08332  3.32848  16.44760 1.000 10.80361  ? 7   TYR A CG   1 
ATOM   166  C CG   B TYR A 1 10  ? 10.09202  3.52384  16.44349 0.000 10.80361  ? 7   TYR A CG   1 
ATOM   167  C CD1  A TYR A 1 10  ? 8.92345   2.55940  16.46866 1.000 10.17361  ? 7   TYR A CD1  1 
ATOM   168  C CD1  B TYR A 1 10  ? 8.85663   2.89545  16.51824 0.000 10.17361  ? 7   TYR A CD1  1 
ATOM   169  C CD2  A TYR A 1 10  ? 11.03648  3.09336  17.42750 1.000 11.96361  ? 7   TYR A CD2  1 
ATOM   170  C CD2  B TYR A 1 10  ? 11.11420  3.05810  17.25997 0.000 11.96361  ? 7   TYR A CD2  1 
ATOM   171  C CE1  A TYR A 1 10  ? 8.72971   1.58779  17.44041 1.000 9.88361   ? 7   TYR A CE1  1 
ATOM   172  C CE1  B TYR A 1 10  ? 8.64333   1.84028  17.38520 0.000 9.88361   ? 7   TYR A CE1  1 
ATOM   173  C CE2  A TYR A 1 10  ? 10.84773  2.13079  18.40030 1.000 11.00361  ? 7   TYR A CE2  1 
ATOM   174  C CE2  B TYR A 1 10  ? 10.91095  2.00374  18.12885 0.000 11.00361  ? 7   TYR A CE2  1 
ATOM   175  C CZ   A TYR A 1 10  ? 9.69935   1.37921  18.39687 1.000 8.88361   ? 7   TYR A CZ   1 
ATOM   176  C CZ   B TYR A 1 10  ? 9.67406   1.39862  18.18768 0.000 8.88361   ? 7   TYR A CZ   1 
ATOM   177  O OH   A TYR A 1 10  ? 9.51727   0.42001  19.35941 1.000 13.45361  ? 7   TYR A OH   1 
ATOM   178  O OH   B TYR A 1 10  ? 9.46770   0.34797  19.05185 0.000 13.45361  ? 7   TYR A OH   1 
ATOM   179  H H    A TYR A 1 10  ? 11.55161  2.76595  14.14482 1.000 28.78033  ? 7   TYR A H    1 
ATOM   180  H H    B TYR A 1 10  ? 11.09213  2.78998  14.19441 0.000 28.78033  ? 7   TYR A H    1 
ATOM   181  H HA   A TYR A 1 10  ? 9.14984   3.81414  13.81603 1.000 26.57233  ? 7   TYR A HA   1 
ATOM   182  H HA   B TYR A 1 10  ? 8.97004   4.25899  13.99962 0.000 26.57233  ? 7   TYR A HA   1 
ATOM   183  H HB2  A TYR A 1 10  ? 11.22566  4.71335  15.50788 1.000 17.48833  ? 7   TYR A HB2  1 
ATOM   184  H HB2  B TYR A 1 10  ? 11.26731  4.89558  15.52028 0.000 17.48833  ? 7   TYR A HB2  1 
ATOM   185  H HB3  A TYR A 1 10  ? 9.70232   5.14671  15.63844 1.000 17.48833  ? 7   TYR A HB3  1 
ATOM   186  H HB3  B TYR A 1 10  ? 9.79826   5.42827  15.80934 0.000 17.48833  ? 7   TYR A HB3  1 
ATOM   187  H HD1  A TYR A 1 10  ? 8.26918   2.69858  15.82254 1.000 12.20833  ? 7   TYR A HD1  1 
ATOM   188  H HD1  B TYR A 1 10  ? 8.16068   3.18934  15.97585 0.000 12.20833  ? 7   TYR A HD1  1 
ATOM   189  H HD2  A TYR A 1 10  ? 11.81978  3.59470  17.42966 1.000 14.35633  ? 7   TYR A HD2  1 
ATOM   190  H HD2  B TYR A 1 10  ? 11.95041  3.46325  17.22107 0.000 14.35633  ? 7   TYR A HD2  1 
ATOM   191  H HE1  A TYR A 1 10  ? 7.95023   1.08057  17.44602 1.000 11.86033  ? 7   TYR A HE1  1 
ATOM   192  H HE1  B TYR A 1 10  ? 7.80949   1.43058  17.42706 0.000 11.86033  ? 7   TYR A HE1  1 
ATOM   193  H HE2  A TYR A 1 10  ? 11.49503  1.99289  19.05367 1.000 13.20433  ? 7   TYR A HE2  1 
ATOM   194  H HE2  B TYR A 1 10  ? 11.60461  1.70396  18.67094 0.000 13.20433  ? 7   TYR A HE2  1 
ATOM   195  H HH   A TYR A 1 10  ? 10.02260  0.56979  20.01348 1.000 16.14433  ? 7   TYR A HH   1 
ATOM   196  H HH   B TYR A 1 10  ? 10.16727  0.19566  19.49116 0.000 16.14433  ? 7   TYR A HH   1 
ATOM   197  N N    A LEU A 1 11  ? 11.66582  5.52996  12.80032 1.000 23.71361  ? 8   LEU A N    1 
ATOM   198  N N    B LEU A 1 11  ? 11.59096  5.67951  12.81728 0.000 23.71361  ? 8   LEU A N    1 
ATOM   199  C CA   A LEU A 1 11  ? 12.10758  6.70499  12.05110 1.000 17.93361  ? 8   LEU A CA   1 
ATOM   200  C CA   B LEU A 1 11  ? 12.10487  6.78891  12.01710 0.000 17.93361  ? 8   LEU A CA   1 
ATOM   201  C C    A LEU A 1 11  ? 12.94719  6.23301  10.86946 1.000 19.44361  ? 8   LEU A C    1 
ATOM   202  C C    B LEU A 1 11  ? 12.93603  6.21030  10.87843 0.000 19.44361  ? 8   LEU A C    1 
ATOM   203  O O    A LEU A 1 11  ? 14.17643  6.13105  10.97197 1.000 16.30361  ? 8   LEU A O    1 
ATOM   204  O O    B LEU A 1 11  ? 14.14678  6.00089  11.02339 0.000 16.30361  ? 8   LEU A O    1 
ATOM   205  C CB   A LEU A 1 11  ? 12.91368  7.64568  12.94591 1.000 14.81361  ? 8   LEU A CB   1 
ATOM   206  C CB   B LEU A 1 11  ? 12.93677  7.73906  12.87644 0.000 14.81361  ? 8   LEU A CB   1 
ATOM   207  C CG   A LEU A 1 11  ? 12.18725  8.24993  14.14758 1.000 14.63361  ? 8   LEU A CG   1 
ATOM   208  C CG   B LEU A 1 11  ? 12.20151  8.37590  14.05710 0.000 14.63361  ? 8   LEU A CG   1 
ATOM   209  C CD1  A LEU A 1 11  ? 13.19281  8.95557  15.04049 1.000 14.38361  ? 8   LEU A CD1  1 
ATOM   210  C CD1  B LEU A 1 11  ? 13.16259  9.18703  14.91252 0.000 14.38361  ? 8   LEU A CD1  1 
ATOM   211  C CD2  A LEU A 1 11  ? 11.10018  9.20962  13.69850 1.000 16.32361  ? 8   LEU A CD2  1 
ATOM   212  C CD2  B LEU A 1 11  ? 11.04968  9.24505  13.57330 0.000 16.32361  ? 8   LEU A CD2  1 
ATOM   213  H H    A LEU A 1 11  ? 12.31279  5.01503  13.03670 1.000 28.45633  ? 8   LEU A H    1 
ATOM   214  H H    B LEU A 1 11  ? 12.19864  5.11559  13.04603 0.000 28.45633  ? 8   LEU A H    1 
ATOM   215  H HA   A LEU A 1 11  ? 11.33422  7.18068  11.70972 1.000 21.52033  ? 8   LEU A HA   1 
ATOM   216  H HA   B LEU A 1 11  ? 11.36435  7.28528  11.63481 0.000 21.52033  ? 8   LEU A HA   1 
ATOM   217  H HB2  A LEU A 1 11  ? 13.67219  7.15070  13.29312 1.000 17.77633  ? 8   LEU A HB2  1 
ATOM   218  H HB2  B LEU A 1 11  ? 13.68848  7.24348  13.23730 0.000 17.77633  ? 8   LEU A HB2  1 
ATOM   219  H HB3  A LEU A 1 11  ? 13.22224  8.38578  12.40007 1.000 17.77633  ? 8   LEU A HB3  1 
ATOM   220  H HB3  B LEU A 1 11  ? 13.25537  8.46018  12.31130 0.000 17.77633  ? 8   LEU A HB3  1 
ATOM   221  H HG   A LEU A 1 11  ? 11.75639  7.54454  14.65521 1.000 17.56033  ? 8   LEU A HG   1 
ATOM   222  H HG   B LEU A 1 11  ? 11.82951  7.67041  14.60918 0.000 17.56033  ? 8   LEU A HG   1 
ATOM   223  H HD11 A LEU A 1 11  ? 12.74161  9.26432  15.84173 1.000 17.26033  ? 8   LEU A HD11 1 
ATOM   224  H HD11 B LEU A 1 11  ? 12.66591  9.61175  15.62933 0.000 17.26033  ? 8   LEU A HD11 1 
ATOM   225  H HD12 A LEU A 1 11  ? 13.89726  8.33210  15.27699 1.000 17.26033  ? 8   LEU A HD12 1 
ATOM   226  H HD12 B LEU A 1 11  ? 13.83445  8.59311  15.28234 0.000 17.26033  ? 8   LEU A HD12 1 
ATOM   227  H HD13 A LEU A 1 11  ? 13.56686  9.71049  14.55978 1.000 17.26033  ? 8   LEU A HD13 1 
ATOM   228  H HD13 B LEU A 1 11  ? 13.58607  9.86147  14.35872 0.000 17.26033  ? 8   LEU A HD13 1 
ATOM   229  H HD21 A LEU A 1 11  ? 10.66507  9.58251  14.48115 1.000 19.58833  ? 8   LEU A HD21 1 
ATOM   230  H HD21 B LEU A 1 11  ? 10.69780  9.74931  14.32350 0.000 19.58833  ? 8   LEU A HD21 1 
ATOM   231  H HD22 A LEU A 1 11  ? 11.50254  9.91949  13.17401 1.000 19.58833  ? 8   LEU A HD22 1 
ATOM   232  H HD22 B LEU A 1 11  ? 11.37696  9.85204  12.89113 0.000 19.58833  ? 8   LEU A HD22 1 
ATOM   233  H HD23 A LEU A 1 11  ? 10.45449  8.72580  13.16008 1.000 19.58833  ? 8   LEU A HD23 1 
ATOM   234  H HD23 B LEU A 1 11  ? 10.35724  8.67487  13.20408 0.000 19.58833  ? 8   LEU A HD23 1 
ATOM   235  N N    . PRO A 1 12  ? 12.30972  5.93761  9.73203  1.000 19.29948  ? 9   PRO A N    1 
ATOM   236  C CA   A PRO A 1 12  ? 13.06915  5.41615  8.58286  0.414 20.53361  ? 9   PRO A CA   1 
ATOM   237  C CA   B PRO A 1 12  ? 13.07763  5.40726  8.59238  0.586 20.53361  ? 9   PRO A CA   1 
ATOM   238  C C    . PRO A 1 12  ? 14.22915  6.32340  8.20581  1.000 20.00512  ? 9   PRO A C    1 
ATOM   239  O O    . PRO A 1 12  ? 14.10831  7.55065  8.20559  1.000 19.11912  ? 9   PRO A O    1 
ATOM   240  C CB   A PRO A 1 12  ? 12.01722  5.34225  7.46472  0.414 23.72361  ? 9   PRO A CB   1 
ATOM   241  C CB   B PRO A 1 12  ? 12.02940  5.31314  7.47431  0.586 23.72361  ? 9   PRO A CB   1 
ATOM   242  C CG   A PRO A 1 12  ? 10.78124  6.03019  8.00470  0.414 26.19361  ? 9   PRO A CG   1 
ATOM   243  C CG   B PRO A 1 12  ? 10.71231  5.25229  8.19162  0.586 26.19361  ? 9   PRO A CG   1 
ATOM   244  C CD   A PRO A 1 12  ? 10.86183  5.91115  9.48931  0.414 21.86361  ? 9   PRO A CD   1 
ATOM   245  C CD   B PRO A 1 12  ? 10.88847  6.12005  9.40178  0.586 21.86361  ? 9   PRO A CD   1 
ATOM   246  H HA   A PRO A 1 12  ? 13.40763  4.52840  8.77838  0.414 24.64033  ? 9   PRO A HA   1 
ATOM   247  H HA   B PRO A 1 12  ? 13.42525  4.52544  8.79847  0.586 24.64033  ? 9   PRO A HA   1 
ATOM   248  H HB2  A PRO A 1 12  ? 12.34770  5.80000  6.67596  0.414 28.46833  ? 9   PRO A HB2  1 
ATOM   249  H HB2  B PRO A 1 12  ? 12.08028  6.09720  6.90548  0.586 28.46833  ? 9   PRO A HB2  1 
ATOM   250  H HB3  A PRO A 1 12  ? 11.82932  4.41396  7.25526  0.414 28.46833  ? 9   PRO A HB3  1 
ATOM   251  H HB3  B PRO A 1 12  ? 12.17690  4.51156  6.94837  0.586 28.46833  ? 9   PRO A HB3  1 
ATOM   252  H HG2  A PRO A 1 12  ? 10.78142  6.96182  7.73457  0.414 31.43233  ? 9   PRO A HG2  1 
ATOM   253  H HG2  B PRO A 1 12  ? 10.00803  5.59465  7.61918  0.586 31.43233  ? 9   PRO A HG2  1 
ATOM   254  H HG3  A PRO A 1 12  ? 9.98696   5.58714  7.66747  0.414 31.43233  ? 9   PRO A HG3  1 
ATOM   255  H HG3  B PRO A 1 12  ? 10.51690  4.33710  8.44686  0.586 31.43233  ? 9   PRO A HG3  1 
ATOM   256  H HD2  A PRO A 1 12  ? 10.42227  6.65919  9.92304  0.414 26.23633  ? 9   PRO A HD2  1 
ATOM   257  H HD2  B PRO A 1 12  ? 10.69709  7.04800  9.19394  0.586 26.23633  ? 9   PRO A HD2  1 
ATOM   258  H HD3  A PRO A 1 12  ? 10.47295  5.07615  9.79335  0.414 26.23633  ? 9   PRO A HD3  1 
ATOM   259  H HD3  B PRO A 1 12  ? 10.32199  5.81942  10.12952 0.586 26.23633  ? 9   PRO A HD3  1 
ATOM   260  N N    . SER A 1 13  ? 15.36015  5.69926  7.86118  1.000 25.09604  ? 10  SER A N    1 
ATOM   261  C CA   A SER A 1 13  ? 16.58818  6.44834  7.62862  0.416 28.24361  ? 10  SER A CA   1 
ATOM   262  C CA   B SER A 1 13  ? 16.59568  6.43120  7.61482  0.584 28.22361  ? 10  SER A CA   1 
ATOM   263  C C    . SER A 1 13  ? 16.51876  7.33931  6.39523  1.000 23.43511  ? 10  SER A C    1 
ATOM   264  O O    . SER A 1 13  ? 17.36665  8.22580  6.24515  1.000 20.19025  ? 10  SER A O    1 
ATOM   265  C CB   A SER A 1 13  ? 17.77466  5.48810  7.51468  0.416 35.97361  ? 10  SER A CB   1 
ATOM   266  C CB   B SER A 1 13  ? 17.75008  5.44281  7.42866  0.584 35.94361  ? 10  SER A CB   1 
ATOM   267  O OG   A SER A 1 13  ? 18.09775  4.92721  8.77549  0.416 38.42361  ? 10  SER A OG   1 
ATOM   268  O OG   B SER A 1 13  ? 17.54291  4.63551  6.28038  0.584 38.31361  ? 10  SER A OG   1 
ATOM   269  H H    A SER A 1 13  ? 15.43816  4.84913  7.75729  0.416 30.11525  ? 10  SER A H    1 
ATOM   270  H H    B SER A 1 13  ? 15.43481  4.84805  7.76387  0.584 30.11525  ? 10  SER A H    1 
ATOM   271  H HA   A SER A 1 13  ? 16.73941  7.02658  8.39259  0.416 33.89233  ? 10  SER A HA   1 
ATOM   272  H HA   B SER A 1 13  ? 16.77495  6.98895  8.38792  0.584 33.86833  ? 10  SER A HA   1 
ATOM   273  H HB2  A SER A 1 13  ? 17.54334  4.77285  6.90165  0.416 43.16833  ? 10  SER A HB2  1 
ATOM   274  H HB2  B SER A 1 13  ? 18.57649  5.93912  7.32085  0.584 43.13233  ? 10  SER A HB2  1 
ATOM   275  H HB3  A SER A 1 13  ? 18.54366  5.97578  7.18045  0.416 43.16833  ? 10  SER A HB3  1 
ATOM   276  H HB3  B SER A 1 13  ? 17.80582  4.87144  8.21054  0.584 43.13233  ? 10  SER A HB3  1 
ATOM   277  H HG   A SER A 1 13  ? 17.43526  4.51300  9.08393  0.416 46.10833  ? 10  SER A HG   1 
ATOM   278  H HG   B SER A 1 13  ? 16.81484  4.22198  6.34748  0.584 45.97633  ? 10  SER A HG   1 
ATOM   279  N N    . THR A 1 14  ? 15.54023  7.13981  5.51447  1.000 19.39774  ? 11  THR A N    1 
ATOM   280  C CA   . THR A 1 14  ? 15.44429  8.01005  4.35015  1.000 17.26694  ? 11  THR A CA   1 
ATOM   281  C C    . THR A 1 14  ? 14.87709  9.38673  4.67959  1.000 16.40845  ? 11  THR A C    1 
ATOM   282  O O    . THR A 1 14  ? 14.87163  10.25457 3.80246  1.000 17.61115  ? 11  THR A O    1 
ATOM   283  C CB   . THR A 1 14  ? 14.58705  7.37757  3.24819  1.000 16.56817  ? 11  THR A CB   1 
ATOM   284  O OG1  . THR A 1 14  ? 13.35816  6.90624  3.81091  1.000 17.78400  ? 11  THR A OG1  1 
ATOM   285  C CG2  . THR A 1 14  ? 15.31629  6.22522  2.58039  1.000 17.23198  ? 11  THR A CG2  1 
ATOM   286  H H    . THR A 1 14  ? 14.93983  6.52649  5.56881  1.000 23.27728  ? 11  THR A H    1 
ATOM   287  H HA   . THR A 1 14  ? 16.34122  8.11852  3.99709  1.000 20.72032  ? 11  THR A HA   1 
ATOM   288  H HB   . THR A 1 14  ? 14.39927  8.04296  2.56783  1.000 19.88181  ? 11  THR A HB   1 
ATOM   289  H HG1  . THR A 1 14  ? 12.86678  6.59274  3.20605  1.000 21.34080  ? 11  THR A HG1  1 
ATOM   290  H HG21 . THR A 1 14  ? 14.74331  5.80992  1.91697  1.000 20.67837  ? 11  THR A HG21 1 
ATOM   291  H HG22 . THR A 1 14  ? 16.11962  6.54936  2.14394  1.000 20.67837  ? 11  THR A HG22 1 
ATOM   292  H HG23 . THR A 1 14  ? 15.56393  5.56105  3.24255  1.000 20.67837  ? 11  THR A HG23 1 
ATOM   293  N N    . ILE A 1 15  ? 14.39688  9.61723  5.89865  1.000 15.10770  ? 12  ILE A N    1 
ATOM   294  C CA   . ILE A 1 15  ? 13.77698  10.88971 6.25889  1.000 16.31378  ? 12  ILE A CA   1 
ATOM   295  C C    . ILE A 1 15  ? 14.50986  11.46121 7.46327  1.000 15.60831  ? 12  ILE A C    1 
ATOM   296  O O    . ILE A 1 15  ? 14.41439  10.92155 8.57232  1.000 17.67536  ? 12  ILE A O    1 
ATOM   297  C CB   . ILE A 1 15  ? 12.27218  10.74217 6.53194  1.000 19.89648  ? 12  ILE A CB   1 
ATOM   298  C CG1  . ILE A 1 15  ? 11.57578  10.19791 5.28033  1.000 21.95562  ? 12  ILE A CG1  1 
ATOM   299  C CG2  . ILE A 1 15  ? 11.68139  12.08300 6.93329  1.000 20.86435  ? 12  ILE A CG2  1 
ATOM   300  C CD1  . ILE A 1 15  ? 10.23696  9.54271  5.53399  1.000 25.07300  ? 12  ILE A CD1  1 
ATOM   301  H H    . ILE A 1 15  ? 14.41909  9.04545  6.54066  1.000 18.12924  ? 12  ILE A H    1 
ATOM   302  H HA   . ILE A 1 15  ? 13.89696  11.51337 5.52571  1.000 19.57654  ? 12  ILE A HA   1 
ATOM   303  H HB   . ILE A 1 15  ? 12.13894  10.11756 7.26201  1.000 23.87578  ? 12  ILE A HB   1 
ATOM   304  H HG12 . ILE A 1 15  ? 11.42861  10.93354 4.66544  1.000 26.34674  ? 12  ILE A HG12 1 
ATOM   305  H HG13 . ILE A 1 15  ? 12.15256  9.53392  4.87126  1.000 26.34674  ? 12  ILE A HG13 1 
ATOM   306  H HG21 . ILE A 1 15  ? 10.71377  12.02516 6.89757  1.000 25.03722  ? 12  ILE A HG21 1 
ATOM   307  H HG22 . ILE A 1 15  ? 11.96691  12.29659 7.83538  1.000 25.03722  ? 12  ILE A HG22 1 
ATOM   308  H HG23 . ILE A 1 15  ? 11.99505  12.76343 6.31723  1.000 25.03722  ? 12  ILE A HG23 1 
ATOM   309  H HD11 . ILE A 1 15  ? 9.85585   9.26457  4.68647  1.000 30.08760  ? 12  ILE A HD11 1 
ATOM   310  H HD12 . ILE A 1 15  ? 10.36653  8.77122  6.10750  1.000 30.08760  ? 12  ILE A HD12 1 
ATOM   311  H HD13 . ILE A 1 15  ? 9.64958   10.18180 5.96695  1.000 30.08760  ? 12  ILE A HD13 1 
ATOM   312  N N    A LYS A 1 16  ? 15.23516  12.55889 7.24868  0.418 14.84361  ? 13  LYS A N    1 
ATOM   313  N N    B LYS A 1 16  ? 15.23414  12.55488 7.25304  0.582 14.31361  ? 13  LYS A N    1 
ATOM   314  C CA   A LYS A 1 16  ? 15.96131  13.21242 8.32517  0.418 12.85361  ? 13  LYS A CA   1 
ATOM   315  C CA   B LYS A 1 16  ? 15.95492  13.17230 8.35071  0.582 12.77361  ? 13  LYS A CA   1 
ATOM   316  C C    A LYS A 1 16  ? 15.00512  13.99399 9.22095  0.418 10.88361  ? 13  LYS A C    1 
ATOM   317  C C    B LYS A 1 16  ? 15.00128  13.97945 9.22742  0.582 12.18361  ? 13  LYS A C    1 
ATOM   318  O O    A LYS A 1 16  ? 13.93148  14.42890 8.79365  0.418 11.95361  ? 13  LYS A O    1 
ATOM   319  O O    B LYS A 1 16  ? 13.92679  14.41050 8.79913  0.582 14.72361  ? 13  LYS A O    1 
ATOM   320  C CB   A LYS A 1 16  ? 17.00058  14.18750 7.76404  0.418 15.29361  ? 13  LYS A CB   1 
ATOM   321  C CB   B LYS A 1 16  ? 17.06066  14.08918 7.82764  0.582 14.61361  ? 13  LYS A CB   1 
ATOM   322  C CG   A LYS A 1 16  ? 18.17270  13.54598 7.02976  0.418 17.85361  ? 13  LYS A CG   1 
ATOM   323  C CG   B LYS A 1 16  ? 18.06797  13.40056 6.91938  0.582 15.93361  ? 13  LYS A CG   1 
ATOM   324  C CD   A LYS A 1 16  ? 19.20784  14.59699 6.62112  0.418 21.65361  ? 13  LYS A CD   1 
ATOM   325  C CD   B LYS A 1 16  ? 19.22181  14.32576 6.56634  0.582 18.36361  ? 13  LYS A CD   1 
ATOM   326  C CE   A LYS A 1 16  ? 20.33306  13.98102 5.80132  0.418 23.23361  ? 13  LYS A CE   1 
ATOM   327  C CE   B LYS A 1 16  ? 20.20540  14.47013 7.71640  0.582 17.78361  ? 13  LYS A CE   1 
ATOM   328  N NZ   A LYS A 1 16  ? 21.30073  14.98388 5.26938  0.418 25.82361  ? 13  LYS A NZ   1 
ATOM   329  N NZ   B LYS A 1 16  ? 21.32217  15.38781 7.34973  0.582 22.65361  ? 13  LYS A NZ   1 
ATOM   330  H H    A LYS A 1 16  ? 15.32052  12.94313 6.48404  0.418 17.81233  ? 13  LYS A H    1 
ATOM   331  H H    B LYS A 1 16  ? 15.32101  12.95037 6.49433  0.582 17.17633  ? 13  LYS A H    1 
ATOM   332  H HA   A LYS A 1 16  ? 16.41418  12.53519 8.85163  0.418 15.42433  ? 13  LYS A HA   1 
ATOM   333  H HA   B LYS A 1 16  ? 16.36425  12.47765 8.88998  0.582 15.32833  ? 13  LYS A HA   1 
ATOM   334  H HB2  A LYS A 1 16  ? 16.55626  14.77950 7.13713  0.418 18.35233  ? 13  LYS A HB2  1 
ATOM   335  H HB2  B LYS A 1 16  ? 16.65246  14.80882 7.32128  0.582 17.53633  ? 13  LYS A HB2  1 
ATOM   336  H HB3  A LYS A 1 16  ? 17.36740  14.70004 8.50137  0.418 18.35233  ? 13  LYS A HB3  1 
ATOM   337  H HB3  B LYS A 1 16  ? 17.54711  14.45080 8.58494  0.582 17.53633  ? 13  LYS A HB3  1 
ATOM   338  H HG2  A LYS A 1 16  ? 18.60406  12.90072 7.61154  0.418 21.42433  ? 13  LYS A HG2  1 
ATOM   339  H HG2  B LYS A 1 16  ? 18.42870  12.62184 7.37144  0.582 19.12033  ? 13  LYS A HG2  1 
ATOM   340  H HG3  A LYS A 1 16  ? 17.84961  13.10585 6.22801  0.418 21.42433  ? 13  LYS A HG3  1 
ATOM   341  H HG3  B LYS A 1 16  ? 17.62889  13.13295 6.09689  0.582 19.12033  ? 13  LYS A HG3  1 
ATOM   342  H HD2  A LYS A 1 16  ? 18.77742  15.28010 6.08353  0.418 25.98433  ? 13  LYS A HD2  1 
ATOM   343  H HD2  B LYS A 1 16  ? 19.69900  13.96479 5.80286  0.582 22.03633  ? 13  LYS A HD2  1 
ATOM   344  H HD3  A LYS A 1 16  ? 19.59318  14.99523 7.41725  0.418 25.98433  ? 13  LYS A HD3  1 
ATOM   345  H HD3  B LYS A 1 16  ? 18.87275  15.20545 6.35376  0.582 22.03633  ? 13  LYS A HD3  1 
ATOM   346  H HE2  A LYS A 1 16  ? 20.82620  13.36167 6.36178  0.418 27.88033  ? 13  LYS A HE2  1 
ATOM   347  H HE2  B LYS A 1 16  ? 19.74770  14.83625 8.48929  0.582 21.34033  ? 13  LYS A HE2  1 
ATOM   348  H HE3  A LYS A 1 16  ? 19.94848  13.51033 5.04537  0.418 27.88033  ? 13  LYS A HE3  1 
ATOM   349  H HE3  B LYS A 1 16  ? 20.57946  13.60174 7.93290  0.582 21.34033  ? 13  LYS A HE3  1 
ATOM   350  H HZ1  A LYS A 1 16  ? 21.96960  14.57023 4.85272  0.418 30.98833  ? 13  LYS A HZ1  1 
ATOM   351  H HZ1  B LYS A 1 16  ? 21.79503  15.03978 6.68087  0.582 27.18433  ? 13  LYS A HZ1  1 
ATOM   352  H HZ2  A LYS A 1 16  ? 20.89215  15.52518 4.69304  0.418 30.98833  ? 13  LYS A HZ2  1 
ATOM   353  H HZ2  B LYS A 1 16  ? 20.99712  16.17593 7.09418  0.582 27.18433  ? 13  LYS A HZ2  1 
ATOM   354  H HZ3  A LYS A 1 16  ? 21.63282  15.47017 5.93671  0.418 30.98833  ? 13  LYS A HZ3  1 
ATOM   355  H HZ3  B LYS A 1 16  ? 21.85827  15.50970 8.04962  0.582 27.18433  ? 13  LYS A HZ3  1 
ATOM   356  N N    . LEU A 1 17  ? 15.41164  14.17563 10.47399 1.000 10.92488  ? 14  LEU A N    1 
ATOM   357  C CA   . LEU A 1 17  ? 14.68292  15.01377 11.41042 1.000 11.02570  ? 14  LEU A CA   1 
ATOM   358  C C    . LEU A 1 17  ? 15.13799  16.45517 11.23440 1.000 12.11083  ? 14  LEU A C    1 
ATOM   359  O O    . LEU A 1 17  ? 16.25571  16.71940 10.78458 1.000 14.42488  ? 14  LEU A O    1 
ATOM   360  C CB   . LEU A 1 17  ? 14.96400  14.56204 12.84061 1.000 12.01787  ? 14  LEU A CB   1 
ATOM   361  C CG   . LEU A 1 17  ? 14.64466  13.09539 13.12633 1.000 12.39683  ? 14  LEU A CG   1 
ATOM   362  C CD1  . LEU A 1 17  ? 15.00363  12.73799 14.55323 1.000 13.55807  ? 14  LEU A CD1  1 
ATOM   363  C CD2  . LEU A 1 17  ? 13.17450  12.81362 12.85822 1.000 13.35295  ? 14  LEU A CD2  1 
ATOM   364  H H    A LEU A 1 17  ? 16.11837  13.81697 10.80791 0.418 13.10986  ? 14  LEU A H    1 
ATOM   365  H H    B LEU A 1 17  ? 16.12384  13.82638 10.80626 0.582 13.10986  ? 14  LEU A H    1 
ATOM   366  H HA   . LEU A 1 17  ? 13.72744  14.95542 11.25369 1.000 13.23084  ? 14  LEU A HA   1 
ATOM   367  H HB2  . LEU A 1 17  ? 15.90667  14.69690 13.02521 1.000 14.42145  ? 14  LEU A HB2  1 
ATOM   368  H HB3  . LEU A 1 17  ? 14.42757  15.10041 13.44335 1.000 14.42145  ? 14  LEU A HB3  1 
ATOM   369  H HG   . LEU A 1 17  ? 15.17406  12.53558 12.53705 1.000 14.87620  ? 14  LEU A HG   1 
ATOM   370  H HD11 . LEU A 1 17  ? 14.75901  11.81400 14.71845 1.000 16.26968  ? 14  LEU A HD11 1 
ATOM   371  H HD12 . LEU A 1 17  ? 15.95857  12.85460 14.67730 1.000 16.26968  ? 14  LEU A HD12 1 
ATOM   372  H HD13 . LEU A 1 17  ? 14.51794  13.32174 15.15674 1.000 16.26968  ? 14  LEU A HD13 1 
ATOM   373  H HD21 . LEU A 1 17  ? 12.97287  11.90409 13.12842 1.000 16.02355  ? 14  LEU A HD21 1 
ATOM   374  H HD22 . LEU A 1 17  ? 12.63514  13.43762 13.36873 1.000 16.02355  ? 14  LEU A HD22 1 
ATOM   375  H HD23 . LEU A 1 17  ? 12.99958  12.92362 11.91048 1.000 16.02355  ? 14  LEU A HD23 1 
ATOM   376  N N    . VAL A 1 18  ? 14.26116  17.38984 11.57532 1.000 11.68856  ? 15  VAL A N    1 
ATOM   377  C CA   A VAL A 1 18  ? 14.57706  18.81016 11.47886 0.348 14.56112  ? 15  VAL A CA   1 
ATOM   378  C CA   B VAL A 1 18  ? 14.56231  18.81081 11.48216 0.652 14.56112  ? 15  VAL A CA   1 
ATOM   379  C C    . VAL A 1 18  ? 15.00149  19.31441 12.84935 1.000 12.47900  ? 15  VAL A C    1 
ATOM   380  O O    . VAL A 1 18  ? 14.42361  18.93940 13.87945 1.000 11.00712  ? 15  VAL A O    1 
ATOM   381  C CB   A VAL A 1 18  ? 13.40980  19.64085 10.90276 0.348 18.12997  ? 15  VAL A CB   1 
ATOM   382  C CB   B VAL A 1 18  ? 13.31175  19.57295 10.99103 0.652 18.12997  ? 15  VAL A CB   1 
ATOM   383  C CG1  A VAL A 1 18  ? 12.13774  19.40269 11.67224 0.348 18.82479  ? 15  VAL A CG1  1 
ATOM   384  C CG1  B VAL A 1 18  ? 13.57233  21.06478 10.91376 0.652 18.82479  ? 15  VAL A CG1  1 
ATOM   385  C CG2  A VAL A 1 18  ? 13.76367  21.12567 10.91310 0.348 20.31970  ? 15  VAL A CG2  1 
ATOM   386  C CG2  B VAL A 1 18  ? 12.84969  19.02019 9.64493  0.652 20.31970  ? 15  VAL A CG2  1 
ATOM   387  H HA   . VAL A 1 18  ? 15.32355  18.91485 10.86838 1.000 17.47334  ? 15  VAL A HA   1 
ATOM   388  H HB   A VAL A 1 18  ? 13.25797  19.36097 9.98651  0.348 21.75596  ? 15  VAL A HB   1 
ATOM   389  H HB   B VAL A 1 18  ? 12.59557  19.44214 11.63202 0.652 21.75596  ? 15  VAL A HB   1 
ATOM   390  H HG11 A VAL A 1 18  ? 11.47949  20.06379 11.40662 0.348 22.58974  ? 15  VAL A HG11 1 
ATOM   391  H HG11 B VAL A 1 18  ? 12.77611  21.50761 10.58085 0.652 22.58974  ? 15  VAL A HG11 1 
ATOM   392  H HG12 A VAL A 1 18  ? 11.81043  18.51152 11.47327 0.348 22.58974  ? 15  VAL A HG12 1 
ATOM   393  H HG12 B VAL A 1 18  ? 13.78774  21.39407 11.80037 0.652 22.58974  ? 15  VAL A HG12 1 
ATOM   394  H HG13 A VAL A 1 18  ? 12.32286  19.48290 12.62103 0.348 22.58974  ? 15  VAL A HG13 1 
ATOM   395  H HG13 B VAL A 1 18  ? 14.31594  21.22471 10.31180 0.652 22.58974  ? 15  VAL A HG13 1 
ATOM   396  H HG21 A VAL A 1 18  ? 13.08369  21.61579 10.42493 0.348 24.38364  ? 15  VAL A HG21 1 
ATOM   397  H HG21 B VAL A 1 18  ? 12.13283  19.57762 9.30391  0.652 24.38364  ? 15  VAL A HG21 1 
ATOM   398  H HG22 A VAL A 1 18  ? 13.79936  21.43542 11.83162 0.348 24.38364  ? 15  VAL A HG22 1 
ATOM   399  H HG22 B VAL A 1 18  ? 13.59730  19.02795 9.02693  0.652 24.38364  ? 15  VAL A HG22 1 
ATOM   400  H HG23 A VAL A 1 18  ? 14.62760  21.24738 10.48918 0.348 24.38364  ? 15  VAL A HG23 1 
ATOM   401  H HG23 B VAL A 1 18  ? 12.53222  18.11201 9.76865  0.652 24.38364  ? 15  VAL A HG23 1 
ATOM   402  N N    . SER A 1 19  ? 16.03208  20.14879 12.86029 1.000 14.80581  ? 16  SER A N    1 
ATOM   403  C CA   . SER A 1 19  ? 16.50920  20.84271 14.04291 1.000 17.90595  ? 16  SER A CA   1 
ATOM   404  C C    . SER A 1 19  ? 16.33999  22.33738 13.79975 1.000 21.29980  ? 16  SER A C    1 
ATOM   405  O O    . SER A 1 19  ? 15.88587  22.76893 12.73689 1.000 23.88151  ? 16  SER A O    1 
ATOM   406  C CB   . SER A 1 19  ? 17.97372  20.51015 14.32900 1.000 19.81777  ? 16  SER A CB   1 
ATOM   407  O OG   . SER A 1 19  ? 18.81864  21.08242 13.34885 1.000 22.58190  ? 16  SER A OG   1 
ATOM   408  H H    . SER A 1 19  ? 16.49215  20.33662 12.15839 1.000 17.76698  ? 16  SER A H    1 
ATOM   409  H HA   . SER A 1 19  ? 15.99078  20.56958 14.81592 1.000 21.48714  ? 16  SER A HA   1 
ATOM   410  H HB2  . SER A 1 19  ? 18.21411  20.86443 15.19940 1.000 23.78133  ? 16  SER A HB2  1 
ATOM   411  H HB3  . SER A 1 19  ? 18.08665  19.54679 14.32021 1.000 23.78133  ? 16  SER A HB3  1 
ATOM   412  H HG   . SER A 1 19  ? 19.62112  21.01898 13.58885 1.000 27.09828  ? 16  SER A HG   1 
ATOM   413  N N    . LYS A 1 20  ? 16.73085  23.13674 14.78692 1.000 25.02900  ? 17  LYS A N    1 
ATOM   414  C CA   . LYS A 1 20  ? 16.54646  24.57351 14.65055 1.000 29.46394  ? 17  LYS A CA   1 
ATOM   415  C C    . LYS A 1 20  ? 17.39940  25.13802 13.52745 1.000 30.48884  ? 17  LYS A C    1 
ATOM   416  O O    . LYS A 1 20  ? 16.99350  26.09851 12.86366 1.000 33.20118  ? 17  LYS A O    1 
ATOM   417  C CB   . LYS A 1 20  ? 16.89604  25.26592 15.95955 1.000 31.08738  ? 17  LYS A CB   1 
ATOM   418  C CG   . LYS A 1 20  ? 16.25243  26.62125 16.11297 1.000 31.32775  ? 17  LYS A CG   1 
ATOM   419  C CD   . LYS A 1 20  ? 16.15528  26.97872 17.57421 1.000 30.74300  ? 17  LYS A CD   1 
ATOM   420  C CE   . LYS A 1 20  ? 14.99919  26.24810 18.22991 1.000 29.61179  ? 17  LYS A CE   1 
ATOM   421  N NZ   . LYS A 1 20  ? 13.71217  26.92109 17.92029 1.000 26.08869  ? 17  LYS A NZ   1 
ATOM   422  H H    . LYS A 1 20  ? 17.09411  22.87974 15.52284 1.000 30.03480  ? 17  LYS A H    1 
ATOM   423  H HA   . LYS A 1 20  ? 15.61482  24.75177 14.44761 1.000 35.35673  ? 17  LYS A HA   1 
ATOM   424  H HB2  . LYS A 1 20  ? 16.59825  24.71020 16.69670 1.000 37.30485  ? 17  LYS A HB2  1 
ATOM   425  H HB3  . LYS A 1 20  ? 17.85752  25.38678 16.00251 1.000 37.30485  ? 17  LYS A HB3  1 
ATOM   426  H HG2  . LYS A 1 20  ? 16.78961  27.29190 15.66290 1.000 37.59330  ? 17  LYS A HG2  1 
ATOM   427  H HG3  . LYS A 1 20  ? 15.35883  26.60418 15.73602 1.000 37.59330  ? 17  LYS A HG3  1 
ATOM   428  H HD2  . LYS A 1 20  ? 16.97566  26.72499 18.02531 1.000 36.89160  ? 17  LYS A HD2  1 
ATOM   429  H HD3  . LYS A 1 20  ? 16.00804  27.93313 17.66543 1.000 36.89160  ? 17  LYS A HD3  1 
ATOM   430  H HE2  . LYS A 1 20  ? 14.95968  25.33799 17.89668 1.000 35.53414  ? 17  LYS A HE2  1 
ATOM   431  H HE3  . LYS A 1 20  ? 15.12181  26.24405 19.19212 1.000 35.53414  ? 17  LYS A HE3  1 
ATOM   432  H HZ1  . LYS A 1 20  ? 13.59713  26.96729 17.03897 1.000 31.30642  ? 17  LYS A HZ1  1 
ATOM   433  H HZ2  . LYS A 1 20  ? 13.03640  26.46420 18.27623 1.000 31.30642  ? 17  LYS A HZ2  1 
ATOM   434  H HZ3  . LYS A 1 20  ? 13.71152  27.74564 18.25527 1.000 31.30642  ? 17  LYS A HZ3  1 
ATOM   435  N N    . SER A 1 21  ? 18.57126  24.54633 13.29405 1.000 30.12214  ? 18  SER A N    1 
ATOM   436  C CA   . SER A 1 21  ? 19.53686  25.06680 12.34164 1.000 30.73165  ? 18  SER A CA   1 
ATOM   437  C C    . SER A 1 21  ? 19.68838  24.21655 11.09024 1.000 29.37304  ? 18  SER A C    1 
ATOM   438  O O    . SER A 1 21  ? 20.16640  24.72851 10.07255 1.000 30.55375  ? 18  SER A O    1 
ATOM   439  C CB   . SER A 1 21  ? 20.91233  25.17959 13.01610 1.000 32.99994  ? 18  SER A CB   1 
ATOM   440  O OG   . SER A 1 21  ? 21.31257  23.92412 13.54251 1.000 33.96336  ? 18  SER A OG   1 
ATOM   441  H H    . SER A 1 21  ? 18.83121  23.82641 13.68615 1.000 36.14657  ? 18  SER A H    1 
ATOM   442  H HA   . SER A 1 21  ? 19.25299  25.95098 12.06137 1.000 36.87797  ? 18  SER A HA   1 
ATOM   443  H HB2  . SER A 1 21  ? 21.56445  25.47059 12.35963 1.000 39.59993  ? 18  SER A HB2  1 
ATOM   444  H HB3  . SER A 1 21  ? 20.85905  25.82409 13.73907 1.000 39.59993  ? 18  SER A HB3  1 
ATOM   445  H HG   . SER A 1 21  ? 22.00066  24.01699 14.01527 1.000 40.75603  ? 18  SER A HG   1 
ATOM   446  N N    . GLY A 1 22  ? 19.30072  22.94515 11.13556 1.000 25.11550  ? 19  GLY A N    1 
ATOM   447  C CA   . GLY A 1 22  ? 19.48786  22.06919 9.99830  1.000 21.36798  ? 19  GLY A CA   1 
ATOM   448  C C    . GLY A 1 22  ? 18.69159  20.78583 10.07822 1.000 19.45496  ? 19  GLY A C    1 
ATOM   449  O O    . GLY A 1 22  ? 17.50677  20.79712 10.42858 1.000 20.95805  ? 19  GLY A O    1 
ATOM   450  H H    . GLY A 1 22  ? 18.92803  22.57171 11.81470 1.000 30.13860  ? 19  GLY A H    1 
ATOM   451  H HA2  . GLY A 1 22  ? 19.22086  22.53785 9.19209  1.000 25.64158  ? 19  GLY A HA2  1 
ATOM   452  H HA3  . GLY A 1 22  ? 20.42694  21.83559 9.93146  1.000 25.64158  ? 19  GLY A HA3  1 
ATOM   453  N N    . THR A 1 23  ? 19.34263  19.67131 9.74884  1.000 17.40910  ? 20  THR A N    1 
ATOM   454  C CA   . THR A 1 23  ? 18.70733  18.36326 9.73709  1.000 16.10232  ? 20  THR A CA   1 
ATOM   455  C C    . THR A 1 23  ? 19.63258  17.35476 10.40273 1.000 17.21845  ? 20  THR A C    1 
ATOM   456  O O    . THR A 1 23  ? 20.85045  17.54210 10.47102 1.000 20.16927  ? 20  THR A O    1 
ATOM   457  C CB   . THR A 1 23  ? 18.36138  17.91062 8.31112  1.000 17.94104  ? 20  THR A CB   1 
ATOM   458  O OG1  . THR A 1 23  ? 19.54682  17.89498 7.50594  1.000 19.36144  ? 20  THR A OG1  1 
ATOM   459  C CG2  . THR A 1 23  ? 17.33102  18.84570 7.69102  1.000 17.92771  ? 20  THR A CG2  1 
ATOM   460  H H    . THR A 1 23  ? 20.17237  19.65028 9.52368  1.000 20.89092  ? 20  THR A H    1 
ATOM   461  H HA   . THR A 1 23  ? 17.88311  18.40127 10.24711 1.000 19.32279  ? 20  THR A HA   1 
ATOM   462  H HB   . THR A 1 23  ? 17.98439  17.01725 8.33695  1.000 21.52925  ? 20  THR A HB   1 
ATOM   463  H HG1  . THR A 1 23  ? 19.36595  17.61844 6.73367  1.000 23.23373  ? 20  THR A HG1  1 
ATOM   464  H HG21 . THR A 1 23  ? 17.02757  18.48859 6.84173  1.000 21.51326  ? 20  THR A HG21 1 
ATOM   465  H HG22 . THR A 1 23  ? 16.56878  18.93922 8.28359  1.000 21.51326  ? 20  THR A HG22 1 
ATOM   466  H HG23 . THR A 1 23  ? 17.72353  19.72024 7.54259  1.000 21.51326  ? 20  THR A HG23 1 
ATOM   467  N N    . VAL A 1 24  ? 19.02570  16.26744 10.87342 1.000 15.80856  ? 21  VAL A N    1 
ATOM   468  C CA   . VAL A 1 24  ? 19.65899  15.29102 11.75104 1.000 19.21127  ? 21  VAL A CA   1 
ATOM   469  C C    . VAL A 1 24  ? 19.19398  13.90990 11.31637 1.000 17.14206  ? 21  VAL A C    1 
ATOM   470  O O    . VAL A 1 24  ? 17.98878  13.67530 11.19715 1.000 18.11478  ? 21  VAL A O    1 
ATOM   471  C CB   . VAL A 1 24  ? 19.20259  15.53459 13.20626 1.000 20.24040  ? 21  VAL A CB   1 
ATOM   472  C CG1  . VAL A 1 24  ? 19.65185  14.41106 14.11738 1.000 22.30255  ? 21  VAL A CG1  1 
ATOM   473  C CG2  . VAL A 1 24  ? 19.69458  16.88159 13.71797 1.000 22.20969  ? 21  VAL A CG2  1 
ATOM   474  H H    . VAL A 1 24  ? 18.21017  16.06613 10.68907 1.000 18.97028  ? 21  VAL A H    1 
ATOM   475  H HA   . VAL A 1 24  ? 20.62517  15.34053 11.68084 1.000 23.05353  ? 21  VAL A HA   1 
ATOM   476  H HB   . VAL A 1 24  ? 18.23281  15.55138 13.21797 1.000 24.28848  ? 21  VAL A HB   1 
ATOM   477  H HG11 . VAL A 1 24  ? 19.52350  14.68207 15.03986 1.000 26.76306  ? 21  VAL A HG11 1 
ATOM   478  H HG12 . VAL A 1 24  ? 19.12276  13.62037 13.92823 1.000 26.76306  ? 21  VAL A HG12 1 
ATOM   479  H HG13 . VAL A 1 24  ? 20.59029  14.22800 13.95391 1.000 26.76306  ? 21  VAL A HG13 1 
ATOM   480  H HG21 . VAL A 1 24  ? 19.44488  16.97549 14.65056 1.000 26.65163  ? 21  VAL A HG21 1 
ATOM   481  H HG22 . VAL A 1 24  ? 20.65967  16.92007 13.62845 1.000 26.65163  ? 21  VAL A HG22 1 
ATOM   482  H HG23 . VAL A 1 24  ? 19.28532  17.58737 13.19329 1.000 26.65163  ? 21  VAL A HG23 1 
ATOM   483  N N    . SER A 1 25  ? 20.12419  12.99129 11.07911 1.000 16.69244  ? 22  SER A N    1 
ATOM   484  C CA   A SER A 1 25  ? 19.73787  11.61936 10.78436 0.156 18.35361  ? 22  SER A CA   1 
ATOM   485  C CA   B SER A 1 25  ? 19.72564  11.62493 10.78199 0.273 16.21361  ? 22  SER A CA   1 
ATOM   486  C CA   C SER A 1 25  ? 19.72366  11.62523 10.78162 0.571 15.11361  ? 22  SER A CA   1 
ATOM   487  C C    . SER A 1 25  ? 19.25503  10.93872 12.06286 1.000 16.04393  ? 22  SER A C    1 
ATOM   488  O O    . SER A 1 25  ? 19.83375  11.15927 13.13333 1.000 16.31812  ? 22  SER A O    1 
ATOM   489  C CB   A SER A 1 25  ? 20.93172  10.84710 10.22589 0.156 22.41361  ? 22  SER A CB   1 
ATOM   490  C CB   B SER A 1 25  ? 20.88380  10.83118 10.18407 0.273 16.73361  ? 22  SER A CB   1 
ATOM   491  C CB   C SER A 1 25  ? 20.88233  10.84019 10.17166 0.571 17.20361  ? 22  SER A CB   1 
ATOM   492  O OG   A SER A 1 25  ? 21.99840  10.81351 11.15959 0.156 24.45361  ? 22  SER A OG   1 
ATOM   493  O OG   B SER A 1 25  ? 20.48526  9.49428  9.92249  0.273 16.80361  ? 22  SER A OG   1 
ATOM   494  O OG   C SER A 1 25  ? 21.20004  11.32712 8.87956  0.571 18.84361  ? 22  SER A OG   1 
ATOM   495  H H    A SER A 1 25  ? 20.97214  13.13469 11.08281 0.156 20.03092  ? 22  SER A H    1 
ATOM   496  H H    B SER A 1 25  ? 20.97271  13.13127 11.08427 0.273 20.03092  ? 22  SER A H    1 
ATOM   497  H H    C SER A 1 25  ? 20.97279  13.13077 11.08443 0.571 20.03092  ? 22  SER A H    1 
ATOM   498  H HA   A SER A 1 25  ? 19.02340  11.61119 10.12833 0.156 22.02433  ? 22  SER A HA   1 
ATOM   499  H HA   B SER A 1 25  ? 19.00242  11.63737 10.13570 0.273 19.45633  ? 22  SER A HA   1 
ATOM   500  H HA   C SER A 1 25  ? 18.99573  11.63249 10.14056 0.571 18.13633  ? 22  SER A HA   1 
ATOM   501  H HB2  A SER A 1 25  ? 20.65533  9.93804  10.03065 0.156 26.89633  ? 22  SER A HB2  1 
ATOM   502  H HB2  B SER A 1 25  ? 21.15913  11.24872 9.35295  0.273 20.08033  ? 22  SER A HB2  1 
ATOM   503  H HB2  C SER A 1 25  ? 21.66066  10.93172 10.74325 0.571 20.64433  ? 22  SER A HB2  1 
ATOM   504  H HB3  A SER A 1 25  ? 21.23689  11.28255 9.41463  0.156 26.89633  ? 22  SER A HB3  1 
ATOM   505  H HB3  B SER A 1 25  ? 21.62239  10.82497 10.81283 0.273 20.08033  ? 22  SER A HB3  1 
ATOM   506  H HB3  C SER A 1 25  ? 20.62898  9.90637  10.10317 0.571 20.64433  ? 22  SER A HB3  1 
ATOM   507  H HG   A SER A 1 25  ? 22.64058  10.37181 10.84637 0.156 29.34433  ? 22  SER A HG   1 
ATOM   508  H HG   B SER A 1 25  ? 20.29474  9.10525  10.64218 0.273 20.16433  ? 22  SER A HG   1 
ATOM   509  H HG   C SER A 1 25  ? 21.80717  10.85835 8.53714  0.571 22.61233  ? 22  SER A HG   1 
ATOM   510  N N    . PRO A 1 26  ? 18.20582  10.11366 11.99758 1.000 14.35133  ? 23  PRO A N    1 
ATOM   511  C CA   . PRO A 1 26  ? 17.76986  9.41585  13.21752 1.000 13.89078  ? 23  PRO A CA   1 
ATOM   512  C C    . PRO A 1 26  ? 18.86987  8.63645  13.91445 1.000 14.28774  ? 23  PRO A C    1 
ATOM   513  O O    . PRO A 1 26  ? 18.84791  8.52426  15.14638 1.000 14.72350  ? 23  PRO A O    1 
ATOM   514  C CB   . PRO A 1 26  ? 16.64999  8.49451  12.71458 1.000 16.24993  ? 23  PRO A CB   1 
ATOM   515  C CG   . PRO A 1 26  ? 16.06530  9.23228  11.58037 1.000 16.09934  ? 23  PRO A CG   1 
ATOM   516  C CD   . PRO A 1 26  ? 17.20097  9.98322  10.92032 1.000 15.65220  ? 23  PRO A CD   1 
ATOM   517  H HA   . PRO A 1 26  ? 17.39913  10.05960 13.84126 1.000 16.66894  ? 23  PRO A HA   1 
ATOM   518  H HB2  . PRO A 1 26  ? 17.01962  7.64491  12.42745 1.000 19.49992  ? 23  PRO A HB2  1 
ATOM   519  H HB3  . PRO A 1 26  ? 15.99473  8.35138  13.41533 1.000 19.49992  ? 23  PRO A HB3  1 
ATOM   520  H HG2  . PRO A 1 26  ? 15.66445  8.60529  10.95820 1.000 19.31920  ? 23  PRO A HG2  1 
ATOM   521  H HG3  . PRO A 1 26  ? 15.39318  9.85027  11.90786 1.000 19.31920  ? 23  PRO A HG3  1 
ATOM   522  H HD2  . PRO A 1 26  ? 17.56005  9.47749  10.17453 1.000 18.78264  ? 23  PRO A HD2  1 
ATOM   523  H HD3  . PRO A 1 26  ? 16.90593  10.85631 10.61772 1.000 18.78264  ? 23  PRO A HD3  1 
ATOM   524  N N    . ILE A 1 27  ? 19.83807  8.09547  13.17198 1.000 14.82292  ? 24  ILE A N    1 
ATOM   525  C CA   . ILE A 1 27  ? 20.89511  7.31025  13.79932 1.000 13.47655  ? 24  ILE A CA   1 
ATOM   526  C C    . ILE A 1 27  ? 21.72471  8.14799  14.76110 1.000 12.67946  ? 24  ILE A C    1 
ATOM   527  O O    . ILE A 1 27  ? 22.38262  7.59558  15.64918 1.000 13.71849  ? 24  ILE A O    1 
ATOM   528  C CB   . ILE A 1 27  ? 21.76403  6.62635  12.72449 1.000 16.26487  ? 24  ILE A CB   1 
ATOM   529  C CG1  . ILE A 1 27  ? 22.70359  5.60073  13.36256 1.000 18.43817  ? 24  ILE A CG1  1 
ATOM   530  C CG2  . ILE A 1 27  ? 22.57495  7.65812  11.95157 1.000 16.96728  ? 24  ILE A CG2  1 
ATOM   531  C CD1  . ILE A 1 27  ? 23.39359  4.69729  12.35629 1.000 21.02161  ? 24  ILE A CD1  1 
ATOM   532  H H    . ILE A 1 27  ? 19.90252  8.16842  12.31751 1.000 17.78750  ? 24  ILE A H    1 
ATOM   533  H HA   . ILE A 1 27  ? 20.48517  6.60557  14.32493 1.000 16.17187  ? 24  ILE A HA   1 
ATOM   534  H HB   . ILE A 1 27  ? 21.16926  6.16833  12.11019 1.000 19.51785  ? 24  ILE A HB   1 
ATOM   535  H HG12 . ILE A 1 27  ? 23.39136  6.07287  13.85749 1.000 22.12580  ? 24  ILE A HG12 1 
ATOM   536  H HG13 . ILE A 1 27  ? 22.19003  5.03793  13.96291 1.000 22.12580  ? 24  ILE A HG13 1 
ATOM   537  H HG21 . ILE A 1 27  ? 22.91477  7.24936  11.14018 1.000 20.36074  ? 24  ILE A HG21 1 
ATOM   538  H HG22 . ILE A 1 27  ? 22.00159  8.40820  11.72901 1.000 20.36074  ? 24  ILE A HG22 1 
ATOM   539  H HG23 . ILE A 1 27  ? 23.31295  7.95861  12.50471 1.000 20.36074  ? 24  ILE A HG23 1 
ATOM   540  H HD11 . ILE A 1 27  ? 23.98179  4.08844  12.82980 1.000 25.22593  ? 24  ILE A HD11 1 
ATOM   541  H HD12 . ILE A 1 27  ? 22.72127  4.19582  11.86905 1.000 25.22593  ? 24  ILE A HD12 1 
ATOM   542  H HD13 . ILE A 1 27  ? 23.90830  5.24384  11.74207 1.000 25.22593  ? 24  ILE A HD13 1 
ATOM   543  N N    . SER A 1 28  ? 21.70470  9.47575  14.61501 1.000 13.30615  ? 25  SER A N    1 
ATOM   544  C CA   A SER A 1 28  ? 22.44731  10.34316 15.51999 0.418 13.73361  ? 25  SER A CA   1 
ATOM   545  C CA   B SER A 1 28  ? 22.44709  10.34318 15.51936 0.582 12.48361  ? 25  SER A CA   1 
ATOM   546  C C    . SER A 1 28  ? 21.89570  10.32276 16.93709 1.000 12.11126  ? 25  SER A C    1 
ATOM   547  O O    . SER A 1 28  ? 22.53595  10.87196 17.83936 1.000 13.30199  ? 25  SER A O    1 
ATOM   548  C CB   A SER A 1 28  ? 22.43346  11.77736 14.99234 0.418 17.46361  ? 25  SER A CB   1 
ATOM   549  C CB   B SER A 1 28  ? 22.42044  11.78573 15.01613 0.582 13.77361  ? 25  SER A CB   1 
ATOM   550  O OG   A SER A 1 28  ? 23.16516  11.87669 13.78411 0.418 20.92361  ? 25  SER A OG   1 
ATOM   551  O OG   B SER A 1 28  ? 21.15845  12.38295 15.25447 0.582 15.19361  ? 25  SER A OG   1 
ATOM   552  H H    A SER A 1 28  ? 21.26975  9.89308  14.00161 0.418 15.96738  ? 25  SER A H    1 
ATOM   553  H H    B SER A 1 28  ? 21.26963  9.89301  14.00165 0.582 15.96738  ? 25  SER A H    1 
ATOM   554  H HA   A SER A 1 28  ? 23.36809  10.03983 15.55237 0.418 16.48033  ? 25  SER A HA   1 
ATOM   555  H HA   B SER A 1 28  ? 23.36746  10.03730 15.53523 0.582 14.98033  ? 25  SER A HA   1 
ATOM   556  H HB2  A SER A 1 28  ? 21.51553  12.04470 14.82850 0.418 20.95633  ? 25  SER A HB2  1 
ATOM   557  H HB2  B SER A 1 28  ? 23.10280  12.29449 15.48137 0.582 16.52833  ? 25  SER A HB2  1 
ATOM   558  H HB3  A SER A 1 28  ? 22.83595  12.36122 15.65416 0.418 20.95633  ? 25  SER A HB3  1 
ATOM   559  H HB3  B SER A 1 28  ? 22.59604  11.79004 14.06216 0.582 16.52833  ? 25  SER A HB3  1 
ATOM   560  H HG   A SER A 1 28  ? 22.85221  11.34487 13.21417 0.418 25.10833  ? 25  SER A HG   1 
ATOM   561  H HG   B SER A 1 28  ? 20.58117  12.04800 14.74441 0.582 18.23233  ? 25  SER A HG   1 
ATOM   562  N N    . LEU A 1 29  ? 20.72902  9.72443  17.14787 1.000 11.75358  ? 26  LEU A N    1 
ATOM   563  C CA   . LEU A 1 29  ? 20.12964  9.59377  18.46772 1.000 10.88703  ? 26  LEU A CA   1 
ATOM   564  C C    . LEU A 1 29  ? 20.57814  8.31540  19.17291 1.000 10.90036  ? 26  LEU A C    1 
ATOM   565  O O    . LEU A 1 29  ? 20.07557  8.00784  20.25797 1.000 10.99009  ? 26  LEU A O    1 
ATOM   566  C CB   . LEU A 1 29  ? 18.60240  9.67677  18.34356 1.000 12.28266  ? 26  LEU A CB   1 
ATOM   567  C CG   . LEU A 1 29  ? 17.99415  11.06773 18.09409 1.000 14.14516  ? 26  LEU A CG   1 
ATOM   568  C CD1  . LEU A 1 29  ? 18.53928  11.75763 16.85161 1.000 17.97642  ? 26  LEU A CD1  1 
ATOM   569  C CD2  . LEU A 1 29  ? 16.46966  10.99224 17.99752 1.000 15.70711  ? 26  LEU A CD2  1 
ATOM   570  H H    . LEU A 1 29  ? 20.25218  9.37612  16.52265 1.000 14.10430  ? 26  LEU A H    1 
ATOM   571  H HA   . LEU A 1 29  ? 20.40047  10.33222 19.03538 1.000 13.06444  ? 26  LEU A HA   1 
ATOM   572  H HB2  . LEU A 1 29  ? 18.33261  9.11330  17.60153 1.000 14.73919  ? 26  LEU A HB2  1 
ATOM   573  H HB3  . LEU A 1 29  ? 18.21769  9.34428  19.16960 1.000 14.73919  ? 26  LEU A HB3  1 
ATOM   574  H HG   . LEU A 1 29  ? 18.24908  11.61050 18.85653 1.000 16.97419  ? 26  LEU A HG   1 
ATOM   575  H HD11 . LEU A 1 29  ? 18.03164  12.56871 16.69236 1.000 21.57170  ? 26  LEU A HD11 1 
ATOM   576  H HD12 . LEU A 1 29  ? 19.47360  11.97504 16.99537 1.000 21.57170  ? 26  LEU A HD12 1 
ATOM   577  H HD13 . LEU A 1 29  ? 18.45188  11.15854 16.09374 1.000 21.57170  ? 26  LEU A HD13 1 
ATOM   578  H HD21 . LEU A 1 29  ? 16.12622  11.86151 17.73808 1.000 18.84853  ? 26  LEU A HD21 1 
ATOM   579  H HD22 . LEU A 1 29  ? 16.22782  10.32903 17.33227 1.000 18.84853  ? 26  LEU A HD22 1 
ATOM   580  H HD23 . LEU A 1 29  ? 16.11057  10.73940 18.86242 1.000 18.84853  ? 26  LEU A HD23 1 
ATOM   581  N N    . ALA A 1 30  ? 21.53688  7.59076  18.59312 1.000 11.30031  ? 27  ALA A N    1 
ATOM   582  C CA   . ALA A 1 30  ? 22.02299  6.34824  19.17783 1.000 10.64747  ? 27  ALA A CA   1 
ATOM   583  C C    . ALA A 1 30  ? 22.39205  6.53308  20.64354 1.000 12.09016  ? 27  ALA A C    1 
ATOM   584  O O    . ALA A 1 30  ? 22.96858  7.54963  21.03525 1.000 13.35621  ? 27  ALA A O    1 
ATOM   585  C CB   . ALA A 1 30  ? 23.25135  5.86889  18.39623 1.000 12.58712  ? 27  ALA A CB   1 
ATOM   586  H H    . ALA A 1 30  ? 21.92368  7.80115  17.85439 1.000 13.56038  ? 27  ALA A H    1 
ATOM   587  H HA   . ALA A 1 30  ? 21.32472  5.67680  19.12797 1.000 12.77697  ? 27  ALA A HA   1 
ATOM   588  H HB1  . ALA A 1 30  ? 23.61125  5.07808  18.82750 1.000 15.10455  ? 27  ALA A HB1  1 
ATOM   589  H HB2  . ALA A 1 30  ? 22.98499  5.65792  17.48769 1.000 15.10455  ? 27  ALA A HB2  1 
ATOM   590  H HB3  . ALA A 1 30  ? 23.91703  6.57439  18.39040 1.000 15.10455  ? 27  ALA A HB3  1 
ATOM   591  N N    . GLY A 1 31  ? 22.04803  5.53384  21.45482 1.000 13.27194  ? 28  GLY A N    1 
ATOM   592  C CA   . GLY A 1 31  ? 22.41363  5.50932  22.85354 1.000 13.88980  ? 28  GLY A CA   1 
ATOM   593  C C    . GLY A 1 31  ? 21.53818  6.32611  23.77538 1.000 13.07074  ? 28  GLY A C    1 
ATOM   594  O O    . GLY A 1 31  ? 21.73630  6.27245  24.99677 1.000 16.20756  ? 28  GLY A O    1 
ATOM   595  H H    . GLY A 1 31  ? 21.59318  4.84763  21.20614 1.000 15.92633  ? 28  GLY A H    1 
ATOM   596  H HA2  . GLY A 1 31  ? 22.38511  4.59019  23.16222 1.000 16.66776  ? 28  GLY A HA2  1 
ATOM   597  H HA3  . GLY A 1 31  ? 23.32017  5.84344  22.93978 1.000 16.66776  ? 28  GLY A HA3  1 
ATOM   598  N N    . LYS A 1 32  ? 20.56449  7.05393  23.24730 1.000 12.07627  ? 29  LYS A N    1 
ATOM   599  C CA   A LYS A 1 32  ? 19.75350  7.95490  24.04614 0.812 11.38361  ? 29  LYS A CA   1 
ATOM   600  C CA   B LYS A 1 32  ? 19.75469  7.95868  24.04318 0.188 12.86361  ? 29  LYS A CA   1 
ATOM   601  C C    . LYS A 1 32  ? 18.37488  7.36877  24.30894 1.000 11.12943  ? 29  LYS A C    1 
ATOM   602  O O    . LYS A 1 32  ? 17.90386  6.47768  23.59909 1.000 12.55701  ? 29  LYS A O    1 
ATOM   603  C CB   A LYS A 1 32  ? 19.58270  9.29050  23.31737 0.812 10.03361  ? 29  LYS A CB   1 
ATOM   604  C CB   B LYS A 1 32  ? 19.57280  9.29463  23.31427 0.188 14.06361  ? 29  LYS A CB   1 
ATOM   605  C CG   A LYS A 1 32  ? 20.88430  10.01099 23.07691 0.812 10.56361  ? 29  LYS A CG   1 
ATOM   606  C CG   B LYS A 1 32  ? 20.85506  10.04919 23.02068 0.188 15.51361  ? 29  LYS A CG   1 
ATOM   607  C CD   A LYS A 1 32  ? 20.67698  11.44370 22.62939 0.812 11.93361  ? 29  LYS A CD   1 
ATOM   608  C CD   B LYS A 1 32  ? 20.54823  11.43544 22.46512 0.188 16.98361  ? 29  LYS A CD   1 
ATOM   609  C CE   A LYS A 1 32  ? 22.00327  12.18304 22.64867 0.812 13.66361  ? 29  LYS A CE   1 
ATOM   610  C CE   B LYS A 1 32  ? 21.81717  12.21711 22.16579 0.188 18.33361  ? 29  LYS A CE   1 
ATOM   611  N NZ   A LYS A 1 32  ? 21.88908  13.56551 22.12884 0.812 13.45361  ? 29  LYS A NZ   1 
ATOM   612  N NZ   B LYS A 1 32  ? 22.67839  12.36813 23.37029 0.188 19.22361  ? 29  LYS A NZ   1 
ATOM   613  H H    A LYS A 1 32  ? 20.35232  7.04161  22.41397 0.812 14.49152  ? 29  LYS A H    1 
ATOM   614  H H    B LYS A 1 32  ? 20.35124  7.03942  22.41428 0.188 14.49152  ? 29  LYS A H    1 
ATOM   615  H HA   A LYS A 1 32  ? 20.19450  8.09757  24.89823 0.812 13.66033  ? 29  LYS A HA   1 
ATOM   616  H HA   B LYS A 1 32  ? 20.20238  8.10626  24.89093 0.188 15.43633  ? 29  LYS A HA   1 
ATOM   617  H HB2  A LYS A 1 32  ? 19.16949  9.12638  22.45526 0.812 12.04033  ? 29  LYS A HB2  1 
ATOM   618  H HB2  B LYS A 1 32  ? 19.13617  9.12330  22.46521 0.188 16.87633  ? 29  LYS A HB2  1 
ATOM   619  H HB3  A LYS A 1 32  ? 19.01649  9.86891  23.85192 0.812 12.04033  ? 29  LYS A HB3  1 
ATOM   620  H HB3  B LYS A 1 32  ? 19.01698  9.86975  23.86307 0.188 16.87633  ? 29  LYS A HB3  1 
ATOM   621  H HG2  A LYS A 1 32  ? 21.39725  10.02395 23.90008 0.812 12.67633  ? 29  LYS A HG2  1 
ATOM   622  H HG2  B LYS A 1 32  ? 21.36624  10.15100 23.83874 0.188 18.61633  ? 29  LYS A HG2  1 
ATOM   623  H HG3  A LYS A 1 32  ? 21.38064  9.54797  22.38397 0.812 12.67633  ? 29  LYS A HG3  1 
ATOM   624  H HG3  B LYS A 1 32  ? 21.37520  9.56156  22.36297 0.188 18.61633  ? 29  LYS A HG3  1 
ATOM   625  H HD2  A LYS A 1 32  ? 20.32475  11.45749 21.72571 0.812 14.32033  ? 29  LYS A HD2  1 
ATOM   626  H HD2  B LYS A 1 32  ? 20.04525  11.34580 21.64057 0.188 20.38033  ? 29  LYS A HD2  1 
ATOM   627  H HD3  A LYS A 1 32  ? 20.06177  11.88997 23.23210 0.812 14.32033  ? 29  LYS A HD3  1 
ATOM   628  H HD3  B LYS A 1 32  ? 20.03098  11.93422 23.11671 0.188 20.38033  ? 29  LYS A HD3  1 
ATOM   629  H HE2  A LYS A 1 32  ? 22.32670  12.23079 23.56191 0.812 16.39633  ? 29  LYS A HE2  1 
ATOM   630  H HE2  B LYS A 1 32  ? 22.32701  11.74935 21.48597 0.188 22.00033  ? 29  LYS A HE2  1 
ATOM   631  H HE3  A LYS A 1 32  ? 22.64094  11.70533 22.09543 0.812 16.39633  ? 29  LYS A HE3  1 
ATOM   632  H HE3  B LYS A 1 32  ? 21.57913  13.10318 21.85097 0.188 22.00033  ? 29  LYS A HE3  1 
ATOM   633  H HZ1  A LYS A 1 32  ? 21.59423  13.55162 21.28921 0.812 16.14433  ? 29  LYS A HZ1  1 
ATOM   634  H HZ1  B LYS A 1 32  ? 22.20530  12.71084 24.04173 0.188 23.06833  ? 29  LYS A HZ1  1 
ATOM   635  H HZ2  A LYS A 1 32  ? 21.31849  14.03212 22.62765 0.812 16.14433  ? 29  LYS A HZ2  1 
ATOM   636  H HZ2  B LYS A 1 32  ? 22.99794  11.57507 23.61738 0.188 23.06833  ? 29  LYS A HZ2  1 
ATOM   637  H HZ3  A LYS A 1 32  ? 22.68411  13.96502 22.14921 0.812 16.14433  ? 29  LYS A HZ3  1 
ATOM   638  H HZ3  B LYS A 1 32  ? 23.36032  12.91112 23.19077 0.188 23.06833  ? 29  LYS A HZ3  1 
ATOM   639  N N    . THR A 1 33  ? 17.73028  7.88662  25.34995 1.000 10.10849  ? 30  THR A N    1 
ATOM   640  C CA   . THR A 1 33  ? 16.29304  7.71945  25.49122 1.000 9.75234   ? 30  THR A CA   1 
ATOM   641  C C    . THR A 1 33  ? 15.65478  8.76284  24.58246 1.000 9.56283   ? 30  THR A C    1 
ATOM   642  O O    . THR A 1 33  ? 16.04538  9.93463  24.60800 1.000 9.97730   ? 30  THR A O    1 
ATOM   643  C CB   . THR A 1 33  ? 15.84955  7.94851  26.92976 1.000 10.02107  ? 30  THR A CB   1 
ATOM   644  O OG1  . THR A 1 33  ? 16.55559  7.05119  27.79199 1.000 11.60862  ? 30  THR A OG1  1 
ATOM   645  C CG2  . THR A 1 33  ? 14.35284  7.69916  27.07005 1.000 12.73592  ? 30  THR A CG2  1 
ATOM   646  H H    . THR A 1 33  ? 18.10207  8.33548  25.98233 1.000 12.13019  ? 30  THR A H    1 
ATOM   647  H HA   . THR A 1 33  ? 16.01821  6.82019  25.25309 1.000 11.70281  ? 30  THR A HA   1 
ATOM   648  H HB   . THR A 1 33  ? 16.03603  8.86517  27.18641 1.000 12.02529  ? 30  THR A HB   1 
ATOM   649  H HG1  . THR A 1 33  ? 17.31005  7.36842  27.98107 1.000 13.93034  ? 30  THR A HG1  1 
ATOM   650  H HG21 . THR A 1 33  ? 14.11628  7.61899  28.00734 1.000 15.28310  ? 30  THR A HG21 1 
ATOM   651  H HG22 . THR A 1 33  ? 13.85589  8.43624  26.68189 1.000 15.28310  ? 30  THR A HG22 1 
ATOM   652  H HG23 . THR A 1 33  ? 14.10876  6.87940  26.61255 1.000 15.28310  ? 30  THR A HG23 1 
ATOM   653  N N    . VAL A 1 34  ? 14.69215  8.34725  23.77019 1.000 9.26654   ? 31  VAL A N    1 
ATOM   654  C CA   . VAL A 1 34  ? 14.06314  9.23279  22.79893 1.000 9.13276   ? 31  VAL A CA   1 
ATOM   655  C C    . VAL A 1 34  ? 12.59090  9.36217  23.14955 1.000 8.67812   ? 31  VAL A C    1 
ATOM   656  O O    . VAL A 1 34  ? 11.86491  8.36057  23.17716 1.000 9.01806   ? 31  VAL A O    1 
ATOM   657  C CB   . VAL A 1 34  ? 14.25160  8.72583  21.35964 1.000 10.88780  ? 31  VAL A CB   1 
ATOM   658  C CG1  . VAL A 1 34  ? 13.46816  9.59363  20.38997 1.000 11.47837  ? 31  VAL A CG1  1 
ATOM   659  C CG2  . VAL A 1 34  ? 15.73494  8.69303  21.00678 1.000 11.50666  ? 31  VAL A CG2  1 
ATOM   660  H H    . VAL A 1 34  ? 14.38198  7.54516  23.76284 1.000 11.11985  ? 31  VAL A H    1 
ATOM   661  H HA   . VAL A 1 34  ? 14.46167  10.11452 22.86703 1.000 10.95931  ? 31  VAL A HA   1 
ATOM   662  H HB   . VAL A 1 34  ? 13.90954  7.82122  21.28504 1.000 13.06536  ? 31  VAL A HB   1 
ATOM   663  H HG11 . VAL A 1 34  ? 13.75986  9.39914  19.48555 1.000 13.77404  ? 31  VAL A HG11 1 
ATOM   664  H HG12 . VAL A 1 34  ? 12.52296  9.39625  20.48232 1.000 13.77404  ? 31  VAL A HG12 1 
ATOM   665  H HG13 . VAL A 1 34  ? 13.63300  10.52678 20.59723 1.000 13.77404  ? 31  VAL A HG13 1 
ATOM   666  H HG21 . VAL A 1 34  ? 15.83410  8.40649  20.08539 1.000 13.80800  ? 31  VAL A HG21 1 
ATOM   667  H HG22 . VAL A 1 34  ? 16.10583  9.58235  21.11835 1.000 13.80800  ? 31  VAL A HG22 1 
ATOM   668  H HG23 . VAL A 1 34  ? 16.18634  8.06988  21.59738 1.000 13.80800  ? 31  VAL A HG23 1 
ATOM   669  N N    . PHE A 1 35  ? 12.15320  10.59282 23.41809 1.000 9.20408   ? 32  PHE A N    1 
ATOM   670  C CA   A PHE A 1 35  ? 10.75511  10.87843 23.70808 0.881 9.19732   ? 32  PHE A CA   1 
ATOM   671  C CA   B PHE A 1 35  ? 10.75582  10.88465 23.70956 0.119 9.19732   ? 32  PHE A CA   1 
ATOM   672  C C    . PHE A 1 35  ? 10.07265  11.32737 22.42343 1.000 8.10965   ? 32  PHE A C    1 
ATOM   673  O O    . PHE A 1 35  ? 10.36708  12.40700 21.90014 1.000 9.89192   ? 32  PHE A O    1 
ATOM   674  C CB   A PHE A 1 35  ? 10.63547  11.96372 24.77701 0.881 10.93437  ? 32  PHE A CB   1 
ATOM   675  C CB   B PHE A 1 35  ? 10.64192  12.03560 24.71071 0.119 10.93437  ? 32  PHE A CB   1 
ATOM   676  C CG   A PHE A 1 35  ? 10.97814  11.48777 26.15685 0.881 12.97672  ? 32  PHE A CG   1 
ATOM   677  C CG   B PHE A 1 35  ? 11.05998  11.70176 26.11171 0.119 12.97672  ? 32  PHE A CG   1 
ATOM   678  C CD1  A PHE A 1 35  ? 12.29654  11.38488 26.55779 0.881 14.96117  ? 32  PHE A CD1  1 
ATOM   679  C CD1  B PHE A 1 35  ? 11.62188  10.47938 26.43025 0.119 14.96117  ? 32  PHE A CD1  1 
ATOM   680  C CD2  A PHE A 1 35  ? 9.98258   11.13035 27.05167 0.881 13.53205  ? 32  PHE A CD2  1 
ATOM   681  C CD2  B PHE A 1 35  ? 10.87551  12.63240 27.12168 0.119 13.53205  ? 32  PHE A CD2  1 
ATOM   682  C CE1  A PHE A 1 35  ? 12.61718  10.94071 27.82607 0.881 15.43491  ? 32  PHE A CE1  1 
ATOM   683  C CE1  B PHE A 1 35  ? 11.99672  10.19651 27.73213 0.119 15.43491  ? 32  PHE A CE1  1 
ATOM   684  C CE2  A PHE A 1 35  ? 10.29937  10.68427 28.32124 0.881 13.89262  ? 32  PHE A CE2  1 
ATOM   685  C CE2  B PHE A 1 35  ? 11.24392  12.35463 28.41862 0.119 13.89262  ? 32  PHE A CE2  1 
ATOM   686  C CZ   A PHE A 1 35  ? 11.61823  10.58854 28.70643 0.881 14.90326  ? 32  PHE A CZ   1 
ATOM   687  C CZ   B PHE A 1 35  ? 11.80455  11.13591 28.72561 0.119 14.90326  ? 32  PHE A CZ   1 
ATOM   688  H H    . PHE A 1 35  ? 12.65958  11.28766 23.43739 1.000 11.04489  ? 32  PHE A H    1 
ATOM   689  H HA   . PHE A 1 35  ? 10.32599  10.06927 24.02750 1.000 11.03678  ? 32  PHE A HA   1 
ATOM   690  H HB2  A PHE A 1 35  ? 11.23983  12.68915 24.55477 0.881 13.12124  ? 32  PHE A HB2  1 
ATOM   691  H HB2  B PHE A 1 35  ? 11.20434  12.76461 24.40555 0.119 13.12124  ? 32  PHE A HB2  1 
ATOM   692  H HB3  A PHE A 1 35  ? 9.72103   12.28689 24.79319 0.881 13.12124  ? 32  PHE A HB3  1 
ATOM   693  H HB3  B PHE A 1 35  ? 9.71596   12.32261 24.74436 0.119 13.12124  ? 32  PHE A HB3  1 
ATOM   694  H HD1  A PHE A 1 35  ? 12.97601  11.61739 25.96690 0.881 17.95340  ? 32  PHE A HD1  1 
ATOM   695  H HD1  B PHE A 1 35  ? 11.74893  9.84238  25.76467 0.119 17.95340  ? 32  PHE A HD1  1 
ATOM   696  H HD2  A PHE A 1 35  ? 9.09071   11.19125 26.79523 0.881 16.23846  ? 32  PHE A HD2  1 
ATOM   697  H HD2  B PHE A 1 35  ? 10.49688  13.45758 26.92015 0.119 16.23846  ? 32  PHE A HD2  1 
ATOM   698  H HE1  A PHE A 1 35  ? 13.50815  10.87946 28.08556 0.881 18.52189  ? 32  PHE A HE1  1 
ATOM   699  H HE1  B PHE A 1 35  ? 12.37807  9.37361  27.93781 0.119 18.52189  ? 32  PHE A HE1  1 
ATOM   700  H HE2  A PHE A 1 35  ? 9.62281   10.44913 28.91443 0.881 16.67114  ? 32  PHE A HE2  1 
ATOM   701  H HE2  B PHE A 1 35  ? 11.11423  12.98925 29.08596 0.119 16.67114  ? 32  PHE A HE2  1 
ATOM   702  H HZ   A PHE A 1 35  ? 11.83382  10.28671 29.55926 0.881 17.88392  ? 32  PHE A HZ   1 
ATOM   703  H HZ   B PHE A 1 35  ? 12.05366  10.94530 29.60112 0.119 17.88392  ? 32  PHE A HZ   1 
ATOM   704  N N    . PHE A 1 36  ? 9.15346   10.50588 21.92443 1.000 7.38197   ? 33  PHE A N    1 
ATOM   705  C CA   . PHE A 1 36  ? 8.25773   10.92675 20.85507 1.000 8.11627   ? 33  PHE A CA   1 
ATOM   706  C C    . PHE A 1 36  ? 7.15986   11.77637 21.48696 1.000 8.50436   ? 33  PHE A C    1 
ATOM   707  O O    . PHE A 1 36  ? 6.40382   11.29127 22.33697 1.000 9.45159   ? 33  PHE A O    1 
ATOM   708  C CB   . PHE A 1 36  ? 7.65563   9.71719  20.14773 1.000 9.31932   ? 33  PHE A CB   1 
ATOM   709  C CG   . PHE A 1 36  ? 8.64304   8.94928  19.31585 1.000 9.45814   ? 33  PHE A CG   1 
ATOM   710  C CD1  . PHE A 1 36  ? 9.17807   9.50427  18.16955 1.000 12.04318  ? 33  PHE A CD1  1 
ATOM   711  C CD2  . PHE A 1 36  ? 9.02367   7.66762  19.67218 1.000 13.17892  ? 33  PHE A CD2  1 
ATOM   712  C CE1  . PHE A 1 36  ? 10.08537  8.80015  17.40143 1.000 14.12401  ? 33  PHE A CE1  1 
ATOM   713  C CE2  . PHE A 1 36  ? 9.92643   6.95721  18.90527 1.000 14.73862  ? 33  PHE A CE2  1 
ATOM   714  C CZ   . PHE A 1 36  ? 10.45866  7.52469  17.77009 1.000 13.98900  ? 33  PHE A CZ   1 
ATOM   715  H H    . PHE A 1 36  ? 9.02908   9.69736  22.18982 1.000 8.85837   ? 33  PHE A H    1 
ATOM   716  H HA   . PHE A 1 36  ? 8.74062   11.44293 20.19078 1.000 9.73953   ? 33  PHE A HA   1 
ATOM   717  H HB2  . PHE A 1 36  ? 7.29705   9.11189  20.81552 1.000 11.18318  ? 33  PHE A HB2  1 
ATOM   718  H HB3  . PHE A 1 36  ? 6.94615   10.02076 19.56004 1.000 11.18318  ? 33  PHE A HB3  1 
ATOM   719  H HD1  . PHE A 1 36  ? 8.92478   10.36125 17.91203 1.000 14.45182  ? 33  PHE A HD1  1 
ATOM   720  H HD2  . PHE A 1 36  ? 8.66692   7.27933  20.43825 1.000 15.81471  ? 33  PHE A HD2  1 
ATOM   721  H HE1  . PHE A 1 36  ? 10.44451  9.18645  16.63547 1.000 16.94882  ? 33  PHE A HE1  1 
ATOM   722  H HE2  . PHE A 1 36  ? 10.17427  6.09653  19.15569 1.000 17.68634  ? 33  PHE A HE2  1 
ATOM   723  H HZ   . PHE A 1 36  ? 11.06833  7.04944  17.25303 1.000 16.78680  ? 33  PHE A HZ   1 
ATOM   724  N N    . TYR A 1 37  ? 7.09466   13.04558 21.09801 1.000 8.22710   ? 34  TYR A N    1 
ATOM   725  C CA   . TYR A 1 37  ? 6.16432   14.01473 21.67240 1.000 8.05182   ? 34  TYR A CA   1 
ATOM   726  C C    . TYR A 1 37  ? 5.06972   14.27671 20.64360 1.000 8.02007   ? 34  TYR A C    1 
ATOM   727  O O    . TYR A 1 37  ? 5.28623   14.98406 19.65542 1.000 6.86722   ? 34  TYR A O    1 
ATOM   728  C CB   . TYR A 1 37  ? 6.89819   15.29897 22.04396 1.000 8.36762   ? 34  TYR A CB   1 
ATOM   729  C CG   . TYR A 1 37  ? 6.01114   16.37425 22.62808 1.000 7.86303   ? 34  TYR A CG   1 
ATOM   730  C CD1  . TYR A 1 37  ? 4.88324   16.04975 23.37393 1.000 8.90369   ? 34  TYR A CD1  1 
ATOM   731  C CD2  . TYR A 1 37  ? 6.29982   17.71593 22.42804 1.000 7.76383   ? 34  TYR A CD2  1 
ATOM   732  C CE1  . TYR A 1 37  ? 4.07632   17.02893 23.90526 1.000 8.85679   ? 34  TYR A CE1  1 
ATOM   733  C CE2  . TYR A 1 37  ? 5.49268   18.70137 22.95058 1.000 8.49784   ? 34  TYR A CE2  1 
ATOM   734  C CZ   . TYR A 1 37  ? 4.38629   18.34815 23.69311 1.000 9.05268   ? 34  TYR A CZ   1 
ATOM   735  O OH   . TYR A 1 37  ? 3.57659   19.32045 24.21833 1.000 9.91970   ? 34  TYR A OH   1 
ATOM   736  H H    . TYR A 1 37  ? 7.59484   13.38003 20.48355 1.000 9.87252   ? 34  TYR A H    1 
ATOM   737  H HA   . TYR A 1 37  ? 5.75539   13.64543 22.47071 1.000 9.66219   ? 34  TYR A HA   1 
ATOM   738  H HB2  . TYR A 1 37  ? 7.57753   15.08800 22.70342 1.000 10.04115  ? 34  TYR A HB2  1 
ATOM   739  H HB3  . TYR A 1 37  ? 7.31240   15.66140 21.24523 1.000 10.04115  ? 34  TYR A HB3  1 
ATOM   740  H HD1  . TYR A 1 37  ? 4.67085   15.15554 23.51593 1.000 10.68443  ? 34  TYR A HD1  1 
ATOM   741  H HD2  . TYR A 1 37  ? 7.05044   17.95373 21.93314 1.000 9.31660   ? 34  TYR A HD2  1 
ATOM   742  H HE1  . TYR A 1 37  ? 3.32635   16.79825 24.40450 1.000 10.62815  ? 34  TYR A HE1  1 
ATOM   743  H HE2  . TYR A 1 37  ? 5.69223   19.59778 22.80382 1.000 10.19740  ? 34  TYR A HE2  1 
ATOM   744  H HH   . TYR A 1 37  ? 3.78278   20.06950 23.89893 1.000 11.90364  ? 34  TYR A HH   1 
ATOM   745  N N    . PHE A 1 38  ? 3.90793   13.66645 20.86864 1.000 7.58782   ? 35  PHE A N    1 
ATOM   746  C CA   . PHE A 1 38  ? 2.73665   13.85944 20.02200 1.000 7.20445   ? 35  PHE A CA   1 
ATOM   747  C C    . PHE A 1 38  ? 2.01441   15.11267 20.50287 1.000 7.20154   ? 35  PHE A C    1 
ATOM   748  O O    . PHE A 1 38  ? 1.60170   15.18216 21.66617 1.000 7.23907   ? 35  PHE A O    1 
ATOM   749  C CB   . PHE A 1 38  ? 1.82604   12.63712 20.12387 1.000 7.24297   ? 35  PHE A CB   1 
ATOM   750  C CG   . PHE A 1 38  ? 2.45701   11.35846 19.63381 1.000 7.63932   ? 35  PHE A CG   1 
ATOM   751  C CD1  . PHE A 1 38  ? 3.35618   10.65995 20.42526 1.000 9.23525   ? 35  PHE A CD1  1 
ATOM   752  C CD2  . PHE A 1 38  ? 2.13999   10.84912 18.38771 1.000 7.96769   ? 35  PHE A CD2  1 
ATOM   753  C CE1  . PHE A 1 38  ? 3.93085   9.48190  19.97858 1.000 9.73673   ? 35  PHE A CE1  1 
ATOM   754  C CE2  . PHE A 1 38  ? 2.70805   9.66899  17.94121 1.000 9.08702   ? 35  PHE A CE2  1 
ATOM   755  C CZ   . PHE A 1 38  ? 3.60904   8.99051  18.73315 1.000 9.54334   ? 35  PHE A CZ   1 
ATOM   756  H H    . PHE A 1 38  ? 3.77060   13.12318 21.52102 1.000 9.10539   ? 35  PHE A H    1 
ATOM   757  H HA   . PHE A 1 38  ? 2.99175   13.97214 19.09295 1.000 8.64534   ? 35  PHE A HA   1 
ATOM   758  H HB2  . PHE A 1 38  ? 1.58207   12.50798 21.05377 1.000 8.69157   ? 35  PHE A HB2  1 
ATOM   759  H HB3  . PHE A 1 38  ? 1.03109   12.79656 19.59139 1.000 8.69157   ? 35  PHE A HB3  1 
ATOM   760  H HD1  . PHE A 1 38  ? 3.57629   10.98710 21.26754 1.000 11.08230  ? 35  PHE A HD1  1 
ATOM   761  H HD2  . PHE A 1 38  ? 1.53853   11.30467 17.84400 1.000 9.56123   ? 35  PHE A HD2  1 
ATOM   762  H HE1  . PHE A 1 38  ? 4.53315   9.02336  20.51884 1.000 11.68407  ? 35  PHE A HE1  1 
ATOM   763  H HE2  . PHE A 1 38  ? 2.48118   9.33274  17.10433 1.000 10.90443  ? 35  PHE A HE2  1 
ATOM   764  H HZ   . PHE A 1 38  ? 3.99846   8.20327  18.42739 1.000 11.45200  ? 35  PHE A HZ   1 
ATOM   765  N N    . SER A 1 39  ? 1.87455   16.10395 19.61857 1.000 7.67889   ? 36  SER A N    1 
ATOM   766  C CA   . SER A 1 39  ? 1.41537   17.42810 20.02107 1.000 8.32572   ? 36  SER A CA   1 
ATOM   767  C C    . SER A 1 39  ? 0.92714   18.20552 18.80686 1.000 7.73655   ? 36  SER A C    1 
ATOM   768  O O    . SER A 1 39  ? 1.31686   17.92664 17.67050 1.000 9.47442   ? 36  SER A O    1 
ATOM   769  C CB   . SER A 1 39  ? 2.56090   18.19590 20.69438 1.000 8.62183   ? 36  SER A CB   1 
ATOM   770  O OG   . SER A 1 39  ? 2.10388   19.33771 21.39031 1.000 9.74115   ? 36  SER A OG   1 
ATOM   771  H H    . SER A 1 39  ? 2.04054   16.03117 18.77789 1.000 9.21467   ? 36  SER A H    1 
ATOM   772  H HA   . SER A 1 39  ? 0.66516   17.33245 20.62847 1.000 9.99086   ? 36  SER A HA   1 
ATOM   773  H HB2  . SER A 1 39  ? 3.00216   17.60484 21.32433 1.000 10.34620  ? 36  SER A HB2  1 
ATOM   774  H HB3  . SER A 1 39  ? 3.18780   18.47977 20.01077 1.000 10.34620  ? 36  SER A HB3  1 
ATOM   775  H HG   . SER A 1 39  ? 1.67723   19.10493 22.07542 1.000 11.68938  ? 36  SER A HG   1 
ATOM   776  N N    . ALA A 1 40  ? 0.09866   19.21988 19.07372 1.000 8.40528   ? 37  ALA A N    1 
ATOM   777  C CA   . ALA A 1 40  ? -0.40708  20.10174 18.03010 1.000 8.95869   ? 37  ALA A CA   1 
ATOM   778  C C    . ALA A 1 40  ? -0.57041  21.51652 18.57025 1.000 8.26368   ? 37  ALA A C    1 
ATOM   779  O O    . ALA A 1 40  ? -0.93295  21.72281 19.73244 1.000 8.95291   ? 37  ALA A O    1 
ATOM   780  C CB   . ALA A 1 40  ? -1.74730  19.61049 17.46260 1.000 10.17865  ? 37  ALA A CB   1 
ATOM   781  H H    . ALA A 1 40  ? -0.18551  19.41629 19.86129 1.000 10.08634  ? 37  ALA A H    1 
ATOM   782  H HA   . ALA A 1 40  ? 0.24598   20.12771 17.31334 1.000 10.75042  ? 37  ALA A HA   1 
ATOM   783  H HB1  . ALA A 1 40  ? -2.11130  20.29267 16.87691 1.000 12.21438  ? 37  ALA A HB1  1 
ATOM   784  H HB2  . ALA A 1 40  ? -1.59812  18.79182 16.96417 1.000 12.21438  ? 37  ALA A HB2  1 
ATOM   785  H HB3  . ALA A 1 40  ? -2.35908  19.44399 18.19670 1.000 12.21438  ? 37  ALA A HB3  1 
ATOM   786  N N    . SER A 1 41  ? -0.31755  22.49071 17.69361 1.000 8.64532   ? 38  SER A N    1 
ATOM   787  C CA   . SER A 1 41  ? -0.42666  23.89331 18.06523 1.000 9.98844   ? 38  SER A CA   1 
ATOM   788  C C    . SER A 1 41  ? -1.85581  24.29254 18.40043 1.000 10.84317  ? 38  SER A C    1 
ATOM   789  O O    . SER A 1 41  ? -2.05666  25.29923 19.08720 1.000 12.63614  ? 38  SER A O    1 
ATOM   790  C CB   . SER A 1 41  ? 0.08195   24.76866 16.91658 1.000 9.91950   ? 38  SER A CB   1 
ATOM   791  O OG   . SER A 1 41  ? -0.86483  24.82759 15.86041 1.000 11.43492  ? 38  SER A OG   1 
ATOM   792  H H    . SER A 1 41  ? -0.08090  22.36185 16.87692 1.000 10.37438  ? 38  SER A H    1 
ATOM   793  H HA   . SER A 1 41  ? 0.12372   24.05157 18.84813 1.000 11.98613  ? 38  SER A HA   1 
ATOM   794  H HB2  . SER A 1 41  ? 0.23763   25.66614 17.25004 1.000 11.90340  ? 38  SER A HB2  1 
ATOM   795  H HB3  . SER A 1 41  ? 0.90917   24.39277 16.57700 1.000 11.90340  ? 38  SER A HB3  1 
ATOM   796  H HG   . SER A 1 41  ? -1.08220  24.05087 15.62576 1.000 13.72191  ? 38  SER A HG   1 
ATOM   797  N N    . TRP A 1 42  ? -2.84600  23.53900 17.92211 1.000 10.21857  ? 39  TRP A N    1 
ATOM   798  C CA   . TRP A 1 42  ? -4.25265  23.85269 18.13712 1.000 10.78102  ? 39  TRP A CA   1 
ATOM   799  C C    . TRP A 1 42  ? -4.80470  23.22176 19.40494 1.000 11.84336  ? 39  TRP A C    1 
ATOM   800  O O    . TRP A 1 42  ? -5.99803  23.36560 19.69345 1.000 13.75720  ? 39  TRP A O    1 
ATOM   801  C CB   . TRP A 1 42  ? -5.09176  23.42534 16.92160 1.000 11.93709  ? 39  TRP A CB   1 
ATOM   802  C CG   . TRP A 1 42  ? -4.81602  22.04366 16.36128 1.000 13.13212  ? 39  TRP A CG   1 
ATOM   803  C CD1  . TRP A 1 42  ? -4.11194  21.73980 15.22800 1.000 13.36465  ? 39  TRP A CD1  1 
ATOM   804  C CD2  . TRP A 1 42  ? -5.26158  20.79404 16.89953 1.000 11.88676  ? 39  TRP A CD2  1 
ATOM   805  N NE1  . TRP A 1 42  ? -4.08813  20.37993 15.03467 1.000 13.91030  ? 39  TRP A NE1  1 
ATOM   806  C CE2  . TRP A 1 42  ? -4.78401  19.77670 16.04863 1.000 12.78535  ? 39  TRP A CE2  1 
ATOM   807  C CE3  . TRP A 1 42  ? -6.00972  20.43565 18.02286 1.000 12.69185  ? 39  TRP A CE3  1 
ATOM   808  C CZ2  . TRP A 1 42  ? -5.03377  18.42737 16.28628 1.000 13.47065  ? 39  TRP A CZ2  1 
ATOM   809  C CZ3  . TRP A 1 42  ? -6.25694  19.09431 18.25552 1.000 13.64585  ? 39  TRP A CZ3  1 
ATOM   810  C CH2  . TRP A 1 42  ? -5.76986  18.10761 17.39245 1.000 13.05925  ? 39  TRP A CH2  1 
ATOM   811  H H    . TRP A 1 42  ? -2.72255  22.82467 17.45940 1.000 12.26228  ? 39  TRP A H    1 
ATOM   812  H HA   . TRP A 1 42  ? -4.34727  24.81431 18.22216 1.000 12.93722  ? 39  TRP A HA   1 
ATOM   813  H HB2  . TRP A 1 42  ? -6.02685  23.44636 17.17863 1.000 14.32450  ? 39  TRP A HB2  1 
ATOM   814  H HB3  . TRP A 1 42  ? -4.93009  24.05974 16.20585 1.000 14.32450  ? 39  TRP A HB3  1 
ATOM   815  H HD1  . TRP A 1 42  ? -3.70784  22.36384 14.66927 1.000 16.03758  ? 39  TRP A HD1  1 
ATOM   816  H HE1  . TRP A 1 42  ? -3.69985  19.97382 14.38358 1.000 16.69237  ? 39  TRP A HE1  1 
ATOM   817  H HE3  . TRP A 1 42  ? -6.33528  21.08554 18.60300 1.000 15.23022  ? 39  TRP A HE3  1 
ATOM   818  H HZ2  . TRP A 1 42  ? -4.71184  17.76885 15.71390 1.000 16.16478  ? 39  TRP A HZ2  1 
ATOM   819  H HZ3  . TRP A 1 42  ? -6.75609  18.84437 18.99934 1.000 16.37501  ? 39  TRP A HZ3  1 
ATOM   820  H HH2  . TRP A 1 42  ? -5.95089  17.21392 17.57533 1.000 15.67110  ? 39  TRP A HH2  1 
ATOM   821  N N    . CYS A 1 43  ? -3.96677  22.55017 20.17053 1.000 10.62956  ? 40  CYS A N    1 
ATOM   822  C CA   . CYS A 1 43  ? -4.41497  21.78831 21.32981 1.000 10.18318  ? 40  CYS A CA   1 
ATOM   823  C C    . CYS A 1 43  ? -4.04411  22.55541 22.58344 1.000 11.15262  ? 40  CYS A C    1 
ATOM   824  O O    . CYS A 1 43  ? -2.84839  22.71338 22.87401 1.000 10.36084  ? 40  CYS A O    1 
ATOM   825  C CB   . CYS A 1 43  ? -3.71799  20.42733 21.29944 1.000 13.38566  ? 40  CYS A CB   1 
ATOM   826  S SG   . CYS A 1 43  ? -3.89964  19.46529 22.78491 1.000 15.00308  ? 40  CYS A SG   1 
ATOM   827  H H    . CYS A 1 43  ? -3.11723  22.51641 20.04117 1.000 12.75547  ? 40  CYS A H    1 
ATOM   828  H HA   . CYS A 1 43  ? -5.37665  21.66160 21.32675 1.000 12.21981  ? 40  CYS A HA   1 
ATOM   829  H HB2  . CYS A 1 43  ? -4.08769  19.90824 20.56816 1.000 16.06279  ? 40  CYS A HB2  1 
ATOM   830  H HB3  . CYS A 1 43  ? -2.76904  20.57037 21.15823 1.000 16.06279  ? 40  CYS A HB3  1 
ATOM   831  H HG   . CYS A 1 43  ? -3.57428  18.33255 22.55899 1.000 18.00369  ? 40  CYS A HG   1 
ATOM   832  N N    . PRO A 1 44  ? -5.00664  23.06199 23.35103 1.000 10.79192  ? 41  PRO A N    1 
ATOM   833  C CA   . PRO A 1 44  ? -4.66589  23.94182 24.47546 1.000 11.83248  ? 41  PRO A CA   1 
ATOM   834  C C    . PRO A 1 44  ? -3.78843  23.25987 25.51095 1.000 12.11009  ? 41  PRO A C    1 
ATOM   835  O O    . PRO A 1 44  ? -2.80338  23.86164 25.96390 1.000 11.25678  ? 41  PRO A O    1 
ATOM   836  C CB   . PRO A 1 44  ? -6.03642  24.33254 25.05008 1.000 14.13510  ? 41  PRO A CB   1 
ATOM   837  C CG   . PRO A 1 44  ? -6.94007  24.28244 23.86715 1.000 14.82145  ? 41  PRO A CG   1 
ATOM   838  C CD   . PRO A 1 44  ? -6.45461  23.10268 23.05515 1.000 12.07623  ? 41  PRO A CD   1 
ATOM   839  H HA   . PRO A 1 44  ? -4.20349  24.73122 24.15307 1.000 14.19898  ? 41  PRO A HA   1 
ATOM   840  H HB2  . PRO A 1 44  ? -6.30959  23.69596 25.72908 1.000 16.96212  ? 41  PRO A HB2  1 
ATOM   841  H HB3  . PRO A 1 44  ? -5.99994  25.22525 25.42775 1.000 16.96212  ? 41  PRO A HB3  1 
ATOM   842  H HG2  . PRO A 1 44  ? -7.85658  24.15088 24.15631 1.000 17.78575  ? 41  PRO A HG2  1 
ATOM   843  H HG3  . PRO A 1 44  ? -6.86718  25.10609 23.36002 1.000 17.78575  ? 41  PRO A HG3  1 
ATOM   844  H HD2  . PRO A 1 44  ? -6.88895  22.28396 23.34140 1.000 14.49148  ? 41  PRO A HD2  1 
ATOM   845  H HD3  . PRO A 1 44  ? -6.60998  23.24724 22.10865 1.000 14.49148  ? 41  PRO A HD3  1 
ATOM   846  N N    . PRO A 1 45  ? -4.09060  22.02787 25.93628 1.000 10.58933  ? 42  PRO A N    1 
ATOM   847  C CA   . PRO A 1 45  ? -3.16877  21.38906 26.89320 1.000 11.09686  ? 42  PRO A CA   1 
ATOM   848  C C    . PRO A 1 45  ? -1.77830  21.15686 26.32269 1.000 8.88882   ? 42  PRO A C    1 
ATOM   849  O O    . PRO A 1 45  ? -0.79902  21.20287 27.07836 1.000 9.76880   ? 42  PRO A O    1 
ATOM   850  C CB   . PRO A 1 45  ? -3.86820  20.08751 27.30749 1.000 11.44056  ? 42  PRO A CB   1 
ATOM   851  C CG   . PRO A 1 45  ? -5.03245  19.93250 26.43713 1.000 14.27829  ? 42  PRO A CG   1 
ATOM   852  C CD   . PRO A 1 45  ? -5.30577  21.22459 25.70476 1.000 11.67547  ? 42  PRO A CD   1 
ATOM   853  H HA   . PRO A 1 45  ? -3.09923  21.94039 27.68824 1.000 13.31624  ? 42  PRO A HA   1 
ATOM   854  H HB2  . PRO A 1 45  ? -3.25696  19.34304 27.19325 1.000 13.72867  ? 42  PRO A HB2  1 
ATOM   855  H HB3  . PRO A 1 45  ? -4.14364  20.15124 28.23538 1.000 13.72867  ? 42  PRO A HB3  1 
ATOM   856  H HG2  . PRO A 1 45  ? -4.85004  19.22560 25.79844 1.000 17.13395  ? 42  PRO A HG2  1 
ATOM   857  H HG3  . PRO A 1 45  ? -5.79855  19.69656 26.98332 1.000 17.13395  ? 42  PRO A HG3  1 
ATOM   858  H HD2  . PRO A 1 45  ? -5.43329  21.06117 24.75716 1.000 14.01057  ? 42  PRO A HD2  1 
ATOM   859  H HD3  . PRO A 1 45  ? -6.08562  21.66883 26.07269 1.000 14.01057  ? 42  PRO A HD3  1 
ATOM   860  N N    . CYS A 1 46  ? -1.65813  20.91289 25.01276 1.000 8.98588   ? 43  CYS A N    1 
ATOM   861  C CA   . CYS A 1 46  ? -0.33637  20.82763 24.40176 1.000 9.09704   ? 43  CYS A CA   1 
ATOM   862  C C    . CYS A 1 46  ? 0.41770   22.13786 24.57096 1.000 7.85467   ? 43  CYS A C    1 
ATOM   863  O O    . CYS A 1 46  ? 1.59412   22.15160 24.94933 1.000 9.57938   ? 43  CYS A O    1 
ATOM   864  C CB   . CYS A 1 46  ? -0.45462  20.52021 22.91051 1.000 10.17186  ? 43  CYS A CB   1 
ATOM   865  S SG   . CYS A 1 46  ? -0.91756  18.85379 22.51601 1.000 12.94940  ? 43  CYS A SG   1 
ATOM   866  H H    . CYS A 1 46  ? -2.31481  20.79586 24.46993 1.000 10.78305  ? 43  CYS A H    1 
ATOM   867  H HA   . CYS A 1 46  ? 0.14969   20.10830 24.83443 1.000 10.91645  ? 43  CYS A HA   1 
ATOM   868  H HB2  . CYS A 1 46  ? -1.12767  21.10588 22.52984 1.000 12.20624  ? 43  CYS A HB2  1 
ATOM   869  H HB3  . CYS A 1 46  ? 0.40527   20.68843 22.49434 1.000 12.20624  ? 43  CYS A HB3  1 
ATOM   870  H HG   . CYS A 1 46  ? -0.93757  18.72587 21.32302 1.000 15.53928  ? 43  CYS A HG   1 
ATOM   871  N N    . ARG A 1 47  ? -0.24215  23.25513 24.25373 1.000 9.57961   ? 44  ARG A N    1 
ATOM   872  C CA   . ARG A 1 47  ? 0.41622   24.55235 24.34746 1.000 11.65441  ? 44  ARG A CA   1 
ATOM   873  C C    . ARG A 1 47  ? 0.88331   24.83258 25.76827 1.000 9.41301   ? 44  ARG A C    1 
ATOM   874  O O    . ARG A 1 47  ? 1.90785   25.49539 25.96441 1.000 10.88006  ? 44  ARG A O    1 
ATOM   875  C CB   . ARG A 1 47  ? -0.51438  25.65987 23.84697 1.000 11.43637  ? 44  ARG A CB   1 
ATOM   876  C CG   . ARG A 1 47  ? -0.77827  25.60465 22.34281 1.000 15.58612  ? 44  ARG A CG   1 
ATOM   877  C CD   . ARG A 1 47  ? -1.50840  26.84598 21.83120 1.000 24.21063  ? 44  ARG A CD   1 
ATOM   878  N NE   . ARG A 1 47  ? -2.73161  27.14909 22.56849 1.000 30.82355  ? 44  ARG A NE   1 
ATOM   879  C CZ   . ARG A 1 47  ? -3.96520  26.94994 22.11706 1.000 34.66676  ? 44  ARG A CZ   1 
ATOM   880  N NH1  . ARG A 1 47  ? -4.19231  26.40592 20.93211 1.000 35.94492  ? 44  ARG A NH1  1 
ATOM   881  N NH2  . ARG A 1 47  ? -4.99806  27.31325 22.87220 1.000 34.70422  ? 44  ARG A NH2  1 
ATOM   882  H H    . ARG A 1 47  ? -1.05882  23.28603 23.98597 1.000 11.49553  ? 44  ARG A H    1 
ATOM   883  H HA   . ARG A 1 47  ? 1.19728   24.55261 23.77228 1.000 13.98529  ? 44  ARG A HA   1 
ATOM   884  H HB2  . ARG A 1 47  ? -1.36775  25.57969 24.30108 1.000 13.72365  ? 44  ARG A HB2  1 
ATOM   885  H HB3  . ARG A 1 47  ? -0.11201  26.51968 24.04626 1.000 13.72365  ? 44  ARG A HB3  1 
ATOM   886  H HG2  . ARG A 1 47  ? 0.06846   25.53938 21.87411 1.000 18.70335  ? 44  ARG A HG2  1 
ATOM   887  H HG3  . ARG A 1 47  ? -1.32751  24.82997 22.14507 1.000 18.70335  ? 44  ARG A HG3  1 
ATOM   888  H HD2  . ARG A 1 47  ? -0.91771  27.61137 21.90977 1.000 29.05275  ? 44  ARG A HD2  1 
ATOM   889  H HD3  . ARG A 1 47  ? -1.74931  26.70685 20.90195 1.000 29.05275  ? 44  ARG A HD3  1 
ATOM   890  H HE   . ARG A 1 47  ? -2.64699  27.48263 23.35665 1.000 36.98826  ? 44  ARG A HE   1 
ATOM   891  H HH11 . ARG A 1 47  ? -3.53238  26.17143 20.43300 1.000 43.13390  ? 44  ARG A HH11 1 
ATOM   892  H HH12 . ARG A 1 47  ? -4.99982  26.28690 20.66124 1.000 43.13390  ? 44  ARG A HH12 1 
ATOM   893  H HH21 . ARG A 1 47  ? -4.86278  27.67202 23.64199 1.000 41.64506  ? 44  ARG A HH21 1 
ATOM   894  H HH22 . ARG A 1 47  ? -5.80118  27.18938 22.59068 1.000 41.64506  ? 44  ARG A HH22 1 
ATOM   895  N N    . GLY A 1 48  ? 0.16496   24.31733 26.76910 1.000 10.34166  ? 45  GLY A N    1 
ATOM   896  C CA   . GLY A 1 48  ? 0.57740   24.51592 28.14592 1.000 11.36716  ? 45  GLY A CA   1 
ATOM   897  C C    . GLY A 1 48  ? 1.65062   23.55535 28.60789 1.000 11.34248  ? 45  GLY A C    1 
ATOM   898  O O    . GLY A 1 48  ? 2.49073   23.91746 29.43828 1.000 13.43785  ? 45  GLY A O    1 
ATOM   899  H H    . GLY A 1 48  ? -0.55447  23.85606 26.67293 1.000 12.40999  ? 45  GLY A H    1 
ATOM   900  H HA2  . GLY A 1 48  ? 0.91974   25.41807 28.24507 1.000 13.64059  ? 45  GLY A HA2  1 
ATOM   901  H HA3  . GLY A 1 48  ? -0.19321  24.40520 28.72455 1.000 13.64059  ? 45  GLY A HA3  1 
ATOM   902  N N    . PHE A 1 49  ? 1.64314   22.32656 28.08649 1.000 10.43712  ? 46  PHE A N    1 
ATOM   903  C CA   . PHE A 1 49  ? 2.64614   21.33916 28.46626 1.000 8.54959   ? 46  PHE A CA   1 
ATOM   904  C C    . PHE A 1 49  ? 3.99265   21.59640 27.79673 1.000 8.05678   ? 46  PHE A C    1 
ATOM   905  O O    . PHE A 1 49  ? 5.03942   21.34116 28.40132 1.000 8.38910   ? 46  PHE A O    1 
ATOM   906  C CB   . PHE A 1 49  ? 2.15037   19.93224 28.11228 1.000 9.24384   ? 46  PHE A CB   1 
ATOM   907  C CG   . PHE A 1 49  ? 3.14543   18.85205 28.41429 1.000 9.26753   ? 46  PHE A CG   1 
ATOM   908  C CD1  . PHE A 1 49  ? 3.46223   18.53618 29.72175 1.000 10.17140  ? 46  PHE A CD1  1 
ATOM   909  C CD2  . PHE A 1 49  ? 3.77105   18.15930 27.39545 1.000 9.61639   ? 46  PHE A CD2  1 
ATOM   910  C CE1  . PHE A 1 49  ? 4.38434   17.55542 30.00847 1.000 10.36106  ? 46  PHE A CE1  1 
ATOM   911  C CE2  . PHE A 1 49  ? 4.69150   17.17269 27.68014 1.000 10.36761  ? 46  PHE A CE2  1 
ATOM   912  C CZ   . PHE A 1 49  ? 4.99676   16.87173 28.98921 1.000 11.43005  ? 46  PHE A CZ   1 
ATOM   913  H H    . PHE A 1 49  ? 1.06871   22.04290 27.51276 1.000 12.52454  ? 46  PHE A H    1 
ATOM   914  H HA   . PHE A 1 49  ? 2.77820   21.38461 29.42615 1.000 10.25951  ? 46  PHE A HA   1 
ATOM   915  H HB2  . PHE A 1 49  ? 1.34661   19.74648 28.62254 1.000 11.09261  ? 46  PHE A HB2  1 
ATOM   916  H HB3  . PHE A 1 49  ? 1.95550   19.89922 27.16263 1.000 11.09261  ? 46  PHE A HB3  1 
ATOM   917  H HD1  . PHE A 1 49  ? 3.04669   18.99252 30.41743 1.000 12.20568  ? 46  PHE A HD1  1 
ATOM   918  H HD2  . PHE A 1 49  ? 3.56962   18.36016 26.51002 1.000 11.53967  ? 46  PHE A HD2  1 
ATOM   919  H HE1  . PHE A 1 49  ? 4.59207   17.35638 30.89286 1.000 12.43327  ? 46  PHE A HE1  1 
ATOM   920  H HE2  . PHE A 1 49  ? 5.10633   16.71032 26.98802 1.000 12.44113  ? 46  PHE A HE2  1 
ATOM   921  H HZ   . PHE A 1 49  ? 5.61707   16.20608 29.18163 1.000 13.71606  ? 46  PHE A HZ   1 
ATOM   922  N N    . THR A 1 50  ? 3.99726   22.10318 26.56833 1.000 9.15859   ? 47  THR A N    1 
ATOM   923  C CA   . THR A 1 50  ? 5.25846   22.31413 25.85566 1.000 8.97935   ? 47  THR A CA   1 
ATOM   924  C C    . THR A 1 50  ? 6.29209   23.08514 26.66373 1.000 7.87928   ? 47  THR A C    1 
ATOM   925  O O    . THR A 1 50  ? 7.42699   22.59683 26.78323 1.000 8.92368   ? 47  THR A O    1 
ATOM   926  C CB   . THR A 1 50  ? 4.96635   22.91520 24.47448 1.000 9.07130   ? 47  THR A CB   1 
ATOM   927  O OG1  . THR A 1 50  ? 4.44521   21.87277 23.63860 1.000 10.07693  ? 47  THR A OG1  1 
ATOM   928  C CG2  . THR A 1 50  ? 6.22019   23.51208 23.84265 1.000 11.62623  ? 47  THR A CG2  1 
ATOM   929  H H    . THR A 1 50  ? 3.29443   22.33121 26.12829 1.000 10.99031  ? 47  THR A H    1 
ATOM   930  H HA   . THR A 1 50  ? 5.66706   21.45013 25.68999 1.000 10.77522  ? 47  THR A HA   1 
ATOM   931  H HB   . THR A 1 50  ? 4.32508   23.63837 24.55628 1.000 10.88556  ? 47  THR A HB   1 
ATOM   932  H HG1  . THR A 1 50  ? 3.92624   22.19794 23.06369 1.000 12.09232  ? 47  THR A HG1  1 
ATOM   933  H HG21 . THR A 1 50  ? 6.05588   23.71672 22.90883 1.000 13.95148  ? 47  THR A HG21 1 
ATOM   934  H HG22 . THR A 1 50  ? 6.46833   24.32802 24.30479 1.000 13.95148  ? 47  THR A HG22 1 
ATOM   935  H HG23 . THR A 1 50  ? 6.95433   22.88089 23.90215 1.000 13.95148  ? 47  THR A HG23 1 
ATOM   936  N N    . PRO A 1 51  ? 5.98591   24.24336 27.25826 1.000 8.85449   ? 48  PRO A N    1 
ATOM   937  C CA   . PRO A 1 51  ? 7.02323   24.94746 28.03624 1.000 8.91885   ? 48  PRO A CA   1 
ATOM   938  C C    . PRO A 1 51  ? 7.52965   24.15493 29.22778 1.000 8.39762   ? 48  PRO A C    1 
ATOM   939  O O    . PRO A 1 51  ? 8.69842   24.29269 29.60945 1.000 9.18799   ? 48  PRO A O    1 
ATOM   940  C CB   . PRO A 1 51  ? 6.34821   26.26068 28.46356 1.000 11.55501  ? 48  PRO A CB   1 
ATOM   941  C CG   . PRO A 1 51  ? 4.91185   26.12886 28.10779 1.000 12.74942  ? 48  PRO A CG   1 
ATOM   942  C CD   . PRO A 1 51  ? 4.77093   25.05563 27.07335 1.000 9.78924   ? 48  PRO A CD   1 
ATOM   943  H HA   . PRO A 1 51  ? 7.76879   25.16256 27.45420 1.000 10.70262  ? 48  PRO A HA   1 
ATOM   944  H HB2  . PRO A 1 51  ? 6.45382   26.38354 29.41993 1.000 13.86601  ? 48  PRO A HB2  1 
ATOM   945  H HB3  . PRO A 1 51  ? 6.75186   27.00296 27.98714 1.000 13.86601  ? 48  PRO A HB3  1 
ATOM   946  H HG2  . PRO A 1 51  ? 4.41006   25.89249 28.90355 1.000 15.29930  ? 48  PRO A HG2  1 
ATOM   947  H HG3  . PRO A 1 51  ? 4.59516   26.97514 27.75507 1.000 15.29930  ? 48  PRO A HG3  1 
ATOM   948  H HD2  . PRO A 1 51  ? 3.97416   24.52573 27.23229 1.000 11.74709  ? 48  PRO A HD2  1 
ATOM   949  H HD3  . PRO A 1 51  ? 4.74330   25.43711 26.18195 1.000 11.74709  ? 48  PRO A HD3  1 
ATOM   950  N N    . THR A 1 52  ? 6.67885   23.33414 29.84049 1.000 9.31184   ? 49  THR A N    1 
ATOM   951  C CA   . THR A 1 52  ? 7.14298   22.47388 30.92310 1.000 8.91725   ? 49  THR A CA   1 
ATOM   952  C C    . THR A 1 52  ? 8.19243   21.49034 30.42060 1.000 7.06140   ? 49  THR A C    1 
ATOM   953  O O    . THR A 1 52  ? 9.22018   21.27438 31.07548 1.000 8.25297   ? 49  THR A O    1 
ATOM   954  C CB   . THR A 1 52  ? 5.94502   21.74098 31.52695 1.000 10.95644  ? 49  THR A CB   1 
ATOM   955  O OG1  . THR A 1 52  ? 4.97601   22.70384 31.96638 1.000 12.94996  ? 49  THR A OG1  1 
ATOM   956  C CG2  . THR A 1 52  ? 6.36739   20.87793 32.70201 1.000 12.29312  ? 49  THR A CG2  1 
ATOM   957  H H    . THR A 1 52  ? 5.84328   23.25773 29.65184 1.000 11.17421  ? 49  THR A H    1 
ATOM   958  H HA   . THR A 1 52  ? 7.55299   23.01007 31.61973 1.000 10.70070  ? 49  THR A HA   1 
ATOM   959  H HB   . THR A 1 52  ? 5.55248   21.15912 30.85744 1.000 13.14773  ? 49  THR A HB   1 
ATOM   960  H HG1  . THR A 1 52  ? 5.34494   23.28192 32.45146 1.000 15.53995  ? 49  THR A HG1  1 
ATOM   961  H HG21 . THR A 1 52  ? 5.58425   20.53212 33.15807 1.000 14.75174  ? 49  THR A HG21 1 
ATOM   962  H HG22 . THR A 1 52  ? 6.90471   20.13295 32.39026 1.000 14.75174  ? 49  THR A HG22 1 
ATOM   963  H HG23 . THR A 1 52  ? 6.89017   21.40283 33.32818 1.000 14.75174  ? 49  THR A HG23 1 
ATOM   964  N N    . LEU A 1 53  ? 7.96046   20.90112 29.24561 1.000 8.47435   ? 50  LEU A N    1 
ATOM   965  C CA   . LEU A 1 53  ? 8.93143   19.97202 28.67620 1.000 8.75926   ? 50  LEU A CA   1 
ATOM   966  C C    . LEU A 1 53  ? 10.18045  20.70546 28.19578 1.000 7.94681   ? 50  LEU A C    1 
ATOM   967  O O    . LEU A 1 53  ? 11.29532  20.18930 28.33640 1.000 8.35483   ? 50  LEU A O    1 
ATOM   968  C CB   . LEU A 1 53  ? 8.27442   19.17051 27.55283 1.000 8.70603   ? 50  LEU A CB   1 
ATOM   969  C CG   . LEU A 1 53  ? 9.10191   18.04800 26.92696 1.000 8.70973   ? 50  LEU A CG   1 
ATOM   970  C CD1  . LEU A 1 53  ? 9.54668   17.02947 27.96599 1.000 10.25361  ? 50  LEU A CD1  1 
ATOM   971  C CD2  . LEU A 1 53  ? 8.30215   17.36702 25.82717 1.000 10.17754  ? 50  LEU A CD2  1 
ATOM   972  H H    . LEU A 1 53  ? 7.25737   21.02156 28.76523 1.000 10.16922  ? 50  LEU A H    1 
ATOM   973  H HA   . LEU A 1 53  ? 9.21656   19.34111 29.35558 1.000 10.51111  ? 50  LEU A HA   1 
ATOM   974  H HB2  . LEU A 1 53  ? 7.46856   18.76387 27.90798 1.000 10.44723  ? 50  LEU A HB2  1 
ATOM   975  H HB3  . LEU A 1 53  ? 8.04805   19.78707 26.83902 1.000 10.44723  ? 50  LEU A HB3  1 
ATOM   976  H HG   . LEU A 1 53  ? 9.90461   18.43410 26.54292 1.000 10.45168  ? 50  LEU A HG   1 
ATOM   977  H HD11 . LEU A 1 53  ? 9.94056   16.26756 27.51294 1.000 12.30433  ? 50  LEU A HD11 1 
ATOM   978  H HD12 . LEU A 1 53  ? 10.20150  17.44096 28.55148 1.000 12.30433  ? 50  LEU A HD12 1 
ATOM   979  H HD13 . LEU A 1 53  ? 8.77495   16.74566 28.48056 1.000 12.30433  ? 50  LEU A HD13 1 
ATOM   980  H HD21 . LEU A 1 53  ? 8.88723   16.77068 25.33426 1.000 12.21305  ? 50  LEU A HD21 1 
ATOM   981  H HD22 . LEU A 1 53  ? 7.57817   16.86219 26.22952 1.000 12.21305  ? 50  LEU A HD22 1 
ATOM   982  H HD23 . LEU A 1 53  ? 7.94285   18.04398 25.23259 1.000 12.21305  ? 50  LEU A HD23 1 
ATOM   983  N N    . VAL A 1 54  ? 10.01821  21.92283 27.66000 1.000 8.60353   ? 51  VAL A N    1 
ATOM   984  C CA   . VAL A 1 54  ? 11.16861  22.72924 27.24626 1.000 8.54510   ? 51  VAL A CA   1 
ATOM   985  C C    . VAL A 1 54  ? 12.09609  22.98120 28.42940 1.000 8.47479   ? 51  VAL A C    1 
ATOM   986  O O    . VAL A 1 54  ? 13.31589  22.79914 28.33498 1.000 9.73188   ? 51  VAL A O    1 
ATOM   987  C CB   . VAL A 1 54  ? 10.70324  24.04955 26.59970 1.000 8.24471   ? 51  VAL A CB   1 
ATOM   988  C CG1  . VAL A 1 54  ? 11.87721  25.01271 26.41524 1.000 9.60603   ? 51  VAL A CG1  1 
ATOM   989  C CG2  . VAL A 1 54  ? 10.01079  23.77442 25.27544 1.000 7.97431   ? 51  VAL A CG2  1 
ATOM   990  H H    . VAL A 1 54  ? 9.25715   22.30057 27.52698 1.000 10.32424  ? 51  VAL A H    1 
ATOM   991  H HA   . VAL A 1 54  ? 11.66537  22.23052 26.57888 1.000 10.25411  ? 51  VAL A HA   1 
ATOM   992  H HB   . VAL A 1 54  ? 10.06480  24.47837 27.19080 1.000 9.89365   ? 51  VAL A HB   1 
ATOM   993  H HG11 . VAL A 1 54  ? 11.59898  25.74345 25.84121 1.000 11.52724  ? 51  VAL A HG11 1 
ATOM   994  H HG12 . VAL A 1 54  ? 12.14317  25.35619 27.28252 1.000 11.52724  ? 51  VAL A HG12 1 
ATOM   995  H HG13 . VAL A 1 54  ? 12.61657  24.53503 26.00773 1.000 11.52724  ? 51  VAL A HG13 1 
ATOM   996  H HG21 . VAL A 1 54  ? 9.78822   24.61924 24.85395 1.000 9.56918   ? 51  VAL A HG21 1 
ATOM   997  H HG22 . VAL A 1 54  ? 10.60992  23.26789 24.70504 1.000 9.56918   ? 51  VAL A HG22 1 
ATOM   998  H HG23 . VAL A 1 54  ? 9.20249   23.26460 25.44166 1.000 9.56918   ? 51  VAL A HG23 1 
ATOM   999  N N    . GLU A 1 55  ? 11.53289  23.40742 29.56189 1.000 9.03809   ? 52  GLU A N    1 
ATOM   1000 C CA   . GLU A 1 55  ? 12.36507  23.68057 30.72808 1.000 10.14389  ? 52  GLU A CA   1 
ATOM   1001 C C    . GLU A 1 55  ? 13.11889  22.43166 31.16632 1.000 9.66569   ? 52  GLU A C    1 
ATOM   1002 O O    . GLU A 1 55  ? 14.31191  22.49469 31.48555 1.000 11.59741  ? 52  GLU A O    1 
ATOM   1003 C CB   . GLU A 1 55  ? 11.50671  24.21347 31.87310 1.000 14.52203  ? 52  GLU A CB   1 
ATOM   1004 C CG   . GLU A 1 55  ? 12.32656  24.58784 33.09070 1.000 23.04180  ? 52  GLU A CG   1 
ATOM   1005 C CD   . GLU A 1 55  ? 11.54391  25.36850 34.12849 1.000 31.48718  ? 52  GLU A CD   1 
ATOM   1006 O OE1  . GLU A 1 55  ? 10.32821  25.59120 33.93777 1.000 33.03992  ? 52  GLU A OE1  1 
ATOM   1007 O OE2  . GLU A 1 55  ? 12.15636  25.76288 35.14248 1.000 35.02235  ? 52  GLU A OE2  1 
ATOM   1008 H H    . GLU A 1 55  ? 10.69137  23.54265 29.67655 1.000 10.84571  ? 52  GLU A H    1 
ATOM   1009 H HA   . GLU A 1 55  ? 13.01436  24.36296 30.49642 1.000 12.17266  ? 52  GLU A HA   1 
ATOM   1010 H HB2  . GLU A 1 55  ? 11.03525  25.00608 31.57243 1.000 17.42644  ? 52  GLU A HB2  1 
ATOM   1011 H HB3  . GLU A 1 55  ? 10.87136  23.52957 32.13676 1.000 17.42644  ? 52  GLU A HB3  1 
ATOM   1012 H HG2  . GLU A 1 55  ? 12.65084  23.77639 33.51177 1.000 27.65017  ? 52  GLU A HG2  1 
ATOM   1013 H HG3  . GLU A 1 55  ? 13.07470  25.13676 32.80811 1.000 27.65017  ? 52  GLU A HG3  1 
ATOM   1014 N N    . PHE A 1 56  ? 12.43410  21.28699 31.19428 1.000 8.33394   ? 53  PHE A N    1 
ATOM   1015 C CA   . PHE A 1 56  ? 13.08396  20.03972 31.58330 1.000 8.48448   ? 53  PHE A CA   1 
ATOM   1016 C C    . PHE A 1 56  ? 14.19542  19.67354 30.60604 1.000 8.36488   ? 53  PHE A C    1 
ATOM   1017 O O    . PHE A 1 56  ? 15.28357  19.25215 31.01596 1.000 9.35735   ? 53  PHE A O    1 
ATOM   1018 C CB   . PHE A 1 56  ? 12.03292  18.92700 31.65357 1.000 8.51521   ? 53  PHE A CB   1 
ATOM   1019 C CG   . PHE A 1 56  ? 12.57397  17.61803 32.13712 1.000 9.07700   ? 53  PHE A CG   1 
ATOM   1020 C CD1  . PHE A 1 56  ? 12.82843  17.41807 33.48173 1.000 10.39025  ? 53  PHE A CD1  1 
ATOM   1021 C CD2  . PHE A 1 56  ? 12.82859  16.58756 31.25121 1.000 10.88858  ? 53  PHE A CD2  1 
ATOM   1022 C CE1  . PHE A 1 56  ? 13.33560  16.21894 33.93289 1.000 10.97039  ? 53  PHE A CE1  1 
ATOM   1023 C CE2  . PHE A 1 56  ? 13.33882  15.38316 31.69588 1.000 11.38490  ? 53  PHE A CE2  1 
ATOM   1024 C CZ   . PHE A 1 56  ? 13.58626  15.19674 33.04032 1.000 11.04621  ? 53  PHE A CZ   1 
ATOM   1025 H H    . PHE A 1 56  ? 11.60140  21.20750 30.99457 1.000 10.00072  ? 53  PHE A H    1 
ATOM   1026 H HA   . PHE A 1 56  ? 13.48449  20.14055 32.46097 1.000 10.18137  ? 53  PHE A HA   1 
ATOM   1027 H HB2  . PHE A 1 56  ? 11.32949  19.20017 32.26305 1.000 10.21825  ? 53  PHE A HB2  1 
ATOM   1028 H HB3  . PHE A 1 56  ? 11.66710  18.78675 30.76621 1.000 10.21825  ? 53  PHE A HB3  1 
ATOM   1029 H HD1  . PHE A 1 56  ? 12.65518  18.10110 34.08866 1.000 12.46830  ? 53  PHE A HD1  1 
ATOM   1030 H HD2  . PHE A 1 56  ? 12.65437  16.70655 30.34545 1.000 13.06629  ? 53  PHE A HD2  1 
ATOM   1031 H HE1  . PHE A 1 56  ? 13.50892  16.09852 34.83863 1.000 13.16446  ? 53  PHE A HE1  1 
ATOM   1032 H HE2  . PHE A 1 56  ? 13.51509  14.69965 31.09037 1.000 13.66187  ? 53  PHE A HE2  1 
ATOM   1033 H HZ   . PHE A 1 56  ? 13.92117  14.38414 33.34433 1.000 13.25545  ? 53  PHE A HZ   1 
ATOM   1034 N N    . TYR A 1 57  ? 13.93730  19.83215 29.30723 1.000 7.83576   ? 54  TYR A N    1 
ATOM   1035 C CA   . TYR A 1 57  ? 14.94543  19.55509 28.28700 1.000 8.47675   ? 54  TYR A CA   1 
ATOM   1036 C C    . TYR A 1 57  ? 16.15661  20.46503 28.44313 1.000 9.29122   ? 54  TYR A C    1 
ATOM   1037 O O    . TYR A 1 57  ? 17.30366  20.00220 28.40555 1.000 9.61769   ? 54  TYR A O    1 
ATOM   1038 C CB   . TYR A 1 57  ? 14.29817  19.75427 26.91799 1.000 9.70137   ? 54  TYR A CB   1 
ATOM   1039 C CG   . TYR A 1 57  ? 15.13123  19.41356 25.70367 1.000 9.87309   ? 54  TYR A CG   1 
ATOM   1040 C CD1  . TYR A 1 57  ? 15.10721  18.13852 25.15302 1.000 9.67783   ? 54  TYR A CD1  1 
ATOM   1041 C CD2  . TYR A 1 57  ? 15.89104  20.38076 25.06880 1.000 10.46851  ? 54  TYR A CD2  1 
ATOM   1042 C CE1  . TYR A 1 57  ? 15.84301  17.83146 24.01436 1.000 9.63609   ? 54  TYR A CE1  1 
ATOM   1043 C CE2  . TYR A 1 57  ? 16.62630  20.08542 23.93287 1.000 10.77706  ? 54  TYR A CE2  1 
ATOM   1044 C CZ   . TYR A 1 57  ? 16.60352  18.81133 23.40939 1.000 9.99116   ? 54  TYR A CZ   1 
ATOM   1045 O OH   . TYR A 1 57  ? 17.33816  18.53399 22.27213 1.000 12.46262  ? 54  TYR A OH   1 
ATOM   1046 H H    . TYR A 1 57  ? 13.18419  20.09979 28.98976 1.000 9.40291   ? 54  TYR A H    1 
ATOM   1047 H HA   . TYR A 1 57  ? 15.25832  18.64076 28.37054 1.000 10.17211  ? 54  TYR A HA   1 
ATOM   1048 H HB2  . TYR A 1 57  ? 13.50435  19.19816 26.87948 1.000 11.64164  ? 54  TYR A HB2  1 
ATOM   1049 H HB3  . TYR A 1 57  ? 14.05255  20.68917 26.83722 1.000 11.64164  ? 54  TYR A HB3  1 
ATOM   1050 H HD1  . TYR A 1 57  ? 14.58925  17.47808 25.55357 1.000 11.61340  ? 54  TYR A HD1  1 
ATOM   1051 H HD2  . TYR A 1 57  ? 15.90815  21.24518 25.41143 1.000 12.56221  ? 54  TYR A HD2  1 
ATOM   1052 H HE1  . TYR A 1 57  ? 15.82292  16.97088 23.66236 1.000 11.56331  ? 54  TYR A HE1  1 
ATOM   1053 H HE2  . TYR A 1 57  ? 17.13544  20.74727 23.52346 1.000 12.93248  ? 54  TYR A HE2  1 
ATOM   1054 H HH   . TYR A 1 57  ? 17.14955  17.76618 21.98841 1.000 14.95515  ? 54  TYR A HH   1 
ATOM   1055 N N    . GLU A 1 58  ? 15.92221  21.76847 28.61608 1.000 9.97125   ? 55  GLU A N    1 
ATOM   1056 C CA   . GLU A 1 58  ? 17.03497  22.69795 28.77545 1.000 9.78466   ? 55  GLU A CA   1 
ATOM   1057 C C    . GLU A 1 58  ? 17.92306  22.29230 29.94399 1.000 10.00979  ? 55  GLU A C    1 
ATOM   1058 O O    . GLU A 1 58  ? 19.15457  22.35905 29.85247 1.000 12.37675  ? 55  GLU A O    1 
ATOM   1059 C CB   . GLU A 1 58  ? 16.51245  24.11710 29.00239 1.000 12.73108  ? 55  GLU A CB   1 
ATOM   1060 C CG   . GLU A 1 58  ? 15.87287  24.78564 27.80248 1.000 16.64163  ? 55  GLU A CG   1 
ATOM   1061 C CD   . GLU A 1 58  ? 15.11009  26.04570 28.19206 1.000 21.71731  ? 55  GLU A CD   1 
ATOM   1062 O OE1  . GLU A 1 58  ? 14.94091  26.29491 29.40798 1.000 24.60558  ? 55  GLU A OE1  1 
ATOM   1063 O OE2  . GLU A 1 58  ? 14.67759  26.78632 27.28429 1.000 22.70749  ? 55  GLU A OE2  1 
ATOM   1064 H H    . GLU A 1 58  ? 15.14279  22.13085 28.64405 1.000 11.96550  ? 55  GLU A H    1 
ATOM   1065 H HA   . GLU A 1 58  ? 17.56066  22.68814 27.96031 1.000 11.74159  ? 55  GLU A HA   1 
ATOM   1066 H HB2  . GLU A 1 58  ? 15.84344  24.08572 29.70406 1.000 15.27730  ? 55  GLU A HB2  1 
ATOM   1067 H HB3  . GLU A 1 58  ? 17.25695  24.67422 29.27852 1.000 15.27730  ? 55  GLU A HB3  1 
ATOM   1068 H HG2  . GLU A 1 58  ? 16.56430  25.03329 27.16883 1.000 19.96996  ? 55  GLU A HG2  1 
ATOM   1069 H HG3  . GLU A 1 58  ? 15.24888  24.16909 27.38848 1.000 19.96996  ? 55  GLU A HG3  1 
ATOM   1070 N N    . LYS A 1 59  ? 17.31627  21.87273 31.05367 1.000 9.80041   ? 56  LYS A N    1 
ATOM   1071 C CA   . LYS A 1 59  ? 18.10055  21.54765 32.23475 1.000 10.44975  ? 56  LYS A CA   1 
ATOM   1072 C C    . LYS A 1 59  ? 18.78291  20.18859 32.13243 1.000 9.59472   ? 56  LYS A C    1 
ATOM   1073 O O    . LYS A 1 59  ? 19.90278  20.02469 32.62853 1.000 11.10224  ? 56  LYS A O    1 
ATOM   1074 C CB   . LYS A 1 59  ? 17.21005  21.55401 33.47810 1.000 14.02181  ? 56  LYS A CB   1 
ATOM   1075 C CG   . LYS A 1 59  ? 16.68977  22.91442 33.88634 1.000 21.69410  ? 56  LYS A CG   1 
ATOM   1076 C CD   . LYS A 1 59  ? 15.88004  22.79966 35.16837 1.000 30.04254  ? 56  LYS A CD   1 
ATOM   1077 C CE   . LYS A 1 59  ? 15.59363  24.15682 35.77579 1.000 37.38843  ? 56  LYS A CE   1 
ATOM   1078 N NZ   . LYS A 1 59  ? 15.08327  24.02090 37.16941 1.000 40.36934  ? 56  LYS A NZ   1 
ATOM   1079 H H    . LYS A 1 59  ? 16.46714  21.77063 31.14401 1.000 11.76049  ? 56  LYS A H    1 
ATOM   1080 H HA   . LYS A 1 59  ? 18.78505  22.22942 32.32160 1.000 12.53970  ? 56  LYS A HA   1 
ATOM   1081 H HB2  . LYS A 1 59  ? 16.44102  20.98797 33.30754 1.000 16.82617  ? 56  LYS A HB2  1 
ATOM   1082 H HB3  . LYS A 1 59  ? 17.72165  21.20283 34.22364 1.000 16.82617  ? 56  LYS A HB3  1 
ATOM   1083 H HG2  . LYS A 1 59  ? 17.43462  23.51601 34.04182 1.000 26.03291  ? 56  LYS A HG2  1 
ATOM   1084 H HG3  . LYS A 1 59  ? 16.11751  23.26857 33.18777 1.000 26.03291  ? 56  LYS A HG3  1 
ATOM   1085 H HD2  . LYS A 1 59  ? 15.03283  22.36889 34.97450 1.000 36.05104  ? 56  LYS A HD2  1 
ATOM   1086 H HD3  . LYS A 1 59  ? 16.37788  22.27623 35.81574 1.000 36.05104  ? 56  LYS A HD3  1 
ATOM   1087 H HE2  . LYS A 1 59  ? 16.41018  24.67997 35.79733 1.000 44.86611  ? 56  LYS A HE2  1 
ATOM   1088 H HE3  . LYS A 1 59  ? 14.92140  24.61274 35.24556 1.000 44.86611  ? 56  LYS A HE3  1 
ATOM   1089 H HZ1  . LYS A 1 59  ? 14.35612  23.50779 37.17860 1.000 48.44321  ? 56  LYS A HZ1  1 
ATOM   1090 H HZ2  . LYS A 1 59  ? 15.70528  23.64968 37.68652 1.000 48.44321  ? 56  LYS A HZ2  1 
ATOM   1091 H HZ3  . LYS A 1 59  ? 14.87568  24.82194 37.49704 1.000 48.44321  ? 56  LYS A HZ3  1 
ATOM   1092 N N    . PHE A 1 60  ? 18.12434  19.19091 31.53780 1.000 10.26507  ? 57  PHE A N    1 
ATOM   1093 C CA   . PHE A 1 60  ? 18.54597  17.81899 31.76247 1.000 11.37082  ? 57  PHE A CA   1 
ATOM   1094 C C    . PHE A 1 60  ? 18.77332  16.95171 30.53208 1.000 9.84873   ? 57  PHE A C    1 
ATOM   1095 O O    . PHE A 1 60  ? 19.19279  15.80229 30.69474 1.000 10.79082  ? 57  PHE A O    1 
ATOM   1096 C CB   . PHE A 1 60  ? 17.54488  17.09615 32.68708 1.000 11.08707  ? 57  PHE A CB   1 
ATOM   1097 C CG   . PHE A 1 60  ? 17.38886  17.74039 34.03110 1.000 11.11150  ? 57  PHE A CG   1 
ATOM   1098 C CD1  . PHE A 1 60  ? 18.45584  17.80256 34.90963 1.000 11.36002  ? 57  PHE A CD1  1 
ATOM   1099 C CD2  . PHE A 1 60  ? 16.17799  18.28585 34.41622 1.000 12.19172  ? 57  PHE A CD2  1 
ATOM   1100 C CE1  . PHE A 1 60  ? 18.31506  18.39566 36.14587 1.000 13.11138  ? 57  PHE A CE1  1 
ATOM   1101 C CE2  . PHE A 1 60  ? 16.03323  18.87686 35.65522 1.000 12.73375  ? 57  PHE A CE2  1 
ATOM   1102 C CZ   . PHE A 1 60  ? 17.10499  18.93817 36.51511 1.000 13.26032  ? 57  PHE A CZ   1 
ATOM   1103 H H    . PHE A 1 60  ? 17.44861  19.28680 31.01455 1.000 12.31809  ? 57  PHE A H    1 
ATOM   1104 H HA   . PHE A 1 60  ? 19.41079  17.88091 32.19738 1.000 13.64498  ? 57  PHE A HA   1 
ATOM   1105 H HB2  . PHE A 1 60  ? 16.67431  17.08953 32.25933 1.000 13.30449  ? 57  PHE A HB2  1 
ATOM   1106 H HB3  . PHE A 1 60  ? 17.85187  16.18696 32.82867 1.000 13.30449  ? 57  PHE A HB3  1 
ATOM   1107 H HD1  . PHE A 1 60  ? 19.27637  17.44050 34.66357 1.000 13.63203  ? 57  PHE A HD1  1 
ATOM   1108 H HD2  . PHE A 1 60  ? 15.45332  18.25418 33.83420 1.000 14.63006  ? 57  PHE A HD2  1 
ATOM   1109 H HE1  . PHE A 1 60  ? 19.03754  18.42931 36.73050 1.000 15.73366  ? 57  PHE A HE1  1 
ATOM   1110 H HE2  . PHE A 1 60  ? 15.21225  19.23306 35.90820 1.000 15.28050  ? 57  PHE A HE2  1 
ATOM   1111 H HZ   . PHE A 1 60  ? 17.01217  19.34603 37.34573 1.000 15.91238  ? 57  PHE A HZ   1 
ATOM   1112 N N    . ARG A 1 61  ? 18.53958  17.44010 29.31616 1.000 10.52503  ? 58  ARG A N    1 
ATOM   1113 C CA   . ARG A 1 61  ? 18.67979  16.53099 28.17953 1.000 10.92362  ? 58  ARG A CA   1 
ATOM   1114 C C    . ARG A 1 61  ? 20.12069  16.04963 28.02000 1.000 9.53267   ? 58  ARG A C    1 
ATOM   1115 O O    . ARG A 1 61  ? 20.34990  14.91506 27.58687 1.000 10.75698  ? 58  ARG A O    1 
ATOM   1116 C CB   . ARG A 1 61  ? 18.12815  17.15438 26.90012 1.000 14.61528  ? 58  ARG A CB   1 
ATOM   1117 C CG   . ARG A 1 61  ? 18.94331  18.27961 26.33367 1.000 18.39334  ? 58  ARG A CG   1 
ATOM   1118 C CD   . ARG A 1 61  ? 19.75120  17.79498 25.14731 1.000 24.05838  ? 58  ARG A CD   1 
ATOM   1119 N NE   . ARG A 1 61  ? 20.52944  18.86980 24.54812 1.000 29.67674  ? 58  ARG A NE   1 
ATOM   1120 C CZ   . ARG A 1 61  ? 21.45815  18.69097 23.62018 1.000 35.62296  ? 58  ARG A CZ   1 
ATOM   1121 N NH1  . ARG A 1 61  ? 21.76670  17.48382 23.17495 1.000 37.12479  ? 58  ARG A NH1  1 
ATOM   1122 N NH2  . ARG A 1 61  ? 22.09573  19.74921 23.12884 1.000 37.27206  ? 58  ARG A NH2  1 
ATOM   1123 H H    . ARG A 1 61  ? 18.31123  18.24826 29.13085 1.000 12.63004  ? 58  ARG A H    1 
ATOM   1124 H HA   . ARG A 1 61  ? 18.13560  15.74439 28.34082 1.000 13.10835  ? 58  ARG A HA   1 
ATOM   1125 H HB2  . ARG A 1 61  ? 18.07605  16.46378 26.22096 1.000 17.53834  ? 58  ARG A HB2  1 
ATOM   1126 H HB3  . ARG A 1 61  ? 17.24262  17.50347 27.08690 1.000 17.53834  ? 58  ARG A HB3  1 
ATOM   1127 H HG2  . ARG A 1 61  ? 18.35505  18.99205 26.03824 1.000 22.07201  ? 58  ARG A HG2  1 
ATOM   1128 H HG3  . ARG A 1 61  ? 19.55402  18.61254 27.00976 1.000 22.07201  ? 58  ARG A HG3  1 
ATOM   1129 H HD2  . ARG A 1 61  ? 20.36422  17.10220 25.43915 1.000 28.87005  ? 58  ARG A HD2  1 
ATOM   1130 H HD3  . ARG A 1 61  ? 19.14955  17.44296 24.47277 1.000 28.87005  ? 58  ARG A HD3  1 
ATOM   1131 H HE   . ARG A 1 61  ? 20.37631  19.67325 24.81387 1.000 35.61209  ? 58  ARG A HE   1 
ATOM   1132 H HH11 . ARG A 1 61  ? 21.36118  16.79325 23.48842 1.000 44.54974  ? 58  ARG A HH11 1 
ATOM   1133 H HH12 . ARG A 1 61  ? 22.37276  17.38977 22.57209 1.000 44.54974  ? 58  ARG A HH12 1 
ATOM   1134 H HH21 . ARG A 1 61  ? 21.90344  20.53756 23.41367 1.000 44.72647  ? 58  ARG A HH21 1 
ATOM   1135 H HH22 . ARG A 1 61  ? 22.70042  19.64535 22.52621 1.000 44.72647  ? 58  ARG A HH22 1 
ATOM   1136 N N    . GLU A 1 62  ? 21.10022  16.87796 28.38315 1.000 11.00022  ? 59  GLU A N    1 
ATOM   1137 C CA   . GLU A 1 62  ? 22.48629  16.42197 28.36360 1.000 11.75374  ? 59  GLU A CA   1 
ATOM   1138 C C    . GLU A 1 62  ? 22.76750  15.46589 29.51717 1.000 11.69969  ? 59  GLU A C    1 
ATOM   1139 O O    . GLU A 1 62  ? 23.23913  14.34230 29.30441 1.000 12.10856  ? 59  GLU A O    1 
ATOM   1140 C CB   . GLU A 1 62  ? 23.42657  17.62747 28.39588 1.000 18.91928  ? 59  GLU A CB   1 
ATOM   1141 C CG   . GLU A 1 62  ? 23.38443  18.42458 27.09871 1.000 27.02346  ? 59  GLU A CG   1 
ATOM   1142 C CD   . GLU A 1 62  ? 24.47249  19.47160 27.00010 1.000 36.11385  ? 59  GLU A CD   1 
ATOM   1143 O OE1  . GLU A 1 62  ? 24.59026  20.30549 27.92233 1.000 39.48220  ? 59  GLU A OE1  1 
ATOM   1144 O OE2  . GLU A 1 62  ? 25.21175  19.45780 25.99358 1.000 40.25560  ? 59  GLU A OE2  1 
ATOM   1145 H H    . GLU A 1 62  ? 20.99036  17.69151 28.63940 1.000 13.20027  ? 59  GLU A H    1 
ATOM   1146 H HA   . GLU A 1 62  ? 22.65219  15.93862 27.53913 1.000 14.10448  ? 59  GLU A HA   1 
ATOM   1147 H HB2  . GLU A 1 62  ? 23.16456  18.21562 29.12136 1.000 22.70314  ? 59  GLU A HB2  1 
ATOM   1148 H HB3  . GLU A 1 62  ? 24.33576  17.31788 28.53165 1.000 22.70314  ? 59  GLU A HB3  1 
ATOM   1149 H HG2  . GLU A 1 62  ? 23.49082  17.81440 26.35221 1.000 32.42815  ? 59  GLU A HG2  1 
ATOM   1150 H HG3  . GLU A 1 62  ? 22.52924  18.87818 27.03714 1.000 32.42815  ? 59  GLU A HG3  1 
ATOM   1151 N N    . SER A 1 63  ? 22.44787  15.88540 30.74291 1.000 10.77980  ? 60  SER A N    1 
ATOM   1152 C CA   A SER A 1 63  ? 22.79740  15.09252 31.91716 0.647 10.59361  ? 60  SER A CA   1 
ATOM   1153 C CA   B SER A 1 63  ? 22.78816  15.09701 31.92073 0.353 10.76361  ? 60  SER A CA   1 
ATOM   1154 C C    . SER A 1 63  ? 22.05950  13.76035 31.95229 1.000 10.03335  ? 60  SER A C    1 
ATOM   1155 O O    . SER A 1 63  ? 22.57572  12.78843 32.51668 1.000 11.99988  ? 60  SER A O    1 
ATOM   1156 C CB   A SER A 1 63  ? 22.49440  15.87886 33.19438 0.647 11.89361  ? 60  SER A CB   1 
ATOM   1157 C CB   B SER A 1 63  ? 22.44562  15.91180 33.16564 0.353 12.38361  ? 60  SER A CB   1 
ATOM   1158 O OG   A SER A 1 63  ? 21.10275  16.11565 33.33494 0.647 14.35361  ? 60  SER A OG   1 
ATOM   1159 O OG   B SER A 1 63  ? 22.73537  15.18480 34.33428 0.353 16.06361  ? 60  SER A OG   1 
ATOM   1160 H H    A SER A 1 63  ? 22.03302  16.61791 30.91875 0.647 12.93576  ? 60  SER A H    1 
ATOM   1161 H H    B SER A 1 63  ? 22.03576  16.61989 30.91694 0.353 12.93576  ? 60  SER A H    1 
ATOM   1162 H HA   A SER A 1 63  ? 23.74948  14.91009 31.88308 0.647 12.71233  ? 60  SER A HA   1 
ATOM   1163 H HA   B SER A 1 63  ? 23.73861  14.90347 31.91175 0.353 12.91633  ? 60  SER A HA   1 
ATOM   1164 H HB2  A SER A 1 63  ? 22.80488  15.36842 33.95855 0.647 14.27233  ? 60  SER A HB2  1 
ATOM   1165 H HB2  B SER A 1 63  ? 22.96997  16.72786 33.16317 0.353 14.86033  ? 60  SER A HB2  1 
ATOM   1166 H HB3  A SER A 1 63  ? 22.95564  16.73128 33.15524 0.647 14.27233  ? 60  SER A HB3  1 
ATOM   1167 H HB3  B SER A 1 63  ? 21.49950  16.12533 33.15292 0.353 14.86033  ? 60  SER A HB3  1 
ATOM   1168 H HG   A SER A 1 63  ? 20.80456  16.49314 32.64632 0.647 17.22433  ? 60  SER A HG   1 
ATOM   1169 H HG   B SER A 1 63  ? 22.17193  14.57041 34.43754 0.353 19.27633  ? 60  SER A HG   1 
ATOM   1170 N N    . LYS A 1 64  ? 20.86185  13.69048 31.37500 1.000 9.64300   ? 61  LYS A N    1 
ATOM   1171 C CA   . LYS A 1 64  ? 20.07366  12.46419 31.36945 1.000 11.42584  ? 61  LYS A CA   1 
ATOM   1172 C C    . LYS A 1 64  ? 20.06406  11.77653 30.01024 1.000 10.69106  ? 61  LYS A C    1 
ATOM   1173 O O    . LYS A 1 64  ? 19.33854  10.79288 29.82986 1.000 12.76008  ? 61  LYS A O    1 
ATOM   1174 C CB   . LYS A 1 64  ? 18.64563  12.74042 31.83969 1.000 12.01128  ? 61  LYS A CB   1 
ATOM   1175 C CG   . LYS A 1 64  ? 18.56931  13.16927 33.29687 1.000 13.50505  ? 61  LYS A CG   1 
ATOM   1176 C CD   . LYS A 1 64  ? 17.14148  13.19054 33.80069 1.000 14.95898  ? 61  LYS A CD   1 
ATOM   1177 C CE   . LYS A 1 64  ? 17.06634  13.63474 35.24813 1.000 15.32352  ? 61  LYS A CE   1 
ATOM   1178 N NZ   . LYS A 1 64  ? 17.70434  12.65932 36.17676 1.000 16.99398  ? 61  LYS A NZ   1 
ATOM   1179 H H    . LYS A 1 64  ? 20.48110  14.34991 30.97527 1.000 11.57160  ? 61  LYS A H    1 
ATOM   1180 H HA   . LYS A 1 64  ? 20.47196  11.84683 32.00279 1.000 13.71101  ? 61  LYS A HA   1 
ATOM   1181 H HB2  . LYS A 1 64  ? 18.26866  13.45181 31.29865 1.000 14.41353  ? 61  LYS A HB2  1 
ATOM   1182 H HB3  . LYS A 1 64  ? 18.11937  11.93194 31.73812 1.000 14.41353  ? 61  LYS A HB3  1 
ATOM   1183 H HG2  . LYS A 1 64  ? 19.07449  12.54542 33.84141 1.000 16.20606  ? 61  LYS A HG2  1 
ATOM   1184 H HG3  . LYS A 1 64  ? 18.93703  14.06225 33.38780 1.000 16.20606  ? 61  LYS A HG3  1 
ATOM   1185 H HD2  . LYS A 1 64  ? 16.62142  13.80975 33.26494 1.000 17.95078  ? 61  LYS A HD2  1 
ATOM   1186 H HD3  . LYS A 1 64  ? 16.76515  12.29886 33.73607 1.000 17.95078  ? 61  LYS A HD3  1 
ATOM   1187 H HE2  . LYS A 1 64  ? 17.52390  14.48471 35.34353 1.000 18.38822  ? 61  LYS A HE2  1 
ATOM   1188 H HE3  . LYS A 1 64  ? 16.13527  13.72869 35.50345 1.000 18.38822  ? 61  LYS A HE3  1 
ATOM   1189 H HZ1  . LYS A 1 64  ? 18.58622  12.65690 36.05683 1.000 20.39278  ? 61  LYS A HZ1  1 
ATOM   1190 H HZ2  . LYS A 1 64  ? 17.52816  12.88204 37.02024 1.000 20.39278  ? 61  LYS A HZ2  1 
ATOM   1191 H HZ3  . LYS A 1 64  ? 17.38959  11.84130 36.02225 1.000 20.39278  ? 61  LYS A HZ3  1 
ATOM   1192 N N    . ASN A 1 65  ? 20.83488  12.28637 29.04874 1.000 9.29512   ? 62  ASN A N    1 
ATOM   1193 C CA   . ASN A 1 65  ? 21.09584  11.61261 27.77644 1.000 9.31100   ? 62  ASN A CA   1 
ATOM   1194 C C    . ASN A 1 65  ? 19.80312  11.25374 27.04177 1.000 8.98198   ? 62  ASN A C    1 
ATOM   1195 O O    . ASN A 1 65  ? 19.55492  10.09936 26.68928 1.000 10.61554  ? 62  ASN A O    1 
ATOM   1196 C CB   . ASN A 1 65  ? 21.97959  10.37915 27.99824 1.000 11.40153  ? 62  ASN A CB   1 
ATOM   1197 C CG   . ASN A 1 65  ? 22.68147  9.93179  26.73977 1.000 14.01064  ? 62  ASN A CG   1 
ATOM   1198 O OD1  . ASN A 1 65  ? 22.67061  8.75156  26.39491 1.000 18.33504  ? 62  ASN A OD1  1 
ATOM   1199 N ND2  . ASN A 1 65  ? 23.29655  10.87666 26.04095 1.000 13.23396  ? 62  ASN A ND2  1 
ATOM   1200 H H    . ASN A 1 65  ? 21.23105  13.04703 29.11237 1.000 11.15415  ? 62  ASN A H    1 
ATOM   1201 H HA   . ASN A 1 65  ? 21.57085  12.23233 27.20092 1.000 11.17320  ? 62  ASN A HA   1 
ATOM   1202 H HB2  . ASN A 1 65  ? 22.65621  10.58978 28.66061 1.000 13.68183  ? 62  ASN A HB2  1 
ATOM   1203 H HB3  . ASN A 1 65  ? 21.42666  9.64586  28.31040 1.000 13.68183  ? 62  ASN A HB3  1 
ATOM   1204 H HD21 . ASN A 1 65  ? 23.71150  10.67368 25.31554 1.000 15.88075  ? 62  ASN A HD21 1 
ATOM   1205 H HD22 . ASN A 1 65  ? 23.28039  11.69224 26.31328 1.000 15.88075  ? 62  ASN A HD22 1 
ATOM   1206 N N    . PHE A 1 66  ? 18.98472  12.27033 26.78790 1.000 8.61590   ? 63  PHE A N    1 
ATOM   1207 C CA   . PHE A 1 66  ? 17.74394  12.05603 26.05973 1.000 8.17217   ? 63  PHE A CA   1 
ATOM   1208 C C    . PHE A 1 66  ? 17.55631  13.10732 24.97669 1.000 8.22454   ? 63  PHE A C    1 
ATOM   1209 O O    . PHE A 1 66  ? 18.22030  14.14700 24.94937 1.000 9.68752   ? 63  PHE A O    1 
ATOM   1210 C CB   . PHE A 1 66  ? 16.50116  11.93560 26.98524 1.000 8.41613   ? 63  PHE A CB   1 
ATOM   1211 C CG   . PHE A 1 66  ? 16.04879  13.22755 27.62986 1.000 9.53227   ? 63  PHE A CG   1 
ATOM   1212 C CD1  . PHE A 1 66  ? 16.51880  13.60105 28.87718 1.000 11.90070  ? 63  PHE A CD1  1 
ATOM   1213 C CD2  . PHE A 1 66  ? 15.09603  14.02702 27.01924 1.000 11.01164  ? 63  PHE A CD2  1 
ATOM   1214 C CE1  . PHE A 1 66  ? 16.07773  14.76918 29.48017 1.000 12.09787  ? 63  PHE A CE1  1 
ATOM   1215 C CE2  . PHE A 1 66  ? 14.66059  15.19504 27.61593 1.000 12.99082  ? 63  PHE A CE2  1 
ATOM   1216 C CZ   . PHE A 1 66  ? 15.15163  15.56466 28.84689 1.000 12.53516  ? 63  PHE A CZ   1 
ATOM   1217 H H    . PHE A 1 66  ? 19.12725  13.08436 27.02590 1.000 10.33909  ? 63  PHE A H    1 
ATOM   1218 H HA   . PHE A 1 66  ? 17.81250  11.20634 25.59689 1.000 9.80661   ? 63  PHE A HA   1 
ATOM   1219 H HB2  . PHE A 1 66  ? 15.75906  11.59914 26.45895 1.000 10.09936  ? 63  PHE A HB2  1 
ATOM   1220 H HB3  . PHE A 1 66  ? 16.71048  11.31339 27.69933 1.000 10.09936  ? 63  PHE A HB3  1 
ATOM   1221 H HD1  . PHE A 1 66  ? 17.13733  13.06247 29.31566 1.000 14.28084  ? 63  PHE A HD1  1 
ATOM   1222 H HD2  . PHE A 1 66  ? 14.74458  13.77406 26.19620 1.000 13.21397  ? 63  PHE A HD2  1 
ATOM   1223 H HE1  . PHE A 1 66  ? 16.40854  15.01505 30.31385 1.000 14.51745  ? 63  PHE A HE1  1 
ATOM   1224 H HE2  . PHE A 1 66  ? 14.03509  15.73168 27.18504 1.000 15.58898  ? 63  PHE A HE2  1 
ATOM   1225 H HZ   . PHE A 1 66  ? 14.85821  16.34999 29.24947 1.000 15.04219  ? 63  PHE A HZ   1 
ATOM   1226 N N    . GLU A 1 67  ? 16.64013  12.79231 24.06737 1.000 8.69457   ? 64  GLU A N    1 
ATOM   1227 C CA   . GLU A 1 67  ? 16.25343  13.66373 22.97184 1.000 8.79644   ? 64  GLU A CA   1 
ATOM   1228 C C    . GLU A 1 67  ? 14.73571  13.63311 22.88226 1.000 8.83456   ? 64  GLU A C    1 
ATOM   1229 O O    . GLU A 1 67  ? 14.09316  12.67480 23.32264 1.000 9.15322   ? 64  GLU A O    1 
ATOM   1230 C CB   . GLU A 1 67  ? 16.87244  13.18796 21.64806 1.000 10.32572  ? 64  GLU A CB   1 
ATOM   1231 C CG   . GLU A 1 67  ? 16.65235  14.11597 20.45828 1.000 11.31507  ? 64  GLU A CG   1 
ATOM   1232 C CD   . GLU A 1 67  ? 17.13871  15.52173 20.72127 1.000 11.64419  ? 64  GLU A CD   1 
ATOM   1233 O OE1  . GLU A 1 67  ? 16.35476  16.32091 21.27301 1.000 11.39010  ? 64  GLU A OE1  1 
ATOM   1234 O OE2  . GLU A 1 67  ? 18.30448  15.82375 20.38922 1.000 14.07534  ? 64  GLU A OE2  1 
ATOM   1235 H H    . GLU A 1 67  ? 16.21162  12.04667 24.06605 1.000 10.43349  ? 64  GLU A H    1 
ATOM   1236 H HA   . GLU A 1 67  ? 16.54520  14.57574 23.12681 1.000 10.55572  ? 64  GLU A HA   1 
ATOM   1237 H HB2  . GLU A 1 67  ? 17.83022  13.09825 21.77264 1.000 12.39087  ? 64  GLU A HB2  1 
ATOM   1238 H HB3  . GLU A 1 67  ? 16.48549  12.32805 21.42064 1.000 12.39087  ? 64  GLU A HB3  1 
ATOM   1239 H HG2  . GLU A 1 67  ? 17.13573  13.76896 19.69223 1.000 13.57808  ? 64  GLU A HG2  1 
ATOM   1240 H HG3  . GLU A 1 67  ? 15.70363  14.15808 20.26065 1.000 13.57808  ? 64  GLU A HG3  1 
ATOM   1241 N N    . VAL A 1 68  ? 14.16646  14.70503 22.33951 1.000 8.28917   ? 65  VAL A N    1 
ATOM   1242 C CA   . VAL A 1 68  ? 12.73596  14.79756 22.08072 1.000 7.86383   ? 65  VAL A CA   1 
ATOM   1243 C C    . VAL A 1 68  ? 12.52760  14.94201 20.58073 1.000 7.65771   ? 65  VAL A C    1 
ATOM   1244 O O    . VAL A 1 68  ? 13.21908  15.72416 19.91854 1.000 8.56435   ? 65  VAL A O    1 
ATOM   1245 C CB   . VAL A 1 68  ? 12.09498  15.97819 22.83855 1.000 7.91212   ? 65  VAL A CB   1 
ATOM   1246 C CG1  . VAL A 1 68  ? 10.64204  16.15318 22.42439 1.000 8.58086   ? 65  VAL A CG1  1 
ATOM   1247 C CG2  . VAL A 1 68  ? 12.19495  15.75445 24.34235 1.000 10.13503  ? 65  VAL A CG2  1 
ATOM   1248 H H    . VAL A 1 68  ? 14.60152  15.40948 22.10698 1.000 9.94700   ? 65  VAL A H    1 
ATOM   1249 H HA   . VAL A 1 68  ? 12.30322  13.98048 22.37399 1.000 9.43660   ? 65  VAL A HA   1 
ATOM   1250 H HB   . VAL A 1 68  ? 12.57303  16.79217 22.61540 1.000 9.49455   ? 65  VAL A HB   1 
ATOM   1251 H HG11 . VAL A 1 68  ? 10.24597  16.86279 22.95399 1.000 10.29703  ? 65  VAL A HG11 1 
ATOM   1252 H HG12 . VAL A 1 68  ? 10.60767  16.38444 21.48298 1.000 10.29703  ? 65  VAL A HG12 1 
ATOM   1253 H HG13 . VAL A 1 68  ? 10.16743  15.32132 22.57820 1.000 10.29703  ? 65  VAL A HG13 1 
ATOM   1254 H HG21 . VAL A 1 68  ? 11.94283  16.57136 24.80062 1.000 12.16204  ? 65  VAL A HG21 1 
ATOM   1255 H HG22 . VAL A 1 68  ? 11.59557  15.03490 24.59511 1.000 12.16204  ? 65  VAL A HG22 1 
ATOM   1256 H HG23 . VAL A 1 68  ? 13.10862  15.51798 24.56640 1.000 12.16204  ? 65  VAL A HG23 1 
ATOM   1257 N N    . VAL A 1 69  ? 11.56422  14.19335 20.05225 1.000 8.57342   ? 66  VAL A N    1 
ATOM   1258 C CA   . VAL A 1 69  ? 11.20440  14.23620 18.64135 1.000 8.65593   ? 66  VAL A CA   1 
ATOM   1259 C C    . VAL A 1 69  ? 9.72198   14.56277 18.56349 1.000 7.64370   ? 66  VAL A C    1 
ATOM   1260 O O    . VAL A 1 69  ? 8.87574   13.74610 18.95069 1.000 8.01321   ? 66  VAL A O    1 
ATOM   1261 C CB   . VAL A 1 69  ? 11.51752  12.91521 17.92820 1.000 8.44735   ? 66  VAL A CB   1 
ATOM   1262 C CG1  . VAL A 1 69  ? 11.05028  12.96710 16.48147 1.000 9.74152   ? 66  VAL A CG1  1 
ATOM   1263 C CG2  . VAL A 1 69  ? 13.00752  12.62917 18.00891 1.000 8.98268   ? 66  VAL A CG2  1 
ATOM   1264 H H    . VAL A 1 69  ? 11.09164  13.63652 20.50635 1.000 10.28810  ? 66  VAL A H    1 
ATOM   1265 H HA   . VAL A 1 69  ? 11.69920  14.94566 18.20233 1.000 10.38712  ? 66  VAL A HA   1 
ATOM   1266 H HB   . VAL A 1 69  ? 11.04227  12.19093 18.36461 1.000 10.13682  ? 66  VAL A HB   1 
ATOM   1267 H HG11 . VAL A 1 69  ? 11.34203  12.16173 16.02631 1.000 11.68982  ? 66  VAL A HG11 1 
ATOM   1268 H HG12 . VAL A 1 69  ? 10.08214  13.02458 16.46415 1.000 11.68982  ? 66  VAL A HG12 1 
ATOM   1269 H HG13 . VAL A 1 69  ? 11.43569  13.74730 16.05293 1.000 11.68982  ? 66  VAL A HG13 1 
ATOM   1270 H HG21 . VAL A 1 69  ? 13.17105  11.72004 17.71287 1.000 10.77922  ? 66  VAL A HG21 1 
ATOM   1271 H HG22 . VAL A 1 69  ? 13.48040  13.25350 17.43663 1.000 10.77922  ? 66  VAL A HG22 1 
ATOM   1272 H HG23 . VAL A 1 69  ? 13.30022  12.73562 18.92755 1.000 10.77922  ? 66  VAL A HG23 1 
ATOM   1273 N N    . LEU A 1 70  ? 9.40848   15.75494 18.06567 1.000 7.62348   ? 67  LEU A N    1 
ATOM   1274 C CA   . LEU A 1 70  ? 8.02393   16.14711 17.85682 1.000 7.59463   ? 67  LEU A CA   1 
ATOM   1275 C C    . LEU A 1 70  ? 7.38995   15.30347 16.75917 1.000 7.35758   ? 67  LEU A C    1 
ATOM   1276 O O    . LEU A 1 70  ? 7.94531   15.16316 15.66374 1.000 7.77618   ? 67  LEU A O    1 
ATOM   1277 C CB   . LEU A 1 70  ? 7.96132   17.62215 17.47103 1.000 9.17115   ? 67  LEU A CB   1 
ATOM   1278 C CG   . LEU A 1 70  ? 6.58289   18.18806 17.12607 1.000 8.69066   ? 67  LEU A CG   1 
ATOM   1279 C CD1  . LEU A 1 70  ? 5.68443   18.25507 18.35446 1.000 11.45074  ? 67  LEU A CD1  1 
ATOM   1280 C CD2  . LEU A 1 70  ? 6.73887   19.55895 16.48678 1.000 9.86439   ? 67  LEU A CD2  1 
ATOM   1281 H H    . LEU A 1 70  ? 9.98177   16.35522 17.84073 1.000 9.14817   ? 67  LEU A H    1 
ATOM   1282 H HA   . LEU A 1 70  ? 7.52347   16.01003 18.67637 1.000 9.11356   ? 67  LEU A HA   1 
ATOM   1283 H HB2  . LEU A 1 70  ? 8.30238   18.14092 18.21632 1.000 11.00538  ? 67  LEU A HB2  1 
ATOM   1284 H HB3  . LEU A 1 70  ? 8.52408   17.75155 16.69164 1.000 11.00538  ? 67  LEU A HB3  1 
ATOM   1285 H HG   . LEU A 1 70  ? 6.14596   17.59778 16.49238 1.000 10.42879  ? 67  LEU A HG   1 
ATOM   1286 H HD11 . LEU A 1 70  ? 4.85851   18.70517 18.11746 1.000 13.74089  ? 67  LEU A HD11 1 
ATOM   1287 H HD12 . LEU A 1 70  ? 5.49466   17.35304 18.65650 1.000 13.74089  ? 67  LEU A HD12 1 
ATOM   1288 H HD13 . LEU A 1 70  ? 6.14135   18.74867 19.05338 1.000 13.74089  ? 67  LEU A HD13 1 
ATOM   1289 H HD21 . LEU A 1 70  ? 5.85896   19.92686 16.30985 1.000 11.83727  ? 67  LEU A HD21 1 
ATOM   1290 H HD22 . LEU A 1 70  ? 7.22323   20.13812 17.09576 1.000 11.83727  ? 67  LEU A HD22 1 
ATOM   1291 H HD23 . LEU A 1 70  ? 7.23160   19.46597 15.65644 1.000 11.83727  ? 67  LEU A HD23 1 
ATOM   1292 N N    . VAL A 1 71  ? 6.22123   14.74462 17.07376 1.000 8.14918   ? 68  VAL A N    1 
ATOM   1293 C CA   . VAL A 1 71  ? 5.35701   14.03005 16.13971 1.000 8.12705   ? 68  VAL A CA   1 
ATOM   1294 C C    . VAL A 1 71  ? 4.10484   14.89140 16.00881 1.000 7.45317   ? 68  VAL A C    1 
ATOM   1295 O O    . VAL A 1 71  ? 3.21505   14.85854 16.86751 1.000 9.17954   ? 68  VAL A O    1 
ATOM   1296 C CB   . VAL A 1 71  ? 5.03138   12.61741 16.64060 1.000 7.39489   ? 68  VAL A CB   1 
ATOM   1297 C CG1  . VAL A 1 71  ? 4.27288   11.82513 15.57968 1.000 9.97065   ? 68  VAL A CG1  1 
ATOM   1298 C CG2  . VAL A 1 71  ? 6.30791   11.88784 17.06042 1.000 8.95792   ? 68  VAL A CG2  1 
ATOM   1299 H H    . VAL A 1 71  ? 5.89100   14.76876 17.86746 1.000 9.77902   ? 68  VAL A H    1 
ATOM   1300 H HA   . VAL A 1 71  ? 5.78062   13.94888 15.27087 1.000 9.75246   ? 68  VAL A HA   1 
ATOM   1301 H HB   . VAL A 1 71  ? 4.45804   12.68916 17.41972 1.000 8.87387   ? 68  VAL A HB   1 
ATOM   1302 H HG11 . VAL A 1 71  ? 3.92131   11.01532 15.98155 1.000 11.96478  ? 68  VAL A HG11 1 
ATOM   1303 H HG12 . VAL A 1 71  ? 3.54492   12.36877 15.23992 1.000 11.96478  ? 68  VAL A HG12 1 
ATOM   1304 H HG13 . VAL A 1 71  ? 4.88149   11.59942 14.85888 1.000 11.96478  ? 68  VAL A HG13 1 
ATOM   1305 H HG21 . VAL A 1 71  ? 6.08532   10.97483 17.30080 1.000 10.74950  ? 68  VAL A HG21 1 
ATOM   1306 H HG22 . VAL A 1 71  ? 6.93242   11.89160 16.31821 1.000 10.74950  ? 68  VAL A HG22 1 
ATOM   1307 H HG23 . VAL A 1 71  ? 6.69691   12.34504 17.82235 1.000 10.74950  ? 68  VAL A HG23 1 
ATOM   1308 N N    . THR A 1 72  ? 4.03928   15.69070 14.94774 1.000 7.50568   ? 69  THR A N    1 
ATOM   1309 C CA   . THR A 1 72  ? 3.03774   16.74308 14.86738 1.000 5.99864   ? 69  THR A CA   1 
ATOM   1310 C C    . THR A 1 72  ? 1.67250   16.20622 14.46236 1.000 7.00277   ? 69  THR A C    1 
ATOM   1311 O O    . THR A 1 72  ? 1.55779   15.35159 13.57921 1.000 7.92782   ? 69  THR A O    1 
ATOM   1312 C CB   . THR A 1 72  ? 3.46766   17.82167 13.86531 1.000 6.41763   ? 69  THR A CB   1 
ATOM   1313 O OG1  . THR A 1 72  ? 2.54880   18.92083 13.92487 1.000 8.75972   ? 69  THR A OG1  1 
ATOM   1314 C CG2  . THR A 1 72  ? 3.49715   17.28350 12.42678 1.000 7.50459   ? 69  THR A CG2  1 
ATOM   1315 H H    . THR A 1 72  ? 4.56139   15.64264 14.26606 1.000 9.00682   ? 69  THR A H    1 
ATOM   1316 H HA   . THR A 1 72  ? 2.95220   17.13900 15.74877 1.000 7.19837   ? 69  THR A HA   1 
ATOM   1317 H HB   . THR A 1 72  ? 4.36360   18.11523 14.09338 1.000 7.70116   ? 69  THR A HB   1 
ATOM   1318 H HG1  . THR A 1 72  ? 2.41796   19.14291 14.72434 1.000 10.51167  ? 69  THR A HG1  1 
ATOM   1319 H HG21 . THR A 1 72  ? 3.86288   17.95424 11.82907 1.000 9.00551   ? 69  THR A HG21 1 
ATOM   1320 H HG22 . THR A 1 72  ? 4.04913   16.48714 12.38174 1.000 9.00551   ? 69  THR A HG22 1 
ATOM   1321 H HG23 . THR A 1 72  ? 2.59855   17.06046 12.13753 1.000 9.00551   ? 69  THR A HG23 1 
ATOM   1322 N N    . TRP A 1 73  ? 0.63564   16.72103 15.12281 1.000 8.14795   ? 70  TRP A N    1 
ATOM   1323 C CA   . TRP A 1 73  ? -0.74168  16.58692 14.67146 1.000 8.93942   ? 70  TRP A CA   1 
ATOM   1324 C C    . TRP A 1 73  ? -1.25874  17.87794 14.03901 1.000 9.57086   ? 70  TRP A C    1 
ATOM   1325 O O    . TRP A 1 73  ? -2.46588  18.01401 13.82120 1.000 10.18262  ? 70  TRP A O    1 
ATOM   1326 C CB   . TRP A 1 73  ? -1.64818  16.13988 15.82189 1.000 8.98695   ? 70  TRP A CB   1 
ATOM   1327 C CG   . TRP A 1 73  ? -1.46652  14.69893 16.23699 1.000 7.68473   ? 70  TRP A CG   1 
ATOM   1328 C CD1  . TRP A 1 73  ? -0.45136  13.86224 15.87835 1.000 9.48402   ? 70  TRP A CD1  1 
ATOM   1329 C CD2  . TRP A 1 73  ? -2.33122  13.93448 17.09121 1.000 6.50086   ? 70  TRP A CD2  1 
ATOM   1330 N NE1  . TRP A 1 73  ? -0.63012  12.62640 16.45268 1.000 9.43393   ? 70  TRP A NE1  1 
ATOM   1331 C CE2  . TRP A 1 73  ? -1.77513  12.64637 17.20433 1.000 7.61084   ? 70  TRP A CE2  1 
ATOM   1332 C CE3  . TRP A 1 73  ? -3.52636  14.21212 17.76259 1.000 8.49980   ? 70  TRP A CE3  1 
ATOM   1333 C CZ2  . TRP A 1 73  ? -2.37073  11.63986 17.96176 1.000 8.91752   ? 70  TRP A CZ2  1 
ATOM   1334 C CZ3  . TRP A 1 73  ? -4.11051  13.21200 18.52406 1.000 8.66013   ? 70  TRP A CZ3  1 
ATOM   1335 C CH2  . TRP A 1 73  ? -3.52946  11.94599 18.62064 1.000 9.51934   ? 70  TRP A CH2  1 
ATOM   1336 H H    . TRP A 1 73  ? 0.71056   17.16449 15.85584 1.000 9.77754   ? 70  TRP A H    1 
ATOM   1337 H HA   . TRP A 1 73  ? -0.78641  15.88823 14.00009 1.000 10.72730  ? 70  TRP A HA   1 
ATOM   1338 H HB2  . TRP A 1 73  ? -1.46132  16.69366 16.59604 1.000 10.78434  ? 70  TRP A HB2  1 
ATOM   1339 H HB3  . TRP A 1 73  ? -2.57224  16.25200 15.54905 1.000 10.78434  ? 70  TRP A HB3  1 
ATOM   1340 H HD1  . TRP A 1 73  ? 0.25927   14.09426 15.32511 1.000 11.38082  ? 70  TRP A HD1  1 
ATOM   1341 H HE1  . TRP A 1 73  ? -0.10774  11.95014 16.35582 1.000 11.32071  ? 70  TRP A HE1  1 
ATOM   1342 H HE3  . TRP A 1 73  ? -3.92153  15.05161 17.69932 1.000 10.19977  ? 70  TRP A HE3  1 
ATOM   1343 H HZ2  . TRP A 1 73  ? -1.99426  10.79128 18.01721 1.000 10.70102  ? 70  TRP A HZ2  1 
ATOM   1344 H HZ3  . TRP A 1 73  ? -4.90287  13.38716 18.97834 1.000 10.39216  ? 70  TRP A HZ3  1 
ATOM   1345 H HH2  . TRP A 1 73  ? -3.93958  11.29638 19.14477 1.000 11.42321  ? 70  TRP A HH2  1 
ATOM   1346 N N    . ASP A 1 74  ? -0.37516  18.82741 13.74386 1.000 9.01451   ? 71  ASP A N    1 
ATOM   1347 C CA   . ASP A 1 74  ? -0.74504  19.96657 12.91821 1.000 8.90155   ? 71  ASP A CA   1 
ATOM   1348 C C    . ASP A 1 74  ? -0.81575  19.52498 11.46252 1.000 9.20857   ? 71  ASP A C    1 
ATOM   1349 O O    . ASP A 1 74  ? -0.01541  18.69913 11.01252 1.000 11.84886  ? 71  ASP A O    1 
ATOM   1350 C CB   . ASP A 1 74  ? 0.29602   21.07468 13.05467 1.000 9.79356   ? 71  ASP A CB   1 
ATOM   1351 C CG   . ASP A 1 74  ? 0.06460   21.94659 14.26471 1.000 10.40194  ? 71  ASP A CG   1 
ATOM   1352 O OD1  . ASP A 1 74  ? -0.93764  22.68899 14.27683 1.000 10.87230  ? 71  ASP A OD1  1 
ATOM   1353 O OD2  . ASP A 1 74  ? 0.89378   21.89746 15.19541 1.000 11.03405  ? 71  ASP A OD2  1 
ATOM   1354 H H    . ASP A 1 74  ? 0.44259   18.83299 14.01006 1.000 10.81741  ? 71  ASP A H    1 
ATOM   1355 H HA   . ASP A 1 74  ? -1.60599  20.31619 13.19649 1.000 10.68186  ? 71  ASP A HA   1 
ATOM   1356 H HB2  . ASP A 1 74  ? 1.17545   20.67385 13.13744 1.000 11.75228  ? 71  ASP A HB2  1 
ATOM   1357 H HB3  . ASP A 1 74  ? 0.26169   21.63953 12.26685 1.000 11.75228  ? 71  ASP A HB3  1 
ATOM   1358 N N    . ASP A 1 75  ? -1.78992  20.06201 10.72658 1.000 10.25687  ? 72  ASP A N    1 
ATOM   1359 C CA   . ASP A 1 75  ? -1.88411  19.80600 9.29331  1.000 9.80108   ? 72  ASP A CA   1 
ATOM   1360 C C    . ASP A 1 75  ? -1.72020  21.07235 8.45807  1.000 10.81636  ? 72  ASP A C    1 
ATOM   1361 O O    . ASP A 1 75  ? -1.89860  21.02308 7.23509  1.000 13.54577  ? 72  ASP A O    1 
ATOM   1362 C CB   . ASP A 1 75  ? -3.17389  19.06385 8.92289  1.000 11.64222  ? 72  ASP A CB   1 
ATOM   1363 C CG   . ASP A 1 75  ? -4.39287  19.95792 8.92824  1.000 11.95555  ? 72  ASP A CG   1 
ATOM   1364 O OD1  . ASP A 1 75  ? -4.44716  20.89474 9.75055  1.000 13.02637  ? 72  ASP A OD1  1 
ATOM   1365 O OD2  . ASP A 1 75  ? -5.30472  19.71497 8.10996  1.000 12.29024  ? 72  ASP A OD2  1 
ATOM   1366 H H    . ASP A 1 75  ? -2.40559  20.57654 11.03610 1.000 12.30824  ? 72  ASP A H    1 
ATOM   1367 H HA   . ASP A 1 75  ? -1.15893  19.20717 9.05582  1.000 11.76129  ? 72  ASP A HA   1 
ATOM   1368 H HB2  . ASP A 1 75  ? -3.07917  18.69310 8.03156  1.000 13.97066  ? 72  ASP A HB2  1 
ATOM   1369 H HB3  . ASP A 1 75  ? -3.32290  18.35164 9.56434  1.000 13.97066  ? 72  ASP A HB3  1 
ATOM   1370 N N    . GLU A 1 76  ? -1.37153  22.19823 9.07526  1.000 11.97698  ? 73  GLU A N    1 
ATOM   1371 C CA   A GLU A 1 76  ? -1.06886  23.42911 8.35372  0.368 15.92707  ? 73  GLU A CA   1 
ATOM   1372 C CA   B GLU A 1 76  ? -1.06882  23.43161 8.35934  0.632 15.92707  ? 73  GLU A CA   1 
ATOM   1373 C C    . GLU A 1 76  ? 0.37169   23.82058 8.65305  1.000 13.42988  ? 73  GLU A C    1 
ATOM   1374 O O    . GLU A 1 76  ? 0.77821   23.89072 9.81859  1.000 11.11973  ? 73  GLU A O    1 
ATOM   1375 C CB   A GLU A 1 76  ? -2.05918  24.54612 8.69861  0.368 24.49652  ? 73  GLU A CB   1 
ATOM   1376 C CB   B GLU A 1 76  ? -2.02731  24.54996 8.77214  0.632 24.49652  ? 73  GLU A CB   1 
ATOM   1377 C CG   A GLU A 1 76  ? -1.96773  25.06149 10.10553 0.368 33.83448  ? 73  GLU A CG   1 
ATOM   1378 C CG   B GLU A 1 76  ? -2.13516  25.66644 7.74743  0.632 33.83448  ? 73  GLU A CG   1 
ATOM   1379 C CD   A GLU A 1 76  ? -3.25514  25.70965 10.57466 0.368 41.16957  ? 73  GLU A CD   1 
ATOM   1380 C CD   B GLU A 1 76  ? -0.93440  26.58933 7.76218  0.632 41.16957  ? 73  GLU A CD   1 
ATOM   1381 O OE1  A GLU A 1 76  ? -3.56081  26.83326 10.12413 0.368 45.62537  ? 73  GLU A OE1  1 
ATOM   1382 O OE1  B GLU A 1 76  ? -0.59417  27.09951 8.85012  0.632 45.62537  ? 73  GLU A OE1  1 
ATOM   1383 O OE2  A GLU A 1 76  ? -3.96667  25.08604 11.39154 0.368 42.29076  ? 73  GLU A OE2  1 
ATOM   1384 O OE2  B GLU A 1 76  ? -0.32631  26.79806 6.69097  0.632 42.29076  ? 73  GLU A OE2  1 
ATOM   1385 H H    . GLU A 1 76  ? -1.30304  22.26951 9.92956  1.000 14.37238  ? 73  GLU A H    1 
ATOM   1386 H HA   . GLU A 1 76  ? -1.14336  23.28787 7.39696  1.000 19.11249  ? 73  GLU A HA   1 
ATOM   1387 H HB2  A GLU A 1 76  ? -1.89729  25.29470 8.10337  0.368 29.39582  ? 73  GLU A HB2  1 
ATOM   1388 H HB2  B GLU A 1 76  ? -2.91266  24.17324 8.89517  0.632 29.39582  ? 73  GLU A HB2  1 
ATOM   1389 H HB3  A GLU A 1 76  ? -2.95953  24.20881 8.57019  0.368 29.39582  ? 73  GLU A HB3  1 
ATOM   1390 H HB3  B GLU A 1 76  ? -1.71392  24.93917 9.60353  0.632 29.39582  ? 73  GLU A HB3  1 
ATOM   1391 H HG2  A GLU A 1 76  ? -1.76927  24.32209 10.70118 0.368 40.60138  ? 73  GLU A HG2  1 
ATOM   1392 H HG2  B GLU A 1 76  ? -2.20423  25.27744 6.86153  0.632 40.60138  ? 73  GLU A HG2  1 
ATOM   1393 H HG3  A GLU A 1 76  ? -1.26213  25.72531 10.15420 0.368 40.60138  ? 73  GLU A HG3  1 
ATOM   1394 H HG3  B GLU A 1 76  ? -2.92423  26.19700 7.93923  0.632 40.60138  ? 73  GLU A HG3  1 
ATOM   1395 N N    . GLU A 1 77  ? 1.14237   24.06503 7.59406  1.000 12.71873  ? 74  GLU A N    1 
ATOM   1396 C CA   . GLU A 1 77  ? 2.58686   24.16682 7.75776  1.000 12.04661  ? 74  GLU A CA   1 
ATOM   1397 C C    . GLU A 1 77  ? 2.99849   25.40557 8.54336  1.000 11.63701  ? 74  GLU A C    1 
ATOM   1398 O O    . GLU A 1 77  ? 3.95562   25.35166 9.32359  1.000 11.60935  ? 74  GLU A O    1 
ATOM   1399 C CB   . GLU A 1 77  ? 3.28676   24.11246 6.40227  1.000 13.86961  ? 74  GLU A CB   1 
ATOM   1400 C CG   . GLU A 1 77  ? 4.78056   23.90768 6.54047  1.000 14.74910  ? 74  GLU A CG   1 
ATOM   1401 C CD   . GLU A 1 77  ? 5.44299   23.49969 5.24544  1.000 19.09775  ? 74  GLU A CD   1 
ATOM   1402 O OE1  . GLU A 1 77  ? 4.76321   23.51140 4.19991  1.000 22.09379  ? 74  GLU A OE1  1 
ATOM   1403 O OE2  . GLU A 1 77  ? 6.64459   23.16161 5.27661  1.000 20.89656  ? 74  GLU A OE2  1 
ATOM   1404 H H    . GLU A 1 77  ? 0.85922   24.17325 6.78925  1.000 15.26247  ? 74  GLU A H    1 
ATOM   1405 H HA   . GLU A 1 77  ? 2.88172   23.39797 8.27043  1.000 14.45593  ? 74  GLU A HA   1 
ATOM   1406 H HB2  . GLU A 1 77  ? 2.92586   23.37399 5.88719  1.000 16.64354  ? 74  GLU A HB2  1 
ATOM   1407 H HB3  . GLU A 1 77  ? 3.13742   24.94832 5.93329  1.000 16.64354  ? 74  GLU A HB3  1 
ATOM   1408 H HG2  . GLU A 1 77  ? 5.18651   24.73788 6.83522  1.000 17.69891  ? 74  GLU A HG2  1 
ATOM   1409 H HG3  . GLU A 1 77  ? 4.94379   23.20863 7.19284  1.000 17.69891  ? 74  GLU A HG3  1 
ATOM   1410 N N    . GLU A 1 78  ? 2.31769   26.53590 8.34897  1.000 12.58106  ? 75  GLU A N    1 
ATOM   1411 C CA   A GLU A 1 78  ? 2.67155   27.73835 9.09887  0.493 13.08361  ? 75  GLU A CA   1 
ATOM   1412 C CA   B GLU A 1 78  ? 2.70209   27.72661 9.09954  0.507 13.08361  ? 75  GLU A CA   1 
ATOM   1413 C C    . GLU A 1 78  ? 2.45542   27.53324 10.59274 1.000 12.22744  ? 75  GLU A C    1 
ATOM   1414 O O    . GLU A 1 78  ? 3.25019   27.99581 11.41806 1.000 12.07869  ? 75  GLU A O    1 
ATOM   1415 C CB   A GLU A 1 78  ? 1.85672   28.93713 8.60985  0.493 19.54361  ? 75  GLU A CB   1 
ATOM   1416 C CB   B GLU A 1 78  ? 1.99383   28.96313 8.55095  0.507 19.54361  ? 75  GLU A CB   1 
ATOM   1417 C CG   A GLU A 1 78  ? 2.16309   30.22493 9.36883  0.493 35.09361  ? 75  GLU A CG   1 
ATOM   1418 C CG   B GLU A 1 78  ? 2.36218   29.28953 7.10044  0.507 35.09361  ? 75  GLU A CG   1 
ATOM   1419 C CD   A GLU A 1 78  ? 1.21951   31.36051 9.02631  0.493 48.01361  ? 75  GLU A CD   1 
ATOM   1420 C CD   B GLU A 1 78  ? 3.86360   29.34088 6.86180  0.507 48.01361  ? 75  GLU A CD   1 
ATOM   1421 O OE1  A GLU A 1 78  ? 0.43272   31.22264 8.06620  0.493 47.52361  ? 75  GLU A OE1  1 
ATOM   1422 O OE1  B GLU A 1 78  ? 4.59042   29.87681 7.72470  0.507 47.52361  ? 75  GLU A OE1  1 
ATOM   1423 O OE2  A GLU A 1 78  ? 1.26672   32.39241 9.72595  0.493 52.62361  ? 75  GLU A OE2  1 
ATOM   1424 O OE2  B GLU A 1 78  ? 4.31701   28.83257 5.81470  0.507 52.62361  ? 75  GLU A OE2  1 
ATOM   1425 H H    A GLU A 1 78  ? 1.66159   26.63063 7.80110  0.493 15.09727  ? 75  GLU A H    1 
ATOM   1426 H H    B GLU A 1 78  ? 1.65545   26.63478 7.80928  0.507 15.09727  ? 75  GLU A H    1 
ATOM   1427 H HA   A GLU A 1 78  ? 3.60935   27.93151 8.94356  0.493 15.70033  ? 75  GLU A HA   1 
ATOM   1428 H HA   B GLU A 1 78  ? 3.65196   27.88440 8.98231  0.507 15.70033  ? 75  GLU A HA   1 
ATOM   1429 H HB2  A GLU A 1 78  ? 2.05444   29.08931 7.67248  0.493 23.45233  ? 75  GLU A HB2  1 
ATOM   1430 H HB2  B GLU A 1 78  ? 1.03573   28.81619 8.58776  0.507 23.45233  ? 75  GLU A HB2  1 
ATOM   1431 H HB3  A GLU A 1 78  ? 0.91326   28.74197 8.72247  0.493 23.45233  ? 75  GLU A HB3  1 
ATOM   1432 H HB3  B GLU A 1 78  ? 2.23336   29.72814 9.09710  0.507 23.45233  ? 75  GLU A HB3  1 
ATOM   1433 H HG2  A GLU A 1 78  ? 2.08968   30.05360 10.32075 0.493 42.11233  ? 75  GLU A HG2  1 
ATOM   1434 H HG2  B GLU A 1 78  ? 1.99115   28.60641 6.52029  0.507 42.11233  ? 75  GLU A HG2  1 
ATOM   1435 H HG3  A GLU A 1 78  ? 3.06423   30.51076 9.15171  0.493 42.11233  ? 75  GLU A HG3  1 
ATOM   1436 H HG3  B GLU A 1 78  ? 1.99368   30.15666 6.86977  0.507 42.11233  ? 75  GLU A HG3  1 
ATOM   1437 N N    . ALA A 1 79  ? 1.37726   26.83771 10.96101 1.000 11.02701  ? 76  ALA A N    1 
ATOM   1438 C CA   . ALA A 1 79  ? 1.12110   26.56307 12.37150 1.000 11.00959  ? 76  ALA A CA   1 
ATOM   1439 C C    . ALA A 1 79  ? 2.20618   25.66733 12.95688 1.000 9.71348   ? 76  ALA A C    1 
ATOM   1440 O O    . ALA A 1 79  ? 2.71916   25.92124 14.05316 1.000 11.33180  ? 76  ALA A O    1 
ATOM   1441 C CB   . ALA A 1 79  ? -0.25023  25.90759 12.52120 1.000 11.71968  ? 76  ALA A CB   1 
ATOM   1442 H H    . ALA A 1 79  ? 0.78855   26.51919 10.42104 1.000 13.23241  ? 76  ALA A H    1 
ATOM   1443 H HA   . ALA A 1 79  ? 1.11991   27.39845 12.86448 1.000 13.21150  ? 76  ALA A HA   1 
ATOM   1444 H HB1  . ALA A 1 79  ? -0.43936  25.78285 13.46437 1.000 14.06362  ? 76  ALA A HB1  1 
ATOM   1445 H HB2  . ALA A 1 79  ? -0.92096  26.48400 12.12274 1.000 14.06362  ? 76  ALA A HB2  1 
ATOM   1446 H HB3  . ALA A 1 79  ? -0.24103  25.04931 12.06934 1.000 14.06362  ? 76  ALA A HB3  1 
ATOM   1447 N N    . TYR A 1 80  ? 2.56279   24.60620 12.23525 1.000 8.43398   ? 77  TYR A N    1 
ATOM   1448 C CA   . TYR A 1 80  ? 3.68778   23.76479 12.63100 1.000 8.28783   ? 77  TYR A CA   1 
ATOM   1449 C C    . TYR A 1 80  ? 4.95658   24.58552 12.80682 1.000 8.76427   ? 77  TYR A C    1 
ATOM   1450 O O    . TYR A 1 80  ? 5.67389   24.42780 13.80039 1.000 10.31145  ? 77  TYR A O    1 
ATOM   1451 C CB   . TYR A 1 80  ? 3.87346   22.68514 11.56038 1.000 9.75220   ? 77  TYR A CB   1 
ATOM   1452 C CG   . TYR A 1 80  ? 5.15030   21.86569 11.58859 1.000 9.02515   ? 77  TYR A CG   1 
ATOM   1453 C CD1  . TYR A 1 80  ? 6.31060   22.33138 10.98554 1.000 9.64514   ? 77  TYR A CD1  1 
ATOM   1454 C CD2  . TYR A 1 80  ? 5.17240   20.59286 12.15108 1.000 9.51431   ? 77  TYR A CD2  1 
ATOM   1455 C CE1  . TYR A 1 80  ? 7.46246   21.57787 10.97596 1.000 9.62658   ? 77  TYR A CE1  1 
ATOM   1456 C CE2  . TYR A 1 80  ? 6.32406   19.82832 12.14557 1.000 9.11457   ? 77  TYR A CE2  1 
ATOM   1457 C CZ   . TYR A 1 80  ? 7.46543   20.32455 11.54455 1.000 10.38635  ? 77  TYR A CZ   1 
ATOM   1458 O OH   . TYR A 1 80  ? 8.62180   19.57687 11.51671 1.000 10.18880  ? 77  TYR A OH   1 
ATOM   1459 H H    . TYR A 1 80  ? 2.17031   24.35226 11.51339 1.000 10.12078  ? 77  TYR A H    1 
ATOM   1460 H HA   . TYR A 1 80  ? 3.50377   23.33970 13.48325 1.000 9.94540   ? 77  TYR A HA   1 
ATOM   1461 H HB2  . TYR A 1 80  ? 3.13871   22.05737 11.64363 1.000 11.70264  ? 77  TYR A HB2  1 
ATOM   1462 H HB3  . TYR A 1 80  ? 3.84169   23.12004 10.69392 1.000 11.70264  ? 77  TYR A HB3  1 
ATOM   1463 H HD1  . TYR A 1 80  ? 6.30972   23.16843 10.58027 1.000 11.57416  ? 77  TYR A HD1  1 
ATOM   1464 H HD2  . TYR A 1 80  ? 4.39876   20.25067 12.53744 1.000 11.41718  ? 77  TYR A HD2  1 
ATOM   1465 H HE1  . TYR A 1 80  ? 8.23673   21.91482 10.58625 1.000 11.55190  ? 77  TYR A HE1  1 
ATOM   1466 H HE2  . TYR A 1 80  ? 6.33078   18.98745 12.54280 1.000 10.93749  ? 77  TYR A HE2  1 
ATOM   1467 H HH   . TYR A 1 80  ? 8.50003   18.84466 11.90994 1.000 12.22656  ? 77  TYR A HH   1 
ATOM   1468 N N    . ASN A 1 81  ? 5.26477   25.45521 11.84213 1.000 9.46114   ? 78  ASN A N    1 
ATOM   1469 C CA   . ASN A 1 81  ? 6.52289   26.19295 11.90189 1.000 10.15054  ? 78  ASN A CA   1 
ATOM   1470 C C    . ASN A 1 81  ? 6.58304   27.10174 13.12480 1.000 10.03360  ? 78  ASN A C    1 
ATOM   1471 O O    . ASN A 1 81  ? 7.62083   27.19108 13.79156 1.000 10.99458  ? 78  ASN A O    1 
ATOM   1472 C CB   . ASN A 1 81  ? 6.71018   27.03214 10.63866 1.000 11.04277  ? 78  ASN A CB   1 
ATOM   1473 C CG   . ASN A 1 81  ? 7.06457   26.20287 9.42524  1.000 13.70198  ? 78  ASN A CG   1 
ATOM   1474 O OD1  . ASN A 1 81  ? 7.51163   25.06105 9.53366  1.000 14.55702  ? 78  ASN A OD1  1 
ATOM   1475 N ND2  . ASN A 1 81  ? 6.88609   26.79024 8.25256  1.000 15.04804  ? 78  ASN A ND2  1 
ATOM   1476 H H    . ASN A 1 81  ? 4.77331   25.63138 11.15873 1.000 11.35337  ? 78  ASN A H    1 
ATOM   1477 H HA   . ASN A 1 81  ? 7.24413   25.54671 11.95734 1.000 12.18064  ? 78  ASN A HA   1 
ATOM   1478 H HB2  . ASN A 1 81  ? 5.88391   27.50306 10.44783 1.000 13.25132  ? 78  ASN A HB2  1 
ATOM   1479 H HB3  . ASN A 1 81  ? 7.42787   27.66779 10.78618 1.000 13.25132  ? 78  ASN A HB3  1 
ATOM   1480 H HD21 . ASN A 1 81  ? 7.07077   26.36695 7.52708  1.000 18.05765  ? 78  ASN A HD21 1 
ATOM   1481 H HD22 . ASN A 1 81  ? 6.58544   27.59515 8.21612  1.000 18.05765  ? 78  ASN A HD22 1 
ATOM   1482 N N    . GLY A 1 82  ? 5.49133   27.81426 13.41291 1.000 10.78268  ? 79  GLY A N    1 
ATOM   1483 C CA   . GLY A 1 82  ? 5.49529   28.73126 14.53926 1.000 10.07967  ? 79  GLY A CA   1 
ATOM   1484 C C    . GLY A 1 82  ? 5.56085   28.02296 15.87349 1.000 10.71730  ? 79  GLY A C    1 
ATOM   1485 O O    . GLY A 1 82  ? 6.16579   28.52768 16.82343 1.000 11.77559  ? 79  GLY A O    1 
ATOM   1486 H H    . GLY A 1 82  ? 4.75093   27.78222 12.97659 1.000 12.93922  ? 79  GLY A H    1 
ATOM   1487 H HA2  . GLY A 1 82  ? 6.26369   29.31909 14.46922 1.000 12.09560  ? 79  GLY A HA2  1 
ATOM   1488 H HA3  . GLY A 1 82  ? 4.68598   29.26556 14.51834 1.000 12.09560  ? 79  GLY A HA3  1 
ATOM   1489 N N    . TYR A 1 83  ? 4.96449   26.83963 15.95884 1.000 10.54484  ? 80  TYR A N    1 
ATOM   1490 C CA   . TYR A 1 83  ? 4.94860   26.07519 17.20114 1.000 9.74392   ? 80  TYR A CA   1 
ATOM   1491 C C    . TYR A 1 83  ? 6.28138   25.37456 17.42951 1.000 10.00116  ? 80  TYR A C    1 
ATOM   1492 O O    . TYR A 1 83  ? 6.81985   25.41818 18.54170 1.000 10.09949  ? 80  TYR A O    1 
ATOM   1493 C CB   . TYR A 1 83  ? 3.76484   25.10929 17.13103 1.000 9.38846   ? 80  TYR A CB   1 
ATOM   1494 C CG   . TYR A 1 83  ? 3.48447   24.27732 18.35719 1.000 9.87997   ? 80  TYR A CG   1 
ATOM   1495 C CD1  . TYR A 1 83  ? 3.44363   24.84130 19.62031 1.000 10.12716  ? 80  TYR A CD1  1 
ATOM   1496 C CD2  . TYR A 1 83  ? 3.20870   22.92141 18.23661 1.000 9.80107   ? 80  TYR A CD2  1 
ATOM   1497 C CE1  . TYR A 1 83  ? 3.16445   24.06549 20.74175 1.000 10.50482  ? 80  TYR A CE1  1 
ATOM   1498 C CE2  . TYR A 1 83  ? 2.92688   22.14256 19.34004 1.000 10.03508  ? 80  TYR A CE2  1 
ATOM   1499 C CZ   . TYR A 1 83  ? 2.90410   22.71615 20.59178 1.000 10.43152  ? 80  TYR A CZ   1 
ATOM   1500 O OH   . TYR A 1 83  ? 2.62778   21.93199 21.69111 1.000 11.06906  ? 80  TYR A OH   1 
ATOM   1501 H H    . TYR A 1 83  ? 4.55798   26.45247 15.30734 1.000 12.65381  ? 80  TYR A H    1 
ATOM   1502 H HA   . TYR A 1 83  ? 4.81871   26.64593 17.97463 1.000 11.69270  ? 80  TYR A HA   1 
ATOM   1503 H HB2  . TYR A 1 83  ? 2.96509   25.62892 16.95413 1.000 11.26615  ? 80  TYR A HB2  1 
ATOM   1504 H HB3  . TYR A 1 83  ? 3.92660   24.49064 16.40165 1.000 11.26615  ? 80  TYR A HB3  1 
ATOM   1505 H HD1  . TYR A 1 83  ? 3.60501   25.75160 19.72130 1.000 12.15260  ? 80  TYR A HD1  1 
ATOM   1506 H HD2  . TYR A 1 83  ? 3.21414   22.52969 17.39314 1.000 11.76129  ? 80  TYR A HD2  1 
ATOM   1507 H HE1  . TYR A 1 83  ? 3.15313   24.45275 21.58721 1.000 12.60579  ? 80  TYR A HE1  1 
ATOM   1508 H HE2  . TYR A 1 83  ? 2.75312   21.23455 19.23896 1.000 12.04209  ? 80  TYR A HE2  1 
ATOM   1509 H HH   . TYR A 1 83  ? 2.27350   21.21036 21.44753 1.000 13.28287  ? 80  TYR A HH   1 
ATOM   1510 N N    . PHE A 1 84  ? 6.85771   24.77159 16.38815 1.000 8.93348   ? 81  PHE A N    1 
ATOM   1511 C CA   . PHE A 1 84  ? 8.16672   24.13931 16.54048 1.000 8.62671   ? 81  PHE A CA   1 
ATOM   1512 C C    . PHE A 1 84  ? 9.25875   25.16936 16.81455 1.000 9.20825   ? 81  PHE A C    1 
ATOM   1513 O O    . PHE A 1 84  ? 10.27354  24.84108 17.43813 1.000 10.20324  ? 81  PHE A O    1 
ATOM   1514 C CB   . PHE A 1 84  ? 8.48519   23.29470 15.29840 1.000 10.41734  ? 81  PHE A CB   1 
ATOM   1515 C CG   . PHE A 1 84  ? 9.82023   22.59662 15.35550 1.000 9.50328   ? 81  PHE A CG   1 
ATOM   1516 C CD1  . PHE A 1 84  ? 10.16102  21.80293 16.44036 1.000 9.58379   ? 81  PHE A CD1  1 
ATOM   1517 C CD2  . PHE A 1 84  ? 10.72632  22.72043 14.31349 1.000 11.42386  ? 81  PHE A CD2  1 
ATOM   1518 C CE1  . PHE A 1 84  ? 11.38301  21.16553 16.49500 1.000 10.06774  ? 81  PHE A CE1  1 
ATOM   1519 C CE2  . PHE A 1 84  ? 11.94804  22.08264 14.36335 1.000 10.66856  ? 81  PHE A CE2  1 
ATOM   1520 C CZ   . PHE A 1 84  ? 12.27636  21.30346 15.45342 1.000 10.79437  ? 81  PHE A CZ   1 
ATOM   1521 H H    . PHE A 1 84  ? 6.51908   24.71579 15.59959 1.000 10.72018  ? 81  PHE A H    1 
ATOM   1522 H HA   . PHE A 1 84  ? 8.14721   23.53672 17.30036 1.000 10.35205  ? 81  PHE A HA   1 
ATOM   1523 H HB2  . PHE A 1 84  ? 7.80070   22.61427 15.20151 1.000 12.50081  ? 81  PHE A HB2  1 
ATOM   1524 H HB3  . PHE A 1 84  ? 8.48887   23.87467 14.52089 1.000 12.50081  ? 81  PHE A HB3  1 
ATOM   1525 H HD1  . PHE A 1 84  ? 9.55763   21.69903 17.14038 1.000 11.50055  ? 81  PHE A HD1  1 
ATOM   1526 H HD2  . PHE A 1 84  ? 10.50793  23.23907 13.57306 1.000 13.70864  ? 81  PHE A HD2  1 
ATOM   1527 H HE1  . PHE A 1 84  ? 11.60401  20.64394 17.23256 1.000 12.08129  ? 81  PHE A HE1  1 
ATOM   1528 H HE2  . PHE A 1 84  ? 12.55096  22.17786 13.66170 1.000 12.80227  ? 81  PHE A HE2  1 
ATOM   1529 H HZ   . PHE A 1 84  ? 13.09936  20.87159 15.48586 1.000 12.95324  ? 81  PHE A HZ   1 
ATOM   1530 N N    . ALA A 1 85  ? 9.06997   26.41271 16.36376 1.000 9.57642   ? 82  ALA A N    1 
ATOM   1531 C CA   . ALA A 1 85  ? 10.04802  27.46122 16.64335 1.000 10.62068  ? 82  ALA A CA   1 
ATOM   1532 C C    . ALA A 1 85  ? 10.22518  27.68878 18.13780 1.000 9.00629   ? 82  ALA A C    1 
ATOM   1533 O O    . ALA A 1 85  ? 11.28023  28.16070 18.57631 1.000 11.56369  ? 82  ALA A O    1 
ATOM   1534 C CB   . ALA A 1 85  ? 9.61745   28.76154 15.96840 1.000 12.29400  ? 82  ALA A CB   1 
ATOM   1535 H H    . ALA A 1 85  ? 8.39295   26.67043 15.90027 1.000 11.49171  ? 82  ALA A H    1 
ATOM   1536 H HA   . ALA A 1 85  ? 10.90475  27.19002 16.27815 1.000 12.74481  ? 82  ALA A HA   1 
ATOM   1537 H HB1  . ALA A 1 85  ? 10.20151  29.47819 16.26199 1.000 14.75280  ? 82  ALA A HB1  1 
ATOM   1538 H HB2  . ALA A 1 85  ? 9.68268   28.65471 15.00651 1.000 14.75280  ? 82  ALA A HB2  1 
ATOM   1539 H HB3  . ALA A 1 85  ? 8.70102   28.95847 16.21795 1.000 14.75280  ? 82  ALA A HB3  1 
ATOM   1540 N N    . LYS A 1 86  ? 9.20750   27.36655 18.93722 1.000 10.00982  ? 83  LYS A N    1 
ATOM   1541 C CA   . LYS A 1 86  ? 9.28112   27.53471 20.38177 1.000 9.44820   ? 83  LYS A CA   1 
ATOM   1542 C C    . LYS A 1 86  ? 10.04658  26.41482 21.07116 1.000 8.21566   ? 83  LYS A C    1 
ATOM   1543 O O    . LYS A 1 86  ? 10.29248  26.50742 22.27954 1.000 11.61642  ? 83  LYS A O    1 
ATOM   1544 C CB   . LYS A 1 86  ? 7.86314   27.60410 20.95523 1.000 11.02463  ? 83  LYS A CB   1 
ATOM   1545 C CG   . LYS A 1 86  ? 7.01067   28.70513 20.34173 1.000 10.13136  ? 83  LYS A CG   1 
ATOM   1546 C CD   . LYS A 1 86  ? 5.60709   28.73654 20.93756 1.000 11.01907  ? 83  LYS A CD   1 
ATOM   1547 C CE   . LYS A 1 86  ? 4.74713   29.81525 20.29550 1.000 11.08863  ? 83  LYS A CE   1 
ATOM   1548 N NZ   . LYS A 1 86  ? 3.37106   29.84163 20.87011 1.000 13.15148  ? 83  LYS A NZ   1 
ATOM   1549 H H    . LYS A 1 86  ? 8.45847   27.04609 18.66179 1.000 12.01178  ? 83  LYS A H    1 
ATOM   1550 H HA   . LYS A 1 86  ? 9.73698   28.36779 20.57946 1.000 11.33784  ? 83  LYS A HA   1 
ATOM   1551 H HB2  . LYS A 1 86  ? 7.41810   26.75799 20.79110 1.000 13.22956  ? 83  LYS A HB2  1 
ATOM   1552 H HB3  . LYS A 1 86  ? 7.91984   27.76954 21.90933 1.000 13.22956  ? 83  LYS A HB3  1 
ATOM   1553 H HG2  . LYS A 1 86  ? 7.42977   29.56403 20.50770 1.000 12.15763  ? 83  LYS A HG2  1 
ATOM   1554 H HG3  . LYS A 1 86  ? 6.93138   28.55365 19.38692 1.000 12.15763  ? 83  LYS A HG3  1 
ATOM   1555 H HD2  . LYS A 1 86  ? 5.17785   27.87894 20.79203 1.000 13.22288  ? 83  LYS A HD2  1 
ATOM   1556 H HD3  . LYS A 1 86  ? 5.66643   28.92079 21.88805 1.000 13.22288  ? 83  LYS A HD3  1 
ATOM   1557 H HE2  . LYS A 1 86  ? 5.15582   30.68198 20.44599 1.000 13.30636  ? 83  LYS A HE2  1 
ATOM   1558 H HE3  . LYS A 1 86  ? 4.67557   29.64298 19.34361 1.000 13.30636  ? 83  LYS A HE3  1 
ATOM   1559 H HZ1  . LYS A 1 86  ? 3.40377   30.07734 21.72771 1.000 15.78177  ? 83  LYS A HZ1  1 
ATOM   1560 H HZ2  . LYS A 1 86  ? 2.86793   30.42802 20.42839 1.000 15.78177  ? 83  LYS A HZ2  1 
ATOM   1561 H HZ3  . LYS A 1 86  ? 2.99894   29.03570 20.80606 1.000 15.78177  ? 83  LYS A HZ3  1 
ATOM   1562 N N    . MET A 1 87  ? 10.43645  25.37020 20.33051 1.000 9.05280   ? 84  MET A N    1 
ATOM   1563 C CA   . MET A 1 87  ? 10.99582  24.15115 20.88372 1.000 10.08004  ? 84  MET A CA   1 
ATOM   1564 C C    . MET A 1 87  ? 12.47766  24.02261 20.56270 1.000 9.82286   ? 84  MET A C    1 
ATOM   1565 O O    . MET A 1 87  ? 12.90805  24.40451 19.46786 1.000 11.09252  ? 84  MET A O    1 
ATOM   1566 C CB   . MET A 1 87  ? 10.26424  22.94197 20.29161 1.000 8.58497   ? 84  MET A CB   1 
ATOM   1567 C CG   . MET A 1 87  ? 8.77124   22.94455 20.52639 1.000 9.41448   ? 84  MET A CG   1 
ATOM   1568 S SD   . MET A 1 87  ? 7.91911   21.63982 19.63541 1.000 9.98062   ? 84  MET A SD   1 
ATOM   1569 C CE   . MET A 1 87  ? 6.21605   21.99526 20.06767 1.000 11.52962  ? 84  MET A CE   1 
ATOM   1570 H H    . MET A 1 87  ? 10.38147  25.35089 19.47249 1.000 10.86335  ? 84  MET A H    1 
ATOM   1571 H HA   . MET A 1 87  ? 10.88994  24.15912 21.84790 1.000 12.09605  ? 84  MET A HA   1 
ATOM   1572 H HB2  . MET A 1 87  ? 10.41123  22.92968 19.33289 1.000 10.30197  ? 84  MET A HB2  1 
ATOM   1573 H HB3  . MET A 1 87  ? 10.62370  22.13525 20.69273 1.000 10.30197  ? 84  MET A HB3  1 
ATOM   1574 H HG2  . MET A 1 87  ? 8.60088   22.82056 21.47323 1.000 11.29737  ? 84  MET A HG2  1 
ATOM   1575 H HG3  . MET A 1 87  ? 8.40743   23.79429 20.23233 1.000 11.29737  ? 84  MET A HG3  1 
ATOM   1576 H HE1  . MET A 1 87  ? 5.64557   21.30264 19.69925 1.000 13.83555  ? 84  MET A HE1  1 
ATOM   1577 H HE2  . MET A 1 87  ? 6.13263   22.01326 21.03390 1.000 13.83555  ? 84  MET A HE2  1 
ATOM   1578 H HE3  . MET A 1 87  ? 5.96989   22.85774 19.69828 1.000 13.83555  ? 84  MET A HE3  1 
ATOM   1579 N N    . PRO A 1 88  ? 13.27291  23.47909 21.48322 1.000 9.34595   ? 85  PRO A N    1 
ATOM   1580 C CA   . PRO A 1 88  ? 14.71229  23.34645 21.25450 1.000 10.95964  ? 85  PRO A CA   1 
ATOM   1581 C C    . PRO A 1 88  ? 15.15874  22.01976 20.66996 1.000 10.67857  ? 85  PRO A C    1 
ATOM   1582 O O    . PRO A 1 88  ? 16.36432  21.84342 20.43656 1.000 13.31554  ? 85  PRO A O    1 
ATOM   1583 C CB   . PRO A 1 88  ? 15.26455  23.49279 22.68128 1.000 11.95665  ? 85  PRO A CB   1 
ATOM   1584 C CG   . PRO A 1 88  ? 14.21768  22.81277 23.51695 1.000 11.03249  ? 85  PRO A CG   1 
ATOM   1585 C CD   . PRO A 1 88  ? 12.91101  23.22721 22.89393 1.000 10.26135  ? 85  PRO A CD   1 
ATOM   1586 H HA   . PRO A 1 88  ? 15.03066  24.06713 20.68867 1.000 13.15157  ? 85  PRO A HA   1 
ATOM   1587 H HB2  . PRO A 1 88  ? 16.12376  23.04938 22.75901 1.000 14.34798  ? 85  PRO A HB2  1 
ATOM   1588 H HB3  . PRO A 1 88  ? 15.35237  24.42985 22.91600 1.000 14.34798  ? 85  PRO A HB3  1 
ATOM   1589 H HG2  . PRO A 1 88  ? 14.33326  21.85052 23.47687 1.000 13.23899  ? 85  PRO A HG2  1 
ATOM   1590 H HG3  . PRO A 1 88  ? 14.27716  23.11605 24.43639 1.000 13.23899  ? 85  PRO A HG3  1 
ATOM   1591 H HD2  . PRO A 1 88  ? 12.25549  22.51534 22.96050 1.000 12.31362  ? 85  PRO A HD2  1 
ATOM   1592 H HD3  . PRO A 1 88  ? 12.56928  24.03304 23.31198 1.000 12.31362  ? 85  PRO A HD3  1 
ATOM   1593 N N    . TRP A 1 89  ? 14.24117  21.08268 20.42007 1.000 9.84511   ? 86  TRP A N    1 
ATOM   1594 C CA   . TRP A 1 89  ? 14.54993  19.68989 20.10345 1.000 9.09944   ? 86  TRP A CA   1 
ATOM   1595 C C    . TRP A 1 89  ? 14.34038  19.42755 18.59563 1.000 9.00512   ? 86  TRP A C    1 
ATOM   1596 O O    . TRP A 1 89  ? 14.49539  20.34841 17.77855 1.000 10.36399  ? 86  TRP A O    1 
ATOM   1597 C CB   . TRP A 1 89  ? 13.76936  18.77730 21.03395 1.000 9.97669   ? 86  TRP A CB   1 
ATOM   1598 C CG   . TRP A 1 89  ? 12.30161  19.09903 21.15881 1.000 7.97315   ? 86  TRP A CG   1 
ATOM   1599 C CD1  . TRP A 1 89  ? 11.35851  19.01895 20.17557 1.000 9.41873   ? 86  TRP A CD1  1 
ATOM   1600 C CD2  . TRP A 1 89  ? 11.60726  19.53028 22.34396 1.000 7.07470   ? 86  TRP A CD2  1 
ATOM   1601 N NE1  . TRP A 1 89  ? 10.12793  19.38441 20.66779 1.000 8.98553   ? 86  TRP A NE1  1 
ATOM   1602 C CE2  . TRP A 1 89  ? 10.25349  19.70586 21.99388 1.000 7.31423   ? 86  TRP A CE2  1 
ATOM   1603 C CE3  . TRP A 1 89  ? 12.00084  19.79007 23.66356 1.000 7.72095   ? 86  TRP A CE3  1 
ATOM   1604 C CZ2  . TRP A 1 89  ? 9.29275   20.12792 22.91164 1.000 8.67870   ? 86  TRP A CZ2  1 
ATOM   1605 C CZ3  . TRP A 1 89  ? 11.04227  20.20881 24.57235 1.000 8.26711   ? 86  TRP A CZ3  1 
ATOM   1606 C CH2  . TRP A 1 89  ? 9.70823   20.37850 24.18934 1.000 8.04525   ? 86  TRP A CH2  1 
ATOM   1607 H H    . TRP A 1 89  ? 13.39580  21.24041 20.42938 1.000 11.81413  ? 86  TRP A H    1 
ATOM   1608 H HA   . TRP A 1 89  ? 15.49189  19.54332 20.28269 1.000 10.91933  ? 86  TRP A HA   1 
ATOM   1609 H HB2  . TRP A 1 89  ? 13.84052  17.86815 20.70337 1.000 11.97203  ? 86  TRP A HB2  1 
ATOM   1610 H HB3  . TRP A 1 89  ? 14.15692  18.83905 21.92101 1.000 11.97203  ? 86  TRP A HB3  1 
ATOM   1611 H HD1  . TRP A 1 89  ? 11.52430  18.75529 19.29927 1.000 11.30248  ? 86  TRP A HD1  1 
ATOM   1612 H HE1  . TRP A 1 89  ? 9.39661   19.40754 20.21587 1.000 10.78263  ? 86  TRP A HE1  1 
ATOM   1613 H HE3  . TRP A 1 89  ? 12.88725  19.68361 23.92405 1.000 9.26514   ? 86  TRP A HE3  1 
ATOM   1614 H HZ2  . TRP A 1 89  ? 8.40278   20.23493 22.66384 1.000 10.41444  ? 86  TRP A HZ2  1 
ATOM   1615 H HZ3  . TRP A 1 89  ? 11.29046  20.37993 25.45213 1.000 9.92054   ? 86  TRP A HZ3  1 
ATOM   1616 H HH2  . TRP A 1 89  ? 9.08870   20.66888 24.81923 1.000 9.65430   ? 86  TRP A HH2  1 
ATOM   1617 N N    . LEU A 1 90  ? 14.01923  18.18335 18.25468 1.000 9.40740   ? 87  LEU A N    1 
ATOM   1618 C CA   . LEU A 1 90  ? 13.93736  17.76372 16.86136 1.000 8.66668   ? 87  LEU A CA   1 
ATOM   1619 C C    . LEU A 1 90  ? 12.48599  17.50991 16.47698 1.000 8.27124   ? 87  LEU A C    1 
ATOM   1620 O O    . LEU A 1 90  ? 11.61482  17.37364 17.33831 1.000 9.20317   ? 87  LEU A O    1 
ATOM   1621 C CB   . LEU A 1 90  ? 14.74853  16.48186 16.64823 1.000 9.22212   ? 87  LEU A CB   1 
ATOM   1622 C CG   . LEU A 1 90  ? 16.20521  16.54615 17.11642 1.000 9.88440   ? 87  LEU A CG   1 
ATOM   1623 C CD1  . LEU A 1 90  ? 16.90580  15.20890 16.91521 1.000 10.65534  ? 87  LEU A CD1  1 
ATOM   1624 C CD2  . LEU A 1 90  ? 16.94549  17.66167 16.38303 1.000 12.20669  ? 87  LEU A CD2  1 
ATOM   1625 H H    . LEU A 1 90  ? 13.84285  17.55900 18.81921 1.000 11.28888  ? 87  LEU A H    1 
ATOM   1626 H HA   . LEU A 1 90  ? 14.28994  18.46212 16.28793 1.000 10.40002  ? 87  LEU A HA   1 
ATOM   1627 H HB2  . LEU A 1 90  ? 14.31778  15.76302 17.13672 1.000 11.06655  ? 87  LEU A HB2  1 
ATOM   1628 H HB3  . LEU A 1 90  ? 14.75689  16.27984 15.69954 1.000 11.06655  ? 87  LEU A HB3  1 
ATOM   1629 H HG   . LEU A 1 90  ? 16.22162  16.74170 18.06636 1.000 11.86128  ? 87  LEU A HG   1 
ATOM   1630 H HD11 . LEU A 1 90  ? 17.75297  15.22202 17.38747 1.000 12.78640  ? 87  LEU A HD11 1 
ATOM   1631 H HD12 . LEU A 1 90  ? 16.34252  14.50136 17.26591 1.000 12.78640  ? 87  LEU A HD12 1 
ATOM   1632 H HD13 . LEU A 1 90  ? 17.05773  15.07149 15.96709 1.000 12.78640  ? 87  LEU A HD13 1 
ATOM   1633 H HD21 . LEU A 1 90  ? 17.87430  17.66131 16.66270 1.000 14.64803  ? 87  LEU A HD21 1 
ATOM   1634 H HD22 . LEU A 1 90  ? 16.88765  17.50412 15.42766 1.000 14.64803  ? 87  LEU A HD22 1 
ATOM   1635 H HD23 . LEU A 1 90  ? 16.53397  18.51191 16.60358 1.000 14.64803  ? 87  LEU A HD23 1 
ATOM   1636 N N    . ALA A 1 91  ? 12.23181  17.42941 15.17364 1.000 8.84067   ? 88  ALA A N    1 
ATOM   1637 C CA   . ALA A 1 91  ? 10.88563  17.14199 14.71359 1.000 7.13370   ? 88  ALA A CA   1 
ATOM   1638 C C    . ALA A 1 91  ? 10.91820  16.29519 13.45438 1.000 8.46558   ? 88  ALA A C    1 
ATOM   1639 O O    . ALA A 1 91  ? 11.78625  16.47204 12.59319 1.000 10.20617  ? 88  ALA A O    1 
ATOM   1640 C CB   . ALA A 1 91  ? 10.10781  18.42503 14.40221 1.000 8.03913   ? 88  ALA A CB   1 
ATOM   1641 H H    . ALA A 1 91  ? 12.81472  17.53613 14.55040 1.000 10.60880  ? 88  ALA A H    1 
ATOM   1642 H HA   . ALA A 1 91  ? 10.43846  16.64168 15.41404 1.000 8.56044   ? 88  ALA A HA   1 
ATOM   1643 H HB1  . ALA A 1 91  ? 9.22757   18.18809 14.07064 1.000 9.64696   ? 88  ALA A HB1  1 
ATOM   1644 H HB2  . ALA A 1 91  ? 10.02536  18.94926 15.21417 1.000 9.64696   ? 88  ALA A HB2  1 
ATOM   1645 H HB3  . ALA A 1 91  ? 10.58961  18.93097 13.72931 1.000 9.64696   ? 88  ALA A HB3  1 
ATOM   1646 N N    . ILE A 1 92  ? 9.95082   15.39286 13.35268 1.000 9.02511   ? 89  ILE A N    1 
ATOM   1647 C CA   . ILE A 1 92  ? 9.68172   14.77264 12.05272 1.000 9.34798   ? 89  ILE A CA   1 
ATOM   1648 C C    . ILE A 1 92  ? 9.22902   15.85712 11.08959 1.000 7.02007   ? 89  ILE A C    1 
ATOM   1649 O O    . ILE A 1 92  ? 8.42722   16.73323 11.47473 1.000 8.49921   ? 89  ILE A O    1 
ATOM   1650 C CB   . ILE A 1 92  ? 8.62055   13.67065 12.20016 1.000 9.81608   ? 89  ILE A CB   1 
ATOM   1651 C CG1  . ILE A 1 92  ? 9.19802   12.53235 13.04602 1.000 11.65540  ? 89  ILE A CG1  1 
ATOM   1652 C CG2  . ILE A 1 92  ? 8.16382   13.14738 10.83573 1.000 10.05345  ? 89  ILE A CG2  1 
ATOM   1653 C CD1  . ILE A 1 92  ? 8.17796   11.52613 13.49324 1.000 13.71261  ? 89  ILE A CD1  1 
ATOM   1654 H H    . ILE A 1 92  ? 9.44779   15.12614 13.99721 1.000 10.83014  ? 89  ILE A H    1 
ATOM   1655 H HA   . ILE A 1 92  ? 10.48924  14.36642 11.70087 1.000 11.21758  ? 89  ILE A HA   1 
ATOM   1656 H HB   . ILE A 1 92  ? 7.84275   14.04607 12.64172 1.000 11.77930  ? 89  ILE A HB   1 
ATOM   1657 H HG12 . ILE A 1 92  ? 9.86535   12.06283 12.52151 1.000 13.98649  ? 89  ILE A HG12 1 
ATOM   1658 H HG13 . ILE A 1 92  ? 9.60648   12.91128 13.84004 1.000 13.98649  ? 89  ILE A HG13 1 
ATOM   1659 H HG21 . ILE A 1 92  ? 7.49892   12.45397 10.96986 1.000 12.06414  ? 89  ILE A HG21 1 
ATOM   1660 H HG22 . ILE A 1 92  ? 7.78010   13.88000 10.32885 1.000 12.06414  ? 89  ILE A HG22 1 
ATOM   1661 H HG23 . ILE A 1 92  ? 8.92982   12.78437 10.36417 1.000 12.06414  ? 89  ILE A HG23 1 
ATOM   1662 H HD11 . ILE A 1 92  ? 8.59752   10.90199 14.10587 1.000 16.45513  ? 89  ILE A HD11 1 
ATOM   1663 H HD12 . ILE A 1 92  ? 7.45163   11.98946 13.93897 1.000 16.45513  ? 89  ILE A HD12 1 
ATOM   1664 H HD13 . ILE A 1 92  ? 7.84087   11.05182 12.71715 1.000 16.45513  ? 89  ILE A HD13 1 
ATOM   1665 N N    . PRO A 1 93  ? 9.72016   15.89175 9.85955  1.000 8.84767   ? 90  PRO A N    1 
ATOM   1666 C CA   . PRO A 1 93  ? 9.32040   16.96972 8.94861  1.000 10.18894  ? 90  PRO A CA   1 
ATOM   1667 C C    . PRO A 1 93  ? 7.81278   17.01310 8.74979  1.000 10.15775  ? 90  PRO A C    1 
ATOM   1668 O O    . PRO A 1 93  ? 7.14652   15.97849 8.67421  1.000 10.07610  ? 90  PRO A O    1 
ATOM   1669 C CB   . PRO A 1 93  ? 10.03970  16.61791 7.64317  1.000 12.59436  ? 90  PRO A CB   1 
ATOM   1670 C CG   . PRO A 1 93  ? 11.15472  15.72976 8.04767  1.000 12.58184  ? 90  PRO A CG   1 
ATOM   1671 C CD   . PRO A 1 93  ? 10.70542  14.98002 9.25459  1.000 10.37302  ? 90  PRO A CD   1 
ATOM   1672 H HA   . PRO A 1 93  ? 9.63103   17.82545 9.28349  1.000 12.22673  ? 90  PRO A HA   1 
ATOM   1673 H HB2  . PRO A 1 93  ? 9.43046   16.15930 7.04366  1.000 15.11324  ? 90  PRO A HB2  1 
ATOM   1674 H HB3  . PRO A 1 93  ? 10.37411  17.42539 7.22240  1.000 15.11324  ? 90  PRO A HB3  1 
ATOM   1675 H HG2  . PRO A 1 93  ? 11.35625  15.11645 7.32370  1.000 15.09821  ? 90  PRO A HG2  1 
ATOM   1676 H HG3  . PRO A 1 93  ? 11.93535  16.26724 8.25415  1.000 15.09821  ? 90  PRO A HG3  1 
ATOM   1677 H HD2  . PRO A 1 93  ? 10.29223  14.13834 9.00610  1.000 12.44763  ? 90  PRO A HD2  1 
ATOM   1678 H HD3  . PRO A 1 93  ? 11.44678  14.81989 9.85928  1.000 12.44763  ? 90  PRO A HD3  1 
ATOM   1679 N N    . PHE A 1 94  ? 7.29111   18.23897 8.62899  1.000 10.14411  ? 91  PHE A N    1 
ATOM   1680 C CA   . PHE A 1 94  ? 5.86072   18.44744 8.42911  1.000 9.74139   ? 91  PHE A CA   1 
ATOM   1681 C C    . PHE A 1 94  ? 5.29427   17.58392 7.30951  1.000 10.20682  ? 91  PHE A C    1 
ATOM   1682 O O    . PHE A 1 94  ? 4.17790   17.06597 7.42273  1.000 11.76263  ? 91  PHE A O    1 
ATOM   1683 C CB   . PHE A 1 94  ? 5.59224   19.92165 8.11528  1.000 9.71132   ? 91  PHE A CB   1 
ATOM   1684 C CG   . PHE A 1 94  ? 4.15938   20.21410 7.78358  1.000 9.60881   ? 91  PHE A CG   1 
ATOM   1685 C CD1  . PHE A 1 94  ? 3.22424   20.36324 8.79191  1.000 9.44281   ? 91  PHE A CD1  1 
ATOM   1686 C CD2  . PHE A 1 94  ? 3.74294   20.32115 6.46960  1.000 12.03036  ? 91  PHE A CD2  1 
ATOM   1687 C CE1  . PHE A 1 94  ? 1.90394   20.62508 8.49551  1.000 11.91369  ? 91  PHE A CE1  1 
ATOM   1688 C CE2  . PHE A 1 94  ? 2.42318   20.58097 6.16829  1.000 12.79607  ? 91  PHE A CE2  1 
ATOM   1689 C CZ   . PHE A 1 94  ? 1.50237   20.73530 7.18417  1.000 12.43146  ? 91  PHE A CZ   1 
ATOM   1690 H H    . PHE A 1 94  ? 7.74778   18.96706 8.65970  1.000 12.17293  ? 91  PHE A H    1 
ATOM   1691 H HA   . PHE A 1 94  ? 5.40901   18.20264 9.25187  1.000 11.68967  ? 91  PHE A HA   1 
ATOM   1692 H HB2  . PHE A 1 94  ? 5.83223   20.45458 8.88942  1.000 11.65358  ? 91  PHE A HB2  1 
ATOM   1693 H HB3  . PHE A 1 94  ? 6.13234   20.18213 7.35283  1.000 11.65358  ? 91  PHE A HB3  1 
ATOM   1694 H HD1  . PHE A 1 94  ? 3.48944   20.28595 9.67994  1.000 11.33137  ? 91  PHE A HD1  1 
ATOM   1695 H HD2  . PHE A 1 94  ? 4.35989   20.21673 5.78158  1.000 14.43643  ? 91  PHE A HD2  1 
ATOM   1696 H HE1  . PHE A 1 94  ? 1.28463   20.72723 9.18174  1.000 14.29642  ? 91  PHE A HE1  1 
ATOM   1697 H HE2  . PHE A 1 94  ? 2.15366   20.65219 5.28105  1.000 15.35528  ? 91  PHE A HE2  1 
ATOM   1698 H HZ   . PHE A 1 94  ? 0.61205   20.91346 6.98292  1.000 14.91775  ? 91  PHE A HZ   1 
ATOM   1699 N N    . SER A 1 95  ? 6.03111   17.43445 6.21067  1.000 10.93261  ? 92  SER A N    1 
ATOM   1700 C CA   . SER A 1 95  ? 5.47442   16.76370 5.04448  1.000 11.80519  ? 92  SER A CA   1 
ATOM   1701 C C    . SER A 1 95  ? 5.46499   15.24343 5.15630  1.000 11.17894  ? 92  SER A C    1 
ATOM   1702 O O    . SER A 1 95  ? 4.90489   14.58251 4.27670  1.000 12.41371  ? 92  SER A O    1 
ATOM   1703 C CB   . SER A 1 95  ? 6.26178   17.15416 3.79112  1.000 15.29936  ? 92  SER A CB   1 
ATOM   1704 O OG   . SER A 1 95  ? 7.60059   16.70118 3.88617  1.000 20.22449  ? 92  SER A OG   1 
ATOM   1705 H H    . SER A 1 95  ? 6.84114   17.70856 6.11951  1.000 13.11913  ? 92  SER A H    1 
ATOM   1706 H HA   . SER A 1 95  ? 4.55608   17.05970 4.94476  1.000 14.16623  ? 92  SER A HA   1 
ATOM   1707 H HB2  . SER A 1 95  ? 5.84411   16.74904 3.01503  1.000 18.35923  ? 92  SER A HB2  1 
ATOM   1708 H HB3  . SER A 1 95  ? 6.25918   18.12014 3.70292  1.000 18.35923  ? 92  SER A HB3  1 
ATOM   1709 H HG   . SER A 1 95  ? 7.99112   16.80240 3.14939  1.000 24.26939  ? 92  SER A HG   1 
ATOM   1710 N N    . SER A 1 96  ? 6.04462   14.67146 6.20701  1.000 10.35046  ? 93  SER A N    1 
ATOM   1711 C CA   A SER A 1 96  ? 6.15980   13.21627 6.32279  0.204 10.53361  ? 93  SER A CA   1 
ATOM   1712 C CA   B SER A 1 96  ? 6.16334   13.21875 6.33199  0.796 10.16361  ? 93  SER A CA   1 
ATOM   1713 C C    . SER A 1 96  ? 4.89441   12.62544 6.94975  1.000 10.42268  ? 93  SER A C    1 
ATOM   1714 O O    . SER A 1 96  ? 4.91274   12.00409 8.01003  1.000 9.77930   ? 93  SER A O    1 
ATOM   1715 C CB   A SER A 1 96  ? 7.40774   12.84884 7.11748  0.204 19.65361  ? 93  SER A CB   1 
ATOM   1716 C CB   B SER A 1 96  ? 7.40054   12.87408 7.15303  0.796 19.29361  ? 93  SER A CB   1 
ATOM   1717 O OG   A SER A 1 96  ? 8.58056   13.28952 6.45468  0.204 26.62361  ? 93  SER A OG   1 
ATOM   1718 O OG   B SER A 1 96  ? 7.82813   11.55008 6.90093  0.796 26.00361  ? 93  SER A OG   1 
ATOM   1719 H H    A SER A 1 96  ? 6.38103   15.10398 6.86985  0.204 12.42055  ? 93  SER A H    1 
ATOM   1720 H H    B SER A 1 96  ? 6.38099   15.10600 6.86855  0.796 12.42055  ? 93  SER A H    1 
ATOM   1721 H HA   A SER A 1 96  ? 6.25209   12.83944 5.43376  0.204 12.64033  ? 93  SER A HA   1 
ATOM   1722 H HA   B SER A 1 96  ? 6.26666   12.83319 5.44793  0.796 12.19633  ? 93  SER A HA   1 
ATOM   1723 H HB2  A SER A 1 96  ? 7.36139   13.27072 7.98970  0.204 23.58433  ? 93  SER A HB2  1 
ATOM   1724 H HB2  B SER A 1 96  ? 8.11528   13.48575 6.91659  0.796 23.15233  ? 93  SER A HB2  1 
ATOM   1725 H HB3  A SER A 1 96  ? 7.44543   11.88468 7.21688  0.204 23.58433  ? 93  SER A HB3  1 
ATOM   1726 H HB3  B SER A 1 96  ? 7.18709   12.96157 8.09520  0.796 23.15233  ? 93  SER A HB3  1 
ATOM   1727 H HG   A SER A 1 96  ? 8.57893   14.12735 6.39447  0.204 31.94833  ? 93  SER A HG   1 
ATOM   1728 H HG   B SER A 1 96  ? 8.50652   11.37417 7.36401  0.796 31.20433  ? 93  SER A HG   1 
ATOM   1729 N N    . ARG A 1 97  ? 3.77520   12.81318 6.24381  1.000 10.77317  ? 94  ARG A N    1 
ATOM   1730 C CA   . ARG A 1 97  ? 2.47263   12.49585 6.82744  1.000 10.81331  ? 94  ARG A CA   1 
ATOM   1731 C C    . ARG A 1 97  ? 2.32461   11.01157 7.15822  1.000 10.09072  ? 94  ARG A C    1 
ATOM   1732 O O    . ARG A 1 97  ? 1.78188   10.65973 8.21212  1.000 11.33666  ? 94  ARG A O    1 
ATOM   1733 C CB   . ARG A 1 97  ? 1.34474   12.97310 5.90897  1.000 11.95253  ? 94  ARG A CB   1 
ATOM   1734 C CG   . ARG A 1 97  ? 1.46990   14.43133 5.44696  1.000 13.78402  ? 94  ARG A CG   1 
ATOM   1735 C CD   . ARG A 1 97  ? 1.78645   15.41411 6.58818  1.000 15.70521  ? 94  ARG A CD   1 
ATOM   1736 N NE   . ARG A 1 97  ? 0.69357   15.53650 7.54656  1.000 16.75351  ? 94  ARG A NE   1 
ATOM   1737 C CZ   . ARG A 1 97  ? 0.67140   16.37558 8.57539  1.000 13.86797  ? 94  ARG A CZ   1 
ATOM   1738 N NH1  . ARG A 1 97  ? 1.69075   17.17715 8.84377  1.000 11.86666  ? 94  ARG A NH1  1 
ATOM   1739 N NH2  . ARG A 1 97  ? -0.40062  16.40550 9.36105  1.000 16.55328  ? 94  ARG A NH2  1 
ATOM   1740 H H    . ARG A 1 97  ? 3.74421   13.11741 5.44002  1.000 12.92781  ? 94  ARG A H    1 
ATOM   1741 H HA   . ARG A 1 97  ? 2.39707   12.97846 7.66546  1.000 12.97598  ? 94  ARG A HA   1 
ATOM   1742 H HB2  . ARG A 1 97  ? 1.33581   12.41480 5.11580  1.000 14.34304  ? 94  ARG A HB2  1 
ATOM   1743 H HB3  . ARG A 1 97  ? 0.50332   12.88806 6.38403  1.000 14.34304  ? 94  ARG A HB3  1 
ATOM   1744 H HG2  . ARG A 1 97  ? 2.18622   14.49328 4.79584  1.000 16.54082  ? 94  ARG A HG2  1 
ATOM   1745 H HG3  . ARG A 1 97  ? 0.63104   14.70552 5.04443  1.000 16.54082  ? 94  ARG A HG3  1 
ATOM   1746 H HD2  . ARG A 1 97  ? 2.57070   15.10190 7.06607  1.000 18.84625  ? 94  ARG A HD2  1 
ATOM   1747 H HD3  . ARG A 1 97  ? 1.95494   16.29213 6.21189  1.000 18.84625  ? 94  ARG A HD3  1 
ATOM   1748 H HE   . ARG A 1 97  ? 0.01061   15.02553 7.43669  1.000 20.10421  ? 94  ARG A HE   1 
ATOM   1749 H HH11 . ARG A 1 97  ? 2.39159   17.16308 8.34556  1.000 14.23999  ? 94  ARG A HH11 1 
ATOM   1750 H HH12 . ARG A 1 97  ? 1.65190   17.71178 9.51627  1.000 14.23999  ? 94  ARG A HH12 1 
ATOM   1751 H HH21 . ARG A 1 97  ? -1.06675  15.88609 9.19953  1.000 19.86393  ? 94  ARG A HH21 1 
ATOM   1752 H HH22 . ARG A 1 97  ? -0.42797  16.94426 10.03082 1.000 19.86393  ? 94  ARG A HH22 1 
ATOM   1753 N N    . ALA A 1 98  ? 2.78461   10.12416 6.27355  1.000 11.48646  ? 95  ALA A N    1 
ATOM   1754 C CA   . ALA A 1 98  ? 2.62057   8.69408  6.52564  1.000 12.18563  ? 95  ALA A CA   1 
ATOM   1755 C C    . ALA A 1 98  ? 3.43586   8.24716  7.73288  1.000 10.92494  ? 95  ALA A C    1 
ATOM   1756 O O    . ALA A 1 98  ? 2.98594   7.40262  8.51630  1.000 11.11007  ? 95  ALA A O    1 
ATOM   1757 C CB   . ALA A 1 98  ? 3.02228   7.89381  5.28770  1.000 14.28693  ? 95  ALA A CB   1 
ATOM   1758 H H    . ALA A 1 98  ? 3.18529   10.31964 5.53813  1.000 13.78375  ? 95  ALA A H    1 
ATOM   1759 H HA   . ALA A 1 98  ? 1.68493   8.51718  6.71053  1.000 14.62276  ? 95  ALA A HA   1 
ATOM   1760 H HB1  . ALA A 1 98  ? 2.94816   6.94717  5.48585  1.000 17.14432  ? 95  ALA A HB1  1 
ATOM   1761 H HB2  . ALA A 1 98  ? 2.42973   8.12591  4.55563  1.000 17.14432  ? 95  ALA A HB2  1 
ATOM   1762 H HB3  . ALA A 1 98  ? 3.93803   8.11213  5.05397  1.000 17.14432  ? 95  ALA A HB3  1 
ATOM   1763 N N    . GLU A 1 99  ? 4.63848   8.80727  7.89348  1.000 10.15570  ? 96  GLU A N    1 
ATOM   1764 C CA   . GLU A 1 99  ? 5.48874   8.46050  9.02824  1.000 10.05428  ? 96  GLU A CA   1 
ATOM   1765 C C    . GLU A 1 99  ? 4.84525   8.89230  10.33603 1.000 8.79111   ? 96  GLU A C    1 
ATOM   1766 O O    . GLU A 1 99  ? 4.84452   8.14096  11.31882 1.000 9.83075   ? 96  GLU A O    1 
ATOM   1767 C CB   . GLU A 1 99  ? 6.85524   9.12798  8.84972  1.000 11.50766  ? 96  GLU A CB   1 
ATOM   1768 C CG   . GLU A 1 99  ? 7.86821   8.84918  9.95397  1.000 13.93397  ? 96  GLU A CG   1 
ATOM   1769 C CD   . GLU A 1 99  ? 9.19983   9.55824  9.73192  1.000 15.25263  ? 96  GLU A CD   1 
ATOM   1770 O OE1  . GLU A 1 99  ? 9.27808   10.45555 8.86417  1.000 17.60074  ? 96  GLU A OE1  1 
ATOM   1771 O OE2  . GLU A 1 99  ? 10.17507  9.21345  10.43005 1.000 16.73171  ? 96  GLU A OE2  1 
ATOM   1772 H H    . GLU A 1 99  ? 4.98231   9.38827  7.36073  1.000 12.18683  ? 96  GLU A H    1 
ATOM   1773 H HA   . GLU A 1 99  ? 5.61736   7.49968  9.06266  1.000 12.06514  ? 96  GLU A HA   1 
ATOM   1774 H HB2  . GLU A 1 99  ? 7.24171   8.81470  8.01702  1.000 13.80920  ? 96  GLU A HB2  1 
ATOM   1775 H HB3  . GLU A 1 99  ? 6.72368   10.08835 8.81381  1.000 13.80920  ? 96  GLU A HB3  1 
ATOM   1776 H HG2  . GLU A 1 99  ? 7.50443   9.15394  10.79995 1.000 16.72077  ? 96  GLU A HG2  1 
ATOM   1777 H HG3  . GLU A 1 99  ? 8.03980   7.89520  9.99103  1.000 16.72077  ? 96  GLU A HG3  1 
ATOM   1778 N N    . LEU A 1 100 ? 4.28363   10.10323 10.36123 1.000 8.97750   ? 97  LEU A N    1 
ATOM   1779 C CA   . LEU A 1 100 ? 3.56717   10.57692 11.53796 1.000 9.10439   ? 97  LEU A CA   1 
ATOM   1780 C C    . LEU A 1 100 ? 2.41633   9.64522  11.89368 1.000 8.97113   ? 97  LEU A C    1 
ATOM   1781 O O    . LEU A 1 100 ? 2.22796   9.28922  13.06168 1.000 9.57449   ? 97  LEU A O    1 
ATOM   1782 C CB   . LEU A 1 100 ? 3.03458   11.98287 11.26740 1.000 10.01780  ? 97  LEU A CB   1 
ATOM   1783 C CG   . LEU A 1 100 ? 4.07297   13.06956 10.99290 1.000 8.90370   ? 97  LEU A CG   1 
ATOM   1784 C CD1  . LEU A 1 100 ? 3.38959   14.28650 10.39112 1.000 8.96514   ? 97  LEU A CD1  1 
ATOM   1785 C CD2  . LEU A 1 100 ? 4.82814   13.43590 12.26125 1.000 9.59986   ? 97  LEU A CD2  1 
ATOM   1786 H H    . LEU A 1 100 ? 4.30459   10.66565 9.71096  1.000 10.77300  ? 97  LEU A H    1 
ATOM   1787 H HA   . LEU A 1 100 ? 4.17805   10.60555 12.29090 1.000 10.92527  ? 97  LEU A HA   1 
ATOM   1788 H HB2  . LEU A 1 100 ? 2.45619   11.93966 10.48990 1.000 12.02136  ? 97  LEU A HB2  1 
ATOM   1789 H HB3  . LEU A 1 100 ? 2.52624   12.26523 12.04377 1.000 12.02136  ? 97  LEU A HB3  1 
ATOM   1790 H HG   . LEU A 1 100 ? 4.72798   12.73873 10.35854 1.000 10.68444  ? 97  LEU A HG   1 
ATOM   1791 H HD11 . LEU A 1 100 ? 4.06681   14.90905 10.08339 1.000 10.75817  ? 97  LEU A HD11 1 
ATOM   1792 H HD12 . LEU A 1 100 ? 2.83807   14.00247 9.64543  1.000 10.75817  ? 97  LEU A HD12 1 
ATOM   1793 H HD13 . LEU A 1 100 ? 2.83790   14.70655 11.06943 1.000 10.75817  ? 97  LEU A HD13 1 
ATOM   1794 H HD21 . LEU A 1 100 ? 5.38158   14.21300 12.08597 1.000 11.51983  ? 97  LEU A HD21 1 
ATOM   1795 H HD22 . LEU A 1 100 ? 4.18883   13.63652 12.96263 1.000 11.51983  ? 97  LEU A HD22 1 
ATOM   1796 H HD23 . LEU A 1 100 ? 5.38441   12.68638 12.52522 1.000 11.51983  ? 97  LEU A HD23 1 
ATOM   1797 N N    . GLU A 1 101 ? 1.61335   9.26079  10.90036 1.000 10.47235  ? 98  GLU A N    1 
ATOM   1798 C CA   A GLU A 1 101 ? 0.46862   8.41037  11.20299 0.497 10.80361  ? 98  GLU A CA   1 
ATOM   1799 C CA   B GLU A 1 101 ? 0.46568   8.39796  11.16098 0.503 10.85361  ? 98  GLU A CA   1 
ATOM   1800 C C    . GLU A 1 101 ? 0.90238   7.01307  11.62271 1.000 10.32340  ? 98  GLU A C    1 
ATOM   1801 O O    . GLU A 1 101 ? 0.24374   6.39270  12.46572 1.000 9.77055   ? 98  GLU A O    1 
ATOM   1802 C CB   A GLU A 1 101 ? -0.48883  8.37087  10.01597 0.497 13.96361  ? 98  GLU A CB   1 
ATOM   1803 C CB   B GLU A 1 101 ? -0.39299  8.27103  9.90130  0.503 13.98361  ? 98  GLU A CB   1 
ATOM   1804 C CG   A GLU A 1 101 ? -1.14744  9.71320  9.75019  0.497 17.82361  ? 98  GLU A CG   1 
ATOM   1805 C CG   B GLU A 1 101 ? -1.08758  9.55000  9.47832  0.503 17.75361  ? 98  GLU A CG   1 
ATOM   1806 C CD   A GLU A 1 101 ? -2.26328  9.63104  8.73310  0.497 22.71361  ? 98  GLU A CD   1 
ATOM   1807 C CD   B GLU A 1 101 ? -2.29464  9.28849  8.59859  0.503 22.75361  ? 98  GLU A CD   1 
ATOM   1808 O OE1  A GLU A 1 101 ? -2.40032  8.57331  8.08299  0.497 22.06361  ? 98  GLU A OE1  1 
ATOM   1809 O OE1  B GLU A 1 101 ? -2.11448  8.88124  7.43177  0.503 21.97361  ? 98  GLU A OE1  1 
ATOM   1810 O OE2  A GLU A 1 101 ? -3.00400  10.62706 8.58622  0.497 29.00361  ? 98  GLU A OE2  1 
ATOM   1811 O OE2  B GLU A 1 101 ? -3.43077  9.47631  9.08246  0.503 29.21361  ? 98  GLU A OE2  1 
ATOM   1812 H H    A GLU A 1 101 ? 1.70760   9.47214  10.07208 0.497 12.56681  ? 98  GLU A H    1 
ATOM   1813 H H    B GLU A 1 101 ? 1.71089   9.48381  10.07553 0.503 12.56681  ? 98  GLU A H    1 
ATOM   1814 H HA   A GLU A 1 101 ? -0.02196  8.79177  11.94782 0.497 12.96433  ? 98  GLU A HA   1 
ATOM   1815 H HA   B GLU A 1 101 ? -0.06682  8.80413  11.86267 0.503 13.02433  ? 98  GLU A HA   1 
ATOM   1816 H HB2  A GLU A 1 101 ? 0.00419   8.11507  9.22073  0.497 16.75633  ? 98  GLU A HB2  1 
ATOM   1817 H HB2  B GLU A 1 101 ? 0.17590   7.99080  9.16731  0.503 16.78033  ? 98  GLU A HB2  1 
ATOM   1818 H HB3  A GLU A 1 101 ? -1.18812  7.72306  10.19548 0.497 16.75633  ? 98  GLU A HB3  1 
ATOM   1819 H HB3  B GLU A 1 101 ? -1.07952  7.60487  10.06195 0.503 16.78033  ? 98  GLU A HB3  1 
ATOM   1820 H HG2  A GLU A 1 101 ? -1.52227  10.05021 10.57894 0.497 21.38833  ? 98  GLU A HG2  1 
ATOM   1821 H HG2  B GLU A 1 101 ? -1.38811  10.02451 10.26916 0.503 21.30433  ? 98  GLU A HG2  1 
ATOM   1822 H HG3  A GLU A 1 101 ? -0.47988  10.33075 9.41270  0.497 21.38833  ? 98  GLU A HG3  1 
ATOM   1823 H HG3  B GLU A 1 101 ? -0.46383  10.09967 8.97862  0.503 21.30433  ? 98  GLU A HG3  1 
ATOM   1824 N N    . ALA A 1 102 ? 2.00228   6.50560  11.06902 1.000 9.70593   ? 99  ALA A N    1 
ATOM   1825 C CA   . ALA A 1 102 ? 2.47186   5.18711  11.47383 1.000 9.27008   ? 99  ALA A CA   1 
ATOM   1826 C C    . ALA A 1 102 ? 2.84375   5.17038  12.95139 1.000 9.58175   ? 99  ALA A C    1 
ATOM   1827 O O    . ALA A 1 102 ? 2.58613   4.18352  13.64920 1.000 10.37180  ? 99  ALA A O    1 
ATOM   1828 C CB   . ALA A 1 102 ? 3.65409   4.76197  10.60598 1.000 11.27039  ? 99  ALA A CB   1 
ATOM   1829 H H    . ALA A 1 102 ? 2.48233   6.89564  10.47151 1.000 11.64711  ? 99  ALA A H    1 
ATOM   1830 H HA   . ALA A 1 102 ? 1.76108   4.54117  11.33804 1.000 11.12410  ? 99  ALA A HA   1 
ATOM   1831 H HB1  . ALA A 1 102 ? 3.95516   3.88477  10.89020 1.000 13.52446  ? 99  ALA A HB1  1 
ATOM   1832 H HB2  . ALA A 1 102 ? 3.37002   4.72992  9.67906  1.000 13.52446  ? 99  ALA A HB2  1 
ATOM   1833 H HB3  . ALA A 1 102 ? 4.37062   5.40743  10.71022 1.000 13.52446  ? 99  ALA A HB3  1 
ATOM   1834 N N    . LEU A 1 103 ? 3.43418   6.26004  13.45304 1.000 8.91402   ? 100 LEU A N    1 
ATOM   1835 C CA   . LEU A 1 103 ? 3.80283   6.30822  14.86592 1.000 10.30143  ? 100 LEU A CA   1 
ATOM   1836 C C    . LEU A 1 103 ? 2.56850   6.33254  15.75824 1.000 8.56640   ? 100 LEU A C    1 
ATOM   1837 O O    . LEU A 1 103 ? 2.55523   5.70351  16.82261 1.000 8.79280   ? 100 LEU A O    1 
ATOM   1838 C CB   . LEU A 1 103 ? 4.69275   7.51603  15.14461 1.000 10.01007  ? 100 LEU A CB   1 
ATOM   1839 C CG   . LEU A 1 103 ? 6.09486   7.42297  14.54288 1.000 12.23766  ? 100 LEU A CG   1 
ATOM   1840 C CD1  . LEU A 1 103 ? 6.79281   8.77003  14.62869 1.000 13.85675  ? 100 LEU A CD1  1 
ATOM   1841 C CD2  . LEU A 1 103 ? 6.91766   6.34410  15.23802 1.000 15.31683  ? 100 LEU A CD2  1 
ATOM   1842 H H    . LEU A 1 103 ? 3.62728   6.96827  13.00502 1.000 10.69683  ? 100 LEU A H    1 
ATOM   1843 H HA   . LEU A 1 103 ? 4.31311   5.51117  15.07861 1.000 12.36172  ? 100 LEU A HA   1 
ATOM   1844 H HB2  . LEU A 1 103 ? 4.26635   8.30492  14.77484 1.000 12.01208  ? 100 LEU A HB2  1 
ATOM   1845 H HB3  . LEU A 1 103 ? 4.79112   7.61137  16.10489 1.000 12.01208  ? 100 LEU A HB3  1 
ATOM   1846 H HG   . LEU A 1 103 ? 6.02045   7.17607  13.60778 1.000 14.68519  ? 100 LEU A HG   1 
ATOM   1847 H HD11 . LEU A 1 103 ? 7.66888   8.69849  14.21847 1.000 16.62811  ? 100 LEU A HD11 1 
ATOM   1848 H HD12 . LEU A 1 103 ? 6.26091   9.43175  14.15952 1.000 16.62811  ? 100 LEU A HD12 1 
ATOM   1849 H HD13 . LEU A 1 103 ? 6.88378   9.01971  15.56158 1.000 16.62811  ? 100 LEU A HD13 1 
ATOM   1850 H HD21 . LEU A 1 103 ? 7.83710   6.40362  14.93471 1.000 18.38019  ? 100 LEU A HD21 1 
ATOM   1851 H HD22 . LEU A 1 103 ? 6.87599   6.48395  16.19698 1.000 18.38019  ? 100 LEU A HD22 1 
ATOM   1852 H HD23 . LEU A 1 103 ? 6.55122   5.47428  15.01436 1.000 18.38019  ? 100 LEU A HD23 1 
ATOM   1853 N N    . ARG A 1 104 ? 1.51357   7.02995  15.33057 1.000 8.23068   ? 101 ARG A N    1 
ATOM   1854 C CA   . ARG A 1 104 ? 0.26581   7.02025  16.08686 1.000 8.76740   ? 101 ARG A CA   1 
ATOM   1855 C C    . ARG A 1 104 ? -0.27492  5.60118  16.22549 1.000 7.89076   ? 101 ARG A C    1 
ATOM   1856 O O    . ARG A 1 104 ? -0.67500  5.18032  17.31663 1.000 9.76749   ? 101 ARG A O    1 
ATOM   1857 C CB   . ARG A 1 104 ? -0.75818  7.92786  15.40575 1.000 7.99953   ? 101 ARG A CB   1 
ATOM   1858 C CG   . ARG A 1 104 ? -2.12541  7.91634  16.07086 1.000 9.08278   ? 101 ARG A CG   1 
ATOM   1859 C CD   . ARG A 1 104 ? -3.09645  8.83758  15.35609 1.000 9.17592   ? 101 ARG A CD   1 
ATOM   1860 N NE   . ARG A 1 104 ? -3.38706  8.36844  14.00777 1.000 9.86000   ? 101 ARG A NE   1 
ATOM   1861 C CZ   . ARG A 1 104 ? -4.12772  9.02727  13.12859 1.000 11.13324  ? 101 ARG A CZ   1 
ATOM   1862 N NH1  . ARG A 1 104 ? -4.68438  10.18943 13.42997 1.000 12.84618  ? 101 ARG A NH1  1 
ATOM   1863 N NH2  . ARG A 1 104 ? -4.30879  8.51008  11.91682 1.000 11.24576  ? 101 ARG A NH2  1 
ATOM   1864 H H    . ARG A 1 104 ? 1.49639   7.50889  14.61648 1.000 9.87681   ? 101 ARG A H    1 
ATOM   1865 H HA   . ARG A 1 104 ? 0.43061   7.36701  16.97764 1.000 10.52088  ? 101 ARG A HA   1 
ATOM   1866 H HB2  . ARG A 1 104 ? -0.42763  8.83962  15.42415 1.000 9.59943   ? 101 ARG A HB2  1 
ATOM   1867 H HB3  . ARG A 1 104 ? -0.87279  7.63498  14.48816 1.000 9.59943   ? 101 ARG A HB3  1 
ATOM   1868 H HG2  . ARG A 1 104 ? -2.48622  7.01620  16.04899 1.000 10.89934  ? 101 ARG A HG2  1 
ATOM   1869 H HG3  . ARG A 1 104 ? -2.03904  8.21692  16.98906 1.000 10.89934  ? 101 ARG A HG3  1 
ATOM   1870 H HD2  . ARG A 1 104 ? -3.92913  8.87319  15.85235 1.000 11.01111  ? 101 ARG A HD2  1 
ATOM   1871 H HD3  . ARG A 1 104 ? -2.70954  9.72485  15.29316 1.000 11.01111  ? 101 ARG A HD3  1 
ATOM   1872 H HE   . ARG A 1 104 ? -3.05538  7.61267  13.76612 1.000 11.83201  ? 101 ARG A HE   1 
ATOM   1873 H HH11 . ARG A 1 104 ? -4.56868  10.53217 14.21019 1.000 15.41542  ? 101 ARG A HH11 1 
ATOM   1874 H HH12 . ARG A 1 104 ? -5.16184  10.60193 12.84561 1.000 15.41542  ? 101 ARG A HH12 1 
ATOM   1875 H HH21 . ARG A 1 104 ? -3.94715  7.75712  11.71223 1.000 13.49491  ? 101 ARG A HH21 1 
ATOM   1876 H HH22 . ARG A 1 104 ? -4.78752  8.92860  11.33781 1.000 13.49491  ? 101 ARG A HH22 1 
ATOM   1877 N N    . SER A 1 105 ? -0.28789  4.84478  15.12463 1.000 9.19006   ? 102 SER A N    1 
ATOM   1878 C CA   . SER A 1 105 ? -0.77050  3.46715  15.16762 1.000 10.08416  ? 102 SER A CA   1 
ATOM   1879 C C    . SER A 1 105 ? 0.15706   2.58022  15.98892 1.000 9.46569   ? 102 SER A C    1 
ATOM   1880 O O    . SER A 1 105 ? -0.29658  1.78788  16.82412 1.000 10.43765  ? 102 SER A O    1 
ATOM   1881 C CB   . SER A 1 105 ? -0.88757  2.92046  13.74396 1.000 11.50545  ? 102 SER A CB   1 
ATOM   1882 O OG   . SER A 1 105 ? -2.03719  3.42717  13.09858 1.000 12.02079  ? 102 SER A OG   1 
ATOM   1883 H H    . SER A 1 105 ? -0.02471  5.10448  14.34817 1.000 11.02807  ? 102 SER A H    1 
ATOM   1884 H HA   . SER A 1 105 ? -1.64709  3.45782  15.58284 1.000 12.10100  ? 102 SER A HA   1 
ATOM   1885 H HB2  . SER A 1 105 ? -0.10172  3.18375  13.23995 1.000 13.80654  ? 102 SER A HB2  1 
ATOM   1886 H HB3  . SER A 1 105 ? -0.94850  1.95313  13.78214 1.000 13.80654  ? 102 SER A HB3  1 
ATOM   1887 H HG   . SER A 1 105 ? -2.04798  3.18077  12.29560 1.000 14.42495  ? 102 SER A HG   1 
ATOM   1888 N N    . THR A 1 106 ? 1.46453   2.70504  15.76214 1.000 9.73895   ? 103 THR A N    1 
ATOM   1889 C CA   . THR A 1 106 ? 2.42903   1.83884  16.43027 1.000 10.13685  ? 103 THR A CA   1 
ATOM   1890 C C    . THR A 1 106 ? 2.31660   1.93746  17.94314 1.000 9.30897   ? 103 THR A C    1 
ATOM   1891 O O    . THR A 1 106 ? 2.32588   0.91920  18.64415 1.000 10.14477  ? 103 THR A O    1 
ATOM   1892 C CB   . THR A 1 106 ? 3.83577   2.21299  15.97178 1.000 11.84412  ? 103 THR A CB   1 
ATOM   1893 O OG1  . THR A 1 106 ? 4.00013   1.80895  14.61032 1.000 13.68813  ? 103 THR A OG1  1 
ATOM   1894 C CG2  . THR A 1 106 ? 4.88283   1.53458  16.82088 1.000 11.95146  ? 103 THR A CG2  1 
ATOM   1895 H H    . THR A 1 106 ? 1.81619   3.28062  15.22862 1.000 11.68674  ? 103 THR A H    1 
ATOM   1896 H HA   . THR A 1 106 ? 2.25068   0.91756  16.18462 1.000 12.16422  ? 103 THR A HA   1 
ATOM   1897 H HB   . THR A 1 106 ? 3.96040   3.17130  16.05545 1.000 14.21294  ? 103 THR A HB   1 
ATOM   1898 H HG1  . THR A 1 106 ? 3.36937   2.10871  14.14353 1.000 16.42576  ? 103 THR A HG1  1 
ATOM   1899 H HG21 . THR A 1 106 ? 5.71708   1.47003  16.33021 1.000 14.34175  ? 103 THR A HG21 1 
ATOM   1900 H HG22 . THR A 1 106 ? 5.03344   2.04447  17.63220 1.000 14.34175  ? 103 THR A HG22 1 
ATOM   1901 H HG23 . THR A 1 106 ? 4.58849   0.64184  17.06022 1.000 14.34175  ? 103 THR A HG23 1 
ATOM   1902 N N    . PHE A 1 107 ? 2.23402   3.15240  18.47008 1.000 9.48039   ? 104 PHE A N    1 
ATOM   1903 C CA   . PHE A 1 107 ? 2.15677   3.35943  19.90864 1.000 9.01736   ? 104 PHE A CA   1 
ATOM   1904 C C    . PHE A 1 107 ? 0.72812   3.52727  20.40535 1.000 10.26316  ? 104 PHE A C    1 
ATOM   1905 O O    . PHE A 1 107 ? 0.52315   3.75316  21.60182 1.000 12.75690  ? 104 PHE A O    1 
ATOM   1906 C CB   . PHE A 1 107 ? 3.03186   4.54967  20.31125 1.000 9.09072   ? 104 PHE A CB   1 
ATOM   1907 C CG   . PHE A 1 107 ? 4.50058   4.34734  20.00528 1.000 9.10172   ? 104 PHE A CG   1 
ATOM   1908 C CD1  . PHE A 1 107 ? 5.21493   3.33846  20.63073 1.000 9.20811   ? 104 PHE A CD1  1 
ATOM   1909 C CD2  . PHE A 1 107 ? 5.16172   5.15421  19.09145 1.000 11.53833  ? 104 PHE A CD2  1 
ATOM   1910 C CE1  . PHE A 1 107 ? 6.55502   3.13846  20.35728 1.000 11.19151  ? 104 PHE A CE1  1 
ATOM   1911 C CE2  . PHE A 1 107 ? 6.50645   4.95974  18.82116 1.000 11.58449  ? 104 PHE A CE2  1 
ATOM   1912 C CZ   . PHE A 1 107 ? 7.19955   3.94909  19.45409 1.000 12.32798  ? 104 PHE A CZ   1 
ATOM   1913 H H    . PHE A 1 107 ? 2.22095   3.87890  18.01005 1.000 11.37647  ? 104 PHE A H    1 
ATOM   1914 H HA   . PHE A 1 107 ? 2.51620   2.58266  20.36508 1.000 10.82084  ? 104 PHE A HA   1 
ATOM   1915 H HB2  . PHE A 1 107 ? 2.73288   5.33583  19.82807 1.000 10.90886  ? 104 PHE A HB2  1 
ATOM   1916 H HB3  . PHE A 1 107 ? 2.94410   4.69401  21.26642 1.000 10.90886  ? 104 PHE A HB3  1 
ATOM   1917 H HD1  . PHE A 1 107 ? 4.78593   2.78690  21.24444 1.000 11.04974  ? 104 PHE A HD1  1 
ATOM   1918 H HD2  . PHE A 1 107 ? 4.69785   5.83243  18.65585 1.000 13.84600  ? 104 PHE A HD2  1 
ATOM   1919 H HE1  . PHE A 1 107 ? 7.02016   2.45568  20.78430 1.000 13.42981  ? 104 PHE A HE1  1 
ATOM   1920 H HE2  . PHE A 1 107 ? 6.94234   5.51124  18.21227 1.000 13.90139  ? 104 PHE A HE2  1 
ATOM   1921 H HZ   . PHE A 1 107 ? 8.10144   3.81651  19.26994 1.000 14.79358  ? 104 PHE A HZ   1 
ATOM   1922 N N    . GLY A 1 108 ? -0.26696  3.39259  19.52931 1.000 9.21589   ? 105 GLY A N    1 
ATOM   1923 C CA   . GLY A 1 108 ? -1.64806  3.46207  19.94685 1.000 11.54621  ? 105 GLY A CA   1 
ATOM   1924 C C    . GLY A 1 108 ? -2.00259  4.76565  20.63697 1.000 10.48539  ? 105 GLY A C    1 
ATOM   1925 O O    . GLY A 1 108 ? -2.66039  4.76167  21.67770 1.000 11.20337  ? 105 GLY A O    1 
ATOM   1926 H H    . GLY A 1 108 ? -0.15931  3.25998  18.68645 1.000 11.05907  ? 105 GLY A H    1 
ATOM   1927 H HA2  . GLY A 1 108 ? -2.21967  3.36728  19.16892 1.000 13.85545  ? 105 GLY A HA2  1 
ATOM   1928 H HA3  . GLY A 1 108 ? -1.83004  2.73526  20.56290 1.000 13.85545  ? 105 GLY A HA3  1 
ATOM   1929 N N    . VAL A 1 109 ? -1.57258  5.88663  20.05689 1.000 9.55628   ? 106 VAL A N    1 
ATOM   1930 C CA   . VAL A 1 109 ? -1.70971  7.19260  20.70182 1.000 8.87268   ? 106 VAL A CA   1 
ATOM   1931 C C    . VAL A 1 109 ? -3.12550  7.70174  20.45437 1.000 7.85012   ? 106 VAL A C    1 
ATOM   1932 O O    . VAL A 1 109 ? -3.46214  8.19018  19.37284 1.000 11.34485  ? 106 VAL A O    1 
ATOM   1933 C CB   . VAL A 1 109 ? -0.64570  8.18729  20.23727 1.000 10.14274  ? 106 VAL A CB   1 
ATOM   1934 C CG1  . VAL A 1 109 ? -0.83195  9.52754  20.93215 1.000 10.96459  ? 106 VAL A CG1  1 
ATOM   1935 C CG2  . VAL A 1 109 ? 0.72791   7.63631  20.54079 1.000 11.00930  ? 106 VAL A CG2  1 
ATOM   1936 H H    . VAL A 1 109 ? -1.19545  5.91663  19.28458 1.000 11.46754  ? 106 VAL A H    1 
ATOM   1937 H HA   . VAL A 1 109 ? -1.60743  7.07330  21.65901 1.000 10.64721  ? 106 VAL A HA   1 
ATOM   1938 H HB   . VAL A 1 109 ? -0.73110  8.32492  19.28088 1.000 12.17128  ? 106 VAL A HB   1 
ATOM   1939 H HG11 . VAL A 1 109 ? -0.06326  10.08918 20.74623 1.000 13.15751  ? 106 VAL A HG11 1 
ATOM   1940 H HG12 . VAL A 1 109 ? -1.63837  9.94848  20.59541 1.000 13.15751  ? 106 VAL A HG12 1 
ATOM   1941 H HG13 . VAL A 1 109 ? -0.91023  9.37969  21.88762 1.000 13.15751  ? 106 VAL A HG13 1 
ATOM   1942 H HG21 . VAL A 1 109 ? 1.39556   8.28611  20.27078 1.000 13.21116  ? 106 VAL A HG21 1 
ATOM   1943 H HG22 . VAL A 1 109 ? 0.79699   7.46742  21.49347 1.000 13.21116  ? 106 VAL A HG22 1 
ATOM   1944 H HG23 . VAL A 1 109 ? 0.85255   6.80989  20.04845 1.000 13.21116  ? 106 VAL A HG23 1 
ATOM   1945 N N    . GLU A 1 110 ? -3.94904  7.60523  21.48787 1.000 8.91545   ? 107 GLU A N    1 
ATOM   1946 C CA   . GLU A 1 110 ? -5.33423  8.01425  21.42928 1.000 8.96397   ? 107 GLU A CA   1 
ATOM   1947 C C    . GLU A 1 110 ? -5.53715  9.47299  21.78841 1.000 8.67403   ? 107 GLU A C    1 
ATOM   1948 O O    . GLU A 1 110 ? -6.61549  10.00149 21.52128 1.000 12.03904  ? 107 GLU A O    1 
ATOM   1949 C CB   . GLU A 1 110 ? -6.15107  7.18226  22.42664 1.000 12.16055  ? 107 GLU A CB   1 
ATOM   1950 C CG   . GLU A 1 110 ? -6.08565  5.68661  22.19263 1.000 17.10210  ? 107 GLU A CG   1 
ATOM   1951 C CD   . GLU A 1 110 ? -6.57010  4.86834  23.38119 1.000 20.99734  ? 107 GLU A CD   1 
ATOM   1952 O OE1  . GLU A 1 110 ? -7.06765  5.44569  24.37215 1.000 23.06645  ? 107 GLU A OE1  1 
ATOM   1953 O OE2  . GLU A 1 110 ? -6.44649  3.63067  23.32093 1.000 25.62782  ? 107 GLU A OE2  1 
ATOM   1954 H H    . GLU A 1 110 ? -3.71792  7.29578  22.25626 1.000 10.69855  ? 107 GLU A H    1 
ATOM   1955 H HA   . GLU A 1 110 ? -5.66060  7.86425  20.52824 1.000 10.75676  ? 107 GLU A HA   1 
ATOM   1956 H HB2  . GLU A 1 110 ? -5.81654  7.35460  23.32067 1.000 14.59266  ? 107 GLU A HB2  1 
ATOM   1957 H HB3  . GLU A 1 110 ? -7.08152  7.44904  22.36342 1.000 14.59266  ? 107 GLU A HB3  1 
ATOM   1958 H HG2  . GLU A 1 110 ? -6.64315  5.46346  21.43086 1.000 20.52252  ? 107 GLU A HG2  1 
ATOM   1959 H HG3  . GLU A 1 110 ? -5.16541  5.43674  22.01479 1.000 20.52252  ? 107 GLU A HG3  1 
ATOM   1960 N N    . THR A 1 111 ? -4.53353  10.13652 22.36294 1.000 8.53920   ? 108 THR A N    1 
ATOM   1961 C CA   A THR A 1 111 ? -4.72775  11.48728 22.86296 0.533 9.81361   ? 108 THR A CA   1 
ATOM   1962 C CA   B THR A 1 111 ? -4.70915  11.45919 22.94847 0.467 8.84361   ? 108 THR A CA   1 
ATOM   1963 C C    . THR A 1 111 ? -3.41149  12.24667 22.84824 1.000 8.57632   ? 108 THR A C    1 
ATOM   1964 O O    . THR A 1 111 ? -2.32459  11.66607 22.89117 1.000 9.59567   ? 108 THR A O    1 
ATOM   1965 C CB   A THR A 1 111 ? -5.31830  11.45938 24.28307 0.533 13.49361  ? 108 THR A CB   1 
ATOM   1966 C CB   B THR A 1 111 ? -5.06706  11.31404 24.43858 0.467 10.35361  ? 108 THR A CB   1 
ATOM   1967 O OG1  A THR A 1 111 ? -5.76006  12.77185 24.65484 0.533 16.57361  ? 108 THR A OG1  1 
ATOM   1968 O OG1  B THR A 1 111 ? -6.18735  10.43276 24.58483 0.467 12.32361  ? 108 THR A OG1  1 
ATOM   1969 C CG2  A THR A 1 111 ? -4.28510  10.96614 25.28374 0.533 12.54361  ? 108 THR A CG2  1 
ATOM   1970 C CG2  B THR A 1 111 ? -5.40217  12.65684 25.05876 0.467 12.07361  ? 108 THR A CG2  1 
ATOM   1971 H H    A THR A 1 111 ? -3.73946  9.82474  22.47175 0.533 10.24704  ? 108 THR A H    1 
ATOM   1972 H H    B THR A 1 111 ? -3.73052  9.83514  22.42576 0.467 10.24704  ? 108 THR A H    1 
ATOM   1973 H HA   A THR A 1 111 ? -5.33473  11.96468 22.27596 0.533 11.77633  ? 108 THR A HA   1 
ATOM   1974 H HA   B THR A 1 111 ? -5.39778  11.94137 22.46454 0.467 10.61233  ? 108 THR A HA   1 
ATOM   1975 H HB   A THR A 1 111 ? -6.07472  10.85248 24.30327 0.533 16.19233  ? 108 THR A HB   1 
ATOM   1976 H HB   B THR A 1 111 ? -4.30149  10.94966 24.90977 0.467 12.42433  ? 108 THR A HB   1 
ATOM   1977 H HG1  A THR A 1 111 ? -6.40769  13.00422 24.17299 0.533 19.88833  ? 108 THR A HG1  1 
ATOM   1978 H HG1  B THR A 1 111 ? -6.41859  10.39347 25.39141 0.467 14.78833  ? 108 THR A HG1  1 
ATOM   1979 H HG21 A THR A 1 111 ? -4.71004  10.78267 26.13618 0.533 15.05233  ? 108 THR A HG21 1 
ATOM   1980 H HG21 B THR A 1 111 ? -5.81091  12.52766 25.92890 0.467 14.48833  ? 108 THR A HG21 1 
ATOM   1981 H HG22 A THR A 1 111 ? -3.86940  10.15265 24.95767 0.533 15.05233  ? 108 THR A HG22 1 
ATOM   1982 H HG22 B THR A 1 111 ? -4.59479  13.18380 25.16534 0.467 14.48833  ? 108 THR A HG22 1 
ATOM   1983 H HG23 A THR A 1 111 ? -3.59959  11.64026 25.41235 0.533 15.05233  ? 108 THR A HG23 1 
ATOM   1984 H HG23 B THR A 1 111 ? -6.02071  13.14030 24.48906 0.467 14.48833  ? 108 THR A HG23 1 
ATOM   1985 N N    . ILE A 1 112 ? -3.53555  13.57057 22.74928 1.000 8.09553   ? 109 ILE A N    1 
ATOM   1986 C CA   . ILE A 1 112 ? -2.40215  14.48352 22.88820 1.000 7.61542   ? 109 ILE A CA   1 
ATOM   1987 C C    . ILE A 1 112 ? -2.71571  15.50283 23.97795 1.000 7.47785   ? 109 ILE A C    1 
ATOM   1988 O O    . ILE A 1 112 ? -3.89026  15.83830 24.18856 1.000 9.42950   ? 109 ILE A O    1 
ATOM   1989 C CB   . ILE A 1 112 ? -2.06867  15.20638 21.57285 1.000 7.63528   ? 109 ILE A CB   1 
ATOM   1990 C CG1  . ILE A 1 112 ? -3.30209  15.90558 20.99854 1.000 8.79116   ? 109 ILE A CG1  1 
ATOM   1991 C CG2  . ILE A 1 112 ? -1.47649  14.23145 20.57380 1.000 9.55863   ? 109 ILE A CG2  1 
ATOM   1992 C CD1  . ILE A 1 112 ? -2.96633  16.87582 19.87426 1.000 9.64828   ? 109 ILE A CD1  1 
ATOM   1993 H H    . ILE A 1 112 ? -4.28118  13.97186 22.59897 1.000 9.71464   ? 109 ILE A H    1 
ATOM   1994 H HA   . ILE A 1 112 ? -1.63065  13.95770 23.15124 1.000 9.13851   ? 109 ILE A HA   1 
ATOM   1995 H HB   . ILE A 1 112 ? -1.40868  15.89143 21.76264 1.000 9.16233   ? 109 ILE A HB   1 
ATOM   1996 H HG12 . ILE A 1 112 ? -3.90764  15.23549 20.64472 1.000 10.54939  ? 109 ILE A HG12 1 
ATOM   1997 H HG13 . ILE A 1 112 ? -3.73798  16.40630 21.70578 1.000 10.54939  ? 109 ILE A HG13 1 
ATOM   1998 H HG21 . ILE A 1 112 ? -1.28401  14.70309 19.74832 1.000 11.47035  ? 109 ILE A HG21 1 
ATOM   1999 H HG22 . ILE A 1 112 ? -0.65899  13.86042 20.94112 1.000 11.47035  ? 109 ILE A HG22 1 
ATOM   2000 H HG23 . ILE A 1 112 ? -2.11648  13.52170 20.40774 1.000 11.47035  ? 109 ILE A HG23 1 
ATOM   2001 H HD11 . ILE A 1 112 ? -3.75328  17.40380 19.66722 1.000 11.57793  ? 109 ILE A HD11 1 
ATOM   2002 H HD12 . ILE A 1 112 ? -2.24503  17.45649 20.16312 1.000 11.57793  ? 109 ILE A HD12 1 
ATOM   2003 H HD13 . ILE A 1 112 ? -2.69178  16.37092 19.09286 1.000 11.57793  ? 109 ILE A HD13 1 
ATOM   2004 N N    . PRO A 1 113 ? -1.70206  16.05221 24.66498 1.000 7.70828   ? 110 PRO A N    1 
ATOM   2005 C CA   . PRO A 1 113 ? -0.27357  15.73810 24.50947 1.000 8.69383   ? 110 PRO A CA   1 
ATOM   2006 C C    . PRO A 1 113 ? 0.08794   14.38037 25.10516 1.000 9.19143   ? 110 PRO A C    1 
ATOM   2007 O O    . PRO A 1 113 ? -0.47048  13.97200 26.12454 1.000 9.48737   ? 110 PRO A O    1 
ATOM   2008 C CB   . PRO A 1 113 ? 0.41581   16.89181 25.25101 1.000 9.94732   ? 110 PRO A CB   1 
ATOM   2009 C CG   . PRO A 1 113 ? -0.56420  17.28079 26.31983 1.000 7.84120   ? 110 PRO A CG   1 
ATOM   2010 C CD   . PRO A 1 113 ? -1.92954  17.08459 25.69762 1.000 7.74609   ? 110 PRO A CD   1 
ATOM   2011 H HA   . PRO A 1 113 ? -0.02395  15.76091 23.57242 1.000 10.43259  ? 110 PRO A HA   1 
ATOM   2012 H HB2  . PRO A 1 113 ? 1.25213   16.58743 25.63677 1.000 11.93678  ? 110 PRO A HB2  1 
ATOM   2013 H HB3  . PRO A 1 113 ? 0.58016   17.62849 24.64176 1.000 11.93678  ? 110 PRO A HB3  1 
ATOM   2014 H HG2  . PRO A 1 113 ? -0.45142  16.70804 27.09451 1.000 9.40944   ? 110 PRO A HG2  1 
ATOM   2015 H HG3  . PRO A 1 113 ? -0.42799  18.20800 26.57011 1.000 9.40944   ? 110 PRO A HG3  1 
ATOM   2016 H HD2  . PRO A 1 113 ? -2.56679  16.77345 26.35945 1.000 9.29531   ? 110 PRO A HD2  1 
ATOM   2017 H HD3  . PRO A 1 113 ? -2.24496  17.90889 25.29520 1.000 9.29531   ? 110 PRO A HD3  1 
ATOM   2018 N N    . THR A 1 114 ? 1.02445   13.67206 24.47143 1.000 8.52338   ? 111 THR A N    1 
ATOM   2019 C CA   . THR A 1 114 ? 1.54112   12.40285 24.96141 1.000 8.49330   ? 111 THR A CA   1 
ATOM   2020 C C    . THR A 1 114 ? 3.02611   12.33279 24.64472 1.000 8.92391   ? 111 THR A C    1 
ATOM   2021 O O    . THR A 1 114 ? 3.45207   12.76000 23.56826 1.000 8.20376   ? 111 THR A O    1 
ATOM   2022 C CB   . THR A 1 114 ? 0.83214   11.22511 24.25987 1.000 10.14775  ? 111 THR A CB   1 
ATOM   2023 O OG1  . THR A 1 114 ? -0.52165  11.12391 24.72259 1.000 12.71182  ? 111 THR A OG1  1 
ATOM   2024 C CG2  . THR A 1 114 ? 1.54983   9.89725  24.50095 1.000 10.70923  ? 111 THR A CG2  1 
ATOM   2025 H H    . THR A 1 114 ? 1.38574   13.91795 23.73075 1.000 10.22805  ? 111 THR A H    1 
ATOM   2026 H HA   . THR A 1 114 ? 1.41157   12.33460 25.92029 1.000 10.19196  ? 111 THR A HA   1 
ATOM   2027 H HB   . THR A 1 114 ? 0.84111   11.39134 23.30426 1.000 12.17731  ? 111 THR A HB   1 
ATOM   2028 H HG1  . THR A 1 114 ? -0.99071  11.72643 24.37253 1.000 15.25418  ? 111 THR A HG1  1 
ATOM   2029 H HG21 . THR A 1 114 ? 0.97503   9.15848  24.24654 1.000 12.85107  ? 111 THR A HG21 1 
ATOM   2030 H HG22 . THR A 1 114 ? 2.36320   9.85926  23.97381 1.000 12.85107  ? 111 THR A HG22 1 
ATOM   2031 H HG23 . THR A 1 114 ? 1.77857   9.80938  25.43949 1.000 12.85107  ? 111 THR A HG23 1 
ATOM   2032 N N    . VAL A 1 115 ? 3.81769   11.79088 25.56887 1.000 8.20479   ? 112 VAL A N    1 
ATOM   2033 C CA   A VAL A 1 115 ? 5.21124   11.46114 25.29099 0.716 9.05519   ? 112 VAL A CA   1 
ATOM   2034 C CA   B VAL A 1 115 ? 5.21310   11.46755 25.30399 0.284 9.05519   ? 112 VAL A CA   1 
ATOM   2035 C C    . VAL A 1 115 ? 5.40939   9.96623  25.48360 1.000 8.81003   ? 112 VAL A C    1 
ATOM   2036 O O    . VAL A 1 115 ? 5.08581   9.41499  26.54421 1.000 8.81841   ? 112 VAL A O    1 
ATOM   2037 C CB   A VAL A 1 115 ? 6.23065   12.27422 26.12011 0.716 11.77394  ? 112 VAL A CB   1 
ATOM   2038 C CB   B VAL A 1 115 ? 6.16002   12.25959 26.22495 0.284 11.77394  ? 112 VAL A CB   1 
ATOM   2039 C CG1  A VAL A 1 115 ? 6.28890   13.71369 25.61100 0.716 13.20306  ? 112 VAL A CG1  1 
ATOM   2040 C CG1  B VAL A 1 115 ? 7.50821   11.56656 26.34216 0.284 13.20306  ? 112 VAL A CG1  1 
ATOM   2041 C CG2  A VAL A 1 115 ? 5.92703   12.22127 27.59936 0.716 13.47678  ? 112 VAL A CG2  1 
ATOM   2042 C CG2  B VAL A 1 115 ? 6.33128   13.68008 25.70850 0.284 13.47678  ? 112 VAL A CG2  1 
ATOM   2043 H H    . VAL A 1 115 ? 3.56310   11.60549 26.36913 1.000 9.84574   ? 112 VAL A H    1 
ATOM   2044 H HA   . VAL A 1 115 ? 5.37987   11.67740 24.36056 1.000 10.86623  ? 112 VAL A HA   1 
ATOM   2045 H HB   A VAL A 1 115 ? 7.10727   11.87433 26.00824 0.716 14.12873  ? 112 VAL A HB   1 
ATOM   2046 H HB   B VAL A 1 115 ? 5.76975   12.30037 27.11204 0.284 14.12873  ? 112 VAL A HB   1 
ATOM   2047 H HG11 A VAL A 1 115 ? 6.92316   14.21336 26.14854 0.716 15.84367  ? 112 VAL A HG11 1 
ATOM   2048 H HG11 B VAL A 1 115 ? 8.15483   12.19277 26.70362 0.284 15.84367  ? 112 VAL A HG11 1 
ATOM   2049 H HG12 A VAL A 1 115 ? 6.57258   13.70936 24.68342 0.716 15.84367  ? 112 VAL A HG12 1 
ATOM   2050 H HG12 B VAL A 1 115 ? 7.42046   10.80314 26.93409 0.284 15.84367  ? 112 VAL A HG12 1 
ATOM   2051 H HG13 A VAL A 1 115 ? 5.40708   14.11089 25.68537 0.716 15.84367  ? 112 VAL A HG13 1 
ATOM   2052 H HG13 B VAL A 1 115 ? 7.78944   11.27193 25.46182 0.284 15.84367  ? 112 VAL A HG13 1 
ATOM   2053 H HG21 A VAL A 1 115 ? 6.61648   12.70481 28.08076 0.716 16.17213  ? 112 VAL A HG21 1 
ATOM   2054 H HG21 B VAL A 1 115 ? 6.92311   14.16397 26.30556 0.284 16.17213  ? 112 VAL A HG21 1 
ATOM   2055 H HG22 A VAL A 1 115 ? 5.06255   12.63119 27.75918 0.716 16.17213  ? 112 VAL A HG22 1 
ATOM   2056 H HG22 B VAL A 1 115 ? 6.71383   13.64826 24.81770 0.284 16.17213  ? 112 VAL A HG22 1 
ATOM   2057 H HG23 A VAL A 1 115 ? 5.91169   11.29460 27.88562 0.716 16.17213  ? 112 VAL A HG23 1 
ATOM   2058 H HG23 B VAL A 1 115 ? 5.46356   14.11272 25.68059 0.284 16.17213  ? 112 VAL A HG23 1 
ATOM   2059 N N    . ILE A 1 116 ? 5.93321   9.31282  24.45080 1.000 9.29451   ? 113 ILE A N    1 
ATOM   2060 C CA   . ILE A 1 116 ? 6.29563   7.90417  24.48842 1.000 9.93775   ? 113 ILE A CA   1 
ATOM   2061 C C    . ILE A 1 116 ? 7.81411   7.84236  24.40666 1.000 9.04819   ? 113 ILE A C    1 
ATOM   2062 O O    . ILE A 1 116 ? 8.39922   8.28472  23.41134 1.000 9.95955   ? 113 ILE A O    1 
ATOM   2063 C CB   . ILE A 1 116 ? 5.68789   7.12673  23.30987 1.000 10.90014  ? 113 ILE A CB   1 
ATOM   2064 C CG1  . ILE A 1 116 ? 4.17477   7.31505  23.23105 1.000 11.52817  ? 113 ILE A CG1  1 
ATOM   2065 C CG2  . ILE A 1 116 ? 6.07860   5.65865  23.41517 1.000 10.11645  ? 113 ILE A CG2  1 
ATOM   2066 C CD1  . ILE A 1 116 ? 3.43019   6.80872  24.43189 1.000 12.61738  ? 113 ILE A CD1  1 
ATOM   2067 H H    . ILE A 1 116 ? 6.09300   9.68043  23.68993 1.000 11.15341  ? 113 ILE A H    1 
ATOM   2068 H HA   . ILE A 1 116 ? 5.98402   7.51131  25.31876 1.000 11.92530  ? 113 ILE A HA   1 
ATOM   2069 H HB   . ILE A 1 116 ? 6.04714   7.48342  22.48246 1.000 13.08017  ? 113 ILE A HB   1 
ATOM   2070 H HG12 . ILE A 1 116 ? 3.98391   8.26210  23.14395 1.000 13.83380  ? 113 ILE A HG12 1 
ATOM   2071 H HG13 . ILE A 1 116 ? 3.84240   6.83692  22.45528 1.000 13.83380  ? 113 ILE A HG13 1 
ATOM   2072 H HG21 . ILE A 1 116 ? 5.53262   5.14181  22.80224 1.000 12.13974  ? 113 ILE A HG21 1 
ATOM   2073 H HG22 . ILE A 1 116 ? 7.01580   5.56390  23.18371 1.000 12.13974  ? 113 ILE A HG22 1 
ATOM   2074 H HG23 . ILE A 1 116 ? 5.93045   5.35691  24.32506 1.000 12.13974  ? 113 ILE A HG23 1 
ATOM   2075 H HD11 . ILE A 1 116 ? 2.47725   6.88916  24.26965 1.000 15.14086  ? 113 ILE A HD11 1 
ATOM   2076 H HD12 . ILE A 1 116 ? 3.66334   5.87872  24.57903 1.000 15.14086  ? 113 ILE A HD12 1 
ATOM   2077 H HD13 . ILE A 1 116 ? 3.68001   7.33867  25.20496 1.000 15.14086  ? 113 ILE A HD13 1 
ATOM   2078 N N    . ALA A 1 117 ? 8.45488   7.28854  25.42845 1.000 8.41877   ? 114 ALA A N    1 
ATOM   2079 C CA   . ALA A 1 117 ? 9.90598   7.17246  25.45044 1.000 8.45574   ? 114 ALA A CA   1 
ATOM   2080 C C    . ALA A 1 117 ? 10.31288  5.78510  24.97375 1.000 9.13219   ? 114 ALA A C    1 
ATOM   2081 O O    . ALA A 1 117 ? 9.71781   4.78333  25.38296 1.000 9.98054   ? 114 ALA A O    1 
ATOM   2082 C CB   . ALA A 1 117 ? 10.44859  7.39842  26.86327 1.000 10.76177  ? 114 ALA A CB   1 
ATOM   2083 H H    . ALA A 1 117 ? 8.06685   6.96995  26.12668 1.000 10.10253  ? 114 ALA A H    1 
ATOM   2084 H HA   . ALA A 1 117 ? 10.29334  7.83781  24.86039 1.000 10.14688  ? 114 ALA A HA   1 
ATOM   2085 H HB1  . ALA A 1 117 ? 11.41812  7.39272  26.83387 1.000 12.91412  ? 114 ALA A HB1  1 
ATOM   2086 H HB2  . ALA A 1 117 ? 10.13258  8.25548  27.18960 1.000 12.91412  ? 114 ALA A HB2  1 
ATOM   2087 H HB3  . ALA A 1 117 ? 10.13099  6.68695  27.44107 1.000 12.91412  ? 114 ALA A HB3  1 
ATOM   2088 N N    . VAL A 1 118 ? 11.32402  5.73185  24.10021 1.000 9.12716   ? 115 VAL A N    1 
ATOM   2089 C CA   . VAL A 1 118 ? 11.90361  4.47266  23.65973 1.000 9.50987   ? 115 VAL A CA   1 
ATOM   2090 C C    . VAL A 1 118 ? 13.41852  4.52447  23.82272 1.000 8.59787   ? 115 VAL A C    1 
ATOM   2091 O O    . VAL A 1 118 ? 14.03592  5.59186  23.85589 1.000 10.20171  ? 115 VAL A O    1 
ATOM   2092 C CB   . VAL A 1 118 ? 11.56488  4.08892  22.19784 1.000 11.79806  ? 115 VAL A CB   1 
ATOM   2093 C CG1  . VAL A 1 118 ? 10.07287  4.06426  21.96460 1.000 11.58864  ? 115 VAL A CG1  1 
ATOM   2094 C CG2  . VAL A 1 118 ? 12.25351  5.02618  21.20968 1.000 14.08133  ? 115 VAL A CG2  1 
ATOM   2095 H H    . VAL A 1 118 ? 11.69166  6.42479  23.74769 1.000 10.95260  ? 115 VAL A H    1 
ATOM   2096 H HA   . VAL A 1 118 ? 11.54179  3.78359  24.23867 1.000 11.41185  ? 115 VAL A HA   1 
ATOM   2097 H HB   . VAL A 1 118 ? 11.89981  3.19222  22.04084 1.000 14.15767  ? 115 VAL A HB   1 
ATOM   2098 H HG11 . VAL A 1 118 ? 9.89247   3.62177  21.12047 1.000 13.90636  ? 115 VAL A HG11 1 
ATOM   2099 H HG12 . VAL A 1 118 ? 9.64788   3.57973  22.68952 1.000 13.90636  ? 115 VAL A HG12 1 
ATOM   2100 H HG13 . VAL A 1 118 ? 9.74237   4.97582  21.93751 1.000 13.90636  ? 115 VAL A HG13 1 
ATOM   2101 H HG21 . VAL A 1 118 ? 11.87844  4.88471  20.32639 1.000 16.89759  ? 115 VAL A HG21 1 
ATOM   2102 H HG22 . VAL A 1 118 ? 12.10569  5.94331  21.48881 1.000 16.89759  ? 115 VAL A HG22 1 
ATOM   2103 H HG23 . VAL A 1 118 ? 13.20390  4.83234  21.20041 1.000 16.89759  ? 115 VAL A HG23 1 
ATOM   2104 N N    . ASN A 1 119 ? 14.00857  3.33808  23.90166 1.000 9.09581   ? 116 ASN A N    1 
ATOM   2105 C CA   . ASN A 1 119 ? 15.45551  3.16812  23.89662 1.000 9.38588   ? 116 ASN A CA   1 
ATOM   2106 C C    . ASN A 1 119 ? 15.92289  3.16549  22.44800 1.000 9.68841   ? 116 ASN A C    1 
ATOM   2107 O O    . ASN A 1 119 ? 15.47939  2.33499  21.64925 1.000 11.47226  ? 116 ASN A O    1 
ATOM   2108 C CB   . ASN A 1 119 ? 15.76678  1.84056  24.58654 1.000 12.61035  ? 116 ASN A CB   1 
ATOM   2109 C CG   . ASN A 1 119 ? 17.24811  1.56496  24.70580 1.000 14.37154  ? 116 ASN A CG   1 
ATOM   2110 O OD1  . ASN A 1 119 ? 17.97872  1.58182  23.72055 1.000 12.63328  ? 116 ASN A OD1  1 
ATOM   2111 N ND2  . ASN A 1 119 ? 17.69454  1.27846  25.91995 1.000 18.19248  ? 116 ASN A ND2  1 
ATOM   2112 H H    . ASN A 1 119 ? 13.58065  2.59444  23.96070 1.000 10.91497  ? 116 ASN A H    1 
ATOM   2113 H HA   . ASN A 1 119 ? 15.91540  3.88439  24.36177 1.000 11.26306  ? 116 ASN A HA   1 
ATOM   2114 H HB2  . ASN A 1 119 ? 15.39343  1.85623  25.48168 1.000 15.13242  ? 116 ASN A HB2  1 
ATOM   2115 H HB3  . ASN A 1 119 ? 15.36962  1.11911  24.07403 1.000 15.13242  ? 116 ASN A HB3  1 
ATOM   2116 H HD21 . ASN A 1 119 ? 18.52950  1.11343  26.04325 1.000 21.83098  ? 116 ASN A HD21 1 
ATOM   2117 H HD22 . ASN A 1 119 ? 17.14934  1.25752  26.58472 1.000 21.83098  ? 116 ASN A HD22 1 
ATOM   2118 N N    . ALA A 1 120 ? 16.80055  4.10727  22.09631 1.000 9.44480   ? 117 ALA A N    1 
ATOM   2119 C CA   . ALA A 1 120 ? 17.18932  4.25168  20.70001 1.000 9.65646   ? 117 ALA A CA   1 
ATOM   2120 C C    . ALA A 1 120 ? 17.95395  3.04816  20.16878 1.000 10.56908  ? 117 ALA A C    1 
ATOM   2121 O O    . ALA A 1 120 ? 17.97971  2.83835  18.95177 1.000 13.45113  ? 117 ALA A O    1 
ATOM   2122 C CB   . ALA A 1 120 ? 18.05499  5.49659  20.50891 1.000 10.69985  ? 117 ALA A CB   1 
ATOM   2123 H H    . ALA A 1 120 ? 17.17522  4.66119  22.63704 1.000 11.33376  ? 117 ALA A H    1 
ATOM   2124 H HA   . ALA A 1 120 ? 16.37507  4.35339  20.18276 1.000 11.58775  ? 117 ALA A HA   1 
ATOM   2125 H HB1  . ALA A 1 120 ? 18.33956  5.54423  19.58281 1.000 12.83982  ? 117 ALA A HB1  1 
ATOM   2126 H HB2  . ALA A 1 120 ? 17.53289  6.28210  20.73535 1.000 12.83982  ? 117 ALA A HB2  1 
ATOM   2127 H HB3  . ALA A 1 120 ? 18.82917  5.43515  21.09009 1.000 12.83982  ? 117 ALA A HB3  1 
ATOM   2128 N N    . ASP A 1 121 ? 18.59717  2.27381  21.03935 1.000 11.03421  ? 118 ASP A N    1 
ATOM   2129 C CA   . ASP A 1 121 ? 19.39381  1.14311  20.58256 1.000 13.87812  ? 118 ASP A CA   1 
ATOM   2130 C C    . ASP A 1 121 ? 18.57876  -0.14021 20.49235 1.000 14.14121  ? 118 ASP A C    1 
ATOM   2131 O O    . ASP A 1 121 ? 18.78538  -0.93554 19.56917 1.000 17.21027  ? 118 ASP A O    1 
ATOM   2132 C CB   . ASP A 1 121 ? 20.59884  0.94356  21.50439 1.000 16.15132  ? 118 ASP A CB   1 
ATOM   2133 C CG   . ASP A 1 121 ? 21.59294  2.09356  21.42550 1.000 16.42284  ? 118 ASP A CG   1 
ATOM   2134 O OD1  . ASP A 1 121 ? 21.58422  2.83751  20.41726 1.000 15.39535  ? 118 ASP A OD1  1 
ATOM   2135 O OD2  . ASP A 1 121 ? 22.39225  2.24656  22.37317 1.000 19.14948  ? 118 ASP A OD2  1 
ATOM   2136 H H    . ASP A 1 121 ? 18.58698  2.38298  21.89233 1.000 13.24105  ? 118 ASP A H    1 
ATOM   2137 H HA   . ASP A 1 121 ? 19.73273  1.33670  19.69456 1.000 16.65375  ? 118 ASP A HA   1 
ATOM   2138 H HB2  . ASP A 1 121 ? 20.28867  0.87677  22.42103 1.000 19.38158  ? 118 ASP A HB2  1 
ATOM   2139 H HB3  . ASP A 1 121 ? 21.06053  0.12923  21.25021 1.000 19.38158  ? 118 ASP A HB3  1 
ATOM   2140 N N    . THR A 1 122 ? 17.64500  -0.35457 21.42099 1.000 13.60577  ? 119 THR A N    1 
ATOM   2141 C CA   . THR A 1 122 ? 16.87642  -1.58862 21.44865 1.000 13.78834  ? 119 THR A CA   1 
ATOM   2142 C C    . THR A 1 122 ? 15.46201  -1.44677 20.90138 1.000 12.98505  ? 119 THR A C    1 
ATOM   2143 O O    . THR A 1 122 ? 14.83179  -2.46356 20.59899 1.000 13.72915  ? 119 THR A O    1 
ATOM   2144 C CB   . THR A 1 122 ? 16.74642  -2.10408 22.88770 1.000 15.22939  ? 119 THR A CB   1 
ATOM   2145 O OG1  . THR A 1 122 ? 15.91521  -1.20049 23.62774 1.000 13.99304  ? 119 THR A OG1  1 
ATOM   2146 C CG2  . THR A 1 122 ? 18.10366  -2.20505 23.55750 1.000 17.31575  ? 119 THR A CG2  1 
ATOM   2147 H H    . THR A 1 122 ? 17.44163  0.20250  22.04382 1.000 16.32693  ? 119 THR A H    1 
ATOM   2148 H HA   . THR A 1 122 ? 17.35519  -2.24046 20.91312 1.000 16.54601  ? 119 THR A HA   1 
ATOM   2149 H HB   . THR A 1 122 ? 16.35445  -2.99134 22.88246 1.000 18.27527  ? 119 THR A HB   1 
ATOM   2150 H HG1  . THR A 1 122 ? 15.75191  -1.51772 24.38819 1.000 16.79164  ? 119 THR A HG1  1 
ATOM   2151 H HG21 . THR A 1 122 ? 18.01606  -2.63807 24.42106 1.000 20.77890  ? 119 THR A HG21 1 
ATOM   2152 H HG22 . THR A 1 122 ? 18.70853  -2.72433 23.00488 1.000 20.77890  ? 119 THR A HG22 1 
ATOM   2153 H HG23 . THR A 1 122 ? 18.47692  -1.31902 23.68605 1.000 20.77890  ? 119 THR A HG23 1 
ATOM   2154 N N    . GLY A 1 123 ? 14.93299  -0.23038 20.79685 1.000 10.95938  ? 120 GLY A N    1 
ATOM   2155 C CA   . GLY A 1 123 ? 13.55889  -0.03900 20.38915 1.000 10.59186  ? 120 GLY A CA   1 
ATOM   2156 C C    . GLY A 1 123 ? 12.53385  -0.25283 21.48030 1.000 9.82240   ? 120 GLY A C    1 
ATOM   2157 O O    . GLY A 1 123 ? 11.34442  0.00385  21.25142 1.000 10.73076  ? 120 GLY A O    1 
ATOM   2158 H H    . GLY A 1 123 ? 15.35785  0.49953  20.95912 1.000 13.15126  ? 120 GLY A H    1 
ATOM   2159 H HA2  . GLY A 1 123 ? 13.45623  0.86800  20.06095 1.000 12.71023  ? 120 GLY A HA2  1 
ATOM   2160 H HA3  . GLY A 1 123 ? 13.35932  -0.65933 19.67062 1.000 12.71023  ? 120 GLY A HA3  1 
ATOM   2161 N N    . ALA A 1 124 ? 12.94698  -0.70522 22.66011 1.000 10.57398  ? 121 ALA A N    1 
ATOM   2162 C CA   . ALA A 1 124 ? 11.99343  -1.00324 23.71679 1.000 9.62945   ? 121 ALA A CA   1 
ATOM   2163 C C    . ALA A 1 124 ? 11.27506  0.26068  24.16605 1.000 10.80914  ? 121 ALA A C    1 
ATOM   2164 O O    . ALA A 1 124 ? 11.87380  1.33440  24.26740 1.000 10.98606  ? 121 ALA A O    1 
ATOM   2165 C CB   . ALA A 1 124 ? 12.72202  -1.62265 24.91003 1.000 12.27067  ? 121 ALA A CB   1 
ATOM   2166 H H    . ALA A 1 124 ? 13.76861  -0.84665 22.87108 1.000 12.68878  ? 121 ALA A H    1 
ATOM   2167 H HA   . ALA A 1 124 ? 11.33379  -1.63209 23.38465 1.000 11.55533  ? 121 ALA A HA   1 
ATOM   2168 H HB1  . ALA A 1 124 ? 12.08180  -1.78826 25.61968 1.000 14.72480  ? 121 ALA A HB1  1 
ATOM   2169 H HB2  . ALA A 1 124 ? 13.13080  -2.45719 24.63193 1.000 14.72480  ? 121 ALA A HB2  1 
ATOM   2170 H HB3  . ALA A 1 124 ? 13.40485  -1.00626 25.21777 1.000 14.72480  ? 121 ALA A HB3  1 
ATOM   2171 N N    . VAL A 1 125 ? 9.98227   0.12255  24.45204 1.000 10.56879  ? 122 VAL A N    1 
ATOM   2172 C CA   . VAL A 1 125 ? 9.22406   1.21431  25.05267 1.000 9.96733   ? 122 VAL A CA   1 
ATOM   2173 C C    . VAL A 1 125 ? 9.64952   1.34103  26.50975 1.000 11.09035  ? 122 VAL A C    1 
ATOM   2174 O O    . VAL A 1 125 ? 9.59642   0.37228  27.27761 1.000 13.78675  ? 122 VAL A O    1 
ATOM   2175 C CB   . VAL A 1 125 ? 7.71562   0.98421  24.90216 1.000 10.05429  ? 122 VAL A CB   1 
ATOM   2176 C CG1  . VAL A 1 125 ? 6.91790   2.08019  25.60940 1.000 11.48236  ? 122 VAL A CG1  1 
ATOM   2177 C CG2  . VAL A 1 125 ? 7.34116   0.93222  23.42226 1.000 12.59415  ? 122 VAL A CG2  1 
ATOM   2178 H H    . VAL A 1 125 ? 9.52360   -0.59060 24.30835 1.000 12.68255  ? 122 VAL A H    1 
ATOM   2179 H HA   . VAL A 1 125 ? 9.43252   2.04878  24.60424 1.000 11.96079  ? 122 VAL A HA   1 
ATOM   2180 H HB   . VAL A 1 125 ? 7.48841   0.13694  25.31619 1.000 12.06515  ? 122 VAL A HB   1 
ATOM   2181 H HG11 . VAL A 1 125 ? 5.98923   2.02158  25.33547 1.000 13.77884  ? 122 VAL A HG11 1 
ATOM   2182 H HG12 . VAL A 1 125 ? 6.98851   1.95326  26.56847 1.000 13.77884  ? 122 VAL A HG12 1 
ATOM   2183 H HG13 . VAL A 1 125 ? 7.28166   2.94484  25.36251 1.000 13.77884  ? 122 VAL A HG13 1 
ATOM   2184 H HG21 . VAL A 1 125 ? 6.41788   0.64643  23.33997 1.000 15.11298  ? 122 VAL A HG21 1 
ATOM   2185 H HG22 . VAL A 1 125 ? 7.44929   1.81623  23.03790 1.000 15.11298  ? 122 VAL A HG22 1 
ATOM   2186 H HG23 . VAL A 1 125 ? 7.92405   0.30175  22.97098 1.000 15.11298  ? 122 VAL A HG23 1 
ATOM   2187 N N    . VAL A 1 126 ? 10.11093  2.53305  26.87762 1.000 9.73742   ? 123 VAL A N    1 
ATOM   2188 C CA   . VAL A 1 126 ? 10.64618  2.80978  28.20566 1.000 11.31438  ? 123 VAL A CA   1 
ATOM   2189 C C    . VAL A 1 126 ? 9.57838   3.37309  29.13164 1.000 10.93023  ? 123 VAL A C    1 
ATOM   2190 O O    . VAL A 1 126 ? 9.53675   3.02229  30.31320 1.000 13.29594  ? 123 VAL A O    1 
ATOM   2191 C CB   . VAL A 1 126 ? 11.84233  3.77445  28.05299 1.000 13.04886  ? 123 VAL A CB   1 
ATOM   2192 C CG1  . VAL A 1 126 ? 12.29521  4.31291  29.40249 1.000 14.64962  ? 123 VAL A CG1  1 
ATOM   2193 C CG2  . VAL A 1 126 ? 12.99228  3.08301  27.32851 1.000 13.30667  ? 123 VAL A CG2  1 
ATOM   2194 H H    . VAL A 1 126 ? 10.12539  3.21970  26.36003 1.000 11.68490  ? 123 VAL A H    1 
ATOM   2195 H HA   . VAL A 1 126 ? 10.95813  1.98542  28.61065 1.000 13.57725  ? 123 VAL A HA   1 
ATOM   2196 H HB   . VAL A 1 126 ? 11.55901  4.53388  27.52018 1.000 15.65864  ? 123 VAL A HB   1 
ATOM   2197 H HG11 . VAL A 1 126 ? 13.14933  4.75964  29.29376 1.000 17.57955  ? 123 VAL A HG11 1 
ATOM   2198 H HG12 . VAL A 1 126 ? 11.63275  4.94106  29.73032 1.000 17.57955  ? 123 VAL A HG12 1 
ATOM   2199 H HG13 . VAL A 1 126 ? 12.38549  3.57324  30.02348 1.000 17.57955  ? 123 VAL A HG13 1 
ATOM   2200 H HG21 . VAL A 1 126 ? 13.77463  3.65564  27.35909 1.000 15.96800  ? 123 VAL A HG21 1 
ATOM   2201 H HG22 . VAL A 1 126 ? 13.18193  2.24004  27.76934 1.000 15.96800  ? 123 VAL A HG22 1 
ATOM   2202 H HG23 . VAL A 1 126 ? 12.73474  2.92378  26.40698 1.000 15.96800  ? 123 VAL A HG23 1 
ATOM   2203 N N    . SER A 1 127 ? 8.70427   4.24061  28.61973 1.000 9.44407   ? 124 SER A N    1 
ATOM   2204 C CA   . SER A 1 127 ? 7.64999   4.83748  29.42925 1.000 9.70254   ? 124 SER A CA   1 
ATOM   2205 C C    . SER A 1 127 ? 6.59881   5.44933  28.51461 1.000 9.30048   ? 124 SER A C    1 
ATOM   2206 O O    . SER A 1 127 ? 6.88110   5.81608  27.37029 1.000 9.18059   ? 124 SER A O    1 
ATOM   2207 C CB   . SER A 1 127 ? 8.20043   5.91445  30.37113 1.000 8.56022   ? 124 SER A CB   1 
ATOM   2208 O OG   . SER A 1 127 ? 8.64601   7.04585  29.64455 1.000 10.28651  ? 124 SER A OG   1 
ATOM   2209 H H    . SER A 1 127 ? 8.70313   4.49981  27.79972 1.000 11.33288  ? 124 SER A H    1 
ATOM   2210 H HA   . SER A 1 127 ? 7.23420   4.13742  29.95645 1.000 11.64305  ? 124 SER A HA   1 
ATOM   2211 H HB2  . SER A 1 127 ? 7.49775   6.18851  30.98107 1.000 10.27226  ? 124 SER A HB2  1 
ATOM   2212 H HB3  . SER A 1 127 ? 8.94684   5.54587  30.86904 1.000 10.27226  ? 124 SER A HB3  1 
ATOM   2213 H HG   . SER A 1 127 ? 8.97856   7.61142  30.16909 1.000 12.34381  ? 124 SER A HG   1 
ATOM   2214 N N    . THR A 1 128 ? 5.37950   5.57682  29.05071 1.000 10.36698  ? 125 THR A N    1 
ATOM   2215 C CA   . THR A 1 128 ? 4.27053   6.15257  28.30590 1.000 9.38115   ? 125 THR A CA   1 
ATOM   2216 C C    . THR A 1 128 ? 3.53003   7.26754  29.03411 1.000 10.66709  ? 125 THR A C    1 
ATOM   2217 O O    . THR A 1 128 ? 2.66529   7.89920  28.41794 1.000 10.65820  ? 125 THR A O    1 
ATOM   2218 C CB   . THR A 1 128 ? 3.24008   5.07115  27.92480 1.000 10.80229  ? 125 THR A CB   1 
ATOM   2219 O OG1  . THR A 1 128 ? 2.62574   4.54957  29.11212 1.000 13.90977  ? 125 THR A OG1  1 
ATOM   2220 C CG2  . THR A 1 128 ? 3.89410   3.94099  27.13592 1.000 12.33048  ? 125 THR A CG2  1 
ATOM   2221 H H    . THR A 1 128 ? 5.17464   5.33372  29.84980 1.000 12.44037  ? 125 THR A H    1 
ATOM   2222 H HA   . THR A 1 128 ? 4.63551   6.52270  27.48695 1.000 11.25737  ? 125 THR A HA   1 
ATOM   2223 H HB   . THR A 1 128 ? 2.55746   5.46512  27.35936 1.000 12.96275  ? 125 THR A HB   1 
ATOM   2224 H HG1  . THR A 1 128 ? 3.21347   4.24774  29.63085 1.000 16.69173  ? 125 THR A HG1  1 
ATOM   2225 H HG21 . THR A 1 128 ? 3.21460   3.34129  26.79016 1.000 14.79657  ? 125 THR A HG21 1 
ATOM   2226 H HG22 . THR A 1 128 ? 4.40045   4.30485  26.39287 1.000 14.79657  ? 125 THR A HG22 1 
ATOM   2227 H HG23 . THR A 1 128 ? 4.49392   3.43952  27.71006 1.000 14.79657  ? 125 THR A HG23 1 
ATOM   2228 N N    . LYS A 1 129 ? 3.84026   7.54577  30.30121 1.000 10.86187  ? 126 LYS A N    1 
ATOM   2229 C CA   A LYS A 1 129 ? 3.07468   8.49664  31.09897 0.485 12.04766  ? 126 LYS A CA   1 
ATOM   2230 C CA   B LYS A 1 129 ? 3.07522   8.49694  31.10010 0.515 12.04766  ? 126 LYS A CA   1 
ATOM   2231 C C    . LYS A 1 129 ? 3.88458   9.72812  31.49656 1.000 10.62506  ? 126 LYS A C    1 
ATOM   2232 O O    . LYS A 1 129 ? 3.51571   10.42794 32.44380 1.000 11.71457  ? 126 LYS A O    1 
ATOM   2233 C CB   A LYS A 1 129 ? 2.49721   7.79153  32.32824 0.485 16.56925  ? 126 LYS A CB   1 
ATOM   2234 C CB   B LYS A 1 129 ? 2.50516   7.80331  32.33938 0.515 16.56925  ? 126 LYS A CB   1 
ATOM   2235 C CG   A LYS A 1 129 ? 1.54264   6.65951  31.96797 0.485 24.58864  ? 126 LYS A CG   1 
ATOM   2236 C CG   B LYS A 1 129 ? 1.58597   6.63273  32.02193 0.515 24.58864  ? 126 LYS A CG   1 
ATOM   2237 C CD   A LYS A 1 129 ? 1.19104   5.79918  33.16970 0.485 35.98737  ? 126 LYS A CD   1 
ATOM   2238 C CD   B LYS A 1 129 ? 0.42546   7.06411  31.13679 0.515 35.98737  ? 126 LYS A CD   1 
ATOM   2239 C CE   A LYS A 1 129 ? 0.22110   4.69002  32.79029 0.485 44.70157  ? 126 LYS A CE   1 
ATOM   2240 C CE   B LYS A 1 129 ? -0.54017  5.92008  30.87826 0.515 44.70157  ? 126 LYS A CE   1 
ATOM   2241 N NZ   A LYS A 1 129 ? -0.18327  3.87584  33.97005 0.485 51.50765  ? 126 LYS A NZ   1 
ATOM   2242 N NZ   B LYS A 1 129 ? -1.42327  6.20415  29.71209 0.515 51.50765  ? 126 LYS A NZ   1 
ATOM   2243 H H    . LYS A 1 129 ? 4.49990   7.18860  30.72181 1.000 13.03424  ? 126 LYS A H    1 
ATOM   2244 H HA   . LYS A 1 129 ? 2.33256   8.82176  30.56563 1.000 14.45719  ? 126 LYS A HA   1 
ATOM   2245 H HB2  A LYS A 1 129 ? 3.22550   7.41592  32.84730 0.485 19.88310  ? 126 LYS A HB2  1 
ATOM   2246 H HB2  B LYS A 1 129 ? 3.24114   7.46502  32.87304 0.515 19.88310  ? 126 LYS A HB2  1 
ATOM   2247 H HB3  A LYS A 1 129 ? 2.00842   8.43766  32.86163 0.485 19.88310  ? 126 LYS A HB3  1 
ATOM   2248 H HB3  B LYS A 1 129 ? 1.99433   8.45010  32.85086 0.515 19.88310  ? 126 LYS A HB3  1 
ATOM   2249 H HG2  A LYS A 1 129 ? 0.72098   7.03582  31.61559 0.485 29.50636  ? 126 LYS A HG2  1 
ATOM   2250 H HG2  B LYS A 1 129 ? 2.08798   5.94670  31.55477 0.515 29.50636  ? 126 LYS A HG2  1 
ATOM   2251 H HG3  A LYS A 1 129 ? 1.95973   6.09114  31.30171 0.485 29.50636  ? 126 LYS A HG3  1 
ATOM   2252 H HG3  B LYS A 1 129 ? 1.22388   6.27466  32.84751 0.515 29.50636  ? 126 LYS A HG3  1 
ATOM   2253 H HD2  A LYS A 1 129 ? 1.99815   5.39233  33.52177 0.485 43.18485  ? 126 LYS A HD2  1 
ATOM   2254 H HD2  B LYS A 1 129 ? -0.06173  7.78019  31.57355 0.515 43.18485  ? 126 LYS A HD2  1 
ATOM   2255 H HD3  A LYS A 1 129 ? 0.77377   6.35084  33.84974 0.485 43.18485  ? 126 LYS A HD3  1 
ATOM   2256 H HD3  B LYS A 1 129 ? 0.76997   7.36980  30.28311 0.515 43.18485  ? 126 LYS A HD3  1 
ATOM   2257 H HE2  A LYS A 1 129 ? -0.57777  5.08246  32.40469 0.485 53.64189  ? 126 LYS A HE2  1 
ATOM   2258 H HE2  B LYS A 1 129 ? -0.03770  5.11184  30.69073 0.515 53.64189  ? 126 LYS A HE2  1 
ATOM   2259 H HE3  A LYS A 1 129 ? 0.64530   4.10116  32.14670 0.485 53.64189  ? 126 LYS A HE3  1 
ATOM   2260 H HE3  B LYS A 1 129 ? -1.09957  5.78913  31.65982 0.515 53.64189  ? 126 LYS A HE3  1 
ATOM   2261 H HZ1  A LYS A 1 129 ? -0.74441  3.23262  33.71810 0.485 61.80918  ? 126 LYS A HZ1  1 
ATOM   2262 H HZ1  B LYS A 1 129 ? -1.99604  5.53336  29.59346 0.515 61.80918  ? 126 LYS A HZ1  1 
ATOM   2263 H HZ2  A LYS A 1 129 ? 0.53387   3.50367  34.34329 0.485 61.80918  ? 126 LYS A HZ2  1 
ATOM   2264 H HZ2  B LYS A 1 129 ? -1.88168  6.95391  29.85290 0.515 61.80918  ? 126 LYS A HZ2  1 
ATOM   2265 H HZ3  A LYS A 1 129 ? -0.58719  4.39204  34.57212 0.485 61.80918  ? 126 LYS A HZ3  1 
ATOM   2266 H HZ3  B LYS A 1 129 ? -0.93326  6.29928  28.97524 0.515 61.80918  ? 126 LYS A HZ3  1 
ATOM   2267 N N    . GLY A 1 130 ? 4.96400   10.02498 30.77462 1.000 8.71052   ? 127 GLY A N    1 
ATOM   2268 C CA   . GLY A 1 130 ? 5.77390   11.18416 31.11325 1.000 9.25858   ? 127 GLY A CA   1 
ATOM   2269 C C    . GLY A 1 130 ? 5.02030   12.50119 31.07761 1.000 8.60537   ? 127 GLY A C    1 
ATOM   2270 O O    . GLY A 1 130 ? 5.35444   13.42876 31.82089 1.000 9.60573   ? 127 GLY A O    1 
ATOM   2271 H H    . GLY A 1 130 ? 5.24253   9.57713  30.09532 1.000 10.45262  ? 127 GLY A H    1 
ATOM   2272 H HA2  . GLY A 1 130 ? 6.12917   11.06807 32.00835 1.000 11.11030  ? 127 GLY A HA2  1 
ATOM   2273 H HA3  . GLY A 1 130 ? 6.51146   11.24562 30.48625 1.000 11.11030  ? 127 GLY A HA3  1 
ATOM   2274 N N    . ARG A 1 131 ? 3.99635   12.60386 30.22403 1.000 9.80096   ? 128 ARG A N    1 
ATOM   2275 C CA   . ARG A 1 131 ? 3.21959   13.83770 30.13985 1.000 10.27449  ? 128 ARG A CA   1 
ATOM   2276 C C    . ARG A 1 131 ? 2.60015   14.18546 31.48364 1.000 10.44366  ? 128 ARG A C    1 
ATOM   2277 O O    . ARG A 1 131 ? 2.47215   15.36609 31.83140 1.000 12.39656  ? 128 ARG A O    1 
ATOM   2278 C CB   . ARG A 1 131 ? 2.12718   13.68986 29.07889 1.000 12.14978  ? 128 ARG A CB   1 
ATOM   2279 C CG   . ARG A 1 131 ? 1.17153   14.87323 28.95882 1.000 12.52148  ? 128 ARG A CG   1 
ATOM   2280 C CD   . ARG A 1 131 ? -0.03658  14.72841 29.87818 1.000 13.30281  ? 128 ARG A CD   1 
ATOM   2281 N NE   . ARG A 1 131 ? -1.00820  15.79433 29.66116 1.000 12.02479  ? 128 ARG A NE   1 
ATOM   2282 C CZ   . ARG A 1 131 ? -0.83620  17.05123 30.04486 1.000 11.88406  ? 128 ARG A CZ   1 
ATOM   2283 N NH1  . ARG A 1 131 ? 0.25672   17.43405 30.68434 1.000 12.33872  ? 128 ARG A NH1  1 
ATOM   2284 N NH2  . ARG A 1 131 ? -1.77880  17.94751 29.76928 1.000 13.94559  ? 128 ARG A NH2  1 
ATOM   2285 H H    . ARG A 1 131 ? 3.73610   11.98124 29.69093 1.000 11.76116  ? 128 ARG A H    1 
ATOM   2286 H HA   . ARG A 1 131 ? 3.80746   14.56325 29.87738 1.000 12.32938  ? 128 ARG A HA   1 
ATOM   2287 H HB2  . ARG A 1 131 ? 2.55322   13.57281 28.21536 1.000 14.57974  ? 128 ARG A HB2  1 
ATOM   2288 H HB3  . ARG A 1 131 ? 1.59477   12.90832 29.29482 1.000 14.57974  ? 128 ARG A HB3  1 
ATOM   2289 H HG2  . ARG A 1 131 ? 1.63982   15.68760 29.20050 1.000 15.02578  ? 128 ARG A HG2  1 
ATOM   2290 H HG3  . ARG A 1 131 ? 0.85110   14.93343 28.04526 1.000 15.02578  ? 128 ARG A HG3  1 
ATOM   2291 H HD2  . ARG A 1 131 ? -0.47205  13.87934 29.70400 1.000 15.96337  ? 128 ARG A HD2  1 
ATOM   2292 H HD3  . ARG A 1 131 ? 0.25697   14.76738 30.80187 1.000 15.96337  ? 128 ARG A HD3  1 
ATOM   2293 H HE   . ARG A 1 131 ? -1.74083  15.59411 29.25772 1.000 14.42975  ? 128 ARG A HE   1 
ATOM   2294 H HH11 . ARG A 1 131 ? 0.87487   16.86241 30.85960 1.000 14.80646  ? 128 ARG A HH11 1 
ATOM   2295 H HH12 . ARG A 1 131 ? 0.34908   18.25456 30.92482 1.000 14.80646  ? 128 ARG A HH12 1 
ATOM   2296 H HH21 . ARG A 1 131 ? -2.48896  17.70871 29.34709 1.000 16.73470  ? 128 ARG A HH21 1 
ATOM   2297 H HH22 . ARG A 1 131 ? -1.67832  18.76605 30.01321 1.000 16.73470  ? 128 ARG A HH22 1 
ATOM   2298 N N    . GLU A 1 132 ? 2.17346   13.17668 32.23621 1.000 10.12125  ? 129 GLU A N    1 
ATOM   2299 C CA   . GLU A 1 132 ? 1.62023   13.37678 33.56318 1.000 10.86567  ? 129 GLU A CA   1 
ATOM   2300 C C    . GLU A 1 132 ? 2.70142   13.42708 34.63396 1.000 11.90496  ? 129 GLU A C    1 
ATOM   2301 O O    . GLU A 1 132 ? 2.64761   14.26561 35.54057 1.000 13.62930  ? 129 GLU A O    1 
ATOM   2302 C CB   . GLU A 1 132 ? 0.65104   12.23502 33.89110 1.000 14.19115  ? 129 GLU A CB   1 
ATOM   2303 C CG   . GLU A 1 132 ? -0.68760  12.31075 33.17475 1.000 18.32391  ? 129 GLU A CG   1 
ATOM   2304 C CD   . GLU A 1 132 ? -0.71573  11.54207 31.86725 1.000 23.56341  ? 129 GLU A CD   1 
ATOM   2305 O OE1  . GLU A 1 132 ? 0.31657   10.94010 31.49784 1.000 25.00521  ? 129 GLU A OE1  1 
ATOM   2306 O OE2  . GLU A 1 132 ? -1.77999  11.53839 31.20906 1.000 27.17691  ? 129 GLU A OE2  1 
ATOM   2307 H H    . GLU A 1 132 ? 2.19542   12.35199 31.99333 1.000 12.14550  ? 129 GLU A H    1 
ATOM   2308 H HA   . GLU A 1 132 ? 1.13476   14.21644 33.57697 1.000 13.03881  ? 129 GLU A HA   1 
ATOM   2309 H HB2  . GLU A 1 132 ? 1.06843   11.39566 33.64174 1.000 17.02938  ? 129 GLU A HB2  1 
ATOM   2310 H HB3  . GLU A 1 132 ? 0.47292   12.24660 34.84453 1.000 17.02938  ? 129 GLU A HB3  1 
ATOM   2311 H HG2  . GLU A 1 132 ? -1.37357  11.94043 33.75200 1.000 21.98869  ? 129 GLU A HG2  1 
ATOM   2312 H HG3  . GLU A 1 132 ? -0.88573  13.23963 32.97771 1.000 21.98869  ? 129 GLU A HG3  1 
ATOM   2313 N N    . ARG A 1 133 ? 3.68660   12.54100 34.54934 1.000 10.61819  ? 130 ARG A N    1 
ATOM   2314 C CA   . ARG A 1 133 ? 4.64301   12.39505 35.63899 1.000 11.55170  ? 130 ARG A CA   1 
ATOM   2315 C C    . ARG A 1 133 ? 5.66267   13.52300 35.67988 1.000 11.35000  ? 130 ARG A C    1 
ATOM   2316 O O    . ARG A 1 133 ? 6.14201   13.86402 36.76593 1.000 12.30015  ? 130 ARG A O    1 
ATOM   2317 C CB   . ARG A 1 133 ? 5.29193   11.01323 35.56556 1.000 14.67197  ? 130 ARG A CB   1 
ATOM   2318 C CG   . ARG A 1 133 ? 4.24479   9.91426  35.50854 1.000 19.46120  ? 130 ARG A CG   1 
ATOM   2319 C CD   . ARG A 1 133 ? 4.54653   8.73184  36.40204 1.000 23.21220  ? 130 ARG A CD   1 
ATOM   2320 N NE   . ARG A 1 133 ? 3.45776   7.76482  36.32284 1.000 24.00180  ? 130 ARG A NE   1 
ATOM   2321 C CZ   . ARG A 1 133 ? 3.59582   6.47897  36.02526 1.000 26.41107  ? 130 ARG A CZ   1 
ATOM   2322 N NH1  . ARG A 1 133 ? 4.78788   5.92697  35.86567 1.000 26.97290  ? 130 ARG A NH1  1 
ATOM   2323 N NH2  . ARG A 1 133 ? 2.50892   5.72358  35.90620 1.000 28.10992  ? 130 ARG A NH2  1 
ATOM   2324 H H    . ARG A 1 133 ? 3.82229   12.01816 33.88014 1.000 12.74183  ? 130 ARG A H    1 
ATOM   2325 H HA   . ARG A 1 133 ? 4.17905   12.43923 36.48969 1.000 13.86203  ? 130 ARG A HA   1 
ATOM   2326 H HB2  . ARG A 1 133 ? 5.83890   10.95723 34.76644 1.000 17.60637  ? 130 ARG A HB2  1 
ATOM   2327 H HB3  . ARG A 1 133 ? 5.84030   10.87356 36.35339 1.000 17.60637  ? 130 ARG A HB3  1 
ATOM   2328 H HG2  . ARG A 1 133 ? 3.39105   10.28221 35.78537 1.000 23.35344  ? 130 ARG A HG2  1 
ATOM   2329 H HG3  . ARG A 1 133 ? 4.18525   9.58711  34.59731 1.000 23.35344  ? 130 ARG A HG3  1 
ATOM   2330 H HD2  . ARG A 1 133 ? 5.36704   8.30307  36.11253 1.000 27.85464  ? 130 ARG A HD2  1 
ATOM   2331 H HD3  . ARG A 1 133 ? 4.63407   9.02932  37.32114 1.000 27.85464  ? 130 ARG A HD3  1 
ATOM   2332 H HE   . ARG A 1 133 ? 2.66242   8.05082  36.48173 1.000 28.80216  ? 130 ARG A HE   1 
ATOM   2333 H HH11 . ARG A 1 133 ? 5.49798   6.40388  35.95463 1.000 32.36748  ? 130 ARG A HH11 1 
ATOM   2334 H HH12 . ARG A 1 133 ? 4.85247   5.09133  35.67298 1.000 32.36748  ? 130 ARG A HH12 1 
ATOM   2335 H HH21 . ARG A 1 133 ? 1.73008   6.06952  36.02168 1.000 33.73191  ? 130 ARG A HH21 1 
ATOM   2336 H HH22 . ARG A 1 133 ? 2.58440   4.88881  35.71369 1.000 33.73191  ? 130 ARG A HH22 1 
ATOM   2337 N N    . LEU A 1 134 ? 5.99759   14.12884 34.53816 1.000 9.98585   ? 131 LEU A N    1 
ATOM   2338 C CA   . LEU A 1 134 ? 6.89074   15.28407 34.57607 1.000 9.95053   ? 131 LEU A CA   1 
ATOM   2339 C C    . LEU A 1 134 ? 6.30544   16.41387 35.41913 1.000 10.12818  ? 131 LEU A C    1 
ATOM   2340 O O    . LEU A 1 134 ? 7.05235   17.14191 36.08749 1.000 10.60581  ? 131 LEU A O    1 
ATOM   2341 C CB   . LEU A 1 134 ? 7.18364   15.77349 33.15315 1.000 9.57758   ? 131 LEU A CB   1 
ATOM   2342 C CG   . LEU A 1 134 ? 7.94235   17.09899 33.03861 1.000 9.47361   ? 131 LEU A CG   1 
ATOM   2343 C CD1  . LEU A 1 134 ? 9.27433   17.05689 33.77169 1.000 8.83097   ? 131 LEU A CD1  1 
ATOM   2344 C CD2  . LEU A 1 134 ? 8.16642   17.46605 31.57214 1.000 11.35551  ? 131 LEU A CD2  1 
ATOM   2345 H H    . LEU A 1 134 ? 5.72955   13.89751 33.75442 1.000 11.98302  ? 131 LEU A H    1 
ATOM   2346 H HA   . LEU A 1 134 ? 7.73267   15.01572 34.97612 1.000 11.94064  ? 131 LEU A HA   1 
ATOM   2347 H HB2  . LEU A 1 134 ? 7.71708   15.09826 32.70547 1.000 11.49310  ? 131 LEU A HB2  1 
ATOM   2348 H HB3  . LEU A 1 134 ? 6.33745   15.88685 32.69271 1.000 11.49310  ? 131 LEU A HB3  1 
ATOM   2349 H HG   . LEU A 1 134 ? 7.40018   17.78639 33.45625 1.000 11.36833  ? 131 LEU A HG   1 
ATOM   2350 H HD11 . LEU A 1 134 ? 9.75106   17.88571 33.60831 1.000 10.59716  ? 131 LEU A HD11 1 
ATOM   2351 H HD12 . LEU A 1 134 ? 9.10877   16.95227 34.72171 1.000 10.59716  ? 131 LEU A HD12 1 
ATOM   2352 H HD13 . LEU A 1 134 ? 9.79285   16.30647 33.44168 1.000 10.59716  ? 131 LEU A HD13 1 
ATOM   2353 H HD21 . LEU A 1 134 ? 8.62299   18.32067 31.52672 1.000 13.62661  ? 131 LEU A HD21 1 
ATOM   2354 H HD22 . LEU A 1 134 ? 8.70835   16.77886 31.15384 1.000 13.62661  ? 131 LEU A HD22 1 
ATOM   2355 H HD23 . LEU A 1 134 ? 7.30682   17.52617 31.12675 1.000 13.62661  ? 131 LEU A HD23 1 
ATOM   2356 N N    . LEU A 1 135 ? 4.98097   16.57319 35.40332 1.000 11.04875  ? 132 LEU A N    1 
ATOM   2357 C CA   . LEU A 1 135 ? 4.36419   17.70963 36.07478 1.000 10.99795  ? 132 LEU A CA   1 
ATOM   2358 C C    . LEU A 1 135 ? 4.69132   17.74114 37.56029 1.000 12.19182  ? 132 LEU A C    1 
ATOM   2359 O O    . LEU A 1 135 ? 4.79945   18.82345 38.14682 1.000 16.56339  ? 132 LEU A O    1 
ATOM   2360 C CB   . LEU A 1 135 ? 2.84803   17.66667 35.89711 1.000 12.41207  ? 132 LEU A CB   1 
ATOM   2361 C CG   . LEU A 1 135 ? 2.32501   17.59833 34.46471 1.000 14.21877  ? 132 LEU A CG   1 
ATOM   2362 C CD1  . LEU A 1 135 ? 0.80486   17.67163 34.47280 1.000 14.68006  ? 132 LEU A CD1  1 
ATOM   2363 C CD2  . LEU A 1 135 ? 2.93788   18.70449 33.62098 1.000 15.21703  ? 132 LEU A CD2  1 
ATOM   2364 H H    . LEU A 1 135 ? 4.42605   16.04304 35.01525 1.000 13.25850  ? 132 LEU A H    1 
ATOM   2365 H HA   . LEU A 1 135 ? 4.70648   18.52015 35.66638 1.000 13.19754  ? 132 LEU A HA   1 
ATOM   2366 H HB2  . LEU A 1 135 ? 2.51471   16.88136 36.35872 1.000 14.89449  ? 132 LEU A HB2  1 
ATOM   2367 H HB3  . LEU A 1 135 ? 2.47699   18.46886 36.29676 1.000 14.89449  ? 132 LEU A HB3  1 
ATOM   2368 H HG   . LEU A 1 135 ? 2.58089   16.75651 34.05635 1.000 17.06252  ? 132 LEU A HG   1 
ATOM   2369 H HD11 . LEU A 1 135 ? 0.48285   17.65148 33.55803 1.000 17.61607  ? 132 LEU A HD11 1 
ATOM   2370 H HD12 . LEU A 1 135 ? 0.45466   16.91175 34.96355 1.000 17.61607  ? 132 LEU A HD12 1 
ATOM   2371 H HD13 . LEU A 1 135 ? 0.53078   18.49728 34.90184 1.000 17.61607  ? 132 LEU A HD13 1 
ATOM   2372 H HD21 . LEU A 1 135 ? 2.53720   18.68683 32.73778 1.000 18.26044  ? 132 LEU A HD21 1 
ATOM   2373 H HD22 . LEU A 1 135 ? 2.76416   19.55894 34.04600 1.000 18.26044  ? 132 LEU A HD22 1 
ATOM   2374 H HD23 . LEU A 1 135 ? 3.89422   18.55705 33.55335 1.000 18.26044  ? 132 LEU A HD23 1 
ATOM   2375 N N    . THR A 1 136 ? 4.82771   16.57622 38.19253 1.000 11.92783  ? 133 THR A N    1 
ATOM   2376 C CA   . THR A 1 136 ? 5.09935   16.50395 39.62260 1.000 14.10717  ? 133 THR A CA   1 
ATOM   2377 C C    . THR A 1 136 ? 6.52082   16.03374 39.91158 1.000 13.25349  ? 133 THR A C    1 
ATOM   2378 O O    . THR A 1 136 ? 6.82190   15.63100 41.03979 1.000 14.16756  ? 133 THR A O    1 
ATOM   2379 C CB   . THR A 1 136 ? 4.05945   15.63603 40.33694 1.000 16.62556  ? 133 THR A CB   1 
ATOM   2380 O OG1  . THR A 1 136 ? 4.04101   14.31691 39.77935 1.000 19.05410  ? 133 THR A OG1  1 
ATOM   2381 C CG2  . THR A 1 136 ? 2.67614   16.25844 40.19814 1.000 18.11799  ? 133 THR A CG2  1 
ATOM   2382 H H    . THR A 1 136 ? 4.76617   15.80895 37.80900 1.000 14.31339  ? 133 THR A H    1 
ATOM   2383 H HA   . THR A 1 136 ? 5.01312   17.39433 39.99770 1.000 16.92860  ? 133 THR A HA   1 
ATOM   2384 H HB   . THR A 1 136 ? 4.28708   15.57468 41.27785 1.000 19.95067  ? 133 THR A HB   1 
ATOM   2385 H HG1  . THR A 1 136 ? 4.80564   13.97287 39.83003 1.000 22.86492  ? 133 THR A HG1  1 
ATOM   2386 H HG21 . THR A 1 136 ? 2.03289   15.75804 40.72418 1.000 21.74159  ? 133 THR A HG21 1 
ATOM   2387 H HG22 . THR A 1 136 ? 2.69250   17.17647 40.51096 1.000 21.74159  ? 133 THR A HG22 1 
ATOM   2388 H HG23 . THR A 1 136 ? 2.39918   16.24751 39.26858 1.000 21.74159  ? 133 THR A HG23 1 
ATOM   2389 N N    . ASP A 1 137 ? 7.40396   16.09106 38.91206 1.000 10.99758  ? 134 ASP A N    1 
ATOM   2390 C CA   . ASP A 1 137 ? 8.79551   15.67929 39.06590 1.000 11.82763  ? 134 ASP A CA   1 
ATOM   2391 C C    . ASP A 1 137 ? 9.67195   16.55763 38.17946 1.000 10.82713  ? 134 ASP A C    1 
ATOM   2392 O O    . ASP A 1 137 ? 10.34478  16.05826 37.26761 1.000 10.68000  ? 134 ASP A O    1 
ATOM   2393 C CB   . ASP A 1 137 ? 8.92459   14.19708 38.71498 1.000 10.67318  ? 134 ASP A CB   1 
ATOM   2394 C CG   . ASP A 1 137 ? 10.30531  13.64410 38.99626 1.000 10.85865  ? 134 ASP A CG   1 
ATOM   2395 O OD1  . ASP A 1 137 ? 11.01384  14.19226 39.86896 1.000 10.44044  ? 134 ASP A OD1  1 
ATOM   2396 O OD2  . ASP A 1 137 ? 10.68393  12.66286 38.32013 1.000 11.22690  ? 134 ASP A OD2  1 
ATOM   2397 H H    . ASP A 1 137 ? 7.21559   16.37055 38.12086 1.000 13.19710  ? 134 ASP A H    1 
ATOM   2398 H HA   . ASP A 1 137 ? 9.10088   15.79278 39.97956 1.000 14.19316  ? 134 ASP A HA   1 
ATOM   2399 H HB2  . ASP A 1 137 ? 8.28633   13.69119 39.24187 1.000 12.80782  ? 134 ASP A HB2  1 
ATOM   2400 H HB3  . ASP A 1 137 ? 8.74171   14.07939 37.76968 1.000 12.80782  ? 134 ASP A HB3  1 
ATOM   2401 N N    . PRO A 1 138 ? 9.70237   17.86942 38.43514 1.000 11.84900  ? 135 PRO A N    1 
ATOM   2402 C CA   . PRO A 1 138 ? 10.46531  18.77772 37.56048 1.000 12.39188  ? 135 PRO A CA   1 
ATOM   2403 C C    . PRO A 1 138 ? 11.96309  18.52541 37.53243 1.000 12.18828  ? 135 PRO A C    1 
ATOM   2404 O O    . PRO A 1 138 ? 12.61137  18.91402 36.55415 1.000 12.64986  ? 135 PRO A O    1 
ATOM   2405 C CB   . PRO A 1 138 ? 10.14310  20.17078 38.12522 1.000 12.44763  ? 135 PRO A CB   1 
ATOM   2406 C CG   . PRO A 1 138 ? 9.72855   19.91786 39.53770 1.000 13.51465  ? 135 PRO A CG   1 
ATOM   2407 C CD   . PRO A 1 138 ? 9.02903   18.58894 39.53179 1.000 13.39458  ? 135 PRO A CD   1 
ATOM   2408 H HA   . PRO A 1 138 ? 10.12358  18.70685 36.65544 1.000 14.87026  ? 135 PRO A HA   1 
ATOM   2409 H HB2  . PRO A 1 138 ? 10.93199  20.73402 38.08901 1.000 14.93716  ? 135 PRO A HB2  1 
ATOM   2410 H HB3  . PRO A 1 138 ? 9.42258   20.57597 37.61771 1.000 14.93716  ? 135 PRO A HB3  1 
ATOM   2411 H HG2  . PRO A 1 138 ? 10.51253  19.89032 40.10824 1.000 16.21759  ? 135 PRO A HG2  1 
ATOM   2412 H HG3  . PRO A 1 138 ? 9.12812   20.62028 39.83263 1.000 16.21759  ? 135 PRO A HG3  1 
ATOM   2413 H HD2  . PRO A 1 138 ? 9.15237   18.12812 40.37638 1.000 16.07350  ? 135 PRO A HD2  1 
ATOM   2414 H HD3  . PRO A 1 138 ? 8.08275   18.69572 39.34723 1.000 16.07350  ? 135 PRO A HD3  1 
ATOM   2415 N N    . GLU A 1 139 ? 12.54275  17.91280 38.56210 1.000 10.40631  ? 136 GLU A N    1 
ATOM   2416 C CA   . GLU A 1 139 ? 13.96082  17.57151 38.54161 1.000 11.18092  ? 136 GLU A CA   1 
ATOM   2417 C C    . GLU A 1 139 ? 14.22190  16.20415 37.92421 1.000 8.98186   ? 136 GLU A C    1 
ATOM   2418 O O    . GLU A 1 139 ? 15.37997  15.77817 37.84971 1.000 11.45019  ? 136 GLU A O    1 
ATOM   2419 C CB   . GLU A 1 139 ? 14.54341  17.61696 39.95702 1.000 15.15146  ? 136 GLU A CB   1 
ATOM   2420 C CG   . GLU A 1 139 ? 14.40557  18.96665 40.63677 1.000 17.56152  ? 136 GLU A CG   1 
ATOM   2421 C CD   . GLU A 1 139 ? 15.15265  20.06784 39.90912 1.000 22.71669  ? 136 GLU A CD   1 
ATOM   2422 O OE1  . GLU A 1 139 ? 16.37586  19.92353 39.69154 1.000 23.20890  ? 136 GLU A OE1  1 
ATOM   2423 O OE2  . GLU A 1 139 ? 14.51035  21.07535 39.54486 1.000 26.80000  ? 136 GLU A OE2  1 
ATOM   2424 H H    . GLU A 1 139 ? 12.13447  17.68480 39.28386 1.000 12.48758  ? 136 GLU A H    1 
ATOM   2425 H HA   . GLU A 1 139 ? 14.43090  18.23565 38.01355 1.000 13.41711  ? 136 GLU A HA   1 
ATOM   2426 H HB2  . GLU A 1 139 ? 14.08233  16.96218 40.50435 1.000 18.18175  ? 136 GLU A HB2  1 
ATOM   2427 H HB3  . GLU A 1 139 ? 15.48875  17.40451 39.91126 1.000 18.18175  ? 136 GLU A HB3  1 
ATOM   2428 H HG2  . GLU A 1 139 ? 13.46727  19.21060 40.66814 1.000 21.07383  ? 136 GLU A HG2  1 
ATOM   2429 H HG3  . GLU A 1 139 ? 14.76274  18.90554 41.53654 1.000 21.07383  ? 136 GLU A HG3  1 
ATOM   2430 N N    . GLY A 1 140 ? 13.17730  15.50350 37.48992 1.000 9.36014   ? 137 GLY A N    1 
ATOM   2431 C CA   . GLY A 1 140 ? 13.37119  14.19920 36.88831 1.000 9.90519   ? 137 GLY A CA   1 
ATOM   2432 C C    . GLY A 1 140 ? 13.99346  13.18666 37.81572 1.000 8.98345   ? 137 GLY A C    1 
ATOM   2433 O O    . GLY A 1 140 ? 14.75990  12.32702 37.36702 1.000 9.62962   ? 137 GLY A O    1 
ATOM   2434 H H    . GLY A 1 140 ? 12.35818  15.76183 37.53357 1.000 11.23217  ? 137 GLY A H    1 
ATOM   2435 H HA2  . GLY A 1 140 ? 12.51144  13.85406 36.60091 1.000 11.88623  ? 137 GLY A HA2  1 
ATOM   2436 H HA3  . GLY A 1 140 ? 13.94885  14.29204 36.11463 1.000 11.88623  ? 137 GLY A HA3  1 
ATOM   2437 N N    . LYS A 1 141 ? 13.67989  13.25287 39.10885 1.000 9.13539   ? 138 LYS A N    1 
ATOM   2438 C CA   . LYS A 1 141 ? 14.23313  12.27954 40.03954 1.000 9.32829   ? 138 LYS A CA   1 
ATOM   2439 C C    . LYS A 1 141 ? 13.79177  10.86679 39.68856 1.000 9.15021   ? 138 LYS A C    1 
ATOM   2440 O O    . LYS A 1 141 ? 14.52246  9.90453  39.95184 1.000 10.53628  ? 138 LYS A O    1 
ATOM   2441 C CB   . LYS A 1 141 ? 13.81275  12.62799 41.46400 1.000 10.45677  ? 138 LYS A CB   1 
ATOM   2442 C CG   . LYS A 1 141 ? 14.15938  14.04618 41.87187 1.000 12.08537  ? 138 LYS A CG   1 
ATOM   2443 C CD   . LYS A 1 141 ? 13.80297  14.28913 43.33077 1.000 13.42747  ? 138 LYS A CD   1 
ATOM   2444 C CE   . LYS A 1 141 ? 13.87050  15.76361 43.65916 1.000 15.63482  ? 138 LYS A CE   1 
ATOM   2445 N NZ   . LYS A 1 141 ? 13.33769  16.07440 45.01366 1.000 18.36715  ? 138 LYS A NZ   1 
ATOM   2446 H H    . LYS A 1 141 ? 13.16031  13.83940 39.46329 1.000 10.96246  ? 138 LYS A H    1 
ATOM   2447 H HA   . LYS A 1 141 ? 15.20155  12.31258 39.99503 1.000 11.19395  ? 138 LYS A HA   1 
ATOM   2448 H HB2  . LYS A 1 141 ? 12.85128  12.52441 41.53975 1.000 12.54813  ? 138 LYS A HB2  1 
ATOM   2449 H HB3  . LYS A 1 141 ? 14.26076  12.02516 42.07783 1.000 12.54813  ? 138 LYS A HB3  1 
ATOM   2450 H HG2  . LYS A 1 141 ? 15.11159  14.19254 41.75883 1.000 14.50245  ? 138 LYS A HG2  1 
ATOM   2451 H HG3  . LYS A 1 141 ? 13.66019  14.67224 41.32436 1.000 14.50245  ? 138 LYS A HG3  1 
ATOM   2452 H HD2  . LYS A 1 141 ? 12.90054  13.97658 43.50057 1.000 16.11296  ? 138 LYS A HD2  1 
ATOM   2453 H HD3  . LYS A 1 141 ? 14.43022  13.81738 43.90078 1.000 16.11296  ? 138 LYS A HD3  1 
ATOM   2454 H HE2  . LYS A 1 141 ? 14.79571  16.05319 43.62689 1.000 18.76179  ? 138 LYS A HE2  1 
ATOM   2455 H HE3  . LYS A 1 141 ? 13.34558  16.25708 43.00967 1.000 18.76179  ? 138 LYS A HE3  1 
ATOM   2456 H HZ1  . LYS A 1 141 ? 12.49513  15.79564 45.08066 1.000 22.04057  ? 138 LYS A HZ1  1 
ATOM   2457 H HZ2  . LYS A 1 141 ? 13.82732  15.66583 45.63449 1.000 22.04057  ? 138 LYS A HZ2  1 
ATOM   2458 H HZ3  . LYS A 1 141 ? 13.36369  16.95241 45.15691 1.000 22.04057  ? 138 LYS A HZ3  1 
ATOM   2459 N N    . ASN A 1 142 ? 12.60660  10.72447 39.09648 1.000 9.76780   ? 139 ASN A N    1 
ATOM   2460 C CA   . ASN A 1 142 ? 12.06519  9.43332  38.69352 1.000 10.27667  ? 139 ASN A CA   1 
ATOM   2461 C C    . ASN A 1 142 ? 12.07452  9.23594  37.18491 1.000 9.78024   ? 139 ASN A C    1 
ATOM   2462 O O    . ASN A 1 142 ? 11.44286  8.29827  36.68954 1.000 10.89438  ? 139 ASN A O    1 
ATOM   2463 C CB   . ASN A 1 142 ? 10.66143  9.27048  39.26721 1.000 10.88661  ? 139 ASN A CB   1 
ATOM   2464 C CG   . ASN A 1 142 ? 10.68236  9.13996  40.76663 1.000 12.77836  ? 139 ASN A CG   1 
ATOM   2465 O OD1  . ASN A 1 142 ? 11.51278  8.41601  41.31712 1.000 14.17614  ? 139 ASN A OD1  1 
ATOM   2466 N ND2  . ASN A 1 142 ? 9.80057   9.86237  41.44262 1.000 12.27801  ? 139 ASN A ND2  1 
ATOM   2467 H H    . ASN A 1 142 ? 12.08404  11.38248 38.91330 1.000 11.72136  ? 139 ASN A H    1 
ATOM   2468 H HA   . ASN A 1 142 ? 12.61630  8.72605  39.06359 1.000 12.33201  ? 139 ASN A HA   1 
ATOM   2469 H HB2  . ASN A 1 142 ? 10.12967  10.04842 39.03713 1.000 13.06393  ? 139 ASN A HB2  1 
ATOM   2470 H HB3  . ASN A 1 142 ? 10.25588  8.47041  38.89801 1.000 13.06393  ? 139 ASN A HB3  1 
ATOM   2471 H HD21 . ASN A 1 142 ? 9.77689   9.81891  42.30120 1.000 14.73361  ? 139 ASN A HD21 1 
ATOM   2472 H HD22 . ASN A 1 142 ? 9.25206   10.37462 41.02271 1.000 14.73361  ? 139 ASN A HD22 1 
ATOM   2473 N N    . PHE A 1 143 ? 12.77659  10.09160 36.45249 1.000 10.22968  ? 140 PHE A N    1 
ATOM   2474 C CA   . PHE A 1 143 ? 12.96965  9.90626  35.02090 1.000 10.28364  ? 140 PHE A CA   1 
ATOM   2475 C C    . PHE A 1 143 ? 13.52568  8.50928  34.75842 1.000 10.77468  ? 140 PHE A C    1 
ATOM   2476 O O    . PHE A 1 143 ? 14.38804  8.03720  35.50904 1.000 12.16866  ? 140 PHE A O    1 
ATOM   2477 C CB   . PHE A 1 143 ? 13.95839  10.97916 34.54254 1.000 10.16066  ? 140 PHE A CB   1 
ATOM   2478 C CG   . PHE A 1 143 ? 14.42373  10.81993 33.12129 1.000 10.43847  ? 140 PHE A CG   1 
ATOM   2479 C CD1  . PHE A 1 143 ? 15.44229  9.93624  32.80530 1.000 10.87898  ? 140 PHE A CD1  1 
ATOM   2480 C CD2  . PHE A 1 143 ? 13.87771  11.59191 32.10921 1.000 12.02514  ? 140 PHE A CD2  1 
ATOM   2481 C CE1  . PHE A 1 143 ? 15.88447  9.80110  31.50082 1.000 12.92558  ? 140 PHE A CE1  1 
ATOM   2482 C CE2  . PHE A 1 143 ? 14.31986  11.46183 30.80408 1.000 12.58059  ? 140 PHE A CE2  1 
ATOM   2483 C CZ   . PHE A 1 143 ? 15.32235  10.56501 30.50188 1.000 12.36366  ? 140 PHE A CZ   1 
ATOM   2484 H H    . PHE A 1 143 ? 13.15702  10.79734 36.76362 1.000 12.27561  ? 140 PHE A H    1 
ATOM   2485 H HA   . PHE A 1 143 ? 12.13596  9.98827  34.53187 1.000 12.34037  ? 140 PHE A HA   1 
ATOM   2486 H HB2  . PHE A 1 143 ? 13.52965  11.84637 34.61349 1.000 12.19279  ? 140 PHE A HB2  1 
ATOM   2487 H HB3  . PHE A 1 143 ? 14.74353  10.94970 35.11139 1.000 12.19279  ? 140 PHE A HB3  1 
ATOM   2488 H HD1  . PHE A 1 143 ? 15.83395  9.42736  33.47801 1.000 13.05477  ? 140 PHE A HD1  1 
ATOM   2489 H HD2  . PHE A 1 143 ? 13.20679  12.20424 32.30872 1.000 14.43017  ? 140 PHE A HD2  1 
ATOM   2490 H HE1  . PHE A 1 143 ? 16.56044  9.19514  31.29890 1.000 15.51070  ? 140 PHE A HE1  1 
ATOM   2491 H HE2  . PHE A 1 143 ? 13.94063  11.97948 30.13093 1.000 15.09671  ? 140 PHE A HE2  1 
ATOM   2492 H HZ   . PHE A 1 143 ? 15.61867  10.47591 29.62487 1.000 14.83639  ? 140 PHE A HZ   1 
ATOM   2493 N N    . PRO A 1 144 ? 13.08901  7.82762  33.68899 1.000 11.48888  ? 141 PRO A N    1 
ATOM   2494 C CA   . PRO A 1 144 ? 12.17360  8.26270  32.62442 1.000 10.85668  ? 141 PRO A CA   1 
ATOM   2495 C C    . PRO A 1 144 ? 10.70622  7.94181  32.89432 1.000 11.58700  ? 141 PRO A C    1 
ATOM   2496 O O    . PRO A 1 144 ? 9.90500   7.85960  31.96741 1.000 11.97112  ? 141 PRO A O    1 
ATOM   2497 C CB   . PRO A 1 144 ? 12.69423  7.47771  31.41207 1.000 12.95146  ? 141 PRO A CB   1 
ATOM   2498 C CG   . PRO A 1 144 ? 13.10835  6.15894  32.02149 1.000 14.15813  ? 141 PRO A CG   1 
ATOM   2499 C CD   . PRO A 1 144 ? 13.67306  6.50627  33.38845 1.000 14.17804  ? 141 PRO A CD   1 
ATOM   2500 H HA   . PRO A 1 144 ? 12.26660  9.21922  32.49286 1.000 13.02802  ? 141 PRO A HA   1 
ATOM   2501 H HB2  . PRO A 1 144 ? 11.98942  7.36034  30.75604 1.000 15.54175  ? 141 PRO A HB2  1 
ATOM   2502 H HB3  . PRO A 1 144 ? 13.44873  7.93596  31.01002 1.000 15.54175  ? 141 PRO A HB3  1 
ATOM   2503 H HG2  . PRO A 1 144 ? 12.33601  5.57796  32.10423 1.000 16.98975  ? 141 PRO A HG2  1 
ATOM   2504 H HG3  . PRO A 1 144 ? 13.78266  5.73734  31.46610 1.000 16.98975  ? 141 PRO A HG3  1 
ATOM   2505 H HD2  . PRO A 1 144 ? 13.39812  5.85164  34.04933 1.000 17.01365  ? 141 PRO A HD2  1 
ATOM   2506 H HD3  . PRO A 1 144 ? 14.64110  6.55871  33.35617 1.000 17.01365  ? 141 PRO A HD3  1 
ATOM   2507 N N    . TRP A 1 145 ? 10.33702  7.73543  34.15904 1.000 11.81684  ? 142 TRP A N    1 
ATOM   2508 C CA   . TRP A 1 145 ? 8.93729   7.59398  34.56635 1.000 12.13769  ? 142 TRP A CA   1 
ATOM   2509 C C    . TRP A 1 145 ? 8.31060   6.30136  34.04802 1.000 14.18772  ? 142 TRP A C    1 
ATOM   2510 O O    . TRP A 1 145 ? 7.14781   6.27387  33.64187 1.000 14.76733  ? 142 TRP A O    1 
ATOM   2511 C CB   . TRP A 1 145 ? 8.10941   8.81830  34.16857 1.000 13.05783  ? 142 TRP A CB   1 
ATOM   2512 C CG   . TRP A 1 145 ? 8.72953   10.08945 34.63234 1.000 11.87859  ? 142 TRP A CG   1 
ATOM   2513 C CD1  . TRP A 1 145 ? 8.90722   10.49066 35.92468 1.000 12.61708  ? 142 TRP A CD1  1 
ATOM   2514 C CD2  . TRP A 1 145 ? 9.26451   11.12994 33.81170 1.000 10.41947  ? 142 TRP A CD2  1 
ATOM   2515 N NE1  . TRP A 1 145 ? 9.52398   11.71703 35.95863 1.000 11.67381  ? 142 TRP A NE1  1 
ATOM   2516 C CE2  . TRP A 1 145 ? 9.74988   12.13313 34.67281 1.000 10.72427  ? 142 TRP A CE2  1 
ATOM   2517 C CE3  . TRP A 1 145 ? 9.37592   11.31377 32.43125 1.000 10.54311  ? 142 TRP A CE3  1 
ATOM   2518 C CZ2  . TRP A 1 145 ? 10.33506  13.30364 34.19632 1.000 12.46829  ? 142 TRP A CZ2  1 
ATOM   2519 C CZ3  . TRP A 1 145 ? 9.95888   12.47352 31.96183 1.000 10.81005  ? 142 TRP A CZ3  1 
ATOM   2520 C CH2  . TRP A 1 145 ? 10.43193  13.45231 32.84008 1.000 12.67105  ? 142 TRP A CH2  1 
ATOM   2521 H H    . TRP A 1 145 ? 10.89054  7.67212  34.81418 1.000 14.18021  ? 142 TRP A H    1 
ATOM   2522 H HA   . TRP A 1 145 ? 8.91644   7.53147  35.53411 1.000 14.56523  ? 142 TRP A HA   1 
ATOM   2523 H HB2  . TRP A 1 145 ? 8.03579   8.85224  33.20196 1.000 15.66940  ? 142 TRP A HB2  1 
ATOM   2524 H HB3  . TRP A 1 145 ? 7.22740   8.74886  34.56623 1.000 15.66940  ? 142 TRP A HB3  1 
ATOM   2525 H HD1  . TRP A 1 145 ? 8.64816   10.00404 36.67368 1.000 15.14049  ? 142 TRP A HD1  1 
ATOM   2526 H HE1  . TRP A 1 145 ? 9.73394   12.15238 36.66996 1.000 14.00858  ? 142 TRP A HE1  1 
ATOM   2527 H HE3  . TRP A 1 145 ? 9.06342   10.66736 31.84015 1.000 12.65173  ? 142 TRP A HE3  1 
ATOM   2528 H HZ2  . TRP A 1 145 ? 10.64781  13.95872 34.77766 1.000 14.96195  ? 142 TRP A HZ2  1 
ATOM   2529 H HZ3  . TRP A 1 145 ? 10.03829  12.60595 31.04474 1.000 12.97207  ? 142 TRP A HZ3  1 
ATOM   2530 H HH2  . TRP A 1 145 ? 10.82165  14.22268 32.49432 1.000 15.20527  ? 142 TRP A HH2  1 
ATOM   2531 N N    . SER A 1 146 ? 9.08022   5.22069  34.08198 1.000 15.15165  ? 143 SER A N    1 
ATOM   2532 C CA   A SER A 1 146 ? 8.57979   3.92520  33.66141 0.592 19.65361  ? 143 SER A CA   1 
ATOM   2533 C CA   B SER A 1 146 ? 8.56092   3.93774  33.64539 0.408 20.94361  ? 143 SER A CA   1 
ATOM   2534 C C    . SER A 1 146 ? 7.49887   3.43219  34.61861 1.000 24.76421  ? 143 SER A C    1 
ATOM   2535 O O    . SER A 1 146 ? 7.37713   3.89752  35.75548 1.000 23.32269  ? 143 SER A O    1 
ATOM   2536 C CB   A SER A 1 146 ? 9.71407   2.90031  33.65466 0.592 19.12361  ? 143 SER A CB   1 
ATOM   2537 C CB   B SER A 1 146 ? 9.69177   2.91508  33.54819 0.408 23.03361  ? 143 SER A CB   1 
ATOM   2538 O OG   A SER A 1 146 ? 10.77734  3.31263  32.81729 0.592 20.06361  ? 143 SER A OG   1 
ATOM   2539 O OG   B SER A 1 146 ? 10.29748  2.70705  34.81175 0.408 24.07361  ? 143 SER A OG   1 
ATOM   2540 H H    A SER A 1 146 ? 9.89872   5.21318  34.34579 0.592 18.18198  ? 143 SER A H    1 
ATOM   2541 H H    B SER A 1 146 ? 9.89699   5.20612  34.35080 0.408 18.18198  ? 143 SER A H    1 
ATOM   2542 H HA   A SER A 1 146 ? 8.20727   4.00461  32.76932 0.592 23.58433  ? 143 SER A HA   1 
ATOM   2543 H HA   B SER A 1 146 ? 8.15539   4.03488  32.76960 0.408 25.13233  ? 143 SER A HA   1 
ATOM   2544 H HB2  A SER A 1 146 ? 10.04907  2.79744  34.55914 0.592 22.94833  ? 143 SER A HB2  1 
ATOM   2545 H HB2  B SER A 1 146 ? 9.32922   2.07352  33.23003 0.408 27.64033  ? 143 SER A HB2  1 
ATOM   2546 H HB3  A SER A 1 146 ? 9.36964   2.05358  33.33013 0.592 22.94833  ? 143 SER A HB3  1 
ATOM   2547 H HB3  B SER A 1 146 ? 10.36132  3.24352  32.92792 0.408 27.64033  ? 143 SER A HB3  1 
ATOM   2548 H HG   A SER A 1 146 ? 10.49433  3.44457  32.03748 0.592 24.07633  ? 143 SER A HG   1 
ATOM   2549 H HG   B SER A 1 146 ? 10.60779  3.43076  35.10424 0.408 28.88833  ? 143 SER A HG   1 
ATOM   2550 N N    . ASP A 1 147 ? 6.71518   2.46966  34.14547 1.000 36.34284  ? 144 ASP A N    1 
ATOM   2551 C CA   . ASP A 1 147 ? 5.73579   1.78647  34.98016 1.000 49.38360  ? 144 ASP A CA   1 
ATOM   2552 C C    . ASP A 1 147 ? 6.36494   0.49019  35.48521 1.000 58.69815  ? 144 ASP A C    1 
ATOM   2553 O O    . ASP A 1 147 ? 7.54844   0.23369  35.25176 1.000 61.68096  ? 144 ASP A O    1 
ATOM   2554 C CB   . ASP A 1 147 ? 4.46825   1.48336  34.19085 1.000 51.97325  ? 144 ASP A CB   1 
ATOM   2555 C CG   . ASP A 1 147 ? 3.63883   2.72368  33.92931 1.000 53.65996  ? 144 ASP A CG   1 
ATOM   2556 O OD1  . ASP A 1 147 ? 3.34473   3.45673  34.89712 1.000 54.66393  ? 144 ASP A OD1  1 
ATOM   2557 O OD2  . ASP A 1 147 ? 3.28793   2.96904  32.75604 1.000 53.63238  ? 144 ASP A OD2  1 
ATOM   2558 O OXT  . ASP A 1 147 ? 5.71245   -0.33028 36.12898 1.000 62.72729  ? 144 ASP A OXT  1 
ATOM   2559 H H    . ASP A 1 147 ? 6.73183   2.19011  33.33234 1.000 43.61141  ? 144 ASP A H    1 
ATOM   2560 H HA   . ASP A 1 147 ? 5.47362   2.34423  35.72920 1.000 59.26032  ? 144 ASP A HA   1 
ATOM   2561 H HB2  . ASP A 1 147 ? 4.71216   1.09809  33.33471 1.000 62.36789  ? 144 ASP A HB2  1 
ATOM   2562 H HB3  . ASP A 1 147 ? 3.92372   0.85733  34.69331 1.000 62.36789  ? 144 ASP A HB3  1 
ATOM   2563 N N    . MET B 1 3   ? -30.15984 21.17570 0.73585  1.000 66.26593  ? 0   MET B N    1 
ATOM   2564 C CA   . MET B 1 3   ? -29.39453 21.92063 1.76293  1.000 65.84503  ? 0   MET B CA   1 
ATOM   2565 C C    . MET B 1 3   ? -28.13656 21.09229 1.95251  1.000 57.37785  ? 0   MET B C    1 
ATOM   2566 O O    . MET B 1 3   ? -27.47424 20.73607 0.97903  1.000 57.01920  ? 0   MET B O    1 
ATOM   2567 C CB   . MET B 1 3   ? -30.20133 22.06492 3.03909  1.000 73.55309  ? 0   MET B CB   1 
ATOM   2568 C CG   . MET B 1 3   ? -31.55610 22.74409 2.84300  1.000 80.67997  ? 0   MET B CG   1 
ATOM   2569 S SD   . MET B 1 3   ? -32.04176 23.75479 4.25885  1.000 85.81400  ? 0   MET B SD   1 
ATOM   2570 C CE   . MET B 1 3   ? -33.81259 23.87856 4.01224  1.000 88.06318  ? 0   MET B CE   1 
ATOM   2571 H H    . MET B 1 3   ? -30.28338 21.69472 0.02349  1.000 79.51911  ? 0   MET B H    1 
ATOM   2572 H HA   . MET B 1 3   ? -29.19044 22.83682 1.51828  1.000 79.01404  ? 0   MET B HA   1 
ATOM   2573 H HB2  . MET B 1 3   ? -30.36404 21.18175 3.40575  1.000 88.26370  ? 0   MET B HB2  1 
ATOM   2574 H HB3  . MET B 1 3   ? -29.69254 22.59758 3.67020  1.000 88.26370  ? 0   MET B HB3  1 
ATOM   2575 H HG2  . MET B 1 3   ? -31.51096 23.32058 2.06421  1.000 96.81596  ? 0   MET B HG2  1 
ATOM   2576 H HG3  . MET B 1 3   ? -32.23504 22.06359 2.71314  1.000 96.81596  ? 0   MET B HG3  1 
ATOM   2577 H HE1  . MET B 1 3   ? -34.18768 24.45231 4.69854  1.000 105.67581 ? 0   MET B HE1  1 
ATOM   2578 H HE2  . MET B 1 3   ? -33.98367 24.25637 3.13537  1.000 105.67581 ? 0   MET B HE2  1 
ATOM   2579 H HE3  . MET B 1 3   ? -34.20251 22.99243 4.07242  1.000 105.67581 ? 0   MET B HE3  1 
ATOM   2580 N N    . GLY B 1 4   ? -27.80698 20.76804 3.19440  1.000 49.36167  ? 1   GLY B N    1 
ATOM   2581 C CA   . GLY B 1 4   ? -26.59870 20.00950 3.44398  1.000 42.24308  ? 1   GLY B CA   1 
ATOM   2582 C C    . GLY B 1 4   ? -25.34817 20.76796 3.04926  1.000 36.92855  ? 1   GLY B C    1 
ATOM   2583 O O    . GLY B 1 4   ? -24.24210 20.22307 3.10888  1.000 32.42008  ? 1   GLY B O    1 
ATOM   2584 H H    . GLY B 1 4   ? -28.26045 20.97324 3.89574  1.000 59.23400  ? 1   GLY B H    1 
ATOM   2585 H HA2  . GLY B 1 4   ? -26.54236 19.79784 4.38893  1.000 50.69170  ? 1   GLY B HA2  1 
ATOM   2586 H HA3  . GLY B 1 4   ? -26.62812 19.18336 2.93651  1.000 50.69170  ? 1   GLY B HA3  1 
ATOM   2587 N N    . SER B 1 5   ? -25.50678 22.02950 2.64122  1.000 35.06464  ? 2   SER B N    1 
ATOM   2588 C CA   . SER B 1 5   ? -24.34575 22.83575 2.28269  1.000 33.67897  ? 2   SER B CA   1 
ATOM   2589 C C    . SER B 1 5   ? -23.52164 23.20071 3.50675  1.000 28.38670  ? 2   SER B C    1 
ATOM   2590 O O    . SER B 1 5   ? -22.35970 23.59229 3.36219  1.000 28.52985  ? 2   SER B O    1 
ATOM   2591 C CB   . SER B 1 5   ? -24.77494 24.09449 1.52808  1.000 38.45851  ? 2   SER B CB   1 
ATOM   2592 O OG   . SER B 1 5   ? -25.55561 24.94780 2.34380  1.000 41.37123  ? 2   SER B OG   1 
ATOM   2593 H H    . SER B 1 5   ? -26.26295 22.43211 2.56563  1.000 42.07756  ? 2   SER B H    1 
ATOM   2594 H HA   . SER B 1 5   ? -23.78143 22.32752 1.67925  1.000 40.41476  ? 2   SER B HA   1 
ATOM   2595 H HB2  . SER B 1 5   ? -23.98164 24.57406 1.24245  1.000 46.15021  ? 2   SER B HB2  1 
ATOM   2596 H HB3  . SER B 1 5   ? -25.30037 23.83272 0.75588  1.000 46.15021  ? 2   SER B HB3  1 
ATOM   2597 H HG   . SER B 1 5   ? -25.74573 25.65071 1.92501  1.000 49.64547  ? 2   SER B HG   1 
ATOM   2598 N N    . GLY B 1 6   ? -24.09752 23.07887 4.70356  1.000 22.85915  ? 3   GLY B N    1 
ATOM   2599 C CA   . GLY B 1 6   ? -23.31192 23.27366 5.90994  1.000 18.92516  ? 3   GLY B CA   1 
ATOM   2600 C C    . GLY B 1 6   ? -22.34408 22.13005 6.14070  1.000 18.87015  ? 3   GLY B C    1 
ATOM   2601 O O    . GLY B 1 6   ? -21.16852 22.34533 6.44912  1.000 20.57830  ? 3   GLY B O    1 
ATOM   2602 H H    . GLY B 1 6   ? -24.92519 22.88780 4.83790  1.000 27.43098  ? 3   GLY B H    1 
ATOM   2603 H HA2  . GLY B 1 6   ? -22.80445 24.09702 5.83615  1.000 22.71019  ? 3   GLY B HA2  1 
ATOM   2604 H HA3  . GLY B 1 6   ? -23.90446 23.33543 6.67544  1.000 22.71019  ? 3   GLY B HA3  1 
ATOM   2605 N N    A LEU B 1 7   ? -22.83104 20.89417 6.00887  0.624 19.66361  ? 4   LEU B N    1 
ATOM   2606 N N    B LEU B 1 7   ? -22.82568 20.89419 5.99394  0.376 19.58361  ? 4   LEU B N    1 
ATOM   2607 C CA   A LEU B 1 7   ? -21.94512 19.74143 6.10379  0.624 20.04361  ? 4   LEU B CA   1 
ATOM   2608 C CA   B LEU B 1 7   ? -21.93598 19.74412 6.09162  0.376 20.14361  ? 4   LEU B CA   1 
ATOM   2609 C C    A LEU B 1 7   ? -20.88404 19.78517 5.01566  0.624 20.13361  ? 4   LEU B C    1 
ATOM   2610 C C    B LEU B 1 7   ? -20.90484 19.75930 4.97278  0.376 20.48361  ? 4   LEU B C    1 
ATOM   2611 O O    A LEU B 1 7   ? -19.70994 19.48769 5.26478  0.624 18.88361  ? 4   LEU B O    1 
ATOM   2612 O O    B LEU B 1 7   ? -19.74548 19.38083 5.17775  0.376 18.75361  ? 4   LEU B O    1 
ATOM   2613 C CB   A LEU B 1 7   ? -22.75656 18.45365 5.97205  0.624 19.90361  ? 4   LEU B CB   1 
ATOM   2614 C CB   B LEU B 1 7   ? -22.75061 18.45365 6.02101  0.376 20.29361  ? 4   LEU B CB   1 
ATOM   2615 C CG   A LEU B 1 7   ? -21.93947 17.16141 5.91278  0.624 26.68361  ? 4   LEU B CG   1 
ATOM   2616 C CG   B LEU B 1 7   ? -21.94421 17.15512 6.08348  0.376 26.77361  ? 4   LEU B CG   1 
ATOM   2617 C CD1  A LEU B 1 7   ? -21.16951 16.96008 7.20820  0.624 29.63361  ? 4   LEU B CD1  1 
ATOM   2618 C CD1  B LEU B 1 7   ? -21.34385 16.96903 7.46815  0.376 29.54361  ? 4   LEU B CD1  1 
ATOM   2619 C CD2  A LEU B 1 7   ? -22.83623 15.96956 5.62427  0.624 28.59361  ? 4   LEU B CD2  1 
ATOM   2620 C CD2  B LEU B 1 7   ? -22.80826 15.96495 5.69990  0.376 28.64361  ? 4   LEU B CD2  1 
ATOM   2621 H H    A LEU B 1 7   ? -23.65708 20.70193 5.86638  0.624 23.59633  ? 4   LEU B H    1 
ATOM   2622 H H    B LEU B 1 7   ? -23.64926 20.70028 5.83994  0.376 23.50033  ? 4   LEU B H    1 
ATOM   2623 H HA   A LEU B 1 7   ? -21.50933 19.75044 6.97034  0.624 24.05233  ? 4   LEU B HA   1 
ATOM   2624 H HA   B LEU B 1 7   ? -21.47355 19.77587 6.94371  0.376 24.17233  ? 4   LEU B HA   1 
ATOM   2625 H HB2  A LEU B 1 7   ? -23.34768 18.38698 6.73824  0.624 23.88433  ? 4   LEU B HB2  1 
ATOM   2626 H HB2  B LEU B 1 7   ? -23.37009 18.44461 6.76738  0.376 24.35233  ? 4   LEU B HB2  1 
ATOM   2627 H HB3  A LEU B 1 7   ? -23.27691 18.50435 5.15500  0.624 23.88433  ? 4   LEU B HB3  1 
ATOM   2628 H HB3  B LEU B 1 7   ? -23.24006 18.44917 5.18356  0.376 24.35233  ? 4   LEU B HB3  1 
ATOM   2629 H HG   A LEU B 1 7   ? -21.29654 17.22719 5.18945  0.624 32.02033  ? 4   LEU B HG   1 
ATOM   2630 H HG   B LEU B 1 7   ? -21.21469 17.20466 5.44611  0.376 32.12833  ? 4   LEU B HG   1 
ATOM   2631 H HD11 A LEU B 1 7   ? -20.71747 16.10243 7.17686  0.624 35.56033  ? 4   LEU B HD11 1 
ATOM   2632 H HD11 B LEU B 1 7   ? -20.88371 16.11574 7.50079  0.376 35.45233  ? 4   LEU B HD11 1 
ATOM   2633 H HD12 A LEU B 1 7   ? -20.51918 17.67349 7.30317  0.624 35.56033  ? 4   LEU B HD12 1 
ATOM   2634 H HD12 B LEU B 1 7   ? -20.71746 17.68941 7.64019  0.376 35.45233  ? 4   LEU B HD12 1 
ATOM   2635 H HD13 A LEU B 1 7   ? -21.79209 16.97887 7.95180  0.624 35.56033  ? 4   LEU B HD13 1 
ATOM   2636 H HD13 B LEU B 1 7   ? -22.05633 16.98601 8.12616  0.376 35.45233  ? 4   LEU B HD13 1 
ATOM   2637 H HD21 A LEU B 1 7   ? -22.31483 15.15548 5.70377  0.624 34.31233  ? 4   LEU B HD21 1 
ATOM   2638 H HD21 B LEU B 1 7   ? -22.30327 15.14911 5.84235  0.376 34.37233  ? 4   LEU B HD21 1 
ATOM   2639 H HD22 A LEU B 1 7   ? -23.56445 15.95985 6.26497  0.624 34.31233  ? 4   LEU B HD22 1 
ATOM   2640 H HD22 B LEU B 1 7   ? -23.60495 15.96170 6.25324  0.376 34.37233  ? 4   LEU B HD22 1 
ATOM   2641 H HD23 A LEU B 1 7   ? -23.18864 16.05008 4.72415  0.624 34.31233  ? 4   LEU B HD23 1 
ATOM   2642 H HD23 B LEU B 1 7   ? -23.05515 16.04218 4.76503  0.376 34.37233  ? 4   LEU B HD23 1 
ATOM   2643 N N    A ALA B 1 8   ? -21.28539 20.15193 3.79738  0.624 21.41361  ? 5   ALA B N    1 
ATOM   2644 N N    B ALA B 1 8   ? -21.31225 20.19693 3.77927  0.376 21.51361  ? 5   ALA B N    1 
ATOM   2645 C CA   A ALA B 1 8   ? -20.38359 20.09734 2.65529  0.624 23.41361  ? 5   ALA B CA   1 
ATOM   2646 C CA   B ALA B 1 8   ? -20.44750 20.08551 2.61079  0.376 23.48361  ? 5   ALA B CA   1 
ATOM   2647 C C    A ALA B 1 8   ? -19.19555 21.03525 2.80519  0.624 22.80361  ? 5   ALA B C    1 
ATOM   2648 C C    B ALA B 1 8   ? -19.16174 20.88430 2.77296  0.376 23.01361  ? 5   ALA B C    1 
ATOM   2649 O O    A ALA B 1 8   ? -18.14850 20.79215 2.19534  0.624 23.42361  ? 5   ALA B O    1 
ATOM   2650 O O    B ALA B 1 8   ? -18.13327 20.52315 2.19019  0.376 25.12361  ? 5   ALA B O    1 
ATOM   2651 C CB   A ALA B 1 8   ? -21.16194 20.42971 1.38022  0.624 22.62361  ? 5   ALA B CB   1 
ATOM   2652 C CB   B ALA B 1 8   ? -21.20602 20.53492 1.36092  0.376 22.55361  ? 5   ALA B CB   1 
ATOM   2653 H H    A ALA B 1 8   ? -22.07500 20.43554 3.60850  0.624 25.69633  ? 5   ALA B H    1 
ATOM   2654 H H    B ALA B 1 8   ? -22.07696 20.55812 3.62316  0.376 25.81633  ? 5   ALA B H    1 
ATOM   2655 H HA   A ALA B 1 8   ? -20.03016 19.19771 2.57373  0.624 28.09633  ? 5   ALA B HA   1 
ATOM   2656 H HA   B ALA B 1 8   ? -20.19789 19.15526 2.49574  0.376 28.18033  ? 5   ALA B HA   1 
ATOM   2657 H HB1  A ALA B 1 8   ? -20.56069 20.37833 0.62077  0.624 27.14833  ? 5   ALA B HB1  1 
ATOM   2658 H HB1  B ALA B 1 8   ? -20.61325 20.48027 0.59506  0.376 27.06433  ? 5   ALA B HB1  1 
ATOM   2659 H HB2  A ALA B 1 8   ? -21.88340 19.78996 1.27482  0.624 27.14833  ? 5   ALA B HB2  1 
ATOM   2660 H HB2  B ALA B 1 8   ? -21.97087 19.95302 1.22940  0.376 27.06433  ? 5   ALA B HB2  1 
ATOM   2661 H HB3  A ALA B 1 8   ? -21.52356 21.32661 1.45573  0.624 27.14833  ? 5   ALA B HB3  1 
ATOM   2662 H HB3  B ALA B 1 8   ? -21.50378 21.44983 1.48413  0.376 27.06433  ? 5   ALA B HB3  1 
ATOM   2663 N N    A LYS B 1 9   ? -19.32494 22.09486 3.60357  0.624 18.37361  ? 6   LYS B N    1 
ATOM   2664 N N    B LYS B 1 9   ? -19.18927 21.96543 3.55287  0.376 20.07361  ? 6   LYS B N    1 
ATOM   2665 C CA   A LYS B 1 9   ? -18.22184 23.02855 3.78935  0.624 20.82361  ? 6   LYS B CA   1 
ATOM   2666 C CA   B LYS B 1 9   ? -17.97646 22.75290 3.75144  0.376 21.48361  ? 6   LYS B CA   1 
ATOM   2667 C C    A LYS B 1 9   ? -17.07805 22.44270 4.60876  0.624 16.58361  ? 6   LYS B C    1 
ATOM   2668 C C    B LYS B 1 9   ? -16.93512 22.01627 4.58923  0.376 18.10361  ? 6   LYS B C    1 
ATOM   2669 O O    A LYS B 1 9   ? -15.99335 23.03493 4.63343  0.624 18.20361  ? 6   LYS B O    1 
ATOM   2670 O O    B LYS B 1 9   ? -15.78186 22.45909 4.63779  0.376 20.38361  ? 6   LYS B O    1 
ATOM   2671 C CB   A LYS B 1 9   ? -18.72897 24.30428 4.46385  0.624 28.20361  ? 6   LYS B CB   1 
ATOM   2672 C CB   B LYS B 1 9   ? -18.31774 24.11393 4.36368  0.376 28.70361  ? 6   LYS B CB   1 
ATOM   2673 C CG   A LYS B 1 9   ? -19.54200 25.22347 3.55754  0.624 39.39361  ? 6   LYS B CG   1 
ATOM   2674 C CG   B LYS B 1 9   ? -19.32894 24.93861 3.55260  0.376 39.51361  ? 6   LYS B CG   1 
ATOM   2675 C CD   A LYS B 1 9   ? -18.65078 26.15698 2.73753  0.624 48.83361  ? 6   LYS B CD   1 
ATOM   2676 C CD   B LYS B 1 9   ? -18.80974 25.33439 2.16718  0.376 48.83361  ? 6   LYS B CD   1 
ATOM   2677 C CE   A LYS B 1 9   ? -18.36931 25.62002 1.34055  0.624 55.88361  ? 6   LYS B CE   1 
ATOM   2678 C CE   B LYS B 1 9   ? -18.11599 26.69190 2.17837  0.376 55.86361  ? 6   LYS B CE   1 
ATOM   2679 N NZ   A LYS B 1 9   ? -19.03680 26.44617 0.29225  0.624 59.76361  ? 6   LYS B NZ   1 
ATOM   2680 N NZ   B LYS B 1 9   ? -17.59683 27.06545 0.82972  0.376 59.71361  ? 6   LYS B NZ   1 
ATOM   2681 H H    A LYS B 1 9   ? -20.03661 22.29177 4.04443  0.624 22.04833  ? 6   LYS B H    1 
ATOM   2682 H H    B LYS B 1 9   ? -19.88344 22.25660 3.96875  0.376 24.08833  ? 6   LYS B H    1 
ATOM   2683 H HA   A LYS B 1 9   ? -17.86996 23.26432 2.91672  0.624 24.98833  ? 6   LYS B HA   1 
ATOM   2684 H HA   B LYS B 1 9   ? -17.57174 22.93469 2.88886  0.376 25.78033  ? 6   LYS B HA   1 
ATOM   2685 H HB2  A LYS B 1 9   ? -19.29561 24.05399 5.21030  0.624 33.84433  ? 6   LYS B HB2  1 
ATOM   2686 H HB2  B LYS B 1 9   ? -18.69597 23.97050 5.24531  0.376 34.44433  ? 6   LYS B HB2  1 
ATOM   2687 H HB3  A LYS B 1 9   ? -17.96456 24.80938 4.78237  0.624 33.84433  ? 6   LYS B HB3  1 
ATOM   2688 H HB3  B LYS B 1 9   ? -17.50257 24.63506 4.43317  0.376 34.44433  ? 6   LYS B HB3  1 
ATOM   2689 H HG2  A LYS B 1 9   ? -20.06328 24.68491 2.94181  0.624 47.27233  ? 6   LYS B HG2  1 
ATOM   2690 H HG2  B LYS B 1 9   ? -20.13611 24.41489 3.42976  0.376 47.41633  ? 6   LYS B HG2  1 
ATOM   2691 H HG3  A LYS B 1 9   ? -20.13115 25.76880 4.10197  0.624 47.27233  ? 6   LYS B HG3  1 
ATOM   2692 H HG3  B LYS B 1 9   ? -19.53269 25.75321 4.03821  0.376 47.41633  ? 6   LYS B HG3  1 
ATOM   2693 H HD2  A LYS B 1 9   ? -19.09133 27.01627 2.64569  0.624 58.60033  ? 6   LYS B HD2  1 
ATOM   2694 H HD2  B LYS B 1 9   ? -18.16993 24.67083 1.86513  0.376 58.60033  ? 6   LYS B HD2  1 
ATOM   2695 H HD3  A LYS B 1 9   ? -17.80177 26.26651 3.19370  0.624 58.60033  ? 6   LYS B HD3  1 
ATOM   2696 H HD3  B LYS B 1 9   ? -19.55564 25.38161 1.54888  0.376 58.60033  ? 6   LYS B HD3  1 
ATOM   2697 H HE2  A LYS B 1 9   ? -17.41322 25.63463 1.17752  0.624 67.06033  ? 6   LYS B HE2  1 
ATOM   2698 H HE2  B LYS B 1 9   ? -18.74891 27.37157 2.45829  0.376 67.03633  ? 6   LYS B HE2  1 
ATOM   2699 H HE3  A LYS B 1 9   ? -18.70369 24.71205 1.27213  0.624 67.06033  ? 6   LYS B HE3  1 
ATOM   2700 H HE3  B LYS B 1 9   ? -17.36687 26.66252 2.79390  0.376 67.03633  ? 6   LYS B HE3  1 
ATOM   2701 H HZ1  A LYS B 1 9   ? -18.85924 26.11549 -0.51474 0.624 71.71633  ? 6   LYS B HZ1  1 
ATOM   2702 H HZ1  B LYS B 1 9   ? -17.21768 27.87001 0.86162  0.376 71.65633  ? 6   LYS B HZ1  1 
ATOM   2703 H HZ2  A LYS B 1 9   ? -19.91788 26.44367 0.41796  0.624 71.71633  ? 6   LYS B HZ2  1 
ATOM   2704 H HZ2  B LYS B 1 9   ? -16.99112 26.47113 0.56138  0.376 71.65633  ? 6   LYS B HZ2  1 
ATOM   2705 H HZ3  A LYS B 1 9   ? -18.74175 27.28489 0.33203  0.624 71.71633  ? 6   LYS B HZ3  1 
ATOM   2706 H HZ3  B LYS B 1 9   ? -18.26408 27.08373 0.24104  0.376 71.65633  ? 6   LYS B HZ3  1 
ATOM   2707 N N    A TYR B 1 10  ? -17.29244 21.31046 5.27872  0.624 14.14361  ? 7   TYR B N    1 
ATOM   2708 N N    B TYR B 1 10  ? -17.31324 20.90931 5.23959  0.376 15.64361  ? 7   TYR B N    1 
ATOM   2709 C CA   A TYR B 1 10  ? -16.25022 20.65069 6.05149  0.624 16.88361  ? 7   TYR B CA   1 
ATOM   2710 C CA   B TYR B 1 10  ? -16.37004 20.03095 5.91442  0.376 17.43361  ? 7   TYR B CA   1 
ATOM   2711 C C    A TYR B 1 10  ? -15.39913 19.70864 5.21608  0.624 22.83361  ? 7   TYR B C    1 
ATOM   2712 C C    B TYR B 1 10  ? -16.04853 18.77874 5.10959  0.376 22.94361  ? 7   TYR B C    1 
ATOM   2713 O O    A TYR B 1 10  ? -14.41248 19.17004 5.72962  0.624 25.31361  ? 7   TYR B O    1 
ATOM   2714 O O    B TYR B 1 10  ? -14.99939 18.16427 5.33283  0.376 26.16361  ? 7   TYR B O    1 
ATOM   2715 C CB   A TYR B 1 10  ? -16.87340 19.84914 7.20111  0.624 12.61361  ? 7   TYR B CB   1 
ATOM   2716 C CB   B TYR B 1 10  ? -16.94420 19.53819 7.25106  0.376 13.54361  ? 7   TYR B CB   1 
ATOM   2717 C CG   A TYR B 1 10  ? -17.41549 20.71773 8.30568  0.624 10.63361  ? 7   TYR B CG   1 
ATOM   2718 C CG   B TYR B 1 10  ? -17.39349 20.61439 8.20401  0.376 11.37361  ? 7   TYR B CG   1 
ATOM   2719 C CD1  A TYR B 1 10  ? -16.55765 21.44967 9.11403  0.624 10.87361  ? 7   TYR B CD1  1 
ATOM   2720 C CD1  B TYR B 1 10  ? -16.47670 21.46393 8.80607  0.376 11.69361  ? 7   TYR B CD1  1 
ATOM   2721 C CD2  A TYR B 1 10  ? -18.78051 20.81656 8.53721  0.624 12.33361  ? 7   TYR B CD2  1 
ATOM   2722 C CD2  B TYR B 1 10  ? -18.73504 20.76250 8.52555  0.376 12.46361  ? 7   TYR B CD2  1 
ATOM   2723 C CE1  A TYR B 1 10  ? -17.03942 22.25319 10.12385 0.624 10.98361  ? 7   TYR B CE1  1 
ATOM   2724 C CE1  B TYR B 1 10  ? -16.88582 22.44464 9.68545  0.376 11.33361  ? 7   TYR B CE1  1 
ATOM   2725 C CE2  A TYR B 1 10  ? -19.27377 21.62042 9.54974  0.624 10.77361  ? 7   TYR B CE2  1 
ATOM   2726 C CE2  B TYR B 1 10  ? -19.15388 21.73813 9.40644  0.376 11.51361  ? 7   TYR B CE2  1 
ATOM   2727 C CZ   A TYR B 1 10  ? -18.39441 22.33655 10.33768 0.624 9.67361   ? 7   TYR B CZ   1 
ATOM   2728 C CZ   B TYR B 1 10  ? -18.22493 22.57543 9.98506  0.376 10.66361  ? 7   TYR B CZ   1 
ATOM   2729 O OH   A TYR B 1 10  ? -18.85957 23.14110 11.34921 0.624 12.36361  ? 7   TYR B OH   1 
ATOM   2730 O OH   B TYR B 1 10  ? -18.63493 23.54993 10.86555 0.376 13.69361  ? 7   TYR B OH   1 
ATOM   2731 H H    A TYR B 1 10  ? -18.04797 20.90017 5.29944  0.624 16.97233  ? 7   TYR B H    1 
ATOM   2732 H H    B TYR B 1 10  ? -18.12942 20.64553 5.30184  0.376 18.77233  ? 7   TYR B H    1 
ATOM   2733 H HA   A TYR B 1 10  ? -15.67275 21.33260 6.42889  0.624 20.26033  ? 7   TYR B HA   1 
ATOM   2734 H HA   B TYR B 1 10  ? -15.56169 20.54126 6.07890  0.376 20.92033  ? 7   TYR B HA   1 
ATOM   2735 H HB2  A TYR B 1 10  ? -17.60634 19.31810 6.85227  0.624 15.13633  ? 7   TYR B HB2  1 
ATOM   2736 H HB2  B TYR B 1 10  ? -17.71460 18.97928 7.06396  0.376 16.25233  ? 7   TYR B HB2  1 
ATOM   2737 H HB3  A TYR B 1 10  ? -16.19591 19.26932 7.58283  0.624 15.13633  ? 7   TYR B HB3  1 
ATOM   2738 H HB3  B TYR B 1 10  ? -16.26043 19.01997 7.70361  0.376 16.25233  ? 7   TYR B HB3  1 
ATOM   2739 H HD1  A TYR B 1 10  ? -15.64017 21.39679 8.97142  0.624 13.04833  ? 7   TYR B HD1  1 
ATOM   2740 H HD1  B TYR B 1 10  ? -15.57162 21.37065 8.61363  0.376 14.03233  ? 7   TYR B HD1  1 
ATOM   2741 H HD2  A TYR B 1 10  ? -19.37190 20.33574 8.00432  0.624 14.80033  ? 7   TYR B HD2  1 
ATOM   2742 H HD2  B TYR B 1 10  ? -19.36269 20.19434 8.14064  0.376 14.95633  ? 7   TYR B HD2  1 
ATOM   2743 H HE1  A TYR B 1 10  ? -16.45110 22.73651 10.65787 0.624 13.18033  ? 7   TYR B HE1  1 
ATOM   2744 H HE1  B TYR B 1 10  ? -16.26181 23.01435 10.07398 0.376 13.60033  ? 7   TYR B HE1  1 
ATOM   2745 H HE2  A TYR B 1 10  ? -20.19001 21.67793 9.69840  0.624 12.92833  ? 7   TYR B HE2  1 
ATOM   2746 H HE2  B TYR B 1 10  ? -20.05703 21.83010 9.60837  0.376 13.81633  ? 7   TYR B HE2  1 
ATOM   2747 H HH   A TYR B 1 10  ? -19.69863 23.17420 11.32717 0.624 14.83633  ? 7   TYR B HH   1 
ATOM   2748 H HH   B TYR B 1 10  ? -19.39315 23.35910 11.17262 0.376 16.43233  ? 7   TYR B HH   1 
ATOM   2749 N N    A LEU B 1 11  ? -15.74539 19.51013 3.95385  0.624 23.14361  ? 8   LEU B N    1 
ATOM   2750 N N    B LEU B 1 11  ? -16.94501 18.37037 4.21108  0.376 23.05361  ? 8   LEU B N    1 
ATOM   2751 C CA   A LEU B 1 11  ? -15.13312 18.49719 3.11266  0.624 22.97361  ? 8   LEU B CA   1 
ATOM   2752 C CA   B LEU B 1 11  ? -16.79715 17.15749 3.40829  0.376 23.82361  ? 8   LEU B CA   1 
ATOM   2753 C C    A LEU B 1 11  ? -14.85947 19.10199 1.74823  0.624 22.75361  ? 8   LEU B C    1 
ATOM   2754 C C    B LEU B 1 11  ? -16.75866 17.58238 1.94744  0.376 23.32361  ? 8   LEU B C    1 
ATOM   2755 O O    A LEU B 1 11  ? -15.48363 20.09759 1.36745  0.624 21.42361  ? 8   LEU B O    1 
ATOM   2756 O O    B LEU B 1 11  ? -17.81217 17.72538 1.30673  0.376 21.82361  ? 8   LEU B O    1 
ATOM   2757 C CB   A LEU B 1 11  ? -16.08577 17.30602 2.94628  0.624 28.50361  ? 8   LEU B CB   1 
ATOM   2758 C CB   B LEU B 1 11  ? -17.95370 16.19569 3.67526  0.376 28.62361  ? 8   LEU B CB   1 
ATOM   2759 C CG   A LEU B 1 11  ? -16.72262 16.78762 4.23661  0.624 35.52361  ? 8   LEU B CG   1 
ATOM   2760 C CG   B LEU B 1 11  ? -18.00846 15.61251 5.08902  0.376 35.46361  ? 8   LEU B CG   1 
ATOM   2761 C CD1  A LEU B 1 11  ? -17.81894 15.78204 3.92265  0.624 32.88361  ? 8   LEU B CD1  1 
ATOM   2762 C CD1  B LEU B 1 11  ? -19.27272 14.79239 5.29027  0.376 32.88361  ? 8   LEU B CD1  1 
ATOM   2763 C CD2  A LEU B 1 11  ? -15.66937 16.17375 5.14524  0.624 40.19361  ? 8   LEU B CD2  1 
ATOM   2764 C CD2  B LEU B 1 11  ? -16.77445 14.76559 5.36882  0.376 39.90361  ? 8   LEU B CD2  1 
ATOM   2765 H H    A LEU B 1 11  ? -16.35292 19.96552 3.54996  0.624 27.77233  ? 8   LEU B H    1 
ATOM   2766 H H    B LEU B 1 11  ? -17.67336 18.79586 4.04359  0.376 27.66433  ? 8   LEU B H    1 
ATOM   2767 H HA   A LEU B 1 11  ? -14.29371 18.19900 3.49654  0.624 27.56833  ? 8   LEU B HA   1 
ATOM   2768 H HA   B LEU B 1 11  ? -15.96722 16.70473 3.62537  0.376 28.58833  ? 8   LEU B HA   1 
ATOM   2769 H HB2  A LEU B 1 11  ? -16.80663 17.57303 2.35470  0.624 34.20433  ? 8   LEU B HB2  1 
ATOM   2770 H HB2  B LEU B 1 11  ? -18.78603 16.67064 3.52513  0.376 34.34833  ? 8   LEU B HB2  1 
ATOM   2771 H HB3  A LEU B 1 11  ? -15.58894 16.57143 2.55329  0.624 34.20433  ? 8   LEU B HB3  1 
ATOM   2772 H HB3  B LEU B 1 11  ? -17.88022 15.45158 3.05735  0.376 34.34833  ? 8   LEU B HB3  1 
ATOM   2773 H HG   A LEU B 1 11  ? -17.12622 17.53120 4.71104  0.624 42.62833  ? 8   LEU B HG   1 
ATOM   2774 H HG   B LEU B 1 11  ? -18.02397 16.34482 5.72492  0.376 42.55633  ? 8   LEU B HG   1 
ATOM   2775 H HD11 A LEU B 1 11  ? -18.19172 15.45117 4.75479  0.624 39.46033  ? 8   LEU B HD11 1 
ATOM   2776 H HD11 B LEU B 1 11  ? -19.34621 14.55002 6.22662  0.376 39.46033  ? 8   LEU B HD11 1 
ATOM   2777 H HD12 A LEU B 1 11  ? -18.50991 16.22048 3.40185  0.624 39.46033  ? 8   LEU B HD12 1 
ATOM   2778 H HD12 B LEU B 1 11  ? -20.03953 15.32394 5.02502  0.376 39.46033  ? 8   LEU B HD12 1 
ATOM   2779 H HD13 A LEU B 1 11  ? -17.43831 15.04787 3.41567  0.624 39.46033  ? 8   LEU B HD13 1 
ATOM   2780 H HD13 B LEU B 1 11  ? -19.22026 13.99216 4.74458  0.376 39.46033  ? 8   LEU B HD13 1 
ATOM   2781 H HD21 A LEU B 1 11  ? -15.70549 16.61048 6.01061  0.624 48.23233  ? 8   LEU B HD21 1 
ATOM   2782 H HD21 B LEU B 1 11  ? -16.91995 14.25377 6.17985  0.376 47.88433  ? 8   LEU B HD21 1 
ATOM   2783 H HD22 A LEU B 1 11  ? -15.85177 15.22629 5.24501  0.624 48.23233  ? 8   LEU B HD22 1 
ATOM   2784 H HD22 B LEU B 1 11  ? -16.62701 14.16561 4.62103  0.376 47.88433  ? 8   LEU B HD22 1 
ATOM   2785 H HD23 A LEU B 1 11  ? -14.79456 16.30197 4.74627  0.624 48.23233  ? 8   LEU B HD23 1 
ATOM   2786 H HD23 B LEU B 1 11  ? -16.00856 15.35041 5.47968  0.376 47.88433  ? 8   LEU B HD23 1 
ATOM   2787 N N    A PRO B 1 12  ? -13.92248 18.53102 0.99398  0.624 20.43361  ? 9   PRO B N    1 
ATOM   2788 N N    B PRO B 1 12  ? -15.57167 17.80326 1.38207  0.376 21.22361  ? 9   PRO B N    1 
ATOM   2789 C CA   A PRO B 1 12  ? -13.77277 18.93890 -0.40668 0.624 21.75361  ? 9   PRO B CA   1 
ATOM   2790 C CA   B PRO B 1 12  ? -15.49101 18.26167 -0.01089 0.376 22.17361  ? 9   PRO B CA   1 
ATOM   2791 C C    A PRO B 1 12  ? -15.06078 18.69229 -1.17718 0.624 22.79361  ? 9   PRO B C    1 
ATOM   2792 C C    B PRO B 1 12  ? -16.30479 17.38423 -0.94929 0.376 23.25361  ? 9   PRO B C    1 
ATOM   2793 O O    A PRO B 1 12  ? -15.82556 17.77210 -0.87860 0.624 24.05361  ? 9   PRO B O    1 
ATOM   2794 O O    B PRO B 1 12  ? -16.22094 16.15451 -0.91259 0.376 24.62361  ? 9   PRO B O    1 
ATOM   2795 C CB   A PRO B 1 12  ? -12.63819 18.04534 -0.92163 0.624 22.99361  ? 9   PRO B CB   1 
ATOM   2796 C CB   B PRO B 1 12  ? -13.98918 18.18789 -0.32438 0.376 23.45361  ? 9   PRO B CB   1 
ATOM   2797 C CG   A PRO B 1 12  ? -11.88203 17.64146 0.29850  0.624 23.53361  ? 9   PRO B CG   1 
ATOM   2798 C CG   B PRO B 1 12  ? -13.38935 17.34876 0.77472  0.376 24.12361  ? 9   PRO B CG   1 
ATOM   2799 C CD   A PRO B 1 12  ? -12.89726 17.55203 1.40277  0.624 22.68361  ? 9   PRO B CD   1 
ATOM   2800 C CD   B PRO B 1 12  ? -14.23493 17.62100 1.97383  0.376 23.11361  ? 9   PRO B CD   1 
ATOM   2801 H HA   A PRO B 1 12  ? -13.51109 19.87037 -0.47583 0.624 26.10433  ? 9   PRO B HA   1 
ATOM   2802 H HA   B PRO B 1 12  ? -15.79841 19.17907 -0.07997 0.376 26.60833  ? 9   PRO B HA   1 
ATOM   2803 H HB2  A PRO B 1 12  ? -13.00726 17.27058 -1.37376 0.624 27.59233  ? 9   PRO B HB2  1 
ATOM   2804 H HB2  B PRO B 1 12  ? -13.85469 17.77087 -1.18978 0.376 28.14433  ? 9   PRO B HB2  1 
ATOM   2805 H HB3  A PRO B 1 12  ? -12.07322 18.54671 -1.53019 0.624 27.59233  ? 9   PRO B HB3  1 
ATOM   2806 H HB3  B PRO B 1 12  ? -13.60957 19.08052 -0.32368 0.376 28.14433  ? 9   PRO B HB3  1 
ATOM   2807 H HG2  A PRO B 1 12  ? -11.45890 16.78119 0.15085  0.624 28.24033  ? 9   PRO B HG2  1 
ATOM   2808 H HG2  B PRO B 1 12  ? -13.42496 16.41050 0.53121  0.376 28.94833  ? 9   PRO B HG2  1 
ATOM   2809 H HG3  A PRO B 1 12  ? -11.21042 18.31074 0.50317  0.624 28.24033  ? 9   PRO B HG3  1 
ATOM   2810 H HG3  B PRO B 1 12  ? -12.47014 17.61635 0.93076  0.376 28.94833  ? 9   PRO B HG3  1 
ATOM   2811 H HD2  A PRO B 1 12  ? -13.27297 16.65932 1.45594  0.624 27.22033  ? 9   PRO B HD2  1 
ATOM   2812 H HD2  B PRO B 1 12  ? -14.22420 16.86885 2.58624  0.376 27.73633  ? 9   PRO B HD2  1 
ATOM   2813 H HD3  A PRO B 1 12  ? -12.50429 17.79788 2.25484  0.624 27.22033  ? 9   PRO B HD3  1 
ATOM   2814 H HD3  B PRO B 1 12  ? -13.94326 18.42526 2.43100  0.376 27.73633  ? 9   PRO B HD3  1 
ATOM   2815 N N    A SER B 1 13  ? -15.29364 19.53130 -2.18735 0.624 25.72361  ? 10  SER B N    1 
ATOM   2816 N N    B SER B 1 13  ? -17.10052 18.03448 -1.80231 0.376 26.00361  ? 10  SER B N    1 
ATOM   2817 C CA   A SER B 1 13  ? -16.49890 19.39616 -2.99528 0.624 27.19361  ? 10  SER B CA   1 
ATOM   2818 C CA   B SER B 1 13  ? -17.97639 17.30824 -2.71246 0.376 27.43361  ? 10  SER B CA   1 
ATOM   2819 C C    A SER B 1 13  ? -16.52734 18.09465 -3.78460 0.624 25.99361  ? 10  SER B C    1 
ATOM   2820 C C    B SER B 1 13  ? -17.20544 16.42679 -3.68589 0.376 26.53361  ? 10  SER B C    1 
ATOM   2821 O O    A SER B 1 13  ? -17.59843 17.69043 -4.25098 0.624 28.29361  ? 10  SER B O    1 
ATOM   2822 O O    B SER B 1 13  ? -17.78586 15.48991 -4.24447 0.376 28.68361  ? 10  SER B O    1 
ATOM   2823 C CB   A SER B 1 13  ? -16.60804 20.57694 -3.96191 0.624 27.75361  ? 10  SER B CB   1 
ATOM   2824 C CB   B SER B 1 13  ? -18.85278 18.29226 -3.49100 0.376 27.97361  ? 10  SER B CB   1 
ATOM   2825 O OG   A SER B 1 13  ? -15.45558 20.66642 -4.78257 0.624 28.83361  ? 10  SER B OG   1 
ATOM   2826 O OG   B SER B 1 13  ? -18.06398 19.14855 -4.29965 0.376 29.68361  ? 10  SER B OG   1 
ATOM   2827 H H    A SER B 1 13  ? -14.77576 20.17712 -2.42043 0.624 30.86833  ? 10  SER B H    1 
ATOM   2828 H H    B SER B 1 13  ? -17.14938 18.89034 -1.87096 0.376 31.20433  ? 10  SER B H    1 
ATOM   2829 H HA   A SER B 1 13  ? -17.26790 19.40520 -2.40413 0.624 32.63233  ? 10  SER B HA   1 
ATOM   2830 H HA   B SER B 1 13  ? -18.55497 16.73364 -2.18713 0.376 32.92033  ? 10  SER B HA   1 
ATOM   2831 H HB2  A SER B 1 13  ? -17.38779 20.45255 -4.52531 0.624 33.30433  ? 10  SER B HB2  1 
ATOM   2832 H HB2  B SER B 1 13  ? -19.45866 17.79210 -4.05989 0.376 33.56833  ? 10  SER B HB2  1 
ATOM   2833 H HB3  A SER B 1 13  ? -16.69565 21.39646 -3.45042 0.624 33.30433  ? 10  SER B HB3  1 
ATOM   2834 H HB3  B SER B 1 13  ? -19.35732 18.83064 -2.86132 0.376 33.56833  ? 10  SER B HB3  1 
ATOM   2835 H HG   A SER B 1 13  ? -15.53152 21.31154 -5.31516 0.624 34.60033  ? 10  SER B HG   1 
ATOM   2836 H HG   B SER B 1 13  ? -17.63425 18.69674 -4.86250 0.376 35.62033  ? 10  SER B HG   1 
ATOM   2837 N N    A THR B 1 14  ? -15.38669 17.42373 -3.93579 0.624 20.86361  ? 11  THR B N    1 
ATOM   2838 N N    B THR B 1 14  ? -15.91772 16.69903 -3.90716 0.376 21.97361  ? 11  THR B N    1 
ATOM   2839 C CA   A THR B 1 14  ? -15.28171 16.24682 -4.78586 0.624 18.63361  ? 11  THR B CA   1 
ATOM   2840 C CA   B THR B 1 14  ? -15.13612 15.85322 -4.80016 0.376 19.01361  ? 11  THR B CA   1 
ATOM   2841 C C    A THR B 1 14  ? -15.35043 14.93094 -4.02265 0.624 21.28361  ? 11  THR B C    1 
ATOM   2842 C C    B THR B 1 14  ? -14.79502 14.50261 -4.18353 0.376 21.60361  ? 11  THR B C    1 
ATOM   2843 O O    A THR B 1 14  ? -15.21754 13.87095 -4.64140 0.624 19.98361  ? 11  THR B O    1 
ATOM   2844 O O    B THR B 1 14  ? -14.21796 13.65896 -4.87554 0.376 20.27361  ? 11  THR B O    1 
ATOM   2845 C CB   A THR B 1 14  ? -13.96890 16.29403 -5.57742 0.624 17.88361  ? 11  THR B CB   1 
ATOM   2846 C CB   B THR B 1 14  ? -13.84198 16.55449 -5.22486 0.376 18.77361  ? 11  THR B CB   1 
ATOM   2847 O OG1  A THR B 1 14  ? -12.86757 16.42437 -4.66831 0.624 20.89361  ? 11  THR B OG1  1 
ATOM   2848 O OG1  B THR B 1 14  ? -13.09675 16.94129 -4.06393 0.376 21.63361  ? 11  THR B OG1  1 
ATOM   2849 C CG2  A THR B 1 14  ? -13.96978 17.46477 -6.54032 0.624 16.74361  ? 11  THR B CG2  1 
ATOM   2850 C CG2  B THR B 1 14  ? -14.14769 17.78149 -6.06830 0.376 18.16361  ? 11  THR B CG2  1 
ATOM   2851 H H    A THR B 1 14  ? -14.64910 17.63697 -3.54836 0.624 25.03633  ? 11  THR B H    1 
ATOM   2852 H H    B THR B 1 14  ? -15.48499 17.35504 -3.55788 0.376 26.36833  ? 11  THR B H    1 
ATOM   2853 H HA   A THR B 1 14  ? -16.02524 16.26179 -5.40862 0.624 22.36033  ? 11  THR B HA   1 
ATOM   2854 H HA   B THR B 1 14  ? -15.66324 15.70091 -5.60006 0.376 22.81633  ? 11  THR B HA   1 
ATOM   2855 H HB   A THR B 1 14  ? -13.86951 15.47755 -6.09160 0.624 21.46033  ? 11  THR B HB   1 
ATOM   2856 H HB   B THR B 1 14  ? -13.30729 15.94653 -5.75907 0.376 22.52833  ? 11  THR B HB   1 
ATOM   2857 H HG1  A THR B 1 14  ? -12.88303 15.79977 -4.10685 0.624 25.07233  ? 11  THR B HG1  1 
ATOM   2858 H HG1  B THR B 1 14  ? -12.42077 17.38514 -4.29118 0.376 25.96033  ? 11  THR B HG1  1 
ATOM   2859 H HG21 A THR B 1 14  ? -13.08246 17.58944 -6.91184 0.624 20.09233  ? 11  THR B HG21 1 
ATOM   2860 H HG21 B THR B 1 14  ? -13.32379 18.23660 -6.30274 0.376 21.79633  ? 11  THR B HG21 1 
ATOM   2861 H HG22 A THR B 1 14  ? -14.59364 17.29847 -7.26423 0.624 20.09233  ? 11  THR B HG22 1 
ATOM   2862 H HG22 B THR B 1 14  ? -14.60491 17.51888 -6.88248 0.376 21.79633  ? 11  THR B HG22 1 
ATOM   2863 H HG23 A THR B 1 14  ? -14.23382 18.27510 -6.07713 0.624 20.09233  ? 11  THR B HG23 1 
ATOM   2864 H HG23 B THR B 1 14  ? -14.71454 18.39242 -5.57197 0.376 21.79633  ? 11  THR B HG23 1 
ATOM   2865 N N    A ILE B 1 15  ? -15.55010 14.95988 -2.71045 0.624 20.80361  ? 12  ILE B N    1 
ATOM   2866 N N    B ILE B 1 15  ? -15.12342 14.27741 -2.91366 0.376 21.76361  ? 12  ILE B N    1 
ATOM   2867 C CA   A ILE B 1 15  ? -15.54774 13.72445 -1.93547 0.624 24.43361  ? 12  ILE B CA   1 
ATOM   2868 C CA   B ILE B 1 15  ? -14.85883 13.00792 -2.24212 0.376 24.87361  ? 12  ILE B CA   1 
ATOM   2869 C C    A ILE B 1 15  ? -16.91217 13.05587 -2.02051 0.624 22.82361  ? 12  ILE B C    1 
ATOM   2870 C C    B ILE B 1 15  ? -16.16673 12.56641 -1.59747 0.376 23.16361  ? 12  ILE B C    1 
ATOM   2871 O O    A ILE B 1 15  ? -17.95304 13.71664 -2.11984 0.624 24.13361  ? 12  ILE B O    1 
ATOM   2872 O O    B ILE B 1 15  ? -16.57275 13.10808 -0.56292 0.376 24.42361  ? 12  ILE B O    1 
ATOM   2873 C CB   A ILE B 1 15  ? -15.14238 13.98680 -0.47330 0.624 30.34361  ? 12  ILE B CB   1 
ATOM   2874 C CB   B ILE B 1 15  ? -13.73654 13.11309 -1.20399 0.376 30.55361  ? 12  ILE B CB   1 
ATOM   2875 C CG1  A ILE B 1 15  ? -14.81064 12.67018 0.23608  0.624 35.72361  ? 12  ILE B CG1  1 
ATOM   2876 C CG1  B ILE B 1 15  ? -12.53826 13.85916 -1.79483 0.376 35.70361  ? 12  ILE B CG1  1 
ATOM   2877 C CG2  A ILE B 1 15  ? -16.26626 14.68056 0.28773  0.624 29.33361  ? 12  ILE B CG2  1 
ATOM   2878 C CG2  B ILE B 1 15  ? -13.31249 11.72389 -0.74318 0.376 29.62361  ? 12  ILE B CG2  1 
ATOM   2879 C CD1  A ILE B 1 15  ? -13.63166 11.92937 -0.35373 0.624 40.74361  ? 12  ILE B CD1  1 
ATOM   2880 C CD1  B ILE B 1 15  ? -11.35780 13.97504 -0.85571 0.376 40.68361  ? 12  ILE B CD1  1 
ATOM   2881 H H    A ILE B 1 15  ? -15.68763 15.67334 -2.25039 0.624 24.96433  ? 12  ILE B H    1 
ATOM   2882 H H    B ILE B 1 15  ? -15.50895 14.85815 -2.40996 0.376 26.11633  ? 12  ILE B H    1 
ATOM   2883 H HA   A ILE B 1 15  ? -14.89174 13.12493 -2.32422 0.624 29.32033  ? 12  ILE B HA   1 
ATOM   2884 H HA   B ILE B 1 15  ? -14.60439 12.34445 -2.90240 0.376 29.84833  ? 12  ILE B HA   1 
ATOM   2885 H HB   A ILE B 1 15  ? -14.35962 14.55946 -0.48893 0.624 36.41233  ? 12  ILE B HB   1 
ATOM   2886 H HB   B ILE B 1 15  ? -14.06963 13.60973 -0.44025 0.376 36.66433  ? 12  ILE B HB   1 
ATOM   2887 H HG12 A ILE B 1 15  ? -14.60369 12.86135 1.16426  0.624 42.86833  ? 12  ILE B HG12 1 
ATOM   2888 H HG12 B ILE B 1 15  ? -12.23873 13.38711 -2.58751 0.376 42.84433  ? 12  ILE B HG12 1 
ATOM   2889 H HG13 A ILE B 1 15  ? -15.58267 12.08542 0.18194  0.624 42.86833  ? 12  ILE B HG13 1 
ATOM   2890 H HG13 B ILE B 1 15  ? -12.81719 14.75805 -2.02955 0.376 42.84433  ? 12  ILE B HG13 1 
ATOM   2891 H HG21 A ILE B 1 15  ? -15.94164 14.93829 1.16471  0.624 35.20033  ? 12  ILE B HG21 1 
ATOM   2892 H HG21 B ILE B 1 15  ? -12.71056 11.81184 0.01236  0.376 35.54833  ? 12  ILE B HG21 1 
ATOM   2893 H HG22 A ILE B 1 15  ? -16.54360 15.46760 -0.20678 0.624 35.20033  ? 12  ILE B HG22 1 
ATOM   2894 H HG22 B ILE B 1 15  ? -14.10118 11.22362 -0.48127 0.376 35.54833  ? 12  ILE B HG22 1 
ATOM   2895 H HG23 A ILE B 1 15  ? -17.01205 14.06696 0.37825  0.624 35.20033  ? 12  ILE B HG23 1 
ATOM   2896 H HG23 B ILE B 1 15  ? -12.86209 11.27251 -1.47414 0.376 35.54833  ? 12  ILE B HG23 1 
ATOM   2897 H HD11 A ILE B 1 15  ? -13.32000 11.27087 0.28669  0.624 48.89233  ? 12  ILE B HD11 1 
ATOM   2898 H HD11 B ILE B 1 15  ? -10.78043 14.69214 -1.16118 0.376 48.82033  ? 12  ILE B HD11 1 
ATOM   2899 H HD12 A ILE B 1 15  ? -13.91230 11.48887 -1.17110 0.624 48.89233  ? 12  ILE B HD12 1 
ATOM   2900 H HD12 B ILE B 1 15  ? -11.68263 14.16956 0.03735  0.376 48.82033  ? 12  ILE B HD12 1 
ATOM   2901 H HD13 A ILE B 1 15  ? -12.92402 12.56425 -0.54630 0.624 48.89233  ? 12  ILE B HD13 1 
ATOM   2902 H HD13 B ILE B 1 15  ? -10.87111 13.13597 -0.85519 0.376 48.82033  ? 12  ILE B HD13 1 
ATOM   2903 N N    A LYS B 1 16  ? -16.90163 11.72495 -1.99382 0.624 17.29361  ? 13  LYS B N    1 
ATOM   2904 N N    B LYS B 1 16  ? -16.83015 11.58542 -2.20397 0.376 18.06361  ? 13  LYS B N    1 
ATOM   2905 C CA   A LYS B 1 16  ? -18.08662 10.92983 -1.71501 0.624 15.38361  ? 13  LYS B CA   1 
ATOM   2906 C CA   B LYS B 1 16  ? -18.05543 11.05480 -1.63542 0.376 15.87361  ? 13  LYS B CA   1 
ATOM   2907 C C    A LYS B 1 16  ? -17.81640 10.04803 -0.50207 0.624 13.86361  ? 13  LYS B C    1 
ATOM   2908 C C    B LYS B 1 16  ? -17.74904 10.25430 -0.36980 0.376 14.00361  ? 13  LYS B C    1 
ATOM   2909 O O    A LYS B 1 16  ? -16.73463 9.46264  -0.37378 0.624 15.75361  ? 13  LYS B O    1 
ATOM   2910 O O    B LYS B 1 16  ? -16.59906 9.91842  -0.06991 0.376 16.17361  ? 13  LYS B O    1 
ATOM   2911 C CB   A LYS B 1 16  ? -18.47036 10.02869 -2.89216 0.624 18.25361  ? 13  LYS B CB   1 
ATOM   2912 C CB   B LYS B 1 16  ? -18.76695 10.15033 -2.64297 0.376 18.40361  ? 13  LYS B CB   1 
ATOM   2913 C CG   A LYS B 1 16  ? -18.99349 10.77023 -4.11104 0.624 21.82361  ? 13  LYS B CG   1 
ATOM   2914 C CG   B LYS B 1 16  ? -19.21267 10.85578 -3.91692 0.376 22.17361  ? 13  LYS B CG   1 
ATOM   2915 C CD   A LYS B 1 16  ? -20.51358 10.87949 -4.09825 0.624 28.37361  ? 13  LYS B CD   1 
ATOM   2916 C CD   B LYS B 1 16  ? -19.91428 9.90019  -4.88143 0.376 27.68361  ? 13  LYS B CD   1 
ATOM   2917 C CE   A LYS B 1 16  ? -21.17834 9.66976  -4.74128 0.624 34.84361  ? 13  LYS B CE   1 
ATOM   2918 C CE   B LYS B 1 16  ? -21.32009 9.53523  -4.41626 0.376 34.74361  ? 13  LYS B CE   1 
ATOM   2919 N NZ   A LYS B 1 16  ? -21.08596 9.69872  -6.22998 0.624 37.01361  ? 13  LYS B NZ   1 
ATOM   2920 N NZ   B LYS B 1 16  ? -22.28127 10.66560 -4.56034 0.376 37.01361  ? 13  LYS B NZ   1 
ATOM   2921 H H    A LYS B 1 16  ? -16.19896 11.25070 -2.13853 0.624 20.75233  ? 13  LYS B H    1 
ATOM   2922 H H    B LYS B 1 16  ? -16.58974 11.21448 -2.94168 0.376 21.67633  ? 13  LYS B H    1 
ATOM   2923 H HA   A LYS B 1 16  ? -18.82873 11.52816 -1.53560 0.624 18.46033  ? 13  LYS B HA   1 
ATOM   2924 H HA   B LYS B 1 16  ? -18.64220 11.79343 -1.40954 0.376 19.04833  ? 13  LYS B HA   1 
ATOM   2925 H HB2  A LYS B 1 16  ? -17.68544 9.52978  -3.16764 0.624 21.90433  ? 13  LYS B HB2  1 
ATOM   2926 H HB2  B LYS B 1 16  ? -18.16192 9.43673  -2.89913 0.376 22.08433  ? 13  LYS B HB2  1 
ATOM   2927 H HB3  A LYS B 1 16  ? -19.16559 9.41860  -2.60002 0.624 21.90433  ? 13  LYS B HB3  1 
ATOM   2928 H HB3  B LYS B 1 16  ? -19.55769 9.77939  -2.22104 0.376 22.08433  ? 13  LYS B HB3  1 
ATOM   2929 H HG2  A LYS B 1 16  ? -18.62478 11.66735 -4.12258 0.624 26.18833  ? 13  LYS B HG2  1 
ATOM   2930 H HG2  B LYS B 1 16  ? -19.83275 11.56603 -3.68903 0.376 26.60833  ? 13  LYS B HG2  1 
ATOM   2931 H HG3  A LYS B 1 16  ? -18.73023 10.29300 -4.91344 0.624 26.18833  ? 13  LYS B HG3  1 
ATOM   2932 H HG3  B LYS B 1 16  ? -18.43640 11.22469 -4.36660 0.376 26.60833  ? 13  LYS B HG3  1 
ATOM   2933 H HD2  A LYS B 1 16  ? -20.82153 10.94190 -3.18055 0.624 34.04833  ? 13  LYS B HD2  1 
ATOM   2934 H HD2  B LYS B 1 16  ? -19.98508 10.32217 -5.75196 0.376 33.22033  ? 13  LYS B HD2  1 
ATOM   2935 H HD3  A LYS B 1 16  ? -20.78107 11.67014 -4.59244 0.624 34.04833  ? 13  LYS B HD3  1 
ATOM   2936 H HD3  B LYS B 1 16  ? -19.39788 9.08197  -4.95038 0.376 33.22033  ? 13  LYS B HD3  1 
ATOM   2937 H HE2  A LYS B 1 16  ? -20.74166 8.86246  -4.42745 0.624 41.81233  ? 13  LYS B HE2  1 
ATOM   2938 H HE2  B LYS B 1 16  ? -21.64728 8.79278  -4.94788 0.376 41.69233  ? 13  LYS B HE2  1 
ATOM   2939 H HE3  A LYS B 1 16  ? -22.11707 9.65543  -4.49738 0.624 41.81233  ? 13  LYS B HE3  1 
ATOM   2940 H HE3  B LYS B 1 16  ? -21.28913 9.28446  -3.47975 0.376 41.69233  ? 13  LYS B HE3  1 
ATOM   2941 H HZ1  A LYS B 1 16  ? -21.40642 10.46900 -6.53992 0.624 44.41633  ? 13  LYS B HZ1  1 
ATOM   2942 H HZ1  B LYS B 1 16  ? -22.01216 11.35830 -4.07060 0.376 44.41633  ? 13  LYS B HZ1  1 
ATOM   2943 H HZ2  A LYS B 1 16  ? -20.23698 9.61601  -6.48394 0.624 44.41633  ? 13  LYS B HZ2  1 
ATOM   2944 H HZ2  B LYS B 1 16  ? -22.33063 10.91641 -5.41285 0.376 44.41633  ? 13  LYS B HZ2  1 
ATOM   2945 H HZ3  A LYS B 1 16  ? -21.55792 9.02887  -6.57734 0.624 44.41633  ? 13  LYS B HZ3  1 
ATOM   2946 H HZ3  B LYS B 1 16  ? -23.08979 10.41453 -4.28585 0.376 44.41633  ? 13  LYS B HZ3  1 
ATOM   2947 N N    . LEU B 1 17  ? -18.80454 9.95210  0.37937  1.000 12.07749  ? 14  LEU B N    1 
ATOM   2948 C CA   . LEU B 1 17  ? -18.71376 9.06591  1.52727  1.000 12.06990  ? 14  LEU B CA   1 
ATOM   2949 C C    . LEU B 1 17  ? -19.01104 7.64625  1.06807  1.000 13.35570  ? 14  LEU B C    1 
ATOM   2950 O O    . LEU B 1 17  ? -19.70183 7.43354  0.06782  1.000 14.39145  ? 14  LEU B O    1 
ATOM   2951 C CB   . LEU B 1 17  ? -19.72747 9.48210  2.58884  1.000 13.73767  ? 14  LEU B CB   1 
ATOM   2952 C CG   . LEU B 1 17  ? -19.62789 10.94432 3.01728  1.000 14.12379  ? 14  LEU B CG   1 
ATOM   2953 C CD1  . LEU B 1 17  ? -20.72661 11.29533 3.99471  1.000 16.35532  ? 14  LEU B CD1  1 
ATOM   2954 C CD2  . LEU B 1 17  ? -18.26468 11.20388 3.63078  1.000 15.56118  ? 14  LEU B CD2  1 
ATOM   2955 H H    A LEU B 1 17  ? -19.54155 10.39288 0.33335  0.624 14.49299  ? 14  LEU B H    1 
ATOM   2956 H H    B LEU B 1 17  ? -19.59717 10.25453 0.23840  0.376 14.49299  ? 14  LEU B H    1 
ATOM   2957 H HA   . LEU B 1 17  ? -17.82918 9.10164  1.92368  1.000 14.48388  ? 14  LEU B HA   1 
ATOM   2958 H HB2  . LEU B 1 17  ? -20.61979 9.33907  2.23641  1.000 16.48521  ? 14  LEU B HB2  1 
ATOM   2959 H HB3  . LEU B 1 17  ? -19.59065 8.93457  3.37775  1.000 16.48521  ? 14  LEU B HB3  1 
ATOM   2960 H HG   . LEU B 1 17  ? -19.73504 11.51532 2.24051  1.000 16.94855  ? 14  LEU B HG   1 
ATOM   2961 H HD11 . LEU B 1 17  ? -20.65427 12.23424 4.22732  1.000 19.62638  ? 14  LEU B HD11 1 
ATOM   2962 H HD12 . LEU B 1 17  ? -21.58595 11.12276 3.57919  1.000 19.62638  ? 14  LEU B HD12 1 
ATOM   2963 H HD13 . LEU B 1 17  ? -20.62812 10.74895 4.79011  1.000 19.62638  ? 14  LEU B HD13 1 
ATOM   2964 H HD21 . LEU B 1 17  ? -18.26717 12.08025 4.04655  1.000 18.67341  ? 14  LEU B HD21 1 
ATOM   2965 H HD22 . LEU B 1 17  ? -18.08312 10.52235 4.29670  1.000 18.67341  ? 14  LEU B HD22 1 
ATOM   2966 H HD23 . LEU B 1 17  ? -17.59255 11.17111 2.93216  1.000 18.67341  ? 14  LEU B HD23 1 
ATOM   2967 N N    . VAL B 1 18  ? -18.46155 6.67185  1.78193  1.000 14.84932  ? 15  VAL B N    1 
ATOM   2968 C CA   A VAL B 1 18  ? -18.70809 5.26829  1.47930  0.737 16.77361  ? 15  VAL B CA   1 
ATOM   2969 C CA   B VAL B 1 18  ? -18.70135 5.26491  1.48480  0.263 16.96361  ? 15  VAL B CA   1 
ATOM   2970 C C    . VAL B 1 18  ? -19.77434 4.73314  2.42258  1.000 13.63432  ? 15  VAL B C    1 
ATOM   2971 O O    . VAL B 1 18  ? -19.80345 5.06931  3.61538  1.000 11.85685  ? 15  VAL B O    1 
ATOM   2972 C CB   A VAL B 1 18  ? -17.42643 4.41313  1.54075  0.737 22.15361  ? 15  VAL B CB   1 
ATOM   2973 C CB   B VAL B 1 18  ? -17.40813 4.43021  1.57635  0.263 22.32361  ? 15  VAL B CB   1 
ATOM   2974 C CG1  A VAL B 1 18  ? -16.44010 4.86704  0.47465  0.737 26.99361  ? 15  VAL B CG1  1 
ATOM   2975 C CG1  B VAL B 1 18  ? -16.74124 4.59864  2.93025  0.263 27.57361  ? 15  VAL B CG1  1 
ATOM   2976 C CG2  A VAL B 1 18  ? -16.79188 4.46346  2.91712  0.737 27.54361  ? 15  VAL B CG2  1 
ATOM   2977 C CG2  B VAL B 1 18  ? -17.70705 2.95937  1.30930  0.263 27.06361  ? 15  VAL B CG2  1 
ATOM   2978 H H    A VAL B 1 18  ? -17.93796 6.80020  2.45200  0.737 17.81918  ? 15  VAL B H    1 
ATOM   2979 H H    B VAL B 1 18  ? -17.93904 6.80230  2.45243  0.263 17.81918  ? 15  VAL B H    1 
ATOM   2980 H HA   A VAL B 1 18  ? -19.04474 5.21374  0.57123  0.737 20.12833  ? 15  VAL B HA   1 
ATOM   2981 H HA   B VAL B 1 18  ? -19.03215 5.19304  0.57579  0.263 20.35633  ? 15  VAL B HA   1 
ATOM   2982 H HB   A VAL B 1 18  ? -17.66506 3.48905  1.36745  0.737 26.58433  ? 15  VAL B HB   1 
ATOM   2983 H HB   B VAL B 1 18  ? -16.78916 4.74813  0.90054  0.263 26.78833  ? 15  VAL B HB   1 
ATOM   2984 H HG11 A VAL B 1 18  ? -15.65963 4.29166  0.50100  0.737 32.39233  ? 15  VAL B HG11 1 
ATOM   2985 H HG11 B VAL B 1 18  ? -16.02850 3.94611  3.01457  0.263 33.08833  ? 15  VAL B HG11 1 
ATOM   2986 H HG12 A VAL B 1 18  ? -16.86560 4.80769  -0.39502 0.737 32.39233  ? 15  VAL B HG12 1 
ATOM   2987 H HG12 B VAL B 1 18  ? -16.37766 5.49567  2.99380  0.263 33.08833  ? 15  VAL B HG12 1 
ATOM   2988 H HG13 A VAL B 1 18  ? -16.18098 5.78438  0.65420  0.737 32.39233  ? 15  VAL B HG13 1 
ATOM   2989 H HG13 B VAL B 1 18  ? -17.40150 4.45920  3.62704  0.263 33.08833  ? 15  VAL B HG13 1 
ATOM   2990 H HG21 A VAL B 1 18  ? -16.00506 3.89621  2.92305  0.737 33.05233  ? 15  VAL B HG21 1 
ATOM   2991 H HG21 B VAL B 1 18  ? -16.87067 2.48584  1.17838  0.263 32.47633  ? 15  VAL B HG21 1 
ATOM   2992 H HG22 A VAL B 1 18  ? -16.54102 5.37913  3.11592  0.737 33.05233  ? 15  VAL B HG22 1 
ATOM   2993 H HG22 B VAL B 1 18  ? -18.18057 2.58999  2.07104  0.263 32.47633  ? 15  VAL B HG22 1 
ATOM   2994 H HG23 A VAL B 1 18  ? -17.43312 4.14649  3.57228  0.737 33.05233  ? 15  VAL B HG23 1 
ATOM   2995 H HG23 B VAL B 1 18  ? -18.25569 2.88821  0.51254  0.263 32.47633  ? 15  VAL B HG23 1 
ATOM   2996 N N    . SER B 1 19  ? -20.66350 3.92262  1.87760  1.000 14.49077  ? 16  SER B N    1 
ATOM   2997 C CA   . SER B 1 19  ? -21.63022 3.14525  2.62457  1.000 16.31992  ? 16  SER B CA   1 
ATOM   2998 C C    . SER B 1 19  ? -21.25222 1.68296  2.43966  1.000 18.50682  ? 16  SER B C    1 
ATOM   2999 O O    . SER B 1 19  ? -20.28490 1.34983  1.74703  1.000 21.96557  ? 16  SER B O    1 
ATOM   3000 C CB   . SER B 1 19  ? -23.04836 3.41176  2.12769  1.000 17.62895  ? 16  SER B CB   1 
ATOM   3001 O OG   . SER B 1 19  ? -23.23520 2.90050  0.82193  1.000 21.23026  ? 16  SER B OG   1 
ATOM   3002 H H    . SER B 1 19  ? -20.72861 3.80057  1.02880  1.000 17.38892  ? 16  SER B H    1 
ATOM   3003 H HA   . SER B 1 19  ? -21.61040 3.38659  3.56386  1.000 19.58390  ? 16  SER B HA   1 
ATOM   3004 H HB2  . SER B 1 19  ? -23.67794 2.98149  2.72719  1.000 21.15474  ? 16  SER B HB2  1 
ATOM   3005 H HB3  . SER B 1 19  ? -23.20292 4.36930  2.11583  1.000 21.15474  ? 16  SER B HB3  1 
ATOM   3006 H HG   . SER B 1 19  ? -24.03696 2.99310  0.58913  1.000 25.47631  ? 16  SER B HG   1 
ATOM   3007 N N    . LYS B 1 20  ? -22.03084 0.79812  3.04887  1.000 20.66120  ? 17  LYS B N    1 
ATOM   3008 C CA   . LYS B 1 20  ? -21.71653 -0.61697 2.92637  1.000 25.22119  ? 17  LYS B CA   1 
ATOM   3009 C C    . LYS B 1 20  ? -21.81456 -1.07752 1.47804  1.000 29.08518  ? 17  LYS B C    1 
ATOM   3010 O O    . LYS B 1 20  ? -21.01269 -1.90358 1.02634  1.000 32.56551  ? 17  LYS B O    1 
ATOM   3011 C CB   . LYS B 1 20  ? -22.63828 -1.43434 3.81855  1.000 25.70015  ? 17  LYS B CB   1 
ATOM   3012 C CG   . LYS B 1 20  ? -21.97459 -2.69171 4.29342  1.000 24.77201  ? 17  LYS B CG   1 
ATOM   3013 C CD   . LYS B 1 20  ? -22.90322 -3.51139 5.14099  1.000 22.18880  ? 17  LYS B CD   1 
ATOM   3014 C CE   . LYS B 1 20  ? -23.03139 -2.94018 6.54210  1.000 21.40913  ? 17  LYS B CE   1 
ATOM   3015 N NZ   . LYS B 1 20  ? -21.75838 -3.05020 7.31065  1.000 18.69053  ? 17  LYS B NZ   1 
ATOM   3016 H H    . LYS B 1 20  ? -22.72365 0.98435  3.52314  1.000 24.79344  ? 17  LYS B H    1 
ATOM   3017 H HA   . LYS B 1 20  ? -20.80572 -0.76534 3.22521  1.000 30.26543  ? 17  LYS B HA   1 
ATOM   3018 H HB2  . LYS B 1 20  ? -22.88319 -0.90660 4.59470  1.000 30.84018  ? 17  LYS B HB2  1 
ATOM   3019 H HB3  . LYS B 1 20  ? -23.43318 -1.67862 3.31920  1.000 30.84018  ? 17  LYS B HB3  1 
ATOM   3020 H HG2  . LYS B 1 20  ? -21.70890 -3.22465 3.52772  1.000 29.72641  ? 17  LYS B HG2  1 
ATOM   3021 H HG3  . LYS B 1 20  ? -21.19606 -2.46391 4.82530  1.000 29.72641  ? 17  LYS B HG3  1 
ATOM   3022 H HD2  . LYS B 1 20  ? -23.78392 -3.52161 4.73458  1.000 26.62656  ? 17  LYS B HD2  1 
ATOM   3023 H HD3  . LYS B 1 20  ? -22.55969 -4.41581 5.21112  1.000 26.62656  ? 17  LYS B HD3  1 
ATOM   3024 H HE2  . LYS B 1 20  ? -23.26927 -2.00164 6.48337  1.000 25.69096  ? 17  LYS B HE2  1 
ATOM   3025 H HE3  . LYS B 1 20  ? -23.71851 -3.42710 7.02342  1.000 25.69096  ? 17  LYS B HE3  1 
ATOM   3026 H HZ1  . LYS B 1 20  ? -21.49804 -3.90044 7.34827  1.000 22.42864  ? 17  LYS B HZ1  1 
ATOM   3027 H HZ2  . LYS B 1 20  ? -21.12161 -2.57038 6.91518  1.000 22.42864  ? 17  LYS B HZ2  1 
ATOM   3028 H HZ3  . LYS B 1 20  ? -21.87586 -2.74717 8.13919  1.000 22.42864  ? 17  LYS B HZ3  1 
ATOM   3029 N N    . SER B 1 21  ? -22.77703 -0.53626 0.72740  1.000 30.61497  ? 18  SER B N    1 
ATOM   3030 C CA   . SER B 1 21  ? -23.04335 -0.98312 -0.63068 1.000 31.90876  ? 18  SER B CA   1 
ATOM   3031 C C    . SER B 1 21  ? -22.56377 -0.02638 -1.71302 1.000 30.33347  ? 18  SER B C    1 
ATOM   3032 O O    . SER B 1 21  ? -22.31894 -0.47407 -2.83789 1.000 31.50127  ? 18  SER B O    1 
ATOM   3033 C CB   . SER B 1 21  ? -24.55173 -1.20761 -0.82180 1.000 33.70804  ? 18  SER B CB   1 
ATOM   3034 O OG   . SER B 1 21  ? -25.27519 -0.01968 -0.54343 1.000 35.71284  ? 18  SER B OG   1 
ATOM   3035 H H    . SER B 1 21  ? -23.29321 0.09928  0.99054  1.000 36.73797  ? 18  SER B H    1 
ATOM   3036 H HA   . SER B 1 21  ? -22.58424 -1.82676 -0.76629 1.000 38.29051  ? 18  SER B HA   1 
ATOM   3037 H HB2  . SER B 1 21  ? -24.71831 -1.47147 -1.74024 1.000 40.44964  ? 18  SER B HB2  1 
ATOM   3038 H HB3  . SER B 1 21  ? -24.84656 -1.90647 -0.21717 1.000 40.44964  ? 18  SER B HB3  1 
ATOM   3039 H HG   . SER B 1 21  ? -26.09748 -0.15175 -0.65292 1.000 42.85541  ? 18  SER B HG   1 
ATOM   3040 N N    . GLY B 1 22  ? -22.42672 1.26412  -1.41587 1.000 26.20057  ? 19  GLY B N    1 
ATOM   3041 C CA   . GLY B 1 22  ? -22.06155 2.21826  -2.44487 1.000 22.98620  ? 19  GLY B CA   1 
ATOM   3042 C C    . GLY B 1 22  ? -21.41058 3.48615  -1.93480 1.000 20.02564  ? 19  GLY B C    1 
ATOM   3043 O O    . GLY B 1 22  ? -20.54261 3.43942  -1.05791 1.000 20.56362  ? 19  GLY B O    1 
ATOM   3044 H H    . GLY B 1 22  ? -22.53950 1.60312  -0.63359 1.000 31.44069  ? 19  GLY B H    1 
ATOM   3045 H HA2  . GLY B 1 22  ? -21.44069 1.79329  -3.05710 1.000 27.58344  ? 19  GLY B HA2  1 
ATOM   3046 H HA3  . GLY B 1 22  ? -22.86120 2.47218  -2.93170 1.000 27.58344  ? 19  GLY B HA3  1 
ATOM   3047 N N    . THR B 1 23  ? -21.82060 4.62616  -2.49116 1.000 17.91123  ? 20  THR B N    1 
ATOM   3048 C CA   . THR B 1 23  ? -21.28534 5.92781  -2.12331 1.000 16.52497  ? 20  THR B CA   1 
ATOM   3049 C C    . THR B 1 23  ? -22.43282 6.90752  -1.91478 1.000 16.93499  ? 20  THR B C    1 
ATOM   3050 O O    . THR B 1 23  ? -23.54003 6.72103  -2.42739 1.000 19.14083  ? 20  THR B O    1 
ATOM   3051 C CB   . THR B 1 23  ? -20.33505 6.47507  -3.20182 1.000 18.44485  ? 20  THR B CB   1 
ATOM   3052 O OG1  . THR B 1 23  ? -20.99371 6.47948  -4.47531 1.000 22.26077  ? 20  THR B OG1  1 
ATOM   3053 C CG2  . THR B 1 23  ? -19.07415 5.62959  -3.28507 1.000 18.26222  ? 20  THR B CG2  1 
ATOM   3054 H H    . THR B 1 23  ? -22.42538 4.66814  -3.10114 1.000 21.49348  ? 20  THR B H    1 
ATOM   3055 H HA   . THR B 1 23  ? -20.79252 5.84587  -1.29186 1.000 19.82997  ? 20  THR B HA   1 
ATOM   3056 H HB   . THR B 1 23  ? -20.07874 7.38194  -2.97207 1.000 22.13382  ? 20  THR B HB   1 
ATOM   3057 H HG1  . THR B 1 23  ? -21.18916 5.69416  -4.70039 1.000 26.71292  ? 20  THR B HG1  1 
ATOM   3058 H HG21 . THR B 1 23  ? -18.49800 5.96176  -3.99120 1.000 21.91467  ? 20  THR B HG21 1 
ATOM   3059 H HG22 . THR B 1 23  ? -18.59371 5.66660  -2.44322 1.000 21.91467  ? 20  THR B HG22 1 
ATOM   3060 H HG23 . THR B 1 23  ? -19.30533 4.70694  -3.47529 1.000 21.91467  ? 20  THR B HG23 1 
ATOM   3061 N N    . VAL B 1 24  ? -22.14061 7.97138  -1.16650 1.000 15.50178  ? 21  VAL B N    1 
ATOM   3062 C CA   . VAL B 1 24  ? -23.13607 8.94990  -0.74242 1.000 16.59929  ? 21  VAL B CA   1 
ATOM   3063 C C    . VAL B 1 24  ? -22.52926 10.33999 -0.87063 1.000 16.39096  ? 21  VAL B C    1 
ATOM   3064 O O    . VAL B 1 24  ? -21.43187 10.59124 -0.36265 1.000 15.71603  ? 21  VAL B O    1 
ATOM   3065 C CB   . VAL B 1 24  ? -23.56699 8.70611  0.71924  1.000 17.09900  ? 21  VAL B CB   1 
ATOM   3066 C CG1  . VAL B 1 24  ? -24.57028 9.75777  1.16759  1.000 19.05922  ? 21  VAL B CG1  1 
ATOM   3067 C CG2  . VAL B 1 24  ? -24.13451 7.30481  0.89226  1.000 18.26284  ? 21  VAL B CG2  1 
ATOM   3068 H H    . VAL B 1 24  ? -21.34827 8.15131  -0.88471 1.000 18.60214  ? 21  VAL B H    1 
ATOM   3069 H HA   . VAL B 1 24  ? -23.91216 8.89405  -1.32162 1.000 19.91915  ? 21  VAL B HA   1 
ATOM   3070 H HB   . VAL B 1 24  ? -22.78410 8.77948  1.28723  1.000 20.51880  ? 21  VAL B HB   1 
ATOM   3071 H HG11 . VAL B 1 24  ? -24.90939 9.51737  2.04401  1.000 22.87107  ? 21  VAL B HG11 1 
ATOM   3072 H HG12 . VAL B 1 24  ? -24.12705 10.61956 1.20938  1.000 22.87107  ? 21  VAL B HG12 1 
ATOM   3073 H HG13 . VAL B 1 24  ? -25.29933 9.79140  0.52864  1.000 22.87107  ? 21  VAL B HG13 1 
ATOM   3074 H HG21 . VAL B 1 24  ? -24.48293 7.21418  1.79298  1.000 21.91541  ? 21  VAL B HG21 1 
ATOM   3075 H HG22 . VAL B 1 24  ? -24.84636 7.17051  0.24718  1.000 21.91541  ? 21  VAL B HG22 1 
ATOM   3076 H HG23 . VAL B 1 24  ? -23.42758 6.65730  0.74435  1.000 21.91541  ? 21  VAL B HG23 1 
ATOM   3077 N N    . SER B 1 25  ? -23.24229 11.24431 -1.53009 1.000 19.09609  ? 22  SER B N    1 
ATOM   3078 C CA   . SER B 1 25  ? -22.78992 12.63095 -1.60169 1.000 21.39087  ? 22  SER B CA   1 
ATOM   3079 C C    . SER B 1 25  ? -23.10522 13.33934 -0.28890 1.000 22.76761  ? 22  SER B C    1 
ATOM   3080 O O    . SER B 1 25  ? -24.23992 13.25743 0.19038  1.000 21.32066  ? 22  SER B O    1 
ATOM   3081 C CB   . SER B 1 25  ? -23.49575 13.35980 -2.74075 1.000 23.41723  ? 22  SER B CB   1 
ATOM   3082 O OG   . SER B 1 25  ? -23.02963 12.91784 -4.00208 1.000 26.89610  ? 22  SER B OG   1 
ATOM   3083 H H    . SER B 1 25  ? -23.98155 11.08519 -1.93969 1.000 22.91531  ? 22  SER B H    1 
ATOM   3084 H HA   . SER B 1 25  ? -21.83281 12.65384 -1.75766 1.000 25.66904  ? 22  SER B HA   1 
ATOM   3085 H HB2  . SER B 1 25  ? -24.44851 13.18799 -2.68051 1.000 28.10067  ? 22  SER B HB2  1 
ATOM   3086 H HB3  . SER B 1 25  ? -23.32432 14.31099 -2.65855 1.000 28.10067  ? 22  SER B HB3  1 
ATOM   3087 H HG   . SER B 1 25  ? -23.46952 13.28565 -4.61592 1.000 32.27532  ? 22  SER B HG   1 
ATOM   3088 N N    . PRO B 1 26  ? -22.13801 14.03767 0.31991  1.000 25.41467  ? 23  PRO B N    1 
ATOM   3089 C CA   . PRO B 1 26  ? -22.43500 14.75145 1.57543  1.000 26.72488  ? 23  PRO B CA   1 
ATOM   3090 C C    . PRO B 1 26  ? -23.71659 15.56428 1.53794  1.000 27.35329  ? 23  PRO B C    1 
ATOM   3091 O O    . PRO B 1 26  ? -24.42120 15.65791 2.55033  1.000 24.82348  ? 23  PRO B O    1 
ATOM   3092 C CB   . PRO B 1 26  ? -21.20007 15.64529 1.76347  1.000 26.80759  ? 23  PRO B CB   1 
ATOM   3093 C CG   . PRO B 1 26  ? -20.09653 14.87822 1.12520  1.000 27.00347  ? 23  PRO B CG   1 
ATOM   3094 C CD   . PRO B 1 26  ? -20.70526 14.11159 -0.02958 1.000 26.62240  ? 23  PRO B CD   1 
ATOM   3095 H HA   . PRO B 1 26  ? -22.48925 14.11202 2.30281  1.000 32.06985  ? 23  PRO B HA   1 
ATOM   3096 H HB2  . PRO B 1 26  ? -21.33505 16.49824 1.32171  1.000 32.16910  ? 23  PRO B HB2  1 
ATOM   3097 H HB3  . PRO B 1 26  ? -21.02941 15.78429 2.70817  1.000 32.16910  ? 23  PRO B HB3  1 
ATOM   3098 H HG2  . PRO B 1 26  ? -19.41861 15.49358 0.80480  1.000 32.40416  ? 23  PRO B HG2  1 
ATOM   3099 H HG3  . PRO B 1 26  ? -19.71091 14.26762 1.77278  1.000 32.40416  ? 23  PRO B HG3  1 
ATOM   3100 H HD2  . PRO B 1 26  ? -20.57889 14.58917 -0.86435 1.000 31.94688  ? 23  PRO B HD2  1 
ATOM   3101 H HD3  . PRO B 1 26  ? -20.32050 13.22349 -0.09391 1.000 31.94688  ? 23  PRO B HD3  1 
ATOM   3102 N N    . ILE B 1 27  ? -24.04141 16.15343 0.38650  1.000 30.02303  ? 24  ILE B N    1 
ATOM   3103 C CA   . ILE B 1 27  ? -25.24194 16.97170 0.26660  1.000 32.76810  ? 24  ILE B CA   1 
ATOM   3104 C C    . ILE B 1 27  ? -26.50863 16.16851 0.52793  1.000 29.93891  ? 24  ILE B C    1 
ATOM   3105 O O    . ILE B 1 27  ? -27.53487 16.74651 0.90071  1.000 30.46347  ? 24  ILE B O    1 
ATOM   3106 C CB   . ILE B 1 27  ? -25.23787 17.64981 -1.12101 1.000 37.95036  ? 24  ILE B CB   1 
ATOM   3107 C CG1  . ILE B 1 27  ? -26.20258 18.83405 -1.15085 1.000 41.34609  ? 24  ILE B CG1  1 
ATOM   3108 C CG2  . ILE B 1 27  ? -25.58917 16.64131 -2.20772 1.000 39.82429  ? 24  ILE B CG2  1 
ATOM   3109 C CD1  . ILE B 1 27  ? -26.02676 19.71711 -2.37284 1.000 42.89961  ? 24  ILE B CD1  1 
ATOM   3110 H H    . ILE B 1 27  ? -23.58236 16.09382 -0.33829 1.000 36.02763  ? 24  ILE B H    1 
ATOM   3111 H HA   . ILE B 1 27  ? -25.23377 17.66888 0.94097  1.000 39.32172  ? 24  ILE B HA   1 
ATOM   3112 H HB   . ILE B 1 27  ? -24.34378 17.98633 -1.28912 1.000 45.54043  ? 24  ILE B HB   1 
ATOM   3113 H HG12 . ILE B 1 27  ? -27.11250 18.49797 -1.15382 1.000 49.61531  ? 24  ILE B HG12 1 
ATOM   3114 H HG13 . ILE B 1 27  ? -26.05339 19.38067 -0.36355 1.000 49.61531  ? 24  ILE B HG13 1 
ATOM   3115 H HG21 . ILE B 1 27  ? -25.29714 16.98700 -3.06570 1.000 47.78915  ? 24  ILE B HG21 1 
ATOM   3116 H HG22 . ILE B 1 27  ? -25.13906 15.80322 -2.01823 1.000 47.78915  ? 24  ILE B HG22 1 
ATOM   3117 H HG23 . ILE B 1 27  ? -26.54974 16.50662 -2.21497 1.000 47.78915  ? 24  ILE B HG23 1 
ATOM   3118 H HD11 . ILE B 1 27  ? -26.63282 20.47161 -2.30708 1.000 51.47953  ? 24  ILE B HD11 1 
ATOM   3119 H HD12 . ILE B 1 27  ? -25.10968 20.03140 -2.40604 1.000 51.47953  ? 24  ILE B HD12 1 
ATOM   3120 H HD13 . ILE B 1 27  ? -26.22803 19.19950 -3.16812 1.000 51.47953  ? 24  ILE B HD13 1 
ATOM   3121 N N    . SER B 1 28  ? -26.45797 14.84094 0.36465  1.000 27.30634  ? 25  SER B N    1 
ATOM   3122 C CA   A SER B 1 28  ? -27.62237 13.99814 0.60805  0.527 25.69361  ? 25  SER B CA   1 
ATOM   3123 C CA   B SER B 1 28  ? -27.62789 14.00542 0.60689  0.473 25.71361  ? 25  SER B CA   1 
ATOM   3124 C C    . SER B 1 28  ? -27.96285 13.86792 2.08725  1.000 23.69881  ? 25  SER B C    1 
ATOM   3125 O O    . SER B 1 28  ? -28.98351 13.25705 2.41986  1.000 21.68310  ? 25  SER B O    1 
ATOM   3126 C CB   A SER B 1 28  ? -27.38486 12.60238 0.02723  0.527 27.67361  ? 25  SER B CB   1 
ATOM   3127 C CB   B SER B 1 28  ? -27.40688 12.61258 0.01419  0.473 27.67361  ? 25  SER B CB   1 
ATOM   3128 O OG   A SER B 1 28  ? -27.22380 12.65914 -1.37828 0.527 33.66361  ? 25  SER B OG   1 
ATOM   3129 O OG   B SER B 1 28  ? -26.31652 11.96320 0.64236  0.473 33.64361  ? 25  SER B OG   1 
ATOM   3130 H H    A SER B 1 28  ? -25.75848 14.40833 0.11334  0.527 32.76760  ? 25  SER B H    1 
ATOM   3131 H H    B SER B 1 28  ? -25.75897 14.40642 0.11530  0.473 32.76760  ? 25  SER B H    1 
ATOM   3132 H HA   A SER B 1 28  ? -28.38430 14.39514 0.15777  0.527 30.83233  ? 25  SER B HA   1 
ATOM   3133 H HA   B SER B 1 28  ? -28.38829 14.41182 0.16244  0.473 30.85633  ? 25  SER B HA   1 
ATOM   3134 H HB2  A SER B 1 28  ? -26.58112 12.22929 0.42184  0.527 33.20833  ? 25  SER B HB2  1 
ATOM   3135 H HB2  B SER B 1 28  ? -28.20845 12.08259 0.14648  0.473 33.20833  ? 25  SER B HB2  1 
ATOM   3136 H HB3  A SER B 1 28  ? -28.14789 12.04056 0.23468  0.527 33.20833  ? 25  SER B HB3  1 
ATOM   3137 H HB3  B SER B 1 28  ? -27.21906 12.69916 -0.93351 0.473 33.20833  ? 25  SER B HB3  1 
ATOM   3138 H HG   A SER B 1 28  ? -26.57118 13.15081 -1.57305 0.527 40.39633  ? 25  SER B HG   1 
ATOM   3139 H HG   B SER B 1 28  ? -25.61208 12.40525 0.52422  0.473 40.37233  ? 25  SER B HG   1 
ATOM   3140 N N    . LEU B 1 29  ? -27.13573 14.40589 2.97274  1.000 20.17187  ? 26  LEU B N    1 
ATOM   3141 C CA   . LEU B 1 29  ? -27.40017 14.38638 4.40399  1.000 17.32301  ? 26  LEU B CA   1 
ATOM   3142 C C    . LEU B 1 29  ? -28.18964 15.61142 4.85019  1.000 15.74254  ? 26  LEU B C    1 
ATOM   3143 O O    . LEU B 1 29  ? -28.32277 15.85161 6.05448  1.000 13.84974  ? 26  LEU B O    1 
ATOM   3144 C CB   . LEU B 1 29  ? -26.07722 14.25680 5.16142  1.000 17.20928  ? 26  LEU B CB   1 
ATOM   3145 C CG   . LEU B 1 29  ? -25.46836 12.84826 5.20332  1.000 19.29499  ? 26  LEU B CG   1 
ATOM   3146 C CD1  . LEU B 1 29  ? -25.17701 12.26257 3.83058  1.000 23.20218  ? 26  LEU B CD1  1 
ATOM   3147 C CD2  . LEU B 1 29  ? -24.18968 12.86005 6.03583  1.000 18.05574  ? 26  LEU B CD2  1 
ATOM   3148 H H    . LEU B 1 29  ? -26.39851 14.79667 2.76441  1.000 24.20624  ? 26  LEU B H    1 
ATOM   3149 H HA   . LEU B 1 29  ? -27.93212 13.60972 4.63792  1.000 20.78761  ? 26  LEU B HA   1 
ATOM   3150 H HB2  . LEU B 1 29  ? -25.42714 14.83946 4.73857  1.000 20.65114  ? 26  LEU B HB2  1 
ATOM   3151 H HB3  . LEU B 1 29  ? -26.22445 14.53469 6.07902  1.000 20.65114  ? 26  LEU B HB3  1 
ATOM   3152 H HG   . LEU B 1 29  ? -26.13183 12.26859 5.60915  1.000 23.15399  ? 26  LEU B HG   1 
ATOM   3153 H HD11 . LEU B 1 29  ? -24.72465 11.41150 3.93987  1.000 27.84261  ? 26  LEU B HD11 1 
ATOM   3154 H HD12 . LEU B 1 29  ? -26.01426 12.13386 3.35797  1.000 27.84261  ? 26  LEU B HD12 1 
ATOM   3155 H HD13 . LEU B 1 29  ? -24.61061 12.87745 3.33862  1.000 27.84261  ? 26  LEU B HD13 1 
ATOM   3156 H HD21 . LEU B 1 29  ? -23.96379 11.94903 6.28059  1.000 21.66689  ? 26  LEU B HD21 1 
ATOM   3157 H HD22 . LEU B 1 29  ? -23.47356 13.24834 5.50924  1.000 21.66689  ? 26  LEU B HD22 1 
ATOM   3158 H HD23 . LEU B 1 29  ? -24.33777 13.39012 6.83458  1.000 21.66689  ? 26  LEU B HD23 1 
ATOM   3159 N N    . ALA B 1 30  ? -28.74131 16.36419 3.89935  1.000 17.04123  ? 27  ALA B N    1 
ATOM   3160 C CA   . ALA B 1 30  ? -29.45285 17.59527 4.20691  1.000 15.78057  ? 27  ALA B CA   1 
ATOM   3161 C C    . ALA B 1 30  ? -30.53848 17.36351 5.24814  1.000 16.63474  ? 27  ALA B C    1 
ATOM   3162 O O    . ALA B 1 30  ? -31.23197 16.34331 5.23619  1.000 18.00597  ? 27  ALA B O    1 
ATOM   3163 C CB   . ALA B 1 30  ? -30.08481 18.14116 2.92337  1.000 18.45674  ? 27  ALA B CB   1 
ATOM   3164 H H    . ALA B 1 30  ? -28.71580 16.17953 3.05980  1.000 20.44948  ? 27  ALA B H    1 
ATOM   3165 H HA   . ALA B 1 30  ? -28.82890 18.24503 4.56663  1.000 18.93668  ? 27  ALA B HA   1 
ATOM   3166 H HB1  . ALA B 1 30  ? -30.55188 18.96642 3.12757  1.000 22.14809  ? 27  ALA B HB1  1 
ATOM   3167 H HB2  . ALA B 1 30  ? -29.38467 18.30943 2.27346  1.000 22.14809  ? 27  ALA B HB2  1 
ATOM   3168 H HB3  . ALA B 1 30  ? -30.70888 17.48538 2.57497  1.000 22.14809  ? 27  ALA B HB3  1 
ATOM   3169 N N    . GLY B 1 31  ? -30.68309 18.33474 6.14939  1.000 15.43200  ? 28  GLY B N    1 
ATOM   3170 C CA   . GLY B 1 31  ? -31.70162 18.30670 7.17388  1.000 15.33176  ? 28  GLY B CA   1 
ATOM   3171 C C    . GLY B 1 31  ? -31.39706 17.44155 8.37511  1.000 13.33755  ? 28  GLY B C    1 
ATOM   3172 O O    . GLY B 1 31  ? -32.18621 17.43977 9.32847  1.000 16.15641  ? 28  GLY B O    1 
ATOM   3173 H H    . GLY B 1 31  ? -30.18595 19.03573 6.18201  1.000 18.51840  ? 28  GLY B H    1 
ATOM   3174 H HA2  . GLY B 1 31  ? -31.84147 19.21188 7.49324  1.000 18.39811  ? 28  GLY B HA2  1 
ATOM   3175 H HA3  . GLY B 1 31  ? -32.52547 17.98013 6.77952  1.000 18.39811  ? 28  GLY B HA3  1 
ATOM   3176 N N    . LYS B 1 32  ? -30.27558 16.73272 8.38091  1.000 13.04324  ? 29  LYS B N    1 
ATOM   3177 C CA   A LYS B 1 32  ? -29.94561 15.79632 9.44139  0.396 12.73361  ? 29  LYS B CA   1 
ATOM   3178 C CA   B LYS B 1 32  ? -29.95319 15.80183 9.44839  0.604 12.71361  ? 29  LYS B CA   1 
ATOM   3179 C C    . LYS B 1 32  ? -28.93593 16.39586 10.41221 1.000 11.90700  ? 29  LYS B C    1 
ATOM   3180 O O    . LYS B 1 32  ? -28.20398 17.33316 10.08766 1.000 13.24374  ? 29  LYS B O    1 
ATOM   3181 C CB   A LYS B 1 32  ? -29.34211 14.51679 8.85186  0.396 13.52361  ? 29  LYS B CB   1 
ATOM   3182 C CB   B LYS B 1 32  ? -29.38783 14.50382 8.86270  0.604 13.08361  ? 29  LYS B CB   1 
ATOM   3183 C CG   A LYS B 1 32  ? -30.27256 13.74350 7.94339  0.396 15.83361  ? 29  LYS B CG   1 
ATOM   3184 C CG   B LYS B 1 32  ? -30.39363 13.74129 8.03147  0.604 13.81361  ? 29  LYS B CG   1 
ATOM   3185 C CD   A LYS B 1 32  ? -29.61989 12.46169 7.44920  0.396 18.18361  ? 29  LYS B CD   1 
ATOM   3186 C CD   B LYS B 1 32  ? -29.85137 12.41797 7.53356  0.604 13.89361  ? 29  LYS B CD   1 
ATOM   3187 C CE   A LYS B 1 32  ? -30.52038 11.73357 6.46592  0.396 21.57361  ? 29  LYS B CE   1 
ATOM   3188 C CE   B LYS B 1 32  ? -30.91432 11.70171 6.71791  0.604 15.87361  ? 29  LYS B CE   1 
ATOM   3189 N NZ   A LYS B 1 32  ? -31.88602 11.51864 7.01922  0.396 21.93361  ? 29  LYS B NZ   1 
ATOM   3190 N NZ   B LYS B 1 32  ? -30.55454 10.28916 6.44362  0.604 16.88361  ? 29  LYS B NZ   1 
ATOM   3191 H H    A LYS B 1 32  ? -29.67672 16.77943 7.76546  0.396 15.65189  ? 29  LYS B H    1 
ATOM   3192 H H    B LYS B 1 32  ? -29.67639 16.77596 7.76552  0.604 15.65189  ? 29  LYS B H    1 
ATOM   3193 H HA   A LYS B 1 32  ? -30.75816 15.58455 9.92700  0.396 15.28033  ? 29  LYS B HA   1 
ATOM   3194 H HA   B LYS B 1 32  ? -30.76224 15.60670 9.94666  0.604 15.25633  ? 29  LYS B HA   1 
ATOM   3195 H HB2  A LYS B 1 32  ? -28.55817 14.75582 8.33302  0.396 16.22833  ? 29  LYS B HB2  1 
ATOM   3196 H HB2  B LYS B 1 32  ? -28.63165 14.71853 8.29437  0.604 15.70033  ? 29  LYS B HB2  1 
ATOM   3197 H HB3  A LYS B 1 32  ? -29.09051 13.92944 9.58166  0.396 16.22833  ? 29  LYS B HB3  1 
ATOM   3198 H HB3  B LYS B 1 32  ? -29.10342 13.92844 9.58999  0.604 15.70033  ? 29  LYS B HB3  1 
ATOM   3199 H HG2  A LYS B 1 32  ? -31.07763 13.50874 8.43089  0.396 19.00033  ? 29  LYS B HG2  1 
ATOM   3200 H HG2  B LYS B 1 32  ? -31.17907 13.56018 8.57108  0.604 16.57633  ? 29  LYS B HG2  1 
ATOM   3201 H HG3  A LYS B 1 32  ? -30.49805 14.28866 7.17342  0.396 19.00033  ? 29  LYS B HG3  1 
ATOM   3202 H HG3  B LYS B 1 32  ? -30.63749 14.27560 7.25949  0.604 16.57633  ? 29  LYS B HG3  1 
ATOM   3203 H HD2  A LYS B 1 32  ? -28.78655 12.67564 7.00124  0.396 21.82033  ? 29  LYS B HD2  1 
ATOM   3204 H HD2  B LYS B 1 32  ? -29.07681 12.57202 6.97033  0.604 16.67233  ? 29  LYS B HD2  1 
ATOM   3205 H HD3  A LYS B 1 32  ? -29.45040 11.87450 8.20245  0.396 21.82033  ? 29  LYS B HD3  1 
ATOM   3206 H HD3  B LYS B 1 32  ? -29.60724 11.85897 8.28776  0.604 16.67233  ? 29  LYS B HD3  1 
ATOM   3207 H HE2  A LYS B 1 32  ? -30.60072 12.26033 5.65539  0.396 25.88833  ? 29  LYS B HE2  1 
ATOM   3208 H HE2  B LYS B 1 32  ? -31.75125 11.71033 7.20819  0.604 19.04833  ? 29  LYS B HE2  1 
ATOM   3209 H HE3  A LYS B 1 32  ? -30.13582 10.86682 6.26154  0.396 25.88833  ? 29  LYS B HE3  1 
ATOM   3210 H HE3  B LYS B 1 32  ? -31.02311 12.15607 5.86784  0.604 19.04833  ? 29  LYS B HE3  1 
ATOM   3211 H HZ1  A LYS B 1 32  ? -32.37367 11.04004 6.44891  0.396 26.32033  ? 29  LYS B HZ1  1 
ATOM   3212 H HZ1  B LYS B 1 32  ? -31.20677 9.89221  5.98632  0.604 20.26033  ? 29  LYS B HZ1  1 
ATOM   3213 H HZ2  A LYS B 1 32  ? -31.83566 11.08216 7.79320  0.396 26.32033  ? 29  LYS B HZ2  1 
ATOM   3214 H HZ2  B LYS B 1 32  ? -29.80408 10.25332 5.96652  0.604 20.26033  ? 29  LYS B HZ2  1 
ATOM   3215 H HZ3  A LYS B 1 32  ? -32.28625 12.30192 7.15485  0.396 26.32033  ? 29  LYS B HZ3  1 
ATOM   3216 H HZ3  B LYS B 1 32  ? -30.43126 9.85228  7.20915  0.604 20.26033  ? 29  LYS B HZ3  1 
ATOM   3217 N N    . THR B 1 33  ? -28.91106 15.83663 11.61843 1.000 10.67037  ? 30  THR B N    1 
ATOM   3218 C CA   . THR B 1 33  ? -27.77033 16.01031 12.50315 1.000 9.99636   ? 30  THR B CA   1 
ATOM   3219 C C    . THR B 1 33  ? -26.74535 14.96335 12.08455 1.000 10.29679  ? 30  THR B C    1 
ATOM   3220 O O    . THR B 1 33  ? -27.09321 13.79402 11.89048 1.000 11.30735  ? 30  THR B O    1 
ATOM   3221 C CB   . THR B 1 33  ? -28.17282 15.78597 13.95377 1.000 10.69078  ? 30  THR B CB   1 
ATOM   3222 O OG1  . THR B 1 33  ? -29.22382 16.69259 14.30178 1.000 12.44633  ? 30  THR B OG1  1 
ATOM   3223 C CG2  . THR B 1 33  ? -26.98806 16.02825 14.87187 1.000 11.94253  ? 30  THR B CG2  1 
ATOM   3224 H H    . THR B 1 33  ? -29.54276 15.35308 11.94514 1.000 12.80445  ? 30  THR B H    1 
ATOM   3225 H HA   . THR B 1 33  ? -27.40668 16.90755 12.44305 1.000 11.99563  ? 30  THR B HA   1 
ATOM   3226 H HB   . THR B 1 33  ? -28.47645 14.87210 14.07016 1.000 12.82893  ? 30  THR B HB   1 
ATOM   3227 H HG1  . THR B 1 33  ? -29.88168 16.57913 13.79193 1.000 14.93560  ? 30  THR B HG1  1 
ATOM   3228 H HG21 . THR B 1 33  ? -27.26986 15.97413 15.79846 1.000 14.33104  ? 30  THR B HG21 1 
ATOM   3229 H HG22 . THR B 1 33  ? -26.30245 15.36098 14.71187 1.000 14.33104  ? 30  THR B HG22 1 
ATOM   3230 H HG23 . THR B 1 33  ? -26.61522 16.90845 14.70712 1.000 14.33104  ? 30  THR B HG23 1 
ATOM   3231 N N    . VAL B 1 34  ? -25.49689 15.37591 11.90672 1.000 10.85323  ? 31  VAL B N    1 
ATOM   3232 C CA   . VAL B 1 34  ? -24.45877 14.48546 11.40169 1.000 10.08774  ? 31  VAL B CA   1 
ATOM   3233 C C    . VAL B 1 34  ? -23.37517 14.36019 12.45655 1.000 7.92661   ? 31  VAL B C    1 
ATOM   3234 O O    . VAL B 1 34  ? -22.78960 15.36844 12.87253 1.000 9.58644   ? 31  VAL B O    1 
ATOM   3235 C CB   . VAL B 1 34  ? -23.87774 14.97830 10.06766 1.000 10.81567  ? 31  VAL B CB   1 
ATOM   3236 C CG1  . VAL B 1 34  ? -22.77020 14.04293 9.58951  1.000 12.76916  ? 31  VAL B CG1  1 
ATOM   3237 C CG2  . VAL B 1 34  ? -24.98371 15.08708 9.03762  1.000 12.20117  ? 31  VAL B CG2  1 
ATOM   3238 H H    . VAL B 1 34  ? -25.22432 16.17444 12.07303 1.000 13.02388  ? 31  VAL B H    1 
ATOM   3239 H HA   . VAL B 1 34  ? -24.84115 13.60502 11.26201 1.000 12.10528  ? 31  VAL B HA   1 
ATOM   3240 H HB   . VAL B 1 34  ? -23.48587 15.85735 10.18847 1.000 12.97880  ? 31  VAL B HB   1 
ATOM   3241 H HG11 . VAL B 1 34  ? -22.51174 14.29397 8.68891  1.000 15.32299  ? 31  VAL B HG11 1 
ATOM   3242 H HG12 . VAL B 1 34  ? -22.00973 14.12292 10.18632 1.000 15.32299  ? 31  VAL B HG12 1 
ATOM   3243 H HG13 . VAL B 1 34  ? -23.10175 13.13138 9.59653  1.000 15.32299  ? 31  VAL B HG13 1 
ATOM   3244 H HG21 . VAL B 1 34  ? -24.60026 15.36322 8.19050  1.000 14.64140  ? 31  VAL B HG21 1 
ATOM   3245 H HG22 . VAL B 1 34  ? -25.41129 14.22180 8.94077  1.000 14.64140  ? 31  VAL B HG22 1 
ATOM   3246 H HG23 . VAL B 1 34  ? -25.63109 15.74422 9.33755  1.000 14.64140  ? 31  VAL B HG23 1 
ATOM   3247 N N    . PHE B 1 35  ? -23.11240 13.12402 12.89029 1.000 7.99827   ? 32  PHE B N    1 
ATOM   3248 C CA   A PHE B 1 35  ? -22.08263 12.84842 13.88392 0.729 9.17363   ? 32  PHE B CA   1 
ATOM   3249 C CA   B PHE B 1 35  ? -22.08631 12.83208 13.88440 0.271 9.17363   ? 32  PHE B CA   1 
ATOM   3250 C C    . PHE B 1 35  ? -20.80947 12.42767 13.16099 1.000 8.67684   ? 32  PHE B C    1 
ATOM   3251 O O    . PHE B 1 35  ? -20.76440 11.37309 12.52091 1.000 10.38722  ? 32  PHE B O    1 
ATOM   3252 C CB   A PHE B 1 35  ? -22.54518 11.76296 14.85335 0.729 11.13176  ? 32  PHE B CB   1 
ATOM   3253 C CB   B PHE B 1 35  ? -22.48412 11.62294 14.74262 0.271 11.13176  ? 32  PHE B CB   1 
ATOM   3254 C CG   A PHE B 1 35  ? -23.55412 12.24019 15.86276 0.729 14.24266  ? 32  PHE B CG   1 
ATOM   3255 C CG   B PHE B 1 35  ? -23.55923 11.86647 15.76453 0.271 14.24266  ? 32  PHE B CG   1 
ATOM   3256 C CD1  A PHE B 1 35  ? -24.88972 12.35994 15.52085 0.729 16.27711  ? 32  PHE B CD1  1 
ATOM   3257 C CD1  B PHE B 1 35  ? -24.21582 13.07739 15.87394 0.271 16.27711  ? 32  PHE B CD1  1 
ATOM   3258 C CD2  A PHE B 1 35  ? -23.16731 12.57803 17.14972 0.729 15.79284  ? 32  PHE B CD2  1 
ATOM   3259 C CD2  B PHE B 1 35  ? -23.90359 10.84189 16.63598 0.271 15.79284  ? 32  PHE B CD2  1 
ATOM   3260 C CE1  A PHE B 1 35  ? -25.82045 12.80146 16.44153 0.729 17.17459  ? 32  PHE B CE1  1 
ATOM   3261 C CE1  B PHE B 1 35  ? -25.20075 13.25575 16.83704 0.271 17.17459  ? 32  PHE B CE1  1 
ATOM   3262 C CE2  A PHE B 1 35  ? -24.09938 13.01770 18.07744 0.729 16.80349  ? 32  PHE B CE2  1 
ATOM   3263 C CE2  B PHE B 1 35  ? -24.87636 11.01484 17.59318 0.271 16.80349  ? 32  PHE B CE2  1 
ATOM   3264 C CZ   A PHE B 1 35  ? -25.42437 13.13365 17.71827 0.729 17.39040  ? 32  PHE B CZ   1 
ATOM   3265 C CZ   B PHE B 1 35  ? -25.52694 12.22054 17.69596 0.271 17.39040  ? 32  PHE B CZ   1 
ATOM   3266 H H    . PHE B 1 35  ? -23.52773 12.42305 12.61508 1.000 9.59792   ? 32  PHE B H    1 
ATOM   3267 H HA   . PHE B 1 35  ? -21.89758 13.65590 14.38852 1.000 11.00836  ? 32  PHE B HA   1 
ATOM   3268 H HB2  A PHE B 1 35  ? -22.95234 11.04404 14.34516 0.729 13.35811  ? 32  PHE B HB2  1 
ATOM   3269 H HB2  B PHE B 1 35  ? -22.80376 10.92345 14.15149 0.271 13.35811  ? 32  PHE B HB2  1 
ATOM   3270 H HB3  A PHE B 1 35  ? -21.77461 11.43039 15.33969 0.729 13.35811  ? 32  PHE B HB3  1 
ATOM   3271 H HB3  B PHE B 1 35  ? -21.69724 11.31881 15.22141 0.271 13.35811  ? 32  PHE B HB3  1 
ATOM   3272 H HD1  A PHE B 1 35  ? -25.16444 12.14030 14.65992 0.729 19.53254  ? 32  PHE B HD1  1 
ATOM   3273 H HD1  B PHE B 1 35  ? -23.99734 13.77600 15.30026 0.271 19.53254  ? 32  PHE B HD1  1 
ATOM   3274 H HD2  A PHE B 1 35  ? -22.27261 12.50913 17.39398 0.729 18.95141  ? 32  PHE B HD2  1 
ATOM   3275 H HD2  B PHE B 1 35  ? -23.46812 10.02270 16.57133 0.271 18.95141  ? 32  PHE B HD2  1 
ATOM   3276 H HE1  A PHE B 1 35  ? -26.71529 12.87444 16.19900 0.729 20.60951  ? 32  PHE B HE1  1 
ATOM   3277 H HE1  B PHE B 1 35  ? -25.64160 14.07181 16.90483 0.271 20.60951  ? 32  PHE B HE1  1 
ATOM   3278 H HE2  A PHE B 1 35  ? -23.83043 13.23404 18.94102 0.729 20.16419  ? 32  PHE B HE2  1 
ATOM   3279 H HE2  B PHE B 1 35  ? -25.09301 10.31753 18.16913 0.271 20.16419  ? 32  PHE B HE2  1 
ATOM   3280 H HZ   A PHE B 1 35  ? -26.05005 13.43558 18.33654 0.729 20.86849  ? 32  PHE B HZ   1 
ATOM   3281 H HZ   B PHE B 1 35  ? -26.18541 12.34094 18.34157 0.271 20.86849  ? 32  PHE B HZ   1 
ATOM   3282 N N    . PHE B 1 36  ? -19.76787 13.24674 13.28075 1.000 8.73460   ? 33  PHE B N    1 
ATOM   3283 C CA   . PHE B 1 36  ? -18.43433 12.82555 12.87244 1.000 8.94200   ? 33  PHE B CA   1 
ATOM   3284 C C    . PHE B 1 36  ? -17.87552 11.97796 14.01171 1.000 9.02758   ? 33  PHE B C    1 
ATOM   3285 O O    . PHE B 1 36  ? -17.72295 12.47019 15.13698 1.000 10.06003  ? 33  PHE B O    1 
ATOM   3286 C CB   . PHE B 1 36  ? -17.52088 14.02002 12.61821 1.000 10.68634  ? 33  PHE B CB   1 
ATOM   3287 C CG   . PHE B 1 36  ? -17.83632 14.78029 11.35996 1.000 10.73982  ? 33  PHE B CG   1 
ATOM   3288 C CD1  . PHE B 1 36  ? -17.61780 14.22277 10.11224 1.000 11.47094  ? 33  PHE B CD1  1 
ATOM   3289 C CD2  . PHE B 1 36  ? -18.31881 16.07346 11.43222 1.000 13.38009  ? 33  PHE B CD2  1 
ATOM   3290 C CE1  . PHE B 1 36  ? -17.89800 14.94080 8.96458  1.000 11.79890  ? 33  PHE B CE1  1 
ATOM   3291 C CE2  . PHE B 1 36  ? -18.59904 16.78986 10.29409 1.000 14.41824  ? 33  PHE B CE2  1 
ATOM   3292 C CZ   . PHE B 1 36  ? -18.38977 16.22507 9.05872  1.000 14.13464  ? 33  PHE B CZ   1 
ATOM   3293 H H    . PHE B 1 36  ? -19.80880 14.04662 13.59399 1.000 10.48152  ? 33  PHE B H    1 
ATOM   3294 H HA   . PHE B 1 36  ? -18.48053 12.32115 12.04518 1.000 10.73040  ? 33  PHE B HA   1 
ATOM   3295 H HB2  . PHE B 1 36  ? -17.60209 14.63657 13.36263 1.000 12.82361  ? 33  PHE B HB2  1 
ATOM   3296 H HB3  . PHE B 1 36  ? -16.60701 13.70237 12.54870 1.000 12.82361  ? 33  PHE B HB3  1 
ATOM   3297 H HD1  . PHE B 1 36  ? -17.28003 13.35886 10.04536 1.000 13.76513  ? 33  PHE B HD1  1 
ATOM   3298 H HD2  . PHE B 1 36  ? -18.45595 16.46484 12.26464 1.000 16.05611  ? 33  PHE B HD2  1 
ATOM   3299 H HE1  . PHE B 1 36  ? -17.75477 14.55754 8.12942  1.000 14.15868  ? 33  PHE B HE1  1 
ATOM   3300 H HE2  . PHE B 1 36  ? -18.93013 17.65646 10.35947 1.000 17.30188  ? 33  PHE B HE2  1 
ATOM   3301 H HZ   . PHE B 1 36  ? -18.57970 16.70869 8.28739  1.000 16.96156  ? 33  PHE B HZ   1 
ATOM   3302 N N    . TYR B 1 37  ? -17.60751 10.70569 13.73397 1.000 8.88051   ? 34  TYR B N    1 
ATOM   3303 C CA   . TYR B 1 37  ? -17.14900 9.74314  14.73395 1.000 8.46334   ? 34  TYR B CA   1 
ATOM   3304 C C    . TYR B 1 37  ? -15.67367 9.46508  14.46677 1.000 8.62174   ? 34  TYR B C    1 
ATOM   3305 O O    . TYR B 1 37  ? -15.32744 8.74794  13.52270 1.000 7.98822   ? 34  TYR B O    1 
ATOM   3306 C CB   . TYR B 1 37  ? -17.97504 8.46153  14.65590 1.000 8.77459   ? 34  TYR B CB   1 
ATOM   3307 C CG   . TYR B 1 37  ? -17.54248 7.36990  15.61367 1.000 7.94893   ? 34  TYR B CG   1 
ATOM   3308 C CD1  . TYR B 1 37  ? -16.98963 7.67546  16.85253 1.000 9.85350   ? 34  TYR B CD1  1 
ATOM   3309 C CD2  . TYR B 1 37  ? -17.68958 6.02951  15.27556 1.000 8.30654   ? 34  TYR B CD2  1 
ATOM   3310 C CE1  . TYR B 1 37  ? -16.59390 6.67805  17.72407 1.000 8.56739   ? 34  TYR B CE1  1 
ATOM   3311 C CE2  . TYR B 1 37  ? -17.29364 5.02683  16.14101 1.000 8.04946   ? 34  TYR B CE2  1 
ATOM   3312 C CZ   . TYR B 1 37  ? -16.75190 5.36124  17.36585 1.000 8.19931   ? 34  TYR B CZ   1 
ATOM   3313 O OH   . TYR B 1 37  ? -16.35567 4.38155  18.24126 1.000 9.66626   ? 34  TYR B OH   1 
ATOM   3314 H H    . TYR B 1 37  ? -17.68604 10.36492 12.94828 1.000 10.65661  ? 34  TYR B H    1 
ATOM   3315 H HA   . TYR B 1 37  ? -17.23965 10.12256 15.62205 1.000 10.15600  ? 34  TYR B HA   1 
ATOM   3316 H HB2  . TYR B 1 37  ? -18.89894 8.67763  14.85745 1.000 10.52951  ? 34  TYR B HB2  1 
ATOM   3317 H HB3  . TYR B 1 37  ? -17.90636 8.10493  13.75644 1.000 10.52951  ? 34  TYR B HB3  1 
ATOM   3318 H HD1  . TYR B 1 37  ? -16.88433 8.56603  17.09892 1.000 11.82420  ? 34  TYR B HD1  1 
ATOM   3319 H HD2  . TYR B 1 37  ? -18.06062 5.80353  14.45327 1.000 9.96785   ? 34  TYR B HD2  1 
ATOM   3320 H HE1  . TYR B 1 37  ? -16.22284 6.89723  18.54819 1.000 10.28087  ? 34  TYR B HE1  1 
ATOM   3321 H HE2  . TYR B 1 37  ? -17.39150 4.13397  15.89991 1.000 9.65936   ? 34  TYR B HE2  1 
ATOM   3322 H HH   . TYR B 1 37  ? -16.40328 3.62905  17.87103 1.000 11.59951  ? 34  TYR B HH   1 
ATOM   3323 N N    . PHE B 1 38  ? -14.81339 10.06027 15.29352 1.000 7.43330   ? 35  PHE B N    1 
ATOM   3324 C CA   . PHE B 1 38  ? -13.37034 9.86028  15.21851 1.000 6.85433   ? 35  PHE B CA   1 
ATOM   3325 C C    . PHE B 1 38  ? -13.02698 8.60209  16.00928 1.000 8.12150   ? 35  PHE B C    1 
ATOM   3326 O O    . PHE B 1 38  ? -13.31159 8.52528  17.20985 1.000 8.74168   ? 35  PHE B O    1 
ATOM   3327 C CB   . PHE B 1 38  ? -12.65353 11.07948 15.79891 1.000 7.36829   ? 35  PHE B CB   1 
ATOM   3328 C CG   . PHE B 1 38  ? -12.91402 12.36381 15.04410 1.000 7.78743   ? 35  PHE B CG   1 
ATOM   3329 C CD1  . PHE B 1 38  ? -14.09593 13.06790 15.21917 1.000 9.01778   ? 35  PHE B CD1  1 
ATOM   3330 C CD2  . PHE B 1 38  ? -11.97364 12.86685 14.16187 1.000 8.27088   ? 35  PHE B CD2  1 
ATOM   3331 C CE1  . PHE B 1 38  ? -14.33149 14.24147 14.52665 1.000 9.78581   ? 35  PHE B CE1  1 
ATOM   3332 C CE2  . PHE B 1 38  ? -12.20770 14.04222 13.47281 1.000 9.71161   ? 35  PHE B CE2  1 
ATOM   3333 C CZ   . PHE B 1 38  ? -13.38386 14.72888 13.65818 1.000 10.03700  ? 35  PHE B CZ   1 
ATOM   3334 H H    . PHE B 1 38  ? -15.04854 10.59810 15.92205 1.000 8.91996   ? 35  PHE B H    1 
ATOM   3335 H HA   . PHE B 1 38  ? -13.08234 9.74767  14.29912 1.000 8.22520   ? 35  PHE B HA   1 
ATOM   3336 H HB2  . PHE B 1 38  ? -12.95108 11.20906 16.71301 1.000 8.84195   ? 35  PHE B HB2  1 
ATOM   3337 H HB3  . PHE B 1 38  ? -11.69762 10.91568 15.78124 1.000 8.84195   ? 35  PHE B HB3  1 
ATOM   3338 H HD1  . PHE B 1 38  ? -14.73837 12.74668 15.80991 1.000 10.82133  ? 35  PHE B HD1  1 
ATOM   3339 H HD2  . PHE B 1 38  ? -11.17493 12.40875 14.03109 1.000 9.92506   ? 35  PHE B HD2  1 
ATOM   3340 H HE1  . PHE B 1 38  ? -15.13087 14.70090 14.64843 1.000 11.74297  ? 35  PHE B HE1  1 
ATOM   3341 H HE2  . PHE B 1 38  ? -11.56780 14.36912 12.88241 1.000 11.65393  ? 35  PHE B HE2  1 
ATOM   3342 H HZ   . PHE B 1 38  ? -13.53827 15.52159 13.19702 1.000 12.04440  ? 35  PHE B HZ   1 
ATOM   3343 N N    . SER B 1 39  ? -12.43676 7.61104  15.33880 1.000 8.52830   ? 36  SER B N    1 
ATOM   3344 C CA   . SER B 1 39  ? -12.28516 6.28929  15.93266 1.000 8.19342   ? 36  SER B CA   1 
ATOM   3345 C C    . SER B 1 39  ? -11.22071 5.50167  15.18297 1.000 7.68295   ? 36  SER B C    1 
ATOM   3346 O O    . SER B 1 39  ? -10.92379 5.78171  14.01968 1.000 9.80875   ? 36  SER B O    1 
ATOM   3347 C CB   . SER B 1 39  ? -13.62024 5.53872  15.87223 1.000 9.08508   ? 36  SER B CB   1 
ATOM   3348 O OG   . SER B 1 39  ? -13.60694 4.38379  16.68358 1.000 10.07090  ? 36  SER B OG   1 
ATOM   3349 H H    . SER B 1 39  ? -12.11854 7.68177  14.54298 1.000 10.23396  ? 36  SER B H    1 
ATOM   3350 H HA   . SER B 1 39  ? -11.98763 6.38149  16.85129 1.000 9.83210   ? 36  SER B HA   1 
ATOM   3351 H HB2  . SER B 1 39  ? -14.32486 6.12940  16.18126 1.000 10.90209  ? 36  SER B HB2  1 
ATOM   3352 H HB3  . SER B 1 39  ? -13.78825 5.27368  14.95439 1.000 10.90209  ? 36  SER B HB3  1 
ATOM   3353 H HG   . SER B 1 39  ? -13.49401 4.59887  17.48769 1.000 12.08509  ? 36  SER B HG   1 
ATOM   3354 N N    . ALA B 1 40  ? -10.65824 4.49628  15.86339 1.000 8.28981   ? 37  ALA B N    1 
ATOM   3355 C CA   . ALA B 1 40  ? -9.65597  3.62290  15.26914 1.000 8.15224   ? 37  ALA B CA   1 
ATOM   3356 C C    . ALA B 1 40  ? -9.81867  2.20245  15.78968 1.000 7.09242   ? 37  ALA B C    1 
ATOM   3357 O O    . ALA B 1 40  ? -10.12257 1.99397  16.96818 1.000 8.94720   ? 37  ALA B O    1 
ATOM   3358 C CB   . ALA B 1 40  ? -8.23111  4.09061  15.59920 1.000 10.48164  ? 37  ALA B CB   1 
ATOM   3359 H H    . ALA B 1 40  ? -10.84685 4.30259  16.67979 1.000 9.94777   ? 37  ALA B H    1 
ATOM   3360 H HA   . ALA B 1 40  ? -9.78623  3.62342  14.30793 1.000 9.78269   ? 37  ALA B HA   1 
ATOM   3361 H HB1  . ALA B 1 40  ? -7.59913  3.56693  15.08222 1.000 12.57796  ? 37  ALA B HB1  1 
ATOM   3362 H HB2  . ALA B 1 40  ? -8.14643  5.02981  15.37198 1.000 12.57796  ? 37  ALA B HB2  1 
ATOM   3363 H HB3  . ALA B 1 40  ? -8.06866  3.96364  16.54703 1.000 12.57796  ? 37  ALA B HB3  1 
ATOM   3364 N N    . SER B 1 41  ? -9.57550  1.23041  14.90338 1.000 8.33949   ? 38  SER B N    1 
ATOM   3365 C CA   . SER B 1 41  ? -9.67354  -0.17627 15.26681 1.000 9.28884   ? 38  SER B CA   1 
ATOM   3366 C C    . SER B 1 41  ? -8.66357  -0.57576 16.33304 1.000 9.82670   ? 38  SER B C    1 
ATOM   3367 O O    . SER B 1 41  ? -8.88021  -1.57292 17.02908 1.000 12.75428  ? 38  SER B O    1 
ATOM   3368 C CB   . SER B 1 41  ? -9.44675  -1.05650 14.03090 1.000 10.19504  ? 38  SER B CB   1 
ATOM   3369 O OG   . SER B 1 41  ? -8.07761  -1.08009 13.64448 1.000 12.10362  ? 38  SER B OG   1 
ATOM   3370 H H    . SER B 1 41  ? -9.35160  1.36419  14.08389 1.000 10.00738  ? 38  SER B H    1 
ATOM   3371 H HA   . SER B 1 41  ? -10.56690 -0.33335 15.61052 1.000 11.14661  ? 38  SER B HA   1 
ATOM   3372 H HB2  . SER B 1 41  ? -9.72873  -1.96159 14.23631 1.000 12.23405  ? 38  SER B HB2  1 
ATOM   3373 H HB3  . SER B 1 41  ? -9.97248  -0.70397 13.29589 1.000 12.23405  ? 38  SER B HB3  1 
ATOM   3374 H HG   . SER B 1 41  ? -7.76779  -0.29935 13.63671 1.000 14.52434  ? 38  SER B HG   1 
ATOM   3375 N N    . TRP B 1 42  ? -7.56705  0.16898  16.47326 1.000 9.77014   ? 39  TRP B N    1 
ATOM   3376 C CA   . TRP B 1 42  ? -6.51184  -0.16417 17.42164 1.000 11.43920  ? 39  TRP B CA   1 
ATOM   3377 C C    . TRP B 1 42  ? -6.73498  0.44957  18.79670 1.000 11.48316  ? 39  TRP B C    1 
ATOM   3378 O O    . TRP B 1 42  ? -5.91883  0.23761  19.70019 1.000 14.52376  ? 39  TRP B O    1 
ATOM   3379 C CB   . TRP B 1 42  ? -5.13903  0.25989  16.87605 1.000 11.98487  ? 39  TRP B CB   1 
ATOM   3380 C CG   . TRP B 1 42  ? -5.05283  1.64665  16.27224 1.000 12.28597  ? 39  TRP B CG   1 
ATOM   3381 C CD1  . TRP B 1 42  ? -5.02409  1.95984  14.94150 1.000 12.97988  ? 39  TRP B CD1  1 
ATOM   3382 C CD2  . TRP B 1 42  ? -4.95714  2.89339  16.97625 1.000 12.30921  ? 39  TRP B CD2  1 
ATOM   3383 N NE1  . TRP B 1 42  ? -4.92284  3.32021  14.77513 1.000 14.28614  ? 39  TRP B NE1  1 
ATOM   3384 C CE2  . TRP B 1 42  ? -4.88349  3.91627  16.00795 1.000 13.17117  ? 39  TRP B CE2  1 
ATOM   3385 C CE3  . TRP B 1 42  ? -4.93403  3.24450  18.32842 1.000 12.56446  ? 39  TRP B CE3  1 
ATOM   3386 C CZ2  . TRP B 1 42  ? -4.78871  5.26433  16.35036 1.000 14.11334  ? 39  TRP B CZ2  1 
ATOM   3387 C CZ3  . TRP B 1 42  ? -4.83984  4.58419  18.66519 1.000 12.43965  ? 39  TRP B CZ3  1 
ATOM   3388 C CH2  . TRP B 1 42  ? -4.76817  5.57657  17.68098 1.000 12.21317  ? 39  TRP B CH2  1 
ATOM   3389 H H    . TRP B 1 42  ? -7.41116  0.88386  16.02133 1.000 11.72417  ? 39  TRP B H    1 
ATOM   3390 H HA   . TRP B 1 42  ? -6.49281  -1.12806 17.52868 1.000 13.72704  ? 39  TRP B HA   1 
ATOM   3391 H HB2  . TRP B 1 42  ? -4.50117  0.22726  17.60611 1.000 14.38185  ? 39  TRP B HB2  1 
ATOM   3392 H HB3  . TRP B 1 42  ? -4.88262  -0.36861 16.18314 1.000 14.38185  ? 39  TRP B HB3  1 
ATOM   3393 H HD1  . TRP B 1 42  ? -5.06691  1.34109  14.24854 1.000 15.57586  ? 39  TRP B HD1  1 
ATOM   3394 H HE1  . TRP B 1 42  ? -4.88960  3.73052  14.02005 1.000 17.14337  ? 39  TRP B HE1  1 
ATOM   3395 H HE3  . TRP B 1 42  ? -4.98097  2.59151  18.98894 1.000 15.07736  ? 39  TRP B HE3  1 
ATOM   3396 H HZ2  . TRP B 1 42  ? -4.74129  5.92587  15.69843 1.000 16.93601  ? 39  TRP B HZ2  1 
ATOM   3397 H HZ3  . TRP B 1 42  ? -4.82389  4.82917  19.56221 1.000 14.92757  ? 39  TRP B HZ3  1 
ATOM   3398 H HH2  . TRP B 1 42  ? -4.70517  6.46814  17.93793 1.000 14.65581  ? 39  TRP B HH2  1 
ATOM   3399 N N    . CYS B 1 43  ? -7.82817  1.18046  18.97576 1.000 10.94821  ? 40  CYS B N    1 
ATOM   3400 C CA   . CYS B 1 43  ? -8.09387  1.92364  20.19547 1.000 10.19026  ? 40  CYS B CA   1 
ATOM   3401 C C    . CYS B 1 43  ? -9.08486  1.14679  21.04563 1.000 11.34242  ? 40  CYS B C    1 
ATOM   3402 O O    . CYS B 1 43  ? -10.24396 0.98850  20.63620 1.000 11.00719  ? 40  CYS B O    1 
ATOM   3403 C CB   . CYS B 1 43  ? -8.67359  3.28129  19.80603 1.000 11.79906  ? 40  CYS B CB   1 
ATOM   3404 S SG   . CYS B 1 43  ? -9.31372  4.23912  21.16203 1.000 15.15381  ? 40  CYS B SG   1 
ATOM   3405 H H    . CYS B 1 43  ? -8.44924  1.26355  18.38672 1.000 13.13785  ? 40  CYS B H    1 
ATOM   3406 H HA   . CYS B 1 43  ? -7.28402  2.04144  20.71621 1.000 12.22831  ? 40  CYS B HA   1 
ATOM   3407 H HB2  . CYS B 1 43  ? -7.97414  3.80454  19.38427 1.000 14.15888  ? 40  CYS B HB2  1 
ATOM   3408 H HB3  . CYS B 1 43  ? -9.40194  3.13681  19.18191 1.000 14.15888  ? 40  CYS B HB3  1 
ATOM   3409 H HG   . CYS B 1 43  ? -9.97688  3.52723  21.86447 1.000 18.18457  ? 40  CYS B HG   1 
ATOM   3410 N N    . PRO B 1 44  ? -8.69460  0.63894  22.21334 1.000 10.78082  ? 41  PRO B N    1 
ATOM   3411 C CA   . PRO B 1 44  ? -9.60091  -0.22967 22.97926 1.000 11.59647  ? 41  PRO B CA   1 
ATOM   3412 C C    . PRO B 1 44  ? -10.90534 0.46149  23.34598 1.000 11.03647  ? 41  PRO B C    1 
ATOM   3413 O O    . PRO B 1 44  ? -11.97809 -0.12427 23.13775 1.000 11.43869  ? 41  PRO B O    1 
ATOM   3414 C CB   . PRO B 1 44  ? -8.77207  -0.61751 24.21413 1.000 15.03323  ? 41  PRO B CB   1 
ATOM   3415 C CG   . PRO B 1 44  ? -7.35541  -0.53538 23.73985 1.000 16.06429  ? 41  PRO B CG   1 
ATOM   3416 C CD   . PRO B 1 44  ? -7.31885  0.60546  22.75196 1.000 11.93151  ? 41  PRO B CD   1 
ATOM   3417 H HA   . PRO B 1 44  ? -9.81296  -1.02672 22.46873 1.000 13.91577  ? 41  PRO B HA   1 
ATOM   3418 H HB2  . PRO B 1 44  ? -8.93675  0.00798  24.93701 1.000 18.03988  ? 41  PRO B HB2  1 
ATOM   3419 H HB3  . PRO B 1 44  ? -8.99553  -1.51797 24.49720 1.000 18.03988  ? 41  PRO B HB3  1 
ATOM   3420 H HG2  . PRO B 1 44  ? -6.76821  -0.35839 24.49137 1.000 19.27715  ? 41  PRO B HG2  1 
ATOM   3421 H HG3  . PRO B 1 44  ? -7.10450  -1.36894 23.31191 1.000 19.27715  ? 41  PRO B HG3  1 
ATOM   3422 H HD2  . PRO B 1 44  ? -7.10270  1.43979  23.19701 1.000 14.31781  ? 41  PRO B HD2  1 
ATOM   3423 H HD3  . PRO B 1 44  ? -6.67680  0.42979  22.04640 1.000 14.31781  ? 41  PRO B HD3  1 
ATOM   3424 N N    . PRO B 1 45  ? -10.89640 1.68866  23.88437 1.000 11.05083  ? 42  PRO B N    1 
ATOM   3425 C CA   A PRO B 1 45  ? -12.19354 2.32720  24.16929 0.478 10.97361  ? 42  PRO B CA   1 
ATOM   3426 C CA   B PRO B 1 45  ? -12.18314 2.35045  24.16448 0.522 11.75361  ? 42  PRO B CA   1 
ATOM   3427 C C    . PRO B 1 45  ? -13.04185 2.54922  22.92825 1.000 10.77494  ? 42  PRO B C    1 
ATOM   3428 O O    . PRO B 1 45  ? -14.27516 2.51941  23.02410 1.000 11.77520  ? 42  PRO B O    1 
ATOM   3429 C CB   A PRO B 1 45  ? -11.82208 3.63738  24.87906 0.478 9.93361   ? 42  PRO B CB   1 
ATOM   3430 C CB   B PRO B 1 45  ? -11.76743 3.68627  24.79724 0.522 12.74361  ? 42  PRO B CB   1 
ATOM   3431 C CG   A PRO B 1 45  ? -10.39087 3.85939  24.58907 0.478 12.73361  ? 42  PRO B CG   1 
ATOM   3432 C CG   B PRO B 1 45  ? -10.41108 3.43180  25.35482 0.522 14.36361  ? 42  PRO B CG   1 
ATOM   3433 C CD   A PRO B 1 45  ? -9.76799  2.50046  24.37809 0.478 12.86361  ? 42  PRO B CD   1 
ATOM   3434 C CD   B PRO B 1 45  ? -9.75677  2.47064  24.39900 0.522 12.77361  ? 42  PRO B CD   1 
ATOM   3435 H HA   A PRO B 1 45  ? -12.69339 1.78351  24.79814 0.478 13.16833  ? 42  PRO B HA   1 
ATOM   3436 H HA   B PRO B 1 45  ? -12.68239 1.83613  24.81802 0.522 14.10433  ? 42  PRO B HA   1 
ATOM   3437 H HB2  A PRO B 1 45  ? -12.36113 4.36351  24.52825 0.478 11.92033  ? 42  PRO B HB2  1 
ATOM   3438 H HB2  B PRO B 1 45  ? -11.74128 4.38020  24.11998 0.522 15.29233  ? 42  PRO B HB2  1 
ATOM   3439 H HB3  A PRO B 1 45  ? -11.96982 3.54555  25.83333 0.478 11.92033  ? 42  PRO B HB3  1 
ATOM   3440 H HB3  B PRO B 1 45  ? -12.39224 3.93002  25.49802 0.522 15.29233  ? 42  PRO B HB3  1 
ATOM   3441 H HG2  A PRO B 1 45  ? -10.30406 4.40050  23.78872 0.478 15.28033  ? 42  PRO B HG2  1 
ATOM   3442 H HG2  B PRO B 1 45  ? -9.91390  4.26336  25.40193 0.522 17.23633  ? 42  PRO B HG2  1 
ATOM   3443 H HG3  A PRO B 1 45  ? -9.97554  4.31009  25.34092 0.478 15.28033  ? 42  PRO B HG3  1 
ATOM   3444 H HG3  B PRO B 1 45  ? -10.48749 3.04039  26.23906 0.522 17.23633  ? 42  PRO B HG3  1 
ATOM   3445 H HD2  A PRO B 1 45  ? -9.05822  2.54384  23.71836 0.478 15.43633  ? 42  PRO B HD2  1 
ATOM   3446 H HD2  B PRO B 1 45  ? -9.31030  2.94602  23.68096 0.522 15.32833  ? 42  PRO B HD2  1 
ATOM   3447 H HD3  A PRO B 1 45  ? -9.42428  2.14412  25.21223 0.478 15.43633  ? 42  PRO B HD3  1 
ATOM   3448 H HD3  B PRO B 1 45  ? -9.12459  1.89848  24.86146 0.522 15.32833  ? 42  PRO B HD3  1 
ATOM   3449 N N    . CYS B 1 46  ? -12.42586 2.76557  21.76530 1.000 9.67333   ? 43  CYS B N    1 
ATOM   3450 C CA   . CYS B 1 46  ? -13.20655 2.86361  20.53823 1.000 10.63554  ? 43  CYS B CA   1 
ATOM   3451 C C    . CYS B 1 46  ? -13.91908 1.55323  20.25841 1.000 8.91034   ? 43  CYS B C    1 
ATOM   3452 O O    . CYS B 1 46  ? -15.10139 1.53046  19.89880 1.000 9.73877   ? 43  CYS B O    1 
ATOM   3453 C CB   . CYS B 1 46  ? -12.28464 3.17522  19.36382 1.000 10.66665  ? 43  CYS B CB   1 
ATOM   3454 S SG   . CYS B 1 46  ? -11.67229 4.84795  19.31451 1.000 13.04690  ? 43  CYS B SG   1 
ATOM   3455 H H    . CYS B 1 46  ? -11.57674 2.85684  21.66397 1.000 11.60799  ? 43  CYS B H    1 
ATOM   3456 H HA   . CYS B 1 46  ? -13.85568 3.57739  20.63850 1.000 12.76265  ? 43  CYS B HA   1 
ATOM   3457 H HB2  . CYS B 1 46  ? -11.51638 2.58493  19.41116 1.000 12.79998  ? 43  CYS B HB2  1 
ATOM   3458 H HB3  . CYS B 1 46  ? -12.77268 3.01916  18.54019 1.000 12.79998  ? 43  CYS B HB3  1 
ATOM   3459 H HG   . CYS B 1 46  ? -10.90297 4.95555  18.39987 1.000 15.65628  ? 43  CYS B HG   1 
ATOM   3460 N N    . ARG B 1 47  ? -13.19214 0.44556  20.38189 1.000 9.68954   ? 44  ARG B N    1 
ATOM   3461 C CA   . ARG B 1 47  ? -13.78424 -0.84905 20.08967 1.000 10.84708  ? 44  ARG B CA   1 
ATOM   3462 C C    . ARG B 1 47  ? -14.95723 -1.13281 21.01135 1.000 9.24693   ? 44  ARG B C    1 
ATOM   3463 O O    . ARG B 1 47  ? -15.92894 -1.77188 20.59564 1.000 11.45242  ? 44  ARG B O    1 
ATOM   3464 C CB   . ARG B 1 47  ? -12.72452 -1.93891 20.20919 1.000 10.97151  ? 44  ARG B CB   1 
ATOM   3465 C CG   . ARG B 1 47  ? -11.65082 -1.87137 19.13925 1.000 13.42830  ? 44  ARG B CG   1 
ATOM   3466 C CD   . ARG B 1 47  ? -10.81604 -3.14269 19.11775 1.000 19.24777  ? 44  ARG B CD   1 
ATOM   3467 N NE   . ARG B 1 47  ? -10.08072 -3.38189 20.35615 1.000 22.71500  ? 44  ARG B NE   1 
ATOM   3468 C CZ   . ARG B 1 47  ? -8.76145  -3.29349 20.48494 1.000 25.34387  ? 44  ARG B CZ   1 
ATOM   3469 N NH1  . ARG B 1 47  ? -7.98738  -2.93798 19.47236 1.000 27.56992  ? 44  ARG B NH1  1 
ATOM   3470 N NH2  . ARG B 1 47  ? -8.20369  -3.57990 21.65796 1.000 25.34026  ? 44  ARG B NH2  1 
ATOM   3471 H H    . ARG B 1 47  ? -12.36880 0.41919  20.62889 1.000 11.62745  ? 44  ARG B H    1 
ATOM   3472 H HA   . ARG B 1 47  ? -14.11341 -0.85636 19.17726 1.000 13.01650  ? 44  ARG B HA   1 
ATOM   3473 H HB2  . ARG B 1 47  ? -12.28823 -1.85572 21.07153 1.000 13.16581  ? 44  ARG B HB2  1 
ATOM   3474 H HB3  . ARG B 1 47  ? -13.15806 -2.80378 20.13879 1.000 13.16581  ? 44  ARG B HB3  1 
ATOM   3475 H HG2  . ARG B 1 47  ? -12.06787 -1.76413 18.27007 1.000 16.11396  ? 44  ARG B HG2  1 
ATOM   3476 H HG3  . ARG B 1 47  ? -11.06238 -1.12164 19.31965 1.000 16.11396  ? 44  ARG B HG3  1 
ATOM   3477 H HD2  . ARG B 1 47  ? -11.40379 -3.90038 18.97156 1.000 23.09732  ? 44  ARG B HD2  1 
ATOM   3478 H HD3  . ARG B 1 47  ? -10.16968 -3.08033 18.39718 1.000 23.09732  ? 44  ARG B HD3  1 
ATOM   3479 H HE   . ARG B 1 47  ? -10.53536 -3.59591 21.05407 1.000 27.25800  ? 44  ARG B HE   1 
ATOM   3480 H HH11 . ARG B 1 47  ? -8.33611  -2.75735 18.70727 1.000 33.08391  ? 44  ARG B HH11 1 
ATOM   3481 H HH12 . ARG B 1 47  ? -7.13555  -2.88754 19.57933 1.000 33.08391  ? 44  ARG B HH12 1 
ATOM   3482 H HH21 . ARG B 1 47  ? -8.69609  -3.81883 22.32133 1.000 30.40831  ? 44  ARG B HH21 1 
ATOM   3483 H HH22 . ARG B 1 47  ? -7.35065  -3.52616 21.75305 1.000 30.40831  ? 44  ARG B HH22 1 
ATOM   3484 N N    . GLY B 1 48  ? -14.89340 -0.65450 22.25756 1.000 10.53326  ? 45  GLY B N    1 
ATOM   3485 C CA   . GLY B 1 48  ? -16.00219 -0.83361 23.17604 1.000 12.24188  ? 45  GLY B CA   1 
ATOM   3486 C C    . GLY B 1 48  ? -17.13243 0.15227  22.97739 1.000 12.85679  ? 45  GLY B C    1 
ATOM   3487 O O    . GLY B 1 48  ? -18.29325 -0.17456 23.24632 1.000 14.92583  ? 45  GLY B O    1 
ATOM   3488 H H    . GLY B 1 48  ? -14.22317 -0.22770 22.58655 1.000 12.63991  ? 45  GLY B H    1 
ATOM   3489 H HA2  . GLY B 1 48  ? -16.36191 -1.72743 23.06380 1.000 14.69025  ? 45  GLY B HA2  1 
ATOM   3490 H HA3  . GLY B 1 48  ? -15.67654 -0.73603 24.08451 1.000 14.69025  ? 45  GLY B HA3  1 
ATOM   3491 N N    . PHE B 1 49  ? -16.82113 1.36432  22.51231 1.000 10.28869  ? 46  PHE B N    1 
ATOM   3492 C CA   . PHE B 1 49  ? -17.86250 2.36320  22.29761 1.000 8.82648   ? 46  PHE B CA   1 
ATOM   3493 C C    . PHE B 1 49  ? -18.64108 2.10735  21.00970 1.000 9.18387   ? 46  PHE B C    1 
ATOM   3494 O O    . PHE B 1 49  ? -19.85240 2.34508  20.95727 1.000 9.58441   ? 46  PHE B O    1 
ATOM   3495 C CB   . PHE B 1 49  ? -17.26067 3.77124  22.28662 1.000 8.79430   ? 46  PHE B CB   1 
ATOM   3496 C CG   . PHE B 1 49  ? -18.26782 4.84466  22.01321 1.000 9.11718   ? 46  PHE B CG   1 
ATOM   3497 C CD1  . PHE B 1 49  ? -19.22743 5.15772  22.95689 1.000 10.82037  ? 46  PHE B CD1  1 
ATOM   3498 C CD2  . PHE B 1 49  ? -18.26461 5.53330  20.81381 1.000 9.76244   ? 46  PHE B CD2  1 
ATOM   3499 C CE1  . PHE B 1 49  ? -20.16385 6.13185  22.71036 1.000 11.25824  ? 46  PHE B CE1  1 
ATOM   3500 C CE2  . PHE B 1 49  ? -19.20337 6.51224  20.56324 1.000 11.01869  ? 46  PHE B CE2  1 
ATOM   3501 C CZ   . PHE B 1 49  ? -20.14976 6.81423  21.51756 1.000 11.30291  ? 46  PHE B CZ   1 
ATOM   3502 H H    . PHE B 1 49  ? -16.02601 1.62736  22.31688 1.000 12.34643  ? 46  PHE B H    1 
ATOM   3503 H HA   . PHE B 1 49  ? -18.48713 2.31312  23.03804 1.000 10.59178  ? 46  PHE B HA   1 
ATOM   3504 H HB2  . PHE B 1 49  ? -16.86361 3.94923  23.15355 1.000 10.55316  ? 46  PHE B HB2  1 
ATOM   3505 H HB3  . PHE B 1 49  ? -16.58187 3.81665  21.59520 1.000 10.55316  ? 46  PHE B HB3  1 
ATOM   3506 H HD1  . PHE B 1 49  ? -19.23938 4.70358  23.76838 1.000 12.98445  ? 46  PHE B HD1  1 
ATOM   3507 H HD2  . PHE B 1 49  ? -17.62344 5.33442  20.17019 1.000 11.71493  ? 46  PHE B HD2  1 
ATOM   3508 H HE1  . PHE B 1 49  ? -20.80804 6.32982  23.35124 1.000 13.50989  ? 46  PHE B HE1  1 
ATOM   3509 H HE2  . PHE B 1 49  ? -19.19743 6.96722  19.75216 1.000 13.22242  ? 46  PHE B HE2  1 
ATOM   3510 H HZ   . PHE B 1 49  ? -20.77884 7.47956  21.35473 1.000 13.56349  ? 46  PHE B HZ   1 
ATOM   3511 N N    . THR B 1 50  ? -17.97523 1.63095  19.96530 1.000 8.79002   ? 47  THR B N    1 
ATOM   3512 C CA   . THR B 1 50  ? -18.65317 1.43020  18.68436 1.000 8.61795   ? 47  THR B CA   1 
ATOM   3513 C C    . THR B 1 50  ? -19.95330 0.64522  18.79222 1.000 8.04689   ? 47  THR B C    1 
ATOM   3514 O O    . THR B 1 50  ? -20.96756 1.11163  18.25037 1.000 9.02777   ? 47  THR B O    1 
ATOM   3515 C CB   . THR B 1 50  ? -17.65856 0.83964  17.67820 1.000 9.59364   ? 47  THR B CB   1 
ATOM   3516 O OG1  . THR B 1 50  ? -16.77115 1.88140  17.25557 1.000 10.04387  ? 47  THR B OG1  1 
ATOM   3517 C CG2  . THR B 1 50  ? -18.38371 0.27315  16.47967 1.000 11.32536  ? 47  THR B CG2  1 
ATOM   3518 H H    . THR B 1 50  ? -17.14200 1.41804  19.96845 1.000 10.54802  ? 47  THR B H    1 
ATOM   3519 H HA   . THR B 1 50  ? -18.91476 2.29806  18.33897 1.000 10.34154  ? 47  THR B HA   1 
ATOM   3520 H HB   . THR B 1 50  ? -17.15586 0.11778  18.08700 1.000 11.51237  ? 47  THR B HB   1 
ATOM   3521 H HG1  . THR B 1 50  ? -15.97364 1.63255  17.34309 1.000 12.05264  ? 47  THR B HG1  1 
ATOM   3522 H HG21 . THR B 1 50  ? -17.75050 0.07429  15.77228 1.000 13.59043  ? 47  THR B HG21 1 
ATOM   3523 H HG22 . THR B 1 50  ? -18.84607 -0.54295 16.72688 1.000 13.59043  ? 47  THR B HG22 1 
ATOM   3524 H HG23 . THR B 1 50  ? -19.03221 0.91497  16.15041 1.000 13.59043  ? 47  THR B HG23 1 
ATOM   3525 N N    . PRO B 1 51  ? -20.01140 -0.51473 19.45200 1.000 9.11362   ? 48  PRO B N    1 
ATOM   3526 C CA   . PRO B 1 51  ? -21.29904 -1.23307 19.52476 1.000 9.35091   ? 48  PRO B CA   1 
ATOM   3527 C C    . PRO B 1 51  ? -22.38169 -0.46902 20.27130 1.000 9.55498   ? 48  PRO B C    1 
ATOM   3528 O O    . PRO B 1 51  ? -23.56795 -0.61716 19.95222 1.000 10.17119  ? 48  PRO B O    1 
ATOM   3529 C CB   . PRO B 1 51  ? -20.94422 -2.56920 20.19708 1.000 11.06187  ? 48  PRO B CB   1 
ATOM   3530 C CG   . PRO B 1 51  ? -19.57357 -2.39367 20.76292 1.000 12.02167  ? 48  PRO B CG   1 
ATOM   3531 C CD   . PRO B 1 51  ? -18.89140 -1.30014 20.00003 1.000 9.28355   ? 48  PRO B CD   1 
ATOM   3532 H HA   . PRO B 1 51  ? -21.61495 -1.42467 18.62788 1.000 11.22110  ? 48  PRO B HA   1 
ATOM   3533 H HB2  . PRO B 1 51  ? -21.58430 -2.76049 20.90037 1.000 13.27425  ? 48  PRO B HB2  1 
ATOM   3534 H HB3  . PRO B 1 51  ? -20.95484 -3.27955 19.53663 1.000 13.27425  ? 48  PRO B HB3  1 
ATOM   3535 H HG2  . PRO B 1 51  ? -19.64489 -2.15435 21.70023 1.000 14.42601  ? 48  PRO B HG2  1 
ATOM   3536 H HG3  . PRO B 1 51  ? -19.08216 -3.22471 20.66916 1.000 14.42601  ? 48  PRO B HG3  1 
ATOM   3537 H HD2  . PRO B 1 51  ? -18.34564 -0.75696 20.58995 1.000 11.14027  ? 48  PRO B HD2  1 
ATOM   3538 H HD3  . PRO B 1 51  ? -18.34555 -1.66625 19.28665 1.000 11.14027  ? 48  PRO B HD3  1 
ATOM   3539 N N    . THR B 1 52  ? -22.01111 0.35044  21.25608 1.000 10.68628  ? 49  THR B N    1 
ATOM   3540 C CA   . THR B 1 52  ? -22.99446 1.20317  21.91502 1.000 9.81695   ? 49  THR B CA   1 
ATOM   3541 C C    . THR B 1 52  ? -23.60048 2.18390  20.92195 1.000 9.01458   ? 49  THR B C    1 
ATOM   3542 O O    . THR B 1 52  ? -24.81896 2.39580  20.90553 1.000 9.69230   ? 49  THR B O    1 
ATOM   3543 C CB   . THR B 1 52  ? -22.31402 1.94148  23.06819 1.000 11.35117  ? 49  THR B CB   1 
ATOM   3544 O OG1  . THR B 1 52  ? -21.66832 0.98674  23.92341 1.000 14.10545  ? 49  THR B OG1  1 
ATOM   3545 C CG2  . THR B 1 52  ? -23.31516 2.75250  23.87279 1.000 12.96139  ? 49  THR B CG2  1 
ATOM   3546 H H    . THR B 1 52  ? -21.20901 0.42965  21.55602 1.000 12.82354  ? 49  THR B H    1 
ATOM   3547 H HA   . THR B 1 52  ? -23.71504 0.66546  22.27906 1.000 11.78034  ? 49  THR B HA   1 
ATOM   3548 H HB   . THR B 1 52  ? -21.65788 2.55998  22.71065 1.000 13.62140  ? 49  THR B HB   1 
ATOM   3549 H HG1  . THR B 1 52  ? -21.27715 1.38287  24.55243 1.000 16.92654  ? 49  THR B HG1  1 
ATOM   3550 H HG21 . THR B 1 52  ? -22.86014 3.22992  24.58408 1.000 15.55367  ? 49  THR B HG21 1 
ATOM   3551 H HG22 . THR B 1 52  ? -23.76077 3.39420  23.29785 1.000 15.55367  ? 49  THR B HG22 1 
ATOM   3552 H HG23 . THR B 1 52  ? -23.98054 2.16478  24.26363 1.000 15.55367  ? 49  THR B HG23 1 
ATOM   3553 N N    . LEU B 1 53  ? -22.77046 2.76228  20.05651 1.000 9.54839   ? 50  LEU B N    1 
ATOM   3554 C CA   . LEU B 1 53  ? -23.29009 3.69905  19.06690 1.000 8.85358   ? 50  LEU B CA   1 
ATOM   3555 C C    . LEU B 1 53  ? -24.06788 2.96893  17.97556 1.000 8.67484   ? 50  LEU B C    1 
ATOM   3556 O O    . LEU B 1 53  ? -25.07974 3.48269  17.48400 1.000 8.61065   ? 50  LEU B O    1 
ATOM   3557 C CB   . LEU B 1 53  ? -22.15017 4.54035  18.49193 1.000 11.27769  ? 50  LEU B CB   1 
ATOM   3558 C CG   . LEU B 1 53  ? -22.52727 5.67158  17.53211 1.000 9.25316   ? 50  LEU B CG   1 
ATOM   3559 C CD1  . LEU B 1 53  ? -23.45574 6.68318  18.18231 1.000 10.47713  ? 50  LEU B CD1  1 
ATOM   3560 C CD2  . LEU B 1 53  ? -21.27580 6.37197  17.01222 1.000 10.13675  ? 50  LEU B CD2  1 
ATOM   3561 H H    . LEU B 1 53  ? -21.92105 2.63217  20.02213 1.000 11.45807  ? 50  LEU B H    1 
ATOM   3562 H HA   . LEU B 1 53  ? -23.90637 4.31295  19.49612 1.000 10.62430  ? 50  LEU B HA   1 
ATOM   3563 H HB2  . LEU B 1 53  ? -21.67715 4.94722  19.23463 1.000 13.53323  ? 50  LEU B HB2  1 
ATOM   3564 H HB3  . LEU B 1 53  ? -21.55713 3.94547  18.00683 1.000 13.53323  ? 50  LEU B HB3  1 
ATOM   3565 H HG   . LEU B 1 53  ? -23.00306 5.27855  16.78374 1.000 11.10380  ? 50  LEU B HG   1 
ATOM   3566 H HD11 . LEU B 1 53  ? -23.64998 7.38855  17.54543 1.000 12.57256  ? 50  LEU B HD11 1 
ATOM   3567 H HD12 . LEU B 1 53  ? -24.27681 6.23685  18.44218 1.000 12.57256  ? 50  LEU B HD12 1 
ATOM   3568 H HD13 . LEU B 1 53  ? -23.01942 7.05498  18.96481 1.000 12.57256  ? 50  LEU B HD13 1 
ATOM   3569 H HD21 . LEU B 1 53  ? -21.53713 7.04903  16.36865 1.000 12.16410  ? 50  LEU B HD21 1 
ATOM   3570 H HD22 . LEU B 1 53  ? -20.81257 6.78531  17.75752 1.000 12.16410  ? 50  LEU B HD22 1 
ATOM   3571 H HD23 . LEU B 1 53  ? -20.70044 5.71655  16.58762 1.000 12.16410  ? 50  LEU B HD23 1 
ATOM   3572 N N    . VAL B 1 54  ? -23.61476 1.77079  17.58660 1.000 10.16171  ? 51  VAL B N    1 
ATOM   3573 C CA   . VAL B 1 54  ? -24.34838 0.97272  16.60219 1.000 8.54703   ? 51  VAL B CA   1 
ATOM   3574 C C    . VAL B 1 54  ? -25.76574 0.69280  17.09120 1.000 9.14003   ? 51  VAL B C    1 
ATOM   3575 O O    . VAL B 1 54  ? -26.73829 0.84086  16.34181 1.000 10.16932  ? 51  VAL B O    1 
ATOM   3576 C CB   . VAL B 1 54  ? -23.59244 -0.33148 16.28295 1.000 9.46901   ? 51  VAL B CB   1 
ATOM   3577 C CG1  . VAL B 1 54  ? -24.47082 -1.29639 15.47217 1.000 10.64830  ? 51  VAL B CG1  1 
ATOM   3578 C CG2  . VAL B 1 54  ? -22.30880 -0.03868 15.52807 1.000 8.31337   ? 51  VAL B CG2  1 
ATOM   3579 H H    . VAL B 1 54  ? -22.89309 1.40256  17.87504 1.000 12.19405  ? 51  VAL B H    1 
ATOM   3580 H HA   . VAL B 1 54  ? -24.41111 1.48712  15.78221 1.000 10.25643  ? 51  VAL B HA   1 
ATOM   3581 H HB   . VAL B 1 54  ? -23.36619 -0.76047 17.12299 1.000 11.36281  ? 51  VAL B HB   1 
ATOM   3582 H HG11 . VAL B 1 54  ? -23.92685 -2.04052 15.17007 1.000 12.77796  ? 51  VAL B HG11 1 
ATOM   3583 H HG12 . VAL B 1 54  ? -25.18945 -1.62008 16.03759 1.000 12.77796  ? 51  VAL B HG12 1 
ATOM   3584 H HG13 . VAL B 1 54  ? -24.83788 -0.82363 14.70884 1.000 12.77796  ? 51  VAL B HG13 1 
ATOM   3585 H HG21 . VAL B 1 54  ? -21.86687 -0.87662 15.31962 1.000 9.97605   ? 51  VAL B HG21 1 
ATOM   3586 H HG22 . VAL B 1 54  ? -22.52488 0.43401  14.70906 1.000 9.97605   ? 51  VAL B HG22 1 
ATOM   3587 H HG23 . VAL B 1 54  ? -21.73333 0.50936  16.08430 1.000 9.97605   ? 51  VAL B HG23 1 
ATOM   3588 N N    . GLU B 1 55  ? -25.90285 0.26483  18.35097 1.000 10.57989  ? 52  GLU B N    1 
ATOM   3589 C CA   . GLU B 1 55  ? -27.22877 -0.04730 18.87604 1.000 10.58184  ? 52  GLU B CA   1 
ATOM   3590 C C    . GLU B 1 55  ? -28.12656 1.18298  18.85523 1.000 10.82557  ? 52  GLU B C    1 
ATOM   3591 O O    . GLU B 1 55  ? -29.29836 1.10034  18.47012 1.000 12.58688  ? 52  GLU B O    1 
ATOM   3592 C CB   . GLU B 1 55  ? -27.12713 -0.61228 20.29265 1.000 13.46766  ? 52  GLU B CB   1 
ATOM   3593 C CG   . GLU B 1 55  ? -28.48343 -0.97079 20.88579 1.000 22.53951  ? 52  GLU B CG   1 
ATOM   3594 C CD   . GLU B 1 55  ? -28.38349 -1.65311 22.23712 1.000 30.10889  ? 52  GLU B CD   1 
ATOM   3595 O OE1  . GLU B 1 55  ? -27.28976 -2.15346 22.57652 1.000 33.02756  ? 52  GLU B OE1  1 
ATOM   3596 O OE2  . GLU B 1 55  ? -29.40262 -1.68858 22.96037 1.000 33.78561  ? 52  GLU B OE2  1 
ATOM   3597 H H    . GLU B 1 55  ? -25.25729 0.15021  18.90749 1.000 12.69587  ? 52  GLU B H    1 
ATOM   3598 H HA   . GLU B 1 55  ? -27.63032 -0.72997 18.31601 1.000 12.69821  ? 52  GLU B HA   1 
ATOM   3599 H HB2  . GLU B 1 55  ? -26.58622 -1.41722 20.27291 1.000 16.16119  ? 52  GLU B HB2  1 
ATOM   3600 H HB3  . GLU B 1 55  ? -26.71421 0.05090  20.86761 1.000 16.16119  ? 52  GLU B HB3  1 
ATOM   3601 H HG2  . GLU B 1 55  ? -29.00137 -0.15858 20.99963 1.000 27.04741  ? 52  GLU B HG2  1 
ATOM   3602 H HG3  . GLU B 1 55  ? -28.94170 -1.57437 20.28034 1.000 27.04741  ? 52  GLU B HG3  1 
ATOM   3603 N N    . PHE B 1 56  ? -27.58838 2.33543  19.26205 1.000 9.33449   ? 53  PHE B N    1 
ATOM   3604 C CA   . PHE B 1 56  ? -28.35177 3.57860  19.21687 1.000 9.29732   ? 53  PHE B CA   1 
ATOM   3605 C C    . PHE B 1 56  ? -28.78677 3.90666  17.79272 1.000 8.57259   ? 53  PHE B C    1 
ATOM   3606 O O    . PHE B 1 56  ? -29.93725 4.29351  17.55569 1.000 10.03962  ? 53  PHE B O    1 
ATOM   3607 C CB   . PHE B 1 56  ? -27.49383 4.71299  19.78781 1.000 9.77052   ? 53  PHE B CB   1 
ATOM   3608 C CG   . PHE B 1 56  ? -28.22958 6.00899  19.93936 1.000 10.42089  ? 53  PHE B CG   1 
ATOM   3609 C CD1  . PHE B 1 56  ? -29.12099 6.19242  20.98018 1.000 12.10949  ? 53  PHE B CD1  1 
ATOM   3610 C CD2  . PHE B 1 56  ? -28.02954 7.04377  19.04832 1.000 11.28973  ? 53  PHE B CD2  1 
ATOM   3611 C CE1  . PHE B 1 56  ? -29.80074 7.37670  21.12077 1.000 13.19830  ? 53  PHE B CE1  1 
ATOM   3612 C CE2  . PHE B 1 56  ? -28.71262 8.22994  19.18431 1.000 13.07801  ? 53  PHE B CE2  1 
ATOM   3613 C CZ   . PHE B 1 56  ? -29.59499 8.39825  20.22211 1.000 13.10081  ? 53  PHE B CZ   1 
ATOM   3614 H H    . PHE B 1 56  ? -26.78865 2.42235  19.56615 1.000 11.20139  ? 53  PHE B H    1 
ATOM   3615 H HA   . PHE B 1 56  ? -29.15137 3.48672  19.75826 1.000 11.15678  ? 53  PHE B HA   1 
ATOM   3616 H HB2  . PHE B 1 56  ? -27.17318 4.45037  20.66480 1.000 11.72462  ? 53  PHE B HB2  1 
ATOM   3617 H HB3  . PHE B 1 56  ? -26.74354 4.86645  19.19249 1.000 11.72462  ? 53  PHE B HB3  1 
ATOM   3618 H HD1  . PHE B 1 56  ? -29.26160 5.50600  21.59170 1.000 14.53138  ? 53  PHE B HD1  1 
ATOM   3619 H HD2  . PHE B 1 56  ? -27.42639 6.93795  18.34838 1.000 13.54768  ? 53  PHE B HD2  1 
ATOM   3620 H HE1  . PHE B 1 56  ? -30.40005 7.48856  21.82306 1.000 15.83796  ? 53  PHE B HE1  1 
ATOM   3621 H HE2  . PHE B 1 56  ? -28.57662 8.91769  18.57324 1.000 15.69362  ? 53  PHE B HE2  1 
ATOM   3622 H HZ   . PHE B 1 56  ? -30.05328 9.20181  20.31782 1.000 15.72097  ? 53  PHE B HZ   1 
ATOM   3623 N N    . TYR B 1 57  ? -27.88083 3.74577  16.83078 1.000 9.10449   ? 54  TYR B N    1 
ATOM   3624 C CA   . TYR B 1 57  ? -28.19725 4.03699  15.43490 1.000 10.03956  ? 54  TYR B CA   1 
ATOM   3625 C C    . TYR B 1 57  ? -29.27479 3.10497  14.90345 1.000 10.21356  ? 54  TYR B C    1 
ATOM   3626 O O    . TYR B 1 57  ? -30.20527 3.54666  14.21788 1.000 10.69004  ? 54  TYR B O    1 
ATOM   3627 C CB   . TYR B 1 57  ? -26.91276 3.87771  14.63342 1.000 10.61579  ? 54  TYR B CB   1 
ATOM   3628 C CG   . TYR B 1 57  ? -26.93718 4.25041  13.17542 1.000 9.58433   ? 54  TYR B CG   1 
ATOM   3629 C CD1  . TYR B 1 57  ? -26.57882 5.52192  12.75692 1.000 11.01126  ? 54  TYR B CD1  1 
ATOM   3630 C CD2  . TYR B 1 57  ? -27.24466 3.31329  12.21064 1.000 11.43448  ? 54  TYR B CD2  1 
ATOM   3631 C CE1  . TYR B 1 57  ? -26.55347 5.85219  11.41142 1.000 10.39582  ? 54  TYR B CE1  1 
ATOM   3632 C CE2  . TYR B 1 57  ? -27.21954 3.63328  10.86849 1.000 11.73095  ? 54  TYR B CE2  1 
ATOM   3633 C CZ   . TYR B 1 57  ? -26.88269 4.90396  10.47386 1.000 10.73480  ? 54  TYR B CZ   1 
ATOM   3634 O OH   . TYR B 1 57  ? -26.85278 5.21533  9.13242  1.000 13.08253  ? 54  TYR B OH   1 
ATOM   3635 H H    . TYR B 1 57  ? -27.07641 3.46969  16.95844 1.000 10.92539  ? 54  TYR B H    1 
ATOM   3636 H HA   . TYR B 1 57  ? -28.53382 4.94241  15.34630 1.000 12.04748  ? 54  TYR B HA   1 
ATOM   3637 H HB2  . TYR B 1 57  ? -26.23437 4.43181  15.05014 1.000 12.73895  ? 54  TYR B HB2  1 
ATOM   3638 H HB3  . TYR B 1 57  ? -26.65166 2.94453  14.67694 1.000 12.73895  ? 54  TYR B HB3  1 
ATOM   3639 H HD1  . TYR B 1 57  ? -26.35152 6.16440  13.38974 1.000 13.21351  ? 54  TYR B HD1  1 
ATOM   3640 H HD2  . TYR B 1 57  ? -27.47313 2.44980  12.46966 1.000 13.72138  ? 54  TYR B HD2  1 
ATOM   3641 H HE1  . TYR B 1 57  ? -26.31500 6.71065  11.14483 1.000 12.47498  ? 54  TYR B HE1  1 
ATOM   3642 H HE2  . TYR B 1 57  ? -27.43059 2.98873  10.23217 1.000 14.07714  ? 54  TYR B HE2  1 
ATOM   3643 H HH   . TYR B 1 57  ? -26.41254 5.92032  9.01087  1.000 15.69903  ? 54  TYR B HH   1 
ATOM   3644 N N    . GLU B 1 58  ? -29.15990 1.80922  15.19682 1.000 10.57592  ? 55  GLU B N    1 
ATOM   3645 C CA   . GLU B 1 58  ? -30.18219 0.86117  14.77450 1.000 10.10154  ? 55  GLU B CA   1 
ATOM   3646 C C    . GLU B 1 58  ? -31.56088 1.27339  15.26980 1.000 11.04014  ? 55  GLU B C    1 
ATOM   3647 O O    . GLU B 1 58  ? -32.55772 1.13886  14.55069 1.000 13.69985  ? 55  GLU B O    1 
ATOM   3648 C CB   . GLU B 1 58  ? -29.85087 -0.52535 15.32441 1.000 14.59116  ? 55  GLU B CB   1 
ATOM   3649 C CG   . GLU B 1 58  ? -28.64785 -1.18470 14.69267 1.000 16.27112  ? 55  GLU B CG   1 
ATOM   3650 C CD   . GLU B 1 58  ? -28.25099 -2.46304 15.40974 1.000 19.18022  ? 55  GLU B CD   1 
ATOM   3651 O OE1  . GLU B 1 58  ? -28.84498 -2.77233 16.46904 1.000 22.45420  ? 55  GLU B OE1  1 
ATOM   3652 O OE2  . GLU B 1 58  ? -27.34289 -3.15949 14.91124 1.000 19.48303  ? 55  GLU B OE2  1 
ATOM   3653 H H    . GLU B 1 58  ? -28.50696 1.45975  15.63402 1.000 12.69110  ? 55  GLU B H    1 
ATOM   3654 H HA   . GLU B 1 58  ? -30.19384 0.83089  13.80504 1.000 12.12184  ? 55  GLU B HA   1 
ATOM   3655 H HB2  . GLU B 1 58  ? -29.67463 -0.44568 16.27493 1.000 17.50940  ? 55  GLU B HB2  1 
ATOM   3656 H HB3  . GLU B 1 58  ? -30.61361 -1.10593 15.17593 1.000 17.50940  ? 55  GLU B HB3  1 
ATOM   3657 H HG2  . GLU B 1 58  ? -28.85394 -1.40660 13.77116 1.000 19.52535  ? 55  GLU B HG2  1 
ATOM   3658 H HG3  . GLU B 1 58  ? -27.89558 -0.57325 14.72641 1.000 19.52535  ? 55  GLU B HG3  1 
ATOM   3659 N N    . LYS B 1 59  ? -31.63982 1.75716  16.50797 1.000 11.22803  ? 56  LYS B N    1 
ATOM   3660 C CA   . LYS B 1 59  ? -32.93421 2.07046  17.09477 1.000 13.03335  ? 56  LYS B CA   1 
ATOM   3661 C C    . LYS B 1 59  ? -33.47546 3.40985  16.61484 1.000 12.85188  ? 56  LYS B C    1 
ATOM   3662 O O    . LYS B 1 59  ? -34.68514 3.54332  16.39667 1.000 13.76077  ? 56  LYS B O    1 
ATOM   3663 C CB   . LYS B 1 59  ? -32.82861 2.06961  18.62061 1.000 18.23343  ? 56  LYS B CB   1 
ATOM   3664 C CG   . LYS B 1 59  ? -32.63817 0.68555  19.20367 1.000 26.19137  ? 56  LYS B CG   1 
ATOM   3665 C CD   . LYS B 1 59  ? -32.53502 0.71216  20.71694 1.000 35.97934  ? 56  LYS B CD   1 
ATOM   3666 C CE   . LYS B 1 59  ? -32.48840 -0.70063 21.27088 1.000 44.26432  ? 56  LYS B CE   1 
ATOM   3667 N NZ   . LYS B 1 59  ? -32.43243 -0.71724 22.75471 1.000 48.85756  ? 56  LYS B NZ   1 
ATOM   3668 H H    . LYS B 1 59  ? -30.96661 1.91031  17.02074 1.000 13.47364  ? 56  LYS B H    1 
ATOM   3669 H HA   . LYS B 1 59  ? -33.56275 1.38240  16.82567 1.000 15.64002  ? 56  LYS B HA   1 
ATOM   3670 H HB2  . LYS B 1 59  ? -32.06810 2.61149  18.88310 1.000 21.88012  ? 56  LYS B HB2  1 
ATOM   3671 H HB3  . LYS B 1 59  ? -33.64427 2.44054  18.99210 1.000 21.88012  ? 56  LYS B HB3  1 
ATOM   3672 H HG2  . LYS B 1 59  ? -33.39626 0.13069  18.96216 1.000 31.42964  ? 56  LYS B HG2  1 
ATOM   3673 H HG3  . LYS B 1 59  ? -31.82013 0.30104  18.85173 1.000 31.42964  ? 56  LYS B HG3  1 
ATOM   3674 H HD2  . LYS B 1 59  ? -31.72354 1.17415  20.97953 1.000 43.17521  ? 56  LYS B HD2  1 
ATOM   3675 H HD3  . LYS B 1 59  ? -33.30897 1.16426  21.08776 1.000 43.17521  ? 56  LYS B HD3  1 
ATOM   3676 H HE2  . LYS B 1 59  ? -33.28535 -1.17859 20.99282 1.000 53.11718  ? 56  LYS B HE2  1 
ATOM   3677 H HE3  . LYS B 1 59  ? -31.69758 -1.14954 20.93327 1.000 53.11718  ? 56  LYS B HE3  1 
ATOM   3678 H HZ1  . LYS B 1 59  ? -31.63834 -0.42694 23.03264 1.000 58.62907  ? 56  LYS B HZ1  1 
ATOM   3679 H HZ2  . LYS B 1 59  ? -33.06618 -0.18940 23.08916 1.000 58.62907  ? 56  LYS B HZ2  1 
ATOM   3680 H HZ3  . LYS B 1 59  ? -32.55836 -1.54560 23.05482 1.000 58.62907  ? 56  LYS B HZ3  1 
ATOM   3681 N N    . PHE B 1 60  ? -32.60448 4.40832  16.43529 1.000 10.80938  ? 57  PHE B N    1 
ATOM   3682 C CA   . PHE B 1 60  ? -33.06747 5.78526  16.35552 1.000 11.06863  ? 57  PHE B CA   1 
ATOM   3683 C C    . PHE B 1 60  ? -32.57722 6.58312  15.15277 1.000 9.28029   ? 57  PHE B C    1 
ATOM   3684 O O    . PHE B 1 60  ? -32.86370 7.78330  15.08342 1.000 11.32383  ? 57  PHE B O    1 
ATOM   3685 C CB   . PHE B 1 60  ? -32.69396 6.54125  17.63909 1.000 11.49997  ? 57  PHE B CB   1 
ATOM   3686 C CG   . PHE B 1 60  ? -33.22241 5.90915  18.88366 1.000 12.57832  ? 57  PHE B CG   1 
ATOM   3687 C CD1  . PHE B 1 60  ? -34.58375 5.81415  19.09509 1.000 15.03521  ? 57  PHE B CD1  1 
ATOM   3688 C CD2  . PHE B 1 60  ? -32.36125 5.41001  19.84482 1.000 14.23457  ? 57  PHE B CD2  1 
ATOM   3689 C CE1  . PHE B 1 60  ? -35.07732 5.23305  20.24606 1.000 15.71745  ? 57  PHE B CE1  1 
ATOM   3690 C CE2  . PHE B 1 60  ? -32.84879 4.83033  20.99740 1.000 16.43255  ? 57  PHE B CE2  1 
ATOM   3691 C CZ   . PHE B 1 60  ? -34.20707 4.73804  21.19637 1.000 16.87592  ? 57  PHE B CZ   1 
ATOM   3692 H H    . PHE B 1 60  ? -31.75369 4.30892  16.35862 1.000 12.97126  ? 57  PHE B H    1 
ATOM   3693 H HA   . PHE B 1 60  ? -34.03202 5.74074  16.26303 1.000 13.28235  ? 57  PHE B HA   1 
ATOM   3694 H HB2  . PHE B 1 60  ? -31.72724 6.57474  17.71137 1.000 13.79996  ? 57  PHE B HB2  1 
ATOM   3695 H HB3  . PHE B 1 60  ? -33.05416 7.44042  17.58763 1.000 13.79996  ? 57  PHE B HB3  1 
ATOM   3696 H HD1  . PHE B 1 60  ? -35.17342 6.14462  18.45636 1.000 18.04225  ? 57  PHE B HD1  1 
ATOM   3697 H HD2  . PHE B 1 60  ? -31.44249 5.46609  19.71202 1.000 17.08149  ? 57  PHE B HD2  1 
ATOM   3698 H HE1  . PHE B 1 60  ? -35.99564 5.17514  20.38107 1.000 18.86094  ? 57  PHE B HE1  1 
ATOM   3699 H HE2  . PHE B 1 60  ? -32.26060 4.50248  21.63884 1.000 19.71906  ? 57  PHE B HE2  1 
ATOM   3700 H HZ   . PHE B 1 60  ? -34.53846 4.34264  21.97016 1.000 20.25110  ? 57  PHE B HZ   1 
ATOM   3701 N N    . ARG B 1 61  ? -31.88092 5.96508  14.19456 1.000 10.92841  ? 58  ARG B N    1 
ATOM   3702 C CA   . ARG B 1 61  ? -31.37890 6.71744  13.04517 1.000 12.11450  ? 58  ARG B CA   1 
ATOM   3703 C C    . ARG B 1 61  ? -32.49060 7.51639  12.37262 1.000 11.48210  ? 58  ARG B C    1 
ATOM   3704 O O    . ARG B 1 61  ? -32.33651 8.71195  12.09615 1.000 12.05610  ? 58  ARG B O    1 
ATOM   3705 C CB   . ARG B 1 61  ? -30.74246 5.77019  12.02289 1.000 15.23608  ? 58  ARG B CB   1 
ATOM   3706 C CG   . ARG B 1 61  ? -30.34491 6.44304  10.71392 1.000 17.03963  ? 58  ARG B CG   1 
ATOM   3707 C CD   . ARG B 1 61  ? -30.08861 5.42533  9.61622  1.000 19.76052  ? 58  ARG B CD   1 
ATOM   3708 N NE   . ARG B 1 61  ? -31.32664 4.87875  9.07421  1.000 24.82564  ? 58  ARG B NE   1 
ATOM   3709 C CZ   . ARG B 1 61  ? -32.14482 5.54006  8.26665  1.000 29.65075  ? 58  ARG B CZ   1 
ATOM   3710 N NH1  . ARG B 1 61  ? -31.91640 6.79963  7.93131  1.000 30.66122  ? 58  ARG B NH1  1 
ATOM   3711 N NH2  . ARG B 1 61  ? -33.21490 4.92020  7.77939  1.000 31.62833  ? 58  ARG B NH2  1 
ATOM   3712 H H    . ARG B 1 61  ? -31.68953 5.12668  14.18707 1.000 13.11409  ? 58  ARG B H    1 
ATOM   3713 H HA   . ARG B 1 61  ? -30.70029 7.33221  13.36522 1.000 14.53740  ? 58  ARG B HA   1 
ATOM   3714 H HB2  . ARG B 1 61  ? -29.94118 5.38634  12.41213 1.000 18.28330  ? 58  ARG B HB2  1 
ATOM   3715 H HB3  . ARG B 1 61  ? -31.37800 5.06832  11.81228 1.000 18.28330  ? 58  ARG B HB3  1 
ATOM   3716 H HG2  . ARG B 1 61  ? -31.06134 7.02923  10.42408 1.000 20.44755  ? 58  ARG B HG2  1 
ATOM   3717 H HG3  . ARG B 1 61  ? -29.53220 6.95472  10.85020 1.000 20.44755  ? 58  ARG B HG3  1 
ATOM   3718 H HD2  . ARG B 1 61  ? -29.60418 5.85241  8.89246  1.000 23.71262  ? 58  ARG B HD2  1 
ATOM   3719 H HD3  . ARG B 1 61  ? -29.56670 4.69175  9.97729  1.000 23.71262  ? 58  ARG B HD3  1 
ATOM   3720 H HE   . ARG B 1 61  ? -31.54043 4.07483  9.29241  1.000 29.79076  ? 58  ARG B HE   1 
ATOM   3721 H HH11 . ARG B 1 61  ? -31.22455 7.20773  8.23856  1.000 36.79346  ? 58  ARG B HH11 1 
ATOM   3722 H HH12 . ARG B 1 61  ? -32.45980 7.21011  7.40613  1.000 36.79346  ? 58  ARG B HH12 1 
ATOM   3723 H HH21 . ARG B 1 61  ? -33.36953 4.10053  7.98872  1.000 37.95400  ? 58  ARG B HH21 1 
ATOM   3724 H HH22 . ARG B 1 61  ? -33.75263 5.33882  7.25478  1.000 37.95400  ? 58  ARG B HH22 1 
ATOM   3725 N N    . GLU B 1 62  ? -33.60543 6.84987  12.06023 1.000 12.39062  ? 59  GLU B N    1 
ATOM   3726 C CA   A GLU B 1 62  ? -34.72581 7.51520  11.40384 0.359 15.02361  ? 59  GLU B CA   1 
ATOM   3727 C CA   B GLU B 1 62  ? -34.70017 7.54280  11.39589 0.641 14.53361  ? 59  GLU B CA   1 
ATOM   3728 C C    . GLU B 1 62  ? -35.47925 8.41245  12.37617 1.000 13.34148  ? 59  GLU B C    1 
ATOM   3729 O O    . GLU B 1 62  ? -35.80246 9.56366  12.06444 1.000 13.02614  ? 59  GLU B O    1 
ATOM   3730 C CB   A GLU B 1 62  ? -35.70405 6.46855  10.86662 0.359 19.56361  ? 59  GLU B CB   1 
ATOM   3731 C CB   B GLU B 1 62  ? -35.62968 6.54285  10.70687 0.641 18.31361  ? 59  GLU B CB   1 
ATOM   3732 C CG   A GLU B 1 62  ? -35.14702 5.52237  9.83832  0.359 25.29361  ? 59  GLU B CG   1 
ATOM   3733 C CG   B GLU B 1 62  ? -36.73517 7.21372  9.90501  0.641 23.27361  ? 59  GLU B CG   1 
ATOM   3734 C CD   A GLU B 1 62  ? -36.10218 4.38323  9.53193  0.359 33.10361  ? 59  GLU B CD   1 
ATOM   3735 C CD   B GLU B 1 62  ? -37.65568 6.22692  9.21636  0.641 31.03361  ? 59  GLU B CD   1 
ATOM   3736 O OE1  A GLU B 1 62  ? -37.25897 4.65861  9.15006  0.359 35.66361  ? 59  GLU B OE1  1 
ATOM   3737 O OE1  B GLU B 1 62  ? -37.36243 5.01333  9.24276  0.641 35.78361  ? 59  GLU B OE1  1 
ATOM   3738 O OE2  A GLU B 1 62  ? -35.69982 3.21115  9.68906  0.359 36.17361  ? 59  GLU B OE2  1 
ATOM   3739 O OE2  B GLU B 1 62  ? -38.67697 6.66964  8.64915  0.641 31.59361  ? 59  GLU B OE2  1 
ATOM   3740 H H    A GLU B 1 62  ? -33.73568 6.01456  12.21800 0.359 14.86874  ? 59  GLU B H    1 
ATOM   3741 H H    B GLU B 1 62  ? -33.74545 6.01651  12.21993 0.641 14.86874  ? 59  GLU B H    1 
ATOM   3742 H HA   A GLU B 1 62  ? -34.37429 8.04853  10.67385 0.359 18.02833  ? 59  GLU B HA   1 
ATOM   3743 H HA   B GLU B 1 62  ? -34.32848 8.11837  10.70926 0.641 17.44033  ? 59  GLU B HA   1 
ATOM   3744 H HB2  A GLU B 1 62  ? -36.01567 5.93224  11.61238 0.359 23.47633  ? 59  GLU B HB2  1 
ATOM   3745 H HB2  B GLU B 1 62  ? -35.10828 5.99603  10.09858 0.641 21.97633  ? 59  GLU B HB2  1 
ATOM   3746 H HB3  A GLU B 1 62  ? -36.45084 6.93225  10.45651 0.359 23.47633  ? 59  GLU B HB3  1 
ATOM   3747 H HB3  B GLU B 1 62  ? -36.04615 5.98388  11.38141 0.641 21.97633  ? 59  GLU B HB3  1 
ATOM   3748 H HG2  A GLU B 1 62  ? -34.98155 6.00810  9.01516  0.359 30.35233  ? 59  GLU B HG2  1 
ATOM   3749 H HG2  B GLU B 1 62  ? -37.27305 7.75561  10.50329 0.641 27.92833  ? 59  GLU B HG2  1 
ATOM   3750 H HG3  A GLU B 1 62  ? -34.31918 5.14180  10.17110 0.359 30.35233  ? 59  GLU B HG3  1 
ATOM   3751 H HG3  B GLU B 1 62  ? -36.33314 7.77299  9.22202  0.641 27.92833  ? 59  GLU B HG3  1 
ATOM   3752 N N    . SER B 1 63  ? -35.79352 7.88029  13.55858 1.000 13.84907  ? 60  SER B N    1 
ATOM   3753 C CA   A SER B 1 63  ? -36.64920 8.61845  14.48046 0.654 13.75361  ? 60  SER B CA   1 
ATOM   3754 C CA   B SER B 1 63  ? -36.63215 8.60407  14.50908 0.346 14.82361  ? 60  SER B CA   1 
ATOM   3755 C C    . SER B 1 63  ? -36.00714 9.93497  14.90476 1.000 13.63143  ? 60  SER B C    1 
ATOM   3756 O O    . SER B 1 63  ? -36.70548 10.94520 15.05013 1.000 15.54477  ? 60  SER B O    1 
ATOM   3757 C CB   A SER B 1 63  ? -37.01521 7.75441  15.68805 0.654 14.12361  ? 60  SER B CB   1 
ATOM   3758 C CB   B SER B 1 63  ? -36.85266 7.73226  15.74567 0.346 16.62361  ? 60  SER B CB   1 
ATOM   3759 O OG   A SER B 1 63  ? -35.88101 7.43526  16.46919 0.654 13.77361  ? 60  SER B OG   1 
ATOM   3760 O OG   B SER B 1 63  ? -37.51658 8.45041  16.76604 0.346 17.43361  ? 60  SER B OG   1 
ATOM   3761 H H    A SER B 1 63  ? -35.53006 7.11248  13.84258 0.654 16.61888  ? 60  SER B H    1 
ATOM   3762 H H    B SER B 1 63  ? -35.53528 7.10691  13.83206 0.346 16.61888  ? 60  SER B H    1 
ATOM   3763 H HA   A SER B 1 63  ? -37.47888 8.83437  14.02668 0.654 16.50433  ? 60  SER B HA   1 
ATOM   3764 H HA   B SER B 1 63  ? -37.49036 8.79242  14.09809 0.346 17.78833  ? 60  SER B HA   1 
ATOM   3765 H HB2  A SER B 1 63  ? -37.64690 8.24149  16.23998 0.654 16.94833  ? 60  SER B HB2  1 
ATOM   3766 H HB2  B SER B 1 63  ? -37.39345 6.96614  15.49768 0.346 19.94833  ? 60  SER B HB2  1 
ATOM   3767 H HB3  A SER B 1 63  ? -37.41763 6.93056  15.37147 0.654 16.94833  ? 60  SER B HB3  1 
ATOM   3768 H HB3  B SER B 1 63  ? -35.99122 7.43628  16.07918 0.346 19.94833  ? 60  SER B HB3  1 
ATOM   3769 H HG   A SER B 1 63  ? -35.64674 8.10299  16.92179 0.654 16.52833  ? 60  SER B HG   1 
ATOM   3770 H HG   B SER B 1 63  ? -37.04231 9.09630  17.01802 0.346 20.92033  ? 60  SER B HG   1 
ATOM   3771 N N    . LYS B 1 64  ? -34.68969 9.95502  15.09602 1.000 12.71826  ? 61  LYS B N    1 
ATOM   3772 C CA   A LYS B 1 64  ? -33.99329 11.18003 15.46888 0.537 11.52361  ? 61  LYS B CA   1 
ATOM   3773 C CA   B LYS B 1 64  ? -33.95845 11.15613 15.47880 0.463 12.03361  ? 61  LYS B CA   1 
ATOM   3774 C C    . LYS B 1 64  ? -33.33777 11.87344 14.28447 1.000 11.26247  ? 61  LYS B C    1 
ATOM   3775 O O    . LYS B 1 64  ? -32.70936 12.92155 14.46505 1.000 15.02823  ? 61  LYS B O    1 
ATOM   3776 C CB   A LYS B 1 64  ? -32.97561 10.88928 16.57015 0.537 12.88361  ? 61  LYS B CB   1 
ATOM   3777 C CB   B LYS B 1 64  ? -32.86374 10.80461 16.49554 0.463 13.37361  ? 61  LYS B CB   1 
ATOM   3778 C CG   A LYS B 1 64  ? -33.65441 10.43111 17.84623 0.537 15.11361  ? 61  LYS B CG   1 
ATOM   3779 C CG   B LYS B 1 64  ? -33.37471 10.24193 17.82141 0.463 16.32361  ? 61  LYS B CG   1 
ATOM   3780 C CD   A LYS B 1 64  ? -32.66994 10.20790 18.96460 0.537 17.16361  ? 61  LYS B CD   1 
ATOM   3781 C CD   B LYS B 1 64  ? -33.91948 11.33705 18.72641 0.463 17.78361  ? 61  LYS B CD   1 
ATOM   3782 C CE   A LYS B 1 64  ? -33.36091 9.59486  20.16671 0.537 20.99361  ? 61  LYS B CE   1 
ATOM   3783 C CE   B LYS B 1 64  ? -34.05545 10.86077 20.16613 0.463 21.72361  ? 61  LYS B CE   1 
ATOM   3784 N NZ   A LYS B 1 64  ? -34.44863 10.47232 20.67806 0.537 22.53361  ? 61  LYS B NZ   1 
ATOM   3785 N NZ   B LYS B 1 64  ? -34.62723 11.92194 21.04079 0.463 25.72361  ? 61  LYS B NZ   1 
ATOM   3786 H H    A LYS B 1 64  ? -34.17772 9.26879  15.01505 0.537 15.26191  ? 61  LYS B H    1 
ATOM   3787 H H    B LYS B 1 64  ? -34.18473 9.26459  15.00705 0.463 15.26191  ? 61  LYS B H    1 
ATOM   3788 H HA   A LYS B 1 64  ? -34.63310 11.80880 15.83793 0.537 13.82833  ? 61  LYS B HA   1 
ATOM   3789 H HA   B LYS B 1 64  ? -34.57429 11.77120 15.90698 0.463 14.44033  ? 61  LYS B HA   1 
ATOM   3790 H HB2  A LYS B 1 64  ? -32.37486 10.18748 16.27437 0.537 15.46033  ? 61  LYS B HB2  1 
ATOM   3791 H HB2  B LYS B 1 64  ? -32.28067 10.13724 16.10116 0.463 16.04833  ? 61  LYS B HB2  1 
ATOM   3792 H HB3  A LYS B 1 64  ? -32.47332 11.69622 16.76369 0.537 15.46033  ? 61  LYS B HB3  1 
ATOM   3793 H HB3  B LYS B 1 64  ? -32.35985 11.60904 16.69526 0.463 16.04833  ? 61  LYS B HB3  1 
ATOM   3794 H HG2  A LYS B 1 64  ? -34.28735 11.10850 18.13160 0.537 18.13633  ? 61  LYS B HG2  1 
ATOM   3795 H HG2  B LYS B 1 64  ? -34.08871 9.60898  17.64685 0.463 19.58833  ? 61  LYS B HG2  1 
ATOM   3796 H HG3  A LYS B 1 64  ? -34.11644 9.59476  17.67903 0.537 18.13633  ? 61  LYS B HG3  1 
ATOM   3797 H HG3  B LYS B 1 64  ? -32.64556 9.80021  18.28416 0.463 19.58833  ? 61  LYS B HG3  1 
ATOM   3798 H HD2  A LYS B 1 64  ? -31.97227 9.60299  18.66753 0.537 20.59633  ? 61  LYS B HD2  1 
ATOM   3799 H HD2  B LYS B 1 64  ? -33.31428 12.09497 18.71267 0.463 21.34033  ? 61  LYS B HD2  1 
ATOM   3800 H HD3  A LYS B 1 64  ? -32.28230 11.05638 19.23052 0.537 20.59633  ? 61  LYS B HD3  1 
ATOM   3801 H HD3  B LYS B 1 64  ? -34.79627 11.60686 18.41123 0.463 21.34033  ? 61  LYS B HD3  1 
ATOM   3802 H HE2  A LYS B 1 64  ? -33.74995 8.74313  19.91351 0.537 25.19233  ? 61  LYS B HE2  1 
ATOM   3803 H HE2  B LYS B 1 64  ? -34.64498 10.09102 20.19535 0.463 26.06833  ? 61  LYS B HE2  1 
ATOM   3804 H HE3  A LYS B 1 64  ? -32.71375 9.46575  20.87764 0.537 25.19233  ? 61  LYS B HE3  1 
ATOM   3805 H HE3  B LYS B 1 64  ? -33.18025 10.62156 20.50920 0.463 26.06833  ? 61  LYS B HE3  1 
ATOM   3806 H HZ1  A LYS B 1 64  ? -35.08347 10.56138 20.06069 0.537 27.04033  ? 61  LYS B HZ1  1 
ATOM   3807 H HZ1  B LYS B 1 64  ? -34.68171 11.62866 21.87931 0.463 30.86833  ? 61  LYS B HZ1  1 
ATOM   3808 H HZ2  A LYS B 1 64  ? -34.80670 10.11732 21.41144 0.537 27.04033  ? 61  LYS B HZ2  1 
ATOM   3809 H HZ2  B LYS B 1 64  ? -34.10870 12.64501 21.02081 0.463 30.86833  ? 61  LYS B HZ2  1 
ATOM   3810 H HZ3  A LYS B 1 64  ? -34.12319 11.27674 20.87583 0.537 27.04033  ? 61  LYS B HZ3  1 
ATOM   3811 H HZ3  B LYS B 1 64  ? -35.44188 12.14283 20.75855 0.463 30.86833  ? 61  LYS B HZ3  1 
ATOM   3812 N N    . ASN B 1 65  ? -33.48704 11.32503 13.08190 1.000 10.03715  ? 62  ASN B N    1 
ATOM   3813 C CA   . ASN B 1 65  ? -33.02418 11.93243 11.83664 1.000 9.50106   ? 62  ASN B CA   1 
ATOM   3814 C C    . ASN B 1 65  ? -31.54955 12.33170 11.89574 1.000 11.32137  ? 62  ASN B C    1 
ATOM   3815 O O    . ASN B 1 65  ? -31.18392 13.50072 11.76145 1.000 11.59952  ? 62  ASN B O    1 
ATOM   3816 C CB   . ASN B 1 65  ? -33.90671 13.12421 11.45041 1.000 12.08284  ? 62  ASN B CB   1 
ATOM   3817 C CG   . ASN B 1 65  ? -33.74151 13.52217 9.99798  1.000 14.34173  ? 62  ASN B CG   1 
ATOM   3818 O OD1  . ASN B 1 65  ? -33.58632 12.66905 9.12590  1.000 18.34308  ? 62  ASN B OD1  1 
ATOM   3819 N ND2  . ASN B 1 65  ? -33.76912 14.82042 9.73087  1.000 17.20797  ? 62  ASN B ND2  1 
ATOM   3820 H H    . ASN B 1 65  ? -33.87114 10.56607 12.95524 1.000 12.04458  ? 62  ASN B H    1 
ATOM   3821 H HA   . ASN B 1 65  ? -33.09717 11.25746 11.14383 1.000 11.40127  ? 62  ASN B HA   1 
ATOM   3822 H HB2  . ASN B 1 65  ? -34.83686 12.88961 11.59420 1.000 14.49941  ? 62  ASN B HB2  1 
ATOM   3823 H HB3  . ASN B 1 65  ? -33.66805 13.88676 12.00036 1.000 14.49941  ? 62  ASN B HB3  1 
ATOM   3824 H HD21 . ASN B 1 65  ? -33.67945 15.09475 8.92075  1.000 20.64956  ? 62  ASN B HD21 1 
ATOM   3825 H HD22 . ASN B 1 65  ? -33.87669 15.38826 10.36773 1.000 20.64956  ? 62  ASN B HD22 1 
ATOM   3826 N N    . PHE B 1 66  ? -30.69106 11.33169 12.06914 1.000 9.92192   ? 63  PHE B N    1 
ATOM   3827 C CA   . PHE B 1 66  ? -29.26002 11.59174 12.13666 1.000 10.03293  ? 63  PHE B CA   1 
ATOM   3828 C C    . PHE B 1 66  ? -28.49979 10.57518 11.30039 1.000 9.60265   ? 63  PHE B C    1 
ATOM   3829 O O    . PHE B 1 66  ? -29.03269 9.54329  10.88301 1.000 10.13051  ? 63  PHE B O    1 
ATOM   3830 C CB   . PHE B 1 66  ? -28.73980 11.69336 13.58953 1.000 10.69081  ? 63  PHE B CB   1 
ATOM   3831 C CG   . PHE B 1 66  ? -28.58097 10.37691 14.30071 1.000 10.28134  ? 63  PHE B CG   1 
ATOM   3832 C CD1  . PHE B 1 66  ? -29.66810 9.74084  14.87414 1.000 12.55428  ? 63  PHE B CD1  1 
ATOM   3833 C CD2  . PHE B 1 66  ? -27.32776 9.80758  14.44920 1.000 12.28669  ? 63  PHE B CD2  1 
ATOM   3834 C CE1  . PHE B 1 66  ? -29.51014 8.54317  15.54836 1.000 14.38209  ? 63  PHE B CE1  1 
ATOM   3835 C CE2  . PHE B 1 66  ? -27.16564 8.61312  15.11510 1.000 14.24543  ? 63  PHE B CE2  1 
ATOM   3836 C CZ   . PHE B 1 66  ? -28.25645 7.98147  15.66941 1.000 12.69771  ? 63  PHE B CZ   1 
ATOM   3837 H H    . PHE B 1 66  ? -30.91182 10.50437 12.14922 1.000 11.90630  ? 63  PHE B H    1 
ATOM   3838 H HA   . PHE B 1 66  ? -29.07625 12.45319 11.73042 1.000 12.03951  ? 63  PHE B HA   1 
ATOM   3839 H HB2  . PHE B 1 66  ? -27.87024 12.12297 13.57512 1.000 12.82897  ? 63  PHE B HB2  1 
ATOM   3840 H HB3  . PHE B 1 66  ? -29.36543 12.22784 14.10316 1.000 12.82897  ? 63  PHE B HB3  1 
ATOM   3841 H HD1  . PHE B 1 66  ? -30.51345 10.12240 14.80554 1.000 15.06513  ? 63  PHE B HD1  1 
ATOM   3842 H HD2  . PHE B 1 66  ? -26.58409 10.23834 14.09382 1.000 14.74403  ? 63  PHE B HD2  1 
ATOM   3843 H HE1  . PHE B 1 66  ? -30.24878 8.11720  15.91966 1.000 17.25851  ? 63  PHE B HE1  1 
ATOM   3844 H HE2  . PHE B 1 66  ? -26.32005 8.23336  15.19038 1.000 17.09452  ? 63  PHE B HE2  1 
ATOM   3845 H HZ   . PHE B 1 66  ? -28.14795 7.17771  16.12448 1.000 15.23726  ? 63  PHE B HZ   1 
ATOM   3846 N N    . GLU B 1 67  ? -27.24912 10.92255 11.02097 1.000 9.42782   ? 64  GLU B N    1 
ATOM   3847 C CA   . GLU B 1 67  ? -26.31788 10.07009 10.30420 1.000 8.77592   ? 64  GLU B CA   1 
ATOM   3848 C C    . GLU B 1 67  ? -24.98857 10.10290 11.04210 1.000 8.33367   ? 64  GLU B C    1 
ATOM   3849 O O    . GLU B 1 67  ? -24.68981 11.05607 11.76621 1.000 10.13163  ? 64  GLU B O    1 
ATOM   3850 C CB   . GLU B 1 67  ? -26.11492 10.56994 8.87127  1.000 9.93902   ? 64  GLU B CB   1 
ATOM   3851 C CG   . GLU B 1 67  ? -25.30107 9.64167  7.98699  1.000 11.55007  ? 64  GLU B CG   1 
ATOM   3852 C CD   . GLU B 1 67  ? -25.85692 8.23461  7.95464  1.000 11.24215  ? 64  GLU B CD   1 
ATOM   3853 O OE1  . GLU B 1 67  ? -25.45716 7.41614  8.80933  1.000 10.65975  ? 64  GLU B OE1  1 
ATOM   3854 O OE2  . GLU B 1 67  ? -26.70208 7.95143  7.08197  1.000 14.89277  ? 64  GLU B OE2  1 
ATOM   3855 H H    . GLU B 1 67  ? -26.90565 11.67805 11.24645 1.000 11.31338  ? 64  GLU B H    1 
ATOM   3856 H HA   . GLU B 1 67  ? -26.64407 9.15732  10.26729 1.000 10.53110  ? 64  GLU B HA   1 
ATOM   3857 H HB2  . GLU B 1 67  ? -26.98499 10.68031 8.45692  1.000 11.92682  ? 64  GLU B HB2  1 
ATOM   3858 H HB3  . GLU B 1 67  ? -25.65273 11.42210 8.90438  1.000 11.92682  ? 64  GLU B HB3  1 
ATOM   3859 H HG2  . GLU B 1 67  ? -25.30210 9.98630  7.08028  1.000 13.86008  ? 64  GLU B HG2  1 
ATOM   3860 H HG3  . GLU B 1 67  ? -24.39268 9.59843  8.32443  1.000 13.86008  ? 64  GLU B HG3  1 
ATOM   3861 N N    . VAL B 1 68  ? -24.20184 9.04489  10.87211 1.000 7.30164   ? 65  VAL B N    1 
ATOM   3862 C CA   . VAL B 1 68  ? -22.86707 8.95007  11.44926 1.000 6.54353   ? 65  VAL B CA   1 
ATOM   3863 C C    . VAL B 1 68  ? -21.86821 8.82139  10.31285 1.000 7.23468   ? 65  VAL B C    1 
ATOM   3864 O O    . VAL B 1 68  ? -22.08748 8.06206  9.36253  1.000 9.09848   ? 65  VAL B O    1 
ATOM   3865 C CB   . VAL B 1 68  ? -22.75287 7.75746  12.42087 1.000 7.57973   ? 65  VAL B CB   1 
ATOM   3866 C CG1  . VAL B 1 68  ? -21.32859 7.60542  12.94604 1.000 7.99116   ? 65  VAL B CG1  1 
ATOM   3867 C CG2  . VAL B 1 68  ? -23.73759 7.93555  13.56592 1.000 9.27504   ? 65  VAL B CG2  1 
ATOM   3868 H H    . VAL B 1 68  ? -24.42625 8.35228  10.41436 1.000 8.76197   ? 65  VAL B H    1 
ATOM   3869 H HA   . VAL B 1 68  ? -22.66793 9.76022  11.94413 1.000 7.85223   ? 65  VAL B HA   1 
ATOM   3870 H HB   . VAL B 1 68  ? -22.97001 6.94030  11.94548 1.000 9.09567   ? 65  VAL B HB   1 
ATOM   3871 H HG11 . VAL B 1 68  ? -21.30045 6.86579  13.57299 1.000 9.58939   ? 65  VAL B HG11 1 
ATOM   3872 H HG12 . VAL B 1 68  ? -20.73404 7.42951  12.20007 1.000 9.58939   ? 65  VAL B HG12 1 
ATOM   3873 H HG13 . VAL B 1 68  ? -21.06680 8.42652  13.39119 1.000 9.58939   ? 65  VAL B HG13 1 
ATOM   3874 H HG21 . VAL B 1 68  ? -23.67595 7.16931  14.15751 1.000 11.13005  ? 65  VAL B HG21 1 
ATOM   3875 H HG22 . VAL B 1 68  ? -23.51550 8.74610  14.05026 1.000 11.13005  ? 65  VAL B HG22 1 
ATOM   3876 H HG23 . VAL B 1 68  ? -24.63481 8.00219  13.20336 1.000 11.13005  ? 65  VAL B HG23 1 
ATOM   3877 N N    . VAL B 1 69  ? -20.76959 9.55982  10.41699 1.000 8.11149   ? 66  VAL B N    1 
ATOM   3878 C CA   . VAL B 1 69  ? -19.69530 9.51889  9.43493  1.000 8.61049   ? 66  VAL B CA   1 
ATOM   3879 C C    . VAL B 1 69  ? -18.40839 9.18131  10.17374 1.000 7.72495   ? 66  VAL B C    1 
ATOM   3880 O O    . VAL B 1 69  ? -17.89422 9.99752  10.94942 1.000 7.80205   ? 66  VAL B O    1 
ATOM   3881 C CB   . VAL B 1 69  ? -19.56229 10.84221 8.67058  1.000 7.99101   ? 66  VAL B CB   1 
ATOM   3882 C CG1  . VAL B 1 69  ? -18.40371 10.77373 7.68093  1.000 9.78465   ? 66  VAL B CG1  1 
ATOM   3883 C CG2  . VAL B 1 69  ? -20.86004 11.17104 7.95385  1.000 8.72062   ? 66  VAL B CG2  1 
ATOM   3884 H H    . VAL B 1 69  ? -20.62105 10.10572 11.06470 1.000 9.73379   ? 66  VAL B H    1 
ATOM   3885 H HA   . VAL B 1 69  ? -19.87390 8.81140  8.79582  1.000 10.33259  ? 66  VAL B HA   1 
ATOM   3886 H HB   . VAL B 1 69  ? -19.37613 11.55389 9.30283  1.000 9.58921   ? 66  VAL B HB   1 
ATOM   3887 H HG11 . VAL B 1 69  ? -18.40279 11.57863 7.13960  1.000 11.74158  ? 66  VAL B HG11 1 
ATOM   3888 H HG12 . VAL B 1 69  ? -17.57102 10.70561 8.17377  1.000 11.74158  ? 66  VAL B HG12 1 
ATOM   3889 H HG13 . VAL B 1 69  ? -18.51767 9.99443  7.11472  1.000 11.74158  ? 66  VAL B HG13 1 
ATOM   3890 H HG21 . VAL B 1 69  ? -20.75626 12.01272 7.48299  1.000 10.46475  ? 66  VAL B HG21 1 
ATOM   3891 H HG22 . VAL B 1 69  ? -21.06103 10.46187 7.32332  1.000 10.46475  ? 66  VAL B HG22 1 
ATOM   3892 H HG23 . VAL B 1 69  ? -21.57249 11.24370 8.60810  1.000 10.46475  ? 66  VAL B HG23 1 
ATOM   3893 N N    . LEU B 1 70  ? -17.88780 7.98322  9.93146  1.000 7.64471   ? 67  LEU B N    1 
ATOM   3894 C CA   . LEU B 1 70  ? -16.61521 7.58155  10.50856 1.000 7.22890   ? 67  LEU B CA   1 
ATOM   3895 C C    . LEU B 1 70  ? -15.48063 8.42877  9.94807  1.000 7.98569   ? 67  LEU B C    1 
ATOM   3896 O O    . LEU B 1 70  ? -15.33164 8.56357  8.72894  1.000 9.06320   ? 67  LEU B O    1 
ATOM   3897 C CB   . LEU B 1 70  ? -16.34965 6.11581  10.17808 1.000 7.96426   ? 67  LEU B CB   1 
ATOM   3898 C CG   . LEU B 1 70  ? -15.01772 5.54359  10.66154 1.000 9.22377   ? 67  LEU B CG   1 
ATOM   3899 C CD1  . LEU B 1 70  ? -14.94274 5.50175  12.18544 1.000 10.54137  ? 67  LEU B CD1  1 
ATOM   3900 C CD2  . LEU B 1 70  ? -14.80920 4.15604  10.07073 1.000 10.03410  ? 67  LEU B CD2  1 
ATOM   3901 H H    . LEU B 1 70  ? -18.25376 7.38405  9.43480  1.000 9.17365   ? 67  LEU B H    1 
ATOM   3902 H HA   . LEU B 1 70  ? -16.64798 7.70214  11.47048 1.000 8.67468   ? 67  LEU B HA   1 
ATOM   3903 H HB2  . LEU B 1 70  ? -17.05294 5.58371  10.58201 1.000 9.55712   ? 67  LEU B HB2  1 
ATOM   3904 H HB3  . LEU B 1 70  ? -16.37051 6.01591  9.21347  1.000 9.55712   ? 67  LEU B HB3  1 
ATOM   3905 H HG   . LEU B 1 70  ? -14.30009 6.12291  10.36105 1.000 11.06852  ? 67  LEU B HG   1 
ATOM   3906 H HD11 . LEU B 1 70  ? -14.09762 5.10543  12.44927 1.000 12.64965  ? 67  LEU B HD11 1 
ATOM   3907 H HD12 . LEU B 1 70  ? -15.00561 6.40643  12.52967 1.000 12.64965  ? 67  LEU B HD12 1 
ATOM   3908 H HD13 . LEU B 1 70  ? -15.67844 4.96742  12.52327 1.000 12.64965  ? 67  LEU B HD13 1 
ATOM   3909 H HD21 . LEU B 1 70  ? -13.98938 3.78053  10.42821 1.000 12.04092  ? 67  LEU B HD21 1 
ATOM   3910 H HD22 . LEU B 1 70  ? -15.56258 3.59414  10.31070 1.000 12.04092  ? 67  LEU B HD22 1 
ATOM   3911 H HD23 . LEU B 1 70  ? -14.74587 4.22998  9.10563  1.000 12.04092  ? 67  LEU B HD23 1 
ATOM   3912 N N    . VAL B 1 71  ? -14.67044 8.97671  10.85128 1.000 8.36209   ? 68  VAL B N    1 
ATOM   3913 C CA   . VAL B 1 71  ? -13.43945 9.69006  10.52632 1.000 7.95310   ? 68  VAL B CA   1 
ATOM   3914 C C    . VAL B 1 71  ? -12.30837 8.83544  11.08915 1.000 7.27327   ? 68  VAL B C    1 
ATOM   3915 O O    . VAL B 1 71  ? -12.01493 8.87488  12.28954 1.000 8.48409   ? 68  VAL B O    1 
ATOM   3916 C CB   . VAL B 1 71  ? -13.42894 11.10699 11.11319 1.000 7.72510   ? 68  VAL B CB   1 
ATOM   3917 C CG1  . VAL B 1 71  ? -12.17961 11.87247 10.65690 1.000 9.71795   ? 68  VAL B CG1  1 
ATOM   3918 C CG2  . VAL B 1 71  ? -14.70184 11.85599 10.73892 1.000 8.98226   ? 68  VAL B CG2  1 
ATOM   3919 H H    . VAL B 1 71  ? -14.82076 8.94622  11.69749 1.000 10.03451  ? 68  VAL B H    1 
ATOM   3920 H HA   . VAL B 1 71  ? -13.33527 9.76394  9.56477  1.000 9.54372   ? 68  VAL B HA   1 
ATOM   3921 H HB   . VAL B 1 71  ? -13.39949 11.04421 12.08071 1.000 9.27012   ? 68  VAL B HB   1 
ATOM   3922 H HG11 . VAL B 1 71  ? -12.21172 12.77260 11.01694 1.000 11.66154  ? 68  VAL B HG11 1 
ATOM   3923 H HG12 . VAL B 1 71  ? -11.39059 11.41311 10.98452 1.000 11.66154  ? 68  VAL B HG12 1 
ATOM   3924 H HG13 . VAL B 1 71  ? -12.16523 11.90427 9.68752  1.000 11.66154  ? 68  VAL B HG13 1 
ATOM   3925 H HG21 . VAL B 1 71  ? -14.60598 12.78757 10.99162 1.000 10.77871  ? 68  VAL B HG21 1 
ATOM   3926 H HG22 . VAL B 1 71  ? -14.83976 11.78550 9.78137  1.000 10.77871  ? 68  VAL B HG22 1 
ATOM   3927 H HG23 . VAL B 1 71  ? -15.45129 11.46062 11.21105 1.000 10.77871  ? 68  VAL B HG23 1 
ATOM   3928 N N    . THR B 1 72  ? -11.68212 8.03636  10.23509 1.000 6.66930   ? 69  THR B N    1 
ATOM   3929 C CA   . THR B 1 72  ? -10.79953 6.98633  10.71729 1.000 6.87176   ? 69  THR B CA   1 
ATOM   3930 C C    . THR B 1 72  ? -9.44939  7.53772  11.15331 1.000 8.15810   ? 69  THR B C    1 
ATOM   3931 O O    . THR B 1 72  ? -8.88514  8.43096  10.51410 1.000 8.38249   ? 69  THR B O    1 
ATOM   3932 C CB   . THR B 1 72  ? -10.60431 5.91894  9.63527  1.000 7.82127   ? 69  THR B CB   1 
ATOM   3933 O OG1  . THR B 1 72  ? -9.87796  4.81306  10.18582 1.000 8.57500   ? 69  THR B OG1  1 
ATOM   3934 C CG2  . THR B 1 72  ? -9.83231  6.46199  8.42670  1.000 9.65889   ? 69  THR B CG2  1 
ATOM   3935 H H    . THR B 1 72  ? -11.75157 8.08205  9.37912  1.000 8.00315   ? 69  THR B H    1 
ATOM   3936 H HA   . THR B 1 72  ? -11.20664 6.57280  11.49456 1.000 8.24611   ? 69  THR B HA   1 
ATOM   3937 H HB   . THR B 1 72  ? -11.47733 5.63256  9.32427  1.000 9.38552   ? 69  THR B HB   1 
ATOM   3938 H HG1  . THR B 1 72  ? -10.29675 4.49077  10.83877 1.000 10.29000  ? 69  THR B HG1  1 
ATOM   3939 H HG21 . THR B 1 72  ? -9.87084  5.82596  7.69535  1.000 11.59067  ? 69  THR B HG21 1 
ATOM   3940 H HG22 . THR B 1 72  ? -10.22093 7.30140  8.13469  1.000 11.59067  ? 69  THR B HG22 1 
ATOM   3941 H HG23 . THR B 1 72  ? -8.90410  6.61108  8.66566  1.000 11.59067  ? 69  THR B HG23 1 
ATOM   3942 N N    . TRP B 1 73  ? -8.94126  6.99811  12.26156 1.000 8.97683   ? 70  TRP B N    1 
ATOM   3943 C CA   . TRP B 1 73  ? -7.54623  7.14207  12.64928 1.000 8.29859   ? 70  TRP B CA   1 
ATOM   3944 C C    . TRP B 1 73  ? -6.75470  5.86022  12.38648 1.000 8.42796   ? 70  TRP B C    1 
ATOM   3945 O O    . TRP B 1 73  ? -5.61869  5.73219  12.85023 1.000 9.99512   ? 70  TRP B O    1 
ATOM   3946 C CB   . TRP B 1 73  ? -7.42398  7.57901  14.11391 1.000 9.15426   ? 70  TRP B CB   1 
ATOM   3947 C CG   . TRP B 1 73  ? -7.79670  9.03148  14.37508 1.000 8.22906   ? 70  TRP B CG   1 
ATOM   3948 C CD1  . TRP B 1 73  ? -8.46373  9.87971  13.53196 1.000 8.51511   ? 70  TRP B CD1  1 
ATOM   3949 C CD2  . TRP B 1 73  ? -7.52470  9.78952  15.56539 1.000 7.48908   ? 70  TRP B CD2  1 
ATOM   3950 N NE1  . TRP B 1 73  ? -8.61895  11.11156 14.12300 1.000 8.29551   ? 70  TRP B NE1  1 
ATOM   3951 C CE2  . TRP B 1 73  ? -8.04989  11.08283 15.36854 1.000 8.28918   ? 70  TRP B CE2  1 
ATOM   3952 C CE3  . TRP B 1 73  ? -6.87975  9.50327  16.77290 1.000 8.65892   ? 70  TRP B CE3  1 
ATOM   3953 C CZ2  . TRP B 1 73  ? -7.96322  12.08043 16.33777 1.000 9.37002   ? 70  TRP B CZ2  1 
ATOM   3954 C CZ3  . TRP B 1 73  ? -6.79313  10.50066 17.73433 1.000 8.83306   ? 70  TRP B CZ3  1 
ATOM   3955 C CH2  . TRP B 1 73  ? -7.33185  11.77068 17.50937 1.000 8.81885   ? 70  TRP B CH2  1 
ATOM   3956 H H    . TRP B 1 73  ? -9.40151  6.53143  12.81832 1.000 10.77219  ? 70  TRP B H    1 
ATOM   3957 H HA   . TRP B 1 73  ? -7.14512  7.85320  12.12554 1.000 9.95830   ? 70  TRP B HA   1 
ATOM   3958 H HB2  . TRP B 1 73  ? -8.01166  7.02518  14.65132 1.000 10.98511  ? 70  TRP B HB2  1 
ATOM   3959 H HB3  . TRP B 1 73  ? -6.50396  7.45791  14.39638 1.000 10.98511  ? 70  TRP B HB3  1 
ATOM   3960 H HD1  . TRP B 1 73  ? -8.76785  9.65506  12.68229 1.000 10.21814  ? 70  TRP B HD1  1 
ATOM   3961 H HE1  . TRP B 1 73  ? -9.01006  11.79024 13.76800 1.000 9.95461   ? 70  TRP B HE1  1 
ATOM   3962 H HE3  . TRP B 1 73  ? -6.51620  8.66154  16.92856 1.000 10.39070  ? 70  TRP B HE3  1 
ATOM   3963 H HZ2  . TRP B 1 73  ? -8.32198  12.92606 16.19251 1.000 11.24402  ? 70  TRP B HZ2  1 
ATOM   3964 H HZ3  . TRP B 1 73  ? -6.36925  10.32077 18.54233 1.000 10.59967  ? 70  TRP B HZ3  1 
ATOM   3965 H HH2  . TRP B 1 73  ? -7.25894  12.41932 18.17183 1.000 10.58262  ? 70  TRP B HH2  1 
ATOM   3966 N N    . ASP B 1 74  ? -7.34576  4.90205  11.67550 1.000 7.76407   ? 71  ASP B N    1 
ATOM   3967 C CA   . ASP B 1 74  ? -6.58262  3.77293  11.16532 1.000 8.38617   ? 71  ASP B CA   1 
ATOM   3968 C C    . ASP B 1 74  ? -5.73636  4.23087  9.98690  1.000 10.71470  ? 71  ASP B C    1 
ATOM   3969 O O    . ASP B 1 74  ? -6.16033  5.07511  9.19205  1.000 12.13152  ? 71  ASP B O    1 
ATOM   3970 C CB   . ASP B 1 74  ? -7.52496  2.66672  10.69847 1.000 9.46285   ? 71  ASP B CB   1 
ATOM   3971 C CG   . ASP B 1 74  ? -7.99727  1.79393  11.82931 1.000 10.05352  ? 71  ASP B CG   1 
ATOM   3972 O OD1  . ASP B 1 74  ? -7.15987  1.06322  12.39811 1.000 12.15255  ? 71  ASP B OD1  1 
ATOM   3973 O OD2  . ASP B 1 74  ? -9.20254  1.84837  12.15034 1.000 10.79172  ? 71  ASP B OD2  1 
ATOM   3974 H H    . ASP B 1 74  ? -8.18239  4.88457  11.47715 1.000 9.31689   ? 71  ASP B H    1 
ATOM   3975 H HA   . ASP B 1 74  ? -6.01113  3.41818  11.86421 1.000 10.06341  ? 71  ASP B HA   1 
ATOM   3976 H HB2  . ASP B 1 74  ? -8.30408  3.06865  10.28335 1.000 11.35541  ? 71  ASP B HB2  1 
ATOM   3977 H HB3  . ASP B 1 74  ? -7.06094  2.10457  10.05848 1.000 11.35541  ? 71  ASP B HB3  1 
ATOM   3978 N N    . ASP B 1 75  ? -4.52743  3.67962  9.87892  1.000 11.01203  ? 72  ASP B N    1 
ATOM   3979 C CA   . ASP B 1 75  ? -3.66578  3.94236  8.73264  1.000 11.59681  ? 72  ASP B CA   1 
ATOM   3980 C C    . ASP B 1 75  ? -3.34965  2.67919  7.93894  1.000 12.61595  ? 72  ASP B C    1 
ATOM   3981 O O    . ASP B 1 75  ? -2.52632  2.72820  7.01816  1.000 13.76132  ? 72  ASP B O    1 
ATOM   3982 C CB   . ASP B 1 75  ? -2.38240  4.67480  9.14206  1.000 12.17354  ? 72  ASP B CB   1 
ATOM   3983 C CG   . ASP B 1 75  ? -1.36012  3.76760  9.79877  1.000 12.81965  ? 72  ASP B CG   1 
ATOM   3984 O OD1  . ASP B 1 75  ? -1.75114  2.80454  10.49180 1.000 13.95577  ? 72  ASP B OD1  1 
ATOM   3985 O OD2  . ASP B 1 75  ? -0.15105  4.03335  9.62762  1.000 14.53994  ? 72  ASP B OD2  1 
ATOM   3986 H H    . ASP B 1 75  ? -4.18451  3.14754  10.46107 1.000 13.21444  ? 72  ASP B H    1 
ATOM   3987 H HA   . ASP B 1 75  ? -4.13731  4.54599  8.13750  1.000 13.91617  ? 72  ASP B HA   1 
ATOM   3988 H HB2  . ASP B 1 75  ? -1.97431  5.06006  8.35091  1.000 14.60825  ? 72  ASP B HB2  1 
ATOM   3989 H HB3  . ASP B 1 75  ? -2.60823  5.37557  9.77358  1.000 14.60825  ? 72  ASP B HB3  1 
ATOM   3990 N N    . GLU B 1 76  ? -3.97975  1.55402  8.26485  1.000 14.26967  ? 73  GLU B N    1 
ATOM   3991 C CA   A GLU B 1 76  ? -3.85173  0.32067  7.49868  0.613 18.26156  ? 73  GLU B CA   1 
ATOM   3992 C CA   B GLU B 1 76  ? -3.84882  0.32367  7.49393  0.387 18.26156  ? 73  GLU B CA   1 
ATOM   3993 C C    . GLU B 1 76  ? -5.22215  -0.04551 6.94807  1.000 14.53466  ? 73  GLU B C    1 
ATOM   3994 O O    . GLU B 1 76  ? -6.19661  -0.13243 7.70499  1.000 12.79386  ? 73  GLU B O    1 
ATOM   3995 C CB   A GLU B 1 76  ? -3.29813  -0.80785 8.36493  0.613 27.23895  ? 73  GLU B CB   1 
ATOM   3996 C CB   B GLU B 1 76  ? -3.23936  -0.80357 8.32558  0.387 27.23895  ? 73  GLU B CB   1 
ATOM   3997 C CG   A GLU B 1 76  ? -2.66063  -1.93473 7.56674  0.613 36.56376  ? 73  GLU B CG   1 
ATOM   3998 C CG   B GLU B 1 76  ? -4.14571  -1.35550 9.38303  0.387 36.56376  ? 73  GLU B CG   1 
ATOM   3999 C CD   A GLU B 1 76  ? -3.68404  -2.82465 6.89454  0.613 43.57775  ? 73  GLU B CD   1 
ATOM   4000 C CD   B GLU B 1 76  ? -3.39787  -2.10953 10.46265 0.387 43.57775  ? 73  GLU B CD   1 
ATOM   4001 O OE1  A GLU B 1 76  ? -4.63647  -3.25144 7.58033  0.613 48.30990  ? 73  GLU B OE1  1 
ATOM   4002 O OE1  B GLU B 1 76  ? -2.85267  -3.19405 10.17335 0.387 48.30990  ? 73  GLU B OE1  1 
ATOM   4003 O OE2  A GLU B 1 76  ? -3.54128  -3.09078 5.68215  0.613 44.99635  ? 73  GLU B OE2  1 
ATOM   4004 O OE2  B GLU B 1 76  ? -3.35348  -1.61011 11.60525 0.387 44.99635  ? 73  GLU B OE2  1 
ATOM   4005 H H    . GLU B 1 76  ? -4.50058  1.48295  8.94550  1.000 17.12360  ? 73  GLU B H    1 
ATOM   4006 H HA   . GLU B 1 76  ? -3.24244  0.44793  6.75471  1.000 21.91387  ? 73  GLU B HA   1 
ATOM   4007 H HB2  A GLU B 1 76  ? -2.62104  -0.44374 8.95644  0.613 32.68674  ? 73  GLU B HB2  1 
ATOM   4008 H HB2  B GLU B 1 76  ? -3.00398  -1.53328 7.73143  0.387 32.68674  ? 73  GLU B HB2  1 
ATOM   4009 H HB3  A GLU B 1 76  ? -4.02396  -1.18679 8.88500  0.613 32.68674  ? 73  GLU B HB3  1 
ATOM   4010 H HB3  B GLU B 1 76  ? -2.44464  -0.46627 8.76778  0.387 32.68674  ? 73  GLU B HB3  1 
ATOM   4011 H HG2  A GLU B 1 76  ? -2.09501  -1.55342 6.87712  0.613 43.87651  ? 73  GLU B HG2  1 
ATOM   4012 H HG2  B GLU B 1 76  ? -4.62225  -0.62314 9.80429  0.387 43.87651  ? 73  GLU B HG2  1 
ATOM   4013 H HG3  A GLU B 1 76  ? -2.13028  -2.48498 8.16412  0.613 43.87651  ? 73  GLU B HG3  1 
ATOM   4014 H HG3  B GLU B 1 76  ? -4.77536  -1.96776 8.97124  0.387 43.87651  ? 73  GLU B HG3  1 
ATOM   4015 N N    . GLU B 1 77  ? -5.29381  -0.25764 5.63290  1.000 12.18190  ? 74  GLU B N    1 
ATOM   4016 C CA   . GLU B 1 77  ? -6.59003  -0.37536 4.97425  1.000 11.51733  ? 74  GLU B CA   1 
ATOM   4017 C C    . GLU B 1 77  ? -7.35442  -1.62352 5.40382  1.000 12.49936  ? 74  GLU B C    1 
ATOM   4018 O O    . GLU B 1 77  ? -8.58380  -1.58098 5.52334  1.000 12.17376  ? 74  GLU B O    1 
ATOM   4019 C CB   . GLU B 1 77  ? -6.42840  -0.32082 3.45448  1.000 13.86734  ? 74  GLU B CB   1 
ATOM   4020 C CG   . GLU B 1 77  ? -7.76194  -0.19609 2.73434  1.000 15.46266  ? 74  GLU B CG   1 
ATOM   4021 C CD   . GLU B 1 77  ? -7.62859  0.30727  1.31447  1.000 18.96196  ? 74  GLU B CD   1 
ATOM   4022 O OE1  . GLU B 1 77  ? -6.48383  0.42250  0.82652  1.000 21.11675  ? 74  GLU B OE1  1 
ATOM   4023 O OE2  . GLU B 1 77  ? -8.67483  0.59288  0.69178  1.000 21.60638  ? 74  GLU B OE2  1 
ATOM   4024 H H    . GLU B 1 77  ? -4.61661  -0.33578 5.10860  1.000 14.61828  ? 74  GLU B H    1 
ATOM   4025 H HA   . GLU B 1 77  ? -7.12649  0.38763  5.24061  1.000 13.82080  ? 74  GLU B HA   1 
ATOM   4026 H HB2  . GLU B 1 77  ? -5.88587  0.44853  3.22071  1.000 16.64081  ? 74  GLU B HB2  1 
ATOM   4027 H HB3  . GLU B 1 77  ? -5.99694  -1.13525 3.15206  1.000 16.64081  ? 74  GLU B HB3  1 
ATOM   4028 H HG2  . GLU B 1 77  ? -8.18475  -1.06851 2.70264  1.000 18.55519  ? 74  GLU B HG2  1 
ATOM   4029 H HG3  . GLU B 1 77  ? -8.32417  0.42761  3.21993  1.000 18.55519  ? 74  GLU B HG3  1 
ATOM   4030 N N    . GLU B 1 78  ? -6.67058  -2.74975 5.62391  1.000 13.06855  ? 75  GLU B N    1 
ATOM   4031 C CA   A GLU B 1 78  ? -7.40040  -3.94844 6.02517  0.511 13.72361  ? 75  GLU B CA   1 
ATOM   4032 C CA   B GLU B 1 78  ? -7.37930  -3.95907 6.03758  0.489 13.72361  ? 75  GLU B CA   1 
ATOM   4033 C C    . GLU B 1 78  ? -8.02401  -3.77247 7.40604  1.000 12.25773  ? 75  GLU B C    1 
ATOM   4034 O O    . GLU B 1 78  ? -9.14626  -4.23195 7.64513  1.000 13.22881  ? 75  GLU B O    1 
ATOM   4035 C CB   A GLU B 1 78  ? -6.49564  -5.17553 5.96051  0.511 29.93361  ? 75  GLU B CB   1 
ATOM   4036 C CB   B GLU B 1 78  ? -6.44316  -5.17095 6.06670  0.489 29.93361  ? 75  GLU B CB   1 
ATOM   4037 C CG   A GLU B 1 78  ? -5.95808  -5.45344 4.56157  0.511 29.93361  ? 75  GLU B CG   1 
ATOM   4038 C CG   B GLU B 1 78  ? -7.14984  -6.46210 6.50529  0.489 29.93361  ? 75  GLU B CG   1 
ATOM   4039 C CD   A GLU B 1 78  ? -7.04586  -5.44527 3.50240  0.511 29.93361  ? 75  GLU B CD   1 
ATOM   4040 C CD   B GLU B 1 78  ? -6.20134  -7.61197 6.80714  0.489 29.93361  ? 75  GLU B CD   1 
ATOM   4041 O OE1  A GLU B 1 78  ? -8.13281  -6.00415 3.75996  0.511 29.93361  ? 75  GLU B OE1  1 
ATOM   4042 O OE1  B GLU B 1 78  ? -4.99457  -7.50057 6.50487  0.489 29.93361  ? 75  GLU B OE1  1 
ATOM   4043 O OE2  A GLU B 1 78  ? -6.81941  -4.86565 2.41939  0.511 29.93361  ? 75  GLU B OE2  1 
ATOM   4044 O OE2  B GLU B 1 78  ? -6.67215  -8.63159 7.35433  0.489 29.93361  ? 75  GLU B OE2  1 
ATOM   4045 H H    A GLU B 1 78  ? -5.81856  -2.84059 5.55035  0.511 15.68226  ? 75  GLU B H    1 
ATOM   4046 H H    B GLU B 1 78  ? -5.81886  -2.83682 5.54274  0.489 15.68226  ? 75  GLU B H    1 
ATOM   4047 H HA   A GLU B 1 78  ? -8.12308  -4.10441 5.39724  0.511 16.46833  ? 75  GLU B HA   1 
ATOM   4048 H HA   B GLU B 1 78  ? -8.07045  -4.13757 5.38081  0.489 16.46833  ? 75  GLU B HA   1 
ATOM   4049 H HB2  A GLU B 1 78  ? -5.73739  -5.03771 6.54955  0.511 35.92033  ? 75  GLU B HB2  1 
ATOM   4050 H HB2  B GLU B 1 78  ? -6.08417  -5.31319 5.17687  0.489 35.92033  ? 75  GLU B HB2  1 
ATOM   4051 H HB3  A GLU B 1 78  ? -7.00051  -5.95303 6.24601  0.511 35.92033  ? 75  GLU B HB3  1 
ATOM   4052 H HB3  B GLU B 1 78  ? -5.72190  -4.99695 6.69153  0.489 35.92033  ? 75  GLU B HB3  1 
ATOM   4053 H HG2  A GLU B 1 78  ? -5.30938  -4.77024 4.33066  0.511 35.92033  ? 75  GLU B HG2  1 
ATOM   4054 H HG2  B GLU B 1 78  ? -7.65906  -6.28052 7.31067  0.489 35.92033  ? 75  GLU B HG2  1 
ATOM   4055 H HG3  A GLU B 1 78  ? -5.53708  -6.32727 4.55248  0.511 35.92033  ? 75  GLU B HG3  1 
ATOM   4056 H HG3  B GLU B 1 78  ? -7.74434  -6.74887 5.79450  0.489 35.92033  ? 75  GLU B HG3  1 
ATOM   4057 N N    . ALA B 1 79  ? -7.32093  -3.10610 8.32348  1.000 11.28264  ? 76  ALA B N    1 
ATOM   4058 C CA   . ALA B 1 79  ? -7.89077  -2.85689 9.64323  1.000 12.18831  ? 76  ALA B CA   1 
ATOM   4059 C C    . ALA B 1 79  ? -9.11317  -1.95168 9.54111  1.000 10.05377  ? 76  ALA B C    1 
ATOM   4060 O O    . ALA B 1 79  ? -10.14280 -2.20377 10.17642 1.000 12.02220  ? 76  ALA B O    1 
ATOM   4061 C CB   . ALA B 1 79  ? -6.83395  -2.24145 10.55889 1.000 12.95150  ? 76  ALA B CB   1 
ATOM   4062 H H    . ALA B 1 79  ? -6.52776  -2.79451 8.20782  1.000 13.53916  ? 76  ALA B H    1 
ATOM   4063 H HA   . ALA B 1 79  ? -8.16994  -3.69976 10.03379 1.000 14.62597  ? 76  ALA B HA   1 
ATOM   4064 H HB1  . ALA B 1 79  ? -7.19177  -2.18151 11.45849 1.000 15.54180  ? 76  ALA B HB1  1 
ATOM   4065 H HB2  . ALA B 1 79  ? -6.04463  -2.80522 10.55373 1.000 15.54180  ? 76  ALA B HB2  1 
ATOM   4066 H HB3  . ALA B 1 79  ? -6.61010  -1.35595 10.23226 1.000 15.54180  ? 76  ALA B HB3  1 
ATOM   4067 N N    . TYR B 1 80  ? -9.00832  -0.87887 8.75308  1.000 9.77326   ? 77  TYR B N    1 
ATOM   4068 C CA   . TYR B 1 80  ? -10.16223 -0.02708 8.46783  1.000 9.54910   ? 77  TYR B CA   1 
ATOM   4069 C C    . TYR B 1 80  ? -11.32548 -0.83861 7.91457  1.000 8.86089   ? 77  TYR B C    1 
ATOM   4070 O O    . TYR B 1 80  ? -12.46622 -0.68934 8.36497  1.000 9.96106   ? 77  TYR B O    1 
ATOM   4071 C CB   . TYR B 1 80  ? -9.72772  1.06806  7.48788  1.000 9.69403   ? 77  TYR B CB   1 
ATOM   4072 C CG   . TYR B 1 80  ? -10.80705 1.90172  6.81665  1.000 9.69023   ? 77  TYR B CG   1 
ATOM   4073 C CD1  . TYR B 1 80  ? -11.47692 1.43377  5.69508  1.000 10.86496  ? 77  TYR B CD1  1 
ATOM   4074 C CD2  . TYR B 1 80  ? -11.10284 3.18691  7.26219  1.000 10.18435  ? 77  TYR B CD2  1 
ATOM   4075 C CE1  . TYR B 1 80  ? -12.43265 2.20300  5.05539  1.000 10.61750  ? 77  TYR B CE1  1 
ATOM   4076 C CE2  . TYR B 1 80  ? -12.06131 3.96624  6.62632  1.000 10.77478  ? 77  TYR B CE2  1 
ATOM   4077 C CZ   . TYR B 1 80  ? -12.72320 3.46553  5.52283  1.000 10.66533  ? 77  TYR B CZ   1 
ATOM   4078 O OH   . TYR B 1 80  ? -13.66755 4.22445  4.86579  1.000 11.35538  ? 77  TYR B OH   1 
ATOM   4079 H H    . TYR B 1 80  ? -8.28106  -0.62307 8.37195  1.000 11.72791  ? 77  TYR B H    1 
ATOM   4080 H HA   . TYR B 1 80  ? -10.47397 0.39340  9.28448  1.000 11.45892  ? 77  TYR B HA   1 
ATOM   4081 H HB2  . TYR B 1 80  ? -9.16021  1.68807  7.97206  1.000 11.63284  ? 77  TYR B HB2  1 
ATOM   4082 H HB3  . TYR B 1 80  ? -9.22360  0.64325  6.77633  1.000 11.63284  ? 77  TYR B HB3  1 
ATOM   4083 H HD1  . TYR B 1 80  ? -11.27953 0.58630  5.36687  1.000 13.03796  ? 77  TYR B HD1  1 
ATOM   4084 H HD2  . TYR B 1 80  ? -10.65068 3.53011  7.99885  1.000 12.22122  ? 77  TYR B HD2  1 
ATOM   4085 H HE1  . TYR B 1 80  ? -12.87818 1.86804  4.31094  1.000 12.74100  ? 77  TYR B HE1  1 
ATOM   4086 H HE2  . TYR B 1 80  ? -12.25572 4.81923  6.94176  1.000 12.92973  ? 77  TYR B HE2  1 
ATOM   4087 H HH   . TYR B 1 80  ? -13.59093 5.03162  5.08535  1.000 13.62646  ? 77  TYR B HH   1 
ATOM   4088 N N    . ASN B 1 81  ? -11.05452 -1.71987 6.94840  1.000 9.05602   ? 78  ASN B N    1 
ATOM   4089 C CA   . ASN B 1 81  ? -12.13934 -2.44992 6.29957  1.000 8.97740   ? 78  ASN B CA   1 
ATOM   4090 C C    . ASN B 1 81  ? -12.86500 -3.35573 7.28612  1.000 9.93355   ? 78  ASN B C    1 
ATOM   4091 O O    . ASN B 1 81  ? -14.09958 -3.42068 7.29387  1.000 12.00596  ? 78  ASN B O    1 
ATOM   4092 C CB   . ASN B 1 81  ? -11.59789 -3.28412 5.13618  1.000 11.81311  ? 78  ASN B CB   1 
ATOM   4093 C CG   . ASN B 1 81  ? -11.22324 -2.44602 3.92391  1.000 13.54113  ? 78  ASN B CG   1 
ATOM   4094 O OD1  . ASN B 1 81  ? -11.64815 -1.30195 3.78345  1.000 14.73886  ? 78  ASN B OD1  1 
ATOM   4095 N ND2  . ASN B 1 81  ? -10.43334 -3.02927 3.02987  1.000 15.64583  ? 78  ASN B ND2  1 
ATOM   4096 H H    . ASN B 1 81  ? -10.26747 -1.90827 6.65745  1.000 10.86723  ? 78  ASN B H    1 
ATOM   4097 H HA   . ASN B 1 81  ? -12.77176 -1.80420 5.94744  1.000 10.77288  ? 78  ASN B HA   1 
ATOM   4098 H HB2  . ASN B 1 81  ? -10.80280 -3.75554 5.43026  1.000 14.17573  ? 78  ASN B HB2  1 
ATOM   4099 H HB3  . ASN B 1 81  ? -12.27755 -3.91926 4.86130  1.000 14.17573  ? 78  ASN B HB3  1 
ATOM   4100 H HD21 . ASN B 1 81  ? -10.19089 -2.59989 2.32527  1.000 18.77500  ? 78  ASN B HD21 1 
ATOM   4101 H HD22 . ASN B 1 81  ? -10.16423 -3.83636 3.15546  1.000 18.77500  ? 78  ASN B HD22 1 
ATOM   4102 N N    . GLY B 1 82  ? -12.11322 -4.08113 8.11650  1.000 9.69902   ? 79  GLY B N    1 
ATOM   4103 C CA   . GLY B 1 82  ? -12.74177 -4.99131 9.05561  1.000 9.86463   ? 79  GLY B CA   1 
ATOM   4104 C C    . GLY B 1 82  ? -13.51980 -4.27314 10.13437 1.000 10.90225  ? 79  GLY B C    1 
ATOM   4105 O O    . GLY B 1 82  ? -14.55192 -4.76576 10.59835 1.000 12.16795  ? 79  GLY B O    1 
ATOM   4106 H H    . GLY B 1 82  ? -11.25416 -4.06139 8.15144  1.000 11.63882  ? 79  GLY B H    1 
ATOM   4107 H HA2  . GLY B 1 82  ? -13.35212 -5.57333 8.57643  1.000 11.83755  ? 79  GLY B HA2  1 
ATOM   4108 H HA3  . GLY B 1 82  ? -12.05873 -5.53226 9.48191  1.000 11.83755  ? 79  GLY B HA3  1 
ATOM   4109 N N    . TYR B 1 83  ? -13.04634 -3.10132 10.54155 1.000 9.51828   ? 80  TYR B N    1 
ATOM   4110 C CA   . TYR B 1 83  ? -13.70643 -2.33396 11.59235 1.000 9.44383   ? 80  TYR B CA   1 
ATOM   4111 C C    . TYR B 1 83  ? -14.95591 -1.64271 11.06203 1.000 10.33438  ? 80  TYR B C    1 
ATOM   4112 O O    . TYR B 1 83  ? -16.00878 -1.68338 11.70782 1.000 10.30658  ? 80  TYR B O    1 
ATOM   4113 C CB   . TYR B 1 83  ? -12.68029 -1.35432 12.16473 1.000 9.53954   ? 80  TYR B CB   1 
ATOM   4114 C CG   . TYR B 1 83  ? -13.10378 -0.53325 13.35624 1.000 9.66064   ? 80  TYR B CG   1 
ATOM   4115 C CD1  . TYR B 1 83  ? -13.74404 -1.10766 14.44192 1.000 11.13603  ? 80  TYR B CD1  1 
ATOM   4116 C CD2  . TYR B 1 83  ? -12.80934 0.82123  13.41049 1.000 10.14734  ? 80  TYR B CD2  1 
ATOM   4117 C CE1  . TYR B 1 83  ? -14.10928 -0.34645 15.53610 1.000 10.97507  ? 80  TYR B CE1  1 
ATOM   4118 C CE2  . TYR B 1 83  ? -13.16178 1.58704  14.49197 1.000 10.02633  ? 80  TYR B CE2  1 
ATOM   4119 C CZ   . TYR B 1 83  ? -13.81209 1.00127  15.55583 1.000 8.69440   ? 80  TYR B CZ   1 
ATOM   4120 O OH   . TYR B 1 83  ? -14.17209 1.76789  16.64017 1.000 9.68966   ? 80  TYR B OH   1 
ATOM   4121 H H    . TYR B 1 83  ? -12.34084 -2.72491 10.22503 1.000 11.42193  ? 80  TYR B H    1 
ATOM   4122 H HA   . TYR B 1 83  ? -14.00774 -2.90423 12.31685 1.000 11.33259  ? 80  TYR B HA   1 
ATOM   4123 H HB2  . TYR B 1 83  ? -11.90056 -1.86336 12.43639 1.000 11.44745  ? 80  TYR B HB2  1 
ATOM   4124 H HB3  . TYR B 1 83  ? -12.44037 -0.72915 11.46295 1.000 11.44745  ? 80  TYR B HB3  1 
ATOM   4125 H HD1  . TYR B 1 83  ? -13.93083 -2.01868 14.43448 1.000 13.36323  ? 80  TYR B HD1  1 
ATOM   4126 H HD2  . TYR B 1 83  ? -12.36317 1.21860  12.69781 1.000 12.17681  ? 80  TYR B HD2  1 
ATOM   4127 H HE1  . TYR B 1 83  ? -14.55188 -0.73927 16.25352 1.000 13.17008  ? 80  TYR B HE1  1 
ATOM   4128 H HE2  . TYR B 1 83  ? -12.96320 2.49546  14.50715 1.000 12.03160  ? 80  TYR B HE2  1 
ATOM   4129 H HH   . TYR B 1 83  ? -13.97581 2.57267  16.50091 1.000 11.62759  ? 80  TYR B HH   1 
ATOM   4130 N N    . PHE B 1 84  ? -14.87395 -1.03355 9.87899  1.000 9.87988   ? 81  PHE B N    1 
ATOM   4131 C CA   . PHE B 1 84  ? -16.05347 -0.41254 9.27785  1.000 9.73915   ? 81  PHE B CA   1 
ATOM   4132 C C    . PHE B 1 84  ? -17.11371 -1.44804 8.91144  1.000 10.35289  ? 81  PHE B C    1 
ATOM   4133 O O    . PHE B 1 84  ? -18.30638 -1.12178 8.88899  1.000 9.75532   ? 81  PHE B O    1 
ATOM   4134 C CB   . PHE B 1 84  ? -15.61896 0.43036  8.06869  1.000 9.44811   ? 81  PHE B CB   1 
ATOM   4135 C CG   . PHE B 1 84  ? -16.74646 1.15866  7.38587  1.000 9.90578   ? 81  PHE B CG   1 
ATOM   4136 C CD1  . PHE B 1 84  ? -17.61382 1.96836  8.10565  1.000 9.45418   ? 81  PHE B CD1  1 
ATOM   4137 C CD2  . PHE B 1 84  ? -16.91536 1.05987  6.01052  1.000 12.31740  ? 81  PHE B CD2  1 
ATOM   4138 C CE1  . PHE B 1 84  ? -18.64677 2.63764  7.47093  1.000 10.38432  ? 81  PHE B CE1  1 
ATOM   4139 C CE2  . PHE B 1 84  ? -17.94604 1.72331  5.37509  1.000 11.98036  ? 81  PHE B CE2  1 
ATOM   4140 C CZ   . PHE B 1 84  ? -18.80835 2.51826  6.10573  1.000 11.64070  ? 81  PHE B CZ   1 
ATOM   4141 H H    . PHE B 1 84  ? -14.15677 -0.96627 9.40918  1.000 11.85586  ? 81  PHE B H    1 
ATOM   4142 H HA   . PHE B 1 84  ? -16.47185 0.18925  9.91323  1.000 11.68698  ? 81  PHE B HA   1 
ATOM   4143 H HB2  . PHE B 1 84  ? -14.97837 1.09449  8.36781  1.000 11.33773  ? 81  PHE B HB2  1 
ATOM   4144 H HB3  . PHE B 1 84  ? -15.20811 -0.15555 7.41385  1.000 11.33773  ? 81  PHE B HB3  1 
ATOM   4145 H HD1  . PHE B 1 84  ? -17.50018 2.06248  9.02387  1.000 11.34501  ? 81  PHE B HD1  1 
ATOM   4146 H HD2  . PHE B 1 84  ? -16.32693 0.54046  5.51167  1.000 14.78088  ? 81  PHE B HD2  1 
ATOM   4147 H HE1  . PHE B 1 84  ? -19.23095 3.16702  7.96427  1.000 12.46118  ? 81  PHE B HE1  1 
ATOM   4148 H HE2  . PHE B 1 84  ? -18.05980 1.63526  4.45628  1.000 14.37643  ? 81  PHE B HE2  1 
ATOM   4149 H HZ   . PHE B 1 84  ? -19.49750 2.97275  5.67746  1.000 13.96884  ? 81  PHE B HZ   1 
ATOM   4150 N N    . ALA B 1 85  ? -16.71354 -2.69442 8.64398  1.000 10.58451  ? 82  ALA B N    1 
ATOM   4151 C CA   . ALA B 1 85  ? -17.68896 -3.74277 8.36124  1.000 10.24636  ? 82  ALA B CA   1 
ATOM   4152 C C    . ALA B 1 85  ? -18.64198 -3.97364 9.52560  1.000 10.64043  ? 82  ALA B C    1 
ATOM   4153 O O    . ALA B 1 85  ? -19.76185 -4.45378 9.31442  1.000 12.03813  ? 82  ALA B O    1 
ATOM   4154 C CB   . ALA B 1 85  ? -16.96632 -5.04900 8.03287  1.000 11.43756  ? 82  ALA B CB   1 
ATOM   4155 H H    . ALA B 1 85  ? -15.89372 -2.95319 8.62089  1.000 12.70141  ? 82  ALA B H    1 
ATOM   4156 H HA   . ALA B 1 85  ? -18.21283 -3.47640 7.58955  1.000 12.29564  ? 82  ALA B HA   1 
ATOM   4157 H HB1  . ALA B 1 85  ? -17.62367 -5.75229 7.91390  1.000 13.72507  ? 82  ALA B HB1  1 
ATOM   4158 H HB2  . ALA B 1 85  ? -16.45648 -4.93115 7.21612  1.000 13.72507  ? 82  ALA B HB2  1 
ATOM   4159 H HB3  . ALA B 1 85  ? -16.37088 -5.27318 8.76506  1.000 13.72507  ? 82  ALA B HB3  1 
ATOM   4160 N N    . LYS B 1 86  ? -18.22859 -3.63195 10.74395 1.000 9.70382   ? 83  LYS B N    1 
ATOM   4161 C CA   . LYS B 1 86  ? -19.06905 -3.79368 11.92097 1.000 10.35127  ? 83  LYS B CA   1 
ATOM   4162 C C    . LYS B 1 86  ? -20.09521 -2.68144 12.07374 1.000 8.88727   ? 83  LYS B C    1 
ATOM   4163 O O    . LYS B 1 86  ? -20.96236 -2.77188 12.95054 1.000 10.61659  ? 83  LYS B O    1 
ATOM   4164 C CB   . LYS B 1 86  ? -18.17996 -3.83245 13.16577 1.000 10.76963  ? 83  LYS B CB   1 
ATOM   4165 C CG   . LYS B 1 86  ? -17.16531 -4.96408 13.16247 1.000 10.23874  ? 83  LYS B CG   1 
ATOM   4166 C CD   . LYS B 1 86  ? -16.28670 -4.94591 14.41193 1.000 10.63049  ? 83  LYS B CD   1 
ATOM   4167 C CE   . LYS B 1 86  ? -15.24545 -6.05676 14.37029 1.000 10.86404  ? 83  LYS B CE   1 
ATOM   4168 N NZ   . LYS B 1 86  ? -14.37745 -6.13572 15.58798 1.000 15.27895  ? 83  LYS B NZ   1 
ATOM   4169 H H    . LYS B 1 86  ? -17.45405 -3.29973 10.91517 1.000 11.64459  ? 83  LYS B H    1 
ATOM   4170 H HA   . LYS B 1 86  ? -19.55262 -4.63189 11.85414 1.000 12.42152  ? 83  LYS B HA   1 
ATOM   4171 H HB2  . LYS B 1 86  ? -17.69072 -2.99696 13.22499 1.000 12.92356  ? 83  LYS B HB2  1 
ATOM   4172 H HB3  . LYS B 1 86  ? -18.74352 -3.94303 13.94748 1.000 12.92356  ? 83  LYS B HB3  1 
ATOM   4173 H HG2  . LYS B 1 86  ? -17.63346 -5.81313 13.13349 1.000 12.28649  ? 83  LYS B HG2  1 
ATOM   4174 H HG3  . LYS B 1 86  ? -16.59028 -4.87562 12.38631 1.000 12.28649  ? 83  LYS B HG3  1 
ATOM   4175 H HD2  . LYS B 1 86  ? -15.82432 -4.09509 14.46848 1.000 12.75659  ? 83  LYS B HD2  1 
ATOM   4176 H HD3  . LYS B 1 86  ? -16.84081 -5.07523 15.19751 1.000 12.75659  ? 83  LYS B HD3  1 
ATOM   4177 H HE2  . LYS B 1 86  ? -15.70291 -6.90744 14.28105 1.000 13.03684  ? 83  LYS B HE2  1 
ATOM   4178 H HE3  . LYS B 1 86  ? -14.66582 -5.91004 13.60647 1.000 13.03684  ? 83  LYS B HE3  1 
ATOM   4179 H HZ1  . LYS B 1 86  ? -13.81220 -6.81930 15.51507 1.000 18.33474  ? 83  LYS B HZ1  1 
ATOM   4180 H HZ2  . LYS B 1 86  ? -13.91069 -5.38335 15.67839 1.000 18.33474  ? 83  LYS B HZ2  1 
ATOM   4181 H HZ3  . LYS B 1 86  ? -14.88013 -6.25267 16.31306 1.000 18.33474  ? 83  LYS B HZ3  1 
ATOM   4182 N N    . MET B 1 87  ? -20.03241 -1.66204 11.23696 1.000 9.21630   ? 84  MET B N    1 
ATOM   4183 C CA   . MET B 1 87  ? -20.80706 -0.45003 11.40321 1.000 9.10169   ? 84  MET B CA   1 
ATOM   4184 C C    . MET B 1 87  ? -21.85031 -0.31760 10.30501 1.000 9.87691   ? 84  MET B C    1 
ATOM   4185 O O    . MET B 1 87  ? -21.63340 -0.75685 9.17257  1.000 12.02653  ? 84  MET B O    1 
ATOM   4186 C CB   . MET B 1 87  ? -19.88346 0.77098  11.32720 1.000 9.79316   ? 84  MET B CB   1 
ATOM   4187 C CG   . MET B 1 87  ? -18.73738 0.75143  12.31739 1.000 9.29964   ? 84  MET B CG   1 
ATOM   4188 S SD   . MET B 1 87  ? -17.56643 2.08288  12.01371 1.000 10.13601  ? 84  MET B SD   1 
ATOM   4189 C CE   . MET B 1 87  ? -16.32619 1.74301  13.25712 1.000 10.40109  ? 84  MET B CE   1 
ATOM   4190 H H    . MET B 1 87  ? -19.52957 -1.64837 10.53942 1.000 11.05956  ? 84  MET B H    1 
ATOM   4191 H HA   . MET B 1 87  ? -21.25121 -0.46868 12.26536 1.000 10.92203  ? 84  MET B HA   1 
ATOM   4192 H HB2  . MET B 1 87  ? -19.50115 0.81463  10.43679 1.000 11.75179  ? 84  MET B HB2  1 
ATOM   4193 H HB3  . MET B 1 87  ? -20.40873 1.56747  11.50213 1.000 11.75179  ? 84  MET B HB3  1 
ATOM   4194 H HG2  . MET B 1 87  ? -19.08921 0.85534  13.21534 1.000 11.15957  ? 84  MET B HG2  1 
ATOM   4195 H HG3  . MET B 1 87  ? -18.26439 -0.09207 12.24195 1.000 11.15957  ? 84  MET B HG3  1 
ATOM   4196 H HE1  . MET B 1 87  ? -15.64069 2.42801  13.21493 1.000 12.48131  ? 84  MET B HE1  1 
ATOM   4197 H HE2  . MET B 1 87  ? -16.74591 1.74850  14.13159 1.000 12.48131  ? 84  MET B HE2  1 
ATOM   4198 H HE3  . MET B 1 87  ? -15.93508 0.87252  13.08339 1.000 12.48131  ? 84  MET B HE3  1 
ATOM   4199 N N    . PRO B 1 88  ? -22.98689 0.30604  10.60827 1.000 9.06992   ? 85  PRO B N    1 
ATOM   4200 C CA   . PRO B 1 88  ? -24.07444 0.44193  9.62258  1.000 10.12407  ? 85  PRO B CA   1 
ATOM   4201 C C    . PRO B 1 88  ? -24.13344 1.78272  8.90146  1.000 9.45991   ? 85  PRO B C    1 
ATOM   4202 O O    . PRO B 1 88  ? -25.02611 1.96149  8.06481  1.000 11.97498  ? 85  PRO B O    1 
ATOM   4203 C CB   . PRO B 1 88  ? -25.30893 0.28857  10.52132 1.000 9.43667   ? 85  PRO B CB   1 
ATOM   4204 C CG   . PRO B 1 88  ? -24.88644 0.96856  11.78613 1.000 9.86383   ? 85  PRO B CG   1 
ATOM   4205 C CD   . PRO B 1 88  ? -23.45633 0.56496  11.98381 1.000 10.12972  ? 85  PRO B CD   1 
ATOM   4206 H HA   . PRO B 1 88  ? -24.03882 -0.27432 8.96942  1.000 12.14889  ? 85  PRO B HA   1 
ATOM   4207 H HB2  . PRO B 1 88  ? -26.07583 0.72767  10.12139 1.000 11.32401  ? 85  PRO B HB2  1 
ATOM   4208 H HB3  . PRO B 1 88  ? -25.50457 -0.64963 10.67104 1.000 11.32401  ? 85  PRO B HB3  1 
ATOM   4209 H HG2  . PRO B 1 88  ? -24.96475 1.93027  11.68666 1.000 11.83660  ? 85  PRO B HG2  1 
ATOM   4210 H HG3  . PRO B 1 88  ? -25.43753 0.66545  12.52459 1.000 11.83660  ? 85  PRO B HG3  1 
ATOM   4211 H HD2  . PRO B 1 88  ? -22.94803 1.28250  12.39328 1.000 12.15567  ? 85  PRO B HD2  1 
ATOM   4212 H HD3  . PRO B 1 88  ? -23.39518 -0.23660 12.52663 1.000 12.15567  ? 85  PRO B HD3  1 
ATOM   4213 N N    . TRP B 1 89  ? -23.22697 2.71253  9.19823  1.000 9.28798   ? 86  TRP B N    1 
ATOM   4214 C CA   . TRP B 1 89  ? -23.31877 4.09968  8.77817  1.000 8.04711   ? 86  TRP B CA   1 
ATOM   4215 C C    . TRP B 1 89  ? -22.30919 4.38032  7.65698  1.000 9.91567   ? 86  TRP B C    1 
ATOM   4216 O O    . TRP B 1 89  ? -21.96275 3.46548  6.88915  1.000 11.24374  ? 86  TRP B O    1 
ATOM   4217 C CB   . TRP B 1 89  ? -23.18660 4.99854  10.01109 1.000 7.30167   ? 86  TRP B CB   1 
ATOM   4218 C CG   . TRP B 1 89  ? -22.03406 4.66802  10.90284 1.000 8.31511   ? 86  TRP B CG   1 
ATOM   4219 C CD1  . TRP B 1 89  ? -20.71383 4.73945  10.58648 1.000 8.96084   ? 86  TRP B CD1  1 
ATOM   4220 C CD2  . TRP B 1 89  ? -22.09778 4.24088  12.26918 1.000 6.74143   ? 86  TRP B CD2  1 
ATOM   4221 N NE1  . TRP B 1 89  ? -19.94663 4.36695  11.66433 1.000 9.00532   ? 86  TRP B NE1  1 
ATOM   4222 C CE2  . TRP B 1 89  ? -20.77400 4.05994  12.71250 1.000 7.22545   ? 86  TRP B CE2  1 
ATOM   4223 C CE3  . TRP B 1 89  ? -23.14586 3.99427  13.16054 1.000 8.10264   ? 86  TRP B CE3  1 
ATOM   4224 C CZ2  . TRP B 1 89  ? -20.47080 3.63301  14.00607 1.000 8.29647   ? 86  TRP B CZ2  1 
ATOM   4225 C CZ3  . TRP B 1 89  ? -22.84352 3.57755  14.44367 1.000 7.77831   ? 86  TRP B CZ3  1 
ATOM   4226 C CH2  . TRP B 1 89  ? -21.51839 3.40247  14.85527 1.000 8.53226   ? 86  TRP B CH2  1 
ATOM   4227 H H    . TRP B 1 89  ? -22.52146 2.55023  9.66246  1.000 11.14558  ? 86  TRP B H    1 
ATOM   4228 H HA   . TRP B 1 89  ? -24.19986 4.24710  8.40023  1.000 9.65653   ? 86  TRP B HA   1 
ATOM   4229 H HB2  . TRP B 1 89  ? -23.07269 5.91487  9.71398  1.000 8.76200   ? 86  TRP B HB2  1 
ATOM   4230 H HB3  . TRP B 1 89  ? -23.99652 4.91918  10.53894 1.000 8.76200   ? 86  TRP B HB3  1 
ATOM   4231 H HD1  . TRP B 1 89  ? -20.37821 5.00242  9.75998  1.000 10.75301  ? 86  TRP B HD1  1 
ATOM   4232 H HE1  . TRP B 1 89  ? -19.08745 4.33224  11.67855 1.000 10.80638  ? 86  TRP B HE1  1 
ATOM   4233 H HE3  . TRP B 1 89  ? -24.02995 4.10836  12.89545 1.000 9.72317   ? 86  TRP B HE3  1 
ATOM   4234 H HZ2  . TRP B 1 89  ? -19.59069 3.50998  14.28024 1.000 9.95577   ? 86  TRP B HZ2  1 
ATOM   4235 H HZ3  . TRP B 1 89  ? -23.53389 3.41062  15.04403 1.000 9.33398   ? 86  TRP B HZ3  1 
ATOM   4236 H HH2  . TRP B 1 89  ? -21.34555 3.12319  15.72535 1.000 10.23871  ? 86  TRP B HH2  1 
ATOM   4237 N N    . LEU B 1 90  ? -21.86785 5.62562  7.53964  1.000 9.34932   ? 87  LEU B N    1 
ATOM   4238 C CA   . LEU B 1 90  ? -21.03815 6.06063  6.42865  1.000 8.64850   ? 87  LEU B CA   1 
ATOM   4239 C C    . LEU B 1 90  ? -19.61133 6.28978  6.90069  1.000 7.73898   ? 87  LEU B C    1 
ATOM   4240 O O    . LEU B 1 90  ? -19.33219 6.35690  8.09853  1.000 8.70547   ? 87  LEU B O    1 
ATOM   4241 C CB   . LEU B 1 90  ? -21.59170 7.36101  5.84375  1.000 8.23156   ? 87  LEU B CB   1 
ATOM   4242 C CG   . LEU B 1 90  ? -23.06944 7.34137  5.44981  1.000 10.47734  ? 87  LEU B CG   1 
ATOM   4243 C CD1  . LEU B 1 90  ? -23.49364 8.68531  4.86868  1.000 12.19945  ? 87  LEU B CD1  1 
ATOM   4244 C CD2  . LEU B 1 90  ? -23.35668 6.19458  4.48376  1.000 11.88728  ? 87  LEU B CD2  1 
ATOM   4245 H H    . LEU B 1 90  ? -22.04085 6.24989  8.10529  1.000 11.21919  ? 87  LEU B H    1 
ATOM   4246 H HA   . LEU B 1 90  ? -21.03269 5.37423  5.74329  1.000 10.37820  ? 87  LEU B HA   1 
ATOM   4247 H HB2  . LEU B 1 90  ? -21.47965 8.06203  6.50474  1.000 9.87788   ? 87  LEU B HB2  1 
ATOM   4248 H HB3  . LEU B 1 90  ? -21.08405 7.57388  5.04508  1.000 9.87788   ? 87  LEU B HB3  1 
ATOM   4249 H HG   . LEU B 1 90  ? -23.60608 7.19031  6.24360  1.000 12.57280  ? 87  LEU B HG   1 
ATOM   4250 H HD11 . LEU B 1 90  ? -24.44151 8.65615  4.66473  1.000 14.63934  ? 87  LEU B HD11 1 
ATOM   4251 H HD12 . LEU B 1 90  ? -23.31686 9.38130  5.52079  1.000 14.63934  ? 87  LEU B HD12 1 
ATOM   4252 H HD13 . LEU B 1 90  ? -22.98618 8.85373  4.05934  1.000 14.63934  ? 87  LEU B HD13 1 
ATOM   4253 H HD21 . LEU B 1 90  ? -24.29006 6.22849  4.22194  1.000 14.26474  ? 87  LEU B HD21 1 
ATOM   4254 H HD22 . LEU B 1 90  ? -22.79021 6.29063  3.70223  1.000 14.26474  ? 87  LEU B HD22 1 
ATOM   4255 H HD23 . LEU B 1 90  ? -23.16801 5.35298  4.92762  1.000 14.26474  ? 87  LEU B HD23 1 
ATOM   4256 N N    . ALA B 1 91  ? -18.70051 6.44307  5.94427  1.000 8.36142   ? 88  ALA B N    1 
ATOM   4257 C CA   . ALA B 1 91  ? -17.32857 6.73059  6.31282  1.000 8.85162   ? 88  ALA B CA   1 
ATOM   4258 C C    . ALA B 1 91  ? -16.65682 7.59999  5.26692  1.000 10.05589  ? 88  ALA B C    1 
ATOM   4259 O O    . ALA B 1 91  ? -16.95009 7.50704  4.07245  1.000 11.54267  ? 88  ALA B O    1 
ATOM   4260 C CB   . ALA B 1 91  ? -16.50546 5.44326  6.45315  1.000 8.66936   ? 88  ALA B CB   1 
ATOM   4261 H H    . ALA B 1 91  ? -18.85279 6.38599  5.09979  1.000 10.03370  ? 88  ALA B H    1 
ATOM   4262 H HA   . ALA B 1 91  ? -17.34767 7.21711  7.15177  1.000 10.62195  ? 88  ALA B HA   1 
ATOM   4263 H HB1  . ALA B 1 91  ? -15.62097 5.66819  6.78177  1.000 10.40323  ? 88  ALA B HB1  1 
ATOM   4264 H HB2  . ALA B 1 91  ? -16.95017 4.85075  7.07930  1.000 10.40323  ? 88  ALA B HB2  1 
ATOM   4265 H HB3  . ALA B 1 91  ? -16.43701 5.01598  5.58502  1.000 10.40323  ? 88  ALA B HB3  1 
ATOM   4266 N N    . ILE B 1 92  ? -15.75996 8.45882  5.73705  1.000 8.84002   ? 89  ILE B N    1 
ATOM   4267 C CA   A ILE B 1 92  ? -14.80191 9.09700  4.82464  0.376 10.15361  ? 89  ILE B CA   1 
ATOM   4268 C CA   B ILE B 1 92  ? -14.82906 9.08354  4.79683  0.624 8.61361   ? 89  ILE B CA   1 
ATOM   4269 C C    . ILE B 1 92  ? -13.94340 7.99747  4.20672  1.000 8.00090   ? 89  ILE B C    1 
ATOM   4270 O O    . ILE B 1 92  ? -13.48306 7.10030  4.93981  1.000 9.01350   ? 89  ILE B O    1 
ATOM   4271 C CB   A ILE B 1 92  ? -13.91427 10.09132 5.59886  0.376 11.88361  ? 89  ILE B CB   1 
ATOM   4272 C CB   B ILE B 1 92  ? -13.99926 10.16250 5.50709  0.624 7.75361   ? 89  ILE B CB   1 
ATOM   4273 C CG1  A ILE B 1 92  ? -14.74297 11.13214 6.36272  0.376 14.04361  ? 89  ILE B CG1  1 
ATOM   4274 C CG1  B ILE B 1 92  ? -14.92527 11.31737 5.89027  0.624 12.73361  ? 89  ILE B CG1  1 
ATOM   4275 C CG2  A ILE B 1 92  ? -12.94067 10.78541 4.64827  0.376 13.64361  ? 89  ILE B CG2  1 
ATOM   4276 C CG2  B ILE B 1 92  ? -12.86226 10.64554 4.61790  0.624 8.78361   ? 89  ILE B CG2  1 
ATOM   4277 C CD1  A ILE B 1 92  ? -15.46045 12.13683 5.49020  0.376 17.15361  ? 89  ILE B CD1  1 
ATOM   4278 C CD1  B ILE B 1 92  ? -14.29183 12.33161 6.77527  0.624 16.90361  ? 89  ILE B CD1  1 
ATOM   4279 H H    A ILE B 1 92  ? -15.68088 8.68917  6.56185  0.376 10.60802  ? 89  ILE B H    1 
ATOM   4280 H H    B ILE B 1 92  ? -15.66947 8.69035  6.56034  0.624 10.60802  ? 89  ILE B H    1 
ATOM   4281 H HA   A ILE B 1 92  ? -15.27222 9.57862  4.12626  0.376 12.18433  ? 89  ILE B HA   1 
ATOM   4282 H HA   B ILE B 1 92  ? -15.31756 9.50886  4.07477  0.624 10.33633  ? 89  ILE B HA   1 
ATOM   4283 H HB   A ILE B 1 92  ? -13.41562 9.57867  6.25418  0.376 14.26033  ? 89  ILE B HB   1 
ATOM   4284 H HB   B ILE B 1 92  ? -13.59989 9.78820  6.30790  0.624 9.30433   ? 89  ILE B HB   1 
ATOM   4285 H HG12 A ILE B 1 92  ? -15.41516 10.66716 6.88508  0.376 16.85233  ? 89  ILE B HG12 1 
ATOM   4286 H HG12 B ILE B 1 92  ? -15.21063 11.76906 5.08068  0.624 15.28033  ? 89  ILE B HG12 1 
ATOM   4287 H HG13 A ILE B 1 92  ? -14.15015 11.62682 6.94987  0.376 16.85233  ? 89  ILE B HG13 1 
ATOM   4288 H HG13 B ILE B 1 92  ? -15.69488 10.95698 6.35796  0.624 15.28033  ? 89  ILE B HG13 1 
ATOM   4289 H HG21 A ILE B 1 92  ? -12.52592 11.53090 5.10993  0.376 16.37233  ? 89  ILE B HG21 1 
ATOM   4290 H HG21 B ILE B 1 92  ? -12.41251 11.38579 5.05454  0.624 10.54033  ? 89  ILE B HG21 1 
ATOM   4291 H HG22 A ILE B 1 92  ? -12.26267 10.14956 4.37094  0.376 16.37233  ? 89  ILE B HG22 1 
ATOM   4292 H HG22 B ILE B 1 92  ? -12.23876 9.91574  4.47812  0.624 10.54033  ? 89  ILE B HG22 1 
ATOM   4293 H HG23 A ILE B 1 92  ? -13.42956 11.10627 3.87436  0.376 16.37233  ? 89  ILE B HG23 1 
ATOM   4294 H HG23 B ILE B 1 92  ? -13.22779 10.93576 3.76757  0.624 10.54033  ? 89  ILE B HG23 1 
ATOM   4295 H HD11 A ILE B 1 92  ? -16.13162 12.59367 6.02099  0.376 20.58433  ? 89  ILE B HD11 1 
ATOM   4296 H HD11 B ILE B 1 92  ? -14.97999 12.91800 7.12665  0.624 20.28433  ? 89  ILE B HD11 1 
ATOM   4297 H HD12 A ILE B 1 92  ? -14.81586 12.77684 5.14993  0.376 20.58433  ? 89  ILE B HD12 1 
ATOM   4298 H HD12 B ILE B 1 92  ? -13.84068 11.87725 7.50392  0.624 20.28433  ? 89  ILE B HD12 1 
ATOM   4299 H HD13 A ILE B 1 92  ? -15.88352 11.66959 4.75291  0.376 20.58433  ? 89  ILE B HD13 1 
ATOM   4300 H HD13 B ILE B 1 92  ? -13.65141 12.84547 6.25883  0.624 20.28433  ? 89  ILE B HD13 1 
ATOM   4301 N N    . PRO B 1 93  ? -13.69759 7.99309  2.89909  1.000 10.28635  ? 90  PRO B N    1 
ATOM   4302 C CA   . PRO B 1 93  ? -12.87032 6.92385  2.32443  1.000 11.20784  ? 90  PRO B CA   1 
ATOM   4303 C C    . PRO B 1 93  ? -11.50082 6.84866  2.98376  1.000 10.23383  ? 90  PRO B C    1 
ATOM   4304 O O    . PRO B 1 93  ? -10.89135 7.86793  3.31315  1.000 10.62696  ? 90  PRO B O    1 
ATOM   4305 C CB   . PRO B 1 93  ? -12.75053 7.31651  0.84829  1.000 12.99965  ? 90  PRO B CB   1 
ATOM   4306 C CG   . PRO B 1 93  ? -13.91480 8.19235  0.58475  1.000 12.87992  ? 90  PRO B CG   1 
ATOM   4307 C CD   . PRO B 1 93  ? -14.21231 8.91266  1.86766  1.000 11.46723  ? 90  PRO B CD   1 
ATOM   4308 H HA   . PRO B 1 93  ? -13.32210 6.06968  2.40926  1.000 13.44941  ? 90  PRO B HA   1 
ATOM   4309 H HB2  . PRO B 1 93  ? -11.91836 7.79247  0.70046  1.000 15.59958  ? 90  PRO B HB2  1 
ATOM   4310 H HB3  . PRO B 1 93  ? -12.78163 6.52214  0.29249  1.000 15.59958  ? 90  PRO B HB3  1 
ATOM   4311 H HG2  . PRO B 1 93  ? -13.69220 8.82429  -0.11667 1.000 15.45590  ? 90  PRO B HG2  1 
ATOM   4312 H HG3  . PRO B 1 93  ? -14.67282 7.65060  0.31490  1.000 15.45590  ? 90  PRO B HG3  1 
ATOM   4313 H HD2  . PRO B 1 93  ? -13.74847 9.76390  1.90137  1.000 13.76067  ? 90  PRO B HD2  1 
ATOM   4314 H HD3  . PRO B 1 93  ? -15.16667 9.05047  1.97305  1.000 13.76067  ? 90  PRO B HD3  1 
ATOM   4315 N N    . PHE B 1 94  ? -11.01192 5.61523  3.14541  1.000 11.30646  ? 91  PHE B N    1 
ATOM   4316 C CA   . PHE B 1 94  ? -9.72642  5.38658  3.79587  1.000 10.12041  ? 91  PHE B CA   1 
ATOM   4317 C C    . PHE B 1 94  ? -8.60694  6.23514  3.20283  1.000 10.58987  ? 91  PHE B C    1 
ATOM   4318 O O    . PHE B 1 94  ? -7.75682  6.75438  3.93521  1.000 11.64333  ? 91  PHE B O    1 
ATOM   4319 C CB   . PHE B 1 94  ? -9.34351  3.90926  3.67365  1.000 11.02426  ? 91  PHE B CB   1 
ATOM   4320 C CG   . PHE B 1 94  ? -7.96147  3.60626  4.16942  1.000 12.64023  ? 91  PHE B CG   1 
ATOM   4321 C CD1  . PHE B 1 94  ? -7.72609  3.42259  5.52034  1.000 12.24813  ? 91  PHE B CD1  1 
ATOM   4322 C CD2  . PHE B 1 94  ? -6.89473  3.52005  3.29133  1.000 12.34585  ? 91  PHE B CD2  1 
ATOM   4323 C CE1  . PHE B 1 94  ? -6.45120  3.15056  5.98785  1.000 12.43142  ? 91  PHE B CE1  1 
ATOM   4324 C CE2  . PHE B 1 94  ? -5.62099  3.24791  3.75380  1.000 12.93823  ? 91  PHE B CE2  1 
ATOM   4325 C CZ   . PHE B 1 94  ? -5.39945  3.06439  5.10205  1.000 13.80171  ? 91  PHE B CZ   1 
ATOM   4326 H H    . PHE B 1 94  ? -11.40655 4.89624  2.88671  1.000 13.56775  ? 91  PHE B H    1 
ATOM   4327 H HA   . PHE B 1 94  ? -9.82472  5.62792  4.73021  1.000 12.14449  ? 91  PHE B HA   1 
ATOM   4328 H HB2  . PHE B 1 94  ? -9.96832  3.38014  4.19379  1.000 13.22912  ? 91  PHE B HB2  1 
ATOM   4329 H HB3  . PHE B 1 94  ? -9.38730  3.65103  2.73967  1.000 13.22912  ? 91  PHE B HB3  1 
ATOM   4330 H HD1  . PHE B 1 94  ? -8.43276  3.48255  6.12194  1.000 14.69775  ? 91  PHE B HD1  1 
ATOM   4331 H HD2  . PHE B 1 94  ? -7.03659  3.64654  2.38096  1.000 14.81502  ? 91  PHE B HD2  1 
ATOM   4332 H HE1  . PHE B 1 94  ? -6.30529  3.02629  6.89789  1.000 14.91770  ? 91  PHE B HE1  1 
ATOM   4333 H HE2  . PHE B 1 94  ? -4.91230  3.18851  3.15453  1.000 15.52588  ? 91  PHE B HE2  1 
ATOM   4334 H HZ   . PHE B 1 94  ? -4.54197  2.88284  5.41296  1.000 16.56205  ? 91  PHE B HZ   1 
ATOM   4335 N N    . SER B 1 95  ? -8.57290  6.37250  1.88227  1.000 12.66908  ? 92  SER B N    1 
ATOM   4336 C CA   A SER B 1 95  ? -7.44774  7.02675  1.22711  0.617 13.53361  ? 92  SER B CA   1 
ATOM   4337 C CA   B SER B 1 95  ? -7.45821  7.02904  1.21280  0.383 13.85361  ? 92  SER B CA   1 
ATOM   4338 C C    . SER B 1 95  ? -7.48796  8.54923  1.31897  1.000 13.10264  ? 92  SER B C    1 
ATOM   4339 O O    . SER B 1 95  ? -6.53621  9.19967  0.87291  1.000 14.04780  ? 92  SER B O    1 
ATOM   4340 C CB   A SER B 1 95  ? -7.37949  6.60360  -0.24326 0.617 17.04361  ? 92  SER B CB   1 
ATOM   4341 C CB   B SER B 1 95  ? -7.43627  6.62484  -0.26499 0.383 17.12361  ? 92  SER B CB   1 
ATOM   4342 O OG   A SER B 1 95  ? -8.49445  7.09888  -0.96024 0.617 19.98361  ? 92  SER B OG   1 
ATOM   4343 O OG   B SER B 1 95  ? -7.17723  5.23969  -0.40610 0.383 19.92361  ? 92  SER B OG   1 
ATOM   4344 H H    A SER B 1 95  ? -9.18647  6.09644  1.34662  0.617 15.20289  ? 92  SER B H    1 
ATOM   4345 H H    B SER B 1 95  ? -9.18670  6.09236  1.34900  0.383 15.20289  ? 92  SER B H    1 
ATOM   4346 H HA   A SER B 1 95  ? -6.63343  6.73323  1.66488  0.617 16.24033  ? 92  SER B HA   1 
ATOM   4347 H HA   B SER B 1 95  ? -6.63494  6.72914  1.62896  0.383 16.62433  ? 92  SER B HA   1 
ATOM   4348 H HB2  A SER B 1 95  ? -6.56732  6.95891  -0.63702 0.617 20.45233  ? 92  SER B HB2  1 
ATOM   4349 H HB2  B SER B 1 95  ? -8.29894  6.82636  -0.66008 0.383 20.54833  ? 92  SER B HB2  1 
ATOM   4350 H HB3  A SER B 1 95  ? -7.37633  5.63491  -0.29355 0.617 20.45233  ? 92  SER B HB3  1 
ATOM   4351 H HB3  B SER B 1 95  ? -6.73900  7.12402  -0.71834 0.383 20.54833  ? 92  SER B HB3  1 
ATOM   4352 H HG   A SER B 1 95  ? -9.20682  6.83523  -0.60161 0.617 23.98033  ? 92  SER B HG   1 
ATOM   4353 H HG   B SER B 1 95  ? -7.71805  4.79731  0.06018  0.383 23.90833  ? 92  SER B HG   1 
ATOM   4354 N N    . SER B 1 96  ? -8.53750  9.13445  1.89454  1.000 11.79330  ? 93  SER B N    1 
ATOM   4355 C CA   A SER B 1 96  ? -8.68220  10.59158 1.94383  0.469 11.30361  ? 93  SER B CA   1 
ATOM   4356 C CA   B SER B 1 96  ? -8.68275  10.59061 1.94358  0.531 12.74361  ? 93  SER B CA   1 
ATOM   4357 C C    . SER B 1 96  ? -7.94979  11.16466 3.15982  1.000 10.78741  ? 93  SER B C    1 
ATOM   4358 O O    . SER B 1 96  ? -8.53695  11.77785 4.05330  1.000 9.47152   ? 93  SER B O    1 
ATOM   4359 C CB   A SER B 1 96  ? -10.15827 10.97449 1.96397  0.469 13.00361  ? 93  SER B CB   1 
ATOM   4360 C CB   B SER B 1 96  ? -10.16204 10.95909 1.95204  0.531 17.70361  ? 93  SER B CB   1 
ATOM   4361 O OG   A SER B 1 96  ? -10.86595 10.36549 0.90074  0.469 16.51361  ? 93  SER B OG   1 
ATOM   4362 O OG   B SER B 1 96  ? -10.37500 12.24320 1.39893  0.531 21.21361  ? 93  SER B OG   1 
ATOM   4363 H H    A SER B 1 96  ? -9.18463  8.70741  2.26664  0.469 14.15196  ? 93  SER B H    1 
ATOM   4364 H H    B SER B 1 96  ? -9.18444  8.70733  2.26687  0.531 14.15196  ? 93  SER B H    1 
ATOM   4365 H HA   A SER B 1 96  ? -8.28074  10.96653 1.14436  0.469 13.56433  ? 93  SER B HA   1 
ATOM   4366 H HA   B SER B 1 96  ? -8.27841  10.97559 1.15035  0.531 15.29233  ? 93  SER B HA   1 
ATOM   4367 H HB2  A SER B 1 96  ? -10.54563 10.68459 2.80469  0.469 15.60433  ? 93  SER B HB2  1 
ATOM   4368 H HB2  B SER B 1 96  ? -10.65116 10.30621 1.42724  0.531 21.24433  ? 93  SER B HB2  1 
ATOM   4369 H HB3  A SER B 1 96  ? -10.23316 11.93784 1.87887  0.469 15.60433  ? 93  SER B HB3  1 
ATOM   4370 H HB3  B SER B 1 96  ? -10.48133 10.95494 2.86797  0.531 21.24433  ? 93  SER B HB3  1 
ATOM   4371 H HG   A SER B 1 96  ? -11.68631 10.33936 1.07940  0.469 19.81633  ? 93  SER B HG   1 
ATOM   4372 H HG   B SER B 1 96  ? -11.19774 12.40970 1.36762  0.531 25.45633  ? 93  SER B HG   1 
ATOM   4373 N N    . ARG B 1 97  ? -6.62717  10.96675 3.16987  1.000 10.92163  ? 94  ARG B N    1 
ATOM   4374 C CA   . ARG B 1 97  ? -5.84457  11.25871 4.37016  1.000 10.98909  ? 94  ARG B CA   1 
ATOM   4375 C C    . ARG B 1 97  ? -5.88204  12.73868 4.74597  1.000 9.93648   ? 94  ARG B C    1 
ATOM   4376 O O    . ARG B 1 97  ? -6.01374  13.07741 5.92793  1.000 10.69650  ? 94  ARG B O    1 
ATOM   4377 C CB   . ARG B 1 97  ? -4.40529  10.76408 4.20588  1.000 12.90536  ? 94  ARG B CB   1 
ATOM   4378 C CG   . ARG B 1 97  ? -4.27272  9.30507  3.73771  1.000 12.81198  ? 94  ARG B CG   1 
ATOM   4379 C CD   . ARG B 1 97  ? -5.15590  8.30940  4.51112  1.000 14.72115  ? 94  ARG B CD   1 
ATOM   4380 N NE   . ARG B 1 97  ? -4.79325  8.20588  5.92014  1.000 16.80442  ? 94  ARG B NE   1 
ATOM   4381 C CZ   . ARG B 1 97  ? -5.36279  7.38687  6.79621  1.000 14.14800  ? 94  ARG B CZ   1 
ATOM   4382 N NH1  . ARG B 1 97  ? -6.36169  6.58684  6.45624  1.000 13.93469  ? 94  ARG B NH1  1 
ATOM   4383 N NH2  . ARG B 1 97  ? -4.91833  7.37213  8.04908  1.000 17.24124  ? 94  ARG B NH2  1 
ATOM   4384 H H    . ARG B 1 97  ? -6.16824  10.66952 2.50606  1.000 13.10595  ? 94  ARG B H    1 
ATOM   4385 H HA   . ARG B 1 97  ? -6.24075  10.77135 5.10937  1.000 13.18690  ? 94  ARG B HA   1 
ATOM   4386 H HB2  . ARG B 1 97  ? -3.96128  11.32254 3.54872  1.000 15.48644  ? 94  ARG B HB2  1 
ATOM   4387 H HB3  . ARG B 1 97  ? -3.95525  10.83749 5.06202  1.000 15.48644  ? 94  ARG B HB3  1 
ATOM   4388 H HG2  . ARG B 1 97  ? -4.52457  9.25488  2.80232  1.000 15.37437  ? 94  ARG B HG2  1 
ATOM   4389 H HG3  . ARG B 1 97  ? -3.35038  9.02590  3.84839  1.000 15.37437  ? 94  ARG B HG3  1 
ATOM   4390 H HD2  . ARG B 1 97  ? -6.07961  8.60111  4.46049  1.000 17.66538  ? 94  ARG B HD2  1 
ATOM   4391 H HD3  . ARG B 1 97  ? -5.06347  7.42976  4.11289  1.000 17.66538  ? 94  ARG B HD3  1 
ATOM   4392 H HE   . ARG B 1 97  ? -4.16151  8.71485  6.20554  1.000 20.16530  ? 94  ARG B HE   1 
ATOM   4393 H HH11 . ARG B 1 97  ? -6.65845  6.58867  5.64906  1.000 16.72163  ? 94  ARG B HH11 1 
ATOM   4394 H HH12 . ARG B 1 97  ? -6.71368  6.06543  7.04261  1.000 16.72163  ? 94  ARG B HH12 1 
ATOM   4395 H HH21 . ARG B 1 97  ? -4.27098  7.88825  8.28178  1.000 20.68948  ? 94  ARG B HH21 1 
ATOM   4396 H HH22 . ARG B 1 97  ? -5.27818  6.84648  8.62683  1.000 20.68948  ? 94  ARG B HH22 1 
ATOM   4397 N N    . ALA B 1 98  ? -5.77069  13.63709 3.76517  1.000 10.62831  ? 95  ALA B N    1 
ATOM   4398 C CA   . ALA B 1 98  ? -5.76213  15.06171 4.08889  1.000 10.54475  ? 95  ALA B CA   1 
ATOM   4399 C C    . ALA B 1 98  ? -7.11052  15.51402 4.63708  1.000 9.09731   ? 95  ALA B C    1 
ATOM   4400 O O    . ALA B 1 98  ? -7.16871  16.36390 5.53379  1.000 11.03340  ? 95  ALA B O    1 
ATOM   4401 C CB   . ALA B 1 98  ? -5.38286  15.88435 2.85819  1.000 12.01505  ? 95  ALA B CB   1 
ATOM   4402 H H    . ALA B 1 98  ? -5.70071  13.45251 2.92813  1.000 12.75397  ? 95  ALA B H    1 
ATOM   4403 H HA   . ALA B 1 98  ? -5.09052  15.21784 4.77114  1.000 12.65370  ? 95  ALA B HA   1 
ATOM   4404 H HB1  . ALA B 1 98  ? -5.35361  16.82267 3.10229  1.000 14.41807  ? 95  ALA B HB1  1 
ATOM   4405 H HB2  . ALA B 1 98  ? -4.51167  15.59732 2.54269  1.000 14.41807  ? 95  ALA B HB2  1 
ATOM   4406 H HB3  . ALA B 1 98  ? -6.04816  15.74306 2.16659  1.000 14.41807  ? 95  ALA B HB3  1 
ATOM   4407 N N    . GLU B 1 99  ? -8.20510  14.97330 4.09416  1.000 10.04636  ? 96  GLU B N    1 
ATOM   4408 C CA   . GLU B 1 99  ? -9.53473  15.33779 4.57372  1.000 10.23953  ? 96  GLU B CA   1 
ATOM   4409 C C    . GLU B 1 99  ? -9.72582  14.88723 6.01294  1.000 8.50875   ? 96  GLU B C    1 
ATOM   4410 O O    . GLU B 1 99  ? -10.28632 15.62247 6.83446  1.000 9.22570   ? 96  GLU B O    1 
ATOM   4411 C CB   . GLU B 1 99  ? -10.59023 14.70445 3.66670  1.000 13.40288  ? 96  GLU B CB   1 
ATOM   4412 C CG   . GLU B 1 99  ? -12.03242 14.94023 4.08062  1.000 20.61748  ? 96  GLU B CG   1 
ATOM   4413 C CD   . GLU B 1 99  ? -13.01658 14.20817 3.17953  1.000 25.88551  ? 96  GLU B CD   1 
ATOM   4414 O OE1  . GLU B 1 99  ? -12.58101 13.33751 2.39535  1.000 27.08632  ? 96  GLU B OE1  1 
ATOM   4415 O OE2  . GLU B 1 99  ? -14.22631 14.50363 3.25186  1.000 28.46957  ? 96  GLU B OE2  1 
ATOM   4416 H H    . GLU B 1 99  ? -8.20322  14.39923 3.45382  1.000 12.05563  ? 96  GLU B H    1 
ATOM   4417 H HA   . GLU B 1 99  ? -9.64271  16.30119 4.54060  1.000 12.28744  ? 96  GLU B HA   1 
ATOM   4418 H HB2  . GLU B 1 99  ? -10.48288 15.06755 2.77365  1.000 16.08345  ? 96  GLU B HB2  1 
ATOM   4419 H HB3  . GLU B 1 99  ? -10.44628 13.74527 3.65436  1.000 16.08345  ? 96  GLU B HB3  1 
ATOM   4420 H HG2  . GLU B 1 99  ? -12.15911 14.62192 4.98811  1.000 24.74097  ? 96  GLU B HG2  1 
ATOM   4421 H HG3  . GLU B 1 99  ? -12.22636 15.88939 4.03185  1.000 24.74097  ? 96  GLU B HG3  1 
ATOM   4422 N N    . LEU B 1 100 ? -9.25189  13.68370 6.33674  1.000 9.16677   ? 97  LEU B N    1 
ATOM   4423 C CA   . LEU B 1 100 ? -9.33144  13.19623 7.70775  1.000 9.34501   ? 97  LEU B CA   1 
ATOM   4424 C C    . LEU B 1 100 ? -8.57940  14.12000 8.65846  1.000 9.68118   ? 97  LEU B C    1 
ATOM   4425 O O    . LEU B 1 100 ? -9.07873  14.46623 9.73490  1.000 9.96954   ? 97  LEU B O    1 
ATOM   4426 C CB   . LEU B 1 100 ? -8.76293  11.77813 7.77846  1.000 9.32616   ? 97  LEU B CB   1 
ATOM   4427 C CG   . LEU B 1 100 ? -9.50193  10.69885 6.98639  1.000 9.97102   ? 97  LEU B CG   1 
ATOM   4428 C CD1  . LEU B 1 100 ? -8.62517  9.46247  6.83021  1.000 10.92564  ? 97  LEU B CD1  1 
ATOM   4429 C CD2  . LEU B 1 100 ? -10.82359 10.31442 7.64503  1.000 11.78103  ? 97  LEU B CD2  1 
ATOM   4430 H H    . LEU B 1 100 ? -8.88336  13.13644 5.78512  1.000 11.00013  ? 97  LEU B H    1 
ATOM   4431 H HA   . LEU B 1 100 ? -10.26097 13.17041 7.98380  1.000 11.21401  ? 97  LEU B HA   1 
ATOM   4432 H HB2  . LEU B 1 100 ? -7.85313  11.80338 7.44301  1.000 11.19139  ? 97  LEU B HB2  1 
ATOM   4433 H HB3  . LEU B 1 100 ? -8.76626  11.50038 8.70784  1.000 11.19139  ? 97  LEU B HB3  1 
ATOM   4434 H HG   . LEU B 1 100 ? -9.70515  11.05944 6.10913  1.000 11.96522  ? 97  LEU B HG   1 
ATOM   4435 H HD11 . LEU B 1 100 ? -9.12423  8.77930  6.35574  1.000 13.11077  ? 97  LEU B HD11 1 
ATOM   4436 H HD12 . LEU B 1 100 ? -7.83029  9.70042  6.32776  1.000 13.11077  ? 97  LEU B HD12 1 
ATOM   4437 H HD13 . LEU B 1 100 ? -8.37584  9.13895  7.71002  1.000 13.11077  ? 97  LEU B HD13 1 
ATOM   4438 H HD21 . LEU B 1 100 ? -11.24341 9.61198  7.12423  1.000 14.13724  ? 97  LEU B HD21 1 
ATOM   4439 H HD22 . LEU B 1 100 ? -10.64777 9.99871  8.54520  1.000 14.13724  ? 97  LEU B HD22 1 
ATOM   4440 H HD23 . LEU B 1 100 ? -11.40019 11.09388 7.67458  1.000 14.13724  ? 97  LEU B HD23 1 
ATOM   4441 N N    . GLU B 1 101 ? -7.36869  14.52838 8.27612  1.000 9.23445   ? 98  GLU B N    1 
ATOM   4442 C CA   . GLU B 1 101 ? -6.57602  15.39760 9.13934  1.000 10.58916  ? 98  GLU B CA   1 
ATOM   4443 C C    . GLU B 1 101 ? -7.18558  16.78716 9.25262  1.000 9.77479   ? 98  GLU B C    1 
ATOM   4444 O O    . GLU B 1 101 ? -7.10782  17.40956 10.31805 1.000 9.50464   ? 98  GLU B O    1 
ATOM   4445 C CB   . GLU B 1 101 ? -5.13593  15.44922 8.62966  1.000 13.64801  ? 98  GLU B CB   1 
ATOM   4446 C CG   . GLU B 1 101 ? -4.44943  14.09641 8.73240  1.000 16.25126  ? 98  GLU B CG   1 
ATOM   4447 C CD   . GLU B 1 101 ? -2.95945  14.15249 8.50630  1.000 19.30216  ? 98  GLU B CD   1 
ATOM   4448 O OE1  . GLU B 1 101 ? -2.48122  15.11436 7.87277  1.000 20.97218  ? 98  GLU B OE1  1 
ATOM   4449 O OE2  . GLU B 1 101 ? -2.26629  13.21791 8.95880  1.000 21.80450  ? 98  GLU B OE2  1 
ATOM   4450 H H    . GLU B 1 101 ? -6.98993  14.31910 7.53292  1.000 11.08134  ? 98  GLU B H    1 
ATOM   4451 H HA   . GLU B 1 101 ? -6.55233  15.03007 10.03670 1.000 12.70699  ? 98  GLU B HA   1 
ATOM   4452 H HB2  . GLU B 1 101 ? -5.13672  15.71982 7.69817  1.000 16.37761  ? 98  GLU B HB2  1 
ATOM   4453 H HB3  . GLU B 1 101 ? -4.63254  16.08668 9.15990  1.000 16.37761  ? 98  GLU B HB3  1 
ATOM   4454 H HG2  . GLU B 1 101 ? -4.60041  13.73628 9.62032  1.000 19.50151  ? 98  GLU B HG2  1 
ATOM   4455 H HG3  . GLU B 1 101 ? -4.82765  13.50284 8.06491  1.000 19.50151  ? 98  GLU B HG3  1 
ATOM   4456 N N    . ALA B 1 102 ? -7.81064  17.28268 8.18470  1.000 9.85349   ? 99  ALA B N    1 
ATOM   4457 C CA   . ALA B 1 102 ? -8.43391  18.59839 8.25374  1.000 9.57496   ? 99  ALA B CA   1 
ATOM   4458 C C    . ALA B 1 102 ? -9.56228  18.60985 9.27191  1.000 8.91493   ? 99  ALA B C    1 
ATOM   4459 O O    . ALA B 1 102 ? -9.73491  19.58909 10.00539 1.000 9.94449   ? 99  ALA B O    1 
ATOM   4460 C CB   . ALA B 1 102 ? -8.95076  19.01037 6.87783  1.000 10.93915  ? 99  ALA B CB   1 
ATOM   4461 H H    . ALA B 1 102 ? -7.88562  16.88508 7.42582  1.000 11.82419  ? 99  ALA B H    1 
ATOM   4462 H HA   . ALA B 1 102 ? -7.76778  19.24807 8.52776  1.000 11.48995  ? 99  ALA B HA   1 
ATOM   4463 H HB1  . ALA B 1 102 ? -9.40281  19.86527 6.95326  1.000 13.12698  ? 99  ALA B HB1  1 
ATOM   4464 H HB2  . ALA B 1 102 ? -8.20013  19.08577 6.26809  1.000 13.12698  ? 99  ALA B HB2  1 
ATOM   4465 H HB3  . ALA B 1 102 ? -9.57012  18.33576 6.55815  1.000 13.12698  ? 99  ALA B HB3  1 
ATOM   4466 N N    . LEU B 1 103 ? -10.33959 17.52637 9.33594  1.000 8.32135   ? 100 LEU B N    1 
ATOM   4467 C CA   . LEU B 1 103 ? -11.41687 17.44820 10.31584 1.000 8.64261   ? 100 LEU B CA   1 
ATOM   4468 C C    . LEU B 1 103 ? -10.87127 17.43038 11.73796 1.000 7.68272   ? 100 LEU B C    1 
ATOM   4469 O O    . LEU B 1 103 ? -11.44860 18.05489 12.63581 1.000 8.61248   ? 100 LEU B O    1 
ATOM   4470 C CB   . LEU B 1 103 ? -12.26795 16.20904 10.05124 1.000 8.24087   ? 100 LEU B CB   1 
ATOM   4471 C CG   . LEU B 1 103 ? -13.10351 16.28685 8.77245  1.000 10.46972  ? 100 LEU B CG   1 
ATOM   4472 C CD1  . LEU B 1 103 ? -13.67121 14.92914 8.40444  1.000 12.93107  ? 100 LEU B CD1  1 
ATOM   4473 C CD2  . LEU B 1 103 ? -14.22332 17.31822 8.90632  1.000 13.04760  ? 100 LEU B CD2  1 
ATOM   4474 H H    . LEU B 1 103 ? -10.26369 16.83476 8.83045  1.000 9.98562   ? 100 LEU B H    1 
ATOM   4475 H HA   . LEU B 1 103 ? -11.98334 18.23021 10.22379 1.000 10.37113  ? 100 LEU B HA   1 
ATOM   4476 H HB2  . LEU B 1 103 ? -11.68096 15.44066 9.97423  1.000 9.88904   ? 100 LEU B HB2  1 
ATOM   4477 H HB3  . LEU B 1 103 ? -12.87786 16.08732 10.79562 1.000 9.88904   ? 100 LEU B HB3  1 
ATOM   4478 H HG   . LEU B 1 103 ? -12.52198 16.57132 8.05009  1.000 12.56367  ? 100 LEU B HG   1 
ATOM   4479 H HD11 . LEU B 1 103 ? -14.14771 15.00366 7.56283  1.000 15.51728  ? 100 LEU B HD11 1 
ATOM   4480 H HD12 . LEU B 1 103 ? -12.94224 14.29524 8.31683  1.000 15.51728  ? 100 LEU B HD12 1 
ATOM   4481 H HD13 . LEU B 1 103 ? -14.27825 14.64056 9.10381  1.000 15.51728  ? 100 LEU B HD13 1 
ATOM   4482 H HD21 . LEU B 1 103 ? -14.85886 17.18977 8.18488  1.000 15.65713  ? 100 LEU B HD21 1 
ATOM   4483 H HD22 . LEU B 1 103 ? -14.66454 17.19611 9.76149  1.000 15.65713  ? 100 LEU B HD22 1 
ATOM   4484 H HD23 . LEU B 1 103 ? -13.84074 18.20814 8.85559  1.000 15.65713  ? 100 LEU B HD23 1 
ATOM   4485 N N    . ARG B 1 104 ? -9.76143  16.72058 11.96079 1.000 8.26796   ? 101 ARG B N    1 
ATOM   4486 C CA   . ARG B 1 104 ? -9.13817  16.71149 13.28125 1.000 9.66675   ? 101 ARG B CA   1 
ATOM   4487 C C    . ARG B 1 104 ? -8.75291  18.12263 13.71020 1.000 7.55400   ? 101 ARG B C    1 
ATOM   4488 O O    . ARG B 1 104 ? -9.02624  18.53509 14.84311 1.000 9.24497   ? 101 ARG B O    1 
ATOM   4489 C CB   . ARG B 1 104 ? -7.91866  15.78783 13.27751 1.000 9.14431   ? 101 ARG B CB   1 
ATOM   4490 C CG   . ARG B 1 104 ? -7.11721  15.81247 14.56572 1.000 9.98456   ? 101 ARG B CG   1 
ATOM   4491 C CD   . ARG B 1 104 ? -5.93988  14.86282 14.50227 1.000 10.06458  ? 101 ARG B CD   1 
ATOM   4492 N NE   . ARG B 1 104 ? -4.94288  15.34314 13.55633 1.000 10.04466  ? 101 ARG B NE   1 
ATOM   4493 C CZ   . ARG B 1 104 ? -3.85502  14.67290 13.20862 1.000 11.49749  ? 101 ARG B CZ   1 
ATOM   4494 N NH1  . ARG B 1 104 ? -3.57608  13.49233 13.73626 1.000 12.50256  ? 101 ARG B NH1  1 
ATOM   4495 N NH2  . ARG B 1 104 ? -3.03628  15.19335 12.29951 1.000 11.40612  ? 101 ARG B NH2  1 
ATOM   4496 H H    . ARG B 1 104 ? -9.35649  16.24300 11.37127 1.000 9.92155   ? 101 ARG B H    1 
ATOM   4497 H HA   . ARG B 1 104 ? -9.77182  16.36411 13.92833 1.000 11.60010  ? 101 ARG B HA   1 
ATOM   4498 H HB2  . ARG B 1 104 ? -8.21991  14.87680 13.13553 1.000 10.97317  ? 101 ARG B HB2  1 
ATOM   4499 H HB3  . ARG B 1 104 ? -7.32726  16.05771 12.55758 1.000 10.97317  ? 101 ARG B HB3  1 
ATOM   4500 H HG2  . ARG B 1 104 ? -6.77858  16.70881 14.71679 1.000 11.98147  ? 101 ARG B HG2  1 
ATOM   4501 H HG3  . ARG B 1 104 ? -7.68643  15.54409 15.30387 1.000 11.98147  ? 101 ARG B HG3  1 
ATOM   4502 H HD2  . ARG B 1 104 ? -5.52815  14.79776 15.37813 1.000 12.07750  ? 101 ARG B HD2  1 
ATOM   4503 H HD3  . ARG B 1 104 ? -6.24385  13.98834 14.21279 1.000 12.07750  ? 101 ARG B HD3  1 
ATOM   4504 H HE   . ARG B 1 104 ? -5.06909  16.11508 13.19885 1.000 12.05359  ? 101 ARG B HE   1 
ATOM   4505 H HH11 . ARG B 1 104 ? -4.10617  13.14513 14.31769 1.000 15.00307  ? 101 ARG B HH11 1 
ATOM   4506 H HH12 . ARG B 1 104 ? -2.86466  13.07204 13.49786 1.000 15.00307  ? 101 ARG B HH12 1 
ATOM   4507 H HH21 . ARG B 1 104 ? -3.21620  15.95606 11.94525 1.000 13.68734  ? 101 ARG B HH21 1 
ATOM   4508 H HH22 . ARG B 1 104 ? -2.32676  14.76729 12.06573 1.000 13.68734  ? 101 ARG B HH22 1 
ATOM   4509 N N    . SER B 1 105 ? -8.12680  18.88414 12.80820 1.000 8.50463   ? 102 SER B N    1 
ATOM   4510 C CA   . SER B 1 105 ? -7.74766  20.25791 13.12547 1.000 11.06658  ? 102 SER B CA   1 
ATOM   4511 C C    . SER B 1 105 ? -8.97040  21.15223 13.29425 1.000 9.63829   ? 102 SER B C    1 
ATOM   4512 O O    . SER B 1 105 ? -9.03813  21.94671 14.23905 1.000 10.43067  ? 102 SER B O    1 
ATOM   4513 C CB   . SER B 1 105 ? -6.83441  20.80698 12.02850 1.000 12.22007  ? 102 SER B CB   1 
ATOM   4514 O OG   . SER B 1 105 ? -5.53719  20.24937 12.12930 1.000 12.33736  ? 102 SER B OG   1 
ATOM   4515 H H    . SER B 1 105 ? -7.91323  18.63044 12.01471 1.000 10.20556  ? 102 SER B H    1 
ATOM   4516 H HA   . SER B 1 105 ? -7.25958  20.26059 13.96372 1.000 13.27990  ? 102 SER B HA   1 
ATOM   4517 H HB2  . SER B 1 105 ? -7.20915  20.58099 11.16282 1.000 14.66408  ? 102 SER B HB2  1 
ATOM   4518 H HB3  . SER B 1 105 ? -6.77237  21.77049 12.12185 1.000 14.66408  ? 102 SER B HB3  1 
ATOM   4519 H HG   . SER B 1 105 ? -5.09829  20.41512 11.43253 1.000 14.80483  ? 102 SER B HG   1 
ATOM   4520 N N    . THR B 1 106 ? -9.95257  21.02563 12.40062 1.000 9.25123   ? 103 THR B N    1 
ATOM   4521 C CA   . THR B 1 106 ? -11.10895 21.91552 12.43195 1.000 9.77902   ? 103 THR B CA   1 
ATOM   4522 C C    . THR B 1 106 ? -11.85854 21.80950 13.75041 1.000 9.70466   ? 103 THR B C    1 
ATOM   4523 O O    . THR B 1 106 ? -12.26633 22.82056 14.33284 1.000 10.95892  ? 103 THR B O    1 
ATOM   4524 C CB   . THR B 1 106 ? -12.04005 21.57729 11.26828 1.000 12.31868  ? 103 THR B CB   1 
ATOM   4525 O OG1  . THR B 1 106 ? -11.42592 21.98443 10.04117 1.000 13.32309  ? 103 THR B OG1  1 
ATOM   4526 C CG2  . THR B 1 106 ? -13.38212 22.27622 11.42470 1.000 14.62020  ? 103 THR B CG2  1 
ATOM   4527 H H    . THR B 1 106 ? -9.97236  20.43827 11.77275 1.000 11.10148  ? 103 THR B H    1 
ATOM   4528 H HA   . THR B 1 106 ? -10.80143 22.83048 12.33618 1.000 11.73483  ? 103 THR B HA   1 
ATOM   4529 H HB   . THR B 1 106 ? -12.20422 20.62145 11.25048 1.000 14.78242  ? 103 THR B HB   1 
ATOM   4530 H HG1  . THR B 1 106 ? -10.69463 21.58392 9.93916  1.000 15.98770  ? 103 THR B HG1  1 
ATOM   4531 H HG21 . THR B 1 106 ? -13.85432 22.28120 10.57741 1.000 17.54424  ? 103 THR B HG21 1 
ATOM   4532 H HG22 . THR B 1 106 ? -13.92263 21.81296 12.08359 1.000 17.54424  ? 103 THR B HG22 1 
ATOM   4533 H HG23 . THR B 1 106 ? -13.24748 23.19177 11.71543 1.000 17.54424  ? 103 THR B HG23 1 
ATOM   4534 N N    . PHE B 1 107 ? -12.08111 20.59279 14.22294 1.000 8.81932   ? 104 PHE B N    1 
ATOM   4535 C CA   . PHE B 1 107 ? -12.81648 20.37399 15.45550 1.000 9.04750   ? 104 PHE B CA   1 
ATOM   4536 C C    . PHE B 1 107 ? -11.90820 20.20958 16.66498 1.000 9.45871   ? 104 PHE B C    1 
ATOM   4537 O O    . PHE B 1 107 ? -12.40562 19.97505 17.76833 1.000 12.11471  ? 104 PHE B O    1 
ATOM   4538 C CB   . PHE B 1 107 ? -13.74671 19.17666 15.28295 1.000 9.95362   ? 104 PHE B CB   1 
ATOM   4539 C CG   . PHE B 1 107 ? -14.80317 19.38763 14.22474 1.000 9.73602   ? 104 PHE B CG   1 
ATOM   4540 C CD1  . PHE B 1 107 ? -15.75843 20.37862 14.37521 1.000 10.62088  ? 104 PHE B CD1  1 
ATOM   4541 C CD2  . PHE B 1 107 ? -14.83496 18.60939 13.07895 1.000 11.30254  ? 104 PHE B CD2  1 
ATOM   4542 C CE1  . PHE B 1 107 ? -16.72993 20.58107 13.41363 1.000 12.12847  ? 104 PHE B CE1  1 
ATOM   4543 C CE2  . PHE B 1 107 ? -15.81355 18.80546 12.11648 1.000 11.95087  ? 104 PHE B CE2  1 
ATOM   4544 C CZ   . PHE B 1 107 ? -16.75149 19.79791 12.28039 1.000 12.29755  ? 104 PHE B CZ   1 
ATOM   4545 H H    . PHE B 1 107 ? -11.81253 19.86997 13.84216 1.000 10.58318  ? 104 PHE B H    1 
ATOM   4546 H HA   . PHE B 1 107 ? -13.37734 21.14253 15.64439 1.000 10.85700  ? 104 PHE B HA   1 
ATOM   4547 H HB2  . PHE B 1 107 ? -13.21904 18.40398 15.02716 1.000 11.94435  ? 104 PHE B HB2  1 
ATOM   4548 H HB3  . PHE B 1 107 ? -14.19795 19.00638 16.12455 1.000 11.94435  ? 104 PHE B HB3  1 
ATOM   4549 H HD1  . PHE B 1 107 ? -15.74601 20.91569 15.13435 1.000 12.74506  ? 104 PHE B HD1  1 
ATOM   4550 H HD2  . PHE B 1 107 ? -14.19292 17.94827 12.95404 1.000 13.56305  ? 104 PHE B HD2  1 
ATOM   4551 H HE1  . PHE B 1 107 ? -17.36930 21.24606 13.53146 1.000 14.55416  ? 104 PHE B HE1  1 
ATOM   4552 H HE2  . PHE B 1 107 ? -15.83571 18.26554 11.35958 1.000 14.34105  ? 104 PHE B HE2  1 
ATOM   4553 H HZ   . PHE B 1 107 ? -17.39870 19.94000 11.62783 1.000 14.75706  ? 104 PHE B HZ   1 
ATOM   4554 N N    . GLY B 1 108 ? -10.59655 20.35461 16.48863 1.000 9.21860   ? 105 GLY B N    1 
ATOM   4555 C CA   . GLY B 1 108 ? -9.65567  20.25791 17.58692 1.000 10.48284  ? 105 GLY B CA   1 
ATOM   4556 C C    . GLY B 1 108 ? -9.74617  18.95151 18.34573 1.000 9.91561   ? 105 GLY B C    1 
ATOM   4557 O O    . GLY B 1 108 ? -9.76223  18.94426 19.58085 1.000 10.91087  ? 105 GLY B O    1 
ATOM   4558 H H    . GLY B 1 108 ? -10.22596 20.51196 15.72869 1.000 11.06232  ? 105 GLY B H    1 
ATOM   4559 H HA2  . GLY B 1 108 ? -8.75395  20.34257 17.23961 1.000 12.57941  ? 105 GLY B HA2  1 
ATOM   4560 H HA3  . GLY B 1 108 ? -9.82274  20.98108 18.21143 1.000 12.57941  ? 105 GLY B HA3  1 
ATOM   4561 N N    . VAL B 1 109 ? -9.79370  17.83693 17.61832 1.000 8.78853   ? 106 VAL B N    1 
ATOM   4562 C CA   . VAL B 1 109 ? -10.01975 16.52777 18.22778 1.000 8.61731   ? 106 VAL B CA   1 
ATOM   4563 C C    . VAL B 1 109 ? -8.69750  16.02275 18.79749 1.000 8.31128   ? 106 VAL B C    1 
ATOM   4564 O O    . VAL B 1 109 ? -7.83131  15.51969 18.07739 1.000 10.85550  ? 106 VAL B O    1 
ATOM   4565 C CB   . VAL B 1 109 ? -10.64395 15.53081 17.25044 1.000 8.97685   ? 106 VAL B CB   1 
ATOM   4566 C CG1  . VAL B 1 109 ? -10.84621 14.19575 17.93914 1.000 10.77677  ? 106 VAL B CG1  1 
ATOM   4567 C CG2  . VAL B 1 109 ? -11.96162 16.06294 16.73283 1.000 10.85906  ? 106 VAL B CG2  1 
ATOM   4568 H H    . VAL B 1 109 ? -9.69721  17.81297 16.76408 1.000 10.54624  ? 106 VAL B H    1 
ATOM   4569 H HA   . VAL B 1 109 ? -10.63025 16.64236 18.97281 1.000 10.34077  ? 106 VAL B HA   1 
ATOM   4570 H HB   . VAL B 1 109 ? -10.04982 15.40330 16.49437 1.000 10.77222  ? 106 VAL B HB   1 
ATOM   4571 H HG11 . VAL B 1 109 ? -11.40090 13.63169 17.37785 1.000 12.93212  ? 106 VAL B HG11 1 
ATOM   4572 H HG12 . VAL B 1 109 ? -9.98199  13.77744 18.07709 1.000 12.93212  ? 106 VAL B HG12 1 
ATOM   4573 H HG13 . VAL B 1 109 ? -11.28216 14.34369 18.79294 1.000 12.93212  ? 106 VAL B HG13 1 
ATOM   4574 H HG21 . VAL B 1 109 ? -12.44141 15.34407 16.29247 1.000 13.03088  ? 106 VAL B HG21 1 
ATOM   4575 H HG22 . VAL B 1 109 ? -12.48168 16.39899 17.47949 1.000 13.03088  ? 106 VAL B HG22 1 
ATOM   4576 H HG23 . VAL B 1 109 ? -11.78718 16.77910 16.10229 1.000 13.03088  ? 106 VAL B HG23 1 
ATOM   4577 N N    . GLU B 1 110 ? -8.56643  16.12541 20.11425 1.000 8.96622   ? 107 GLU B N    1 
ATOM   4578 C CA   . GLU B 1 110 ? -7.38033  15.70015 20.82738 1.000 9.43262   ? 107 GLU B CA   1 
ATOM   4579 C C    . GLU B 1 110 ? -7.40915  14.23539 21.22519 1.000 9.82582   ? 107 GLU B C    1 
ATOM   4580 O O    . GLU B 1 110 ? -6.36914  13.71124 21.62108 1.000 11.69259  ? 107 GLU B O    1 
ATOM   4581 C CB   . GLU B 1 110 ? -7.24778  16.51391 22.12264 1.000 13.84222  ? 107 GLU B CB   1 
ATOM   4582 C CG   . GLU B 1 110 ? -7.21221  18.01133 21.90475 1.000 17.68173  ? 107 GLU B CG   1 
ATOM   4583 C CD   . GLU B 1 110 ? -7.42708  18.81036 23.17909 1.000 21.76213  ? 107 GLU B CD   1 
ATOM   4584 O OE1  . GLU B 1 110 ? -7.50462  18.21058 24.27203 1.000 22.82303  ? 107 GLU B OE1  1 
ATOM   4585 O OE2  . GLU B 1 110 ? -7.52489  20.05002 23.08399 1.000 26.58942  ? 107 GLU B OE2  1 
ATOM   4586 H H    . GLU B 1 110 ? -9.17332  16.44948 20.63025 1.000 10.75947  ? 107 GLU B H    1 
ATOM   4587 H HA   . GLU B 1 110 ? -6.61290  15.85389 20.25439 1.000 11.31915  ? 107 GLU B HA   1 
ATOM   4588 H HB2  . GLU B 1 110 ? -8.00668  16.31622 22.69351 1.000 16.61067  ? 107 GLU B HB2  1 
ATOM   4589 H HB3  . GLU B 1 110 ? -6.42358  16.26017 22.56673 1.000 16.61067  ? 107 GLU B HB3  1 
ATOM   4590 H HG2  . GLU B 1 110 ? -6.34584  18.25538 21.54317 1.000 21.21808  ? 107 GLU B HG2  1 
ATOM   4591 H HG3  . GLU B 1 110 ? -7.91298  18.25426 21.27962 1.000 21.21808  ? 107 GLU B HG3  1 
ATOM   4592 N N    . THR B 1 111 ? -8.55552  13.56321 21.12975 1.000 8.94644   ? 108 THR B N    1 
ATOM   4593 C CA   A THR B 1 111 ? -8.74077  12.25133 21.73867 0.447 7.53361   ? 108 THR B CA   1 
ATOM   4594 C CA   B THR B 1 111 ? -8.67156  12.22177 21.67552 0.553 8.62361   ? 108 THR B CA   1 
ATOM   4595 C C    . THR B 1 111 ? -9.75537  11.45240 20.93770 1.000 6.69944   ? 108 THR B C    1 
ATOM   4596 O O    . THR B 1 111 ? -10.68443 12.02541 20.36554 1.000 9.22912   ? 108 THR B O    1 
ATOM   4597 C CB   A THR B 1 111 ? -9.28104  12.43432 23.16951 0.447 8.55361   ? 108 THR B CB   1 
ATOM   4598 C CB   B THR B 1 111 ? -8.97868  12.25517 23.18317 0.553 10.09361  ? 108 THR B CB   1 
ATOM   4599 O OG1  A THR B 1 111 ? -8.33576  13.18425 23.94354 0.447 8.99361   ? 108 THR B OG1  1 
ATOM   4600 O OG1  B THR B 1 111 ? -8.72804  10.96413 23.75589 0.553 12.75361  ? 108 THR B OG1  1 
ATOM   4601 C CG2  A THR B 1 111 ? -9.55833  11.09779 23.84241 0.447 14.66361  ? 108 THR B CG2  1 
ATOM   4602 C CG2  B THR B 1 111 ? -10.42601 12.64887 23.43207 0.553 10.69361  ? 108 THR B CG2  1 
ATOM   4603 H H    A THR B 1 111 ? -9.24954  13.85117 20.71140 0.447 10.73573  ? 108 THR B H    1 
ATOM   4604 H H    B THR B 1 111 ? -9.27008  13.86300 20.75675 0.553 10.73573  ? 108 THR B H    1 
ATOM   4605 H HA   A THR B 1 111 ? -7.90339  11.76174 21.73823 0.447 9.04033   ? 108 THR B HA   1 
ATOM   4606 H HA   B THR B 1 111 ? -7.83415  11.75210 21.53751 0.553 10.34833  ? 108 THR B HA   1 
ATOM   4607 H HB   A THR B 1 111 ? -10.12329 12.91387 23.13017 0.447 10.26433  ? 108 THR B HB   1 
ATOM   4608 H HB   B THR B 1 111 ? -8.40953  12.91371 23.61128 0.553 12.11233  ? 108 THR B HB   1 
ATOM   4609 H HG1  A THR B 1 111 ? -8.61915  13.28058 24.72840 0.447 10.79233  ? 108 THR B HG1  1 
ATOM   4610 H HG1  B THR B 1 111 ? -7.90181  10.84902 23.85438 0.553 15.30433  ? 108 THR B HG1  1 
ATOM   4611 H HG21 A THR B 1 111 ? -9.74331  11.23296 24.78497 0.447 17.59633  ? 108 THR B HG21 1 
ATOM   4612 H HG21 B THR B 1 111 ? -10.54936 12.88734 24.36417 0.553 12.83233  ? 108 THR B HG21 1 
ATOM   4613 H HG22 A THR B 1 111 ? -10.32516 10.67107 23.42916 0.447 17.59633  ? 108 THR B HG22 1 
ATOM   4614 H HG22 B THR B 1 111 ? -10.66284 13.40941 22.87855 0.553 12.83233  ? 108 THR B HG22 1 
ATOM   4615 H HG23 A THR B 1 111 ? -8.78788  10.51526 23.75319 0.447 17.59633  ? 108 THR B HG23 1 
ATOM   4616 H HG23 B THR B 1 111 ? -11.01326 11.90756 23.21642 0.553 12.83233  ? 108 THR B HG23 1 
ATOM   4617 N N    . ILE B 1 112 ? -9.59284  10.12886 20.93226 1.000 7.60906   ? 109 ILE B N    1 
ATOM   4618 C CA   . ILE B 1 112 ? -10.61550 9.21941  20.41574 1.000 7.30415   ? 109 ILE B CA   1 
ATOM   4619 C C    . ILE B 1 112 ? -10.95785 8.20794  21.50388 1.000 7.69383   ? 109 ILE B C    1 
ATOM   4620 O O    . ILE B 1 112 ? -10.10143 7.87849  22.33700 1.000 9.09847   ? 109 ILE B O    1 
ATOM   4621 C CB   . ILE B 1 112 ? -10.18433 8.49080  19.12939 1.000 7.71173   ? 109 ILE B CB   1 
ATOM   4622 C CG1  . ILE B 1 112 ? -8.85096  7.76654  19.32329 1.000 9.33908   ? 109 ILE B CG1  1 
ATOM   4623 C CG2  . ILE B 1 112 ? -10.14832 9.46152  17.96667 1.000 9.83882   ? 109 ILE B CG2  1 
ATOM   4624 C CD1  . ILE B 1 112 ? -8.50463  6.80542  18.18899 1.000 9.19455   ? 109 ILE B CD1  1 
ATOM   4625 H H    . ILE B 1 112 ? -8.89047  9.72881  21.22592 1.000 9.13087   ? 109 ILE B H    1 
ATOM   4626 H HA   . ILE B 1 112 ? -11.39801 9.75080  20.20079 1.000 8.76499   ? 109 ILE B HA   1 
ATOM   4627 H HB   . ILE B 1 112 ? -10.84194 7.80773  18.92480 1.000 9.25408   ? 109 ILE B HB   1 
ATOM   4628 H HG12 . ILE B 1 112 ? -8.14240  8.42663  19.37917 1.000 11.20689  ? 109 ILE B HG12 1 
ATOM   4629 H HG13 . ILE B 1 112 ? -8.89137  7.25283  20.14509 1.000 11.20689  ? 109 ILE B HG13 1 
ATOM   4630 H HG21 . ILE B 1 112 ? -9.84525  8.99288  17.17330 1.000 11.80659  ? 109 ILE B HG21 1 
ATOM   4631 H HG22 . ILE B 1 112 ? -11.04026 9.81425  17.82201 1.000 11.80659  ? 109 ILE B HG22 1 
ATOM   4632 H HG23 . ILE B 1 112 ? -9.53692  10.18442 18.17762 1.000 11.80659  ? 109 ILE B HG23 1 
ATOM   4633 H HD11 . ILE B 1 112 ? -7.75291  6.25535  18.45960 1.000 11.03346  ? 109 ILE B HD11 1 
ATOM   4634 H HD12 . ILE B 1 112 ? -9.27455  6.24531  18.00351 1.000 11.03346  ? 109 ILE B HD12 1 
ATOM   4635 H HD13 . ILE B 1 112 ? -8.27150  7.31912  17.39990 1.000 11.03346  ? 109 ILE B HD13 1 
ATOM   4636 N N    . PRO B 1 113 ? -12.17662 7.67120  21.52325 1.000 7.88550   ? 110 PRO B N    1 
ATOM   4637 C CA   . PRO B 1 113 ? -13.28834 7.98500  20.61738 1.000 7.25683   ? 110 PRO B CA   1 
ATOM   4638 C C    . PRO B 1 113 ? -13.92303 9.34057  20.91245 1.000 8.77011   ? 110 PRO B C    1 
ATOM   4639 O O    . PRO B 1 113 ? -14.04403 9.74720  22.06652 1.000 9.78967   ? 110 PRO B O    1 
ATOM   4640 C CB   . PRO B 1 113 ? -14.26404 6.82582  20.86498 1.000 9.80618   ? 110 PRO B CB   1 
ATOM   4641 C CG   . PRO B 1 113 ? -14.03690 6.45833  22.30364 1.000 10.06690  ? 110 PRO B CG   1 
ATOM   4642 C CD   . PRO B 1 113 ? -12.55455 6.66726  22.53706 1.000 8.42824   ? 110 PRO B CD   1 
ATOM   4643 H HA   . PRO B 1 113 ? -12.98528 7.96657  19.69613 1.000 8.70820   ? 110 PRO B HA   1 
ATOM   4644 H HB2  . PRO B 1 113 ? -15.17648 7.12044  20.71816 1.000 11.76742  ? 110 PRO B HB2  1 
ATOM   4645 H HB3  . PRO B 1 113 ? -14.05640 6.08329  20.27639 1.000 11.76742  ? 110 PRO B HB3  1 
ATOM   4646 H HG2  . PRO B 1 113 ? -14.56273 7.03618  22.87852 1.000 12.08028  ? 110 PRO B HG2  1 
ATOM   4647 H HG3  . PRO B 1 113 ? -14.28321 5.53162  22.45006 1.000 12.08028  ? 110 PRO B HG3  1 
ATOM   4648 H HD2  . PRO B 1 113 ? -12.39213 7.00489  23.43178 1.000 10.11389  ? 110 PRO B HD2  1 
ATOM   4649 H HD3  . PRO B 1 113 ? -12.06566 5.84066  22.40056 1.000 10.11389  ? 110 PRO B HD3  1 
ATOM   4650 N N    . THR B 1 114 ? -14.34257 10.04900 19.86540 1.000 9.03453   ? 111 THR B N    1 
ATOM   4651 C CA   . THR B 1 114 ? -15.06256 11.30563 19.99471 1.000 9.33141   ? 111 THR B CA   1 
ATOM   4652 C C    . THR B 1 114 ? -16.13450 11.36554 18.91973 1.000 9.44977   ? 111 THR B C    1 
ATOM   4653 O O    . THR B 1 114 ? -15.90598 10.93686 17.78454 1.000 8.76759   ? 111 THR B O    1 
ATOM   4654 C CB   . THR B 1 114 ? -14.10738 12.49948 19.80874 1.000 9.99136   ? 111 THR B CB   1 
ATOM   4655 O OG1  . THR B 1 114 ? -13.21521 12.58235 20.92757 1.000 12.11239  ? 111 THR B OG1  1 
ATOM   4656 C CG2  . THR B 1 114 ? -14.86633 13.81638 19.66371 1.000 10.76263  ? 111 THR B CG2  1 
ATOM   4657 H H    . THR B 1 114 ? -14.21676 9.81255  19.04817 1.000 10.84143  ? 111 THR B H    1 
ATOM   4658 H HA   . THR B 1 114 ? -15.48153 11.36140 20.86778 1.000 11.19770  ? 111 THR B HA   1 
ATOM   4659 H HB   . THR B 1 114 ? -13.59954 12.36566 18.99321 1.000 11.98963  ? 111 THR B HB   1 
ATOM   4660 H HG1  . THR B 1 114 ? -12.75786 11.87996 20.98297 1.000 14.53487  ? 111 THR B HG1  1 
ATOM   4661 H HG21 . THR B 1 114 ? -14.24046 14.55468 19.59972 1.000 12.91515  ? 111 THR B HG21 1 
ATOM   4662 H HG22 . THR B 1 114 ? -15.41369 13.79741 18.86312 1.000 12.91515  ? 111 THR B HG22 1 
ATOM   4663 H HG23 . THR B 1 114 ? -15.43956 13.95547 20.43374 1.000 12.91515  ? 111 THR B HG23 1 
ATOM   4664 N N    . VAL B 1 115 ? -17.29761 11.90908 19.27352 1.000 7.85438   ? 112 VAL B N    1 
ATOM   4665 C CA   A VAL B 1 115 ? -18.33234 12.23197 18.29733 0.648 8.90781   ? 112 VAL B CA   1 
ATOM   4666 C CA   B VAL B 1 115 ? -18.34132 12.22963 18.30758 0.352 8.90781   ? 112 VAL B CA   1 
ATOM   4667 C C    . VAL B 1 115 ? -18.58808 13.73209 18.34980 1.000 8.71335   ? 112 VAL B C    1 
ATOM   4668 O O    . VAL B 1 115 ? -18.88628 14.28699 19.41656 1.000 9.55969   ? 112 VAL B O    1 
ATOM   4669 C CB   A VAL B 1 115 ? -19.62627 11.41226 18.47896 0.648 12.17662  ? 112 VAL B CB   1 
ATOM   4670 C CB   B VAL B 1 115 ? -19.64041 11.45705 18.60482 0.352 12.17662  ? 112 VAL B CB   1 
ATOM   4671 C CG1  A VAL B 1 115 ? -19.38861 9.96238  18.03297 0.648 13.34518  ? 112 VAL B CG1  1 
ATOM   4672 C CG1  B VAL B 1 115 ? -20.82350 12.10882 17.90435 0.352 13.34518  ? 112 VAL B CG1  1 
ATOM   4673 C CG2  A VAL B 1 115 ? -20.13563 11.46611 19.89953 0.648 13.97157  ? 112 VAL B CG2  1 
ATOM   4674 C CG2  B VAL B 1 115 ? -19.50066 9.99913  18.18934 0.352 13.97157  ? 112 VAL B CG2  1 
ATOM   4675 H H    . VAL B 1 115 ? -17.50829 12.10056 20.08503 1.000 9.42526   ? 112 VAL B H    1 
ATOM   4676 H HA   . VAL B 1 115 ? -17.99520 12.02049 17.41274 1.000 10.68937  ? 112 VAL B HA   1 
ATOM   4677 H HB   A VAL B 1 115 ? -20.31856 11.80286 17.92301 0.648 14.61195  ? 112 VAL B HB   1 
ATOM   4678 H HB   B VAL B 1 115 ? -19.80858 11.48211 19.55981 0.352 14.61195  ? 112 VAL B HB   1 
ATOM   4679 H HG11 A VAL B 1 115 ? -20.20654 9.45583  18.15664 0.648 16.01422  ? 112 VAL B HG11 1 
ATOM   4680 H HG11 B VAL B 1 115 ? -21.55545 11.47361 17.86358 0.352 16.01422  ? 112 VAL B HG11 1 
ATOM   4681 H HG12 A VAL B 1 115 ? -19.13488 9.95752  17.09675 0.648 16.01422  ? 112 VAL B HG12 1 
ATOM   4682 H HG12 B VAL B 1 115 ? -21.09422 12.89370 18.40592 0.352 16.01422  ? 112 VAL B HG12 1 
ATOM   4683 H HG13 A VAL B 1 115 ? -18.67776 9.57918  18.57032 0.648 16.01422  ? 112 VAL B HG13 1 
ATOM   4684 H HG13 B VAL B 1 115 ? -20.55748 12.36497 17.00740 0.352 16.01422  ? 112 VAL B HG13 1 
ATOM   4685 H HG21 A VAL B 1 115 ? -20.94539 10.93610 19.96497 0.648 16.76589  ? 112 VAL B HG21 1 
ATOM   4686 H HG21 B VAL B 1 115 ? -20.33316 9.53688  18.37420 0.352 16.76589  ? 112 VAL B HG21 1 
ATOM   4687 H HG22 A VAL B 1 115 ? -19.45673 11.10742 20.49226 0.648 16.76589  ? 112 VAL B HG22 1 
ATOM   4688 H HG22 B VAL B 1 115 ? -19.30349 9.95868  17.24045 0.352 16.76589  ? 112 VAL B HG22 1 
ATOM   4689 H HG23 A VAL B 1 115 ? -20.32434 12.38858 20.13260 0.648 16.76589  ? 112 VAL B HG23 1 
ATOM   4690 H HG23 B VAL B 1 115 ? -18.77836 9.59455  18.69481 0.352 16.76589  ? 112 VAL B HG23 1 
ATOM   4691 N N    . ILE B 1 116 ? -18.44195 14.38777 17.19829 1.000 8.26591   ? 113 ILE B N    1 
ATOM   4692 C CA   A ILE B 1 116 ? -18.78257 15.79486 17.02234 0.490 8.97361   ? 113 ILE B CA   1 
ATOM   4693 C CA   B ILE B 1 116 ? -18.78258 15.79488 17.02247 0.489 8.97361   ? 113 ILE B CA   1 
ATOM   4694 C CA   C ILE B 1 116 ? -18.80190 15.79010 17.04058 0.021 10.09361  ? 113 ILE B CA   1 
ATOM   4695 C C    . ILE B 1 116 ? -20.02137 15.85570 16.13655 1.000 9.12986   ? 113 ILE B C    1 
ATOM   4696 O O    . ILE B 1 116 ? -19.98271 15.41131 14.98203 1.000 10.31692  ? 113 ILE B O    1 
ATOM   4697 C CB   A ILE B 1 116 ? -17.63431 16.58557 16.37268 0.490 9.70361   ? 113 ILE B CB   1 
ATOM   4698 C CB   B ILE B 1 116 ? -17.63430 16.58592 16.37332 0.489 9.71361   ? 113 ILE B CB   1 
ATOM   4699 C CB   C ILE B 1 116 ? -17.63681 16.62183 16.48711 0.021 13.38361  ? 113 ILE B CB   1 
ATOM   4700 C CG1  A ILE B 1 116 ? -16.32167 16.39883 17.13812 0.490 10.77361  ? 113 ILE B CG1  1 
ATOM   4701 C CG1  B ILE B 1 116 ? -16.32166 16.39848 17.13860 0.489 10.79361  ? 113 ILE B CG1  1 
ATOM   4702 C CG1  C ILE B 1 116 ? -16.57009 16.80353 17.56914 0.021 18.52361  ? 113 ILE B CG1  1 
ATOM   4703 C CG2  A ILE B 1 116 ? -18.01576 18.05862 16.26914 0.490 10.86361  ? 113 ILE B CG2  1 
ATOM   4704 C CG2  B ILE B 1 116 ? -18.01556 18.05911 16.27126 0.489 10.88361  ? 113 ILE B CG2  1 
ATOM   4705 C CG2  C ILE B 1 116 ? -18.13140 17.97733 16.00610 0.021 12.04361  ? 113 ILE B CG2  1 
ATOM   4706 C CD1  A ILE B 1 116 ? -16.36045 16.86140 18.57743 0.490 10.21361  ? 113 ILE B CD1  1 
ATOM   4707 C CD1  B ILE B 1 116 ? -16.36027 16.86038 18.57818 0.489 10.24361  ? 113 ILE B CD1  1 
ATOM   4708 C CD1  C ILE B 1 116 ? -15.20299 16.31297 17.17078 0.021 21.83361  ? 113 ILE B CD1  1 
ATOM   4709 H H    A ILE B 1 116 ? -18.13652 14.02367 16.48153 0.490 9.91909   ? 113 ILE B H    1 
ATOM   4710 H H    B ILE B 1 116 ? -18.13654 14.02369 16.48151 0.489 9.91909   ? 113 ILE B H    1 
ATOM   4711 H H    C ILE B 1 116 ? -18.12930 14.03048 16.48122 0.021 9.91909   ? 113 ILE B H    1 
ATOM   4712 H HA   A ILE B 1 116 ? -18.98017 16.18520 17.88807 0.490 10.76833  ? 113 ILE B HA   1 
ATOM   4713 H HA   B ILE B 1 116 ? -18.98032 16.18510 17.88822 0.489 10.76833  ? 113 ILE B HA   1 
ATOM   4714 H HA   C ILE B 1 116 ? -19.04474 16.16181 17.90300 0.021 12.11233  ? 113 ILE B HA   1 
ATOM   4715 H HB   A ILE B 1 116 ? -17.49005 16.23761 15.47880 0.490 11.64433  ? 113 ILE B HB   1 
ATOM   4716 H HB   B ILE B 1 116 ? -17.49017 16.23866 15.47915 0.489 11.65633  ? 113 ILE B HB   1 
ATOM   4717 H HB   C ILE B 1 116 ? -17.24939 16.14941 15.73371 0.021 16.06033  ? 113 ILE B HB   1 
ATOM   4718 H HG12 A ILE B 1 116 ? -16.09730 15.45514 17.14025 0.490 12.92833  ? 113 ILE B HG12 1 
ATOM   4719 H HG12 B ILE B 1 116 ? -16.09752 15.45473 17.14026 0.489 12.95233  ? 113 ILE B HG12 1 
ATOM   4720 H HG12 C ILE B 1 116 ? -16.49557 17.74813 17.77669 0.021 22.22833  ? 113 ILE B HG12 1 
ATOM   4721 H HG13 A ILE B 1 116 ? -15.62705 16.90397 16.68729 0.490 12.92833  ? 113 ILE B HG13 1 
ATOM   4722 H HG13 B ILE B 1 116 ? -15.62694 16.90366 16.68798 0.489 12.95233  ? 113 ILE B HG13 1 
ATOM   4723 H HG13 C ILE B 1 116 ? -16.84163 16.31067 18.35924 0.021 22.22833  ? 113 ILE B HG13 1 
ATOM   4724 H HG21 A ILE B 1 116 ? -17.24147 18.56569 15.97888 0.490 13.03633  ? 113 ILE B HG21 1 
ATOM   4725 H HG21 B ILE B 1 116 ? -17.24113 18.56642 15.98177 0.489 13.06033  ? 113 ILE B HG21 1 
ATOM   4726 H HG21 C ILE B 1 116 ? -17.36986 18.56464 15.87954 0.021 14.45233  ? 113 ILE B HG21 1 
ATOM   4727 H HG22 A ILE B 1 116 ? -18.73435 18.15421 15.62464 0.490 13.03633  ? 113 ILE B HG22 1 
ATOM   4728 H HG22 B ILE B 1 116 ? -18.73395 18.15547 15.62665 0.489 13.06033  ? 113 ILE B HG22 1 
ATOM   4729 H HG22 C ILE B 1 116 ? -18.60304 17.86163 15.16642 0.021 14.45233  ? 113 ILE B HG22 1 
ATOM   4730 H HG23 A ILE B 1 116 ? -18.30840 18.37099 17.13959 0.490 13.03633  ? 113 ILE B HG23 1 
ATOM   4731 H HG23 B ILE B 1 116 ? -18.30842 18.37058 17.14196 0.489 13.06033  ? 113 ILE B HG23 1 
ATOM   4732 H HG23 C ILE B 1 116 ? -18.72938 18.35006 16.67274 0.021 14.45233  ? 113 ILE B HG23 1 
ATOM   4733 H HD11 A ILE B 1 116 ? -15.48474 16.73263 18.97423 0.490 12.25633  ? 113 ILE B HD11 1 
ATOM   4734 H HD11 B ILE B 1 116 ? -15.48476 16.73058 18.97508 0.489 12.29233  ? 113 ILE B HD11 1 
ATOM   4735 H HD11 C ILE B 1 116 ? -14.59863 16.41738 17.92228 0.021 26.20033  ? 113 ILE B HD11 1 
ATOM   4736 H HD12 A ILE B 1 116 ? -16.59920 17.80127 18.60076 0.490 12.25633  ? 113 ILE B HD12 1 
ATOM   4737 H HD12 B ILE B 1 116 ? -16.59814 17.80046 18.60193 0.489 12.29233  ? 113 ILE B HD12 1 
ATOM   4738 H HD12 C ILE B 1 116 ? -15.26325 15.37728 16.92228 0.021 26.20033  ? 113 ILE B HD12 1 
ATOM   4739 H HD13 A ILE B 1 116 ? -17.02170 16.34009 19.05897 0.490 12.25633  ? 113 ILE B HD13 1 
ATOM   4740 H HD13 B ILE B 1 116 ? -17.02210 16.33945 19.05934 0.489 12.29233  ? 113 ILE B HD13 1 
ATOM   4741 H HD13 C ILE B 1 116 ? -14.88711 16.83567 16.41718 0.021 26.20033  ? 113 ILE B HD13 1 
ATOM   4742 N N    . ALA B 1 117 ? -21.10926 16.40770 16.65942 1.000 8.81087   ? 114 ALA B N    1 
ATOM   4743 C CA   . ALA B 1 117 ? -22.34159 16.53809 15.89433 1.000 8.96827   ? 114 ALA B CA   1 
ATOM   4744 C C    . ALA B 1 117 ? -22.42081 17.93129 15.28437 1.000 8.97470   ? 114 ALA B C    1 
ATOM   4745 O O    . ALA B 1 117 ? -22.15659 18.92630 15.96844 1.000 9.12185   ? 114 ALA B O    1 
ATOM   4746 C CB   . ALA B 1 117 ? -23.56603 16.29479 16.77837 1.000 11.14083  ? 114 ALA B CB   1 
ATOM   4747 H H    . ALA B 1 117 ? -21.15796 16.71605 17.46076 1.000 10.57304  ? 114 ALA B H    1 
ATOM   4748 H HA   . ALA B 1 117 ? -22.34089 15.88266 15.17927 1.000 10.76193  ? 114 ALA B HA   1 
ATOM   4749 H HB1  . ALA B 1 117 ? -24.36615 16.35579 16.23341 1.000 13.36900  ? 114 ALA B HB1  1 
ATOM   4750 H HB2  . ALA B 1 117 ? -23.50061 15.41073 17.17213 1.000 13.36900  ? 114 ALA B HB2  1 
ATOM   4751 H HB3  . ALA B 1 117 ? -23.58968 16.96718 17.47711 1.000 13.36900  ? 114 ALA B HB3  1 
ATOM   4752 N N    . VAL B 1 118 ? -22.78027 17.99574 13.99879 1.000 9.98953   ? 115 VAL B N    1 
ATOM   4753 C CA   . VAL B 1 118 ? -23.02587 19.25490 13.31120 1.000 9.97117   ? 115 VAL B CA   1 
ATOM   4754 C C    . VAL B 1 118 ? -24.39175 19.20782 12.63904 1.000 9.82736   ? 115 VAL B C    1 
ATOM   4755 O O    . VAL B 1 118 ? -24.90503 18.13966 12.29038 1.000 11.19302  ? 115 VAL B O    1 
ATOM   4756 C CB   . VAL B 1 118 ? -21.95143 19.59082 12.24935 1.000 10.69615  ? 115 VAL B CB   1 
ATOM   4757 C CG1  . VAL B 1 118 ? -20.57743 19.67136 12.87571 1.000 10.98742  ? 115 VAL B CG1  1 
ATOM   4758 C CG2  . VAL B 1 118 ? -21.98430 18.57585 11.11472 1.000 14.18546  ? 115 VAL B CG2  1 
ATOM   4759 H H    . VAL B 1 118 ? -22.88920 17.30533 13.49772 1.000 11.98744  ? 115 VAL B H    1 
ATOM   4760 H HA   . VAL B 1 118 ? -23.02315 19.95371 13.98392 1.000 11.96541  ? 115 VAL B HA   1 
ATOM   4761 H HB   . VAL B 1 118 ? -22.14842 20.46251 11.87219 1.000 12.83538  ? 115 VAL B HB   1 
ATOM   4762 H HG11 . VAL B 1 118 ? -19.97987 20.13424 12.26779 1.000 13.18490  ? 115 VAL B HG11 1 
ATOM   4763 H HG12 . VAL B 1 118 ? -20.63987 20.15787 13.71256 1.000 13.18490  ? 115 VAL B HG12 1 
ATOM   4764 H HG13 . VAL B 1 118 ? -20.25171 18.77243 13.03921 1.000 13.18490  ? 115 VAL B HG13 1 
ATOM   4765 H HG21 . VAL B 1 118 ? -21.17951 18.67177 10.58179 1.000 17.02255  ? 115 VAL B HG21 1 
ATOM   4766 H HG22 . VAL B 1 118 ? -22.02739 17.68284 11.49099 1.000 17.02255  ? 115 VAL B HG22 1 
ATOM   4767 H HG23 . VAL B 1 118 ? -22.76645 18.74145 10.56544 1.000 17.02255  ? 115 VAL B HG23 1 
ATOM   4768 N N    . ASN B 1 119 ? -24.96848 20.38599 12.43838 1.000 9.85074   ? 116 ASN B N    1 
ATOM   4769 C CA   . ASN B 1 119 ? -26.18415 20.52060 11.64942 1.000 10.23994  ? 116 ASN B CA   1 
ATOM   4770 C C    . ASN B 1 119 ? -25.79077 20.54824 10.17780 1.000 10.09938  ? 116 ASN B C    1 
ATOM   4771 O O    . ASN B 1 119 ? -24.98271 21.38583 9.76377  1.000 11.66292  ? 116 ASN B O    1 
ATOM   4772 C CB   . ASN B 1 119 ? -26.90012 21.80890 12.04183 1.000 11.31877  ? 116 ASN B CB   1 
ATOM   4773 C CG   . ASN B 1 119 ? -28.20385 21.99863 11.29950 1.000 14.95822  ? 116 ASN B CG   1 
ATOM   4774 O OD1  . ASN B 1 119 ? -28.21480 22.24668 10.09427 1.000 14.94032  ? 116 ASN B OD1  1 
ATOM   4775 N ND2  . ASN B 1 119 ? -29.31345 21.89818 12.01949 1.000 22.14119  ? 116 ASN B ND2  1 
ATOM   4776 H H    . ASN B 1 119 ? -24.67184 21.12983 12.75192 1.000 11.82089  ? 116 ASN B H    1 
ATOM   4777 H HA   . ASN B 1 119 ? -26.78546 19.77531 11.80391 1.000 12.28793  ? 116 ASN B HA   1 
ATOM   4778 H HB2  . ASN B 1 119 ? -27.09564 21.78585 12.99164 1.000 13.58252  ? 116 ASN B HB2  1 
ATOM   4779 H HB3  . ASN B 1 119 ? -26.32632 22.56434 11.83947 1.000 13.58252  ? 116 ASN B HB3  1 
ATOM   4780 H HD21 . ASN B 1 119 ? -30.08047 21.99802 11.64358 1.000 26.56943  ? 116 ASN B HD21 1 
ATOM   4781 H HD22 . ASN B 1 119 ? -29.26579 21.73321 12.86217 1.000 26.56943  ? 116 ASN B HD22 1 
ATOM   4782 N N    . ALA B 1 120 ? -26.34935 19.62852 9.38906  1.000 10.71058  ? 117 ALA B N    1 
ATOM   4783 C CA   . ALA B 1 120 ? -25.93373 19.49816 7.99928  1.000 10.26731  ? 117 ALA B CA   1 
ATOM   4784 C C    . ALA B 1 120 ? -26.27635 20.72100 7.16147  1.000 11.39276  ? 117 ALA B C    1 
ATOM   4785 O O    . ALA B 1 120 ? -25.62785 20.95359 6.13652  1.000 14.25623  ? 117 ALA B O    1 
ATOM   4786 C CB   . ALA B 1 120 ? -26.59114 18.27502 7.36156  1.000 12.09990  ? 117 ALA B CB   1 
ATOM   4787 H H    . ALA B 1 120 ? -26.96217 19.07698 9.63371  1.000 12.85269  ? 117 ALA B H    1 
ATOM   4788 H HA   . ALA B 1 120 ? -24.97102 19.37969 7.99145  1.000 12.32077  ? 117 ALA B HA   1 
ATOM   4789 H HB1  . ALA B 1 120 ? -26.22678 18.14872 6.47151  1.000 14.51988  ? 117 ALA B HB1  1 
ATOM   4790 H HB2  . ALA B 1 120 ? -26.40578 17.49569 7.90853  1.000 14.51988  ? 117 ALA B HB2  1 
ATOM   4791 H HB3  . ALA B 1 120 ? -27.54846 18.42231 7.30924  1.000 14.51988  ? 117 ALA B HB3  1 
ATOM   4792 N N    . ASP B 1 121 ? -27.28271 21.49496 7.55693  1.000 12.30522  ? 118 ASP B N    1 
ATOM   4793 C CA   . ASP B 1 121 ? -27.69133 22.64055 6.75522  1.000 14.24752  ? 118 ASP B CA   1 
ATOM   4794 C C    . ASP B 1 121 ? -26.91879 23.90516 7.11327  1.000 14.18228  ? 118 ASP B C    1 
ATOM   4795 O O    . ASP B 1 121 ? -26.53129 24.66125 6.21736  1.000 16.22971  ? 118 ASP B O    1 
ATOM   4796 C CB   . ASP B 1 121 ? -29.19857 22.86751 6.89589  1.000 16.69835  ? 118 ASP B CB   1 
ATOM   4797 C CG   . ASP B 1 121 ? -30.01717 21.70499 6.35589  1.000 18.78663  ? 118 ASP B CG   1 
ATOM   4798 O OD1  . ASP B 1 121 ? -29.48091 20.90891 5.55373  1.000 18.46254  ? 118 ASP B OD1  1 
ATOM   4799 O OD2  . ASP B 1 121 ? -31.20200 21.59171 6.73135  1.000 21.53199  ? 118 ASP B OD2  1 
ATOM   4800 H H    . ASP B 1 121 ? -27.73839 21.37814 8.27687  1.000 14.76626  ? 118 ASP B H    1 
ATOM   4801 H HA   . ASP B 1 121 ? -27.51346 22.45176 5.82055  1.000 17.09703  ? 118 ASP B HA   1 
ATOM   4802 H HB2  . ASP B 1 121 ? -29.41603 22.97789 7.83473  1.000 20.03802  ? 118 ASP B HB2  1 
ATOM   4803 H HB3  . ASP B 1 121 ? -29.44632 23.66475 6.40200  1.000 20.03802  ? 118 ASP B HB3  1 
ATOM   4804 N N    . THR B 1 122 ? -26.67264 24.14676 8.40263  1.000 14.44977  ? 119 THR B N    1 
ATOM   4805 C CA   . THR B 1 122 ? -26.01343 25.36898 8.83680  1.000 13.59872  ? 119 THR B CA   1 
ATOM   4806 C C    . THR B 1 122 ? -24.53227 25.19011 9.13298  1.000 13.04337  ? 119 THR B C    1 
ATOM   4807 O O    . THR B 1 122 ? -23.81581 26.19047 9.25019  1.000 14.36225  ? 119 THR B O    1 
ATOM   4808 C CB   . THR B 1 122 ? -26.66907 25.88394 10.12518 1.000 14.38513  ? 119 THR B CB   1 
ATOM   4809 O OG1  . THR B 1 122 ? -26.38298 24.97066 11.19304 1.000 14.64440  ? 119 THR B OG1  1 
ATOM   4810 C CG2  . THR B 1 122 ? -28.16723 25.99849 9.94827  1.000 16.75630  ? 119 THR B CG2  1 
ATOM   4811 H H    . THR B 1 122 ? -26.88046 23.61312 9.04422  1.000 17.33972  ? 119 THR B H    1 
ATOM   4812 H HA   . THR B 1 122 ? -26.11272 26.02916 8.13310  1.000 16.31846  ? 119 THR B HA   1 
ATOM   4813 H HB   . THR B 1 122 ? -26.32213 26.76306 10.34355 1.000 17.26216  ? 119 THR B HB   1 
ATOM   4814 H HG1  . THR B 1 122 ? -26.80105 25.19797 11.88525 1.000 17.57329  ? 119 THR B HG1  1 
ATOM   4815 H HG21 . THR B 1 122 ? -28.55446 26.47518 10.69908 1.000 20.10756  ? 119 THR B HG21 1 
ATOM   4816 H HG22 . THR B 1 122 ? -28.36889 26.48091 9.13127  1.000 20.10756  ? 119 THR B HG22 1 
ATOM   4817 H HG23 . THR B 1 122 ? -28.56390 25.11473 9.89809  1.000 20.10756  ? 119 THR B HG23 1 
ATOM   4818 N N    . GLY B 1 123 ? -24.06677 23.95050 9.27493  1.000 11.94718  ? 120 GLY B N    1 
ATOM   4819 C CA   . GLY B 1 123 ? -22.71218 23.68681 9.70465  1.000 12.09043  ? 120 GLY B CA   1 
ATOM   4820 C C    . GLY B 1 123 ? -22.44357 23.92964 11.17271 1.000 10.96408  ? 120 GLY B C    1 
ATOM   4821 O O    . GLY B 1 123 ? -21.31692 23.69194 11.62357 1.000 10.54291  ? 120 GLY B O    1 
ATOM   4822 H H    . GLY B 1 123 ? -24.52842 23.24068 9.12450  1.000 14.33662  ? 120 GLY B H    1 
ATOM   4823 H HA2  . GLY B 1 123 ? -22.50348 22.75833 9.51681  1.000 14.50852  ? 120 GLY B HA2  1 
ATOM   4824 H HA3  . GLY B 1 123 ? -22.11095 24.25447 9.19751  1.000 14.50852  ? 120 GLY B HA3  1 
ATOM   4825 N N    . ALA B 1 124 ? -23.43449 24.38503 11.93615 1.000 12.50703  ? 121 ALA B N    1 
ATOM   4826 C CA   . ALA B 1 124 ? -23.20577 24.69395 13.34018 1.000 10.47599  ? 121 ALA B CA   1 
ATOM   4827 C C    . ALA B 1 124 ? -22.82591 23.43861 14.11253 1.000 10.09554  ? 121 ALA B C    1 
ATOM   4828 O O    . ALA B 1 124 ? -23.37655 22.35776 13.88335 1.000 11.10584  ? 121 ALA B O    1 
ATOM   4829 C CB   . ALA B 1 124 ? -24.46949 25.29065 13.96153 1.000 12.61269  ? 121 ALA B CB   1 
ATOM   4830 H H    . ALA B 1 124 ? -24.23956 24.52182 11.66643 1.000 15.00844  ? 121 ALA B H    1 
ATOM   4831 H HA   . ALA B 1 124 ? -22.48292 25.33754 13.40486 1.000 12.57119  ? 121 ALA B HA   1 
ATOM   4832 H HB1  . ALA B 1 124 ? -24.28661 25.52625 14.88454 1.000 15.13523  ? 121 ALA B HB1  1 
ATOM   4833 H HB2  . ALA B 1 124 ? -24.72336 26.08249 13.46210 1.000 15.13523  ? 121 ALA B HB2  1 
ATOM   4834 H HB3  . ALA B 1 124 ? -25.18130 24.63284 13.92286 1.000 15.13523  ? 121 ALA B HB3  1 
ATOM   4835 N N    . VAL B 1 125 ? -21.88029 23.59019 15.03897 1.000 10.39629  ? 122 VAL B N    1 
ATOM   4836 C CA   . VAL B 1 125 ? -21.54892 22.50602 15.95743 1.000 10.07214  ? 122 VAL B CA   1 
ATOM   4837 C C    . VAL B 1 125 ? -22.68409 22.36486 16.96451 1.000 11.27068  ? 122 VAL B C    1 
ATOM   4838 O O    . VAL B 1 125 ? -23.03133 23.31450 17.67733 1.000 14.57048  ? 122 VAL B O    1 
ATOM   4839 C CB   . VAL B 1 125 ? -20.19554 22.74251 16.63864 1.000 9.05017   ? 122 VAL B CB   1 
ATOM   4840 C CG1  . VAL B 1 125 ? -19.92316 21.65339 17.67266 1.000 10.79249  ? 122 VAL B CG1  1 
ATOM   4841 C CG2  . VAL B 1 125 ? -19.08131 22.76649 15.59401 1.000 12.68596  ? 122 VAL B CG2  1 
ATOM   4842 H H    . VAL B 1 125 ? -21.41953 24.30707 15.15464 1.000 12.47555  ? 122 VAL B H    1 
ATOM   4843 H HA   . VAL B 1 125 ? -21.47784 21.67450 15.46302 1.000 12.08657  ? 122 VAL B HA   1 
ATOM   4844 H HB   . VAL B 1 125 ? -20.21492 23.59879 17.09395 1.000 10.86020  ? 122 VAL B HB   1 
ATOM   4845 H HG11 . VAL B 1 125 ? -18.98285 21.67143 17.91011 1.000 12.95099  ? 122 VAL B HG11 1 
ATOM   4846 H HG12 . VAL B 1 125 ? -20.46611 21.82134 18.45872 1.000 12.95099  ? 122 VAL B HG12 1 
ATOM   4847 H HG13 . VAL B 1 125 ? -20.15146 20.79136 17.29097 1.000 12.95099  ? 122 VAL B HG13 1 
ATOM   4848 H HG21 . VAL B 1 125 ? -18.24981 23.01913 16.02493 1.000 15.22316  ? 122 VAL B HG21 1 
ATOM   4849 H HG22 . VAL B 1 125 ? -18.99604 21.88295 15.20289 1.000 15.22316  ? 122 VAL B HG22 1 
ATOM   4850 H HG23 . VAL B 1 125 ? -19.30700 23.41228 14.90632 1.000 15.22316  ? 122 VAL B HG23 1 
ATOM   4851 N N    . VAL B 1 126 ? -23.27800 21.17719 17.00562 1.000 10.88096  ? 123 VAL B N    1 
ATOM   4852 C CA   . VAL B 1 126 ? -24.43674 20.90006 17.84668 1.000 12.27902  ? 123 VAL B CA   1 
ATOM   4853 C C    . VAL B 1 126 ? -24.02771 20.33213 19.19896 1.000 10.56853  ? 123 VAL B C    1 
ATOM   4854 O O    . VAL B 1 126 ? -24.62027 20.67209 20.22671 1.000 12.39740  ? 123 VAL B O    1 
ATOM   4855 C CB   . VAL B 1 126 ? -25.36166 19.93551 17.07239 1.000 13.21413  ? 123 VAL B CB   1 
ATOM   4856 C CG1  . VAL B 1 126 ? -26.43835 19.38133 17.98161 1.000 15.59234  ? 123 VAL B CG1  1 
ATOM   4857 C CG2  . VAL B 1 126 ? -25.96538 20.63292 15.85514 1.000 15.37010  ? 123 VAL B CG2  1 
ATOM   4858 H H    . VAL B 1 126 ? -23.02308 20.49756 16.54440 1.000 13.05715  ? 123 VAL B H    1 
ATOM   4859 H HA   . VAL B 1 126 ? -24.91608 21.72319 18.02999 1.000 14.73482  ? 123 VAL B HA   1 
ATOM   4860 H HB   . VAL B 1 126 ? -24.83697 19.18557 16.75116 1.000 15.85695  ? 123 VAL B HB   1 
ATOM   4861 H HG11 . VAL B 1 126 ? -27.17854 19.06678 17.43932 1.000 18.71081  ? 123 VAL B HG11 1 
ATOM   4862 H HG12 . VAL B 1 126 ? -26.06963 18.64643 18.49627 1.000 18.71081  ? 123 VAL B HG12 1 
ATOM   4863 H HG13 . VAL B 1 126 ? -26.74050 20.08405 18.57809 1.000 18.71081  ? 123 VAL B HG13 1 
ATOM   4864 H HG21 . VAL B 1 126 ? -26.60223 20.03564 15.43256 1.000 18.44412  ? 123 VAL B HG21 1 
ATOM   4865 H HG22 . VAL B 1 126 ? -26.41359 21.44278 16.14521 1.000 18.44412  ? 123 VAL B HG22 1 
ATOM   4866 H HG23 . VAL B 1 126 ? -25.25483 20.85297 15.23257 1.000 18.44412  ? 123 VAL B HG23 1 
ATOM   4867 N N    . SER B 1 127 ? -23.02760 19.45716 19.22690 1.000 10.14129  ? 124 SER B N    1 
ATOM   4868 C CA   . SER B 1 127 ? -22.58983 18.85269 20.47574 1.000 10.25742  ? 124 SER B CA   1 
ATOM   4869 C C    . SER B 1 127 ? -21.21344 18.24179 20.27217 1.000 9.80609   ? 124 SER B C    1 
ATOM   4870 O O    . SER B 1 127 ? -20.82349 17.89925 19.15339 1.000 9.42169   ? 124 SER B O    1 
ATOM   4871 C CB   . SER B 1 127 ? -23.57040 17.77797 20.95764 1.000 9.46921   ? 124 SER B CB   1 
ATOM   4872 O OG   . SER B 1 127 ? -23.57278 16.66268 20.08304 1.000 10.07478  ? 124 SER B OG   1 
ATOM   4873 H H    . SER B 1 127 ? -22.58738 19.19815 18.53500 1.000 12.16955  ? 124 SER B H    1 
ATOM   4874 H HA   . SER B 1 127 ? -22.52673 19.54428 21.15294 1.000 12.30890  ? 124 SER B HA   1 
ATOM   4875 H HB2  . SER B 1 127 ? -23.30493 17.48350 21.84291 1.000 11.36305  ? 124 SER B HB2  1 
ATOM   4876 H HB3  . SER B 1 127 ? -24.46294 18.15660 20.98772 1.000 11.36305  ? 124 SER B HB3  1 
ATOM   4877 H HG   . SER B 1 127 ? -23.97526 16.01795 20.44072 1.000 12.08974  ? 124 SER B HG   1 
ATOM   4878 N N    . THR B 1 128 ? -20.48542 18.10332 21.38044 1.000 11.15408  ? 125 THR B N    1 
ATOM   4879 C CA   . THR B 1 128 ? -19.15725 17.51827 21.35822 1.000 11.69490  ? 125 THR B CA   1 
ATOM   4880 C C    . THR B 1 128 ? -18.94604 16.40131 22.37245 1.000 10.79428  ? 125 THR B C    1 
ATOM   4881 O O    . THR B 1 128 ? -17.88312 15.77368 22.34140 1.000 11.66229  ? 125 THR B O    1 
ATOM   4882 C CB   . THR B 1 128 ? -18.08936 18.59593 21.61249 1.000 12.83046  ? 125 THR B CB   1 
ATOM   4883 O OG1  . THR B 1 128 ? -18.27563 19.14726 22.92316 1.000 15.76437  ? 125 THR B OG1  1 
ATOM   4884 C CG2  . THR B 1 128 ? -18.17691 19.71053 20.57809 1.000 13.61104  ? 125 THR B CG2  1 
ATOM   4885 H H    . THR B 1 128 ? -20.74655 18.34496 22.16339 1.000 13.38489  ? 125 THR B H    1 
ATOM   4886 H HA   . THR B 1 128 ? -19.01238 17.14741 20.47370 1.000 14.03388  ? 125 THR B HA   1 
ATOM   4887 H HB   . THR B 1 128 ? -17.20807 18.19628 21.54526 1.000 15.39655  ? 125 THR B HB   1 
ATOM   4888 H HG1  . THR B 1 128 ? -19.04211 19.48504 22.98649 1.000 18.91724  ? 125 THR B HG1  1 
ATOM   4889 H HG21 . THR B 1 128 ? -17.48174 20.36766 20.73881 1.000 16.33325  ? 125 THR B HG21 1 
ATOM   4890 H HG22 . THR B 1 128 ? -18.06476 19.34528 19.68651 1.000 16.33325  ? 125 THR B HG22 1 
ATOM   4891 H HG23 . THR B 1 128 ? -19.04142 20.14699 20.63304 1.000 16.33325  ? 125 THR B HG23 1 
ATOM   4892 N N    . LYS B 1 129 ? -19.90415 16.13145 23.26138 1.000 10.23058  ? 126 LYS B N    1 
ATOM   4893 C CA   . LYS B 1 129 ? -19.71936 15.18701 24.35883 1.000 11.09041  ? 126 LYS B CA   1 
ATOM   4894 C C    . LYS B 1 129 ? -20.60776 13.94998 24.23972 1.000 10.19246  ? 126 LYS B C    1 
ATOM   4895 O O    . LYS B 1 129 ? -20.81306 13.23949 25.22915 1.000 11.74759  ? 126 LYS B O    1 
ATOM   4896 C CB   . LYS B 1 129 ? -19.95621 15.90826 25.68562 1.000 14.59861  ? 126 LYS B CB   1 
ATOM   4897 C CG   . LYS B 1 129 ? -19.00869 17.07662 25.90989 1.000 21.46070  ? 126 LYS B CG   1 
ATOM   4898 C CD   . LYS B 1 129 ? -17.56528 16.60442 25.92489 1.000 31.38340  ? 126 LYS B CD   1 
ATOM   4899 C CE   . LYS B 1 129 ? -16.60755 17.70577 26.34544 1.000 38.60360  ? 126 LYS B CE   1 
ATOM   4900 N NZ   . LYS B 1 129 ? -15.19831 17.34432 26.01567 1.000 42.01887  ? 126 LYS B NZ   1 
ATOM   4901 H H    . LYS B 1 129 ? -20.68497 16.49162 23.24716 1.000 12.27669  ? 126 LYS B H    1 
ATOM   4902 H HA   . LYS B 1 129 ? -18.80517 14.86311 24.34354 1.000 13.30849  ? 126 LYS B HA   1 
ATOM   4903 H HB2  . LYS B 1 129 ? -20.86295 16.25259 25.69829 1.000 17.51833  ? 126 LYS B HB2  1 
ATOM   4904 H HB3  . LYS B 1 129 ? -19.83042 15.27817 26.41230 1.000 17.51833  ? 126 LYS B HB3  1 
ATOM   4905 H HG2  . LYS B 1 129 ? -19.11421 17.72163 25.19314 1.000 25.75284  ? 126 LYS B HG2  1 
ATOM   4906 H HG3  . LYS B 1 129 ? -19.20502 17.49388 26.76327 1.000 25.75284  ? 126 LYS B HG3  1 
ATOM   4907 H HD2  . LYS B 1 129 ? -17.47633 15.87047 26.55282 1.000 37.66008  ? 126 LYS B HD2  1 
ATOM   4908 H HD3  . LYS B 1 129 ? -17.31638 16.31119 25.03440 1.000 37.66008  ? 126 LYS B HD3  1 
ATOM   4909 H HE2  . LYS B 1 129 ? -16.83198 18.52510 25.87722 1.000 46.32432  ? 126 LYS B HE2  1 
ATOM   4910 H HE3  . LYS B 1 129 ? -16.67330 17.84249 27.30351 1.000 46.32432  ? 126 LYS B HE3  1 
ATOM   4911 H HZ1  . LYS B 1 129 ? -14.64429 17.97140 26.31889 1.000 50.42265  ? 126 LYS B HZ1  1 
ATOM   4912 H HZ2  . LYS B 1 129 ? -14.98755 16.56602 26.39241 1.000 50.42265  ? 126 LYS B HZ2  1 
ATOM   4913 H HZ3  . LYS B 1 129 ? -15.10040 17.27427 25.13385 1.000 50.42265  ? 126 LYS B HZ3  1 
ATOM   4914 N N    . GLY B 1 130 ? -21.12470 13.66598 23.04432 1.000 9.13586   ? 127 GLY B N    1 
ATOM   4915 C CA   . GLY B 1 130 ? -21.97966 12.50272 22.87435 1.000 10.23016  ? 127 GLY B CA   1 
ATOM   4916 C C    . GLY B 1 130 ? -21.32075 11.18688 23.24653 1.000 10.09241  ? 127 GLY B C    1 
ATOM   4917 O O    . GLY B 1 130 ? -22.00209 10.24580 23.66197 1.000 10.85467  ? 127 GLY B O    1 
ATOM   4918 H H    . GLY B 1 130 ? -20.99603 14.12547 22.32884 1.000 10.96303  ? 127 GLY B H    1 
ATOM   4919 H HA2  . GLY B 1 130 ? -22.76800 12.60891 23.42945 1.000 12.27619  ? 127 GLY B HA2  1 
ATOM   4920 H HA3  . GLY B 1 130 ? -22.25279 12.44711 21.94526 1.000 12.27619  ? 127 GLY B HA3  1 
ATOM   4921 N N    . ARG B 1 131 ? -19.99866 11.08776 23.08942 1.000 10.23229  ? 128 ARG B N    1 
ATOM   4922 C CA   . ARG B 1 131 ? -19.31868 9.83995  23.43290 1.000 11.29866  ? 128 ARG B CA   1 
ATOM   4923 C C    . ARG B 1 131 ? -19.52621 9.49603  24.90095 1.000 12.48362  ? 128 ARG B C    1 
ATOM   4924 O O    . ARG B 1 131 ? -19.64402 8.31939  25.26315 1.000 13.57116  ? 128 ARG B O    1 
ATOM   4925 C CB   . ARG B 1 131 ? -17.83053 9.94124  23.09338 1.000 12.56037  ? 128 ARG B CB   1 
ATOM   4926 C CG   . ARG B 1 131 ? -16.98077 8.75251  23.53434 1.000 12.78124  ? 128 ARG B CG   1 
ATOM   4927 C CD   . ARG B 1 131 ? -16.45184 8.92666  24.95600 1.000 12.72267  ? 128 ARG B CD   1 
ATOM   4928 N NE   . ARG B 1 131 ? -15.52429 7.86377  25.32716 1.000 13.06539  ? 128 ARG B NE   1 
ATOM   4929 C CZ   . ARG B 1 131 ? -15.88078 6.61191  25.57735 1.000 13.55520  ? 128 ARG B CZ   1 
ATOM   4930 N NH1  . ARG B 1 131 ? -17.14702 6.23143  25.52518 1.000 14.29706  ? 128 ARG B NH1  1 
ATOM   4931 N NH2  . ARG B 1 131 ? -14.94357 5.71852  25.87853 1.000 14.64188  ? 128 ARG B NH2  1 
ATOM   4932 H H    . ARG B 1 131 ? -19.48619 11.71185 22.79365 1.000 12.27875  ? 128 ARG B H    1 
ATOM   4933 H HA   . ARG B 1 131 ? -19.68929 9.11726  22.90254 1.000 13.55839  ? 128 ARG B HA   1 
ATOM   4934 H HB2  . ARG B 1 131 ? -17.74084 10.02055 22.13079 1.000 15.07245  ? 128 ARG B HB2  1 
ATOM   4935 H HB3  . ARG B 1 131 ? -17.47082 10.73123 23.52630 1.000 15.07245  ? 128 ARG B HB3  1 
ATOM   4936 H HG2  . ARG B 1 131 ? -17.52008 7.94669  23.50813 1.000 15.33748  ? 128 ARG B HG2  1 
ATOM   4937 H HG3  . ARG B 1 131 ? -16.22156 8.66316  22.93725 1.000 15.33748  ? 128 ARG B HG3  1 
ATOM   4938 H HD2  . ARG B 1 131 ? -15.98379 9.77377  25.02102 1.000 15.26720  ? 128 ARG B HD2  1 
ATOM   4939 H HD3  . ARG B 1 131 ? -17.19611 8.91027  25.57784 1.000 15.26720  ? 128 ARG B HD3  1 
ATOM   4940 H HE   . ARG B 1 131 ? -14.68984 8.06281  25.38775 1.000 15.67847  ? 128 ARG B HE   1 
ATOM   4941 H HH11 . ARG B 1 131 ? -17.75938 6.80131  25.32552 1.000 17.15647  ? 128 ARG B HH11 1 
ATOM   4942 H HH12 . ARG B 1 131 ? -17.35765 5.41427  25.69094 1.000 17.15647  ? 128 ARG B HH12 1 
ATOM   4943 H HH21 . ARG B 1 131 ? -14.11747 5.95564  25.90920 1.000 17.57026  ? 128 ARG B HH21 1 
ATOM   4944 H HH22 . ARG B 1 131 ? -15.16336 4.90345  26.04269 1.000 17.57026  ? 128 ARG B HH22 1 
ATOM   4945 N N    . GLU B 1 132 ? -19.55531 10.50722 25.76333 1.000 12.36400  ? 129 GLU B N    1 
ATOM   4946 C CA   A GLU B 1 132 ? -19.80968 10.28206 27.17910 0.463 15.24541  ? 129 GLU B CA   1 
ATOM   4947 C CA   B GLU B 1 132 ? -19.80812 10.28645 27.17881 0.537 15.24541  ? 129 GLU B CA   1 
ATOM   4948 C C    . GLU B 1 132 ? -21.29960 10.26057 27.49702 1.000 12.99851  ? 129 GLU B C    1 
ATOM   4949 O O    . GLU B 1 132 ? -21.74938 9.43755  28.30058 1.000 14.05337  ? 129 GLU B O    1 
ATOM   4950 C CB   A GLU B 1 132 ? -19.13224 11.36739 28.02249 0.463 23.66484  ? 129 GLU B CB   1 
ATOM   4951 C CB   B GLU B 1 132 ? -19.13507 11.39418 27.99748 0.537 23.66484  ? 129 GLU B CB   1 
ATOM   4952 C CG   A GLU B 1 132 ? -17.61612 11.26889 28.08235 0.463 33.17914  ? 129 GLU B CG   1 
ATOM   4953 C CG   B GLU B 1 132 ? -17.62625 11.47819 27.81428 0.537 33.17914  ? 129 GLU B CG   1 
ATOM   4954 C CD   A GLU B 1 132 ? -16.92475 12.07378 26.99670 0.463 41.33012  ? 129 GLU B CD   1 
ATOM   4955 C CD   B GLU B 1 132 ? -17.07801 12.87700 28.04880 0.537 41.33012  ? 129 GLU B CD   1 
ATOM   4956 O OE1  A GLU B 1 132 ? -17.62020 12.76649 26.22396 0.463 43.80147  ? 129 GLU B OE1  1 
ATOM   4957 O OE1  B GLU B 1 132 ? -17.80649 13.72439 28.60758 0.537 43.80147  ? 129 GLU B OE1  1 
ATOM   4958 O OE2  A GLU B 1 132 ? -15.67922 12.01632 26.92045 0.463 44.95950  ? 129 GLU B OE2  1 
ATOM   4959 O OE2  B GLU B 1 132 ? -15.91676 13.13068 27.66469 0.537 44.95950  ? 129 GLU B OE2  1 
ATOM   4960 H H    . GLU B 1 132 ? -19.43119 11.33141 25.55141 1.000 14.83680  ? 129 GLU B H    1 
ATOM   4961 H HA   . GLU B 1 132 ? -19.42766 9.42534  27.42603 1.000 18.29449  ? 129 GLU B HA   1 
ATOM   4962 H HB2  A GLU B 1 132 ? -19.35442 12.23360 27.64668 0.463 28.39781  ? 129 GLU B HB2  1 
ATOM   4963 H HB2  B GLU B 1 132 ? -19.51146 12.24787 27.73207 0.537 28.39781  ? 129 GLU B HB2  1 
ATOM   4964 H HB3  A GLU B 1 132 ? -19.46549 11.30469 28.93129 0.463 28.39781  ? 129 GLU B HB3  1 
ATOM   4965 H HB3  B GLU B 1 132 ? -19.30853 11.23321 28.93817 0.537 28.39781  ? 129 GLU B HB3  1 
ATOM   4966 H HG2  A GLU B 1 132 ? -17.31246 11.60284 28.94094 0.463 39.81497  ? 129 GLU B HG2  1 
ATOM   4967 H HG2  B GLU B 1 132 ? -17.19799 10.87922 28.44573 0.537 39.81497  ? 129 GLU B HG2  1 
ATOM   4968 H HG3  A GLU B 1 132 ? -17.35642 10.34027 27.97688 0.463 39.81497  ? 129 GLU B HG3  1 
ATOM   4969 H HG3  B GLU B 1 132 ? -17.40370 11.21786 26.90676 0.537 39.81497  ? 129 GLU B HG3  1 
ATOM   4970 N N    . ARG B 1 133 ? -22.07884 11.14400 26.87149 1.000 11.69811  ? 130 ARG B N    1 
ATOM   4971 C CA   . ARG B 1 133 ? -23.48127 11.29191 27.24874 1.000 11.64714  ? 130 ARG B CA   1 
ATOM   4972 C C    . ARG B 1 133 ? -24.33896 10.12520 26.76971 1.000 10.29844  ? 130 ARG B C    1 
ATOM   4973 O O    . ARG B 1 133 ? -25.31468 9.76721  27.43999 1.000 12.70580  ? 130 ARG B O    1 
ATOM   4974 C CB   . ARG B 1 133 ? -24.01363 12.62825 26.72840 1.000 15.18408  ? 130 ARG B CB   1 
ATOM   4975 C CG   . ARG B 1 133 ? -23.13445 13.82300 27.07983 1.000 20.51479  ? 130 ARG B CG   1 
ATOM   4976 C CD   . ARG B 1 133 ? -23.66128 14.62903 28.24753 1.000 25.11065  ? 130 ARG B CD   1 
ATOM   4977 N NE   . ARG B 1 133 ? -22.74263 15.70996 28.58758 1.000 26.47222  ? 130 ARG B NE   1 
ATOM   4978 C CZ   . ARG B 1 133 ? -22.90473 16.98328 28.24779 1.000 29.91779  ? 130 ARG B CZ   1 
ATOM   4979 N NH1  . ARG B 1 133 ? -23.97205 17.39268 27.58067 1.000 31.76132  ? 130 ARG B NH1  1 
ATOM   4980 N NH2  . ARG B 1 133 ? -21.97526 17.86873 28.59361 1.000 31.48691  ? 130 ARG B NH2  1 
ATOM   4981 H H    . ARG B 1 133 ? -21.82297 11.66209 26.23453 1.000 14.03773  ? 130 ARG B H    1 
ATOM   4982 H HA   . ARG B 1 133 ? -23.54774 11.30207 28.21640 1.000 13.97657  ? 130 ARG B HA   1 
ATOM   4983 H HB2  . ARG B 1 133 ? -24.07733 12.58257 25.76157 1.000 18.22090  ? 130 ARG B HB2  1 
ATOM   4984 H HB3  . ARG B 1 133 ? -24.89095 12.78416 27.11169 1.000 18.22090  ? 130 ARG B HB3  1 
ATOM   4985 H HG2  . ARG B 1 133 ? -22.24887 13.50394 27.31401 1.000 24.61774  ? 130 ARG B HG2  1 
ATOM   4986 H HG3  . ARG B 1 133 ? -23.08226 14.41222 26.31106 1.000 24.61774  ? 130 ARG B HG3  1 
ATOM   4987 H HD2  . ARG B 1 133 ? -24.51909 15.01629 28.01281 1.000 30.13278  ? 130 ARG B HD2  1 
ATOM   4988 H HD3  . ARG B 1 133 ? -23.75824 14.05235 29.02145 1.000 30.13278  ? 130 ARG B HD3  1 
ATOM   4989 H HE   . ARG B 1 133 ? -22.04210 15.50687 29.04322 1.000 31.76667  ? 130 ARG B HE   1 
ATOM   4990 H HH11 . ARG B 1 133 ? -24.58159 16.82884 27.35672 1.000 38.11358  ? 130 ARG B HH11 1 
ATOM   4991 H HH12 . ARG B 1 133 ? -24.05601 18.22253 27.37114 1.000 38.11358  ? 130 ARG B HH12 1 
ATOM   4992 H HH21 . ARG B 1 133 ? -21.28040 17.61390 29.03159 1.000 37.78429  ? 130 ARG B HH21 1 
ATOM   4993 H HH22 . ARG B 1 133 ? -22.06887 18.69632 28.37932 1.000 37.78429  ? 130 ARG B HH22 1 
ATOM   4994 N N    . LEU B 1 134 ? -23.99867 9.50879  25.63620 1.000 9.86465   ? 131 LEU B N    1 
ATOM   4995 C CA   . LEU B 1 134 ? -24.77828 8.35964  25.18285 1.000 9.06001   ? 131 LEU B CA   1 
ATOM   4996 C C    . LEU B 1 134 ? -24.73890 7.22933  26.20305 1.000 9.86516   ? 131 LEU B C    1 
ATOM   4997 O O    . LEU B 1 134 ? -25.69495 6.45084  26.30844 1.000 11.88819  ? 131 LEU B O    1 
ATOM   4998 C CB   . LEU B 1 134 ? -24.26064 7.87161  23.82670 1.000 9.22977   ? 131 LEU B CB   1 
ATOM   4999 C CG   . LEU B 1 134 ? -24.85225 6.56878  23.27852 1.000 9.66563   ? 131 LEU B CG   1 
ATOM   5000 C CD1  . LEU B 1 134 ? -26.36602 6.63480  23.12582 1.000 12.34860  ? 131 LEU B CD1  1 
ATOM   5001 C CD2  . LEU B 1 134 ? -24.21212 6.21664  21.93426 1.000 12.25694  ? 131 LEU B CD2  1 
ATOM   5002 H H    . LEU B 1 134 ? -23.34131 9.72964  25.12756 1.000 11.83758  ? 131 LEU B H    1 
ATOM   5003 H HA   . LEU B 1 134 ? -25.70195 8.63220  25.06684 1.000 10.87202  ? 131 LEU B HA   1 
ATOM   5004 H HB2  . LEU B 1 134 ? -24.44512 8.56268  23.17150 1.000 11.07573  ? 131 LEU B HB2  1 
ATOM   5005 H HB3  . LEU B 1 134 ? -23.30341 7.73563  23.90491 1.000 11.07573  ? 131 LEU B HB3  1 
ATOM   5006 H HG   . LEU B 1 134 ? -24.65897 5.86880  23.92161 1.000 11.59876  ? 131 LEU B HG   1 
ATOM   5007 H HD11 . LEU B 1 134 ? -26.67473 5.82657  22.68724 1.000 14.81832  ? 131 LEU B HD11 1 
ATOM   5008 H HD12 . LEU B 1 134 ? -26.76917 6.70870  24.00497 1.000 14.81832  ? 131 LEU B HD12 1 
ATOM   5009 H HD13 . LEU B 1 134 ? -26.59588 7.41020  22.59027 1.000 14.81832  ? 131 LEU B HD13 1 
ATOM   5010 H HD21 . LEU B 1 134 ? -24.63736 5.41954  21.58114 1.000 14.70833  ? 131 LEU B HD21 1 
ATOM   5011 H HD22 . LEU B 1 134 ? -24.33745 6.95769  21.32103 1.000 14.70833  ? 131 LEU B HD22 1 
ATOM   5012 H HD23 . LEU B 1 134 ? -23.26517 6.05466  22.06820 1.000 14.70833  ? 131 LEU B HD23 1 
ATOM   5013 N N    . LEU B 1 135 ? -23.64305 7.12295  26.95840 1.000 11.60129  ? 132 LEU B N    1 
ATOM   5014 C CA   . LEU B 1 135 ? -23.46625 5.98090  27.84501 1.000 11.48145  ? 132 LEU B CA   1 
ATOM   5015 C C    . LEU B 1 135 ? -24.52720 5.94534  28.93138 1.000 12.55971  ? 132 LEU B C    1 
ATOM   5016 O O    . LEU B 1 135 ? -24.89863 4.86405  29.40023 1.000 15.96651  ? 132 LEU B O    1 
ATOM   5017 C CB   . LEU B 1 135 ? -22.08626 6.03104  28.49421 1.000 12.23050  ? 132 LEU B CB   1 
ATOM   5018 C CG   . LEU B 1 135 ? -20.89914 6.06695  27.53656 1.000 13.61802  ? 132 LEU B CG   1 
ATOM   5019 C CD1  . LEU B 1 135 ? -19.59568 6.02032  28.31811 1.000 15.42335  ? 132 LEU B CD1  1 
ATOM   5020 C CD2  . LEU B 1 135 ? -20.98064 4.92408  26.53522 1.000 15.00168  ? 132 LEU B CD2  1 
ATOM   5021 H H    . LEU B 1 135 ? -22.99813 7.69167  26.97374 1.000 13.92155  ? 132 LEU B H    1 
ATOM   5022 H HA   . LEU B 1 135 ? -23.53481 5.17088  27.31580 1.000 13.77774  ? 132 LEU B HA   1 
ATOM   5023 H HB2  . LEU B 1 135 ? -22.03823 6.83034  29.04167 1.000 14.67660  ? 132 LEU B HB2  1 
ATOM   5024 H HB3  . LEU B 1 135 ? -21.98408 5.24212  29.04925 1.000 14.67660  ? 132 LEU B HB3  1 
ATOM   5025 H HG   . LEU B 1 135 ? -20.91730 6.89550  27.03251 1.000 16.34163  ? 132 LEU B HG   1 
ATOM   5026 H HD11 . LEU B 1 135 ? -18.85506 5.96592  27.69407 1.000 18.50802  ? 132 LEU B HD11 1 
ATOM   5027 H HD12 . LEU B 1 135 ? -19.51912 6.82596  28.85289 1.000 18.50802  ? 132 LEU B HD12 1 
ATOM   5028 H HD13 . LEU B 1 135 ? -19.60070 5.24004  28.89434 1.000 18.50802  ? 132 LEU B HD13 1 
ATOM   5029 H HD21 . LEU B 1 135 ? -20.13534 4.85588  26.06436 1.000 18.00202  ? 132 LEU B HD21 1 
ATOM   5030 H HD22 . LEU B 1 135 ? -21.16127 4.09883  27.01191 1.000 18.00202  ? 132 LEU B HD22 1 
ATOM   5031 H HD23 . LEU B 1 135 ? -21.69606 5.10598  25.90594 1.000 18.00202  ? 132 LEU B HD23 1 
ATOM   5032 N N    . THR B 1 136 ? -25.00836 7.11033  29.35980 1.000 12.56278  ? 133 THR B N    1 
ATOM   5033 C CA   . THR B 1 136 ? -26.02504 7.19974  30.39753 1.000 14.12927  ? 133 THR B CA   1 
ATOM   5034 C C    . THR B 1 136 ? -27.37099 7.64516  29.84324 1.000 14.44961  ? 133 THR B C    1 
ATOM   5035 O O    . THR B 1 136 ? -28.25237 8.03467  30.61569 1.000 14.85766  ? 133 THR B O    1 
ATOM   5036 C CB   . THR B 1 136 ? -25.56967 8.13651  31.52035 1.000 16.61013  ? 133 THR B CB   1 
ATOM   5037 O OG1  . THR B 1 136 ? -25.23989 9.42144  30.98029 1.000 18.53943  ? 133 THR B OG1  1 
ATOM   5038 C CG2  . THR B 1 136 ? -24.35763 7.56209  32.23459 1.000 18.18336  ? 133 THR B CG2  1 
ATOM   5039 H H    . THR B 1 136 ? -24.75524 7.87463  29.05751 1.000 15.07533  ? 133 THR B H    1 
ATOM   5040 H HA   . THR B 1 136 ? -26.14274 6.32094  30.79093 1.000 16.95513  ? 133 THR B HA   1 
ATOM   5041 H HB   . THR B 1 136 ? -26.28731 8.23653  32.16525 1.000 19.93216  ? 133 THR B HB   1 
ATOM   5042 H HG1  . THR B 1 136 ? -25.90994 9.75248  30.59681 1.000 22.24732  ? 133 THR B HG1  1 
ATOM   5043 H HG21 . THR B 1 136 ? -23.97632 8.22749  32.82851 1.000 21.82003  ? 133 THR B HG21 1 
ATOM   5044 H HG22 . THR B 1 136 ? -24.61665 6.78623  32.75599 1.000 21.82003  ? 133 THR B HG22 1 
ATOM   5045 H HG23 . THR B 1 136 ? -23.68608 7.29631  31.58707 1.000 21.82003  ? 133 THR B HG23 1 
ATOM   5046 N N    . ASP B 1 137 ? -27.54784 7.59872  28.52625 1.000 12.50375  ? 134 ASP B N    1 
ATOM   5047 C CA   . ASP B 1 137 ? -28.80659 7.97296  27.89135 1.000 12.35488  ? 134 ASP B CA   1 
ATOM   5048 C C    . ASP B 1 137 ? -29.01115 7.07632  26.67630 1.000 12.34855  ? 134 ASP B C    1 
ATOM   5049 O O    . ASP B 1 137 ? -29.03545 7.56362  25.53883 1.000 12.11793  ? 134 ASP B O    1 
ATOM   5050 C CB   . ASP B 1 137 ? -28.75765 9.44810  27.49896 1.000 11.55488  ? 134 ASP B CB   1 
ATOM   5051 C CG   . ASP B 1 137 ? -30.07284 9.95787  26.93972 1.000 10.92887  ? 134 ASP B CG   1 
ATOM   5052 O OD1  . ASP B 1 137 ? -31.14474 9.40256  27.26434 1.000 10.72751  ? 134 ASP B OD1  1 
ATOM   5053 O OD2  . ASP B 1 137 ? -30.02743 10.93957 26.17178 1.000 12.04059  ? 134 ASP B OD2  1 
ATOM   5054 H H    . ASP B 1 137 ? -26.94268 7.34919  27.96847 1.000 15.00450  ? 134 ASP B H    1 
ATOM   5055 H HA   . ASP B 1 137 ? -29.56000 7.85214  28.49025 1.000 14.82585  ? 134 ASP B HA   1 
ATOM   5056 H HB2  . ASP B 1 137 ? -28.54218 9.97584  28.28379 1.000 13.86585  ? 134 ASP B HB2  1 
ATOM   5057 H HB3  . ASP B 1 137 ? -28.07647 9.57085  26.81938 1.000 13.86585  ? 134 ASP B HB3  1 
ATOM   5058 N N    . PRO B 1 138 ? -29.15233 5.76155  26.87624 1.000 13.34456  ? 135 PRO B N    1 
ATOM   5059 C CA   . PRO B 1 138 ? -29.25087 4.84899  25.72295 1.000 12.97810  ? 135 PRO B CA   1 
ATOM   5060 C C    . PRO B 1 138 ? -30.47480 5.06529  24.85036 1.000 13.65931  ? 135 PRO B C    1 
ATOM   5061 O O    . PRO B 1 138 ? -30.45490 4.65853  23.68120 1.000 14.13928  ? 135 PRO B O    1 
ATOM   5062 C CB   . PRO B 1 138 ? -29.26334 3.45477  26.37004 1.000 14.79167  ? 135 PRO B CB   1 
ATOM   5063 C CG   . PRO B 1 138 ? -29.74882 3.69277  27.76534 1.000 14.92063  ? 135 PRO B CG   1 
ATOM   5064 C CD   . PRO B 1 138 ? -29.19431 5.03595  28.15986 1.000 13.70511  ? 135 PRO B CD   1 
ATOM   5065 H HA   . PRO B 1 138 ? -28.45707 4.94272  25.17341 1.000 15.57371  ? 135 PRO B HA   1 
ATOM   5066 H HB2  . PRO B 1 138 ? -29.86653 2.86939  25.88591 1.000 17.75001  ? 135 PRO B HB2  1 
ATOM   5067 H HB3  . PRO B 1 138 ? -28.36816 3.08120  26.37112 1.000 17.75001  ? 135 PRO B HB3  1 
ATOM   5068 H HG2  . PRO B 1 138 ? -30.71868 3.70253  27.77875 1.000 17.90475  ? 135 PRO B HG2  1 
ATOM   5069 H HG3  . PRO B 1 138 ? -29.41589 2.99617  28.35253 1.000 17.90475  ? 135 PRO B HG3  1 
ATOM   5070 H HD2  . PRO B 1 138 ? -29.78030 5.48152  28.79152 1.000 16.44613  ? 135 PRO B HD2  1 
ATOM   5071 H HD3  . PRO B 1 138 ? -28.30535 4.94717  28.53770 1.000 16.44613  ? 135 PRO B HD3  1 
ATOM   5072 N N    . GLU B 1 139 ? -31.54362 5.66176  25.37320 1.000 15.13104  ? 136 GLU B N    1 
ATOM   5073 C CA   . GLU B 1 139 ? -32.71522 5.96354  24.56189 1.000 18.81454  ? 136 GLU B CA   1 
ATOM   5074 C C    . GLU B 1 139 ? -32.61805 7.32647  23.88772 1.000 14.39955  ? 136 GLU B C    1 
ATOM   5075 O O    . GLU B 1 139 ? -33.52818 7.70054  23.14199 1.000 16.36884  ? 136 GLU B O    1 
ATOM   5076 C CB   . GLU B 1 139 ? -33.99166 5.88781  25.40729 1.000 28.62110  ? 136 GLU B CB   1 
ATOM   5077 C CG   . GLU B 1 139 ? -34.13805 4.59297  26.19622 1.000 39.65280  ? 136 GLU B CG   1 
ATOM   5078 C CD   . GLU B 1 139 ? -34.02108 3.35349  25.32777 1.000 50.47723  ? 136 GLU B CD   1 
ATOM   5079 O OE1  . GLU B 1 139 ? -34.66202 3.31133  24.25675 1.000 57.49565  ? 136 GLU B OE1  1 
ATOM   5080 O OE2  . GLU B 1 139 ? -33.28036 2.42362  25.71402 1.000 52.28605  ? 136 GLU B OE2  1 
ATOM   5081 H H    . GLU B 1 139 ? -31.61218 5.90083  26.19645 1.000 18.15724  ? 136 GLU B H    1 
ATOM   5082 H HA   . GLU B 1 139 ? -32.79447 5.29021  23.86817 1.000 22.57745  ? 136 GLU B HA   1 
ATOM   5083 H HB2  . GLU B 1 139 ? -33.98767 6.62110  26.04224 1.000 34.34532  ? 136 GLU B HB2  1 
ATOM   5084 H HB3  . GLU B 1 139 ? -34.75900 5.96281  24.81868 1.000 34.34532  ? 136 GLU B HB3  1 
ATOM   5085 H HG2  . GLU B 1 139 ? -33.44071 4.55335  26.86930 1.000 47.58336  ? 136 GLU B HG2  1 
ATOM   5086 H HG3  . GLU B 1 139 ? -35.01009 4.57937  26.62079 1.000 47.58336  ? 136 GLU B HG3  1 
ATOM   5087 N N    . GLY B 1 140 ? -31.54668 8.07556  24.13407 1.000 12.87121  ? 137 GLY B N    1 
ATOM   5088 C CA   . GLY B 1 140 ? -31.39741 9.37777  23.51053 1.000 11.75081  ? 137 GLY B CA   1 
ATOM   5089 C C    . GLY B 1 140 ? -32.45508 10.37948 23.90991 1.000 10.98018  ? 137 GLY B C    1 
ATOM   5090 O O    . GLY B 1 140 ? -32.83229 11.23226 23.09865 1.000 11.16019  ? 137 GLY B O    1 
ATOM   5091 H H    . GLY B 1 140 ? -30.89957 7.85161  24.65436 1.000 15.44545  ? 137 GLY B H    1 
ATOM   5092 H HA2  . GLY B 1 140 ? -30.53258 9.74421  23.75278 1.000 14.10098  ? 137 GLY B HA2  1 
ATOM   5093 H HA3  . GLY B 1 140 ? -31.43637 9.27057  22.54726 1.000 14.10098  ? 137 GLY B HA3  1 
ATOM   5094 N N    . LYS B 1 141 ? -32.94437 10.31079 25.14675 1.000 10.44482  ? 138 LYS B N    1 
ATOM   5095 C CA   . LYS B 1 141 ? -33.94671 11.28133 25.56949 1.000 10.74386  ? 138 LYS B CA   1 
ATOM   5096 C C    . LYS B 1 141 ? -33.38531 12.69551 25.55729 1.000 10.34987  ? 138 LYS B C    1 
ATOM   5097 O O    . LYS B 1 141 ? -34.14126 13.65657 25.37967 1.000 10.73394  ? 138 LYS B O    1 
ATOM   5098 C CB   . LYS B 1 141 ? -34.49115 10.91489 26.94646 1.000 11.28513  ? 138 LYS B CB   1 
ATOM   5099 C CG   . LYS B 1 141 ? -35.15740 9.55009  26.96263 1.000 12.68696  ? 138 LYS B CG   1 
ATOM   5100 C CD   . LYS B 1 141 ? -35.78185 9.23221  28.30631 1.000 14.48663  ? 138 LYS B CD   1 
ATOM   5101 C CE   . LYS B 1 141 ? -36.28198 7.79758  28.33786 1.000 17.90494  ? 138 LYS B CE   1 
ATOM   5102 N NZ   . LYS B 1 141 ? -36.74214 7.38871  29.69326 1.000 22.21001  ? 138 LYS B NZ   1 
ATOM   5103 H H    . LYS B 1 141 ? -32.71963 9.73070  25.74054 1.000 12.53378  ? 138 LYS B H    1 
ATOM   5104 H HA   . LYS B 1 141 ? -34.69409 11.25599 24.95169 1.000 12.89263  ? 138 LYS B HA   1 
ATOM   5105 H HB2  . LYS B 1 141 ? -33.75937 10.90089 27.58302 1.000 13.54215  ? 138 LYS B HB2  1 
ATOM   5106 H HB3  . LYS B 1 141 ? -35.14986 11.57528 27.21270 1.000 13.54215  ? 138 LYS B HB3  1 
ATOM   5107 H HG2  . LYS B 1 141 ? -35.85795 9.52976  26.29202 1.000 15.22435  ? 138 LYS B HG2  1 
ATOM   5108 H HG3  . LYS B 1 141 ? -34.49372 8.86945  26.76982 1.000 15.22435  ? 138 LYS B HG3  1 
ATOM   5109 H HD2  . LYS B 1 141 ? -35.11988 9.34370  29.00650 1.000 17.38395  ? 138 LYS B HD2  1 
ATOM   5110 H HD3  . LYS B 1 141 ? -36.53372 9.82464  28.46322 1.000 17.38395  ? 138 LYS B HD3  1 
ATOM   5111 H HE2  . LYS B 1 141 ? -37.02924 7.70783  27.72593 1.000 21.48593  ? 138 LYS B HE2  1 
ATOM   5112 H HE3  . LYS B 1 141 ? -35.56231 7.20405  28.07198 1.000 21.48593  ? 138 LYS B HE3  1 
ATOM   5113 H HZ1  . LYS B 1 141 ? -36.05795 7.39710  30.26239 1.000 26.65202  ? 138 LYS B HZ1  1 
ATOM   5114 H HZ2  . LYS B 1 141 ? -37.36736 7.95097  29.98493 1.000 26.65202  ? 138 LYS B HZ2  1 
ATOM   5115 H HZ3  . LYS B 1 141 ? -37.08339 6.56726  29.66394 1.000 26.65202  ? 138 LYS B HZ3  1 
ATOM   5116 N N    . ASN B 1 142 ? -32.06924 12.84003 25.72597 1.000 10.44335  ? 139 ASN B N    1 
ATOM   5117 C CA   . ASN B 1 142 ? -31.39478 14.13279 25.68463 1.000 10.22796  ? 139 ASN B CA   1 
ATOM   5118 C C    . ASN B 1 142 ? -30.54567 14.31556 24.43501 1.000 11.10934  ? 139 ASN B C    1 
ATOM   5119 O O    . ASN B 1 142 ? -29.72300 15.23539 24.38211 1.000 12.39194  ? 139 ASN B O    1 
ATOM   5120 C CB   . ASN B 1 142 ? -30.56427 14.32249 26.95040 1.000 10.62446  ? 139 ASN B CB   1 
ATOM   5121 C CG   . ASN B 1 142 ? -31.43068 14.55058 28.16409 1.000 13.44002  ? 139 ASN B CG   1 
ATOM   5122 O OD1  . ASN B 1 142 ? -32.30861 15.41229 28.15410 1.000 15.93727  ? 139 ASN B OD1  1 
ATOM   5123 N ND2  . ASN B 1 142 ? -31.22045 13.75692 29.20164 1.000 11.63041  ? 139 ASN B ND2  1 
ATOM   5124 H H    . ASN B 1 142 ? -31.53297 12.18326 25.86974 1.000 12.53203  ? 139 ASN B H    1 
ATOM   5125 H HA   . ASN B 1 142 ? -32.06298 14.83574 25.66793 1.000 12.27355  ? 139 ASN B HA   1 
ATOM   5126 H HB2  . ASN B 1 142 ? -30.03022 13.52744 27.10395 1.000 12.74935  ? 139 ASN B HB2  1 
ATOM   5127 H HB3  . ASN B 1 142 ? -29.98669 15.09401 26.84061 1.000 12.74935  ? 139 ASN B HB3  1 
ATOM   5128 H HD21 . ASN B 1 142 ? -31.69029 13.84947 29.91598 1.000 13.95649  ? 139 ASN B HD21 1 
ATOM   5129 H HD22 . ASN B 1 142 ? -30.61396 13.14850 29.16169 1.000 13.95649  ? 139 ASN B HD22 1 
ATOM   5130 N N    . PHE B 1 143 ? -30.72823 13.46535 23.43552 1.000 10.05506  ? 140 PHE B N    1 
ATOM   5131 C CA   . PHE B 1 143 ? -30.10407 13.66634 22.13679 1.000 10.60589  ? 140 PHE B CA   1 
ATOM   5132 C C    . PHE B 1 143 ? -30.42828 15.07018 21.63368 1.000 12.62947  ? 140 PHE B C    1 
ATOM   5133 O O    . PHE B 1 143 ? -31.55678 15.54285 21.81552 1.000 13.58589  ? 140 PHE B O    1 
ATOM   5134 C CB   . PHE B 1 143 ? -30.67909 12.61579 21.17808 1.000 12.57596  ? 140 PHE B CB   1 
ATOM   5135 C CG   . PHE B 1 143 ? -30.24991 12.77130 19.74474 1.000 12.52666  ? 140 PHE B CG   1 
ATOM   5136 C CD1  . PHE B 1 143 ? -30.89900 13.66070 18.90083 1.000 14.02870  ? 140 PHE B CD1  1 
ATOM   5137 C CD2  . PHE B 1 143 ? -29.22864 11.99068 19.22545 1.000 13.42570  ? 140 PHE B CD2  1 
ATOM   5138 C CE1  . PHE B 1 143 ? -30.51523 13.78943 17.57770 1.000 14.65549  ? 140 PHE B CE1  1 
ATOM   5139 C CE2  . PHE B 1 143 ? -28.84442 12.11627 17.90220 1.000 14.33154  ? 140 PHE B CE2  1 
ATOM   5140 C CZ   . PHE B 1 143 ? -29.48777 13.01629 17.08076 1.000 14.30843  ? 140 PHE B CZ   1 
ATOM   5141 H H    . PHE B 1 143 ? -31.21340 12.75682 23.48249 1.000 12.06608  ? 140 PHE B H    1 
ATOM   5142 H HA   . PHE B 1 143 ? -29.13925 13.57805 22.18399 1.000 12.72707  ? 140 PHE B HA   1 
ATOM   5143 H HB2  . PHE B 1 143 ? -30.39276 11.73789 21.47508 1.000 15.09115  ? 140 PHE B HB2  1 
ATOM   5144 H HB3  . PHE B 1 143 ? -31.64704 12.67445 21.20112 1.000 15.09115  ? 140 PHE B HB3  1 
ATOM   5145 H HD1  . PHE B 1 143 ? -31.60024 14.17642 19.22823 1.000 16.83444  ? 140 PHE B HD1  1 
ATOM   5146 H HD2  . PHE B 1 143 ? -28.79675 11.37537 19.77296 1.000 16.11084  ? 140 PHE B HD2  1 
ATOM   5147 H HE1  . PHE B 1 143 ? -30.95012 14.39708 17.02405 1.000 17.58659  ? 140 PHE B HE1  1 
ATOM   5148 H HE2  . PHE B 1 143 ? -28.15212 11.59336 17.56726 1.000 17.19784  ? 140 PHE B HE2  1 
ATOM   5149 H HZ   . PHE B 1 143 ? -29.22899 13.10211 16.19162 1.000 17.17012  ? 140 PHE B HZ   1 
ATOM   5150 N N    . PRO B 1 144 ? -29.48214 15.76361 20.97556 1.000 12.90687  ? 141 PRO B N    1 
ATOM   5151 C CA   . PRO B 1 144 ? -28.12602 15.34678 20.58639 1.000 12.25414  ? 141 PRO B CA   1 
ATOM   5152 C C    . PRO B 1 144 ? -27.03788 15.66160 21.61653 1.000 11.87922  ? 141 PRO B C    1 
ATOM   5153 O O    . PRO B 1 144 ? -25.85529 15.72837 21.27724 1.000 13.18591  ? 141 PRO B O    1 
ATOM   5154 C CB   . PRO B 1 144 ? -27.90519 16.14075 19.28757 1.000 14.54561  ? 141 PRO B CB   1 
ATOM   5155 C CG   . PRO B 1 144 ? -28.59645 17.44639 19.57545 1.000 15.45268  ? 141 PRO B CG   1 
ATOM   5156 C CD   . PRO B 1 144 ? -29.82948 17.07074 20.38329 1.000 15.96149  ? 141 PRO B CD   1 
ATOM   5157 H HA   . PRO B 1 144 ? -28.12636 14.39053 20.42365 1.000 14.70497  ? 141 PRO B HA   1 
ATOM   5158 H HB2  . PRO B 1 144 ? -26.95746 16.26851 19.12516 1.000 17.45474  ? 141 PRO B HB2  1 
ATOM   5159 H HB3  . PRO B 1 144 ? -28.31161 15.68146 18.53606 1.000 17.45474  ? 141 PRO B HB3  1 
ATOM   5160 H HG2  . PRO B 1 144 ? -28.00967 18.02488 20.08724 1.000 18.54321  ? 141 PRO B HG2  1 
ATOM   5161 H HG3  . PRO B 1 144 ? -28.84545 17.87865 18.74356 1.000 18.54321  ? 141 PRO B HG3  1 
ATOM   5162 H HD2  . PRO B 1 144 ? -29.99792 17.72746 21.07700 1.000 19.15379  ? 141 PRO B HD2  1 
ATOM   5163 H HD3  . PRO B 1 144 ? -30.60552 16.99052 19.80691 1.000 19.15379  ? 141 PRO B HD3  1 
ATOM   5164 N N    . TRP B 1 145 ? -27.41524 15.87113 22.87882 1.000 13.54371  ? 142 TRP B N    1 
ATOM   5165 C CA   . TRP B 1 145 ? -26.46269 16.00230 23.98502 1.000 13.79662  ? 142 TRP B CA   1 
ATOM   5166 C C    . TRP B 1 145 ? -25.67020 17.30607 23.92111 1.000 15.70084  ? 142 TRP B C    1 
ATOM   5167 O O    . TRP B 1 145 ? -24.47455 17.33908 24.21570 1.000 16.33496  ? 142 TRP B O    1 
ATOM   5168 C CB   . TRP B 1 145 ? -25.54256 14.78297 24.08738 1.000 13.90757  ? 142 TRP B CB   1 
ATOM   5169 C CG   . TRP B 1 145 ? -26.31741 13.51673 24.15134 1.000 12.39357  ? 142 TRP B CG   1 
ATOM   5170 C CD1  . TRP B 1 145 ? -27.17978 13.13080 25.13787 1.000 12.61120  ? 142 TRP B CD1  1 
ATOM   5171 C CD2  . TRP B 1 145 ? -26.31621 12.46643 23.18523 1.000 12.52681  ? 142 TRP B CD2  1 
ATOM   5172 N NE1  . TRP B 1 145 ? -27.71579 11.90082 24.84280 1.000 12.07769  ? 142 TRP B NE1  1 
ATOM   5173 C CE2  . TRP B 1 145 ? -27.20041 11.47149 23.64814 1.000 12.01867  ? 142 TRP B CE2  1 
ATOM   5174 C CE3  . TRP B 1 145 ? -25.65268 12.26873 21.97243 1.000 12.57453  ? 142 TRP B CE3  1 
ATOM   5175 C CZ2  . TRP B 1 145 ? -27.43343 10.29663 22.94016 1.000 13.71499  ? 142 TRP B CZ2  1 
ATOM   5176 C CZ3  . TRP B 1 145 ? -25.88649 11.10287 21.27158 1.000 14.46724  ? 142 TRP B CZ3  1 
ATOM   5177 C CH2  . TRP B 1 145 ? -26.76856 10.13215 21.75581 1.000 13.44620  ? 142 TRP B CH2  1 
ATOM   5178 H H    . TRP B 1 145 ? -28.23575 15.94272 23.12629 1.000 16.25245  ? 142 TRP B H    1 
ATOM   5179 H HA   . TRP B 1 145 ? -26.97379 16.04551 24.80832 1.000 16.55594  ? 142 TRP B HA   1 
ATOM   5180 H HB2  . TRP B 1 145 ? -24.96724 14.74954 23.30713 1.000 16.68908  ? 142 TRP B HB2  1 
ATOM   5181 H HB3  . TRP B 1 145 ? -25.00603 14.85335 24.89242 1.000 16.68908  ? 142 TRP B HB3  1 
ATOM   5182 H HD1  . TRP B 1 145 ? -27.37560 13.62842 25.89875 1.000 15.13344  ? 142 TRP B HD1  1 
ATOM   5183 H HE1  . TRP B 1 145 ? -28.28137 11.47130 25.32781 1.000 14.49323  ? 142 TRP B HE1  1 
ATOM   5184 H HE3  . TRP B 1 145 ? -25.06486 12.90996 21.64349 1.000 15.08943  ? 142 TRP B HE3  1 
ATOM   5185 H HZ2  . TRP B 1 145 ? -28.01853 9.64818  23.25966 1.000 16.45798  ? 142 TRP B HZ2  1 
ATOM   5186 H HZ3  . TRP B 1 145 ? -25.44961 10.96050 20.46303 1.000 17.36069  ? 142 TRP B HZ3  1 
ATOM   5187 H HH2  . TRP B 1 145 ? -26.90654 9.35667  21.26136 1.000 16.13544  ? 142 TRP B HH2  1 
ATOM   5188 N N    . SER B 1 146 ? -26.35735 18.39357 23.58772 1.000 16.11570  ? 143 SER B N    1 
ATOM   5189 C CA   . SER B 1 146 ? -25.71313 19.68850 23.46240 1.000 22.51766  ? 143 SER B CA   1 
ATOM   5190 C C    . SER B 1 146 ? -25.25405 20.20612 24.82222 1.000 32.01142  ? 143 SER B C    1 
ATOM   5191 O O    . SER B 1 146 ? -25.69381 19.74230 25.87816 1.000 30.37621  ? 143 SER B O    1 
ATOM   5192 C CB   . SER B 1 146 ? -26.68033 20.69305 22.83901 1.000 22.20467  ? 143 SER B CB   1 
ATOM   5193 O OG   . SER B 1 146 ? -27.08332 20.26761 21.55023 1.000 23.43283  ? 143 SER B OG   1 
ATOM   5194 H H    . SER B 1 146 ? -27.20239 18.40551 23.42849 1.000 19.33884  ? 143 SER B H    1 
ATOM   5195 H HA   . SER B 1 146 ? -24.93280 19.60289 22.89262 1.000 27.02119  ? 143 SER B HA   1 
ATOM   5196 H HB2  . SER B 1 146 ? -27.46380 20.77104 23.40557 1.000 26.64560  ? 143 SER B HB2  1 
ATOM   5197 H HB3  . SER B 1 146 ? -26.23811 21.55312 22.76414 1.000 26.64560  ? 143 SER B HB3  1 
ATOM   5198 H HG   . SER B 1 146 ? -26.40894 20.13911 21.06618 1.000 28.11939  ? 143 SER B HG   1 
ATOM   5199 N N    . ASP B 1 147 ? -24.35555 21.19064 24.77237 1.000 42.69130  ? 144 ASP B N    1 
ATOM   5200 C CA   . ASP B 1 147 ? -23.79134 21.85108 25.95208 1.000 54.49019  ? 144 ASP B CA   1 
ATOM   5201 C C    . ASP B 1 147 ? -22.62125 21.04861 26.52065 1.000 57.29059  ? 144 ASP B C    1 
ATOM   5202 O O    . ASP B 1 147 ? -22.60187 20.70577 27.70386 1.000 57.97763  ? 144 ASP B O    1 
ATOM   5203 C CB   . ASP B 1 147 ? -24.85172 22.08682 27.03147 1.000 62.34752  ? 144 ASP B CB   1 
ATOM   5204 C CG   . ASP B 1 147 ? -26.12275 22.70197 26.47665 1.000 69.35269  ? 144 ASP B CG   1 
ATOM   5205 O OD1  . ASP B 1 147 ? -26.04813 23.39272 25.43885 1.000 71.84211  ? 144 ASP B OD1  1 
ATOM   5206 O OD2  . ASP B 1 147 ? -27.19829 22.48712 27.07535 1.000 71.26507  ? 144 ASP B OD2  1 
ATOM   5207 O OXT  . ASP B 1 147 ? -21.66883 20.72866 25.80583 1.000 58.18748  ? 144 ASP B OXT  1 
ATOM   5208 H H    . ASP B 1 147 ? -24.04292 21.50815 24.03682 1.000 51.22956  ? 144 ASP B H    1 
ATOM   5209 H HA   . ASP B 1 147 ? -23.46154 22.72320 25.68460 1.000 65.38823  ? 144 ASP B HA   1 
ATOM   5210 H HB2  . ASP B 1 147 ? -25.08222 21.23761 27.43965 1.000 74.81702  ? 144 ASP B HB2  1 
ATOM   5211 H HB3  . ASP B 1 147 ? -24.49325 22.69028 27.70098 1.000 74.81702  ? 144 ASP B HB3  1 
HETATM 5212 C C1   . GOL C 2 .   ? 25.92013  7.47304  22.31049 1.000 24.51588  ? 201 GOL A C1   1 
HETATM 5213 O O1   . GOL C 2 .   ? 26.80575  8.23073  21.52391 1.000 26.43744  ? 201 GOL A O1   1 
HETATM 5214 C C2   . GOL C 2 .   ? 25.00426  8.44540  23.11527 1.000 26.85888  ? 201 GOL A C2   1 
HETATM 5215 O O2   . GOL C 2 .   ? 24.74431  7.94836  24.38446 1.000 25.29403  ? 201 GOL A O2   1 
HETATM 5216 C C3   . GOL C 2 .   ? 25.72939  9.80205  23.12281 1.000 26.89510  ? 201 GOL A C3   1 
HETATM 5217 O O3   . GOL C 2 .   ? 25.12300  10.58925 24.10617 1.000 25.13484  ? 201 GOL A O3   1 
HETATM 5218 H H11  . GOL C 2 .   ? 26.38636  6.89498  22.93450 1.000 29.41905  ? 201 GOL A H11  1 
HETATM 5219 H H12  . GOL C 2 .   ? 25.36092  6.88925  21.77442 1.000 29.41905  ? 201 GOL A H12  1 
HETATM 5220 H HO1  . GOL C 2 .   ? 26.53739  8.16808  20.72467 1.000 31.72493  ? 201 GOL A HO1  1 
HETATM 5221 H H2   . GOL C 2 .   ? 24.14154  8.54865  22.68405 1.000 32.23065  ? 201 GOL A H2   1 
HETATM 5222 H H31  . GOL C 2 .   ? 25.67718  10.18919 22.23495 1.000 32.27412  ? 201 GOL A H31  1 
HETATM 5223 H H32  . GOL C 2 .   ? 26.67430  9.65042  23.28112 1.000 32.27412  ? 201 GOL A H32  1 
HETATM 5224 H HO3  . GOL C 2 .   ? 25.34307  11.39342 23.94751 1.000 30.16180  ? 201 GOL A HO3  1 
HETATM 5225 O O    . HOH D 3 .   ? 27.63886  -1.27496 16.24011 1.000 33.21686  ? 301 HOH A O    1 
HETATM 5226 O O    . HOH D 3 .   ? 22.24409  22.66224 12.04338 1.000 38.04975  ? 302 HOH A O    1 
HETATM 5227 O O    . HOH D 3 .   ? 19.196    9.105    8.088    1.000 38.25417  ? 303 HOH A O    1 
HETATM 5228 O O    . HOH D 3 .   ? 12.47579  1.06975  15.25565 1.000 25.97383  ? 304 HOH A O    1 
HETATM 5229 O O    . HOH D 3 .   ? 3.68724   2.47724  30.49787 1.000 25.57896  ? 305 HOH A O    1 
HETATM 5230 O O    . HOH D 3 .   ? 0.28922   10.43642 29.11512 1.000 21.91331  ? 306 HOH A O    1 
HETATM 5231 O O    . HOH D 3 .   ? 8.98298   14.04105 4.17153  1.000 36.54544  ? 307 HOH A O    1 
HETATM 5232 O O    . HOH D 3 .   ? 12.64374  22.51436 40.28811 1.000 42.20818  ? 308 HOH A O    1 
HETATM 5233 O O    . HOH D 3 .   ? 13.134    -0.988   17.109   1.000 22.31471  ? 309 HOH A O    1 
HETATM 5234 O O    A HOH D 3 .   ? 12.77953  27.34844 30.01030 0.634 40.11192  ? 310 HOH A O    1 
HETATM 5235 O O    B HOH D 3 .   ? 12.33625  27.70886 28.51888 0.366 40.18246  ? 310 HOH A O    1 
HETATM 5236 O O    . HOH D 3 .   ? -3.27639  11.77513 10.76713 1.000 21.99929  ? 311 HOH A O    1 
HETATM 5237 O O    . HOH D 3 .   ? -0.92897  7.02356  6.26938  1.000 22.02878  ? 312 HOH A O    1 
HETATM 5238 O O    . HOH D 3 .   ? -5.36743  10.76471 7.76762  1.000 15.28307  ? 313 HOH A O    1 
HETATM 5239 O O    . HOH D 3 .   ? 16.90137  5.55960  10.91165 1.000 26.22261  ? 314 HOH A O    1 
HETATM 5240 O O    . HOH D 3 .   ? 13.139    6.633    40.550   1.000 36.92851  ? 315 HOH A O    1 
HETATM 5241 O O    . HOH D 3 .   ? 12.63512  9.36606  9.80051  1.000 14.53723  ? 316 HOH A O    1 
HETATM 5242 O O    . HOH D 3 .   ? 22.66082  0.61400  24.31169 1.000 41.02174  ? 317 HOH A O    1 
HETATM 5243 O O    . HOH D 3 .   ? 23.00028  13.31326 11.66702 1.000 24.95347  ? 318 HOH A O    1 
HETATM 5244 O O    . HOH D 3 .   ? 23.00145  21.31027 29.66709 1.000 42.25294  ? 319 HOH A O    1 
HETATM 5245 O O    . HOH D 3 .   ? 19.19844  7.28858  10.35912 1.000 21.69300  ? 320 HOH A O    1 
HETATM 5246 O O    . HOH D 3 .   ? -4.35107  2.53926  22.25429 0.487 16.35298  ? 321 HOH A O    1 
HETATM 5247 O O    . HOH D 3 .   ? 2.88473   20.26739 16.12181 1.000 17.91147  ? 322 HOH A O    1 
HETATM 5248 O O    . HOH D 3 .   ? 23.75179  9.80733  20.01150 1.000 21.48816  ? 323 HOH A O    1 
HETATM 5249 O O    . HOH D 3 .   ? 15.04661  25.88034 24.87278 1.000 16.58735  ? 324 HOH A O    1 
HETATM 5250 O O    . HOH D 3 .   ? 15.70099  3.45015  4.86811  1.000 33.16061  ? 325 HOH A O    1 
HETATM 5251 O O    . HOH D 3 .   ? 16.003    28.847   26.378   1.000 21.96928  ? 326 HOH A O    1 
HETATM 5252 O O    . HOH D 3 .   ? -8.42431  24.00278 18.91943 1.000 26.90932  ? 327 HOH A O    1 
HETATM 5253 O O    A HOH D 3 .   ? -6.880    21.734   7.529    0.425 25.25201  ? 328 HOH A O    1 
HETATM 5254 O O    B HOH D 3 .   ? -9.440    24.582   3.508    0.575 27.75506  ? 328 HOH A O    1 
HETATM 5255 O O    . HOH D 3 .   ? 7.06877   20.93236 3.90365  1.000 30.83439  ? 329 HOH A O    1 
HETATM 5256 O O    . HOH D 3 .   ? -2.38363  22.61006 12.04790 1.000 12.53662  ? 330 HOH A O    1 
HETATM 5257 O O    . HOH D 3 .   ? 13.33573  2.80269  33.36146 1.000 42.33300  ? 331 HOH A O    1 
HETATM 5258 O O    . HOH D 3 .   ? 18.68795  8.14701  28.95587 1.000 14.40682  ? 332 HOH A O    1 
HETATM 5259 O O    . HOH D 3 .   ? 17.053    10.055   40.849   1.000 28.85664  ? 333 HOH A O    1 
HETATM 5260 O O    . HOH D 3 .   ? -2.94864  26.52276 15.73429 1.000 24.10280  ? 334 HOH A O    1 
HETATM 5261 O O    . HOH D 3 .   ? -5.65383  16.44469 26.13748 1.000 24.48285  ? 335 HOH A O    1 
HETATM 5262 O O    . HOH D 3 .   ? -5.07829  18.14591 5.92066  1.000 13.43048  ? 336 HOH A O    1 
HETATM 5263 O O    . HOH D 3 .   ? 14.67328  23.02685 17.44481 1.000 18.69136  ? 337 HOH A O    1 
HETATM 5264 O O    . HOH D 3 .   ? 0.49824   14.68987 37.13113 1.000 26.13348  ? 338 HOH A O    1 
HETATM 5265 O O    . HOH D 3 .   ? 11.070    7.078    2.369    1.000 28.53710  ? 339 HOH A O    1 
HETATM 5266 O O    . HOH D 3 .   ? 9.954     26.168   12.865   1.000 17.87384  ? 340 HOH A O    1 
HETATM 5267 O O    . HOH D 3 .   ? 23.49350  4.69389  26.32857 1.000 33.74133  ? 341 HOH A O    1 
HETATM 5268 O O    . HOH D 3 .   ? 8.01797   23.08203 7.61711  1.000 18.22618  ? 342 HOH A O    1 
HETATM 5269 O O    . HOH D 3 .   ? 6.04755   24.39972 33.80398 1.000 35.90033  ? 343 HOH A O    1 
HETATM 5270 O O    . HOH D 3 .   ? 8.74519   23.56796 34.84427 1.000 33.43933  ? 344 HOH A O    1 
HETATM 5271 O O    A HOH D 3 .   ? 24.01545  13.41892 26.72273 0.533 12.62550  ? 345 HOH A O    1 
HETATM 5272 O O    B HOH D 3 .   ? 23.34998  13.66855 26.37799 0.467 16.64636  ? 345 HOH A O    1 
HETATM 5273 O O    . HOH D 3 .   ? 2.33484   22.13221 32.35855 1.000 20.16414  ? 346 HOH A O    1 
HETATM 5274 O O    . HOH D 3 .   ? 20.93576  21.70788 34.51792 1.000 21.73770  ? 347 HOH A O    1 
HETATM 5275 O O    . HOH D 3 .   ? 12.85009  24.81475 16.40116 1.000 13.70317  ? 348 HOH A O    1 
HETATM 5276 O O    . HOH D 3 .   ? 21.49018  14.27518 24.93540 1.000 20.21027  ? 349 HOH A O    1 
HETATM 5277 O O    . HOH D 3 .   ? 9.90015   24.55900 10.77639 1.000 28.28974  ? 350 HOH A O    1 
HETATM 5278 O O    . HOH D 3 .   ? -1.23571  21.15942 29.79111 1.000 18.99542  ? 351 HOH A O    1 
HETATM 5279 O O    . HOH D 3 .   ? 15.70447  15.49697 46.28599 1.000 32.23334  ? 352 HOH A O    1 
HETATM 5280 O O    . HOH D 3 .   ? 5.89989   12.23828 38.97127 1.000 15.37949  ? 353 HOH A O    1 
HETATM 5281 O O    . HOH D 3 .   ? 0.28357   7.38407  27.13862 1.000 25.58967  ? 354 HOH A O    1 
HETATM 5282 O O    . HOH D 3 .   ? 16.86053  4.45801  26.90483 1.000 25.24702  ? 355 HOH A O    1 
HETATM 5283 O O    . HOH D 3 .   ? 5.29324   22.01020 15.07229 1.000 26.84817  ? 356 HOH A O    1 
HETATM 5284 O O    . HOH D 3 .   ? -0.338    29.891   5.777    1.000 35.17106  ? 357 HOH A O    1 
HETATM 5285 O O    . HOH D 3 .   ? 12.18645  21.05732 34.86571 1.000 13.70438  ? 358 HOH A O    1 
HETATM 5286 O O    . HOH D 3 .   ? -2.62886  14.50558 27.76236 1.000 15.72712  ? 359 HOH A O    1 
HETATM 5287 O O    A HOH D 3 .   ? 5.77373   14.09066 43.08254 0.543 15.20137  ? 360 HOH A O    1 
HETATM 5288 O O    B HOH D 3 .   ? -28.28325 13.23602 29.24660 0.457 15.31295  ? 360 HOH A O    1 
HETATM 5289 O O    . HOH D 3 .   ? 19.32490  18.20770 19.41614 1.000 25.48289  ? 361 HOH A O    1 
HETATM 5290 O O    . HOH D 3 .   ? 0.69636   10.97428 14.64049 1.000 11.41407  ? 362 HOH A O    1 
HETATM 5291 O O    . HOH D 3 .   ? 2.71803   1.45575  12.17514 1.000 32.51677  ? 363 HOH A O    1 
HETATM 5292 O O    . HOH D 3 .   ? 2.00593   27.68907 21.96847 1.000 19.05892  ? 364 HOH A O    1 
HETATM 5293 O O    . HOH D 3 .   ? 9.94592   26.75632 29.30695 1.000 16.42981  ? 365 HOH A O    1 
HETATM 5294 O O    . HOH D 3 .   ? 2.24140   23.06429 3.11719  1.000 32.88883  ? 366 HOH A O    1 
HETATM 5295 O O    . HOH D 3 .   ? -0.26818  14.10047 11.88724 1.000 11.63719  ? 367 HOH A O    1 
HETATM 5296 O O    . HOH D 3 .   ? 24.99772  3.21459  22.15523 1.000 27.80482  ? 368 HOH A O    1 
HETATM 5297 O O    . HOH D 3 .   ? 26.14755  13.09621 23.43691 1.000 26.99359  ? 369 HOH A O    1 
HETATM 5298 O O    . HOH D 3 .   ? 17.31412  22.38111 38.76024 1.000 38.27435  ? 370 HOH A O    1 
HETATM 5299 O O    . HOH D 3 .   ? 0.87749   8.79134  36.02886 1.000 29.62421  ? 371 HOH A O    1 
HETATM 5300 O O    . HOH D 3 .   ? 21.98241  18.67144 31.34578 1.000 17.70453  ? 372 HOH A O    1 
HETATM 5301 O O    . HOH D 3 .   ? 6.56344   16.46157 13.61039 1.000 8.23946   ? 373 HOH A O    1 
HETATM 5302 O O    . HOH D 3 .   ? 7.59737   26.15747 5.62284  1.000 25.28495  ? 374 HOH A O    1 
HETATM 5303 O O    . HOH D 3 .   ? 1.77375   28.20074 15.37438 1.000 18.84188  ? 375 HOH A O    1 
HETATM 5304 O O    . HOH D 3 .   ? 8.90101   2.12163  9.05705  1.000 35.91692  ? 376 HOH A O    1 
HETATM 5305 O O    . HOH D 3 .   ? 20.35081  23.97320 27.89628 1.000 35.31015  ? 377 HOH A O    1 
HETATM 5306 O O    . HOH D 3 .   ? 6.21645   3.08348  13.44457 1.000 19.95865  ? 378 HOH A O    1 
HETATM 5307 O O    . HOH D 3 .   ? 13.80625  24.38784 11.75533 1.000 28.74970  ? 379 HOH A O    1 
HETATM 5308 O O    . HOH D 3 .   ? 8.846     27.722   24.363   1.000 9.61676   ? 380 HOH A O    1 
HETATM 5309 O O    . HOH D 3 .   ? 19.70252  15.42694 22.92650 1.000 17.46789  ? 381 HOH A O    1 
HETATM 5310 O O    . HOH D 3 .   ? 6.68916   8.92569  28.83527 1.000 8.64938   ? 382 HOH A O    1 
HETATM 5311 O O    . HOH D 3 .   ? 7.77381   19.82898 35.63195 1.000 15.09790  ? 383 HOH A O    1 
HETATM 5312 O O    . HOH D 3 .   ? 19.72791  3.79383  23.76222 1.000 35.73819  ? 384 HOH A O    1 
HETATM 5313 O O    . HOH D 3 .   ? 20.18243  13.78075 19.86299 1.000 19.32563  ? 385 HOH A O    1 
HETATM 5314 O O    . HOH D 3 .   ? -2.58715  6.14354  12.45660 1.000 12.32589  ? 386 HOH A O    1 
HETATM 5315 O O    . HOH D 3 .   ? 2.25855   3.05408  23.72291 1.000 18.78008  ? 387 HOH A O    1 
HETATM 5316 O O    . HOH D 3 .   ? 20.39335  14.72358 35.85258 0.660 16.54850  ? 388 HOH A O    1 
HETATM 5317 O O    . HOH D 3 .   ? 15.50392  2.94080  8.47950  1.000 31.46472  ? 389 HOH A O    1 
HETATM 5318 O O    . HOH D 3 .   ? 18.87305  4.66320  13.24085 1.000 32.17536  ? 390 HOH A O    1 
HETATM 5319 O O    . HOH D 3 .   ? -7.03262  3.28820  26.22888 1.000 39.76009  ? 391 HOH A O    1 
HETATM 5320 O O    . HOH D 3 .   ? 5.08214   5.25746  31.96723 1.000 14.56470  ? 392 HOH A O    1 
HETATM 5321 O O    . HOH D 3 .   ? 9.60612   21.13025 33.89454 1.000 13.34394  ? 393 HOH A O    1 
HETATM 5322 O O    . HOH D 3 .   ? 21.72010  22.89042 30.97295 1.000 49.25911  ? 394 HOH A O    1 
HETATM 5323 O O    . HOH D 3 .   ? 21.56106  -0.27152 18.19991 1.000 25.74361  ? 395 HOH A O    1 
HETATM 5324 O O    . HOH D 3 .   ? -4.71495  28.13139 25.58951 1.000 32.14101  ? 396 HOH A O    1 
HETATM 5325 O O    . HOH D 3 .   ? 11.45928  16.78370 40.97484 1.000 13.52510  ? 397 HOH A O    1 
HETATM 5326 O O    . HOH D 3 .   ? 2.86807   10.73723 28.13753 1.000 8.44698   ? 398 HOH A O    1 
HETATM 5327 O O    . HOH D 3 .   ? 12.39143  23.21792 36.60760 1.000 30.60927  ? 399 HOH A O    1 
HETATM 5328 O O    A HOH D 3 .   ? 6.86020   5.80392  11.52163 0.584 17.90283  ? 400 HOH A O    1 
HETATM 5329 O O    B HOH D 3 .   ? 7.18747   4.44816  12.23142 0.416 22.13385  ? 400 HOH A O    1 
HETATM 5330 O O    . HOH D 3 .   ? -1.46948  8.69033  25.91893 1.000 35.53756  ? 401 HOH A O    1 
HETATM 5331 O O    . HOH D 3 .   ? 9.41643   17.74342 1.90905  1.000 32.31546  ? 402 HOH A O    1 
HETATM 5332 O O    . HOH D 3 .   ? 6.84197   1.74297  31.34293 1.000 26.29651  ? 403 HOH A O    1 
HETATM 5333 O O    . HOH D 3 .   ? 2.58112   26.42035 30.89810 1.000 29.04461  ? 404 HOH A O    1 
HETATM 5334 O O    . HOH D 3 .   ? 2.448     -1.906   17.969   1.000 16.96781  ? 405 HOH A O    1 
HETATM 5335 O O    A HOH D 3 .   ? 18.963    22.999   21.044   0.482 28.60727  ? 406 HOH A O    1 
HETATM 5336 O O    B HOH D 3 .   ? 19.216    22.059   22.522   0.518 29.92481  ? 406 HOH A O    1 
HETATM 5337 O O    . HOH D 3 .   ? 15.97066  6.07654  30.46955 1.000 37.43378  ? 407 HOH A O    1 
HETATM 5338 O O    . HOH D 3 .   ? -2.13885  4.62024  24.54570 1.000 36.71792  ? 408 HOH A O    1 
HETATM 5339 O O    . HOH D 3 .   ? 9.54252   -2.52279 26.89858 1.000 16.41483  ? 409 HOH A O    1 
HETATM 5340 O O    . HOH D 3 .   ? 0.59800   30.64074 21.32241 1.000 24.61610  ? 410 HOH A O    1 
HETATM 5341 O O    . HOH D 3 .   ? 2.89346   15.41325 2.32482  1.000 25.31119  ? 411 HOH A O    1 
HETATM 5342 O O    . HOH D 3 .   ? -4.41687  17.08896 28.83199 1.000 20.87102  ? 412 HOH A O    1 
HETATM 5343 O O    . HOH D 3 .   ? 3.67684   26.11738 23.70527 1.000 13.97657  ? 413 HOH A O    1 
HETATM 5344 O O    . HOH D 3 .   ? -2.02039  28.86870 24.84394 1.000 36.78160  ? 414 HOH A O    1 
HETATM 5345 O O    . HOH D 3 .   ? 13.32874  -4.04287 22.57703 1.000 16.76903  ? 415 HOH A O    1 
HETATM 5346 O O    . HOH D 3 .   ? -6.02207  11.91856 11.45260 1.000 13.99035  ? 416 HOH A O    1 
HETATM 5347 O O    . HOH D 3 .   ? 0.51139   20.26537 31.47367 1.000 16.84189  ? 417 HOH A O    1 
HETATM 5348 O O    . HOH D 3 .   ? 2.18621   28.41901 26.27539 1.000 29.52159  ? 418 HOH A O    1 
HETATM 5349 O O    . HOH D 3 .   ? 0.09839   23.57109 4.87304  1.000 21.91852  ? 419 HOH A O    1 
HETATM 5350 O O    A HOH D 3 .   ? 5.88864   10.00620 5.49693  0.582 12.76397  ? 420 HOH A O    1 
HETATM 5351 O O    B HOH D 3 .   ? 6.50275   9.63627  5.69353  0.418 14.07771  ? 420 HOH A O    1 
HETATM 5352 O O    A HOH D 3 .   ? 3.77896   31.38081 23.37278 0.688 13.92518  ? 421 HOH A O    1 
HETATM 5353 O O    B HOH D 3 .   ? 2.53003   31.68251 22.65043 0.312 17.81499  ? 421 HOH A O    1 
HETATM 5354 O O    . HOH D 3 .   ? 21.47354  14.72057 17.05647 1.000 33.32442  ? 422 HOH A O    1 
HETATM 5355 O O    . HOH D 3 .   ? 8.32086   19.22399 5.58783  1.000 15.03478  ? 423 HOH A O    1 
HETATM 5356 O O    . HOH D 3 .   ? -5.87991  23.52138 9.73814  1.000 25.63358  ? 424 HOH A O    1 
HETATM 5357 O O    . HOH D 3 .   ? 9.10535   20.50170 7.96414  1.000 15.28208  ? 425 HOH A O    1 
HETATM 5358 O O    . HOH D 3 .   ? -1.38179  11.37006 27.56214 1.000 35.18586  ? 426 HOH A O    1 
HETATM 5359 O O    . HOH D 3 .   ? 7.78757   17.63388 43.02375 1.000 34.85813  ? 427 HOH A O    1 
HETATM 5360 O O    A HOH D 3 .   ? 0.36351   27.02436 6.14570  0.432 25.32713  ? 428 HOH A O    1 
HETATM 5361 O O    B HOH D 3 .   ? -4.64965  24.48853 12.29477 0.568 25.30794  ? 428 HOH A O    1 
HETATM 5362 O O    . HOH D 3 .   ? -0.22379  6.49363  36.83744 1.000 36.36823  ? 429 HOH A O    1 
HETATM 5363 O O    . HOH D 3 .   ? 19.66157  4.75826  26.53045 1.000 31.67871  ? 430 HOH A O    1 
HETATM 5364 O O    . HOH D 3 .   ? 7.38074   -0.25056 29.19455 1.000 41.79768  ? 431 HOH A O    1 
HETATM 5365 O O    . HOH D 3 .   ? 15.82971  22.89600 9.08516  1.000 38.54987  ? 432 HOH A O    1 
HETATM 5366 O O    A HOH D 3 .   ? 3.29281   11.01513 3.44620  0.576 16.70173  ? 433 HOH A O    1 
HETATM 5367 O O    B HOH D 3 .   ? 4.20484   10.71286 3.69660  0.424 18.03948  ? 433 HOH A O    1 
HETATM 5368 O O    . HOH D 3 .   ? 11.40834  5.21781  36.06796 1.000 26.63400  ? 434 HOH A O    1 
HETATM 5369 O O    . HOH D 3 .   ? 8.87015   5.66371  37.69673 1.000 28.58528  ? 435 HOH A O    1 
HETATM 5370 O O    . HOH D 3 .   ? 22.13692  1.37965  13.25442 1.000 30.72892  ? 436 HOH A O    1 
HETATM 5371 O O    . HOH D 3 .   ? 5.93878   21.38574 36.98477 1.000 32.04774  ? 437 HOH A O    1 
HETATM 5372 O O    A HOH D 3 .   ? -2.89418  6.97795  24.28653 0.714 17.48478  ? 438 HOH A O    1 
HETATM 5373 O O    B HOH D 3 .   ? -2.29812  8.30781  24.18546 0.286 11.28522  ? 438 HOH A O    1 
HETATM 5374 O O    . HOH D 3 .   ? 20.76665  19.89699 29.00969 1.000 18.47905  ? 439 HOH A O    1 
HETATM 5375 O O    . HOH D 3 .   ? 20.75975  6.81861  27.85668 1.000 22.56474  ? 440 HOH A O    1 
HETATM 5376 O O    . HOH D 3 .   ? -5.31424  14.51920 27.14653 1.000 33.22351  ? 441 HOH A O    1 
HETATM 5377 O O    . HOH D 3 .   ? -1.06967  -0.26661 18.98152 1.000 31.29888  ? 442 HOH A O    1 
HETATM 5378 O O    A HOH D 3 .   ? 16.89846  9.71122  36.56103 0.578 28.32287  ? 443 HOH A O    1 
HETATM 5379 O O    B HOH D 3 .   ? 17.28889  10.13708 35.88344 0.422 25.58922  ? 443 HOH A O    1 
HETATM 5380 O O    . HOH D 3 .   ? 20.39330  11.19204 35.85262 0.50  28.08505  ? 444 HOH A O    1 
HETATM 5381 O O    . HOH D 3 .   ? 11.14019  0.53161  31.22173 1.000 40.81969  ? 445 HOH A O    1 
HETATM 5382 O O    . HOH D 3 .   ? -0.74254  18.60377 5.61551  1.000 29.05571  ? 446 HOH A O    1 
HETATM 5383 O O    . HOH D 3 .   ? 4.97097   30.61425 11.23598 1.000 33.05607  ? 447 HOH A O    1 
HETATM 5384 O O    . HOH D 3 .   ? 17.38689  21.54654 17.44546 1.000 33.37713  ? 448 HOH A O    1 
HETATM 5385 O O    . HOH D 3 .   ? 10.915    5.315    41.477   1.000 35.78302  ? 449 HOH A O    1 
HETATM 5386 O O    A HOH D 3 .   ? 24.56563  15.21426 22.54838 0.556 31.96003  ? 450 HOH A O    1 
HETATM 5387 O O    B HOH D 3 .   ? 24.69740  14.06077 21.75169 0.444 33.72551  ? 450 HOH A O    1 
HETATM 5388 O O    . HOH D 3 .   ? 21.06102  2.35066  25.25748 1.000 35.65552  ? 451 HOH A O    1 
HETATM 5389 O O    . HOH D 3 .   ? 15.57071  0.34360  28.16187 1.000 34.83416  ? 452 HOH A O    1 
HETATM 5390 O O    . HOH D 3 .   ? 16.55940  2.52965  28.66961 1.000 29.30699  ? 453 HOH A O    1 
HETATM 5391 O O    A HOH D 3 .   ? 5.64089   29.77235 8.30593  0.537 25.45075  ? 454 HOH A O    1 
HETATM 5392 O O    B HOH D 3 .   ? 1.46206   32.40633 9.91973  0.463 25.09677  ? 454 HOH A O    1 
HETATM 5393 O O    . HOH D 3 .   ? 7.25554   7.41099  37.49123 1.000 27.18535  ? 455 HOH A O    1 
HETATM 5394 O O    . HOH D 3 .   ? 7.04411   0.67110  12.10257 1.000 36.42005  ? 456 HOH A O    1 
HETATM 5395 O O    . HOH D 3 .   ? 12.36042  -0.65377 28.89309 1.000 34.80009  ? 457 HOH A O    1 
HETATM 5396 O O    . HOH D 3 .   ? -3.18517  26.58914 27.91778 1.000 40.61305  ? 458 HOH A O    1 
HETATM 5397 O O    A HOH D 3 .   ? -0.90492  9.94958  5.30054  0.498 27.05499  ? 459 HOH A O    1 
HETATM 5398 O O    B HOH D 3 .   ? -1.64454  11.10418 5.90179  0.502 26.64984  ? 459 HOH A O    1 
HETATM 5399 O O    A HOH D 3 .   ? 0.78589   27.25414 19.56224 0.578 14.10682  ? 460 HOH A O    1 
HETATM 5400 O O    B HOH D 3 .   ? -0.24216  27.70700 19.42121 0.422 15.01162  ? 460 HOH A O    1 
HETATM 5401 O O    . HOH D 3 .   ? 24.53088  15.09712 8.67768  1.000 40.40158  ? 461 HOH A O    1 
HETATM 5402 O O    . HOH D 3 .   ? -2.54739  6.21117  35.17836 1.000 41.09490  ? 462 HOH A O    1 
HETATM 5403 O O    . HOH D 3 .   ? -1.31064  -1.41056 15.61048 1.000 43.00364  ? 463 HOH A O    1 
HETATM 5404 O O    . HOH D 3 .   ? 1.39887   19.63417 38.96765 1.000 38.47120  ? 464 HOH A O    1 
HETATM 5405 O O    . HOH D 3 .   ? 18.56084  -1.87719 27.48437 1.000 36.49155  ? 465 HOH A O    1 
HETATM 5406 O O    . HOH D 3 .   ? 1.17280   30.16064 13.49161 0.702 18.48470  ? 466 HOH A O    1 
HETATM 5407 O O    . HOH D 3 .   ? -3.98346  1.37295  24.80145 1.000 40.62240  ? 467 HOH A O    1 
HETATM 5408 O O    . HOH D 3 .   ? 6.54679   21.64498 39.70603 1.000 44.20753  ? 468 HOH A O    1 
HETATM 5409 O O    . HOH D 3 .   ? 18.86939  25.48644 31.88038 1.000 40.83242  ? 469 HOH A O    1 
HETATM 5410 O O    . HOH D 3 .   ? 5.66140   5.23732  7.03936  1.000 32.15982  ? 470 HOH A O    1 
HETATM 5411 O O    . HOH D 3 .   ? 7.24134   4.87661  9.05352  1.000 26.65957  ? 471 HOH A O    1 
HETATM 5412 O O    . HOH D 3 .   ? -3.385    30.955   22.610   1.000 34.71069  ? 472 HOH A O    1 
HETATM 5413 O O    . HOH D 3 .   ? -1.12844  27.92837 27.31887 1.000 36.60583  ? 473 HOH A O    1 
HETATM 5414 O O    . HOH D 3 .   ? 7.08364   7.14193  5.34547  1.000 35.58139  ? 474 HOH A O    1 
HETATM 5415 O O    . HOH D 3 .   ? -3.21019  9.26604  28.05203 1.000 36.30206  ? 475 HOH A O    1 
HETATM 5416 O O    . HOH D 3 .   ? -2.65338  17.91022 33.58682 1.000 38.40579  ? 476 HOH A O    1 
HETATM 5417 O O    . HOH D 3 .   ? 0.88829   29.20018 23.89989 1.000 21.07003  ? 477 HOH A O    1 
HETATM 5418 O O    . HOH D 3 .   ? -3.46035  3.06936  25.89022 1.000 46.08583  ? 478 HOH A O    1 
HETATM 5419 O O    . HOH D 3 .   ? 5.95055   1.44196  29.39181 1.000 41.23390  ? 479 HOH A O    1 
HETATM 5420 O O    . HOH D 3 .   ? 0.54934   4.35095  25.59133 1.000 27.92619  ? 480 HOH A O    1 
HETATM 5421 O O    . HOH D 3 .   ? -6.84389  27.55017 26.58284 1.000 37.72114  ? 481 HOH A O    1 
HETATM 5422 O O    A HOH D 3 .   ? 18.509    25.155   21.748   0.682 30.75913  ? 482 HOH A O    1 
HETATM 5423 O O    B HOH D 3 .   ? 18.755    24.089   23.082   0.318 31.72062  ? 482 HOH A O    1 
HETATM 5424 O O    . HOH D 3 .   ? 12.482    25.839   13.966   1.000 21.88911  ? 483 HOH A O    1 
HETATM 5425 O O    . HOH D 3 .   ? 18.38961  8.66144  34.25892 1.000 40.96555  ? 484 HOH A O    1 
HETATM 5426 O O    . HOH D 3 .   ? 17.622    25.082   24.724   1.000 20.23086  ? 485 HOH A O    1 
HETATM 5427 O O    . HOH D 3 .   ? -5.45447  11.08490 29.09499 1.000 38.94680  ? 486 HOH A O    1 
HETATM 5428 O O    . HOH D 3 .   ? 20.67057  17.39180 17.20702 1.000 38.06910  ? 487 HOH A O    1 
HETATM 5429 O O    . HOH D 3 .   ? 18.51481  22.60675 25.11819 1.000 43.75497  ? 488 HOH A O    1 
HETATM 5430 O O    . HOH D 3 .   ? 6.03922   27.56345 24.51743 1.000 13.78353  ? 489 HOH A O    1 
HETATM 5431 O O    . HOH D 3 .   ? 8.622     -1.780   30.903   1.000 30.85560  ? 490 HOH A O    1 
HETATM 5432 O O    . HOH D 3 .   ? 18.10772  6.93528  31.83761 1.000 44.67854  ? 491 HOH A O    1 
HETATM 5433 O O    . HOH D 3 .   ? 0.74639   28.91707 28.40175 1.000 41.64358  ? 492 HOH A O    1 
HETATM 5434 O O    . HOH D 3 .   ? 11.47034  20.81866 42.70353 1.000 43.23271  ? 493 HOH A O    1 
HETATM 5435 O O    . HOH D 3 .   ? -1.73874  14.45688 35.88052 1.000 34.60383  ? 494 HOH A O    1 
HETATM 5436 O O    . HOH D 3 .   ? -6.09498  18.91924 30.08402 1.000 31.74480  ? 495 HOH A O    1 
HETATM 5437 O O    . HOH D 3 .   ? -2.86674  26.02935 29.85386 1.000 37.64585  ? 496 HOH A O    1 
HETATM 5438 O O    . HOH D 3 .   ? 3.82420   19.38485 2.78498  1.000 39.50188  ? 497 HOH A O    1 
HETATM 5439 O O    . HOH D 3 .   ? 1.57516   17.70726 3.74185  1.000 34.15229  ? 498 HOH A O    1 
HETATM 5440 O O    . HOH D 3 .   ? 5.220     -0.337   27.903   1.000 32.29175  ? 499 HOH A O    1 
HETATM 5441 O O    . HOH D 3 .   ? 4.94963   17.69810 0.40851  1.000 31.76670  ? 500 HOH A O    1 
HETATM 5442 O O    . HOH D 3 .   ? -8.23918  2.66243  27.87699 1.000 43.00420  ? 501 HOH A O    1 
HETATM 5443 O O    . HOH D 3 .   ? -1.32035  20.70064 33.71800 1.000 33.53309  ? 502 HOH A O    1 
HETATM 5444 O O    . HOH D 3 .   ? 20.52879  24.57387 33.79897 1.000 47.55495  ? 503 HOH A O    1 
HETATM 5445 O O    . HOH D 3 .   ? 13.509    3.165    0.817    1.000 40.37387  ? 504 HOH A O    1 
HETATM 5446 O O    . HOH D 3 .   ? 4.411     29.600   25.602   1.000 23.45773  ? 505 HOH A O    1 
HETATM 5447 O O    . HOH D 3 .   ? 19.410    25.878   26.545   1.000 38.13890  ? 506 HOH A O    1 
HETATM 5448 O O    . HOH D 3 .   ? 15.61466  3.51971  30.99003 1.000 39.10417  ? 507 HOH A O    1 
HETATM 5449 O O    A HOH D 3 .   ? -0.24495  17.28391 38.20988 0.626 24.65423  ? 508 HOH A O    1 
HETATM 5450 O O    B HOH D 3 .   ? -0.43126  15.75469 38.59607 0.374 28.81387  ? 508 HOH A O    1 
HETATM 5451 O O    . HOH D 3 .   ? -9.03036  24.52962 27.42804 1.000 34.94268  ? 509 HOH A O    1 
HETATM 5452 O O    . HOH E 3 .   ? -2.84950  -0.61047 13.11947 1.000 36.87619  ? 201 HOH B O    1 
HETATM 5453 O O    . HOH E 3 .   ? -35.60556 1.47806  23.10923 1.000 37.94634  ? 202 HOH B O    1 
HETATM 5454 O O    . HOH E 3 .   ? -30.71656 0.68418  23.68268 1.000 34.31535  ? 203 HOH B O    1 
HETATM 5455 O O    . HOH E 3 .   ? -16.25341 13.25562 24.24657 1.000 21.55000  ? 204 HOH B O    1 
HETATM 5456 O O    . HOH E 3 .   ? 0.18912   13.00395 9.33217  1.000 16.04777  ? 205 HOH B O    1 
HETATM 5457 O O    . HOH E 3 .   ? -41.14627 6.39922  8.88355  1.000 29.33031  ? 206 HOH B O    1 
HETATM 5458 O O    . HOH E 3 .   ? -36.33430 8.71694  18.96734 1.000 22.39522  ? 207 HOH B O    1 
HETATM 5459 O O    . HOH E 3 .   ? -11.36037 3.47454  11.79772 1.000 15.69190  ? 208 HOH B O    1 
HETATM 5460 O O    . HOH E 3 .   ? -8.88239  20.95914 21.08725 1.000 31.15390  ? 209 HOH B O    1 
HETATM 5461 O O    . HOH E 3 .   ? -2.70235  16.71259 5.85569  1.000 22.56943  ? 210 HOH B O    1 
HETATM 5462 O O    . HOH E 3 .   ? -20.61921 14.85820 29.84114 1.000 30.34464  ? 211 HOH B O    1 
HETATM 5463 O O    . HOH E 3 .   ? -21.06215 4.34660  -5.98669 1.000 40.08620  ? 212 HOH B O    1 
HETATM 5464 O O    . HOH E 3 .   ? -16.09340 22.40886 -6.65620 1.000 44.03581  ? 213 HOH B O    1 
HETATM 5465 O O    . HOH E 3 .   ? -27.956   -5.231   13.398   1.000 19.57712  ? 214 HOH B O    1 
HETATM 5466 O O    . HOH E 3 .   ? -3.41761  -0.24103 20.39272 1.000 26.30723  ? 215 HOH B O    1 
HETATM 5467 O O    . HOH E 3 .   ? -28.96681 19.25441 13.71379 1.000 25.24765  ? 216 HOH B O    1 
HETATM 5468 O O    . HOH E 3 .   ? -20.73194 -5.51547 7.09877  1.000 20.61379  ? 217 HOH B O    1 
HETATM 5469 O O    . HOH E 3 .   ? 0.97972   5.52522  7.76350  1.000 14.69706  ? 218 HOH B O    1 
HETATM 5470 O O    . HOH E 3 .   ? -19.74884 1.54696  25.65696 1.000 22.33049  ? 219 HOH B O    1 
HETATM 5471 O O    . HOH E 3 .   ? -11.00501 0.74536  1.95582  1.000 18.31200  ? 220 HOH B O    1 
HETATM 5472 O O    . HOH E 3 .   ? -31.60847 15.54822 13.99594 1.000 16.66693  ? 221 HOH B O    1 
HETATM 5473 O O    . HOH E 3 .   ? -28.78949 9.77329  32.56621 1.000 21.94694  ? 222 HOH B O    1 
HETATM 5474 O O    . HOH E 3 .   ? -13.14085 14.72052 22.52179 1.000 34.38827  ? 223 HOH B O    1 
HETATM 5475 O O    . HOH E 3 .   ? -19.93307 21.17041 23.48712 1.000 31.54494  ? 224 HOH B O    1 
HETATM 5476 O O    . HOH E 3 .   ? -10.34093 16.99058 -3.98487 1.000 35.68021  ? 225 HOH B O    1 
HETATM 5477 O O    . HOH E 3 .   ? -38.588   9.350    8.716    1.000 36.10332  ? 226 HOH B O    1 
HETATM 5478 O O    . HOH E 3 .   ? -9.45314  7.19331  24.85189 1.000 27.28182  ? 227 HOH B O    1 
HETATM 5479 O O    A HOH E 3 .   ? -34.30115 13.14758 20.47962 0.488 29.08929  ? 228 HOH B O    1 
HETATM 5480 O O    B HOH E 3 .   ? -33.98828 14.56485 22.47727 0.512 29.62237  ? 228 HOH B O    1 
HETATM 5481 O O    . HOH E 3 .   ? -15.05945 25.32075 3.56429  1.000 27.93971  ? 229 HOH B O    1 
HETATM 5482 O O    . HOH E 3 .   ? -8.61330  3.02406  -0.95179 1.000 31.69533  ? 230 HOH B O    1 
HETATM 5483 O O    A HOH E 3 .   ? -19.44739 16.07819 -3.12518 0.586 25.12039  ? 231 HOH B O    1 
HETATM 5484 O O    B HOH E 3 .   ? -21.83526 16.86658 -1.67622 0.414 28.12123  ? 231 HOH B O    1 
HETATM 5485 O O    . HOH E 3 .   ? -31.22890 13.95314 3.97012  1.000 26.80113  ? 232 HOH B O    1 
HETATM 5486 O O    . HOH E 3 .   ? -15.71669 18.87096 23.76530 1.000 48.06505  ? 233 HOH B O    1 
HETATM 5487 O O    . HOH E 3 .   ? -9.12523  22.16747 8.62335  1.000 30.24775  ? 234 HOH B O    1 
HETATM 5488 O O    . HOH E 3 .   ? -29.61364 17.04601 -0.81103 1.000 35.39781  ? 235 HOH B O    1 
HETATM 5489 O O    . HOH E 3 .   ? -11.14933 18.78823 -4.46074 1.000 39.65211  ? 236 HOH B O    1 
HETATM 5490 O O    . HOH E 3 .   ? -4.78107  17.65654 11.83856 1.000 11.77885  ? 237 HOH B O    1 
HETATM 5491 O O    . HOH E 3 .   ? -6.27568  -2.89633 14.56777 1.000 25.99430  ? 238 HOH B O    1 
HETATM 5492 O O    . HOH E 3 .   ? -29.29347 2.49712  22.50701 1.000 12.88471  ? 239 HOH B O    1 
HETATM 5493 O O    . HOH E 3 .   ? -4.65790  1.11085  11.30617 1.000 13.05668  ? 240 HOH B O    1 
HETATM 5494 O O    . HOH E 3 .   ? -26.31169 -2.16567 12.58392 1.000 14.21747  ? 241 HOH B O    1 
HETATM 5495 O O    . HOH E 3 .   ? -3.78878  0.60942  1.26893  1.000 31.70379  ? 242 HOH B O    1 
HETATM 5496 O O    . HOH E 3 .   ? -14.95357 20.60049 18.56645 1.000 18.92222  ? 243 HOH B O    1 
HETATM 5497 O O    A HOH E 3 .   ? -12.06801 17.75425 5.53521  0.585 30.15088  ? 244 HOH B O    1 
HETATM 5498 O O    B HOH E 3 .   ? -12.42017 19.62938 6.34457  0.415 32.83307  ? 244 HOH B O    1 
HETATM 5499 O O    . HOH E 3 .   ? -19.84108 -1.03269 6.61219  1.000 15.75680  ? 245 HOH B O    1 
HETATM 5500 O O    . HOH E 3 .   ? -15.58172 -2.68898 5.09604  1.000 17.35240  ? 246 HOH B O    1 
HETATM 5501 O O    . HOH E 3 .   ? -23.02686 21.92189 22.47703 1.000 29.67395  ? 247 HOH B O    1 
HETATM 5502 O O    . HOH E 3 .   ? -21.95410 0.72663  6.56141  1.000 15.83203  ? 248 HOH B O    1 
HETATM 5503 O O    . HOH E 3 .   ? -26.39379 11.45758 29.33699 1.000 17.00070  ? 249 HOH B O    1 
HETATM 5504 O O    . HOH E 3 .   ? -15.19350 16.27865 22.72478 1.000 25.56022  ? 250 HOH B O    1 
HETATM 5505 O O    . HOH E 3 .   ? -8.74084  12.73625 11.86632 1.000 12.51857  ? 251 HOH B O    1 
HETATM 5506 O O    . HOH E 3 .   ? -6.41259  9.58332  10.05402 1.000 11.74579  ? 252 HOH B O    1 
HETATM 5507 O O    . HOH E 3 .   ? -4.73604  11.86363 15.65972 1.000 10.83276  ? 253 HOH B O    1 
HETATM 5508 O O    A HOH E 3 .   ? -15.26393 2.60995  25.61717 0.556 11.85025  ? 254 HOH B O    1 
HETATM 5509 O O    B HOH E 3 .   ? -15.61623 3.41467  27.05698 0.444 22.02645  ? 254 HOH B O    1 
HETATM 5510 O O    . HOH E 3 .   ? -35.05758 10.31368 9.27262  1.000 38.98415  ? 255 HOH B O    1 
HETATM 5511 O O    . HOH E 3 .   ? -33.42597 15.38161 6.64943  1.000 20.06361  ? 256 HOH B O    1 
HETATM 5512 O O    . HOH E 3 .   ? -3.94147  8.35544  0.31716  1.000 27.85883  ? 257 HOH B O    1 
HETATM 5513 O O    . HOH E 3 .   ? -14.37803 -0.78080 3.60043  1.000 23.68654  ? 258 HOH B O    1 
HETATM 5514 O O    . HOH E 3 .   ? -13.06673 7.27595  7.73575  1.000 8.41851   ? 259 HOH B O    1 
HETATM 5515 O O    . HOH E 3 .   ? -10.06191 -4.48811 11.77483 1.000 18.97953  ? 260 HOH B O    1 
HETATM 5516 O O    . HOH E 3 .   ? -12.87012 1.75300  9.65674  1.000 26.31914  ? 261 HOH B O    1 
HETATM 5517 O O    . HOH E 3 .   ? -29.35266 8.46684  8.32542  1.000 24.87097  ? 262 HOH B O    1 
HETATM 5518 O O    . HOH E 3 .   ? -19.13240 -2.60732 24.33715 1.000 26.92513  ? 263 HOH B O    1 
HETATM 5519 O O    . HOH E 3 .   ? -26.06886 3.81203  25.46463 1.000 15.65971  ? 264 HOH B O    1 
HETATM 5520 O O    A HOH E 3 .   ? -18.21742 18.40579 0.43238  0.349 20.16125  ? 265 HOH B O    1 
HETATM 5521 O O    B HOH E 3 .   ? -20.24382 17.96433 -0.90385 0.651 26.78577  ? 265 HOH B O    1 
HETATM 5522 O O    . HOH E 3 .   ? -25.75619 10.52569 -2.55127 1.000 26.94021  ? 266 HOH B O    1 
HETATM 5523 O O    . HOH E 3 .   ? -34.32293 19.25328 9.49574  1.000 40.29237  ? 267 HOH B O    1 
HETATM 5524 O O    . HOH E 3 .   ? -11.70547 -4.74661 22.19486 1.000 37.98908  ? 268 HOH B O    1 
HETATM 5525 O O    . HOH E 3 .   ? -21.44130 14.78753 20.48851 1.000 9.56234   ? 269 HOH B O    1 
HETATM 5526 O O    A HOH E 3 .   ? -8.73615  20.77093 25.51913 0.569 29.64798  ? 270 HOH B O    1 
HETATM 5527 O O    B HOH E 3 .   ? -9.07390  22.19610 25.33356 0.431 29.97435  ? 270 HOH B O    1 
HETATM 5528 O O    . HOH E 3 .   ? -17.88244 12.98349 21.95331 1.000 8.95113   ? 271 HOH B O    1 
HETATM 5529 O O    . HOH E 3 .   ? -35.42652 4.95493  14.07117 1.000 16.07333  ? 272 HOH B O    1 
HETATM 5530 O O    . HOH E 3 .   ? -13.80814 -3.87858 17.18404 1.000 19.20235  ? 273 HOH B O    1 
HETATM 5531 O O    . HOH E 3 .   ? -20.70160 9.03576  30.89070 1.000 39.78617  ? 274 HOH B O    1 
HETATM 5532 O O    . HOH E 3 .   ? -13.09150 9.21820  24.67511 1.000 14.77206  ? 275 HOH B O    1 
HETATM 5533 O O    A HOH E 3 .   ? -16.21712 -4.57773 20.81209 0.535 19.13330  ? 276 HOH B O    1 
HETATM 5534 O O    B HOH E 3 .   ? -16.09853 -6.02652 20.48333 0.465 31.16305  ? 276 HOH B O    1 
HETATM 5535 O O    . HOH E 3 .   ? -25.82411 -3.97823 17.15969 1.000 27.14148  ? 277 HOH B O    1 
HETATM 5536 O O    . HOH E 3 .   ? -26.59683 2.45834  23.11469 1.000 14.69454  ? 278 HOH B O    1 
HETATM 5537 O O    . HOH E 3 .   ? -16.19191 -2.35108 17.82978 1.000 13.26825  ? 279 HOH B O    1 
HETATM 5538 O O    . HOH E 3 .   ? -32.08677 6.78033  27.92741 1.000 14.83216  ? 280 HOH B O    1 
HETATM 5539 O O    . HOH E 3 .   ? -27.70877 3.32540  7.17632  1.000 36.79858  ? 281 HOH B O    1 
HETATM 5540 O O    . HOH E 3 .   ? -24.49765 -3.14372 19.00940 1.000 20.34679  ? 282 HOH B O    1 
HETATM 5541 O O    . HOH E 3 .   ? -27.90003 9.80125  5.26527  1.000 37.15856  ? 283 HOH B O    1 
HETATM 5542 O O    . HOH E 3 .   ? -31.79177 9.57342  9.10906  1.000 44.90906  ? 284 HOH B O    1 
HETATM 5543 O O    . HOH E 3 .   ? -12.30320 6.59234  26.53120 1.000 24.26441  ? 285 HOH B O    1 
HETATM 5544 O O    . HOH E 3 .   ? -13.97165 11.98810 23.83867 1.000 32.35501  ? 286 HOH B O    1 
HETATM 5545 O O    A HOH E 3 .   ? -21.80079 18.55383 23.95500 0.617 11.89912  ? 287 HOH B O    1 
HETATM 5546 O O    B HOH E 3 .   ? -22.07964 17.81092 24.06670 0.383 12.94283  ? 287 HOH B O    1 
HETATM 5547 O O    . HOH E 3 .   ? -20.850   -4.045   15.508   1.000 11.35364  ? 288 HOH B O    1 
HETATM 5548 O O    . HOH E 3 .   ? -32.11666 1.95349  11.83538 1.000 37.34437  ? 289 HOH B O    1 
HETATM 5549 O O    A HOH E 3 .   ? -12.67219 20.51628 7.91029  0.624 16.02799  ? 290 HOH B O    1 
HETATM 5550 O O    B HOH E 3 .   ? -13.20160 21.46523 7.74886  0.376 15.46327  ? 290 HOH B O    1 
HETATM 5551 O O    . HOH E 3 .   ? -34.02703 14.72748 16.26949 1.000 38.81164  ? 291 HOH B O    1 
HETATM 5552 O O    . HOH E 3 .   ? -32.25234 18.24205 28.65427 1.000 29.39418  ? 292 HOH B O    1 
HETATM 5553 O O    . HOH E 3 .   ? -9.80058  -2.28157 0.32422  1.000 26.69797  ? 293 HOH B O    1 
HETATM 5554 O O    . HOH E 3 .   ? -29.82289 20.73962 20.79856 1.000 38.91878  ? 294 HOH B O    1 
HETATM 5555 O O    . HOH E 3 .   ? -32.72334 -0.13515 11.95828 1.000 37.85617  ? 295 HOH B O    1 
HETATM 5556 O O    . HOH E 3 .   ? -23.638   27.730   11.696   1.000 14.47549  ? 296 HOH B O    1 
HETATM 5557 O O    . HOH E 3 .   ? -30.30730 17.57084 16.83950 1.000 36.28996  ? 297 HOH B O    1 
HETATM 5558 O O    . HOH E 3 .   ? -11.94642 25.61621 13.64122 1.000 17.99709  ? 298 HOH B O    1 
HETATM 5559 O O    . HOH E 3 .   ? -20.33195 17.13746 30.87321 1.000 36.01010  ? 299 HOH B O    1 
HETATM 5560 O O    A HOH E 3 .   ? -16.07852 -7.61143 17.42390 0.675 16.16890  ? 300 HOH B O    1 
HETATM 5561 O O    B HOH E 3 .   ? -14.56075 -7.85405 17.54951 0.325 19.31248  ? 300 HOH B O    1 
HETATM 5562 O O    A HOH E 3 .   ? -8.06636  13.76060 1.45716  0.544 11.99539  ? 301 HOH B O    1 
HETATM 5563 O O    B HOH E 3 .   ? -8.86599  14.04626 1.33319  0.456 13.14080  ? 301 HOH B O    1 
HETATM 5564 O O    . HOH E 3 .   ? -17.68504 3.42632  26.07973 1.000 17.64552  ? 302 HOH B O    1 
HETATM 5565 O O    . HOH E 3 .   ? -29.60253 19.88588 9.10681  1.000 39.81211  ? 303 HOH B O    1 
HETATM 5566 O O    . HOH E 3 .   ? -32.88321 16.90326 12.10353 1.000 26.16143  ? 304 HOH B O    1 
HETATM 5567 O O    . HOH E 3 .   ? -9.53664  23.85705 16.39427 1.000 27.36261  ? 305 HOH B O    1 
HETATM 5568 O O    . HOH E 3 .   ? -1.35564  11.79976 12.83697 1.000 14.67793  ? 306 HOH B O    1 
HETATM 5569 O O    . HOH E 3 .   ? -18.072   -0.556   2.121    1.000 34.31123  ? 307 HOH B O    1 
HETATM 5570 O O    . HOH E 3 .   ? -37.43123 12.18369 20.17989 1.000 37.08279  ? 308 HOH B O    1 
HETATM 5571 O O    . HOH E 3 .   ? -26.82608 5.32612  5.75334  1.000 32.99006  ? 309 HOH B O    1 
HETATM 5572 O O    A HOH E 3 .   ? -2.976    -5.895   4.979    0.495 31.65034  ? 310 HOH B O    1 
HETATM 5573 O O    B HOH E 3 .   ? -3.815    -3.216   5.045    0.505 29.48655  ? 310 HOH B O    1 
HETATM 5574 O O    . HOH E 3 .   ? -2.86863  0.13763  4.00287  1.000 21.77210  ? 311 HOH B O    1 
HETATM 5575 O O    . HOH E 3 .   ? -4.84594  12.96459 1.03021  1.000 20.41215  ? 312 HOH B O    1 
HETATM 5576 O O    . HOH E 3 .   ? -24.68485 2.43036  27.70633 1.000 35.71464  ? 313 HOH B O    1 
HETATM 5577 O O    . HOH E 3 .   ? -33.93176 3.89179  12.19232 1.000 23.89278  ? 314 HOH B O    1 
HETATM 5578 O O    . HOH E 3 .   ? -31.29893 23.77182 10.82073 1.000 41.38322  ? 315 HOH B O    1 
HETATM 5579 O O    . HOH E 3 .   ? -10.96698 16.61659 21.82097 1.000 21.34027  ? 316 HOH B O    1 
HETATM 5580 O O    . HOH E 3 .   ? -12.20522 3.31260  1.66484  1.000 17.35631  ? 317 HOH B O    1 
HETATM 5581 O O    . HOH E 3 .   ? -29.236   11.851   30.376   1.000 24.48901  ? 318 HOH B O    1 
HETATM 5582 O O    . HOH E 3 .   ? -0.700    0.145    11.416   1.000 27.41038  ? 319 HOH B O    1 
HETATM 5583 O O    . HOH E 3 .   ? -22.780   26.294   17.371   1.000 17.43461  ? 320 HOH B O    1 
HETATM 5584 O O    . HOH E 3 .   ? -10.59813 -6.68795 6.69236  1.000 30.59274  ? 321 HOH B O    1 
HETATM 5585 O O    . HOH E 3 .   ? -2.81434  5.26756  5.41410  1.000 31.77604  ? 322 HOH B O    1 
HETATM 5586 O O    . HOH E 3 .   ? -24.06662 1.79881  5.04115  1.000 31.11787  ? 323 HOH B O    1 
HETATM 5587 O O    . HOH E 3 .   ? -28.18185 18.17493 26.58276 1.000 26.13568  ? 324 HOH B O    1 
HETATM 5588 O O    . HOH E 3 .   ? -26.19621 0.01087  24.38834 1.000 34.08191  ? 325 HOH B O    1 
HETATM 5589 O O    . HOH E 3 .   ? -10.22863 4.64408  -0.00996 1.000 18.19027  ? 326 HOH B O    1 
HETATM 5590 O O    A HOH E 3 .   ? -12.34017 -2.97462 24.18207 0.440 34.32497  ? 327 HOH B O    1 
HETATM 5591 O O    B HOH E 3 .   ? -12.92863 -3.44517 26.11392 0.560 35.14140  ? 327 HOH B O    1 
HETATM 5592 O O    . HOH E 3 .   ? -11.95878 -6.45559 17.43555 1.000 35.00284  ? 328 HOH B O    1 
HETATM 5593 O O    . HOH E 3 .   ? -33.02076 9.10547  5.04742  1.000 45.46691  ? 329 HOH B O    1 
HETATM 5594 O O    . HOH E 3 .   ? -29.45093 18.29625 23.99058 1.000 26.26863  ? 330 HOH B O    1 
HETATM 5595 O O    . HOH E 3 .   ? -26.76881 16.05869 27.50806 1.000 31.64469  ? 331 HOH B O    1 
HETATM 5596 O O    . HOH E 3 .   ? -37.20156 12.59019 17.72151 1.000 36.02432  ? 332 HOH B O    1 
HETATM 5597 O O    . HOH E 3 .   ? -23.89851 4.08686  -4.86330 1.000 37.47615  ? 333 HOH B O    1 
HETATM 5598 O O    . HOH E 3 .   ? -31.76597 21.60919 9.90383  1.000 34.70458  ? 334 HOH B O    1 
HETATM 5599 O O    . HOH E 3 .   ? -29.68568 21.00071 15.09759 1.000 35.63943  ? 335 HOH B O    1 
HETATM 5600 O O    . HOH E 3 .   ? -30.16682 5.61068  31.64708 1.000 34.21230  ? 336 HOH B O    1 
HETATM 5601 O O    A HOH E 3 .   ? -2.15110  13.16355 5.15387  0.571 24.85563  ? 337 HOH B O    1 
HETATM 5602 O O    B HOH E 3 .   ? -2.20611  14.58831 4.53156  0.429 26.31663  ? 337 HOH B O    1 
HETATM 5603 O O    A HOH E 3 .   ? -11.46415 -3.47320 15.96587 0.534 16.76178  ? 338 HOH B O    1 
HETATM 5604 O O    B HOH E 3 .   ? -10.66928 -4.17569 16.44773 0.466 22.59550  ? 338 HOH B O    1 
HETATM 5605 O O    . HOH E 3 .   ? -33.491   15.515   2.850    1.000 37.22159  ? 339 HOH B O    1 
HETATM 5606 O O    . HOH E 3 .   ? -15.98352 30.04658 1.12014  1.000 39.75084  ? 340 HOH B O    1 
HETATM 5607 O O    . HOH E 3 .   ? -11.20262 0.30070  26.99848 1.000 27.77513  ? 341 HOH B O    1 
HETATM 5608 O O    . HOH E 3 .   ? -26.30476 24.48453 17.43187 1.000 30.18248  ? 342 HOH B O    1 
HETATM 5609 O O    . HOH E 3 .   ? -15.85827 17.09502 29.44788 1.000 40.47027  ? 343 HOH B O    1 
HETATM 5610 O O    . HOH E 3 .   ? -12.644   23.303   5.970    1.000 37.78166  ? 344 HOH B O    1 
HETATM 5611 O O    . HOH E 3 .   ? -8.481    23.826   10.622   1.000 24.58023  ? 345 HOH B O    1 
HETATM 5612 O O    . HOH E 3 .   ? -7.46990  25.05534 13.51576 1.000 37.94254  ? 346 HOH B O    1 
HETATM 5613 O O    . HOH E 3 .   ? -8.51953  18.37203 2.80456  1.000 25.78301  ? 347 HOH B O    1 
HETATM 5614 O O    . HOH E 3 .   ? -36.14461 14.17061 16.68116 1.000 39.12936  ? 348 HOH B O    1 
HETATM 5615 O O    . HOH E 3 .   ? -5.17957  -3.31824 17.03877 1.000 24.65010  ? 349 HOH B O    1 
HETATM 5616 O O    . HOH E 3 .   ? -6.46120  12.84350 -0.12607 1.000 32.90948  ? 350 HOH B O    1 
HETATM 5617 O O    . HOH E 3 .   ? -28.32808 23.40287 15.35996 1.000 30.94533  ? 351 HOH B O    1 
HETATM 5618 O O    . HOH E 3 .   ? -21.26943 22.27445 21.29084 1.000 41.42036  ? 352 HOH B O    1 
HETATM 5619 O O    . HOH E 3 .   ? -4.059    8.209    -1.926   1.000 35.59416  ? 353 HOH B O    1 
HETATM 5620 O O    . HOH E 3 .   ? -6.37058  19.74778 3.69664  1.000 40.21466  ? 354 HOH B O    1 
HETATM 5621 O O    . HOH E 3 .   ? -38.884   1.131    10.709   1.000 41.20568  ? 355 HOH B O    1 
HETATM 5622 O O    . HOH E 3 .   ? -9.885    -7.304   20.812   1.000 40.08978  ? 356 HOH B O    1 
HETATM 5623 O O    . HOH E 3 .   ? -31.23090 15.61927 -0.00070 0.508 40.56970  ? 357 HOH B O    1 
HETATM 5624 O O    . HOH E 3 .   ? -13.93480 -5.47863 19.53875 1.000 23.71216  ? 358 HOH B O    1 
HETATM 5625 O O    . HOH E 3 .   ? -10.93771 19.19764 3.64333  1.000 29.10000  ? 359 HOH B O    1 
HETATM 5626 O O    A HOH E 3 .   ? -14.62889 19.26708 21.17298 0.578 21.71761  ? 360 HOH B O    1 
HETATM 5627 O O    B HOH E 3 .   ? -12.97195 18.74319 20.74889 0.422 27.15409  ? 360 HOH B O    1 
HETATM 5628 O O    . HOH E 3 .   ? -24.37448 -4.75057 21.33300 1.000 32.62060  ? 361 HOH B O    1 
HETATM 5629 O O    . HOH E 3 .   ? -30.29531 19.82330 16.77674 1.000 44.54508  ? 362 HOH B O    1 
HETATM 5630 O O    . HOH E 3 .   ? -18.30938 28.42139 4.69772  1.000 17.94401  ? 363 HOH B O    1 
HETATM 5631 O O    . HOH E 3 .   ? -16.96590 3.64884  28.89418 1.000 37.72252  ? 364 HOH B O    1 
HETATM 5632 O O    . HOH E 3 .   ? -30.779   -4.462   12.814   1.000 39.33781  ? 365 HOH B O    1 
HETATM 5633 O O    . HOH E 3 .   ? -28.27258 -0.71081 8.73664  1.000 44.71277  ? 366 HOH B O    1 
HETATM 5634 O O    . HOH E 3 .   ? -18.53929 -3.77253 17.12662 1.000 12.72695  ? 367 HOH B O    1 
HETATM 5635 O O    . HOH E 3 .   ? -11.68504 4.67911  28.49119 1.000 33.60228  ? 368 HOH B O    1 
HETATM 5636 O O    . HOH E 3 .   ? -28.31810 -1.08245 11.15846 1.000 25.44779  ? 369 HOH B O    1 
HETATM 5637 O O    . HOH E 3 .   ? -1.46122  13.53060 2.85348  1.000 35.51339  ? 370 HOH B O    1 
HETATM 5638 O O    . HOH E 3 .   ? -11.690   21.125   -7.037   1.000 35.55070  ? 371 HOH B O    1 
HETATM 5639 O O    . HOH E 3 .   ? -35.51282 17.06887 6.07564  1.000 32.35187  ? 372 HOH B O    1 
HETATM 5640 O O    . HOH E 3 .   ? -19.72745 23.96613 20.54924 1.000 28.80896  ? 373 HOH B O    1 
HETATM 5641 O O    . HOH E 3 .   ? -17.17241 17.50536 30.84733 1.000 40.14116  ? 374 HOH B O    1 
HETATM 5642 O O    . HOH E 3 .   ? -8.87994  -3.98086 26.06669 1.000 31.77691  ? 375 HOH B O    1 
HETATM 5643 O O    . HOH E 3 .   ? -17.827   -5.872   19.063   1.000 23.14353  ? 376 HOH B O    1 
HETATM 5644 O O    . HOH E 3 .   ? -30.808   -2.246   11.574   1.000 28.93114  ? 377 HOH B O    1 
HETATM 5645 O O    . HOH E 3 .   ? -20.87104 6.49188  32.13538 1.000 30.35795  ? 378 HOH B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 2   ? 0.37073 0.39791 0.38377 0.00200  0.04801  -0.02012 -1  ALA A N   
2    C CA  . ALA A 2   ? 0.35814 0.37093 0.36813 0.00588  0.05974  -0.02396 -1  ALA A CA  
3    C C   . ALA A 2   ? 0.34844 0.37875 0.36284 -0.00262 0.07069  -0.02006 -1  ALA A C   
4    O O   . ALA A 2   ? 0.33850 0.37676 0.36357 -0.02188 0.07543  -0.03272 -1  ALA A O   
5    C CB  . ALA A 2   ? 0.35968 0.37569 0.36229 -0.00495 0.06089  -0.01152 -1  ALA A CB  
11   N N   . MET A 3   ? 0.33069 0.35698 0.35583 0.01437  0.06720  0.00643  0   MET A N   
12   C CA  . MET A 3   ? 0.31630 0.33279 0.33445 0.02650  0.05298  0.00879  0   MET A CA  
13   C C   . MET A 3   ? 0.29708 0.27492 0.30752 0.00975  0.04150  -0.01938 0   MET A C   
14   O O   . MET A 3   ? 0.28935 0.27035 0.30427 0.03650  0.05040  -0.05550 0   MET A O   
15   C CB  . MET A 3   ? 0.34071 0.35484 0.35997 0.00383  0.04447  0.01301  0   MET A CB  
16   C CG  . MET A 3   ? 0.36837 0.38487 0.40671 -0.01290 0.03544  0.02482  0   MET A CG  
17   S SD  . MET A 3   ? 0.40158 0.45735 0.43651 0.01835  0.03594  0.04246  0   MET A SD  
18   C CE  . MET A 3   ? 0.38410 0.44518 0.42469 0.05905  0.03571  0.01232  0   MET A CE  
28   N N   . GLY A 4   ? 0.28183 0.24827 0.29024 -0.00669 0.03248  -0.02549 1   GLY A N   
29   C CA  . GLY A 4   ? 0.28352 0.25037 0.29660 -0.01211 0.04320  -0.01742 1   GLY A CA  
30   C C   . GLY A 4   ? 0.29613 0.28650 0.29118 -0.00217 0.07484  0.01498  1   GLY A C   
31   O O   . GLY A 4   ? 0.29474 0.26974 0.27038 -0.00684 0.08722  0.04405  1   GLY A O   
35   N N   . SER A 5   ? 0.32448 0.31701 0.32433 -0.00715 0.09096  0.02584  2   SER A N   
36   C CA  . SER A 5   ? 0.38738 0.39300 0.38649 0.00089  0.09189  0.01339  2   SER A CA  
37   C C   . SER A 5   ? 0.32378 0.31268 0.32831 -0.00319 0.05527  0.00164  2   SER A C   
38   O O   . SER A 5   ? 0.30486 0.29397 0.29301 0.01140  0.05611  -0.03483 2   SER A O   
39   C CB  . SER A 5   ? 0.50125 0.54470 0.48695 -0.00040 0.13888  0.00235  2   SER A CB  
40   O OG  . SER A 5   ? 0.58937 0.65611 0.57807 0.00205  0.18334  -0.00004 2   SER A OG  
46   N N   . GLY A 6   ? 0.25746 0.23184 0.28823 -0.02497 0.01171  0.05173  3   GLY A N   
47   C CA  . GLY A 6   ? 0.24310 0.21743 0.27617 -0.05148 0.01558  0.07824  3   GLY A CA  
48   C C   . GLY A 6   ? 0.24095 0.24296 0.26225 -0.03520 -0.00889 0.10384  3   GLY A C   
49   O O   . GLY A 6   ? 0.26964 0.30821 0.31923 -0.04530 -0.00032 0.09058  3   GLY A O   
235  N N   . PRO A 12  ? 0.25269 0.22589 0.25471 -0.00678 0.09342  0.07650  9   PRO A N   
238  C C   . PRO A 12  ? 0.26622 0.25552 0.23835 0.03522  0.09660  0.00971  9   PRO A C   
239  O O   . PRO A 12  ? 0.23997 0.30976 0.17671 0.01365  0.08721  0.01746  9   PRO A O   
260  N N   . SER A 13  ? 0.32541 0.32269 0.30544 0.04459  0.06010  -0.00987 10  SER A N   
263  C C   . SER A 13  ? 0.30985 0.29763 0.28295 -0.00906 0.06179  -0.01799 10  SER A C   
264  O O   . SER A 13  ? 0.27813 0.27789 0.21112 -0.00869 0.06313  -0.05735 10  SER A O   
279  N N   . THR A 14  ? 0.25644 0.24618 0.23441 0.01288  0.07472  -0.00870 11  THR A N   
280  C CA  . THR A 14  ? 0.20913 0.23142 0.21552 -0.00911 0.05744  -0.01787 11  THR A CA  
281  C C   . THR A 14  ? 0.20546 0.23192 0.18607 -0.01377 0.06887  -0.03467 11  THR A C   
282  O O   . THR A 14  ? 0.20933 0.23589 0.22393 -0.05293 0.07286  -0.05685 11  THR A O   
283  C CB  . THR A 14  ? 0.21724 0.20301 0.20926 0.00710  0.03227  -0.03991 11  THR A CB  
284  O OG1 . THR A 14  ? 0.21420 0.20968 0.25183 -0.01096 0.02379  -0.08728 11  THR A OG1 
285  C CG2 . THR A 14  ? 0.23384 0.24619 0.17471 0.02331  0.00947  -0.04278 11  THR A CG2 
293  N N   . ILE A 15  ? 0.17590 0.22973 0.16840 -0.04516 0.03868  -0.04461 12  ILE A N   
294  C CA  . ILE A 15  ? 0.19634 0.23102 0.19248 -0.06161 0.05979  -0.02381 12  ILE A CA  
295  C C   . ILE A 15  ? 0.20424 0.21498 0.17383 -0.03459 0.05581  -0.02695 12  ILE A C   
296  O O   . ILE A 15  ? 0.23255 0.27195 0.16709 -0.06156 0.04814  0.00005  12  ILE A O   
297  C CB  . ILE A 15  ? 0.24280 0.27385 0.23933 0.00172  0.05813  -0.01648 12  ILE A CB  
298  C CG1 . ILE A 15  ? 0.26317 0.31188 0.25917 0.00293  0.03360  -0.03884 12  ILE A CG1 
299  C CG2 . ILE A 15  ? 0.24231 0.30461 0.24583 -0.01048 0.06711  -0.00828 12  ILE A CG2 
300  C CD1 . ILE A 15  ? 0.30306 0.35560 0.29400 -0.00260 0.03799  -0.01862 12  ILE A CD1 
356  N N   . LEU A 17  ? 0.13097 0.15821 0.12591 -0.03161 -0.01434 0.00809  14  LEU A N   
357  C CA  . LEU A 17  ? 0.12696 0.16170 0.13027 -0.03118 0.01321  -0.02914 14  LEU A CA  
358  C C   . LEU A 17  ? 0.13095 0.18962 0.13958 -0.01279 0.03351  -0.02405 14  LEU A C   
359  O O   . LEU A 17  ? 0.12358 0.24033 0.18417 -0.03160 0.04225  -0.00329 14  LEU A O   
360  C CB  . LEU A 17  ? 0.13511 0.18986 0.13165 -0.00020 0.00597  -0.00754 14  LEU A CB  
361  C CG  . LEU A 17  ? 0.13411 0.19704 0.13986 -0.00858 -0.01001 0.00374  14  LEU A CG  
362  C CD1 . LEU A 17  ? 0.16188 0.21305 0.14022 -0.02876 -0.00637 0.02558  14  LEU A CD1 
363  C CD2 . LEU A 17  ? 0.14764 0.18513 0.17458 0.00366  -0.01752 0.04163  14  LEU A CD2 
376  N N   . VAL A 18  ? 0.14852 0.16310 0.13250 -0.01273 0.05013  -0.00555 15  VAL A N   
377  C CA  A VAL A 18  ? 0.18365 0.20755 0.16205 -0.02670 0.02940  -0.01070 15  VAL A CA  
378  C CA  B VAL A 18  ? 0.18365 0.20755 0.16205 -0.02670 0.02940  -0.01070 15  VAL A CA  
379  C C   . VAL A 18  ? 0.16854 0.17089 0.13471 -0.04632 0.02724  -0.00147 15  VAL A C   
380  O O   . VAL A 18  ? 0.15368 0.15419 0.11035 -0.01145 0.01410  0.01769  15  VAL A O   
381  C CB  A VAL A 18  ? 0.24685 0.24535 0.19665 -0.01720 0.01230  -0.00240 15  VAL A CB  
382  C CB  B VAL A 18  ? 0.24685 0.24535 0.19665 -0.01720 0.01230  -0.00240 15  VAL A CB  
383  C CG1 A VAL A 18  ? 0.24895 0.27145 0.19485 -0.03390 0.03460  0.00990  15  VAL A CG1 
384  C CG1 B VAL A 18  ? 0.24895 0.27145 0.19485 -0.03390 0.03460  0.00990  15  VAL A CG1 
385  C CG2 A VAL A 18  ? 0.26815 0.29565 0.20825 -0.00830 -0.00690 -0.00400 15  VAL A CG2 
386  C CG2 B VAL A 18  ? 0.26815 0.29565 0.20825 -0.00830 -0.00690 -0.00400 15  VAL A CG2 
402  N N   . SER A 19  ? 0.22085 0.19227 0.14943 -0.04512 0.04016  0.02666  16  SER A N   
403  C CA  . SER A 19  ? 0.25001 0.23014 0.20020 -0.05793 0.04362  0.01992  16  SER A CA  
404  C C   . SER A 19  ? 0.28442 0.27866 0.24621 -0.00991 0.02431  0.00858  16  SER A C   
405  O O   . SER A 19  ? 0.32779 0.29730 0.28230 -0.00575 -0.01109 -0.02847 16  SER A O   
406  C CB  . SER A 19  ? 0.26314 0.27389 0.21595 -0.04669 0.04364  0.05670  16  SER A CB  
407  O OG  . SER A 19  ? 0.26621 0.32318 0.26862 -0.04942 0.01611  0.07646  16  SER A OG  
413  N N   . LYS A 20  ? 0.32158 0.34146 0.28794 -0.00559 0.04297  -0.00992 17  LYS A N   
414  C CA  . LYS A 20  ? 0.37449 0.40927 0.33573 -0.00418 0.03434  0.00815  17  LYS A CA  
415  C C   . LYS A 20  ? 0.39397 0.39859 0.36588 -0.02492 0.02843  0.01595  17  LYS A C   
416  O O   . LYS A 20  ? 0.41925 0.44375 0.39849 0.01388  0.00785  -0.00981 17  LYS A O   
417  C CB  . LYS A 20  ? 0.39208 0.43114 0.35796 -0.00556 0.02815  -0.00949 17  LYS A CB  
418  C CG  . LYS A 20  ? 0.40269 0.42150 0.36612 -0.01414 0.02768  0.01405  17  LYS A CG  
419  C CD  . LYS A 20  ? 0.40132 0.40504 0.36173 -0.01387 0.03063  -0.01968 17  LYS A CD  
420  C CE  . LYS A 20  ? 0.40075 0.38556 0.33881 -0.02878 0.04725  -0.03264 17  LYS A CE  
421  N NZ  . LYS A 20  ? 0.36957 0.31762 0.30406 -0.01971 0.04957  -0.05016 17  LYS A NZ  
435  N N   . SER A 21  ? 0.38152 0.39698 0.36601 -0.03476 0.05059  0.00048  18  SER A N   
436  C CA  . SER A 21  ? 0.38406 0.41429 0.36931 -0.04288 0.04442  0.01845  18  SER A CA  
437  C C   . SER A 21  ? 0.37519 0.40238 0.33848 -0.04133 0.07456  0.02349  18  SER A C   
438  O O   . SER A 21  ? 0.38517 0.42662 0.34911 -0.04256 0.08381  0.04897  18  SER A O   
439  C CB  . SER A 21  ? 0.40574 0.44827 0.39984 -0.02488 0.03312  0.02681  18  SER A CB  
440  O OG  . SER A 21  ? 0.41401 0.46072 0.41573 -0.00483 0.02862  0.01673  18  SER A OG  
446  N N   . GLY A 22  ? 0.33700 0.32458 0.29270 -0.06686 0.07924  0.01220  19  GLY A N   
447  C CA  . GLY A 22  ? 0.29256 0.25480 0.26453 -0.07834 0.07406  0.00014  19  GLY A CA  
448  C C   . GLY A 22  ? 0.25936 0.25250 0.22734 -0.08976 0.09228  0.01520  19  GLY A C   
449  O O   . GLY A 22  ? 0.28144 0.27487 0.24000 -0.06887 0.13017  -0.03007 19  GLY A O   
453  N N   . THR A 23  ? 0.21414 0.24323 0.20410 -0.04845 0.04947  0.04672  20  THR A N   
454  C CA  . THR A 23  ? 0.19033 0.21605 0.20543 -0.02456 0.05072  0.01556  20  THR A CA  
455  C C   . THR A 23  ? 0.19309 0.22591 0.23522 -0.02361 0.02803  0.00722  20  THR A C   
456  O O   . THR A 23  ? 0.20623 0.28314 0.27697 -0.04432 0.01640  0.01339  20  THR A O   
457  C CB  . THR A 23  ? 0.20882 0.26454 0.20832 0.01040  0.04925  -0.00875 20  THR A CB  
458  O OG1 . THR A 23  ? 0.22332 0.29207 0.22027 0.01078  0.04935  -0.00563 20  THR A OG1 
459  C CG2 . THR A 23  ? 0.22051 0.27374 0.18692 0.00681  0.04540  -0.01624 20  THR A CG2 
467  N N   . VAL A 24  ? 0.20390 0.18838 0.20837 -0.02110 0.01114  0.00100  21  VAL A N   
468  C CA  . VAL A 24  ? 0.22316 0.27083 0.23595 -0.00760 0.01480  -0.03354 21  VAL A CA  
469  C C   . VAL A 24  ? 0.19675 0.23634 0.21823 0.00910  0.02057  -0.06064 21  VAL A C   
470  O O   . VAL A 24  ? 0.15894 0.30222 0.22712 -0.00887 -0.02057 -0.05643 21  VAL A O   
471  C CB  . VAL A 24  ? 0.25280 0.27443 0.24181 0.00291  0.01076  -0.02106 21  VAL A CB  
472  C CG1 . VAL A 24  ? 0.25953 0.34068 0.24719 -0.01591 0.05783  -0.02428 21  VAL A CG1 
473  C CG2 . VAL A 24  ? 0.27666 0.31906 0.24814 -0.00090 0.01423  -0.01768 21  VAL A CG2 
483  N N   . SER A 25  ? 0.19936 0.22454 0.21034 -0.01446 0.07005  -0.02093 22  SER A N   
487  C C   . SER A 25  ? 0.18538 0.21873 0.20549 -0.01985 0.01954  -0.00198 22  SER A C   
488  O O   . SER A 25  ? 0.15350 0.27159 0.19493 -0.00219 -0.00388 -0.00910 22  SER A O   
510  N N   . PRO A 26  ? 0.14951 0.20918 0.18660 -0.01103 0.01772  -0.01532 23  PRO A N   
511  C CA  . PRO A 26  ? 0.13794 0.20842 0.18143 -0.03889 0.01788  -0.03012 23  PRO A CA  
512  C C   . PRO A 26  ? 0.13131 0.21757 0.19399 -0.02337 0.02167  -0.03089 23  PRO A C   
513  O O   . PRO A 26  ? 0.14191 0.24386 0.17365 -0.03113 0.02361  -0.00638 23  PRO A O   
514  C CB  . PRO A 26  ? 0.16323 0.25424 0.19996 -0.05021 0.02311  -0.02582 23  PRO A CB  
515  C CG  . PRO A 26  ? 0.18054 0.22344 0.20772 -0.03408 0.01763  0.00553  23  PRO A CG  
516  C CD  . PRO A 26  ? 0.15670 0.24364 0.19437 -0.01864 0.00721  0.01146  23  PRO A CD  
524  N N   . ILE A 27  ? 0.16282 0.21073 0.18966 0.02864  0.03629  -0.02606 24  ILE A N   
525  C CA  . ILE A 27  ? 0.17220 0.15412 0.18573 0.00624  0.02564  -0.01914 24  ILE A CA  
526  C C   . ILE A 27  ? 0.16427 0.14191 0.17558 -0.00543 0.04329  -0.00135 24  ILE A C   
527  O O   . ILE A 27  ? 0.15146 0.19056 0.17922 0.03076  0.02147  0.00478  24  ILE A O   
528  C CB  . ILE A 27  ? 0.20049 0.22566 0.19184 0.02191  0.02890  -0.03406 24  ILE A CB  
529  C CG1 . ILE A 27  ? 0.23128 0.26030 0.20898 0.02802  0.03828  -0.05040 24  ILE A CG1 
530  C CG2 . ILE A 27  ? 0.19388 0.25495 0.19585 0.03532  0.05524  -0.02818 24  ILE A CG2 
531  C CD1 . ILE A 27  ? 0.25600 0.31943 0.22329 0.02059  0.03224  -0.04317 24  ILE A CD1 
543  N N   . SER A 28  ? 0.16543 0.17132 0.16882 -0.01317 0.06031  -0.01423 25  SER A N   
546  C C   . SER A 28  ? 0.15727 0.14516 0.15774 -0.02302 0.03899  0.00851  25  SER A C   
547  O O   . SER A 28  ? 0.16486 0.17835 0.16221 -0.00155 0.03844  -0.00337 25  SER A O   
562  N N   . LEU A 29  ? 0.13436 0.17680 0.13542 0.02957  0.01052  0.00242  26  LEU A N   
563  C CA  . LEU A 29  ? 0.11836 0.18387 0.11144 0.03984  -0.00378 0.00721  26  LEU A CA  
564  C C   . LEU A 29  ? 0.10703 0.18039 0.12675 0.00435  0.00452  -0.00571 26  LEU A C   
565  O O   . LEU A 29  ? 0.08978 0.19479 0.13300 -0.00308 0.01374  0.00342  26  LEU A O   
566  C CB  . LEU A 29  ? 0.14277 0.19255 0.13136 0.03487  0.00783  -0.00929 26  LEU A CB  
567  C CG  . LEU A 29  ? 0.15324 0.20218 0.18204 0.05384  0.00342  0.02669  26  LEU A CG  
568  C CD1 . LEU A 29  ? 0.18751 0.26312 0.23240 0.07849  0.02001  0.01323  26  LEU A CD1 
569  C CD2 . LEU A 29  ? 0.16940 0.21895 0.20844 0.04334  0.02262  -0.00625 26  LEU A CD2 
581  N N   . ALA A 30  ? 0.14136 0.15000 0.13800 -0.00069 0.03136  0.01242  27  ALA A N   
582  C CA  . ALA A 30  ? 0.13989 0.11483 0.14984 0.00140  0.02879  0.00415  27  ALA A CA  
583  C C   . ALA A 30  ? 0.13622 0.15040 0.17275 0.00784  0.01418  -0.01914 27  ALA A C   
584  O O   . ALA A 30  ? 0.14381 0.17514 0.18853 -0.01760 -0.00859 -0.05380 27  ALA A O   
585  C CB  . ALA A 30  ? 0.16329 0.15310 0.16187 0.00867  0.04733  -0.01763 27  ALA A CB  
591  N N   . GLY A 31  ? 0.14357 0.17610 0.18460 0.02820  0.02817  0.01296  28  GLY A N   
592  C CA  . GLY A 31  ? 0.14794 0.20225 0.17755 0.07686  -0.00669 -0.00045 28  GLY A CA  
593  C C   . GLY A 31  ? 0.14526 0.19104 0.16033 0.05225  -0.02420 -0.00580 28  GLY A C   
594  O O   . GLY A 31  ? 0.20023 0.24012 0.17546 0.06278  -0.01173 -0.00382 28  GLY A O   
598  N N   . LYS A 32  ? 0.12394 0.18248 0.15243 0.05078  -0.01858 0.02300  29  LYS A N   
601  C C   . LYS A 32  ? 0.12514 0.15421 0.14352 -0.01581 -0.04812 -0.02244 29  LYS A C   
602  O O   . LYS A 32  ? 0.13067 0.18744 0.15899 -0.02423 -0.00715 -0.04063 29  LYS A O   
639  N N   . THR A 33  ? 0.11118 0.13081 0.14209 -0.01488 -0.04970 -0.03968 30  THR A N   
640  C CA  . THR A 33  ? 0.09169 0.13652 0.14233 -0.00493 -0.06141 -0.01297 30  THR A CA  
641  C C   . THR A 33  ? 0.08821 0.14834 0.12679 -0.03144 -0.01538 -0.00007 30  THR A C   
642  O O   . THR A 33  ? 0.10596 0.15116 0.12197 -0.01687 -0.02603 0.00179  30  THR A O   
643  C CB  . THR A 33  ? 0.10137 0.12380 0.15558 0.02857  -0.04048 0.00476  30  THR A CB  
644  O OG1 . THR A 33  ? 0.14493 0.15914 0.13701 -0.00121 -0.00287 0.01358  30  THR A OG1 
645  C CG2 . THR A 33  ? 0.12133 0.18686 0.17572 -0.02042 -0.02988 0.00535  30  THR A CG2 
653  N N   . VAL A 34  ? 0.09252 0.12126 0.13830 -0.00348 -0.00047 -0.01094 31  VAL A N   
654  C CA  . VAL A 34  ? 0.08138 0.11256 0.15306 0.02699  -0.02169 -0.00648 31  VAL A CA  
655  C C   . VAL A 34  ? 0.09647 0.10309 0.13017 -0.01142 -0.00555 0.00508  31  VAL A C   
656  O O   . VAL A 34  ? 0.12552 0.09443 0.12269 -0.02427 0.01498  0.00077  31  VAL A O   
657  C CB  . VAL A 34  ? 0.11747 0.12259 0.17363 0.04354  0.00315  -0.00367 31  VAL A CB  
658  C CG1 . VAL A 34  ? 0.13381 0.14395 0.15836 0.01343  0.01310  -0.01753 31  VAL A CG1 
659  C CG2 . VAL A 34  ? 0.11652 0.14039 0.18029 0.03092  0.02056  -0.00273 31  VAL A CG2 
669  N N   . PHE A 35  ? 0.10114 0.12373 0.12484 0.00205  -0.00458 0.01946  32  PHE A N   
670  C CA  A PHE A 35  ? 0.10525 0.11565 0.12855 0.00070  -0.00660 0.02080  32  PHE A CA  
671  C CA  B PHE A 35  ? 0.10525 0.11565 0.12855 0.00070  -0.00660 0.02080  32  PHE A CA  
672  C C   . PHE A 35  ? 0.08122 0.11212 0.11479 -0.03222 -0.01771 0.00807  32  PHE A C   
673  O O   . PHE A 35  ? 0.07832 0.16310 0.13442 -0.03071 -0.00353 0.00965  32  PHE A O   
674  C CB  A PHE A 35  ? 0.13715 0.14655 0.13175 -0.00110 -0.00030 -0.00990 32  PHE A CB  
675  C CB  B PHE A 35  ? 0.13715 0.14655 0.13175 -0.00110 -0.00030 -0.00990 32  PHE A CB  
676  C CG  A PHE A 35  ? 0.16135 0.20545 0.12625 0.00230  0.00700  -0.00310 32  PHE A CG  
677  C CG  B PHE A 35  ? 0.16135 0.20545 0.12625 0.00230  0.00700  -0.00310 32  PHE A CG  
678  C CD1 A PHE A 35  ? 0.19225 0.24265 0.13355 -0.00300 0.01680  -0.00160 32  PHE A CD1 
679  C CD1 B PHE A 35  ? 0.19225 0.24265 0.13355 -0.00300 0.01680  -0.00160 32  PHE A CD1 
680  C CD2 A PHE A 35  ? 0.16905 0.20905 0.13605 -0.00420 0.00570  0.02050  32  PHE A CD2 
681  C CD2 B PHE A 35  ? 0.16905 0.20905 0.13605 -0.00420 0.00570  0.02050  32  PHE A CD2 
682  C CE1 A PHE A 35  ? 0.20695 0.23365 0.14585 0.01190  0.01920  -0.00930 32  PHE A CE1 
683  C CE1 B PHE A 35  ? 0.20695 0.23365 0.14585 0.01190  0.01920  -0.00930 32  PHE A CE1 
684  C CE2 A PHE A 35  ? 0.17945 0.21095 0.13745 -0.00090 0.00110  -0.00020 32  PHE A CE2 
685  C CE2 B PHE A 35  ? 0.17945 0.21095 0.13745 -0.00090 0.00110  -0.00020 32  PHE A CE2 
686  C CZ  A PHE A 35  ? 0.19765 0.21885 0.14975 0.00250  0.01290  -0.01140 32  PHE A CZ  
687  C CZ  B PHE A 35  ? 0.19765 0.21885 0.14975 0.00250  0.01290  -0.01140 32  PHE A CZ  
704  N N   . PHE A 36  ? 0.07101 0.11323 0.09624 -0.02124 -0.01801 -0.00063 33  PHE A N   
705  C CA  . PHE A 36  ? 0.09604 0.11557 0.09677 -0.00563 -0.01085 -0.01637 33  PHE A CA  
706  C C   . PHE A 36  ? 0.11091 0.12594 0.08628 0.02456  -0.01227 0.02979  33  PHE A C   
707  O O   . PHE A 36  ? 0.12025 0.14091 0.09796 0.00937  0.02582  0.03368  33  PHE A O   
708  C CB  . PHE A 36  ? 0.12821 0.12900 0.09689 -0.00556 0.01191  -0.00409 33  PHE A CB  
709  C CG  . PHE A 36  ? 0.12769 0.09929 0.13238 -0.03375 -0.00520 -0.01942 33  PHE A CG  
710  C CD1 . PHE A 36  ? 0.14360 0.16337 0.15062 -0.01572 0.01582  -0.00624 33  PHE A CD1 
711  C CD2 . PHE A 36  ? 0.15517 0.18748 0.15809 0.01942  0.03307  -0.01257 33  PHE A CD2 
712  C CE1 . PHE A 36  ? 0.15602 0.21715 0.16347 0.01237  0.02768  -0.01467 33  PHE A CE1 
713  C CE2 . PHE A 36  ? 0.18671 0.20207 0.17122 0.03326  0.04240  -0.02851 33  PHE A CE2 
714  C CZ  . PHE A 36  ? 0.16928 0.20276 0.15947 0.02640  0.04122  -0.03106 33  PHE A CZ  
724  N N   . TYR A 37  ? 0.10529 0.11885 0.08846 -0.01702 -0.00879 0.01026  34  TYR A N   
725  C CA  . TYR A 37  ? 0.11942 0.08932 0.09719 -0.01506 0.02693  -0.01801 34  TYR A CA  
726  C C   . TYR A 37  ? 0.10679 0.10139 0.09655 -0.01356 -0.01501 -0.02492 34  TYR A C   
727  O O   . TYR A 37  ? 0.08071 0.10152 0.07869 -0.00072 -0.01501 0.00922  34  TYR A O   
728  C CB  . TYR A 37  ? 0.09802 0.12190 0.09802 -0.02312 0.00443  -0.02150 34  TYR A CB  
729  C CG  . TYR A 37  ? 0.10718 0.08305 0.10853 -0.01369 0.01091  -0.01344 34  TYR A CG  
730  C CD1 . TYR A 37  ? 0.13528 0.10114 0.10188 0.01938  0.02317  0.00242  34  TYR A CD1 
731  C CD2 . TYR A 37  ? 0.09760 0.08854 0.10885 -0.01033 -0.01995 -0.01597 34  TYR A CD2 
732  C CE1 . TYR A 37  ? 0.13089 0.09393 0.11169 -0.01950 0.02809  0.00031  34  TYR A CE1 
733  C CE2 . TYR A 37  ? 0.13296 0.09022 0.09970 -0.00373 -0.00339 0.01756  34  TYR A CE2 
734  C CZ  . TYR A 37  ? 0.14601 0.08130 0.11665 -0.00789 0.02977  0.01189  34  TYR A CZ  
735  O OH  . TYR A 37  ? 0.13744 0.11458 0.12488 -0.00294 0.01980  -0.02109 34  TYR A OH  
745  N N   . PHE A 38  ? 0.10360 0.07137 0.11333 -0.00146 -0.00919 -0.00186 35  PHE A N   
746  C CA  . PHE A 38  ? 0.11092 0.06251 0.10030 -0.00659 0.00478  0.01757  35  PHE A CA  
747  C C   . PHE A 38  ? 0.09914 0.08505 0.08943 -0.03696 -0.01262 -0.00094 35  PHE A C   
748  O O   . PHE A 38  ? 0.09297 0.09005 0.09203 0.00253  -0.00709 0.00461  35  PHE A O   
749  C CB  . PHE A 38  ? 0.11623 0.05405 0.10491 0.01381  -0.02133 0.01401  35  PHE A CB  
750  C CG  . PHE A 38  ? 0.10546 0.07771 0.10709 -0.00456 -0.02895 0.00699  35  PHE A CG  
751  C CD1 . PHE A 38  ? 0.10500 0.13890 0.10700 0.01931  -0.01389 -0.00270 35  PHE A CD1 
752  C CD2 . PHE A 38  ? 0.10649 0.09295 0.10330 -0.03823 -0.02866 0.00376  35  PHE A CD2 
753  C CE1 . PHE A 38  ? 0.12448 0.11957 0.12590 0.00199  -0.00480 0.02369  35  PHE A CE1 
754  C CE2 . PHE A 38  ? 0.14093 0.11734 0.08700 -0.01465 -0.00673 -0.01864 35  PHE A CE2 
755  C CZ  . PHE A 38  ? 0.13384 0.10023 0.12853 0.00234  0.00948  0.00235  35  PHE A CZ  
765  N N   . SER A 39  ? 0.11633 0.09533 0.08011 0.00886  0.01336  -0.00153 36  SER A N   
766  C CA  . SER A 39  ? 0.10866 0.11092 0.09675 0.01106  0.00083  -0.01003 36  SER A CA  
767  C C   . SER A 39  ? 0.09302 0.09255 0.10839 0.00495  -0.01656 0.01639  36  SER A C   
768  O O   . SER A 39  ? 0.13854 0.12840 0.09304 0.02534  0.01062  0.00954  36  SER A O   
769  C CB  . SER A 39  ? 0.10920 0.11676 0.10164 0.00457  -0.02043 -0.02347 36  SER A CB  
770  O OG  . SER A 39  ? 0.13784 0.11194 0.12035 -0.00700 0.01036  0.00517  36  SER A OG  
776  N N   . ALA A 40  ? 0.09961 0.09935 0.12041 0.00538  -0.01318 0.00705  37  ALA A N   
777  C CA  . ALA A 40  ? 0.13508 0.09995 0.10536 0.00886  -0.01993 -0.00411 37  ALA A CA  
778  C C   . ALA A 40  ? 0.13018 0.08505 0.09876 0.00856  -0.02829 0.02737  37  ALA A C   
779  O O   . ALA A 40  ? 0.15106 0.09327 0.09584 0.01771  -0.00289 0.01184  37  ALA A O   
780  C CB  . ALA A 40  ? 0.15101 0.14028 0.09545 -0.06424 -0.04505 0.00647  37  ALA A CB  
786  N N   . SER A 41  ? 0.14064 0.09067 0.09718 0.00488  -0.02288 0.01874  38  SER A N   
787  C CA  . SER A 41  ? 0.16525 0.09080 0.12347 0.01109  -0.02116 -0.01524 38  SER A CA  
788  C C   . SER A 41  ? 0.17656 0.09286 0.14258 0.02292  -0.00627 -0.01862 38  SER A C   
789  O O   . SER A 41  ? 0.20672 0.10667 0.16672 0.03420  0.00874  -0.01505 38  SER A O   
790  C CB  . SER A 41  ? 0.17870 0.05460 0.14360 0.00364  -0.04101 -0.00981 38  SER A CB  
791  O OG  . SER A 41  ? 0.20420 0.09512 0.13515 -0.00999 -0.00829 0.02217  38  SER A OG  
797  N N   . TRP A 42  ? 0.14716 0.08787 0.15323 0.03214  -0.00984 0.03389  39  TRP A N   
798  C CA  . TRP A 42  ? 0.15076 0.10005 0.15882 0.03300  -0.00282 0.01104  39  TRP A CA  
799  C C   . TRP A 42  ? 0.14243 0.15528 0.15229 0.02691  0.00450  0.00256  39  TRP A C   
800  O O   . TRP A 42  ? 0.16460 0.21485 0.14327 0.05216  0.02844  0.04763  39  TRP A O   
801  C CB  . TRP A 42  ? 0.15293 0.16065 0.13997 0.00303  0.00522  0.06197  39  TRP A CB  
802  C CG  . TRP A 42  ? 0.15392 0.21911 0.12593 -0.00846 -0.00633 0.04805  39  TRP A CG  
803  C CD1 . TRP A 42  ? 0.17521 0.20297 0.12962 -0.01628 0.00626  0.05514  39  TRP A CD1 
804  C CD2 . TRP A 42  ? 0.15091 0.18740 0.11334 -0.01091 -0.00693 -0.00450 39  TRP A CD2 
805  N NE1 . TRP A 42  ? 0.17155 0.23629 0.12069 -0.03636 0.03446  0.02232  39  TRP A NE1 
806  C CE2 . TRP A 42  ? 0.14910 0.20739 0.12929 -0.03019 0.01023  -0.01095 39  TRP A CE2 
807  C CE3 . TRP A 42  ? 0.15192 0.20154 0.12878 -0.00704 0.01835  -0.01488 39  TRP A CE3 
808  C CZ2 . TRP A 42  ? 0.14858 0.21609 0.14716 -0.02175 -0.01604 -0.01111 39  TRP A CZ2 
809  C CZ3 . TRP A 42  ? 0.16033 0.19891 0.15924 0.01492  0.00980  0.01480  39  TRP A CZ3 
810  C CH2 . TRP A 42  ? 0.15249 0.17338 0.17032 -0.00241 -0.00528 0.01169  39  TRP A CH2 
821  N N   . CYS A 43  ? 0.12889 0.13203 0.14296 0.01293  -0.00297 0.00357  40  CYS A N   
822  C CA  . CYS A 43  ? 0.12346 0.12540 0.13805 0.02489  -0.02320 0.03076  40  CYS A CA  
823  C C   . CYS A 43  ? 0.11882 0.15845 0.14648 -0.01155 0.00627  -0.00385 40  CYS A C   
824  O O   . CYS A 43  ? 0.13443 0.13494 0.12429 -0.00273 0.01577  0.01397  40  CYS A O   
825  C CB  . CYS A 43  ? 0.17571 0.17935 0.15354 0.02634  -0.00671 0.07155  40  CYS A CB  
826  S SG  . CYS A 43  ? 0.21054 0.18279 0.17671 -0.01041 0.00725  -0.00485 40  CYS A SG  
832  N N   . PRO A 44  ? 0.10104 0.12924 0.17976 0.00577  -0.02602 -0.01032 41  PRO A N   
833  C CA  . PRO A 44  ? 0.13432 0.11729 0.19797 0.04139  -0.00643 -0.01460 41  PRO A CA  
834  C C   . PRO A 44  ? 0.12915 0.15918 0.17180 0.00568  0.01556  -0.02332 41  PRO A C   
835  O O   . PRO A 44  ? 0.13679 0.13585 0.15507 0.02160  0.00472  -0.03654 41  PRO A O   
836  C CB  . PRO A 44  ? 0.14299 0.18598 0.20810 0.04244  -0.00753 -0.04275 41  PRO A CB  
837  C CG  . PRO A 44  ? 0.14566 0.20695 0.21054 0.01176  0.00750  -0.02610 41  PRO A CG  
838  C CD  . PRO A 44  ? 0.12260 0.13169 0.20455 0.01328  -0.01697 -0.02058 41  PRO A CD  
846  N N   . PRO A 45  ? 0.10750 0.14574 0.14911 0.00938  0.00590  -0.01520 42  PRO A N   
847  C CA  . PRO A 45  ? 0.13922 0.13217 0.15024 0.03360  0.01708  -0.01966 42  PRO A CA  
848  C C   . PRO A 45  ? 0.12393 0.11074 0.10307 0.02106  -0.02221 -0.02060 42  PRO A C   
849  O O   . PRO A 45  ? 0.13218 0.15465 0.08434 0.02564  -0.01512 -0.02157 42  PRO A O   
850  C CB  . PRO A 45  ? 0.13516 0.13347 0.16606 -0.01661 -0.01752 -0.01860 42  PRO A CB  
851  C CG  . PRO A 45  ? 0.16093 0.21735 0.16422 -0.05920 -0.03325 0.02911  42  PRO A CG  
852  C CD  . PRO A 45  ? 0.12593 0.17356 0.14413 0.01812  -0.00678 0.02036  42  PRO A CD  
860  N N   . CYS A 46  ? 0.10712 0.11969 0.11462 0.01833  -0.01831 -0.01305 43  CYS A N   
861  C CA  . CYS A 46  ? 0.11128 0.12551 0.10886 0.02904  -0.03125 -0.02714 43  CYS A CA  
862  C C   . CYS A 46  ? 0.11547 0.08660 0.09637 0.01101  -0.01233 -0.02520 43  CYS A C   
863  O O   . CYS A 46  ? 0.13708 0.13253 0.09436 0.01588  -0.00573 -0.00187 43  CYS A O   
864  C CB  . CYS A 46  ? 0.15294 0.11176 0.12179 -0.00476 -0.01659 -0.03971 43  CYS A CB  
865  S SG  . CYS A 46  ? 0.26806 0.10825 0.11571 -0.00858 -0.00494 -0.00181 43  CYS A SG  
871  N N   . ARG A 47  ? 0.13006 0.10475 0.12918 0.01630  0.00982  0.00871  44  ARG A N   
872  C CA  . ARG A 47  ? 0.16336 0.11801 0.16145 0.00548  0.00834  -0.00683 44  ARG A CA  
873  C C   . ARG A 47  ? 0.13992 0.07908 0.13864 -0.01810 -0.00241 -0.01232 44  ARG A C   
874  O O   . ARG A 47  ? 0.13421 0.12941 0.14978 -0.03434 -0.00312 0.00883  44  ARG A O   
875  C CB  . ARG A 47  ? 0.19762 0.05734 0.17957 0.01001  0.00737  0.00732  44  ARG A CB  
876  C CG  . ARG A 47  ? 0.24053 0.13031 0.22137 0.04301  0.00614  0.01658  44  ARG A CG  
877  C CD  . ARG A 47  ? 0.31462 0.30947 0.29580 0.02703  0.03410  0.02010  44  ARG A CD  
878  N NE  . ARG A 47  ? 0.38475 0.41923 0.36717 0.01748  0.07227  -0.00377 44  ARG A NE  
879  C CZ  . ARG A 47  ? 0.43139 0.47380 0.41199 0.01795  0.07071  -0.00295 44  ARG A CZ  
880  N NH1 . ARG A 47  ? 0.44428 0.48843 0.43304 0.01586  0.06446  -0.03105 44  ARG A NH1 
881  N NH2 . ARG A 47  ? 0.42767 0.45745 0.43348 0.02911  0.08975  -0.00128 44  ARG A NH2 
895  N N   . GLY A 48  ? 0.14445 0.10671 0.14178 -0.00359 0.00017  -0.02491 45  GLY A N   
896  C CA  . GLY A 48  ? 0.16017 0.14440 0.12733 0.00003  -0.00662 -0.01866 45  GLY A CA  
897  C C   . GLY A 48  ? 0.14480 0.16479 0.12137 -0.00835 -0.02949 -0.01500 45  GLY A C   
898  O O   . GLY A 48  ? 0.19163 0.16494 0.15401 -0.03396 -0.03395 -0.02500 45  GLY A O   
902  N N   . PHE A 49  ? 0.13676 0.14502 0.11479 0.01270  0.00009  -0.01263 46  PHE A N   
903  C CA  . PHE A 49  ? 0.11737 0.11148 0.09599 -0.01058 -0.00810 -0.00237 46  PHE A CA  
904  C C   . PHE A 49  ? 0.11300 0.08394 0.10918 0.03116  0.00033  0.00408  46  PHE A C   
905  O O   . PHE A 49  ? 0.10820 0.09912 0.11143 0.01477  -0.02134 0.02704  46  PHE A O   
906  C CB  . PHE A 49  ? 0.12531 0.13212 0.09379 -0.00467 -0.01022 -0.01804 46  PHE A CB  
907  C CG  . PHE A 49  ? 0.12514 0.11318 0.11380 -0.01637 -0.01315 0.00610  46  PHE A CG  
908  C CD1 . PHE A 49  ? 0.12544 0.14620 0.11484 -0.00408 -0.02744 0.03086  46  PHE A CD1 
909  C CD2 . PHE A 49  ? 0.10756 0.13710 0.12072 0.00125  -0.00858 -0.02064 46  PHE A CD2 
910  C CE1 . PHE A 49  ? 0.13401 0.13994 0.11972 -0.01271 -0.01126 0.02870  46  PHE A CE1 
911  C CE2 . PHE A 49  ? 0.12484 0.13385 0.13524 -0.00997 0.02094  -0.02019 46  PHE A CE2 
912  C CZ  . PHE A 49  ? 0.13722 0.15676 0.14031 -0.02088 0.01614  0.01625  46  PHE A CZ  
922  N N   . THR A 50  ? 0.12810 0.11780 0.10209 -0.00585 -0.01393 0.00072  47  THR A N   
923  C CA  . THR A 50  ? 0.15411 0.08928 0.09778 -0.00567 0.01668  0.02479  47  THR A CA  
924  C C   . THR A 50  ? 0.12065 0.07367 0.10505 0.00971  0.01649  0.00368  47  THR A C   
925  O O   . THR A 50  ? 0.11663 0.10932 0.11310 0.01437  0.00923  -0.00671 47  THR A O   
926  C CB  . THR A 50  ? 0.16888 0.07107 0.10472 -0.01468 0.00723  -0.00432 47  THR A CB  
927  O OG1 . THR A 50  ? 0.17065 0.11184 0.10039 -0.02105 -0.00608 0.00403  47  THR A OG1 
928  C CG2 . THR A 50  ? 0.18874 0.14398 0.10902 0.01492  0.01989  0.00731  47  THR A CG2 
936  N N   . PRO A 51  ? 0.09131 0.12129 0.12383 0.01237  -0.02469 -0.00532 48  PRO A N   
937  C CA  . PRO A 51  ? 0.10208 0.10752 0.12928 -0.01377 -0.02547 -0.02177 48  PRO A CA  
938  C C   . PRO A 51  ? 0.09118 0.11430 0.11359 -0.00906 -0.02682 0.01499  48  PRO A C   
939  O O   . PRO A 51  ? 0.10873 0.11582 0.12455 -0.00189 -0.00768 0.00460  48  PRO A O   
940  C CB  . PRO A 51  ? 0.14019 0.13759 0.16126 -0.00311 -0.04141 -0.03815 48  PRO A CB  
941  C CG  . PRO A 51  ? 0.14066 0.15688 0.18688 -0.00638 -0.03114 -0.04515 48  PRO A CG  
942  C CD  . PRO A 51  ? 0.09627 0.13212 0.14355 0.03083  -0.02481 -0.00217 48  PRO A CD  
950  N N   . THR A 52  ? 0.11054 0.10111 0.14216 0.01367  -0.01271 -0.01464 49  THR A N   
951  C CA  . THR A 52  ? 0.13431 0.07551 0.12900 0.01263  -0.01586 -0.00197 49  THR A CA  
952  C C   . THR A 52  ? 0.11743 0.06544 0.08543 -0.00556 -0.02325 0.00965  49  THR A C   
953  O O   . THR A 52  ? 0.09251 0.13942 0.08165 0.01600  -0.02069 0.00935  49  THR A O   
954  C CB  . THR A 52  ? 0.14543 0.12836 0.14251 -0.00642 -0.00687 -0.02289 49  THR A CB  
955  O OG1 . THR A 52  ? 0.18501 0.14192 0.16511 0.03698  0.03070  -0.01774 49  THR A OG1 
956  C CG2 . THR A 52  ? 0.14358 0.17903 0.14447 -0.02832 0.02549  -0.00748 49  THR A CG2 
964  N N   . LEU A 53  ? 0.12892 0.09693 0.09614 0.00271  -0.00909 -0.00684 50  LEU A N   
965  C CA  . LEU A 53  ? 0.13880 0.07036 0.12366 -0.03669 0.00015  -0.02433 50  LEU A CA  
966  C C   . LEU A 53  ? 0.13073 0.06656 0.10465 -0.01151 0.00507  0.03173  50  LEU A C   
967  O O   . LEU A 53  ? 0.09817 0.11513 0.10414 0.00705  0.00522  0.02092  50  LEU A O   
968  C CB  . LEU A 53  ? 0.12517 0.08279 0.12283 -0.02456 -0.00700 -0.01147 50  LEU A CB  
969  C CG  . LEU A 53  ? 0.13083 0.09117 0.10893 -0.00054 -0.01019 -0.01941 50  LEU A CG  
970  C CD1 . LEU A 53  ? 0.15646 0.12810 0.10502 0.00900  0.01321  -0.01569 50  LEU A CD1 
971  C CD2 . LEU A 53  ? 0.11817 0.15941 0.10912 0.00713  -0.00365 -0.00096 50  LEU A CD2 
983  N N   . VAL A 54  ? 0.14792 0.08683 0.09214 -0.03679 0.00946  0.01846  51  VAL A N   
984  C CA  . VAL A 54  ? 0.14072 0.07768 0.10627 -0.02555 -0.00205 0.04429  51  VAL A CA  
985  C C   . VAL A 54  ? 0.11687 0.09611 0.10903 0.04422  -0.03503 0.01594  51  VAL A C   
986  O O   . VAL A 54  ? 0.12724 0.09660 0.14593 0.00575  -0.01630 0.02359  51  VAL A O   
987  C CB  . VAL A 54  ? 0.11143 0.08498 0.11685 -0.01969 -0.03279 0.03951  51  VAL A CB  
988  C CG1 . VAL A 54  ? 0.12422 0.10362 0.13715 -0.01048 -0.01025 -0.01481 51  VAL A CG1 
989  C CG2 . VAL A 54  ? 0.09937 0.08162 0.12200 0.01885  -0.01797 0.03230  51  VAL A CG2 
999  N N   . GLU A 55  ? 0.10819 0.11330 0.12192 0.00178  -0.02690 -0.00736 52  GLU A N   
1000 C CA  . GLU A 55  ? 0.12608 0.11061 0.14873 -0.02195 -0.02610 -0.03468 52  GLU A CA  
1001 C C   . GLU A 55  ? 0.11190 0.12067 0.13469 -0.01762 -0.01741 -0.02058 52  GLU A C   
1002 O O   . GLU A 55  ? 0.13260 0.17570 0.13235 -0.02570 -0.02193 0.02212  52  GLU A O   
1003 C CB  . GLU A 55  ? 0.19476 0.17282 0.18419 -0.00267 0.00367  -0.06230 52  GLU A CB  
1004 C CG  . GLU A 55  ? 0.29340 0.31837 0.26371 0.01050  0.03168  -0.04559 52  GLU A CG  
1005 C CD  . GLU A 55  ? 0.38704 0.45252 0.35681 0.01939  0.05213  -0.04493 52  GLU A CD  
1006 O OE1 . GLU A 55  ? 0.40254 0.47272 0.38011 0.02162  0.08679  -0.06018 52  GLU A OE1 
1007 O OE2 . GLU A 55  ? 0.43742 0.49372 0.39955 0.03435  0.04031  -0.03828 52  GLU A OE2 
1014 N N   . PHE A 56  ? 0.10154 0.09613 0.11898 -0.00295 -0.02872 0.01256  53  PHE A N   
1015 C CA  . PHE A 56  ? 0.09302 0.12327 0.10608 0.00367  -0.02602 0.03430  53  PHE A CA  
1016 C C   . PHE A 56  ? 0.07442 0.13494 0.10847 -0.00261 -0.03242 0.03430  53  PHE A C   
1017 O O   . PHE A 56  ? 0.07956 0.15437 0.12161 0.01320  -0.01674 0.04716  53  PHE A O   
1018 C CB  . PHE A 56  ? 0.10482 0.11189 0.10683 0.01426  -0.01433 0.01061  53  PHE A CB  
1019 C CG  . PHE A 56  ? 0.11646 0.10974 0.11869 0.01374  -0.00474 0.03391  53  PHE A CG  
1020 C CD1 . PHE A 56  ? 0.15231 0.11413 0.12834 0.03222  0.00265  0.03108  53  PHE A CD1 
1021 C CD2 . PHE A 56  ? 0.15076 0.12037 0.14258 0.03432  0.02627  0.01526  53  PHE A CD2 
1022 C CE1 . PHE A 56  ? 0.17191 0.11853 0.12638 0.03305  0.00364  0.03229  53  PHE A CE1 
1023 C CE2 . PHE A 56  ? 0.16793 0.12776 0.13688 0.01966  0.04504  0.00572  53  PHE A CE2 
1024 C CZ  . PHE A 56  ? 0.15525 0.12481 0.13965 0.03431  0.01269  0.02064  53  PHE A CZ  
1034 N N   . TYR A 57  ? 0.08166 0.10123 0.11483 -0.00235 -0.03152 0.00176  54  TYR A N   
1035 C CA  . TYR A 57  ? 0.07813 0.12378 0.12017 0.00852  -0.03714 0.00027  54  TYR A CA  
1036 C C   . TYR A 57  ? 0.09554 0.12733 0.13015 0.00056  -0.01020 -0.00764 54  TYR A C   
1037 O O   . TYR A 57  ? 0.10162 0.14105 0.12276 -0.00212 -0.00284 0.00457  54  TYR A O   
1038 C CB  . TYR A 57  ? 0.11216 0.13751 0.11893 0.00829  -0.01299 0.00582  54  TYR A CB  
1039 C CG  . TYR A 57  ? 0.12455 0.13550 0.11508 0.02484  -0.01343 0.00636  54  TYR A CG  
1040 C CD1 . TYR A 57  ? 0.12785 0.13173 0.10813 -0.01184 -0.00457 -0.01910 54  TYR A CD1 
1041 C CD2 . TYR A 57  ? 0.14360 0.14724 0.10692 -0.03982 -0.00181 -0.03466 54  TYR A CD2 
1042 C CE1 . TYR A 57  ? 0.12386 0.12742 0.11486 0.00427  -0.00215 0.00220  54  TYR A CE1 
1043 C CE2 . TYR A 57  ? 0.14609 0.15884 0.10455 -0.05786 0.01674  -0.04056 54  TYR A CE2 
1044 C CZ  . TYR A 57  ? 0.14119 0.13834 0.10009 -0.01558 0.00094  0.01342  54  TYR A CZ  
1045 O OH  . TYR A 57  ? 0.15963 0.20442 0.10948 -0.00969 0.02554  -0.01215 54  TYR A OH  
1055 N N   . GLU A 58  ? 0.12410 0.12584 0.12892 -0.01525 0.00904  0.00127  55  GLU A N   
1056 C CA  . GLU A 58  ? 0.12280 0.09933 0.14964 -0.03639 -0.00962 0.00594  55  GLU A CA  
1057 C C   . GLU A 58  ? 0.10111 0.13494 0.14427 -0.04870 -0.01573 -0.02545 55  GLU A C   
1058 O O   . GLU A 58  ? 0.10725 0.18928 0.17373 -0.03507 -0.01074 0.01491  55  GLU A O   
1059 C CB  . GLU A 58  ? 0.16117 0.14625 0.17631 -0.05298 -0.01644 -0.00548 55  GLU A CB  
1060 C CG  . GLU A 58  ? 0.19146 0.20970 0.23115 -0.05845 -0.01725 0.00819  55  GLU A CG  
1061 C CD  . GLU A 58  ? 0.27457 0.28686 0.26373 -0.04621 -0.00323 0.01407  55  GLU A CD  
1062 O OE1 . GLU A 58  ? 0.31464 0.32120 0.29905 0.00042  0.01226  0.02203  55  GLU A OE1 
1063 O OE2 . GLU A 58  ? 0.29972 0.29921 0.26386 -0.07401 -0.01243 0.05755  55  GLU A OE2 
1070 N N   . LYS A 59  ? 0.10964 0.12848 0.13426 -0.00528 -0.01278 -0.01182 56  LYS A N   
1071 C CA  . LYS A 59  ? 0.12821 0.13105 0.13778 -0.01212 -0.01576 0.03714  56  LYS A CA  
1072 C C   . LYS A 59  ? 0.09520 0.14599 0.12337 -0.03120 -0.02125 0.00708  56  LYS A C   
1073 O O   . LYS A 59  ? 0.10286 0.17780 0.14117 -0.00485 -0.01993 0.01884  56  LYS A O   
1074 C CB  . LYS A 59  ? 0.18823 0.16669 0.17785 -0.02620 -0.00642 0.03881  56  LYS A CB  
1075 C CG  . LYS A 59  ? 0.28586 0.28019 0.25822 -0.00156 0.04359  0.02683  56  LYS A CG  
1076 C CD  . LYS A 59  ? 0.37699 0.41121 0.35328 0.00538  0.08697  0.00233  56  LYS A CD  
1077 C CE  . LYS A 59  ? 0.45623 0.53433 0.43002 -0.00071 0.11985  0.00499  56  LYS A CE  
1078 N NZ  . LYS A 59  ? 0.48017 0.58646 0.46723 0.00062  0.14065  -0.00258 56  LYS A NZ  
1092 N N   . PHE A 60  ? 0.11000 0.15881 0.12121 -0.03169 -0.02498 0.06770  57  PHE A N   
1093 C CA  . PHE A 60  ? 0.12908 0.15866 0.14430 -0.00021 -0.01793 0.05953  57  PHE A CA  
1094 C C   . PHE A 60  ? 0.11506 0.11783 0.14131 0.01522  -0.03087 0.04575  57  PHE A C   
1095 O O   . PHE A 60  ? 0.11595 0.11820 0.17585 0.00217  -0.02869 0.02161  57  PHE A O   
1096 C CB  . PHE A 60  ? 0.11847 0.15630 0.14649 -0.02663 -0.02421 0.03428  57  PHE A CB  
1097 C CG  . PHE A 60  ? 0.11749 0.16132 0.14338 0.01793  -0.01788 0.05733  57  PHE A CG  
1098 C CD1 . PHE A 60  ? 0.11740 0.17503 0.13920 0.03317  -0.01246 0.03187  57  PHE A CD1 
1099 C CD2 . PHE A 60  ? 0.13393 0.19346 0.13584 0.01294  0.01678  0.04679  57  PHE A CD2 
1100 C CE1 . PHE A 60  ? 0.15620 0.20164 0.14033 0.00101  -0.00695 0.03975  57  PHE A CE1 
1101 C CE2 . PHE A 60  ? 0.13607 0.22385 0.12390 0.02857  0.03137  0.05486  57  PHE A CE2 
1102 C CZ  . PHE A 60  ? 0.16075 0.22218 0.12091 0.00853  0.01915  0.02683  57  PHE A CZ  
1112 N N   . ARG A 61  ? 0.11985 0.13576 0.14429 0.00308  -0.01319 -0.00126 58  ARG A N   
1113 C CA  . ARG A 61  ? 0.13622 0.11871 0.16012 0.05555  -0.03634 0.00585  58  ARG A CA  
1114 C C   . ARG A 61  ? 0.11995 0.10325 0.13900 0.01584  -0.04245 -0.01901 58  ARG A C   
1115 O O   . ARG A 61  ? 0.09657 0.13370 0.17845 0.02877  -0.03662 -0.01950 58  ARG A O   
1116 C CB  . ARG A 61  ? 0.19521 0.17247 0.18763 0.04179  -0.01524 -0.01490 58  ARG A CB  
1117 C CG  . ARG A 61  ? 0.25273 0.21917 0.22697 0.02840  0.01053  -0.00962 58  ARG A CG  
1118 C CD  . ARG A 61  ? 0.32247 0.30849 0.28315 0.02842  0.03512  -0.04224 58  ARG A CD  
1119 N NE  . ARG A 61  ? 0.37476 0.40752 0.34530 0.00266  0.06770  -0.01030 58  ARG A NE  
1120 C CZ  . ARG A 61  ? 0.43706 0.50477 0.41168 -0.00019 0.09608  -0.00930 58  ARG A CZ  
1121 N NH1 . ARG A 61  ? 0.45265 0.53006 0.42786 -0.00466 0.11749  -0.01186 58  ARG A NH1 
1122 N NH2 . ARG A 61  ? 0.45320 0.53135 0.43161 -0.00264 0.11174  -0.00269 58  ARG A NH2 
1136 N N   . GLU A 62  ? 0.11870 0.15673 0.14253 -0.02468 -0.02447 -0.00230 59  GLU A N   
1137 C CA  . GLU A 62  ? 0.13760 0.14213 0.16686 -0.01044 -0.01401 -0.01813 59  GLU A CA  
1138 C C   . GLU A 62  ? 0.09962 0.17787 0.16705 -0.00546 -0.01605 -0.02211 59  GLU A C   
1139 O O   . GLU A 62  ? 0.11102 0.18066 0.16840 0.00520  -0.00845 -0.03945 59  GLU A O   
1140 C CB  . GLU A 62  ? 0.22809 0.23439 0.25637 -0.01837 0.00734  -0.02163 59  GLU A CB  
1141 C CG  . GLU A 62  ? 0.33750 0.34457 0.34469 -0.02205 0.03863  0.01111  59  GLU A CG  
1142 C CD  . GLU A 62  ? 0.44031 0.49918 0.43267 -0.01230 0.06314  0.01499  59  GLU A CD  
1143 O OE1 . GLU A 62  ? 0.49117 0.53696 0.47201 -0.01926 0.07137  0.01976  59  GLU A OE1 
1144 O OE2 . GLU A 62  ? 0.49110 0.56312 0.47530 -0.01187 0.09349  0.01223  59  GLU A OE2 
1151 N N   . SER A 63  ? 0.11823 0.14547 0.14588 -0.01357 0.00266  -0.01088 60  SER A N   
1154 C C   . SER A 63  ? 0.11398 0.13617 0.13108 0.05033  -0.04338 0.02276  60  SER A C   
1155 O O   . SER A 63  ? 0.13668 0.16677 0.15249 0.03764  -0.05515 -0.00700 60  SER A O   
1170 N N   . LYS A 64  ? 0.11093 0.12580 0.12966 0.00064  -0.04053 0.00179  61  LYS A N   
1171 C CA  . LYS A 64  ? 0.14032 0.16512 0.12869 0.00601  -0.02433 0.00834  61  LYS A CA  
1172 C C   . LYS A 64  ? 0.12160 0.15058 0.13404 0.01292  -0.01976 0.00146  61  LYS A C   
1173 O O   . LYS A 64  ? 0.15339 0.17196 0.15947 -0.03569 0.00403  -0.01118 61  LYS A O   
1174 C CB  . LYS A 64  ? 0.16913 0.15495 0.13230 -0.01482 0.01560  -0.00557 61  LYS A CB  
1175 C CG  . LYS A 64  ? 0.19657 0.16047 0.15610 0.00851  0.04315  -0.01628 61  LYS A CG  
1176 C CD  . LYS A 64  ? 0.19315 0.21348 0.16174 -0.02873 0.04802  -0.04074 61  LYS A CD  
1177 C CE  . LYS A 64  ? 0.20210 0.22022 0.15990 -0.03667 0.04360  -0.01962 61  LYS A CE  
1178 N NZ  . LYS A 64  ? 0.23922 0.25651 0.14997 -0.04551 0.01958  -0.06467 61  LYS A NZ  
1192 N N   . ASN A 65  ? 0.10637 0.12017 0.12664 0.01226  -0.02576 -0.00227 62  ASN A N   
1193 C CA  . ASN A 65  ? 0.10401 0.11723 0.13254 -0.00449 -0.02483 -0.01568 62  ASN A CA  
1194 C C   . ASN A 65  ? 0.09291 0.13089 0.11747 -0.00208 -0.01822 0.00238  62  ASN A C   
1195 O O   . ASN A 65  ? 0.10263 0.17032 0.13039 -0.00116 -0.03914 -0.02097 62  ASN A O   
1196 C CB  . ASN A 65  ? 0.13086 0.14163 0.16071 0.00902  -0.02324 -0.00357 62  ASN A CB  
1197 C CG  . ASN A 65  ? 0.15547 0.18149 0.19538 0.01543  -0.01434 -0.04310 62  ASN A CG  
1198 O OD1 . ASN A 65  ? 0.20331 0.26431 0.22902 0.03648  -0.00417 -0.04441 62  ASN A OD1 
1199 N ND2 . ASN A 65  ? 0.14157 0.17965 0.18161 0.00724  0.00120  -0.03122 62  ASN A ND2 
1206 N N   . PHE A 66  ? 0.08597 0.12991 0.11149 -0.01654 -0.00373 0.00285  63  PHE A N   
1207 C CA  . PHE A 66  ? 0.07686 0.11981 0.11383 -0.03042 -0.03257 -0.00298 63  PHE A CA  
1208 C C   . PHE A 66  ? 0.06134 0.12434 0.12682 -0.03737 -0.01560 -0.00375 63  PHE A C   
1209 O O   . PHE A 66  ? 0.09290 0.14291 0.13227 -0.00893 -0.00731 0.02393  63  PHE A O   
1210 C CB  . PHE A 66  ? 0.10361 0.10701 0.10915 -0.00821 -0.01765 -0.00649 63  PHE A CB  
1211 C CG  . PHE A 66  ? 0.11125 0.14523 0.10570 -0.00655 -0.01841 0.00171  63  PHE A CG  
1212 C CD1 . PHE A 66  ? 0.13750 0.18970 0.12497 0.00066  -0.00739 -0.01823 63  PHE A CD1 
1213 C CD2 . PHE A 66  ? 0.13521 0.16519 0.11799 -0.00229 0.00339  -0.00606 63  PHE A CD2 
1214 C CE1 . PHE A 66  ? 0.14820 0.17072 0.14075 0.00662  -0.00663 -0.03598 63  PHE A CE1 
1215 C CE2 . PHE A 66  ? 0.16941 0.17432 0.14987 0.00917  0.00510  0.01822  63  PHE A CE2 
1216 C CZ  . PHE A 66  ? 0.17763 0.14008 0.15858 -0.00872 0.02026  -0.00638 63  PHE A CZ  
1226 N N   . GLU A 67  ? 0.08381 0.13176 0.11478 -0.01015 -0.02428 0.00188  64  GLU A N   
1227 C CA  . GLU A 67  ? 0.09300 0.14686 0.09437 -0.03232 -0.04340 0.00112  64  GLU A CA  
1228 C C   . GLU A 67  ? 0.10101 0.11725 0.11741 -0.04331 -0.03292 -0.00524 64  GLU A C   
1229 O O   . GLU A 67  ? 0.11243 0.09451 0.14084 -0.00927 -0.00582 0.00140  64  GLU A O   
1230 C CB  . GLU A 67  ? 0.12186 0.15627 0.11420 -0.00517 0.00359  0.01406  64  GLU A CB  
1231 C CG  . GLU A 67  ? 0.13835 0.16764 0.12393 -0.02670 0.02719  0.00448  64  GLU A CG  
1232 C CD  . GLU A 67  ? 0.12548 0.18037 0.13658 -0.03288 0.03935  0.00659  64  GLU A CD  
1233 O OE1 . GLU A 67  ? 0.10406 0.18737 0.14134 -0.00231 0.01853  0.01542  64  GLU A OE1 
1234 O OE2 . GLU A 67  ? 0.15649 0.22615 0.15216 0.01089  0.05740  0.01622  64  GLU A OE2 
1241 N N   . VAL A 68  ? 0.10328 0.10140 0.11027 -0.03534 -0.00346 -0.00233 65  VAL A N   
1242 C CA  . VAL A 68  ? 0.08906 0.11719 0.09254 -0.04646 -0.02731 -0.00609 65  VAL A CA  
1243 C C   . VAL A 68  ? 0.08652 0.11404 0.09039 -0.01417 -0.01211 -0.01397 65  VAL A C   
1244 O O   . VAL A 68  ? 0.10946 0.10974 0.10621 0.00377  -0.00843 -0.00009 65  VAL A O   
1245 C CB  . VAL A 68  ? 0.09384 0.10107 0.10571 -0.02453 -0.03086 -0.00729 65  VAL A CB  
1246 C CG1 . VAL A 68  ? 0.10036 0.09869 0.12698 -0.02022 -0.03885 -0.00251 65  VAL A CG1 
1247 C CG2 . VAL A 68  ? 0.11697 0.15009 0.11803 0.02555  -0.01341 0.02371  65  VAL A CG2 
1257 N N   . VAL A 69  ? 0.08690 0.15510 0.08375 -0.03301 -0.00973 -0.01738 66  VAL A N   
1258 C CA  . VAL A 69  ? 0.10555 0.13197 0.09136 -0.04117 -0.02077 -0.00819 66  VAL A CA  
1259 C C   . VAL A 69  ? 0.09250 0.09500 0.10293 -0.01538 -0.02134 -0.00210 66  VAL A C   
1260 O O   . VAL A 69  ? 0.07667 0.11685 0.11095 -0.00262 -0.00773 0.00490  66  VAL A O   
1261 C CB  . VAL A 69  ? 0.11183 0.11816 0.09096 0.00274  -0.02756 0.01414  66  VAL A CB  
1262 C CG1 . VAL A 69  ? 0.14235 0.12711 0.10067 0.00790  0.01437  -0.00915 66  VAL A CG1 
1263 C CG2 . VAL A 69  ? 0.09819 0.12868 0.11443 -0.02588 -0.02839 0.01114  66  VAL A CG2 
1273 N N   . LEU A 70  ? 0.10530 0.09622 0.08813 -0.01180 0.00035  0.03383  67  LEU A N   
1274 C CA  . LEU A 70  ? 0.10663 0.08883 0.09310 -0.00672 -0.02060 0.03232  67  LEU A CA  
1275 C C   . LEU A 70  ? 0.10376 0.07600 0.09979 0.00507  0.02239  0.03142  67  LEU A C   
1276 O O   . LEU A 70  ? 0.08844 0.12412 0.08290 -0.02148 0.00929  0.02721  67  LEU A O   
1277 C CB  . LEU A 70  ? 0.12501 0.13377 0.08968 -0.01938 0.00029  0.03243  67  LEU A CB  
1278 C CG  . LEU A 70  ? 0.13037 0.09238 0.10746 0.00675  0.02320  0.01829  67  LEU A CG  
1279 C CD1 . LEU A 70  ? 0.14663 0.14566 0.14279 0.01571  0.04818  0.03763  67  LEU A CD1 
1280 C CD2 . LEU A 70  ? 0.13557 0.12489 0.11434 0.00699  0.01606  0.03246  67  LEU A CD2 
1292 N N   . VAL A 71  ? 0.09957 0.12295 0.08712 0.00037  0.01551  0.00126  68  VAL A N   
1293 C CA  . VAL A 71  ? 0.10151 0.11151 0.09577 0.02206  0.00672  0.00927  68  VAL A CA  
1294 C C   . VAL A 71  ? 0.09774 0.07732 0.10812 0.01213  0.00231  0.00703  68  VAL A C   
1295 O O   . VAL A 71  ? 0.11187 0.10935 0.12756 0.00618  0.01759  0.00222  68  VAL A O   
1296 C CB  . VAL A 71  ? 0.09654 0.08221 0.10222 0.01621  -0.01394 0.01793  68  VAL A CB  
1297 C CG1 . VAL A 71  ? 0.12619 0.14013 0.11252 -0.00914 -0.00874 0.03722  68  VAL A CG1 
1298 C CG2 . VAL A 71  ? 0.12124 0.10534 0.11377 0.02409  -0.00066 0.01025  68  VAL A CG2 
1308 N N   . THR A 72  ? 0.11034 0.07023 0.10462 0.00582  -0.01663 0.00517  69  THR A N   
1309 C CA  . THR A 72  ? 0.09267 0.04287 0.09238 0.01184  -0.02986 0.00833  69  THR A CA  
1310 C C   . THR A 72  ? 0.12543 0.05287 0.08777 -0.02044 -0.00178 -0.00489 69  THR A C   
1311 O O   . THR A 72  ? 0.13478 0.06194 0.10450 -0.01134 0.01292  -0.03005 69  THR A O   
1312 C CB  . THR A 72  ? 0.08710 0.05418 0.10256 0.02721  -0.02927 0.00309  69  THR A CB  
1313 O OG1 . THR A 72  ? 0.11168 0.09299 0.12815 0.02550  0.01689  0.00515  69  THR A OG1 
1314 C CG2 . THR A 72  ? 0.10044 0.08319 0.10151 0.01147  -0.03221 -0.00700 69  THR A CG2 
1322 N N   . TRP A 73  ? 0.11648 0.10318 0.08992 -0.00325 0.00189  -0.00217 70  TRP A N   
1323 C CA  . TRP A 73  ? 0.13312 0.12194 0.08460 -0.01942 0.01421  0.02636  70  TRP A CA  
1324 C C   . TRP A 73  ? 0.11596 0.13766 0.11003 -0.00520 0.00001  0.00376  70  TRP A C   
1325 O O   . TRP A 73  ? 0.11327 0.14568 0.12794 -0.01676 0.00455  0.00191  70  TRP A O   
1326 C CB  . TRP A 73  ? 0.12855 0.10357 0.10934 0.00193  -0.00478 0.01932  70  TRP A CB  
1327 C CG  . TRP A 73  ? 0.10914 0.06477 0.11808 0.01009  -0.00176 0.02795  70  TRP A CG  
1328 C CD1 . TRP A 73  ? 0.10800 0.12662 0.12574 0.01033  0.01707  0.03587  70  TRP A CD1 
1329 C CD2 . TRP A 73  ? 0.09719 0.04966 0.10015 -0.00231 -0.00271 0.01179  70  TRP A CD2 
1330 N NE1 . TRP A 73  ? 0.10469 0.12925 0.12451 -0.02277 0.02392  -0.00946 70  TRP A NE1 
1331 C CE2 . TRP A 73  ? 0.09773 0.09473 0.09672 -0.01214 -0.00931 0.01360  70  TRP A CE2 
1332 C CE3 . TRP A 73  ? 0.09804 0.10118 0.12373 -0.01810 -0.00893 -0.00926 70  TRP A CE3 
1333 C CZ2 . TRP A 73  ? 0.11942 0.08869 0.13072 -0.01742 -0.00017 0.01468  70  TRP A CZ2 
1334 C CZ3 . TRP A 73  ? 0.10547 0.09072 0.13286 0.00291  -0.00134 0.01011  70  TRP A CZ3 
1335 C CH2 . TRP A 73  ? 0.11450 0.11019 0.13700 -0.00680 -0.02594 0.03079  70  TRP A CH2 
1346 N N   . ASP A 74  ? 0.09908 0.12053 0.12290 0.02336  -0.02930 0.00546  71  ASP A N   
1347 C CA  . ASP A 74  ? 0.12482 0.09256 0.12084 0.01820  -0.00417 0.01352  71  ASP A CA  
1348 C C   . ASP A 74  ? 0.13591 0.09602 0.11796 0.03450  -0.01993 0.00250  71  ASP A C   
1349 O O   . ASP A 74  ? 0.17606 0.12458 0.14957 0.05170  -0.01613 -0.00063 71  ASP A O   
1350 C CB  . ASP A 74  ? 0.11927 0.12657 0.12627 0.02410  0.00134  -0.00042 71  ASP A CB  
1351 C CG  . ASP A 74  ? 0.13280 0.12645 0.13598 0.02981  0.00487  -0.00783 71  ASP A CG  
1352 O OD1 . ASP A 74  ? 0.14291 0.12449 0.14570 0.02853  0.01980  -0.00356 71  ASP A OD1 
1353 O OD2 . ASP A 74  ? 0.15644 0.12158 0.14123 -0.01387 -0.00371 -0.01860 71  ASP A OD2 
1358 N N   . ASP A 75  ? 0.15198 0.14363 0.09410 0.01399  -0.01779 0.00395  72  ASP A N   
1359 C CA  . ASP A 75  ? 0.15318 0.10806 0.11115 0.02400  -0.00802 0.00737  72  ASP A CA  
1360 C C   . ASP A 75  ? 0.17905 0.09335 0.13857 0.00904  -0.00412 0.02898  72  ASP A C   
1361 O O   . ASP A 75  ? 0.21671 0.17707 0.12090 -0.00831 0.02323  0.01159  72  ASP A O   
1362 C CB  . ASP A 75  ? 0.14634 0.17628 0.11974 0.00408  0.00608  -0.01600 72  ASP A CB  
1363 C CG  . ASP A 75  ? 0.15015 0.15789 0.14621 -0.02387 -0.00503 -0.01594 72  ASP A CG  
1364 O OD1 . ASP A 75  ? 0.15871 0.17638 0.15985 0.01092  0.02046  -0.03271 72  ASP A OD1 
1365 O OD2 . ASP A 75  ? 0.15571 0.14157 0.16969 -0.03834 -0.02289 -0.01624 72  ASP A OD2 
1370 N N   . GLU A 76  ? 0.20293 0.08273 0.16941 0.01450  -0.01215 0.03687  73  GLU A N   
1371 C CA  A GLU A 76  ? 0.23525 0.15915 0.21075 -0.01760 -0.01120 0.04040  73  GLU A CA  
1372 C CA  B GLU A 76  ? 0.23525 0.15915 0.21075 -0.01760 -0.01120 0.04040  73  GLU A CA  
1373 C C   . GLU A 76  ? 0.20405 0.13383 0.17239 -0.01699 -0.01266 0.03047  73  GLU A C   
1374 O O   . GLU A 76  ? 0.15661 0.10836 0.15753 -0.00781 -0.00773 0.03390  73  GLU A O   
1375 C CB  A GLU A 76  ? 0.32845 0.29595 0.30635 -0.01260 -0.00810 0.04350  73  GLU A CB  
1376 C CB  B GLU A 76  ? 0.32845 0.29595 0.30635 -0.01260 -0.00810 0.04350  73  GLU A CB  
1377 C CG  A GLU A 76  ? 0.43425 0.44055 0.41075 -0.00370 0.01430  0.02450  73  GLU A CG  
1378 C CG  B GLU A 76  ? 0.43425 0.44055 0.41075 -0.00370 0.01430  0.02450  73  GLU A CG  
1379 C CD  A GLU A 76  ? 0.52035 0.55205 0.49185 -0.00100 0.06490  0.00670  73  GLU A CD  
1380 C CD  B GLU A 76  ? 0.52035 0.55205 0.49185 -0.00100 0.06490  0.00670  73  GLU A CD  
1381 O OE1 A GLU A 76  ? 0.56115 0.61765 0.55475 -0.00390 0.08770  -0.00030 73  GLU A OE1 
1382 O OE1 B GLU A 76  ? 0.56115 0.61765 0.55475 -0.00390 0.08770  -0.00030 73  GLU A OE1 
1383 O OE2 A GLU A 76  ? 0.53185 0.56595 0.50905 0.00470  0.04950  0.00090  73  GLU A OE2 
1384 O OE2 B GLU A 76  ? 0.53185 0.56595 0.50905 0.00470  0.04950  0.00090  73  GLU A OE2 
1395 N N   . GLU A 77  ? 0.19603 0.14668 0.14054 -0.00398 0.00385  0.02598  74  GLU A N   
1396 C CA  . GLU A 77  ? 0.19044 0.13808 0.12919 -0.02584 -0.00619 -0.00088 74  GLU A CA  
1397 C C   . GLU A 77  ? 0.18143 0.14821 0.11251 -0.00235 -0.00407 0.01033  74  GLU A C   
1398 O O   . GLU A 77  ? 0.18104 0.13813 0.12193 -0.02454 -0.01341 0.01509  74  GLU A O   
1399 C CB  . GLU A 77  ? 0.20574 0.19098 0.13026 -0.03530 0.01704  0.00588  74  GLU A CB  
1400 C CG  . GLU A 77  ? 0.20810 0.22787 0.12443 -0.00889 0.01802  -0.01257 74  GLU A CG  
1401 C CD  . GLU A 77  ? 0.26124 0.29528 0.16910 0.01015  0.02831  -0.01225 74  GLU A CD  
1402 O OE1 . GLU A 77  ? 0.31151 0.35202 0.17593 -0.00547 0.04867  0.00038  74  GLU A OE1 
1403 O OE2 . GLU A 77  ? 0.27794 0.33204 0.18399 0.01366  0.03748  -0.02631 74  GLU A OE2 
1410 N N   . GLU A 78  ? 0.18613 0.15592 0.13597 -0.01491 0.00924  0.01546  75  GLU A N   
1413 C C   . GLU A 78  ? 0.18119 0.13737 0.14602 0.01226  -0.00709 0.01533  75  GLU A C   
1414 O O   . GLU A 78  ? 0.21908 0.11531 0.12455 0.00197  -0.00074 -0.02474 75  GLU A O   
1437 N N   . ALA A 79  ? 0.17766 0.08651 0.15480 0.03904  0.00402  0.03930  76  ALA A N   
1438 C CA  . ALA A 79  ? 0.16790 0.11366 0.13675 0.04650  0.00913  0.03343  76  ALA A CA  
1439 C C   . ALA A 79  ? 0.16311 0.09113 0.11483 0.01103  -0.01226 -0.00054 76  ALA A C   
1440 O O   . ALA A 79  ? 0.16808 0.13180 0.13068 0.01487  -0.00667 0.00214  76  ALA A O   
1441 C CB  . ALA A 79  ? 0.18340 0.14259 0.11930 0.02617  0.02977  0.01329  76  ALA A CB  
1447 N N   . TYR A 80  ? 0.16420 0.05008 0.10617 -0.01905 -0.00444 0.01550  77  TYR A N   
1448 C CA  . TYR A 80  ? 0.14017 0.06893 0.10580 0.00877  -0.01082 0.01048  77  TYR A CA  
1449 C C   . TYR A 80  ? 0.15987 0.06905 0.10408 -0.00016 -0.00704 0.01384  77  TYR A C   
1450 O O   . TYR A 80  ? 0.16453 0.12859 0.09867 0.01621  -0.00351 -0.00916 77  TYR A O   
1451 C CB  . TYR A 80  ? 0.15927 0.09341 0.11786 -0.00900 -0.00669 0.03335  77  TYR A CB  
1452 C CG  . TYR A 80  ? 0.14792 0.08657 0.10842 0.00537  0.01260  0.01128  77  TYR A CG  
1453 C CD1 . TYR A 80  ? 0.14473 0.10752 0.11423 -0.00226 0.01753  0.00927  77  TYR A CD1 
1454 C CD2 . TYR A 80  ? 0.13589 0.09273 0.13288 -0.00204 0.01664  0.02962  77  TYR A CD2 
1455 C CE1 . TYR A 80  ? 0.13888 0.09873 0.12816 0.00523  0.03348  0.02687  77  TYR A CE1 
1456 C CE2 . TYR A 80  ? 0.12777 0.08585 0.13269 0.00555  0.01403  0.03911  77  TYR A CE2 
1457 C CZ  . TYR A 80  ? 0.14007 0.11681 0.13775 0.02134  0.01062  0.03534  77  TYR A CZ  
1458 O OH  . TYR A 80  ? 0.14169 0.10380 0.14164 0.00893  0.00182  0.02438  77  TYR A OH  
1468 N N   . ASN A 81  ? 0.17148 0.09319 0.09481 -0.00745 0.00933  0.02709  78  ASN A N   
1469 C CA  . ASN A 81  ? 0.18441 0.08157 0.11970 -0.02643 0.00454  0.00441  78  ASN A CA  
1470 C C   . ASN A 81  ? 0.16609 0.10621 0.10892 -0.03698 0.00329  0.02097  78  ASN A C   
1471 O O   . ASN A 81  ? 0.17061 0.15165 0.09548 -0.03611 -0.00062 -0.00619 78  ASN A O   
1472 C CB  . ASN A 81  ? 0.19581 0.09108 0.13269 -0.02988 -0.00701 0.00757  78  ASN A CB  
1473 C CG  . ASN A 81  ? 0.23054 0.14667 0.14340 -0.04236 0.00756  0.02342  78  ASN A CG  
1474 O OD1 . ASN A 81  ? 0.24457 0.15870 0.14983 -0.01551 0.06920  -0.01378 78  ASN A OD1 
1475 N ND2 . ASN A 81  ? 0.25730 0.17494 0.13951 -0.07410 -0.00524 0.03181  78  ASN A ND2 
1482 N N   . GLY A 82  ? 0.16030 0.12139 0.12800 -0.00282 -0.00637 0.02581  79  GLY A N   
1483 C CA  . GLY A 82  ? 0.15720 0.11231 0.11347 -0.03571 -0.00504 -0.00041 79  GLY A CA  
1484 C C   . GLY A 82  ? 0.16676 0.10580 0.13465 -0.04772 -0.01220 0.00862  79  GLY A C   
1485 O O   . GLY A 82  ? 0.19568 0.10927 0.14247 -0.03565 -0.02679 0.01865  79  GLY A O   
1489 N N   . TYR A 83  ? 0.14573 0.12067 0.13425 -0.02662 -0.00360 -0.00498 80  TYR A N   
1490 C CA  . TYR A 83  ? 0.14411 0.11164 0.11448 0.00700  -0.01214 -0.01781 80  TYR A CA  
1491 C C   . TYR A 83  ? 0.16344 0.11554 0.10103 0.01129  -0.01042 -0.01368 80  TYR A C   
1492 O O   . TYR A 83  ? 0.15962 0.10968 0.11443 -0.00725 0.01860  0.00634  80  TYR A O   
1493 C CB  . TYR A 83  ? 0.14926 0.09583 0.11163 -0.01870 -0.02105 -0.00532 80  TYR A CB  
1494 C CG  . TYR A 83  ? 0.15018 0.08526 0.13996 -0.00857 -0.00330 -0.03784 80  TYR A CG  
1495 C CD1 . TYR A 83  ? 0.15693 0.09295 0.13491 -0.00634 0.00452  0.00891  80  TYR A CD1 
1496 C CD2 . TYR A 83  ? 0.15405 0.06841 0.14993 -0.00822 -0.00762 -0.03316 80  TYR A CD2 
1497 C CE1 . TYR A 83  ? 0.15359 0.13033 0.11521 -0.03031 0.00887  0.04268  80  TYR A CE1 
1498 C CE2 . TYR A 83  ? 0.13194 0.09520 0.15414 -0.00072 -0.00118 0.00148  80  TYR A CE2 
1499 C CZ  . TYR A 83  ? 0.14025 0.11976 0.13635 -0.03415 0.01119  0.02360  80  TYR A CZ  
1500 O OH  . TYR A 83  ? 0.13279 0.13743 0.15035 -0.02674 -0.00081 0.02797  80  TYR A OH  
1510 N N   . PHE A 84  ? 0.14022 0.10202 0.09719 -0.00160 -0.01363 -0.00364 81  PHE A N   
1511 C CA  . PHE A 84  ? 0.14037 0.08475 0.10266 0.02337  -0.00021 -0.01217 81  PHE A CA  
1512 C C   . PHE A 84  ? 0.15406 0.10800 0.08781 0.00948  0.01747  -0.01148 81  PHE A C   
1513 O O   . PHE A 84  ? 0.17201 0.12226 0.09341 0.00848  0.00151  -0.01565 81  PHE A O   
1514 C CB  . PHE A 84  ? 0.14245 0.12554 0.12783 0.00343  0.00778  -0.00339 81  PHE A CB  
1515 C CG  . PHE A 84  ? 0.12854 0.10576 0.12678 -0.01982 0.00291  -0.02003 81  PHE A CG  
1516 C CD1 . PHE A 84  ? 0.12869 0.09494 0.14051 -0.00884 -0.00310 -0.02297 81  PHE A CD1 
1517 C CD2 . PHE A 84  ? 0.13167 0.17802 0.12436 0.01333  -0.00072 -0.00631 81  PHE A CD2 
1518 C CE1 . PHE A 84  ? 0.14993 0.10242 0.13018 0.00654  -0.00257 -0.02556 81  PHE A CE1 
1519 C CE2 . PHE A 84  ? 0.11739 0.15298 0.13498 0.03113  -0.01627 -0.00206 81  PHE A CE2 
1520 C CZ  . PHE A 84  ? 0.13134 0.14762 0.13118 0.00320  -0.02321 -0.03710 81  PHE A CZ  
1530 N N   . ALA A 85  ? 0.14075 0.12533 0.09778 -0.03291 0.00184  -0.01440 82  ALA A N   
1531 C CA  . ALA A 85  ? 0.15883 0.14681 0.09789 -0.02574 0.00147  -0.03494 82  ALA A CA  
1532 C C   . ALA A 85  ? 0.15497 0.08705 0.10018 -0.04901 -0.00391 -0.02921 82  ALA A C   
1533 O O   . ALA A 85  ? 0.17584 0.14778 0.11575 -0.08376 0.00598  -0.01757 82  ALA A O   
1534 C CB  . ALA A 85  ? 0.17569 0.18221 0.10922 -0.01315 -0.02000 -0.03630 82  ALA A CB  
1540 N N   . LYS A 86  ? 0.15633 0.11240 0.11160 -0.03572 0.01762  -0.01368 83  LYS A N   
1541 C CA  . LYS A 86  ? 0.13439 0.10743 0.11717 0.00180  0.00551  -0.00858 83  LYS A CA  
1542 C C   . LYS A 86  ? 0.15497 0.06086 0.09633 -0.01430 -0.01642 -0.02579 83  LYS A C   
1543 O O   . LYS A 86  ? 0.17195 0.14370 0.12572 0.00777  -0.01460 -0.02709 83  LYS A O   
1544 C CB  . LYS A 86  ? 0.13233 0.15494 0.13162 -0.01220 -0.01916 -0.01696 83  LYS A CB  
1545 C CG  . LYS A 86  ? 0.14650 0.11690 0.12154 -0.01987 -0.02373 -0.02271 83  LYS A CG  
1546 C CD  . LYS A 86  ? 0.14516 0.14716 0.12635 0.00698  -0.01723 0.02369  83  LYS A CD  
1547 C CE  . LYS A 86  ? 0.13524 0.14159 0.14449 0.01567  -0.03455 0.02150  83  LYS A CE  
1548 N NZ  . LYS A 86  ? 0.16305 0.15924 0.17741 0.00634  -0.02362 0.04466  83  LYS A NZ  
1562 N N   . MET A 87  ? 0.15465 0.09484 0.09448 -0.02030 0.00228  -0.01785 84  MET A N   
1563 C CA  . MET A 87  ? 0.14625 0.15118 0.08556 -0.02329 -0.00587 -0.01817 84  MET A CA  
1564 C C   . MET A 87  ? 0.13883 0.15204 0.08235 0.00762  -0.01543 -0.02070 84  MET A C   
1565 O O   . MET A 87  ? 0.15123 0.18241 0.08782 -0.00601 -0.00424 -0.00018 84  MET A O   
1566 C CB  . MET A 87  ? 0.13619 0.09696 0.09304 -0.05420 0.00001  -0.02218 84  MET A CB  
1567 C CG  . MET A 87  ? 0.13092 0.10693 0.11986 -0.04907 -0.01153 0.01324  84  MET A CG  
1568 S SD  . MET A 87  ? 0.13778 0.10634 0.13510 -0.00339 -0.00420 -0.00271 84  MET A SD  
1569 C CE  . MET A 87  ? 0.12558 0.14798 0.16451 0.03977  -0.02261 0.01122  84  MET A CE  
1579 N N   . PRO A 88  ? 0.13079 0.12458 0.09974 -0.01443 0.01187  0.00090  85  PRO A N   
1580 C CA  . PRO A 88  ? 0.13273 0.14267 0.14101 -0.05380 0.00546  -0.03008 85  PRO A CA  
1581 C C   . PRO A 88  ? 0.11757 0.13928 0.14888 -0.03408 -0.01518 -0.01998 85  PRO A C   
1582 O O   . PRO A 88  ? 0.13829 0.17486 0.19278 -0.05018 0.00398  -0.03245 85  PRO A O   
1583 C CB  . PRO A 88  ? 0.14318 0.16755 0.14357 -0.04588 -0.00720 -0.01664 85  PRO A CB  
1584 C CG  . PRO A 88  ? 0.14602 0.14991 0.12326 -0.01515 -0.03492 0.01507  85  PRO A CG  
1585 C CD  . PRO A 88  ? 0.11812 0.17946 0.09230 -0.00306 -0.03329 0.01390  85  PRO A CD  
1593 N N   . TRP A 89  ? 0.12033 0.13040 0.12334 -0.03832 -0.00562 -0.01351 86  TRP A N   
1594 C CA  . TRP A 89  ? 0.11998 0.12052 0.10524 -0.02262 -0.01525 -0.01691 86  TRP A CA  
1595 C C   . TRP A 89  ? 0.12221 0.12586 0.09408 -0.00406 0.00267  0.00334  86  TRP A C   
1596 O O   . TRP A 89  ? 0.16729 0.12615 0.10034 -0.02836 0.01756  0.00098  86  TRP A O   
1597 C CB  . TRP A 89  ? 0.12844 0.12456 0.12607 -0.01106 -0.02439 0.00452  86  TRP A CB  
1598 C CG  . TRP A 89  ? 0.10525 0.09944 0.09825 -0.02687 -0.02667 -0.00193 86  TRP A CG  
1599 C CD1 . TRP A 89  ? 0.12125 0.11637 0.12024 -0.02863 -0.00230 0.00460  86  TRP A CD1 
1600 C CD2 . TRP A 89  ? 0.09673 0.08678 0.08529 -0.02856 -0.02676 -0.00734 86  TRP A CD2 
1601 N NE1 . TRP A 89  ? 0.13123 0.09099 0.11919 -0.04653 -0.00381 -0.02806 86  TRP A NE1 
1602 C CE2 . TRP A 89  ? 0.10807 0.07344 0.09640 -0.02718 -0.01957 -0.03615 86  TRP A CE2 
1603 C CE3 . TRP A 89  ? 0.10934 0.09982 0.08420 -0.04080 -0.00942 -0.02324 86  TRP A CE3 
1604 C CZ2 . TRP A 89  ? 0.11486 0.09206 0.12283 -0.02688 -0.01342 -0.02477 86  TRP A CZ2 
1605 C CZ3 . TRP A 89  ? 0.12549 0.12373 0.06489 0.01605  -0.00085 0.01422  86  TRP A CZ3 
1606 C CH2 . TRP A 89  ? 0.11381 0.08609 0.10578 0.02464  -0.00478 -0.00739 86  TRP A CH2 
1617 N N   . LEU A 90  ? 0.11723 0.14208 0.09813 -0.02975 0.00580  -0.03595 87  LEU A N   
1618 C CA  . LEU A 90  ? 0.09974 0.13049 0.09907 -0.01570 -0.00157 0.00153  87  LEU A CA  
1619 C C   . LEU A 90  ? 0.10672 0.13284 0.07471 -0.03282 -0.02340 -0.00992 87  LEU A C   
1620 O O   . LEU A 90  ? 0.13691 0.12456 0.08821 -0.01303 0.01468  -0.00261 87  LEU A O   
1621 C CB  . LEU A 90  ? 0.10639 0.13756 0.10645 0.01066  0.02203  0.01257  87  LEU A CB  
1622 C CG  . LEU A 90  ? 0.10633 0.15615 0.11308 0.01217  0.02456  0.01905  87  LEU A CG  
1623 C CD1 . LEU A 90  ? 0.08993 0.19249 0.12243 0.02376  -0.00590 0.03403  87  LEU A CD1 
1624 C CD2 . LEU A 90  ? 0.12175 0.17332 0.16873 0.03838  0.02216  0.01283  87  LEU A CD2 
1636 N N   . ALA A 91  ? 0.08939 0.16760 0.07891 0.00310  -0.01683 -0.02144 88  ALA A N   
1637 C CA  . ALA A 91  ? 0.08723 0.11112 0.07270 0.01561  -0.01988 -0.01384 88  ALA A CA  
1638 C C   . ALA A 91  ? 0.09961 0.13509 0.08695 0.02119  0.00507  -0.00053 88  ALA A C   
1639 O O   . ALA A 91  ? 0.12542 0.17313 0.08924 -0.02536 0.02827  -0.01119 88  ALA A O   
1640 C CB  . ALA A 91  ? 0.10578 0.09860 0.10107 -0.03984 0.02158  -0.00250 88  ALA A CB  
1646 N N   . ILE A 92  ? 0.13008 0.12040 0.09243 0.00565  0.02177  -0.02225 89  ILE A N   
1647 C CA  . ILE A 92  ? 0.13187 0.11382 0.10948 0.00666  0.00609  -0.05535 89  ILE A CA  
1648 C C   . ILE A 92  ? 0.09933 0.07563 0.09177 0.02123  -0.00845 0.01057  89  ILE A C   
1649 O O   . ILE A 92  ? 0.10013 0.10326 0.11954 -0.01218 0.00050  -0.00882 89  ILE A O   
1650 C CB  . ILE A 92  ? 0.14462 0.10525 0.12310 -0.00670 -0.00403 -0.01460 89  ILE A CB  
1651 C CG1 . ILE A 92  ? 0.16562 0.13257 0.14466 0.00455  -0.02951 -0.01579 89  ILE A CG1 
1652 C CG2 . ILE A 92  ? 0.13426 0.12192 0.12580 0.03216  -0.01352 -0.02964 89  ILE A CG2 
1653 C CD1 . ILE A 92  ? 0.18029 0.17595 0.16478 -0.02515 -0.00904 0.00975  89  ILE A CD1 
1665 N N   . PRO A 93  ? 0.11655 0.12447 0.09515 0.02640  0.00470  -0.02586 90  PRO A N   
1666 C CA  . PRO A 93  ? 0.13541 0.16194 0.08979 -0.01359 0.00649  -0.00713 90  PRO A CA  
1667 C C   . PRO A 93  ? 0.13369 0.15223 0.10003 -0.00605 0.00569  -0.01396 90  PRO A C   
1668 O O   . PRO A 93  ? 0.12517 0.15767 0.10000 0.03092  -0.01210 -0.00021 90  PRO A O   
1669 C CB  . PRO A 93  ? 0.13212 0.24130 0.10510 0.02317  0.04161  0.01761  90  PRO A CB  
1670 C CG  . PRO A 93  ? 0.13548 0.22311 0.11947 0.05929  0.03767  -0.00383 90  PRO A CG  
1671 C CD  . PRO A 93  ? 0.11411 0.17253 0.10748 0.01699  -0.00939 -0.05383 90  PRO A CD  
1679 N N   . PHE A 94  ? 0.13420 0.13978 0.11145 -0.05518 -0.00021 -0.01325 91  PHE A N   
1680 C CA  . PHE A 94  ? 0.13074 0.12450 0.11488 -0.02261 -0.01819 0.01208  91  PHE A CA  
1681 C C   . PHE A 94  ? 0.12552 0.13298 0.12931 -0.03466 -0.01817 0.02848  91  PHE A C   
1682 O O   . PHE A 94  ? 0.13630 0.14175 0.16888 -0.02134 -0.01904 0.00088  91  PHE A O   
1683 C CB  . PHE A 94  ? 0.13201 0.12669 0.11029 -0.00923 0.00601  0.00246  91  PHE A CB  
1684 C CG  . PHE A 94  ? 0.13605 0.09285 0.13619 -0.01053 0.00028  -0.00702 91  PHE A CG  
1685 C CD1 . PHE A 94  ? 0.11970 0.09987 0.13922 0.01377  -0.00625 -0.02110 91  PHE A CD1 
1686 C CD2 . PHE A 94  ? 0.15570 0.15058 0.15081 0.00676  -0.01083 -0.00189 91  PHE A CD2 
1687 C CE1 . PHE A 94  ? 0.14478 0.13936 0.16853 0.02898  0.00248  -0.02040 91  PHE A CE1 
1688 C CE2 . PHE A 94  ? 0.15864 0.17779 0.14977 0.00361  -0.02716 -0.01165 91  PHE A CE2 
1689 C CZ  . PHE A 94  ? 0.15585 0.13771 0.17878 0.01024  -0.00582 -0.00235 91  PHE A CZ  
1699 N N   . SER A 95  ? 0.15083 0.17083 0.09373 -0.01425 -0.02006 0.00614  92  SER A N   
1700 C CA  . SER A 95  ? 0.18488 0.15276 0.11090 -0.00644 -0.03169 0.02091  92  SER A CA  
1701 C C   . SER A 95  ? 0.17206 0.12934 0.12335 -0.02563 -0.03240 0.01348  92  SER A C   
1702 O O   . SER A 95  ? 0.17614 0.17696 0.11856 -0.03278 -0.03867 0.01238  92  SER A O   
1703 C CB  . SER A 95  ? 0.22090 0.22952 0.13089 -0.03910 -0.00106 0.01452  92  SER A CB  
1704 O OG  . SER A 95  ? 0.28482 0.29657 0.18705 -0.03529 0.07753  -0.03175 92  SER A OG  
1710 N N   . SER A 96  ? 0.15984 0.10415 0.12928 -0.02269 -0.00203 -0.00419 93  SER A N   
1713 C C   . SER A 96  ? 0.13372 0.13140 0.13090 0.01792  -0.04099 -0.03072 93  SER A C   
1714 O O   . SER A 96  ? 0.11698 0.12295 0.13164 0.00497  -0.01723 -0.03785 93  SER A O   
1729 N N   . ARG A 97  ? 0.13594 0.14177 0.13162 0.00347  -0.03391 0.00272  94  ARG A N   
1730 C CA  . ARG A 97  ? 0.12861 0.15007 0.13218 0.01121  -0.02841 -0.00770 94  ARG A CA  
1731 C C   . ARG A 97  ? 0.12033 0.12108 0.14198 -0.01719 -0.02614 -0.01852 94  ARG A C   
1732 O O   . ARG A 97  ? 0.12714 0.16839 0.13521 -0.02694 0.00309  -0.00675 94  ARG A O   
1733 C CB  . ARG A 97  ? 0.16313 0.14087 0.15014 0.01165  -0.03388 -0.01572 94  ARG A CB  
1734 C CG  . ARG A 97  ? 0.19342 0.14470 0.18561 0.01092  -0.02032 0.00481  94  ARG A CG  
1735 C CD  . ARG A 97  ? 0.22250 0.18105 0.19318 -0.01307 -0.00412 0.01020  94  ARG A CD  
1736 N NE  . ARG A 97  ? 0.24468 0.19446 0.19742 0.03595  0.00790  0.00705  94  ARG A NE  
1737 C CZ  . ARG A 97  ? 0.20437 0.13497 0.18758 0.00397  0.00414  -0.01684 94  ARG A CZ  
1738 N NH1 . ARG A 97  ? 0.17712 0.12353 0.15024 -0.00388 0.00458  -0.02208 94  ARG A NH1 
1739 N NH2 . ARG A 97  ? 0.21268 0.16844 0.24783 -0.01049 0.01593  -0.02896 94  ARG A NH2 
1753 N N   . ALA A 98  ? 0.14168 0.14273 0.15203 -0.02187 -0.01340 -0.01008 95  ALA A N   
1754 C CA  . ALA A 98  ? 0.15918 0.14138 0.16243 -0.01876 0.01602  0.00196  95  ALA A CA  
1755 C C   . ALA A 98  ? 0.15737 0.10477 0.15296 -0.00185 0.02160  0.01373  95  ALA A C   
1756 O O   . ALA A 98  ? 0.14900 0.11769 0.15545 -0.00474 0.00796  0.00180  95  ALA A O   
1757 C CB  . ALA A 98  ? 0.18423 0.18482 0.17379 -0.01354 0.01689  -0.04609 95  ALA A CB  
1763 N N   . GLU A 99  ? 0.15711 0.08416 0.14460 0.00588  0.01661  0.01113  96  GLU A N   
1764 C CA  . GLU A 99  ? 0.14952 0.07643 0.15607 0.01787  -0.01001 0.00220  96  GLU A CA  
1765 C C   . GLU A 99  ? 0.13310 0.05061 0.15031 0.02602  -0.01631 -0.00313 96  GLU A C   
1766 O O   . GLU A 99  ? 0.13268 0.07830 0.16255 0.01950  -0.00620 0.01843  96  GLU A O   
1767 C CB  . GLU A 99  ? 0.16307 0.11298 0.16119 -0.00109 -0.00619 -0.03216 96  GLU A CB  
1768 C CG  . GLU A 99  ? 0.18488 0.15535 0.18920 0.01887  0.00789  -0.00915 96  GLU A CG  
1769 C CD  . GLU A 99  ? 0.18783 0.20219 0.18951 0.01092  -0.00289 0.03804  96  GLU A CD  
1770 O OE1 . GLU A 99  ? 0.18098 0.29514 0.19263 -0.02424 -0.01733 0.05846  96  GLU A OE1 
1771 O OE2 . GLU A 99  ? 0.20604 0.22511 0.20457 0.02123  0.00101  0.03513  96  GLU A OE2 
1778 N N   . LEU A 100 ? 0.11518 0.09072 0.13521 0.00947  0.00459  -0.00235 97  LEU A N   
1779 C CA  . LEU A 100 ? 0.11032 0.09397 0.14163 0.01967  0.00649  -0.03143 97  LEU A CA  
1780 C C   . LEU A 100 ? 0.10742 0.11323 0.12021 0.00785  -0.00668 -0.04828 97  LEU A C   
1781 O O   . LEU A 100 ? 0.13482 0.12948 0.09949 0.01462  0.02605  -0.01283 97  LEU A O   
1782 C CB  . LEU A 100 ? 0.10585 0.12223 0.15255 -0.00981 -0.00603 -0.05010 97  LEU A CB  
1783 C CG  . LEU A 100 ? 0.10693 0.09856 0.13281 0.01252  -0.02272 -0.02241 97  LEU A CG  
1784 C CD1 . LEU A 100 ? 0.12262 0.11721 0.10080 0.01729  -0.02746 0.00140  97  LEU A CD1 
1785 C CD2 . LEU A 100 ? 0.10853 0.13991 0.11630 0.00959  0.01280  0.00473  97  LEU A CD2 
1797 N N   . GLU A 101 ? 0.13967 0.13406 0.12418 -0.00419 -0.00394 -0.01794 98  GLU A N   
1800 C C   . GLU A 101 ? 0.11638 0.14177 0.13410 -0.01196 0.00642  -0.01381 98  GLU A C   
1801 O O   . GLU A 101 ? 0.10191 0.13279 0.13654 -0.02848 0.00386  -0.02046 98  GLU A O   
1824 N N   . ALA A 102 ? 0.12179 0.09398 0.15301 -0.00460 0.00440  -0.00714 99  ALA A N   
1825 C CA  . ALA A 102 ? 0.14821 0.07584 0.12817 0.00206  0.01241  -0.01512 99  ALA A CA  
1826 C C   . ALA A 102 ? 0.14554 0.09388 0.12464 0.02841  0.01405  0.00373  99  ALA A C   
1827 O O   . ALA A 102 ? 0.17290 0.08192 0.13926 -0.00513 0.03814  0.00699  99  ALA A O   
1828 C CB  . ALA A 102 ? 0.15659 0.16023 0.11140 0.01791  0.02511  0.00240  99  ALA A CB  
1834 N N   . LEU A 103 ? 0.14086 0.06674 0.13109 0.00655  0.01985  0.00052  100 LEU A N   
1835 C CA  . LEU A 103 ? 0.12819 0.12814 0.13507 0.00038  0.02608  -0.03602 100 LEU A CA  
1836 C C   . LEU A 103 ? 0.10810 0.08527 0.13212 0.03821  -0.00163 0.02076  100 LEU A C   
1837 O O   . LEU A 103 ? 0.13775 0.06157 0.13477 0.01363  -0.01227 0.00892  100 LEU A O   
1838 C CB  . LEU A 103 ? 0.10993 0.11402 0.15639 -0.00072 0.00376  -0.04416 100 LEU A CB  
1839 C CG  . LEU A 103 ? 0.10870 0.15981 0.19647 0.01327  -0.01338 -0.04558 100 LEU A CG  
1840 C CD1 . LEU A 103 ? 0.11508 0.18080 0.23061 -0.03534 -0.00626 -0.06521 100 LEU A CD1 
1841 C CD2 . LEU A 103 ? 0.15129 0.20326 0.22742 0.02146  0.02888  -0.02710 100 LEU A CD2 
1853 N N   . ARG A 104 ? 0.10497 0.08297 0.12478 0.02555  0.00334  0.00661  101 ARG A N   
1854 C CA  . ARG A 104 ? 0.09623 0.10481 0.13208 0.03326  0.01373  0.00836  101 ARG A CA  
1855 C C   . ARG A 104 ? 0.07317 0.09124 0.13541 0.02637  -0.01915 0.00308  101 ARG A C   
1856 O O   . ARG A 104 ? 0.11182 0.11714 0.14215 -0.01693 0.01528  -0.01644 101 ARG A O   
1857 C CB  . ARG A 104 ? 0.09076 0.07710 0.13608 0.03313  0.01541  0.01729  101 ARG A CB  
1858 C CG  . ARG A 104 ? 0.07502 0.13155 0.13853 0.00170  -0.00657 -0.00208 101 ARG A CG  
1859 C CD  . ARG A 104 ? 0.09322 0.12768 0.12774 0.02291  -0.01478 -0.01284 101 ARG A CD  
1860 N NE  . ARG A 104 ? 0.11030 0.12098 0.14336 0.03209  -0.03462 -0.01334 101 ARG A NE  
1861 C CZ  . ARG A 104 ? 0.11771 0.15717 0.14813 0.03848  -0.02347 0.00652  101 ARG A CZ  
1862 N NH1 . ARG A 104 ? 0.13834 0.18490 0.16485 0.04208  -0.00233 0.04219  101 ARG A NH1 
1863 N NH2 . ARG A 104 ? 0.12247 0.16160 0.14323 -0.01091 -0.03288 0.00173  101 ARG A NH2 
1877 N N   . SER A 105 ? 0.11629 0.11332 0.11957 -0.01881 -0.00283 -0.00274 102 SER A N   
1878 C CA  . SER A 105 ? 0.15513 0.11093 0.11709 0.01151  -0.00937 0.05773  102 SER A CA  
1879 C C   . SER A 105 ? 0.16006 0.08045 0.11915 -0.00383 -0.00580 0.03769  102 SER A C   
1880 O O   . SER A 105 ? 0.13735 0.10137 0.15786 0.02021  -0.01161 0.04751  102 SER A O   
1881 C CB  . SER A 105 ? 0.14840 0.15754 0.13121 0.04338  -0.06245 0.02188  102 SER A CB  
1882 O OG  . SER A 105 ? 0.13513 0.16828 0.15333 0.00727  -0.01717 0.00998  102 SER A OG  
1888 N N   . THR A 106 ? 0.16145 0.09162 0.11696 0.00777  0.03077  0.01453  103 THR A N   
1889 C CA  . THR A 106 ? 0.14502 0.11872 0.12141 0.02298  -0.00242 0.02761  103 THR A CA  
1890 C C   . THR A 106 ? 0.15995 0.07869 0.11505 0.00387  0.01367  0.01499  103 THR A C   
1891 O O   . THR A 106 ? 0.16707 0.10651 0.11187 0.00905  0.00146  -0.00994 103 THR A O   
1892 C CB  . THR A 106 ? 0.17403 0.14021 0.13578 0.02881  -0.02147 0.01803  103 THR A CB  
1893 O OG1 . THR A 106 ? 0.22117 0.17604 0.12287 0.04389  0.01350  -0.00795 103 THR A OG1 
1894 C CG2 . THR A 106 ? 0.17931 0.12830 0.14649 0.04923  -0.02316 0.01761  103 THR A CG2 
1902 N N   . PHE A 107 ? 0.15945 0.07192 0.12884 0.01317  0.01679  -0.01882 104 PHE A N   
1903 C CA  . PHE A 107 ? 0.13017 0.07917 0.13328 0.00459  0.00859  -0.00128 104 PHE A CA  
1904 C C   . PHE A 107 ? 0.13747 0.10818 0.14430 0.01911  0.00954  0.01234  104 PHE A C   
1905 O O   . PHE A 107 ? 0.15366 0.17548 0.15557 0.03459  0.02167  -0.00599 104 PHE A O   
1906 C CB  . PHE A 107 ? 0.12871 0.08891 0.12778 0.03715  -0.00397 -0.01013 104 PHE A CB  
1907 C CG  . PHE A 107 ? 0.10525 0.10208 0.13849 0.02005  -0.02687 -0.01969 104 PHE A CG  
1908 C CD1 . PHE A 107 ? 0.09269 0.08737 0.16981 0.02165  -0.04431 -0.00452 104 PHE A CD1 
1909 C CD2 . PHE A 107 ? 0.11172 0.16356 0.16313 0.02926  -0.01507 0.05462  104 PHE A CD2 
1910 C CE1 . PHE A 107 ? 0.10673 0.13880 0.17970 0.02620  -0.03847 0.01152  104 PHE A CE1 
1911 C CE2 . PHE A 107 ? 0.10411 0.19018 0.14587 0.01806  -0.03255 0.03506  104 PHE A CE2 
1912 C CZ  . PHE A 107 ? 0.11028 0.19148 0.16665 0.02838  -0.01777 -0.00507 104 PHE A CZ  
1922 N N   . GLY A 108 ? 0.15125 0.07230 0.12662 0.01487  0.01301  0.02159  105 GLY A N   
1923 C CA  . GLY A 108 ? 0.15857 0.12093 0.15920 0.03585  0.02467  0.02228  105 GLY A CA  
1924 C C   . GLY A 108 ? 0.12774 0.11724 0.15341 0.03289  0.00886  0.01980  105 GLY A C   
1925 O O   . GLY A 108 ? 0.12230 0.13501 0.16837 0.04314  0.02793  0.03213  105 GLY A O   
1929 N N   . VAL A 109 ? 0.12851 0.08091 0.15368 0.01429  0.00993  0.02453  106 VAL A N   
1930 C CA  . VAL A 109 ? 0.11849 0.07549 0.14314 0.02026  -0.01009 0.02310  106 VAL A CA  
1931 C C   . VAL A 109 ? 0.11794 0.07487 0.10545 0.02287  -0.02653 0.00310  106 VAL A C   
1932 O O   . VAL A 109 ? 0.14749 0.15437 0.12919 0.04282  -0.02143 0.01869  106 VAL A O   
1933 C CB  . VAL A 109 ? 0.12149 0.09996 0.16393 -0.00406 -0.00516 -0.00571 106 VAL A CB  
1934 C CG1 . VAL A 109 ? 0.14995 0.14865 0.11801 0.00262  0.00108  -0.04027 106 VAL A CG1 
1935 C CG2 . VAL A 109 ? 0.11721 0.08218 0.21891 -0.00807 0.00213  0.00171  106 VAL A CG2 
1945 N N   . GLU A 110 ? 0.10326 0.13446 0.10102 0.01193  0.00849  0.02793  107 GLU A N   
1946 C CA  . GLU A 110 ? 0.09633 0.10423 0.14002 0.02842  -0.00869 0.01375  107 GLU A CA  
1947 C C   . GLU A 110 ? 0.10435 0.08445 0.14077 0.04547  -0.02594 0.01021  107 GLU A C   
1948 O O   . GLU A 110 ? 0.15425 0.09141 0.21177 0.03130  -0.06484 -0.03259 107 GLU A O   
1949 C CB  . GLU A 110 ? 0.10850 0.14935 0.20420 -0.00786 0.02648  0.02191  107 GLU A CB  
1950 C CG  . GLU A 110 ? 0.17606 0.21680 0.25695 -0.02294 0.04614  0.00571  107 GLU A CG  
1951 C CD  . GLU A 110 ? 0.24225 0.26026 0.29529 -0.00341 0.03792  0.00841  107 GLU A CD  
1952 O OE1 . GLU A 110 ? 0.28045 0.31620 0.27977 -0.03197 0.01893  0.04176  107 GLU A OE1 
1953 O OE2 . GLU A 110 ? 0.28140 0.34279 0.34955 -0.02366 0.05165  0.02715  107 GLU A OE2 
1960 N N   . THR A 111 ? 0.11182 0.10137 0.11126 -0.01689 -0.01537 0.01671  108 THR A N   
1963 C C   . THR A 111 ? 0.10289 0.08617 0.13681 0.04592  0.00217  -0.02979 108 THR A C   
1964 O O   . THR A 111 ? 0.11339 0.10422 0.14698 0.03031  -0.00933 0.00177  108 THR A O   
1985 N N   . ILE A 112 ? 0.07570 0.09744 0.13446 0.02569  -0.01480 -0.02186 109 ILE A N   
1986 C CA  . ILE A 112 ? 0.07409 0.10270 0.11257 -0.00500 -0.01723 -0.03782 109 ILE A CA  
1987 C C   . ILE A 112 ? 0.06960 0.10240 0.11213 -0.00392 -0.01968 -0.00903 109 ILE A C   
1988 O O   . ILE A 112 ? 0.11435 0.11374 0.13019 0.02742  -0.01479 0.00568  109 ILE A O   
1989 C CB  . ILE A 112 ? 0.08047 0.10752 0.10212 -0.00545 -0.02151 -0.02435 109 ILE A CB  
1990 C CG1 . ILE A 112 ? 0.10627 0.10642 0.12134 -0.02410 0.00547  -0.00392 109 ILE A CG1 
1991 C CG2 . ILE A 112 ? 0.09799 0.14882 0.11638 -0.02428 -0.00932 -0.03305 109 ILE A CG2 
1992 C CD1 . ILE A 112 ? 0.10617 0.13896 0.12146 -0.02545 -0.00049 -0.02313 109 ILE A CD1 
2004 N N   . PRO A 113 ? 0.08027 0.12293 0.08968 0.00855  -0.01903 -0.01374 110 PRO A N   
2005 C CA  . PRO A 113 ? 0.08270 0.13398 0.11365 0.00201  -0.02828 -0.00471 110 PRO A CA  
2006 C C   . PRO A 113 ? 0.08938 0.15132 0.10854 0.00939  -0.02500 0.00540  110 PRO A C   
2007 O O   . PRO A 113 ? 0.14254 0.10998 0.10796 0.01625  0.01507  0.00090  110 PRO A O   
2008 C CB  . PRO A 113 ? 0.12423 0.16116 0.09256 -0.04175 -0.00776 -0.01524 110 PRO A CB  
2009 C CG  . PRO A 113 ? 0.12679 0.08805 0.08309 -0.00927 -0.00656 -0.02106 110 PRO A CG  
2010 C CD  . PRO A 113 ? 0.09790 0.11118 0.08524 0.00081  -0.02471 -0.02919 110 PRO A CD  
2018 N N   . THR A 114 ? 0.10452 0.10600 0.11333 -0.00212 -0.00682 -0.02322 111 THR A N   
2019 C CA  . THR A 114 ? 0.11333 0.09989 0.10949 0.00185  -0.02130 0.00932  111 THR A CA  
2020 C C   . THR A 114 ? 0.12984 0.10186 0.10737 0.01049  -0.02073 -0.00008 111 THR A C   
2021 O O   . THR A 114 ? 0.12258 0.11216 0.07697 -0.00390 0.00194  0.01607  111 THR A O   
2022 C CB  . THR A 114 ? 0.12156 0.13135 0.13265 0.01286  -0.03501 0.04370  111 THR A CB  
2023 O OG1 . THR A 114 ? 0.11384 0.20887 0.16028 -0.02131 -0.02325 0.03561  111 THR A OG1 
2024 C CG2 . THR A 114 ? 0.15161 0.12713 0.12816 -0.00953 -0.02655 0.01832  111 THR A CG2 
2032 N N   . VAL A 115 ? 0.11556 0.08200 0.11418 0.01574  -0.02306 -0.00523 112 VAL A N   
2033 C CA  A VAL A 115 ? 0.11385 0.10245 0.12775 0.01060  -0.01320 0.00540  112 VAL A CA  
2034 C CA  B VAL A 115 ? 0.11385 0.10245 0.12775 0.01060  -0.01320 0.00540  112 VAL A CA  
2035 C C   . VAL A 115 ? 0.10365 0.11241 0.11869 0.00853  -0.01194 -0.00415 112 VAL A C   
2036 O O   . VAL A 115 ? 0.09142 0.12042 0.12322 0.00439  -0.01494 0.02232  112 VAL A O   
2037 C CB  A VAL A 115 ? 0.16315 0.12415 0.16005 -0.00460 -0.00900 0.00730  112 VAL A CB  
2038 C CB  B VAL A 115 ? 0.16315 0.12415 0.16005 -0.00460 -0.00900 0.00730  112 VAL A CB  
2039 C CG1 A VAL A 115 ? 0.17555 0.16095 0.16515 -0.00330 -0.00650 0.00990  112 VAL A CG1 
2040 C CG1 B VAL A 115 ? 0.17555 0.16095 0.16515 -0.00330 -0.00650 0.00990  112 VAL A CG1 
2041 C CG2 A VAL A 115 ? 0.18135 0.14855 0.18215 0.00420  0.00270  0.00730  112 VAL A CG2 
2042 C CG2 B VAL A 115 ? 0.18135 0.14855 0.18215 0.00420  0.00270  0.00730  112 VAL A CG2 
2059 N N   . ILE A 116 ? 0.11529 0.11874 0.11912 -0.00567 -0.00398 -0.02221 113 ILE A N   
2060 C CA  . ILE A 116 ? 0.13846 0.09528 0.14385 0.01631  0.02270  0.00833  113 ILE A CA  
2061 C C   . ILE A 116 ? 0.13700 0.07499 0.13180 0.02599  0.00018  0.01879  113 ILE A C   
2062 O O   . ILE A 116 ? 0.11364 0.15246 0.11231 0.00811  0.01412  0.03518  113 ILE A O   
2063 C CB  . ILE A 116 ? 0.13817 0.11535 0.16063 0.01228  0.01408  -0.01768 113 ILE A CB  
2064 C CG1 . ILE A 116 ? 0.15232 0.12309 0.16261 0.01147  -0.00040 -0.01485 113 ILE A CG1 
2065 C CG2 . ILE A 116 ? 0.12228 0.12019 0.14191 0.01998  -0.00339 -0.02983 113 ILE A CG2 
2066 C CD1 . ILE A 116 ? 0.13936 0.16975 0.17029 0.00373  -0.01177 0.00218  113 ILE A CD1 
2078 N N   . ALA A 117 ? 0.11654 0.07241 0.13093 -0.00588 0.01112  0.01831  114 ALA A N   
2079 C CA  . ALA A 117 ? 0.10957 0.08752 0.12420 -0.01733 0.01362  0.02247  114 ALA A CA  
2080 C C   . ALA A 117 ? 0.12493 0.08659 0.13546 -0.01009 0.01561  0.01357  114 ALA A C   
2081 O O   . ALA A 117 ? 0.14525 0.09054 0.14343 0.00711  0.00542  0.00889  114 ALA A O   
2082 C CB  . ALA A 117 ? 0.14382 0.12049 0.14459 0.00920  0.01661  0.02932  114 ALA A CB  
2088 N N   . VAL A 118 ? 0.10591 0.11027 0.13062 -0.00585 0.00066  0.00994  115 VAL A N   
2089 C CA  . VAL A 118 ? 0.10017 0.12729 0.13387 -0.03045 -0.03239 -0.02285 115 VAL A CA  
2090 C C   . VAL A 118 ? 0.10115 0.08499 0.14055 -0.02822 -0.01925 -0.00724 115 VAL A C   
2091 O O   . VAL A 118 ? 0.11648 0.10777 0.16337 0.00373  0.00493  0.00224  115 VAL A O   
2092 C CB  . VAL A 118 ? 0.11399 0.20313 0.13116 -0.03187 -0.02590 -0.04397 115 VAL A CB  
2093 C CG1 . VAL A 118 ? 0.10839 0.19859 0.13334 -0.06236 -0.01932 -0.03559 115 VAL A CG1 
2094 C CG2 . VAL A 118 ? 0.14155 0.26035 0.13312 -0.04810 -0.02140 0.01021  115 VAL A CG2 
2104 N N   . ASN A 119 ? 0.09598 0.10248 0.14713 -0.02279 -0.01582 0.02733  116 ASN A N   
2105 C CA  . ASN A 119 ? 0.09165 0.11322 0.15175 -0.00917 -0.02691 0.01763  116 ASN A CA  
2106 C C   . ASN A 119 ? 0.08365 0.13592 0.14855 0.00397  -0.02557 0.01165  116 ASN A C   
2107 O O   . ASN A 119 ? 0.12909 0.13170 0.17511 -0.00824 0.00800  0.00627  116 ASN A O   
2108 C CB  . ASN A 119 ? 0.13619 0.17518 0.16776 -0.00872 -0.00974 0.02160  116 ASN A CB  
2109 C CG  . ASN A 119 ? 0.14800 0.21615 0.18190 0.01840  -0.01509 0.00962  116 ASN A CG  
2110 O OD1 . ASN A 119 ? 0.11928 0.19343 0.16729 0.04089  -0.02814 0.02426  116 ASN A OD1 
2111 N ND2 . ASN A 119 ? 0.18850 0.29218 0.21055 0.03525  -0.00575 0.00544  116 ASN A ND2 
2118 N N   . ALA A 120 ? 0.08506 0.11616 0.15763 0.00559  -0.00629 -0.01281 117 ALA A N   
2119 C CA  . ALA A 120 ? 0.10807 0.09486 0.16397 0.01400  0.01059  -0.00292 117 ALA A CA  
2120 C C   . ALA A 120 ? 0.13998 0.10054 0.16106 -0.00950 0.02694  0.00424  117 ALA A C   
2121 O O   . ALA A 120 ? 0.17634 0.17815 0.15659 0.01291  0.04260  0.00232  117 ALA A O   
2122 C CB  . ALA A 120 ? 0.12267 0.13196 0.15192 -0.02496 -0.00308 -0.01553 117 ALA A CB  
2128 N N   . ASP A 121 ? 0.14220 0.12256 0.15449 0.03538  0.02545  0.01759  118 ASP A N   
2129 C CA  . ASP A 121 ? 0.16966 0.17772 0.17992 0.03414  0.03782  0.02146  118 ASP A CA  
2130 C C   . ASP A 121 ? 0.19363 0.15809 0.18558 0.01963  0.03056  0.02357  118 ASP A C   
2131 O O   . ASP A 121 ? 0.22976 0.19944 0.22471 -0.01038 0.05464  -0.00190 118 ASP A O   
2132 C CB  . ASP A 121 ? 0.16918 0.24828 0.19622 0.02402  0.04783  0.00290  118 ASP A CB  
2133 C CG  . ASP A 121 ? 0.19061 0.22379 0.20959 0.02554  0.02920  0.03335  118 ASP A CG  
2134 O OD1 . ASP A 121 ? 0.18081 0.18407 0.22008 0.01100  0.01566  0.03779  118 ASP A OD1 
2135 O OD2 . ASP A 121 ? 0.22578 0.27552 0.22629 0.04264  0.00129  0.04462  118 ASP A OD2 
2140 N N   . THR A 122 ? 0.16689 0.15649 0.19358 0.02158  0.03011  -0.00895 119 THR A N   
2141 C CA  . THR A 122 ? 0.15991 0.16712 0.19686 0.02201  0.01925  -0.00270 119 THR A CA  
2142 C C   . THR A 122 ? 0.15925 0.14654 0.18759 0.00027  0.01823  0.00862  119 THR A C   
2143 O O   . THR A 122 ? 0.18222 0.13617 0.20326 0.00934  0.01708  0.00629  119 THR A O   
2144 C CB  . THR A 122 ? 0.15518 0.20309 0.22038 0.02045  -0.00013 0.02506  119 THR A CB  
2145 O OG1 . THR A 122 ? 0.15503 0.14319 0.23345 0.01732  0.00627  0.02047  119 THR A OG1 
2146 C CG2 . THR A 122 ? 0.17811 0.25426 0.22556 0.02049  -0.01269 0.04389  119 THR A CG2 
2154 N N   . GLY A 123 ? 0.13203 0.12942 0.15496 0.01140  0.00319  0.00473  120 GLY A N   
2155 C CA  . GLY A 123 ? 0.13199 0.13233 0.13813 0.02445  -0.00071 0.02327  120 GLY A CA  
2156 C C   . GLY A 123 ? 0.11239 0.10623 0.15459 0.00472  0.00005  0.03223  120 GLY A C   
2157 O O   . GLY A 123 ? 0.11975 0.12512 0.16285 0.00119  -0.00523 -0.01104 120 GLY A O   
2161 N N   . ALA A 124 ? 0.12005 0.12254 0.15917 0.00909  0.00276  0.02871  121 ALA A N   
2162 C CA  . ALA A 124 ? 0.12455 0.08577 0.15555 0.01619  -0.01227 0.01315  121 ALA A CA  
2163 C C   . ALA A 124 ? 0.13284 0.12712 0.15074 -0.05026 0.01453  -0.02079 121 ALA A C   
2164 O O   . ALA A 124 ? 0.14043 0.13280 0.14420 -0.05688 0.01827  -0.01341 121 ALA A O   
2165 C CB  . ALA A 124 ? 0.11893 0.17025 0.17705 0.00683  -0.02439 0.01812  121 ALA A CB  
2171 N N   . VAL A 125 ? 0.13236 0.12114 0.14806 -0.02133 0.01324  -0.02399 122 VAL A N   
2172 C CA  . VAL A 125 ? 0.15387 0.08261 0.14224 -0.01496 0.00796  -0.00090 122 VAL A CA  
2173 C C   . VAL A 125 ? 0.18855 0.11170 0.12113 -0.02908 0.00639  0.00363  122 VAL A C   
2174 O O   . VAL A 125 ? 0.24968 0.14356 0.13060 -0.02519 -0.00469 -0.02215 122 VAL A O   
2175 C CB  . VAL A 125 ? 0.13764 0.07872 0.16566 -0.01471 0.01396  0.00076  122 VAL A CB  
2176 C CG1 . VAL A 125 ? 0.15880 0.08002 0.19745 -0.01787 0.06316  -0.00239 122 VAL A CG1 
2177 C CG2 . VAL A 125 ? 0.13957 0.16794 0.17101 -0.03873 -0.01961 -0.04973 122 VAL A CG2 
2187 N N   . VAL A 126 ? 0.15926 0.10500 0.10571 -0.00274 -0.01176 -0.00695 123 VAL A N   
2188 C CA  . VAL A 126 ? 0.17098 0.12906 0.12985 0.02607  -0.01347 0.00296  123 VAL A CA  
2189 C C   . VAL A 126 ? 0.17803 0.11768 0.11959 0.01749  0.00706  0.00850  123 VAL A C   
2190 O O   . VAL A 126 ? 0.20760 0.15633 0.14126 0.04592  0.04948  0.06018  123 VAL A O   
2191 C CB  . VAL A 126 ? 0.15433 0.17797 0.16350 0.02074  -0.01494 -0.01511 123 VAL A CB  
2192 C CG1 . VAL A 126 ? 0.18186 0.16928 0.20548 0.01140  0.00117  -0.07045 123 VAL A CG1 
2193 C CG2 . VAL A 126 ? 0.17821 0.19128 0.13610 0.03113  -0.00901 -0.05152 123 VAL A CG2 
2203 N N   . SER A 127 ? 0.14877 0.11151 0.09855 -0.00080 0.01023  -0.01403 124 SER A N   
2204 C CA  . SER A 127 ? 0.12255 0.15202 0.09409 -0.03869 -0.01807 -0.00620 124 SER A CA  
2205 C C   . SER A 127 ? 0.12496 0.11952 0.10890 -0.02193 -0.00360 0.01313  124 SER A C   
2206 O O   . SER A 127 ? 0.12121 0.12046 0.10716 -0.00873 -0.00055 -0.00583 124 SER A O   
2207 C CB  . SER A 127 ? 0.10288 0.11909 0.10328 0.00505  -0.04805 0.00468  124 SER A CB  
2208 O OG  . SER A 127 ? 0.13173 0.12160 0.13751 0.02784  -0.02311 -0.00255 124 SER A OG  
2214 N N   . THR A 128 ? 0.15250 0.14596 0.09544 -0.02206 0.02276  0.02276  125 THR A N   
2215 C CA  . THR A 128 ? 0.12896 0.13279 0.09469 -0.01799 0.00835  0.02521  125 THR A CA  
2216 C C   . THR A 128 ? 0.14264 0.16430 0.09836 0.00028  -0.00380 0.03080  125 THR A C   
2217 O O   . THR A 128 ? 0.15116 0.14064 0.11316 0.01827  0.00172  0.01189  125 THR A O   
2218 C CB  . THR A 128 ? 0.14644 0.11747 0.14653 -0.05150 0.02367  -0.00959 125 THR A CB  
2219 O OG1 . THR A 128 ? 0.17881 0.16827 0.18143 -0.05347 0.06734  -0.01094 125 THR A OG1 
2220 C CG2 . THR A 128 ? 0.17172 0.14036 0.15642 -0.06573 0.00978  -0.03067 125 THR A CG2 
2228 N N   . LYS A 129 ? 0.16795 0.12352 0.12123 -0.02848 0.00435  0.02198  126 LYS A N   
2229 C CA  A LYS A 129 ? 0.18465 0.13465 0.13845 -0.00360 0.02810  0.01360  126 LYS A CA  
2230 C CA  B LYS A 129 ? 0.18465 0.13465 0.13845 -0.00360 0.02810  0.01360  126 LYS A CA  
2231 C C   . LYS A 129 ? 0.16010 0.13108 0.11252 -0.00563 0.01770  -0.01039 126 LYS A C   
2232 O O   . LYS A 129 ? 0.16180 0.17438 0.10891 -0.00183 0.03531  -0.04490 126 LYS A O   
2233 C CB  A LYS A 129 ? 0.24715 0.17125 0.21115 -0.00410 0.04670  0.01170  126 LYS A CB  
2234 C CB  B LYS A 129 ? 0.24715 0.17125 0.21115 -0.00410 0.04670  0.01170  126 LYS A CB  
2235 C CG  A LYS A 129 ? 0.35635 0.25935 0.31855 -0.00990 0.05350  -0.00110 126 LYS A CG  
2236 C CG  B LYS A 129 ? 0.35635 0.25935 0.31855 -0.00990 0.05350  -0.00110 126 LYS A CG  
2237 C CD  A LYS A 129 ? 0.47665 0.44315 0.44755 -0.01220 0.08380  -0.00360 126 LYS A CD  
2238 C CD  B LYS A 129 ? 0.47665 0.44315 0.44755 -0.01220 0.08380  -0.00360 126 LYS A CD  
2239 C CE  A LYS A 129 ? 0.56575 0.59555 0.53715 -0.01080 0.12950  -0.00360 126 LYS A CE  
2240 C CE  B LYS A 129 ? 0.56575 0.59555 0.53715 -0.01080 0.12950  -0.00360 126 LYS A CE  
2241 N NZ  A LYS A 129 ? 0.63715 0.68955 0.63035 -0.00720 0.15870  0.00020  126 LYS A NZ  
2242 N NZ  B LYS A 129 ? 0.63715 0.68955 0.63035 -0.00720 0.15870  0.00020  126 LYS A NZ  
2267 N N   . GLY A 130 ? 0.13358 0.08683 0.11054 -0.01663 0.01655  -0.03367 127 GLY A N   
2268 C CA  . GLY A 130 ? 0.12956 0.11642 0.10581 -0.01490 0.01588  -0.01474 127 GLY A CA  
2269 C C   . GLY A 130 ? 0.12545 0.11122 0.09030 -0.00737 -0.00133 -0.02503 127 GLY A C   
2270 O O   . GLY A 130 ? 0.14424 0.11885 0.10188 -0.01341 -0.00003 0.00313  127 GLY A O   
2274 N N   . ARG A 131 ? 0.14027 0.11876 0.11336 -0.01335 0.00439  -0.03895 128 ARG A N   
2275 C CA  . ARG A 131 ? 0.13222 0.13862 0.11954 -0.00856 0.01782  -0.03472 128 ARG A CA  
2276 C C   . ARG A 131 ? 0.13623 0.13710 0.12348 0.02636  -0.00107 0.00268  128 ARG A C   
2277 O O   . ARG A 131 ? 0.21243 0.10844 0.15014 0.01630  0.04124  0.00079  128 ARG A O   
2278 C CB  . ARG A 131 ? 0.16016 0.16582 0.13565 0.03323  0.01265  -0.04936 128 ARG A CB  
2279 C CG  . ARG A 131 ? 0.18593 0.16429 0.12553 0.05824  0.01639  -0.00812 128 ARG A CG  
2280 C CD  . ARG A 131 ? 0.17257 0.18352 0.14935 0.02940  0.01675  0.00594  128 ARG A CD  
2281 N NE  . ARG A 131 ? 0.14817 0.16288 0.14584 -0.00266 0.01080  -0.00475 128 ARG A NE  
2282 C CZ  . ARG A 131 ? 0.14668 0.18141 0.12345 0.01181  0.02311  -0.02188 128 ARG A CZ  
2283 N NH1 . ARG A 131 ? 0.15987 0.17280 0.13614 -0.00289 0.03075  0.00613  128 ARG A NH1 
2284 N NH2 . ARG A 131 ? 0.16618 0.23102 0.13267 0.01187  0.02589  -0.00826 128 ARG A NH2 
2298 N N   . GLU A 132 ? 0.10976 0.15804 0.11676 0.00131  -0.00345 -0.01876 129 GLU A N   
2299 C CA  . GLU A 132 ? 0.11051 0.16121 0.14112 0.00044  -0.00048 -0.00058 129 GLU A CA  
2300 C C   . GLU A 132 ? 0.14819 0.17794 0.12620 0.01844  0.02665  0.03417  129 GLU A C   
2301 O O   . GLU A 132 ? 0.17848 0.19953 0.13984 0.02865  0.00604  0.00350  129 GLU A O   
2302 C CB  . GLU A 132 ? 0.14759 0.20503 0.18659 -0.02831 -0.00929 0.01231  129 GLU A CB  
2303 C CG  . GLU A 132 ? 0.21186 0.25053 0.23383 -0.02323 -0.01510 0.02821  129 GLU A CG  
2304 C CD  . GLU A 132 ? 0.25007 0.35940 0.28584 0.01749  -0.00562 0.00991  129 GLU A CD  
2305 O OE1 . GLU A 132 ? 0.28770 0.35061 0.31177 0.05063  0.00513  0.00398  129 GLU A OE1 
2306 O OE2 . GLU A 132 ? 0.27098 0.44747 0.31414 0.01640  0.00501  -0.00496 129 GLU A OE2 
2313 N N   . ARG A 133 ? 0.15860 0.12583 0.11902 -0.00622 0.02166  0.03235  130 ARG A N   
2314 C CA  . ARG A 133 ? 0.14209 0.17238 0.12445 -0.00957 -0.01468 0.04206  130 ARG A CA  
2315 C C   . ARG A 133 ? 0.14843 0.17004 0.11279 -0.01934 0.01291  0.04703  130 ARG A C   
2316 O O   . ARG A 133 ? 0.17761 0.18222 0.10752 -0.01855 0.00588  0.03193  130 ARG A O   
2317 C CB  . ARG A 133 ? 0.17212 0.20166 0.18369 -0.06089 -0.03837 0.01860  130 ARG A CB  
2318 C CG  . ARG A 133 ? 0.23658 0.26371 0.23915 -0.06375 -0.02289 0.03533  130 ARG A CG  
2319 C CD  . ARG A 133 ? 0.26610 0.32286 0.29299 -0.08851 0.02361  0.05277  130 ARG A CD  
2320 N NE  . ARG A 133 ? 0.29037 0.31961 0.30198 -0.09709 0.06005  0.05136  130 ARG A NE  
2321 C CZ  . ARG A 133 ? 0.31496 0.35807 0.33047 -0.05139 0.08043  0.04810  130 ARG A CZ  
2322 N NH1 . ARG A 133 ? 0.32621 0.35111 0.34753 -0.04226 0.09972  0.08327  130 ARG A NH1 
2323 N NH2 . ARG A 133 ? 0.33461 0.38520 0.34824 -0.03931 0.06965  0.00485  130 ARG A NH2 
2337 N N   . LEU A 134 ? 0.11240 0.16693 0.10008 -0.02923 0.00414  0.00690  131 LEU A N   
2338 C CA  . LEU A 134 ? 0.09740 0.15789 0.12278 -0.02642 -0.00315 -0.01070 131 LEU A CA  
2339 C C   . LEU A 134 ? 0.11876 0.15355 0.11252 -0.02182 0.00573  0.00432  131 LEU A C   
2340 O O   . LEU A 134 ? 0.14356 0.16215 0.09726 -0.00077 0.03351  -0.01102 131 LEU A O   
2341 C CB  . LEU A 134 ? 0.10300 0.15087 0.11004 -0.01727 0.00628  -0.00521 131 LEU A CB  
2342 C CG  . LEU A 134 ? 0.11013 0.14670 0.10313 0.00525  0.00809  -0.01455 131 LEU A CG  
2343 C CD1 . LEU A 134 ? 0.10776 0.12234 0.10543 0.02121  0.01945  -0.01709 131 LEU A CD1 
2344 C CD2 . LEU A 134 ? 0.15936 0.16235 0.10974 -0.01091 0.01702  0.00839  131 LEU A CD2 
2356 N N   . LEU A 135 ? 0.13148 0.15856 0.12977 0.01462  0.00069  0.01921  132 LEU A N   
2357 C CA  . LEU A 135 ? 0.13526 0.15617 0.12644 0.05041  -0.01280 0.01173  132 LEU A CA  
2358 C C   . LEU A 135 ? 0.16081 0.18141 0.12102 0.03939  -0.00331 -0.01391 132 LEU A C   
2359 O O   . LEU A 135 ? 0.22124 0.26908 0.13902 0.01091  0.01455  -0.05773 132 LEU A O   
2360 C CB  . LEU A 135 ? 0.15506 0.17495 0.14160 0.02322  -0.03493 0.00797  132 LEU A CB  
2361 C CG  . LEU A 135 ? 0.17591 0.20869 0.15564 0.03384  -0.02477 0.00335  132 LEU A CG  
2362 C CD1 . LEU A 135 ? 0.19114 0.20612 0.16052 0.02666  -0.03194 -0.00530 132 LEU A CD1 
2363 C CD2 . LEU A 135 ? 0.20477 0.21939 0.15402 0.04865  -0.01628 0.01139  132 LEU A CD2 
2375 N N   . THR A 136 ? 0.12888 0.20711 0.11722 0.03739  0.00367  0.01599  133 THR A N   
2376 C CA  . THR A 136 ? 0.12663 0.27381 0.13557 0.04699  0.02942  0.03260  133 THR A CA  
2377 C C   . THR A 136 ? 0.14024 0.25022 0.11311 0.01707  0.01677  0.02672  133 THR A C   
2378 O O   . THR A 136 ? 0.16900 0.25820 0.11110 0.00719  0.01245  -0.00412 133 THR A O   
2379 C CB  . THR A 136 ? 0.14842 0.30719 0.17608 0.03068  0.00910  0.07524  133 THR A CB  
2380 O OG1 . THR A 136 ? 0.16043 0.35212 0.21142 -0.02879 -0.00210 0.07307  133 THR A OG1 
2381 C CG2 . THR A 136 ? 0.16499 0.33366 0.18975 0.04784  0.03474  0.07730  133 THR A CG2 
2389 N N   . ASP A 137 ? 0.10966 0.21059 0.09760 0.02855  0.00714  -0.00571 134 ASP A N   
2390 C CA  . ASP A 137 ? 0.11030 0.21616 0.12294 0.04978  0.00621  0.00573  134 ASP A CA  
2391 C C   . ASP A 137 ? 0.10946 0.17760 0.12432 0.04275  0.01479  0.01049  134 ASP A C   
2392 O O   . ASP A 137 ? 0.11097 0.17267 0.12214 0.01431  0.00664  -0.00159 134 ASP A O   
2393 C CB  . ASP A 137 ? 0.12362 0.15745 0.12447 0.02237  0.00357  0.01082  134 ASP A CB  
2394 C CG  . ASP A 137 ? 0.13096 0.18264 0.09898 -0.02166 -0.00077 0.00469  134 ASP A CG  
2395 O OD1 . ASP A 137 ? 0.13360 0.16102 0.10207 0.00240  0.02590  -0.00720 134 ASP A OD1 
2396 O OD2 . ASP A 137 ? 0.13081 0.18334 0.11242 -0.01231 -0.02155 -0.03747 134 ASP A OD2 
2401 N N   . PRO A 138 ? 0.12263 0.18385 0.14373 0.02769  0.02055  -0.01701 135 PRO A N   
2402 C CA  . PRO A 138 ? 0.14394 0.17454 0.15236 0.02002  -0.00417 -0.02018 135 PRO A CA  
2403 C C   . PRO A 138 ? 0.14831 0.18620 0.12860 0.02382  -0.01415 0.01622  135 PRO A C   
2404 O O   . PRO A 138 ? 0.16485 0.19023 0.12556 0.00985  0.01603  0.00468  135 PRO A O   
2405 C CB  . PRO A 138 ? 0.15207 0.14920 0.17168 0.03210  -0.00128 -0.00194 135 PRO A CB  
2406 C CG  . PRO A 138 ? 0.15491 0.17963 0.17895 -0.00697 0.01950  -0.03582 135 PRO A CG  
2407 C CD  . PRO A 138 ? 0.14653 0.19713 0.16527 0.01239  0.02781  -0.01771 135 PRO A CD  
2415 N N   . GLU A 139 ? 0.13433 0.14938 0.11168 0.00981  -0.01475 -0.02007 136 GLU A N   
2416 C CA  . GLU A 139 ? 0.13828 0.14513 0.14142 -0.01021 -0.01442 0.01017  136 GLU A CA  
2417 C C   . GLU A 139 ? 0.08037 0.11934 0.14156 -0.01512 -0.02935 0.03605  136 GLU A C   
2418 O O   . GLU A 139 ? 0.08179 0.17967 0.17360 0.01013  -0.04725 0.01564  136 GLU A O   
2419 C CB  . GLU A 139 ? 0.19448 0.19816 0.18305 0.00332  -0.00160 -0.00194 136 GLU A CB  
2420 C CG  . GLU A 139 ? 0.23071 0.22287 0.21368 0.02693  -0.00150 -0.01846 136 GLU A CG  
2421 C CD  . GLU A 139 ? 0.28258 0.30535 0.27520 0.01895  -0.00476 -0.02319 136 GLU A CD  
2422 O OE1 . GLU A 139 ? 0.28752 0.31886 0.27545 -0.01509 0.03274  -0.01605 136 GLU A OE1 
2423 O OE2 . GLU A 139 ? 0.33847 0.33992 0.33989 0.00352  -0.02497 0.00814  136 GLU A OE2 
2430 N N   . GLY A 140 ? 0.08878 0.14451 0.12235 -0.02003 -0.00550 0.02008  137 GLY A N   
2431 C CA  . GLY A 140 ? 0.12332 0.15252 0.10051 -0.02139 -0.00349 0.00193  137 GLY A CA  
2432 C C   . GLY A 140 ? 0.10491 0.13934 0.09708 -0.02294 -0.01123 -0.01030 137 GLY A C   
2433 O O   . GLY A 140 ? 0.11574 0.14299 0.10715 -0.02253 0.01388  -0.01265 137 GLY A O   
2437 N N   . LYS A 141 ? 0.14304 0.11383 0.09023 -0.00732 0.01408  0.00280  138 LYS A N   
2438 C CA  . LYS A 141 ? 0.15811 0.10142 0.09490 -0.02209 0.01035  -0.01433 138 LYS A CA  
2439 C C   . LYS A 141 ? 0.15181 0.12923 0.06663 -0.02729 0.00034  -0.00838 138 LYS A C   
2440 O O   . LYS A 141 ? 0.14739 0.15766 0.09528 -0.00369 0.00176  0.01635  138 LYS A O   
2441 C CB  . LYS A 141 ? 0.15325 0.13974 0.10431 -0.04094 0.00674  -0.02105 138 LYS A CB  
2442 C CG  . LYS A 141 ? 0.15814 0.18391 0.11714 -0.07397 0.01341  -0.03364 138 LYS A CG  
2443 C CD  . LYS A 141 ? 0.19376 0.19991 0.11652 -0.06014 0.03305  -0.01782 138 LYS A CD  
2444 C CE  . LYS A 141 ? 0.23523 0.22417 0.13465 -0.06023 0.04973  -0.00187 138 LYS A CE  
2445 N NZ  . LYS A 141 ? 0.27886 0.25711 0.16189 -0.05026 0.06921  -0.02362 138 LYS A NZ  
2459 N N   . ASN A 142 ? 0.14929 0.15252 0.06933 -0.04180 0.00613  -0.01434 139 ASN A N   
2460 C CA  . ASN A 142 ? 0.14045 0.16425 0.08577 -0.05056 0.00011  -0.00884 139 ASN A CA  
2461 C C   . ASN A 142 ? 0.13412 0.14286 0.09463 -0.00914 0.00204  -0.02011 139 ASN A C   
2462 O O   . ASN A 142 ? 0.15854 0.14849 0.10691 -0.01546 -0.00676 -0.01557 139 ASN A O   
2463 C CB  . ASN A 142 ? 0.15052 0.16437 0.09875 -0.05362 -0.00149 0.01791  139 ASN A CB  
2464 C CG  . ASN A 142 ? 0.17903 0.19917 0.10733 -0.01707 0.02486  0.02351  139 ASN A CG  
2465 O OD1 . ASN A 142 ? 0.19665 0.24158 0.10040 -0.00037 0.03803  0.02455  139 ASN A OD1 
2466 N ND2 . ASN A 142 ? 0.18120 0.18227 0.10304 -0.02041 0.02630  0.00244  139 ASN A ND2 
2473 N N   . PHE A 143 ? 0.12138 0.15874 0.10856 -0.01792 0.00163  0.00039  140 PHE A N   
2474 C CA  . PHE A 143 ? 0.12387 0.15954 0.10732 -0.02429 0.00118  -0.01864 140 PHE A CA  
2475 C C   . PHE A 143 ? 0.15110 0.15973 0.09855 -0.00112 -0.00127 0.01041  140 PHE A C   
2476 O O   . PHE A 143 ? 0.16877 0.18978 0.10380 0.02405  -0.00957 0.02376  140 PHE A O   
2477 C CB  . PHE A 143 ? 0.12842 0.15661 0.10103 -0.03539 0.01170  0.01079  140 PHE A CB  
2478 C CG  . PHE A 143 ? 0.13066 0.15693 0.10902 -0.03684 0.00925  -0.00972 140 PHE A CG  
2479 C CD1 . PHE A 143 ? 0.12332 0.16019 0.12985 -0.03532 0.02350  -0.00993 140 PHE A CD1 
2480 C CD2 . PHE A 143 ? 0.15020 0.19028 0.11642 -0.04524 0.01905  -0.00925 140 PHE A CD2 
2481 C CE1 . PHE A 143 ? 0.15662 0.18467 0.14983 -0.03826 0.03482  -0.00018 140 PHE A CE1 
2482 C CE2 . PHE A 143 ? 0.17192 0.17081 0.13527 -0.04443 0.03195  0.05028  140 PHE A CE2 
2483 C CZ  . PHE A 143 ? 0.18103 0.14348 0.14525 -0.06806 0.03396  -0.00236 140 PHE A CZ  
2493 N N   . PRO A 144 ? 0.16527 0.15315 0.11810 0.00273  -0.00554 -0.00835 141 PRO A N   
2494 C CA  . PRO A 144 ? 0.15810 0.13695 0.11746 -0.00463 -0.01651 -0.02302 141 PRO A CA  
2495 C C   . PRO A 144 ? 0.15903 0.16881 0.11241 -0.05384 -0.02311 -0.01636 141 PRO A C   
2496 O O   . PRO A 144 ? 0.18126 0.17082 0.10277 -0.04747 -0.01956 -0.01818 141 PRO A O   
2497 C CB  . PRO A 144 ? 0.19336 0.17376 0.12498 -0.00198 0.01023  -0.01169 141 PRO A CB  
2498 C CG  . PRO A 144 ? 0.20190 0.18069 0.15535 -0.01461 0.00509  -0.03585 141 PRO A CG  
2499 C CD  . PRO A 144 ? 0.18617 0.18998 0.16255 0.00809  -0.00822 -0.02192 141 PRO A CD  
2507 N N   . TRP A 145 ? 0.15482 0.17172 0.12245 -0.04335 -0.00249 0.01234  142 TRP A N   
2508 C CA  . TRP A 145 ? 0.15247 0.18355 0.12516 -0.07349 -0.00176 -0.00220 142 TRP A CA  
2509 C C   . TRP A 145 ? 0.18566 0.23783 0.11558 -0.07418 0.00777  0.00976  142 TRP A C   
2510 O O   . TRP A 145 ? 0.19034 0.25602 0.11473 -0.08627 -0.02077 0.00162  142 TRP A O   
2511 C CB  . TRP A 145 ? 0.15351 0.21535 0.12728 -0.00963 0.00238  0.01573  142 TRP A CB  
2512 C CG  . TRP A 145 ? 0.13887 0.19163 0.12082 0.00250  -0.00727 0.01622  142 TRP A CG  
2513 C CD1 . TRP A 145 ? 0.15698 0.19967 0.12274 -0.01478 0.00506  0.00792  142 TRP A CD1 
2514 C CD2 . TRP A 145 ? 0.11940 0.15613 0.12036 0.01299  -0.03107 -0.00990 142 TRP A CD2 
2515 N NE1 . TRP A 145 ? 0.13991 0.17291 0.13073 -0.00871 -0.01008 -0.02225 142 TRP A NE1 
2516 C CE2 . TRP A 145 ? 0.10577 0.16761 0.13409 0.03193  -0.03215 -0.01499 142 TRP A CE2 
2517 C CE3 . TRP A 145 ? 0.12367 0.14988 0.12703 0.03306  -0.02567 0.02064  142 TRP A CE3 
2518 C CZ2 . TRP A 145 ? 0.14123 0.17961 0.15289 0.06044  -0.01084 -0.01682 142 TRP A CZ2 
2519 C CZ3 . TRP A 145 ? 0.13788 0.13014 0.14271 0.03155  -0.01682 0.01765  142 TRP A CZ3 
2520 C CH2 . TRP A 145 ? 0.14267 0.17839 0.16038 0.02196  -0.01922 -0.00027 142 TRP A CH2 
2531 N N   . SER A 146 ? 0.22352 0.17940 0.17277 -0.03655 0.01749  0.01838  143 SER A N   
2534 C C   . SER A 146 ? 0.33114 0.31085 0.29894 -0.02950 0.06976  -0.00776 143 SER A C   
2535 O O   . SER A 146 ? 0.33694 0.28866 0.26056 -0.10408 0.04379  0.01629  143 SER A O   
2550 N N   . ASP A 147 ? 0.47526 0.46097 0.44463 -0.03689 0.07843  0.00149  144 ASP A N   
2551 C CA  . ASP A 147 ? 0.62361 0.65171 0.60103 -0.01216 0.08289  0.00637  144 ASP A CA  
2552 C C   . ASP A 147 ? 0.72624 0.80252 0.70151 -0.00956 0.11270  0.00658  144 ASP A C   
2553 O O   . ASP A 147 ? 0.76587 0.84358 0.73415 -0.00809 0.12365  0.00899  144 ASP A O   
2554 C CB  . ASP A 147 ? 0.65802 0.67782 0.63891 -0.00540 0.06460  0.00359  144 ASP A CB  
2555 C CG  . ASP A 147 ? 0.67724 0.69969 0.66190 -0.00426 0.04191  -0.00449 144 ASP A CG  
2556 O OD1 . ASP A 147 ? 0.69121 0.71612 0.66964 -0.00081 0.03692  -0.01150 144 ASP A OD1 
2557 O OD2 . ASP A 147 ? 0.68012 0.69541 0.66225 -0.01084 0.03857  0.00163  144 ASP A OD2 
2558 O OXT . ASP A 147 ? 0.76495 0.86818 0.75022 -0.00402 0.13906  0.00505  144 ASP A OXT 
2563 N N   . MET B 3   ? 0.83101 0.85287 0.83392 -0.00255 0.00711  0.00544  0   MET B N   
2564 C CA  . MET B 3   ? 0.83060 0.84636 0.82485 -0.00177 0.01493  0.00327  0   MET B CA  
2565 C C   . MET B 3   ? 0.73353 0.71075 0.73582 -0.00698 -0.02060 0.00063  0   MET B C   
2566 O O   . MET B 3   ? 0.73103 0.70381 0.73163 -0.01024 -0.02653 0.00413  0   MET B O   
2567 C CB  . MET B 3   ? 0.92030 0.96792 0.90646 0.00364  0.05678  -0.00059 0   MET B CB  
2568 C CG  . MET B 3   ? 1.00029 1.07508 0.99010 0.00494  0.07493  0.00143  0   MET B CG  
2569 S SD  . MET B 3   ? 1.06511 1.15938 1.03604 0.00613  0.09672  0.00819  0   MET B SD  
2570 C CE  . MET B 3   ? 1.08796 1.19333 1.06471 0.00486  0.11955  0.00350  0   MET B CE  
2580 N N   . GLY B 4   ? 0.64389 0.58738 0.64425 -0.01617 -0.03853 -0.00904 1   GLY B N   
2581 C CA  . GLY B 4   ? 0.56589 0.47132 0.56783 -0.00864 -0.05729 -0.01841 1   GLY B CA  
2582 C C   . GLY B 4   ? 0.49972 0.40412 0.49927 0.00448  -0.06563 -0.03673 1   GLY B C   
2583 O O   . GLY B 4   ? 0.45308 0.31232 0.46641 -0.00104 -0.10201 -0.08330 1   GLY B O   
2587 N N   . SER B 5   ? 0.46619 0.40049 0.46562 0.01231  -0.04030 -0.02820 2   SER B N   
2588 C CA  . SER B 5   ? 0.43593 0.39827 0.44545 0.01568  0.01410  -0.00473 2   SER B CA  
2589 C C   . SER B 5   ? 0.36673 0.32478 0.38706 0.01396  -0.00185 -0.00631 2   SER B C   
2590 O O   . SER B 5   ? 0.36057 0.33517 0.38826 0.00375  -0.01023 -0.02572 2   SER B O   
2591 C CB  . SER B 5   ? 0.47315 0.50934 0.47875 0.00923  0.06062  0.00059  2   SER B CB  
2592 O OG  . SER B 5   ? 0.50635 0.56067 0.50489 0.01112  0.07178  0.01023  2   SER B OG  
2598 N N   . GLY B 6   ? 0.29755 0.23962 0.33138 0.01067  -0.03096 0.00144  3   GLY B N   
2599 C CA  . GLY B 6   ? 0.25762 0.17315 0.28829 0.00476  -0.04728 0.00380  3   GLY B CA  
2600 C C   . GLY B 6   ? 0.24815 0.19786 0.27097 -0.03768 -0.06347 -0.02433 3   GLY B C   
2601 O O   . GLY B 6   ? 0.26440 0.21479 0.30269 -0.05918 -0.06974 -0.04100 3   GLY B O   
2947 N N   . LEU B 17  ? 0.14709 0.16347 0.14833 -0.04705 0.02484  0.01148  14  LEU B N   
2948 C CA  . LEU B 17  ? 0.14229 0.18208 0.13423 -0.06973 0.00490  0.02708  14  LEU B CA  
2949 C C   . LEU B 17  ? 0.16133 0.20167 0.14446 -0.05098 -0.01824 0.00678  14  LEU B C   
2950 O O   . LEU B 17  ? 0.18750 0.20939 0.14992 -0.04419 -0.03985 -0.02447 14  LEU B O   
2951 C CB  . LEU B 17  ? 0.16882 0.23282 0.12033 -0.04258 0.02869  0.02139  14  LEU B CB  
2952 C CG  . LEU B 17  ? 0.16550 0.23604 0.13510 -0.03719 0.02101  0.00454  14  LEU B CG  
2953 C CD1 . LEU B 17  ? 0.19258 0.27306 0.15579 -0.04421 0.05322  0.01138  14  LEU B CD1 
2954 C CD2 . LEU B 17  ? 0.18082 0.26852 0.14191 -0.02393 0.02676  -0.01314 14  LEU B CD2 
2967 N N   . VAL B 18  ? 0.18697 0.21915 0.15809 -0.01188 -0.04112 0.00375  15  VAL B N   
2970 C C   . VAL B 18  ? 0.18997 0.16717 0.16091 -0.04681 0.00727  -0.03027 15  VAL B C   
2971 O O   . VAL B 18  ? 0.14931 0.16388 0.13732 -0.00368 0.01011  -0.02683 15  VAL B O   
2996 N N   . SER B 19  ? 0.21810 0.19479 0.13769 -0.05876 0.03058  -0.04297 16  SER B N   
2997 C CA  . SER B 19  ? 0.23013 0.22015 0.16980 -0.03899 0.03101  -0.00355 16  SER B CA  
2998 C C   . SER B 19  ? 0.25930 0.23301 0.21086 -0.01992 0.04626  0.05229  16  SER B C   
2999 O O   . SER B 19  ? 0.30306 0.29387 0.23766 0.01423  0.06485  0.02991  16  SER B O   
3000 C CB  . SER B 19  ? 0.22759 0.25534 0.18689 -0.01430 0.02287  -0.02203 16  SER B CB  
3001 O OG  . SER B 19  ? 0.25959 0.32083 0.22624 -0.00582 -0.01219 -0.04422 16  SER B OG  
3007 N N   . LYS B 20  ? 0.27944 0.26250 0.24309 -0.02527 0.05705  0.04267  17  LYS B N   
3008 C CA  . LYS B 20  ? 0.31990 0.33789 0.30050 -0.01138 0.05409  0.03495  17  LYS B CA  
3009 C C   . LYS B 20  ? 0.36980 0.38202 0.35329 -0.00504 0.04731  -0.01136 17  LYS B C   
3010 O O   . LYS B 20  ? 0.39503 0.44328 0.39904 -0.00369 0.05519  -0.01720 17  LYS B O   
3011 C CB  . LYS B 20  ? 0.32082 0.34504 0.31063 -0.02146 0.04004  0.03089  17  LYS B CB  
3012 C CG  . LYS B 20  ? 0.30658 0.33700 0.29764 -0.00911 0.02236  0.01862  17  LYS B CG  
3013 C CD  . LYS B 20  ? 0.28864 0.28772 0.26671 -0.02617 0.04128  0.03833  17  LYS B CD  
3014 C CE  . LYS B 20  ? 0.26972 0.29674 0.24699 -0.01380 0.06203  0.02781  17  LYS B CE  
3015 N NZ  . LYS B 20  ? 0.25630 0.23537 0.21848 -0.02749 0.06031  0.07336  17  LYS B NZ  
3029 N N   . SER B 21  ? 0.39980 0.40763 0.35581 -0.02760 0.03941  -0.00595 18  SER B N   
3030 C CA  . SER B 21  ? 0.41618 0.43155 0.36466 -0.02416 0.03498  -0.01190 18  SER B CA  
3031 C C   . SER B 21  ? 0.41112 0.40400 0.33741 -0.02511 0.01879  -0.00201 18  SER B C   
3032 O O   . SER B 21  ? 0.42861 0.41972 0.34857 -0.03614 0.01649  -0.01726 18  SER B O   
3033 C CB  . SER B 21  ? 0.42304 0.46952 0.38819 -0.01974 0.04496  0.00276  18  SER B CB  
3034 O OG  . SER B 21  ? 0.44139 0.50932 0.40622 -0.02363 0.05398  0.01379  18  SER B OG  
3040 N N   . GLY B 22  ? 0.37721 0.33040 0.28789 -0.04213 0.00529  0.00435  19  GLY B N   
3041 C CA  . GLY B 22  ? 0.33206 0.29383 0.24747 -0.03927 0.00116  -0.00172 19  GLY B CA  
3042 C C   . GLY B 22  ? 0.28504 0.26260 0.21324 -0.04762 -0.01545 -0.02512 19  GLY B C   
3043 O O   . GLY B 22  ? 0.28654 0.27352 0.22126 -0.04339 -0.00746 -0.01914 19  GLY B O   
3047 N N   . THR B 23  ? 0.24923 0.25378 0.17754 -0.04280 -0.02692 -0.03061 20  THR B N   
3048 C CA  . THR B 23  ? 0.22371 0.23727 0.16689 -0.03505 -0.03506 -0.00790 20  THR B CA  
3049 C C   . THR B 23  ? 0.19794 0.26079 0.18473 -0.03420 -0.03254 0.00235  20  THR B C   
3050 O O   . THR B 23  ? 0.18873 0.32776 0.21078 -0.03133 -0.04227 0.00693  20  THR B O   
3051 C CB  . THR B 23  ? 0.25528 0.26037 0.18517 -0.04307 -0.02299 0.02656  20  THR B CB  
3052 O OG1 . THR B 23  ? 0.29457 0.34705 0.20419 -0.02746 -0.01420 0.02193  20  THR B OG1 
3053 C CG2 . THR B 23  ? 0.24364 0.24531 0.20494 -0.04374 0.01057  0.01443  20  THR B CG2 
3061 N N   . VAL B 24  ? 0.19129 0.20690 0.19081 -0.02362 -0.02582 -0.00651 21  VAL B N   
3062 C CA  . VAL B 24  ? 0.19759 0.24130 0.19181 0.00377  0.00371  0.01960  21  VAL B CA  
3063 C C   . VAL B 24  ? 0.19841 0.23321 0.19116 0.00797  0.02102  0.00420  21  VAL B C   
3064 O O   . VAL B 24  ? 0.17316 0.23867 0.18530 -0.00860 -0.00221 0.00712  21  VAL B O   
3065 C CB  . VAL B 24  ? 0.20696 0.25364 0.18909 -0.01323 0.02770  0.01209  21  VAL B CB  
3066 C CG1 . VAL B 24  ? 0.22704 0.30006 0.19706 -0.03786 0.02886  0.02715  21  VAL B CG1 
3067 C CG2 . VAL B 24  ? 0.23068 0.28607 0.17716 0.01033  0.05675  -0.00962 21  VAL B CG2 
3077 N N   . SER B 25  ? 0.23242 0.29302 0.20012 -0.00110 0.04099  0.01359  22  SER B N   
3078 C CA  . SER B 25  ? 0.28181 0.30937 0.22158 0.01434  0.04305  0.02155  22  SER B CA  
3079 C C   . SER B 25  ? 0.29959 0.33095 0.23452 0.00036  0.03423  0.01608  22  SER B C   
3080 O O   . SER B 25  ? 0.28527 0.30055 0.22427 0.03067  0.04876  -0.00365 22  SER B O   
3081 C CB  . SER B 25  ? 0.30964 0.35113 0.22897 0.00358  0.04657  0.01880  22  SER B CB  
3082 O OG  . SER B 25  ? 0.35122 0.40400 0.26670 0.02479  0.05273  -0.00024 22  SER B OG  
3088 N N   . PRO B 26  ? 0.33531 0.34655 0.28379 -0.02004 0.02894  0.02422  23  PRO B N   
3089 C CA  . PRO B 26  ? 0.35411 0.35394 0.30737 -0.02870 0.03023  0.02608  23  PRO B CA  
3090 C C   . PRO B 26  ? 0.37132 0.34057 0.32741 -0.01498 0.03313  0.02167  23  PRO B C   
3091 O O   . PRO B 26  ? 0.35886 0.26811 0.31621 -0.04678 0.06110  0.05698  23  PRO B O   
3092 C CB  . PRO B 26  ? 0.35191 0.35612 0.31054 -0.03274 0.01924  0.01677  23  PRO B CB  
3093 C CG  . PRO B 26  ? 0.34620 0.36965 0.31016 -0.03835 0.02691  0.01386  23  PRO B CG  
3094 C CD  . PRO B 26  ? 0.33991 0.37593 0.29569 -0.03275 0.02915  0.00913  23  PRO B CD  
3102 N N   . ILE B 27  ? 0.40432 0.37491 0.36151 0.01259  0.03638  0.03455  24  ILE B N   
3103 C CA  . ILE B 27  ? 0.42892 0.43641 0.37970 0.01459  0.03545  0.03030  24  ILE B CA  
3104 C C   . ILE B 27  ? 0.39624 0.39874 0.34256 0.03446  0.00514  0.03227  24  ILE B C   
3105 O O   . ILE B 27  ? 0.39862 0.42051 0.33835 0.04085  -0.00796 0.07128  24  ILE B O   
3106 C CB  . ILE B 27  ? 0.48184 0.51906 0.44105 0.01148  0.04760  0.02107  24  ILE B CB  
3107 C CG1 . ILE B 27  ? 0.51209 0.57926 0.47961 0.00631  0.05790  0.01542  24  ILE B CG1 
3108 C CG2 . ILE B 27  ? 0.50029 0.54756 0.46529 0.01703  0.05050  0.01781  24  ILE B CG2 
3109 C CD1 . ILE B 27  ? 0.52658 0.60448 0.49893 0.00311  0.05509  0.01104  24  ILE B CD1 
3121 N N   . SER B 28  ? 0.35695 0.35951 0.32105 0.05647  -0.00173 0.03273  25  SER B N   
3124 C C   . SER B 28  ? 0.30985 0.31624 0.27436 0.04453  -0.02736 -0.05958 25  SER B C   
3125 O O   . SER B 28  ? 0.30333 0.30464 0.21589 0.03962  -0.05354 -0.11393 25  SER B O   
3140 N N   . LEU B 29  ? 0.27290 0.26386 0.22968 0.04549  -0.00832 -0.04788 26  LEU B N   
3141 C CA  . LEU B 29  ? 0.25162 0.21646 0.19011 0.03081  0.00968  -0.00904 26  LEU B CA  
3142 C C   . LEU B 29  ? 0.23618 0.18755 0.17442 0.03658  -0.02495 0.00885  26  LEU B C   
3143 O O   . LEU B 29  ? 0.19491 0.16921 0.16210 0.00365  -0.03904 0.00200  26  LEU B O   
3144 C CB  . LEU B 29  ? 0.24933 0.23463 0.16991 0.03103  0.03503  0.01025  26  LEU B CB  
3145 C CG  . LEU B 29  ? 0.25588 0.27076 0.20648 0.00856  0.02600  0.00620  26  LEU B CG  
3146 C CD1 . LEU B 29  ? 0.28506 0.34520 0.25132 -0.00938 0.03109  0.02932  26  LEU B CD1 
3147 C CD2 . LEU B 29  ? 0.25229 0.22968 0.20407 0.04273  0.00011  0.03414  26  LEU B CD2 
3159 N N   . ALA B 30  ? 0.25226 0.23147 0.16376 0.04349  -0.03565 0.03433  27  ALA B N   
3160 C CA  . ALA B 30  ? 0.23516 0.18074 0.18370 0.01350  -0.06053 0.00681  27  ALA B CA  
3161 C C   . ALA B 30  ? 0.23231 0.19515 0.20458 0.01768  -0.03350 0.01678  27  ALA B C   
3162 O O   . ALA B 30  ? 0.21984 0.23862 0.22568 -0.00738 -0.03282 0.04878  27  ALA B O   
3163 C CB  . ALA B 30  ? 0.25537 0.23175 0.21415 0.03543  -0.06064 0.01649  27  ALA B CB  
3169 N N   . GLY B 31  ? 0.21134 0.20320 0.17180 0.01621  -0.05168 0.00446  28  GLY B N   
3170 C CA  . GLY B 31  ? 0.20359 0.17528 0.20366 0.02639  -0.03171 0.05225  28  GLY B CA  
3171 C C   . GLY B 31  ? 0.17640 0.13852 0.19185 0.04620  -0.03249 0.05434  28  GLY B C   
3172 O O   . GLY B 31  ? 0.18337 0.21831 0.21219 0.04673  -0.00601 0.03284  28  GLY B O   
3176 N N   . LYS B 32  ? 0.15420 0.18838 0.15301 0.05201  -0.04036 0.04298  29  LYS B N   
3179 C C   . LYS B 32  ? 0.14607 0.14690 0.15945 -0.02610 -0.01935 0.01124  29  LYS B C   
3180 O O   . LYS B 32  ? 0.17042 0.15202 0.18076 -0.01615 -0.02777 0.00701  29  LYS B O   
3217 N N   . THR B 33  ? 0.12483 0.13286 0.14774 -0.00921 -0.00275 0.03250  30  THR B N   
3218 C CA  . THR B 33  ? 0.10162 0.11329 0.16490 0.02300  -0.00991 0.01914  30  THR B CA  
3219 C C   . THR B 33  ? 0.11833 0.10527 0.16763 -0.00060 0.00600  -0.00059 30  THR B C   
3220 O O   . THR B 33  ? 0.11348 0.13036 0.18579 -0.00876 -0.01291 -0.00541 30  THR B O   
3221 C CB  . THR B 33  ? 0.09478 0.14146 0.16996 0.03194  -0.03073 0.02013  30  THR B CB  
3222 O OG1 . THR B 33  ? 0.11980 0.17035 0.18276 0.03867  -0.02420 0.00401  30  THR B OG1 
3223 C CG2 . THR B 33  ? 0.11096 0.15092 0.19188 -0.00171 -0.01963 0.02315  30  THR B CG2 
3231 N N   . VAL B 34  ? 0.12669 0.10394 0.18174 -0.01236 0.01482  -0.02807 31  VAL B N   
3232 C CA  . VAL B 34  ? 0.11100 0.11547 0.15681 0.01357  0.02270  -0.00803 31  VAL B CA  
3233 C C   . VAL B 34  ? 0.10200 0.05786 0.14131 -0.00364 0.00996  -0.00993 31  VAL B C   
3234 O O   . VAL B 34  ? 0.11961 0.07024 0.17439 -0.01242 -0.00437 -0.00798 31  VAL B O   
3235 C CB  . VAL B 34  ? 0.14171 0.12503 0.14421 0.04613  0.03043  0.03015  31  VAL B CB  
3236 C CG1 . VAL B 34  ? 0.16235 0.18483 0.13799 0.02558  0.05745  0.03210  31  VAL B CG1 
3237 C CG2 . VAL B 34  ? 0.16090 0.15196 0.15073 0.03957  0.00243  0.01414  31  VAL B CG2 
3247 N N   . PHE B 35  ? 0.07771 0.08729 0.13890 0.02395  0.00282  -0.01824 32  PHE B N   
3248 C CA  A PHE B 35  ? 0.09735 0.11355 0.13765 0.01250  0.00650  0.00160  32  PHE B CA  
3249 C CA  B PHE B 35  ? 0.09735 0.11355 0.13765 0.01250  0.00650  0.00160  32  PHE B CA  
3250 C C   . PHE B 35  ? 0.09366 0.11371 0.12232 -0.00479 0.01131  -0.02036 32  PHE B C   
3251 O O   . PHE B 35  ? 0.10369 0.14561 0.14537 -0.01197 -0.00398 -0.06340 32  PHE B O   
3252 C CB  A PHE B 35  ? 0.13885 0.13645 0.14765 -0.00480 0.02180  0.02130  32  PHE B CB  
3253 C CB  B PHE B 35  ? 0.13885 0.13645 0.14765 -0.00480 0.02180  0.02130  32  PHE B CB  
3254 C CG  A PHE B 35  ? 0.16875 0.20805 0.16435 -0.00030 0.03210  0.02130  32  PHE B CG  
3255 C CG  B PHE B 35  ? 0.16875 0.20805 0.16435 -0.00030 0.03210  0.02130  32  PHE B CG  
3256 C CD1 A PHE B 35  ? 0.18935 0.24135 0.18775 0.00730  0.04370  0.02850  32  PHE B CD1 
3257 C CD1 B PHE B 35  ? 0.18935 0.24135 0.18775 0.00730  0.04370  0.02850  32  PHE B CD1 
3258 C CD2 A PHE B 35  ? 0.18655 0.23035 0.18315 0.01120  0.04540  -0.01470 32  PHE B CD2 
3259 C CD2 B PHE B 35  ? 0.18655 0.23035 0.18315 0.01120  0.04540  -0.01470 32  PHE B CD2 
3260 C CE1 A PHE B 35  ? 0.20315 0.24865 0.20075 0.01320  0.03790  0.01560  32  PHE B CE1 
3261 C CE1 B PHE B 35  ? 0.20315 0.24865 0.20075 0.01320  0.03790  0.01560  32  PHE B CE1 
3262 C CE2 A PHE B 35  ? 0.18735 0.25755 0.19355 0.00670  0.04480  -0.00020 32  PHE B CE2 
3263 C CE2 B PHE B 35  ? 0.18735 0.25755 0.19355 0.00670  0.04480  -0.00020 32  PHE B CE2 
3264 C CZ  A PHE B 35  ? 0.19615 0.26855 0.19605 0.00860  0.04590  0.00790  32  PHE B CZ  
3265 C CZ  B PHE B 35  ? 0.19615 0.26855 0.19605 0.00860  0.04590  0.00790  32  PHE B CZ  
3282 N N   . PHE B 36  ? 0.11434 0.10974 0.10780 -0.00034 0.03225  -0.00168 33  PHE B N   
3283 C CA  . PHE B 36  ? 0.13224 0.09262 0.11490 -0.00738 0.00353  0.01308  33  PHE B CA  
3284 C C   . PHE B 36  ? 0.13684 0.09221 0.11395 -0.02117 0.02288  -0.02713 33  PHE B C   
3285 O O   . PHE B 36  ? 0.15624 0.12234 0.10366 0.01305  0.00267  -0.02697 33  PHE B O   
3286 C CB  . PHE B 36  ? 0.12978 0.14718 0.12907 -0.02472 0.01646  0.01000  33  PHE B CB  
3287 C CG  . PHE B 36  ? 0.13475 0.13697 0.13634 0.01543  0.01408  0.00197  33  PHE B CG  
3288 C CD1 . PHE B 36  ? 0.15179 0.14207 0.14198 -0.01412 0.02867  -0.00551 33  PHE B CD1 
3289 C CD2 . PHE B 36  ? 0.18693 0.17050 0.15095 0.01408  0.00670  0.03087  33  PHE B CD2 
3290 C CE1 . PHE B 36  ? 0.16919 0.13890 0.14021 0.01233  0.00055  0.01782  33  PHE B CE1 
3291 C CE2 . PHE B 36  ? 0.21633 0.16802 0.16348 0.02580  0.00493  0.03482  33  PHE B CE2 
3292 C CZ  . PHE B 36  ? 0.20936 0.17759 0.15011 -0.00281 0.00922  0.04478  33  PHE B CZ  
3302 N N   . TYR B 37  ? 0.12161 0.10034 0.11547 -0.00608 0.00161  -0.06189 34  TYR B N   
3303 C CA  . TYR B 37  ? 0.11633 0.10295 0.10229 0.00540  -0.03100 -0.02123 34  TYR B CA  
3304 C C   . TYR B 37  ? 0.09169 0.13992 0.09598 -0.01168 -0.03294 -0.01016 34  TYR B C   
3305 O O   . TYR B 37  ? 0.08928 0.12289 0.09134 -0.00473 0.00196  -0.00454 34  TYR B O   
3306 C CB  . TYR B 37  ? 0.11320 0.12228 0.09792 -0.00418 -0.02974 -0.01600 34  TYR B CB  
3307 C CG  . TYR B 37  ? 0.11280 0.09159 0.09763 0.00261  -0.01871 -0.00018 34  TYR B CG  
3308 C CD1 . TYR B 37  ? 0.15474 0.11401 0.10564 0.00870  -0.01738 -0.01701 34  TYR B CD1 
3309 C CD2 . TYR B 37  ? 0.11384 0.10026 0.10151 -0.01234 0.00893  -0.02649 34  TYR B CD2 
3310 C CE1 . TYR B 37  ? 0.14908 0.07668 0.09976 0.00514  0.00230  -0.02827 34  TYR B CE1 
3311 C CE2 . TYR B 37  ? 0.11631 0.08613 0.10340 -0.02480 -0.02311 -0.00530 34  TYR B CE2 
3312 C CZ  . TYR B 37  ? 0.14694 0.07019 0.09440 -0.00914 -0.00782 0.01564  34  TYR B CZ  
3313 O OH  . TYR B 37  ? 0.16810 0.08756 0.11162 0.00580  0.00287  0.00834  34  TYR B OH  
3323 N N   . PHE B 38  ? 0.10250 0.08296 0.09697 -0.00030 -0.03081 0.00929  35  PHE B N   
3324 C CA  . PHE B 38  ? 0.09804 0.05883 0.10356 0.00949  -0.02390 0.00323  35  PHE B CA  
3325 C C   . PHE B 38  ? 0.10045 0.10551 0.10262 -0.01006 -0.00996 -0.00158 35  PHE B C   
3326 O O   . PHE B 38  ? 0.10227 0.13269 0.09718 -0.00720 0.00874  -0.00398 35  PHE B O   
3327 C CB  . PHE B 38  ? 0.08411 0.08961 0.10624 -0.01565 -0.00206 -0.02668 35  PHE B CB  
3328 C CG  . PHE B 38  ? 0.09279 0.09773 0.10536 0.00815  -0.02378 -0.00014 35  PHE B CG  
3329 C CD1 . PHE B 38  ? 0.12187 0.09595 0.12481 -0.00669 -0.01300 0.01414  35  PHE B CD1 
3330 C CD2 . PHE B 38  ? 0.10051 0.10719 0.10656 0.00407  -0.02328 0.01048  35  PHE B CD2 
3331 C CE1 . PHE B 38  ? 0.14362 0.07944 0.14876 0.01642  -0.00656 -0.02484 35  PHE B CE1 
3332 C CE2 . PHE B 38  ? 0.11968 0.12749 0.12183 0.00104  -0.00041 -0.00354 35  PHE B CE2 
3333 C CZ  . PHE B 38  ? 0.15349 0.09451 0.13336 0.02833  0.00090  0.00295  35  PHE B CZ  
3343 N N   . SER B 39  ? 0.10400 0.12188 0.09815 -0.00727 0.00361  -0.00147 36  SER B N   
3344 C CA  . SER B 39  ? 0.12176 0.09174 0.09780 -0.00229 -0.01040 -0.00088 36  SER B CA  
3345 C C   . SER B 39  ? 0.12602 0.06321 0.10269 -0.01485 -0.00849 -0.01141 36  SER B C   
3346 O O   . SER B 39  ? 0.14722 0.11806 0.10741 0.02802  0.03284  0.02183  36  SER B O   
3347 C CB  . SER B 39  ? 0.12894 0.09859 0.11767 -0.02289 -0.01002 0.01117  36  SER B CB  
3348 O OG  . SER B 39  ? 0.17107 0.09489 0.11669 -0.00832 0.00367  0.00667  36  SER B OG  
3354 N N   . ALA B 40  ? 0.11451 0.10222 0.09825 0.02556  0.00429  0.00890  37  ALA B N   
3355 C CA  . ALA B 40  ? 0.10644 0.07140 0.13190 0.00726  -0.00523 -0.00573 37  ALA B CA  
3356 C C   . ALA B 40  ? 0.09461 0.04855 0.12632 0.02399  -0.01888 -0.00994 37  ALA B C   
3357 O O   . ALA B 40  ? 0.09449 0.11535 0.13010 0.00903  0.00151  -0.00438 37  ALA B O   
3358 C CB  . ALA B 40  ? 0.10076 0.11652 0.18098 -0.02302 0.01581  -0.01023 37  ALA B CB  
3364 N N   . SER B 41  ? 0.12513 0.05204 0.13970 0.01295  0.00694  -0.00727 38  SER B N   
3365 C CA  . SER B 41  ? 0.12844 0.06281 0.16169 0.04095  0.00807  -0.00101 38  SER B CA  
3366 C C   . SER B 41  ? 0.15171 0.05897 0.16269 0.01461  -0.00632 -0.01351 38  SER B C   
3367 O O   . SER B 41  ? 0.21072 0.09924 0.17464 0.02093  0.00969  0.00143  38  SER B O   
3368 C CB  . SER B 41  ? 0.14075 0.06707 0.17955 0.00001  0.02404  0.01188  38  SER B CB  
3369 O OG  . SER B 41  ? 0.16561 0.12106 0.17321 -0.00713 0.03061  -0.02441 38  SER B OG  
3375 N N   . TRP B 42  ? 0.13107 0.08257 0.15758 0.02348  -0.02247 -0.00232 39  TRP B N   
3376 C CA  . TRP B 42  ? 0.15124 0.13330 0.15009 0.06559  0.00716  -0.00473 39  TRP B CA  
3377 C C   . TRP B 42  ? 0.15476 0.14902 0.13253 0.06721  -0.00916 -0.00338 39  TRP B C   
3378 O O   . TRP B 42  ? 0.19603 0.22481 0.13099 0.06112  0.00934  -0.00060 39  TRP B O   
3379 C CB  . TRP B 42  ? 0.13589 0.17313 0.14635 0.04476  0.00809  -0.03053 39  TRP B CB  
3380 C CG  . TRP B 42  ? 0.11378 0.21994 0.13310 0.02372  -0.00592 -0.02561 39  TRP B CG  
3381 C CD1 . TRP B 42  ? 0.14757 0.19966 0.14595 -0.00732 0.03074  -0.04085 39  TRP B CD1 
3382 C CD2 . TRP B 42  ? 0.11939 0.20654 0.14176 0.00521  -0.00102 0.01476  39  TRP B CD2 
3383 N NE1 . TRP B 42  ? 0.14976 0.23416 0.15888 -0.02250 0.02099  -0.03938 39  TRP B NE1 
3384 C CE2 . TRP B 42  ? 0.13487 0.21269 0.15288 -0.01203 -0.00109 0.00316  39  TRP B CE2 
3385 C CE3 . TRP B 42  ? 0.14533 0.19105 0.14101 0.03022  0.02888  0.01138  39  TRP B CE3 
3386 C CZ2 . TRP B 42  ? 0.14497 0.22927 0.16200 -0.01047 -0.00173 0.00713  39  TRP B CZ2 
3387 C CZ3 . TRP B 42  ? 0.15751 0.17241 0.14273 0.02630  0.01425  0.02501  39  TRP B CZ3 
3388 C CH2 . TRP B 42  ? 0.13406 0.16931 0.16067 0.00706  0.00543  0.00310  39  TRP B CH2 
3399 N N   . CYS B 43  ? 0.15442 0.10600 0.15557 0.05052  0.01225  0.00185  40  CYS B N   
3400 C CA  . CYS B 43  ? 0.12974 0.09331 0.16413 0.01746  0.00751  -0.01146 40  CYS B CA  
3401 C C   . CYS B 43  ? 0.11821 0.14837 0.16438 0.00207  0.00944  0.01452  40  CYS B C   
3402 O O   . CYS B 43  ? 0.11121 0.13265 0.17436 0.01053  0.03295  -0.00471 40  CYS B O   
3403 C CB  . CYS B 43  ? 0.16829 0.09631 0.18371 0.02198  0.03053  -0.00281 40  CYS B CB  
3404 S SG  . CYS B 43  ? 0.22972 0.14224 0.20381 -0.01257 0.08914  -0.01839 40  CYS B SG  
3410 N N   . PRO B 44  ? 0.11006 0.13393 0.16564 0.02543  -0.03372 0.03080  41  PRO B N   
3411 C CA  . PRO B 44  ? 0.13690 0.11953 0.18418 0.03931  -0.02912 0.05160  41  PRO B CA  
3412 C C   . PRO B 44  ? 0.14106 0.12243 0.15584 -0.00570 -0.00935 0.00955  41  PRO B C   
3413 O O   . PRO B 44  ? 0.14671 0.13134 0.15657 0.00168  0.00551  0.02895  41  PRO B O   
3414 C CB  . PRO B 44  ? 0.17182 0.20147 0.19791 0.01539  -0.02532 0.04211  41  PRO B CB  
3415 C CG  . PRO B 44  ? 0.18697 0.24143 0.18197 -0.00330 -0.01978 0.02667  41  PRO B CG  
3416 C CD  . PRO B 44  ? 0.13112 0.16244 0.15978 -0.00552 -0.04015 0.03403  41  PRO B CD  
3424 N N   . PRO B 45  ? 0.14016 0.13688 0.14284 -0.00851 -0.02653 0.01835  42  PRO B N   
3427 C C   . PRO B 45  ? 0.13747 0.13158 0.14035 0.03650  0.01201  0.03515  42  PRO B C   
3428 O O   . PRO B 45  ? 0.14026 0.17336 0.13378 0.01681  0.04975  0.03115  42  PRO B O   
3449 N N   . CYS B 46  ? 0.12787 0.10572 0.13396 0.00466  0.01398  0.01933  43  CYS B N   
3450 C CA  . CYS B 46  ? 0.13535 0.14149 0.12726 0.01950  0.01395  0.04081  43  CYS B CA  
3451 C C   . CYS B 46  ? 0.09629 0.12012 0.12215 0.01762  0.01178  0.04630  43  CYS B C   
3452 O O   . CYS B 46  ? 0.09884 0.15129 0.11989 0.03581  -0.00148 0.02940  43  CYS B O   
3453 C CB  . CYS B 46  ? 0.16414 0.11928 0.12186 -0.02791 0.01254  -0.00558 43  CYS B CB  
3454 S SG  . CYS B 46  ? 0.20937 0.11968 0.16667 -0.01785 0.06732  -0.00830 43  CYS B SG  
3460 N N   . ARG B 47  ? 0.11213 0.11953 0.13649 -0.01721 -0.02597 0.00748  44  ARG B N   
3461 C CA  . ARG B 47  ? 0.13776 0.12867 0.14570 -0.03356 -0.00745 0.01365  44  ARG B CA  
3462 C C   . ARG B 47  ? 0.11727 0.07628 0.15779 -0.00485 -0.00900 0.00382  44  ARG B C   
3463 O O   . ARG B 47  ? 0.09315 0.14861 0.19338 -0.01903 -0.01421 -0.01400 44  ARG B O   
3464 C CB  . ARG B 47  ? 0.15825 0.10182 0.15680 0.00364  0.00314  0.02569  44  ARG B CB  
3465 C CG  . ARG B 47  ? 0.17066 0.15919 0.18037 0.01279  0.00518  0.00671  44  ARG B CG  
3466 C CD  . ARG B 47  ? 0.23951 0.26465 0.22717 0.04119  0.02513  -0.00515 44  ARG B CD  
3467 N NE  . ARG B 47  ? 0.27609 0.31295 0.27403 0.03469  0.03772  -0.01679 44  ARG B NE  
3468 C CZ  . ARG B 47  ? 0.29810 0.35883 0.30602 0.03545  0.04754  -0.00199 44  ARG B CZ  
3469 N NH1 . ARG B 47  ? 0.30857 0.41010 0.32887 -0.01524 0.03946  0.02706  44  ARG B NH1 
3470 N NH2 . ARG B 47  ? 0.29633 0.35555 0.31093 0.04612  0.04992  -0.01764 44  ARG B NH2 
3484 N N   . GLY B 48  ? 0.14310 0.10380 0.15331 0.02349  0.00166  0.01287  45  GLY B N   
3485 C CA  . GLY B 48  ? 0.15186 0.16525 0.14802 0.00743  0.00965  0.03443  45  GLY B CA  
3486 C C   . GLY B 48  ? 0.14059 0.18098 0.16693 -0.02120 0.01491  0.03222  45  GLY B C   
3487 O O   . GLY B 48  ? 0.14982 0.19268 0.22462 -0.03989 0.02613  0.01827  45  GLY B O   
3491 N N   . PHE B 49  ? 0.13216 0.13793 0.12083 -0.00745 0.02932  0.00667  46  PHE B N   
3492 C CA  . PHE B 49  ? 0.11491 0.09346 0.12700 -0.01424 0.03051  -0.02115 46  PHE B CA  
3493 C C   . PHE B 49  ? 0.09720 0.12679 0.12495 0.00407  0.01918  0.00385  46  PHE B C   
3494 O O   . PHE B 49  ? 0.10765 0.12950 0.12701 0.00646  0.03384  -0.00585 46  PHE B O   
3495 C CB  . PHE B 49  ? 0.09905 0.12379 0.11130 0.02161  0.02001  -0.02767 46  PHE B CB  
3496 C CG  . PHE B 49  ? 0.11910 0.07815 0.14916 0.01644  0.02109  0.01677  46  PHE B CG  
3497 C CD1 . PHE B 49  ? 0.13409 0.11802 0.15901 0.03349  0.04209  -0.00854 46  PHE B CD1 
3498 C CD2 . PHE B 49  ? 0.13202 0.09068 0.14823 -0.01706 0.01894  0.00674  46  PHE B CD2 
3499 C CE1 . PHE B 49  ? 0.14259 0.13604 0.14913 0.00974  0.01928  0.00277  46  PHE B CE1 
3500 C CE2 . PHE B 49  ? 0.15397 0.12771 0.13698 -0.00979 0.01013  -0.03084 46  PHE B CE2 
3501 C CZ  . PHE B 49  ? 0.14845 0.14136 0.13965 0.00662  -0.00580 -0.00919 46  PHE B CZ  
3511 N N   . THR B 50  ? 0.09753 0.12667 0.10978 0.01770  -0.00401 0.02957  47  THR B N   
3512 C CA  . THR B 50  ? 0.12661 0.08122 0.11962 0.00616  -0.00459 0.00617  47  THR B CA  
3513 C C   . THR B 50  ? 0.11080 0.08755 0.10739 0.01256  0.01108  0.00469  47  THR B C   
3514 O O   . THR B 50  ? 0.10986 0.11755 0.11561 0.01435  0.01458  0.00945  47  THR B O   
3515 C CB  . THR B 50  ? 0.14036 0.08687 0.13728 -0.01212 -0.01243 0.01955  47  THR B CB  
3516 O OG1 . THR B 50  ? 0.13600 0.10321 0.14241 -0.00547 0.01972  0.00975  47  THR B OG1 
3517 C CG2 . THR B 50  ? 0.14886 0.15161 0.12984 0.01055  0.00815  -0.00549 47  THR B CG2 
3525 N N   . PRO B 51  ? 0.11403 0.09965 0.13259 0.01745  -0.00044 -0.00142 48  PRO B N   
3526 C CA  . PRO B 51  ? 0.12668 0.08943 0.13918 -0.01977 0.00693  0.00022  48  PRO B CA  
3527 C C   . PRO B 51  ? 0.12020 0.10362 0.13923 -0.01807 0.01542  -0.00734 48  PRO B C   
3528 O O   . PRO B 51  ? 0.11051 0.13640 0.13955 -0.00750 0.00796  0.00509  48  PRO B O   
3529 C CB  . PRO B 51  ? 0.13258 0.12136 0.16637 -0.00129 -0.00978 0.04830  48  PRO B CB  
3530 C CG  . PRO B 51  ? 0.15670 0.11680 0.18327 0.00228  -0.01474 0.06581  48  PRO B CG  
3531 C CD  . PRO B 51  ? 0.12014 0.08019 0.15240 0.01974  -0.01257 0.01503  48  PRO B CD  
3539 N N   . THR B 52  ? 0.13803 0.10395 0.16405 -0.01355 0.02345  0.03324  49  THR B N   
3540 C CA  . THR B 52  ? 0.12888 0.08898 0.15514 0.00491  0.00506  -0.00624 49  THR B CA  
3541 C C   . THR B 52  ? 0.09339 0.11539 0.13373 0.01769  0.00486  -0.02120 49  THR B C   
3542 O O   . THR B 52  ? 0.10141 0.13527 0.13158 0.00410  0.02194  0.01288  49  THR B O   
3543 C CB  . THR B 52  ? 0.16200 0.11962 0.14968 0.01717  -0.00461 0.01733  49  THR B CB  
3544 O OG1 . THR B 52  ? 0.19737 0.17755 0.16103 0.01221  -0.00430 0.02138  49  THR B OG1 
3545 C CG2 . THR B 52  ? 0.15898 0.18805 0.14544 0.02324  -0.00399 -0.00741 49  THR B CG2 
3553 N N   . LEU B 53  ? 0.12020 0.10978 0.13281 0.00660  0.02862  0.00233  50  LEU B N   
3554 C CA  . LEU B 53  ? 0.14578 0.04444 0.14618 -0.01346 0.00635  -0.00530 50  LEU B CA  
3555 C C   . LEU B 53  ? 0.12658 0.08656 0.11646 0.00809  -0.00501 0.01719  50  LEU B C   
3556 O O   . LEU B 53  ? 0.11248 0.10032 0.11437 0.00376  -0.00749 0.00067  50  LEU B O   
3557 C CB  . LEU B 53  ? 0.14917 0.12124 0.15809 -0.01183 0.00454  -0.01000 50  LEU B CB  
3558 C CG  . LEU B 53  ? 0.12111 0.09527 0.13520 -0.01041 -0.00069 0.01259  50  LEU B CG  
3559 C CD1 . LEU B 53  ? 0.13671 0.12892 0.13246 0.04210  0.03176  0.02071  50  LEU B CD1 
3560 C CD2 . LEU B 53  ? 0.12723 0.10626 0.15167 -0.01910 0.00056  0.00761  50  LEU B CD2 
3572 N N   . VAL B 54  ? 0.12525 0.12088 0.13996 -0.00271 -0.00387 0.01104  51  VAL B N   
3573 C CA  . VAL B 54  ? 0.11511 0.07148 0.13816 -0.00760 0.00271  -0.03003 51  VAL B CA  
3574 C C   . VAL B 54  ? 0.12186 0.09019 0.13523 -0.01410 0.01207  -0.02786 51  VAL B C   
3575 O O   . VAL B 54  ? 0.12258 0.13133 0.13248 -0.00206 0.01963  -0.03796 51  VAL B O   
3576 C CB  . VAL B 54  ? 0.12471 0.09970 0.13537 -0.00604 0.00377  -0.00859 51  VAL B CB  
3577 C CG1 . VAL B 54  ? 0.13619 0.11931 0.14909 -0.00256 0.02717  0.01708  51  VAL B CG1 
3578 C CG2 . VAL B 54  ? 0.10656 0.09388 0.11543 -0.00749 -0.01062 0.00137  51  VAL B CG2 
3588 N N   . GLU B 55  ? 0.13190 0.12227 0.14783 -0.01105 0.01543  -0.01063 52  GLU B N   
3589 C CA  . GLU B 55  ? 0.14859 0.09259 0.16088 -0.03881 0.02752  0.00579  52  GLU B CA  
3590 C C   . GLU B 55  ? 0.13108 0.13801 0.14223 -0.00156 0.03267  0.01061  52  GLU B C   
3591 O O   . GLU B 55  ? 0.12806 0.17505 0.17514 -0.01160 0.04338  -0.03063 52  GLU B O   
3592 C CB  . GLU B 55  ? 0.17650 0.13317 0.20204 -0.03977 0.05496  0.00652  52  GLU B CB  
3593 C CG  . GLU B 55  ? 0.26596 0.29694 0.29350 -0.01647 0.10232  0.03615  52  GLU B CG  
3594 C CD  . GLU B 55  ? 0.34869 0.43281 0.36250 -0.00736 0.11471  0.04520  52  GLU B CD  
3595 O OE1 . GLU B 55  ? 0.40048 0.46860 0.38581 -0.02739 0.13232  0.05116  52  GLU B OE1 
3596 O OE2 . GLU B 55  ? 0.39377 0.47956 0.41036 0.00817  0.11455  0.05050  52  GLU B OE2 
3603 N N   . PHE B 56  ? 0.12464 0.10524 0.12479 -0.00409 0.01627  0.01793  53  PHE B N   
3604 C CA  . PHE B 56  ? 0.10067 0.11846 0.13413 0.01210  -0.00988 0.00522  53  PHE B CA  
3605 C C   . PHE B 56  ? 0.07650 0.14252 0.10669 0.03055  -0.02347 -0.01230 53  PHE B C   
3606 O O   . PHE B 56  ? 0.08939 0.15453 0.13755 0.04873  -0.03134 -0.03696 53  PHE B O   
3607 C CB  . PHE B 56  ? 0.10761 0.12683 0.13680 -0.01281 -0.00873 -0.01800 53  PHE B CB  
3608 C CG  . PHE B 56  ? 0.14228 0.12143 0.13224 0.00974  0.01783  -0.02399 53  PHE B CG  
3609 C CD1 . PHE B 56  ? 0.14905 0.13517 0.17589 0.00981  0.04782  -0.03267 53  PHE B CD1 
3610 C CD2 . PHE B 56  ? 0.16616 0.13090 0.13190 0.01304  0.01256  -0.03485 53  PHE B CD2 
3611 C CE1 . PHE B 56  ? 0.16511 0.14796 0.18841 0.03081  0.04945  -0.03885 53  PHE B CE1 
3612 C CE2 . PHE B 56  ? 0.18721 0.16916 0.14053 0.04123  0.01543  -0.00140 53  PHE B CE2 
3613 C CZ  . PHE B 56  ? 0.18011 0.14861 0.16906 0.05354  0.02147  -0.03235 53  PHE B CZ  
3623 N N   . TYR B 57  ? 0.10762 0.12795 0.11036 0.00927  0.01669  -0.00963 54  TYR B N   
3624 C CA  . TYR B 57  ? 0.13113 0.11822 0.13211 0.03478  0.00969  -0.00927 54  TYR B CA  
3625 C C   . TYR B 57  ? 0.12365 0.13295 0.13147 0.00702  0.00380  -0.00923 54  TYR B C   
3626 O O   . TYR B 57  ? 0.11116 0.16374 0.13126 0.02083  0.00130  0.00017  54  TYR B O   
3627 C CB  . TYR B 57  ? 0.13202 0.12998 0.14135 -0.00570 0.02715  0.01063  54  TYR B CB  
3628 C CG  . TYR B 57  ? 0.13073 0.10142 0.13200 -0.01415 0.03355  0.00152  54  TYR B CG  
3629 C CD1 . TYR B 57  ? 0.12652 0.16309 0.12877 -0.02813 0.02855  -0.00798 54  TYR B CD1 
3630 C CD2 . TYR B 57  ? 0.15614 0.13623 0.14208 -0.03697 0.04062  -0.01111 54  TYR B CD2 
3631 C CE1 . TYR B 57  ? 0.13632 0.12451 0.13416 0.00902  0.04127  0.01068  54  TYR B CE1 
3632 C CE2 . TYR B 57  ? 0.15739 0.15917 0.12916 -0.03819 0.04171  -0.02117 54  TYR B CE2 
3633 C CZ  . TYR B 57  ? 0.13524 0.14245 0.13019 -0.02471 0.02299  -0.01517 54  TYR B CZ  
3634 O OH  . TYR B 57  ? 0.14678 0.19552 0.15477 -0.03236 0.02140  0.00570  54  TYR B OH  
3644 N N   . GLU B 58  ? 0.15009 0.12300 0.12874 -0.00555 0.02507  -0.02038 55  GLU B N   
3645 C CA  . GLU B 58  ? 0.14478 0.08318 0.15586 -0.03623 -0.00878 -0.04569 55  GLU B CA  
3646 C C   . GLU B 58  ? 0.13222 0.11418 0.17307 -0.02978 -0.02162 -0.05592 55  GLU B C   
3647 O O   . GLU B 58  ? 0.14967 0.18921 0.18165 -0.01193 -0.03412 -0.06335 55  GLU B O   
3648 C CB  . GLU B 58  ? 0.17616 0.18425 0.19399 -0.03125 -0.00863 -0.04848 55  GLU B CB  
3649 C CG  . GLU B 58  ? 0.20257 0.20306 0.21260 -0.04396 0.02217  -0.06640 55  GLU B CG  
3650 C CD  . GLU B 58  ? 0.23295 0.24214 0.25367 -0.02607 0.05781  -0.02360 55  GLU B CD  
3651 O OE1 . GLU B 58  ? 0.27245 0.30721 0.27350 0.00280  0.08403  0.00676  55  GLU B OE1 
3652 O OE2 . GLU B 58  ? 0.23657 0.24393 0.25976 -0.01415 0.05885  -0.04866 55  GLU B OE2 
3659 N N   . LYS B 59  ? 0.12900 0.10948 0.18814 -0.00493 -0.00012 -0.04134 56  LYS B N   
3660 C CA  . LYS B 59  ? 0.14431 0.13340 0.21750 0.02614  -0.02155 -0.02298 56  LYS B CA  
3661 C C   . LYS B 59  ? 0.11893 0.16061 0.20877 0.01191  -0.02299 -0.05150 56  LYS B C   
3662 O O   . LYS B 59  ? 0.11863 0.18317 0.22104 -0.01088 -0.03511 -0.05662 56  LYS B O   
3663 C CB  . LYS B 59  ? 0.22266 0.18618 0.28395 0.02446  -0.00882 -0.03675 56  LYS B CB  
3664 C CG  . LYS B 59  ? 0.33819 0.29074 0.36623 0.02808  0.04143  -0.01179 56  LYS B CG  
3665 C CD  . LYS B 59  ? 0.45518 0.45064 0.46123 0.01481  0.08161  -0.00014 56  LYS B CD  
3666 C CE  . LYS B 59  ? 0.54648 0.59918 0.53618 0.01189  0.11537  0.00212  56  LYS B CE  
3667 N NZ  . LYS B 59  ? 0.58945 0.68492 0.58200 0.00696  0.14193  0.00114  56  LYS B NZ  
3681 N N   . PHE B 60  ? 0.08692 0.14043 0.18335 -0.00432 -0.01902 -0.04385 57  PHE B N   
3682 C CA  . PHE B 60  ? 0.10162 0.12984 0.18909 0.01228  0.01055  -0.03487 57  PHE B CA  
3683 C C   . PHE B 60  ? 0.10703 0.06969 0.17589 -0.00020 -0.00179 -0.02637 57  PHE B C   
3684 O O   . PHE B 60  ? 0.12569 0.11405 0.19052 -0.00484 -0.00252 0.00583  57  PHE B O   
3685 C CB  . PHE B 60  ? 0.12326 0.14900 0.16468 -0.00824 -0.00120 -0.00895 57  PHE B CB  
3686 C CG  . PHE B 60  ? 0.15234 0.16417 0.16141 0.00137  0.02006  -0.03381 57  PHE B CG  
3687 C CD1 . PHE B 60  ? 0.17647 0.22843 0.16636 -0.00493 0.04078  -0.01652 57  PHE B CD1 
3688 C CD2 . PHE B 60  ? 0.18312 0.22032 0.13741 0.02917  0.03383  -0.04972 57  PHE B CD2 
3689 C CE1 . PHE B 60  ? 0.19297 0.23319 0.17102 -0.00186 0.04353  -0.01443 57  PHE B CE1 
3690 C CE2 . PHE B 60  ? 0.22547 0.23976 0.15914 0.01467  0.04459  -0.02717 57  PHE B CE2 
3691 C CZ  . PHE B 60  ? 0.21954 0.24699 0.17468 -0.00001 0.04927  -0.00904 57  PHE B CZ  
3701 N N   . ARG B 61  ? 0.13316 0.10828 0.17379 0.00147  0.01500  -0.02039 58  ARG B N   
3702 C CA  . ARG B 61  ? 0.13137 0.13687 0.19206 0.00718  0.01698  -0.02236 58  ARG B CA  
3703 C C   . ARG B 61  ? 0.13193 0.11588 0.18846 -0.00652 0.00295  -0.02790 58  ARG B C   
3704 O O   . ARG B 61  ? 0.11765 0.15412 0.18631 0.01003  -0.03011 -0.01696 58  ARG B O   
3705 C CB  . ARG B 61  ? 0.16322 0.21522 0.20047 0.00568  0.03210  0.01772  58  ARG B CB  
3706 C CG  . ARG B 61  ? 0.20076 0.21669 0.22997 -0.02059 0.02806  -0.01814 58  ARG B CG  
3707 C CD  . ARG B 61  ? 0.24332 0.24925 0.25823 -0.02355 0.03279  -0.00281 58  ARG B CD  
3708 N NE  . ARG B 61  ? 0.31196 0.32743 0.30386 -0.02089 0.04141  0.00632  58  ARG B NE  
3709 C CZ  . ARG B 61  ? 0.36290 0.41287 0.35082 -0.02974 0.03096  0.01796  58  ARG B CZ  
3710 N NH1 . ARG B 61  ? 0.38455 0.41659 0.36384 -0.03668 0.02099  0.01663  58  ARG B NH1 
3711 N NH2 . ARG B 61  ? 0.38208 0.44974 0.36992 -0.03893 0.03925  0.00852  58  ARG B NH2 
3725 N N   . GLU B 62  ? 0.14118 0.14229 0.18732 -0.03073 -0.02320 -0.01023 59  GLU B N   
3728 C C   . GLU B 62  ? 0.15561 0.16340 0.18791 -0.01067 -0.01003 0.02294  59  GLU B C   
3729 O O   . GLU B 62  ? 0.12433 0.18053 0.19007 -0.00600 -0.01343 0.04201  59  GLU B O   
3752 N N   . SER B 63  ? 0.15935 0.17422 0.19263 -0.01482 -0.01131 -0.00442 60  SER B N   
3755 C C   . SER B 63  ? 0.13204 0.17358 0.21232 0.00586  0.00914  0.00639  60  SER B C   
3756 O O   . SER B 63  ? 0.13749 0.18466 0.26848 -0.00723 0.02873  0.01961  60  SER B O   
3771 N N   . LYS B 64  ? 0.11896 0.18626 0.17802 -0.02537 0.00991  -0.00556 61  LYS B N   
3774 C C   . LYS B 64  ? 0.11456 0.14602 0.16734 0.00043  -0.01315 0.00674  61  LYS B C   
3775 O O   . LYS B 64  ? 0.16279 0.21079 0.19742 -0.04058 0.03643  -0.01098 61  LYS B O   
3812 N N   . ASN B 65  ? 0.09165 0.13211 0.15761 0.00783  -0.02309 -0.00587 62  ASN B N   
3813 C CA  . ASN B 65  ? 0.10002 0.12518 0.13579 0.01950  -0.00985 -0.00135 62  ASN B CA  
3814 C C   . ASN B 65  ? 0.11232 0.15964 0.15820 -0.02319 -0.00979 0.00151  62  ASN B C   
3815 O O   . ASN B 65  ? 0.08964 0.16363 0.18745 0.00609  -0.00817 0.01033  62  ASN B O   
3816 C CB  . ASN B 65  ? 0.11697 0.18951 0.15262 0.01638  0.00883  -0.00597 62  ASN B CB  
3817 C CG  . ASN B 65  ? 0.15281 0.19772 0.19438 0.01744  0.00896  0.01366  62  ASN B CG  
3818 O OD1 . ASN B 65  ? 0.21884 0.25989 0.21823 0.01024  0.01438  0.02178  62  ASN B OD1 
3819 N ND2 . ASN B 65  ? 0.18283 0.25787 0.21312 0.01243  0.01060  0.04123  62  ASN B ND2 
3826 N N   . PHE B 66  ? 0.09171 0.13195 0.15333 -0.01088 -0.03494 -0.00925 63  PHE B N   
3827 C CA  . PHE B 66  ? 0.09462 0.13166 0.15493 -0.01220 -0.03551 -0.04204 63  PHE B CA  
3828 C C   . PHE B 66  ? 0.08638 0.11980 0.15868 -0.02289 -0.03691 -0.04071 63  PHE B C   
3829 O O   . PHE B 66  ? 0.10041 0.15112 0.13339 -0.01863 -0.00242 -0.03415 63  PHE B O   
3830 C CB  . PHE B 66  ? 0.13035 0.12121 0.15464 -0.03703 -0.00172 -0.03516 63  PHE B CB  
3831 C CG  . PHE B 66  ? 0.13402 0.12005 0.13657 -0.01320 0.02148  -0.02087 63  PHE B CG  
3832 C CD1 . PHE B 66  ? 0.14662 0.17481 0.15557 -0.04025 0.01113  0.00879  63  PHE B CD1 
3833 C CD2 . PHE B 66  ? 0.16622 0.15177 0.14884 0.01296  0.06321  0.00351  63  PHE B CD2 
3834 C CE1 . PHE B 66  ? 0.17064 0.22044 0.15538 -0.06274 0.01931  0.02729  63  PHE B CE1 
3835 C CE2 . PHE B 66  ? 0.18558 0.20083 0.15485 0.01214  0.05672  -0.00387 63  PHE B CE2 
3836 C CZ  . PHE B 66  ? 0.17950 0.13583 0.16712 -0.03341 0.03755  -0.00662 63  PHE B CZ  
3846 N N   . GLU B 67  ? 0.08125 0.11486 0.16210 -0.01263 -0.03111 -0.00240 64  GLU B N   
3847 C CA  . GLU B 67  ? 0.08567 0.12243 0.12534 0.00474  0.01109  0.00286  64  GLU B CA  
3848 C C   . GLU B 67  ? 0.10043 0.10351 0.11270 -0.01092 0.01462  0.00729  64  GLU B C   
3849 O O   . GLU B 67  ? 0.13079 0.11559 0.13858 0.00426  0.02268  -0.01933 64  GLU B O   
3850 C CB  . GLU B 67  ? 0.09103 0.15194 0.13467 0.00871  0.01083  0.00897  64  GLU B CB  
3851 C CG  . GLU B 67  ? 0.12412 0.16756 0.14717 -0.01300 0.03118  -0.00164 64  GLU B CG  
3852 C CD  . GLU B 67  ? 0.11691 0.16460 0.14565 -0.00081 -0.00684 -0.02208 64  GLU B CD  
3853 O OE1 . GLU B 67  ? 0.11226 0.14004 0.15272 0.00697  -0.01953 -0.03677 64  GLU B OE1 
3854 O OE2 . GLU B 67  ? 0.16585 0.23470 0.16531 -0.00006 0.00911  0.00458  64  GLU B OE2 
3861 N N   . VAL B 68  ? 0.09611 0.08410 0.09722 -0.01890 -0.00967 -0.00022 65  VAL B N   
3862 C CA  . VAL B 68  ? 0.08643 0.08190 0.08030 -0.03956 -0.00009 -0.02407 65  VAL B CA  
3863 C C   . VAL B 68  ? 0.09272 0.07986 0.10231 0.00469  0.01019  -0.01008 65  VAL B C   
3864 O O   . VAL B 68  ? 0.10346 0.12225 0.11999 0.00067  0.01336  -0.02675 65  VAL B O   
3865 C CB  . VAL B 68  ? 0.08324 0.09809 0.10666 -0.01961 -0.00008 -0.01921 65  VAL B CB  
3866 C CG1 . VAL B 68  ? 0.09867 0.07874 0.12622 0.00146  -0.00189 -0.02000 65  VAL B CG1 
3867 C CG2 . VAL B 68  ? 0.11552 0.10784 0.12904 0.00473  0.03541  -0.01233 65  VAL B CG2 
3877 N N   . VAL B 69  ? 0.07341 0.13474 0.10005 -0.01288 0.01165  -0.00625 66  VAL B N   
3878 C CA  . VAL B 69  ? 0.08274 0.15389 0.09054 -0.00989 0.01491  0.01417  66  VAL B CA  
3879 C C   . VAL B 69  ? 0.07579 0.11207 0.10566 0.00082  0.00258  -0.00491 66  VAL B C   
3880 O O   . VAL B 69  ? 0.09026 0.09123 0.11496 0.00146  -0.00427 -0.01968 66  VAL B O   
3881 C CB  . VAL B 69  ? 0.08602 0.12775 0.08986 -0.01229 -0.00026 -0.00255 66  VAL B CB  
3882 C CG1 . VAL B 69  ? 0.10353 0.15177 0.11648 0.00539  0.02516  0.01819  66  VAL B CG1 
3883 C CG2 . VAL B 69  ? 0.07285 0.12976 0.12874 -0.04102 -0.00534 -0.03563 66  VAL B CG2 
3893 N N   . LEU B 70  ? 0.08695 0.10607 0.09744 0.02119  -0.00383 0.01103  67  LEU B N   
3894 C CA  . LEU B 70  ? 0.08553 0.08698 0.10216 0.01563  -0.01374 0.01051  67  LEU B CA  
3895 C C   . LEU B 70  ? 0.10382 0.09405 0.10555 0.00371  -0.00451 0.00089  67  LEU B C   
3896 O O   . LEU B 70  ? 0.10571 0.15077 0.08788 -0.02040 0.01008  -0.02882 67  LEU B O   
3897 C CB  . LEU B 70  ? 0.10645 0.10525 0.09090 0.00452  -0.01139 0.01744  67  LEU B CB  
3898 C CG  . LEU B 70  ? 0.12745 0.11081 0.11220 0.03128  -0.02675 0.00220  67  LEU B CG  
3899 C CD1 . LEU B 70  ? 0.14847 0.13612 0.11594 0.04224  -0.05176 -0.00881 67  LEU B CD1 
3900 C CD2 . LEU B 70  ? 0.13092 0.10765 0.14268 0.00566  -0.00012 -0.01877 67  LEU B CD2 
3912 N N   . VAL B 71  ? 0.09881 0.11072 0.10819 0.00056  -0.02746 -0.01413 68  VAL B N   
3913 C CA  . VAL B 71  ? 0.09926 0.10208 0.10084 0.02794  -0.00890 -0.00449 68  VAL B CA  
3914 C C   . VAL B 71  ? 0.09641 0.08044 0.09950 0.01191  -0.02688 -0.01234 68  VAL B C   
3915 O O   . VAL B 71  ? 0.09962 0.11997 0.10276 0.00058  -0.01453 -0.00030 68  VAL B O   
3916 C CB  . VAL B 71  ? 0.10045 0.07945 0.11362 0.03346  -0.00537 0.00292  68  VAL B CB  
3917 C CG1 . VAL B 71  ? 0.11647 0.12670 0.12607 -0.02481 0.01616  -0.00406 68  VAL B CG1 
3918 C CG2 . VAL B 71  ? 0.11875 0.11075 0.11178 0.03122  -0.00875 -0.00178 68  VAL B CG2 
3928 N N   . THR B 72  ? 0.08307 0.09699 0.07334 0.00804  -0.00476 -0.00852 69  THR B N   
3929 C CA  . THR B 72  ? 0.08058 0.10300 0.07752 -0.01264 -0.01953 -0.00037 69  THR B CA  
3930 C C   . THR B 72  ? 0.13120 0.07835 0.10042 0.00720  -0.00662 0.00169  69  THR B C   
3931 O O   . THR B 72  ? 0.11921 0.10004 0.09925 0.00121  -0.00251 0.02016  69  THR B O   
3932 C CB  . THR B 72  ? 0.10209 0.10857 0.08652 -0.00780 -0.01758 0.00750  69  THR B CB  
3933 O OG1 . THR B 72  ? 0.11905 0.10108 0.10568 0.00191  -0.00625 0.00590  69  THR B OG1 
3934 C CG2 . THR B 72  ? 0.12878 0.15641 0.08181 -0.02192 -0.01252 0.01753  69  THR B CG2 
3942 N N   . TRP B 73  ? 0.13689 0.09533 0.10886 0.00064  0.01257  0.00197  70  TRP B N   
3943 C CA  . TRP B 73  ? 0.11952 0.08929 0.10650 0.01198  -0.00938 -0.01136 70  TRP B CA  
3944 C C   . TRP B 73  ? 0.09463 0.11732 0.10828 -0.01701 -0.00862 -0.00733 70  TRP B C   
3945 O O   . TRP B 73  ? 0.11127 0.15310 0.11540 0.01291  0.00410  -0.01156 70  TRP B O   
3946 C CB  . TRP B 73  ? 0.12165 0.11988 0.10629 0.03436  -0.01426 0.00757  70  TRP B CB  
3947 C CG  . TRP B 73  ? 0.12709 0.06974 0.11584 0.02482  -0.01628 0.00055  70  TRP B CG  
3948 C CD1 . TRP B 73  ? 0.13569 0.06299 0.12485 0.01301  -0.01296 -0.03092 70  TRP B CD1 
3949 C CD2 . TRP B 73  ? 0.09475 0.07731 0.11249 0.00423  -0.02555 -0.01031 70  TRP B CD2 
3950 N NE1 . TRP B 73  ? 0.11106 0.08579 0.11834 -0.00470 -0.02295 -0.02715 70  TRP B NE1 
3951 C CE2 . TRP B 73  ? 0.09930 0.09924 0.11641 0.00547  -0.02431 -0.00476 70  TRP B CE2 
3952 C CE3 . TRP B 73  ? 0.08264 0.11261 0.13375 0.00824  -0.03651 -0.04067 70  TRP B CE3 
3953 C CZ2 . TRP B 73  ? 0.11999 0.08719 0.14884 -0.00705 -0.02527 -0.03384 70  TRP B CZ2 
3954 C CZ3 . TRP B 73  ? 0.08934 0.13441 0.11187 -0.01977 -0.03045 0.00873  70  TRP B CZ3 
3955 C CH2 . TRP B 73  ? 0.09407 0.10284 0.13817 -0.00451 -0.01864 -0.02322 70  TRP B CH2 
3966 N N   . ASP B 74  ? 0.08229 0.08930 0.12341 0.00416  -0.01331 -0.00229 71  ASP B N   
3967 C CA  . ASP B 74  ? 0.10943 0.08477 0.12444 0.00442  0.00806  -0.01770 71  ASP B CA  
3968 C C   . ASP B 74  ? 0.14259 0.12777 0.13675 0.04255  0.01785  0.01114  71  ASP B C   
3969 O O   . ASP B 74  ? 0.16568 0.15420 0.14105 0.00825  0.03169  0.00520  71  ASP B O   
3970 C CB  . ASP B 74  ? 0.12616 0.11773 0.11565 0.01111  0.01413  -0.01591 71  ASP B CB  
3971 C CG  . ASP B 74  ? 0.13698 0.10791 0.13709 0.03233  0.00918  -0.00871 71  ASP B CG  
3972 O OD1 . ASP B 74  ? 0.14484 0.15653 0.16038 0.02174  0.00932  0.02939  71  ASP B OD1 
3973 O OD2 . ASP B 74  ? 0.14731 0.10191 0.16082 0.02145  0.00798  -0.01594 71  ASP B OD2 
3978 N N   . ASP B 75  ? 0.14207 0.13037 0.14597 0.01362  0.03427  -0.00575 72  ASP B N   
3979 C CA  . ASP B 75  ? 0.14613 0.13548 0.15901 -0.02700 0.04255  -0.01326 72  ASP B CA  
3980 C C   . ASP B 75  ? 0.17499 0.13533 0.16902 -0.02149 0.03318  -0.04339 72  ASP B C   
3981 O O   . ASP B 75  ? 0.18618 0.17244 0.16425 -0.01453 0.03329  -0.04976 72  ASP B O   
3982 C CB  . ASP B 75  ? 0.13797 0.16873 0.15584 0.00175  0.03185  0.00351  72  ASP B CB  
3983 C CG  . ASP B 75  ? 0.14488 0.14936 0.19284 -0.00269 0.02845  -0.00981 72  ASP B CG  
3984 O OD1 . ASP B 75  ? 0.13678 0.20216 0.19131 -0.02796 0.00950  -0.01757 72  ASP B OD1 
3985 O OD2 . ASP B 75  ? 0.18029 0.15353 0.21863 -0.03272 0.03648  -0.03733 72  ASP B OD2 
3990 N N   . GLU B 76  ? 0.19602 0.14628 0.19988 0.01376  0.03951  -0.04135 73  GLU B N   
3991 C CA  A GLU B 76  ? 0.24245 0.20295 0.24845 -0.00600 0.02930  -0.03530 73  GLU B CA  
3992 C CA  B GLU B 76  ? 0.24245 0.20295 0.24845 -0.00600 0.02930  -0.03530 73  GLU B CA  
3993 C C   . GLU B 76  ? 0.20073 0.13928 0.21224 -0.00966 0.02928  -0.01913 73  GLU B C   
3994 O O   . GLU B 76  ? 0.17111 0.12299 0.19201 -0.00518 0.03341  -0.01457 73  GLU B O   
3995 C CB  A GLU B 76  ? 0.34475 0.33765 0.35255 0.00590  0.03390  -0.03940 73  GLU B CB  
3996 C CB  B GLU B 76  ? 0.34475 0.33765 0.35255 0.00590  0.03390  -0.03940 73  GLU B CB  
3997 C CG  A GLU B 76  ? 0.46105 0.48255 0.44565 0.00470  0.05730  -0.02010 73  GLU B CG  
3998 C CG  B GLU B 76  ? 0.46105 0.48255 0.44565 0.00470  0.05730  -0.02010 73  GLU B CG  
3999 C CD  A GLU B 76  ? 0.54465 0.59175 0.51935 0.00250  0.09410  -0.00490 73  GLU B CD  
4000 C CD  B GLU B 76  ? 0.54465 0.59175 0.51935 0.00250  0.09410  -0.00490 73  GLU B CD  
4001 O OE1 A GLU B 76  ? 0.59465 0.65185 0.58905 0.00170  0.11720  -0.00500 73  GLU B OE1 
4002 O OE1 B GLU B 76  ? 0.59465 0.65185 0.58905 0.00170  0.11720  -0.00500 73  GLU B OE1 
4003 O OE2 A GLU B 76  ? 0.56095 0.60565 0.54305 0.00180  0.08290  0.00690  73  GLU B OE2 
4004 O OE2 B GLU B 76  ? 0.56095 0.60565 0.54305 0.00180  0.08290  0.00690  73  GLU B OE2 
4015 N N   . GLU B 77  ? 0.17315 0.12832 0.16138 0.00411  0.02337  -0.02084 74  GLU B N   
4016 C CA  . GLU B 77  ? 0.16298 0.11184 0.16278 -0.01694 0.03606  -0.00664 74  GLU B CA  
4017 C C   . GLU B 77  ? 0.16914 0.13628 0.16950 -0.02214 0.03840  -0.02552 74  GLU B C   
4018 O O   . GLU B 77  ? 0.15120 0.13639 0.17495 -0.02117 0.04435  -0.01349 74  GLU B O   
4019 C CB  . GLU B 77  ? 0.19637 0.17378 0.15675 -0.01268 0.05693  0.00598  74  GLU B CB  
4020 C CG  . GLU B 77  ? 0.22034 0.22628 0.14089 -0.01436 0.03550  0.01418  74  GLU B CG  
4021 C CD  . GLU B 77  ? 0.25713 0.28514 0.17820 0.00564  0.02510  0.00907  74  GLU B CD  
4022 O OE1 . GLU B 77  ? 0.27256 0.33059 0.19919 -0.01634 0.05202  0.00221  74  GLU B OE1 
4023 O OE2 . GLU B 77  ? 0.28910 0.33985 0.19200 0.00382  0.02870  0.00875  74  GLU B OE2 
4030 N N   . GLU B 78  ? 0.17322 0.15961 0.16371 -0.04273 0.04530  -0.02967 75  GLU B N   
4033 C C   . GLU B 78  ? 0.18460 0.10057 0.18057 0.00895  0.04490  -0.00534 75  GLU B C   
4034 O O   . GLU B 78  ? 0.21463 0.08879 0.19922 0.01931  0.08079  -0.00901 75  GLU B O   
4057 N N   . ALA B 79  ? 0.18368 0.07892 0.16608 -0.00443 0.03014  -0.02093 76  ALA B N   
4058 C CA  . ALA B 79  ? 0.16369 0.14732 0.15210 0.00467  0.00368  -0.00079 76  ALA B CA  
4059 C C   . ALA B 79  ? 0.15335 0.07783 0.15083 -0.00977 0.00049  -0.01582 76  ALA B C   
4060 O O   . ALA B 79  ? 0.16890 0.13584 0.15205 0.00282  0.03044  0.01758  76  ALA B O   
4061 C CB  . ALA B 79  ? 0.18449 0.15234 0.15526 -0.00401 0.02781  -0.02496 76  ALA B CB  
4067 N N   . TYR B 80  ? 0.14083 0.08619 0.14431 0.01046  0.01630  -0.02057 77  TYR B N   
4068 C CA  . TYR B 80  ? 0.13572 0.10625 0.12084 -0.00156 0.00479  0.01498  77  TYR B CA  
4069 C C   . TYR B 80  ? 0.15291 0.06184 0.12191 -0.00915 0.00692  -0.01817 77  TYR B C   
4070 O O   . TYR B 80  ? 0.12835 0.13057 0.11955 0.00562  0.02206  -0.00626 77  TYR B O   
4071 C CB  . TYR B 80  ? 0.14427 0.10143 0.12263 0.00223  0.00241  -0.00283 77  TYR B CB  
4072 C CG  . TYR B 80  ? 0.14496 0.08587 0.13736 0.00753  0.01213  0.00037  77  TYR B CG  
4073 C CD1 . TYR B 80  ? 0.14956 0.11476 0.14849 -0.01355 0.01604  0.00098  77  TYR B CD1 
4074 C CD2 . TYR B 80  ? 0.13246 0.10025 0.15425 0.03618  -0.00175 -0.02328 77  TYR B CD2 
4075 C CE1 . TYR B 80  ? 0.13735 0.10942 0.15664 0.02343  0.00684  -0.01100 77  TYR B CE1 
4076 C CE2 . TYR B 80  ? 0.12658 0.12861 0.15421 0.03705  0.00713  -0.03656 77  TYR B CE2 
4077 C CZ  . TYR B 80  ? 0.12635 0.12315 0.15573 0.04286  -0.01386 -0.02069 77  TYR B CZ  
4078 O OH  . TYR B 80  ? 0.13362 0.12954 0.16830 0.01514  -0.00211 -0.03892 77  TYR B OH  
4088 N N   . ASN B 81  ? 0.14850 0.07784 0.11775 -0.02840 0.00657  -0.01618 78  ASN B N   
4089 C CA  . ASN B 81  ? 0.14459 0.09555 0.10096 -0.01910 0.01492  -0.00163 78  ASN B CA  
4090 C C   . ASN B 81  ? 0.15313 0.08763 0.13667 -0.01350 0.02499  -0.01362 78  ASN B C   
4091 O O   . ASN B 81  ? 0.15243 0.14508 0.15866 -0.02882 0.03055  -0.02525 78  ASN B O   
4092 C CB  . ASN B 81  ? 0.16457 0.16946 0.11481 -0.01229 0.05229  -0.01498 78  ASN B CB  
4093 C CG  . ASN B 81  ? 0.18969 0.18941 0.13540 -0.00732 0.03968  -0.03988 78  ASN B CG  
4094 O OD1 . ASN B 81  ? 0.21449 0.20133 0.14419 -0.00298 0.00339  -0.03869 78  ASN B OD1 
4095 N ND2 . ASN B 81  ? 0.20747 0.20629 0.18071 -0.03794 0.08200  -0.04642 78  ASN B ND2 
4102 N N   . GLY B 82  ? 0.14621 0.09682 0.12549 0.01374  0.02303  -0.01537 79  GLY B N   
4103 C CA  . GLY B 82  ? 0.15406 0.10362 0.11713 -0.01483 0.01845  -0.02059 79  GLY B CA  
4104 C C   . GLY B 82  ? 0.15672 0.11533 0.14219 -0.03756 0.03031  -0.02454 79  GLY B C   
4105 O O   . GLY B 82  ? 0.16331 0.12525 0.17376 -0.01048 0.02878  -0.01946 79  GLY B O   
4109 N N   . TYR B 83  ? 0.13585 0.09650 0.12930 -0.03139 0.02818  -0.02618 80  TYR B N   
4110 C CA  . TYR B 83  ? 0.14091 0.08366 0.13425 -0.00592 0.02010  -0.02125 80  TYR B CA  
4111 C C   . TYR B 83  ? 0.14978 0.10522 0.13766 0.02719  0.02081  -0.00266 80  TYR B C   
4112 O O   . TYR B 83  ? 0.15987 0.10508 0.12666 0.00233  0.03683  -0.01019 80  TYR B O   
4113 C CB  . TYR B 83  ? 0.14400 0.07274 0.14572 -0.01747 0.01884  -0.01491 80  TYR B CB  
4114 C CG  . TYR B 83  ? 0.13989 0.08874 0.13843 -0.02758 0.01842  -0.01268 80  TYR B CG  
4115 C CD1 . TYR B 83  ? 0.15782 0.10903 0.15627 -0.02763 0.02175  -0.01931 80  TYR B CD1 
4116 C CD2 . TYR B 83  ? 0.13392 0.12122 0.13042 -0.01431 0.01417  0.02609  80  TYR B CD2 
4117 C CE1 . TYR B 83  ? 0.15925 0.10730 0.15045 -0.00829 0.02553  -0.01694 80  TYR B CE1 
4118 C CE2 . TYR B 83  ? 0.13840 0.11212 0.13044 0.00516  0.01092  0.02207  80  TYR B CE2 
4119 C CZ  . TYR B 83  ? 0.14625 0.05356 0.13054 0.01331  0.02400  0.00315  80  TYR B CZ  
4120 O OH  . TYR B 83  ? 0.15503 0.08044 0.13269 0.00444  0.03911  -0.02082 80  TYR B OH  
4130 N N   . PHE B 84  ? 0.13076 0.10410 0.14053 0.01481  0.02679  -0.00410 81  PHE B N   
4131 C CA  . PHE B 84  ? 0.13658 0.11733 0.11614 0.01885  0.02165  -0.00112 81  PHE B CA  
4132 C C   . PHE B 84  ? 0.14848 0.11644 0.12845 0.01888  0.01943  -0.00597 81  PHE B C   
4133 O O   . PHE B 84  ? 0.14845 0.08147 0.14075 0.01334  0.00398  0.02423  81  PHE B O   
4134 C CB  . PHE B 84  ? 0.13651 0.12040 0.10208 0.02183  0.02250  0.03193  81  PHE B CB  
4135 C CG  . PHE B 84  ? 0.12553 0.12792 0.12293 0.00575  0.03909  0.05744  81  PHE B CG  
4136 C CD1 . PHE B 84  ? 0.11039 0.11774 0.13109 0.00070  -0.00372 0.02018  81  PHE B CD1 
4137 C CD2 . PHE B 84  ? 0.16007 0.17526 0.13268 0.00732  0.03539  0.06036  81  PHE B CD2 
4138 C CE1 . PHE B 84  ? 0.12972 0.11652 0.14833 -0.00393 0.00309  0.01704  81  PHE B CE1 
4139 C CE2 . PHE B 84  ? 0.14516 0.18591 0.12413 0.00905  -0.00010 0.03069  81  PHE B CE2 
4140 C CZ  . PHE B 84  ? 0.14552 0.14991 0.14687 -0.02344 0.00999  0.02084  81  PHE B CZ  
4150 N N   . ALA B 85  ? 0.13479 0.13909 0.12828 -0.01727 0.02103  -0.02043 82  ALA B N   
4151 C CA  . ALA B 85  ? 0.14849 0.12781 0.11302 -0.02457 0.00268  -0.03647 82  ALA B CA  
4152 C C   . ALA B 85  ? 0.15982 0.11134 0.13312 -0.06379 0.00394  -0.03668 82  ALA B C   
4153 O O   . ALA B 85  ? 0.14266 0.15874 0.15600 -0.05495 0.01708  -0.04875 82  ALA B O   
4154 C CB  . ALA B 85  ? 0.18432 0.10914 0.14111 -0.04583 0.03474  0.01226  82  ALA B CB  
4160 N N   . LYS B 86  ? 0.17284 0.07882 0.11704 -0.02456 0.02551  -0.01918 83  LYS B N   
4161 C CA  . LYS B 86  ? 0.14266 0.13171 0.11893 -0.01277 0.01034  -0.00084 83  LYS B CA  
4162 C C   . LYS B 86  ? 0.15077 0.06756 0.11935 -0.02659 0.02748  0.00086  83  LYS B C   
4163 O O   . LYS B 86  ? 0.17010 0.11980 0.11348 -0.00259 0.02958  0.02497  83  LYS B O   
4164 C CB  . LYS B 86  ? 0.12379 0.15706 0.12835 -0.03802 0.00935  0.00079  83  LYS B CB  
4165 C CG  . LYS B 86  ? 0.14443 0.11720 0.12739 -0.00555 0.02128  0.01214  83  LYS B CG  
4166 C CD  . LYS B 86  ? 0.14375 0.13347 0.12669 0.00821  0.01910  0.00770  83  LYS B CD  
4167 C CE  . LYS B 86  ? 0.15024 0.10077 0.16178 0.03322  0.02546  0.01708  83  LYS B CE  
4168 N NZ  . LYS B 86  ? 0.18820 0.18373 0.20860 0.02359  0.02257  -0.03267 83  LYS B NZ  
4182 N N   . MET B 87  ? 0.14988 0.07929 0.12101 -0.03074 0.01335  -0.00423 84  MET B N   
4183 C CA  . MET B 87  ? 0.12838 0.09946 0.11798 -0.02725 0.01906  -0.01816 84  MET B CA  
4184 C C   . MET B 87  ? 0.12838 0.12825 0.11865 0.01982  0.00559  0.00311  84  MET B C   
4185 O O   . MET B 87  ? 0.16302 0.18210 0.11184 0.00721  0.02942  -0.00503 84  MET B O   
4186 C CB  . MET B 87  ? 0.10889 0.11356 0.14965 -0.04605 -0.00136 -0.00434 84  MET B CB  
4187 C CG  . MET B 87  ? 0.10390 0.08374 0.16571 -0.02760 -0.01387 -0.00617 84  MET B CG  
4188 S SD  . MET B 87  ? 0.12335 0.10428 0.15750 -0.00023 -0.00090 0.00574  84  MET B SD  
4189 C CE  . MET B 87  ? 0.07715 0.11368 0.20436 0.02369  -0.01961 0.00922  84  MET B CE  
4199 N N   . PRO B 88  ? 0.13237 0.10801 0.10424 -0.00517 0.00640  -0.00789 85  PRO B N   
4200 C CA  . PRO B 88  ? 0.13693 0.13429 0.11346 -0.04221 0.00151  -0.01703 85  PRO B CA  
4201 C C   . PRO B 88  ? 0.11223 0.13218 0.11502 -0.02871 -0.02459 0.00572  85  PRO B C   
4202 O O   . PRO B 88  ? 0.15107 0.15658 0.14734 -0.03781 -0.02256 0.01710  85  PRO B O   
4203 C CB  . PRO B 88  ? 0.14177 0.07648 0.14031 -0.02703 -0.00856 -0.01113 85  PRO B CB  
4204 C CG  . PRO B 88  ? 0.11843 0.11071 0.14565 0.01319  0.01285  0.01355  85  PRO B CG  
4205 C CD  . PRO B 88  ? 0.12570 0.13289 0.12629 0.02133  0.02971  0.01964  85  PRO B CD  
4213 N N   . TRP B 89  ? 0.10642 0.13219 0.11429 -0.00811 -0.00118 0.00407  86  TRP B N   
4214 C CA  . TRP B 89  ? 0.11212 0.09087 0.10277 0.01304  -0.00846 0.00407  86  TRP B CA  
4215 C C   . TRP B 89  ? 0.13578 0.12430 0.11666 -0.01293 0.00031  -0.02377 86  TRP B C   
4216 O O   . TRP B 89  ? 0.14989 0.13823 0.13910 -0.02784 0.02632  -0.02800 86  TRP B O   
4217 C CB  . TRP B 89  ? 0.08846 0.07033 0.11864 0.00911  -0.01062 -0.02870 86  TRP B CB  
4218 C CG  . TRP B 89  ? 0.10421 0.11022 0.10151 0.01500  -0.00187 -0.00425 86  TRP B CG  
4219 C CD1 . TRP B 89  ? 0.11368 0.12292 0.10387 0.01148  -0.00377 -0.01928 86  TRP B CD1 
4220 C CD2 . TRP B 89  ? 0.07757 0.10045 0.07813 -0.00096 -0.01055 0.02105  86  TRP B CD2 
4221 N NE1 . TRP B 89  ? 0.11860 0.11056 0.11300 -0.01766 0.00714  -0.02275 86  TRP B NE1 
4222 C CE2 . TRP B 89  ? 0.08244 0.09578 0.09631 0.00678  -0.00313 0.01811  86  TRP B CE2 
4223 C CE3 . TRP B 89  ? 0.10964 0.10216 0.09606 -0.03627 0.00839  0.01198  86  TRP B CE3 
4224 C CZ2 . TRP B 89  ? 0.09568 0.10262 0.11692 -0.01393 -0.00303 -0.00364 86  TRP B CZ2 
4225 C CZ3 . TRP B 89  ? 0.12463 0.07869 0.09223 0.01149  0.01271  0.00416  86  TRP B CZ3 
4226 C CH2 . TRP B 89  ? 0.12069 0.11234 0.09115 0.03891  0.00117  -0.00976 86  TRP B CH2 
4237 N N   . LEU B 90  ? 0.12413 0.13945 0.09165 -0.01770 0.01739  -0.01755 87  LEU B N   
4238 C CA  . LEU B 90  ? 0.11005 0.14668 0.07187 0.00465  -0.00221 -0.00292 87  LEU B CA  
4239 C C   . LEU B 90  ? 0.10627 0.11060 0.07719 -0.01666 -0.02426 -0.00288 87  LEU B C   
4240 O O   . LEU B 90  ? 0.10264 0.12639 0.10174 -0.00876 -0.01008 -0.00680 87  LEU B O   
4241 C CB  . LEU B 90  ? 0.11325 0.12510 0.07441 0.01267  0.00835  0.00345  87  LEU B CB  
4242 C CG  . LEU B 90  ? 0.13292 0.17685 0.08832 0.00402  -0.00163 -0.01040 87  LEU B CG  
4243 C CD1 . LEU B 90  ? 0.13489 0.22603 0.10260 -0.00202 0.02257  0.01099  87  LEU B CD1 
4244 C CD2 . LEU B 90  ? 0.12903 0.22334 0.09929 0.04634  -0.04113 0.00172  87  LEU B CD2 
4256 N N   . ALA B 91  ? 0.08937 0.15905 0.06928 -0.00128 -0.01846 0.01169  88  ALA B N   
4257 C CA  . ALA B 91  ? 0.10142 0.15218 0.08272 -0.00088 -0.01991 0.02882  88  ALA B CA  
4258 C C   . ALA B 91  ? 0.12147 0.16151 0.09910 -0.01885 -0.01708 0.02175  88  ALA B C   
4259 O O   . ALA B 91  ? 0.13062 0.18184 0.12611 -0.03051 -0.00775 -0.00348 88  ALA B O   
4260 C CB  . ALA B 91  ? 0.12073 0.12522 0.08344 -0.00903 0.00449  0.03291  88  ALA B CB  
4266 N N   . ILE B 92  ? 0.13322 0.10673 0.09594 -0.01440 0.02631  0.01138  89  ILE B N   
4269 C C   . ILE B 92  ? 0.11157 0.11973 0.07270 -0.00830 -0.00424 0.02200  89  ILE B C   
4270 O O   . ILE B 92  ? 0.12298 0.12705 0.09244 -0.02312 0.01101  0.01303  89  ILE B O   
4301 N N   . PRO B 93  ? 0.11248 0.19460 0.08376 -0.03244 0.00792  0.00874  90  PRO B N   
4302 C CA  . PRO B 93  ? 0.12639 0.21279 0.08667 -0.01954 0.02315  -0.02696 90  PRO B CA  
4303 C C   . PRO B 93  ? 0.13141 0.15805 0.09938 -0.04535 0.03796  -0.01620 90  PRO B C   
4304 O O   . PRO B 93  ? 0.12105 0.14658 0.13615 -0.00679 0.01295  -0.00402 90  PRO B O   
4305 C CB  . PRO B 93  ? 0.14807 0.25740 0.08846 -0.01417 0.01573  -0.03000 90  PRO B CB  
4306 C CG  . PRO B 93  ? 0.14230 0.24202 0.10506 -0.00476 0.01723  -0.01316 90  PRO B CG  
4307 C CD  . PRO B 93  ? 0.11969 0.22213 0.09388 -0.02413 -0.02085 0.01342  90  PRO B CD  
4315 N N   . PHE B 94  ? 0.14712 0.17422 0.10825 -0.05031 0.01780  -0.02653 91  PHE B N   
4316 C CA  . PHE B 94  ? 0.14275 0.11475 0.12703 -0.03139 0.00647  -0.01935 91  PHE B CA  
4317 C C   . PHE B 94  ? 0.14523 0.10612 0.15102 -0.01874 -0.00284 -0.01450 91  PHE B C   
4318 O O   . PHE B 94  ? 0.13947 0.15987 0.14305 -0.02712 -0.00228 -0.01923 91  PHE B O   
4319 C CB  . PHE B 94  ? 0.15162 0.12551 0.14174 -0.05031 0.02087  -0.01990 91  PHE B CB  
4320 C CG  . PHE B 94  ? 0.15799 0.15631 0.16598 -0.04679 0.02515  -0.00921 91  PHE B CG  
4321 C CD1 . PHE B 94  ? 0.16607 0.12897 0.17033 -0.04677 0.02467  0.00036  91  PHE B CD1 
4322 C CD2 . PHE B 94  ? 0.15170 0.15618 0.16121 -0.00849 0.02258  0.02184  91  PHE B CD2 
4323 C CE1 . PHE B 94  ? 0.17796 0.12998 0.16440 -0.00440 0.01749  0.01068  91  PHE B CE1 
4324 C CE2 . PHE B 94  ? 0.15495 0.16534 0.17130 0.00598  0.02231  0.03116  91  PHE B CE2 
4325 C CZ  . PHE B 94  ? 0.17979 0.16812 0.17648 0.00314  0.02092  0.00538  91  PHE B CZ  
4335 N N   . SER B 95  ? 0.15686 0.15591 0.16860 -0.04504 0.02394  -0.00475 92  SER B N   
4338 C C   . SER B 95  ? 0.16526 0.16904 0.16355 -0.01274 0.06339  -0.02605 92  SER B C   
4339 O O   . SER B 95  ? 0.16248 0.21083 0.16044 -0.03269 0.05554  -0.02352 92  SER B O   
4354 N N   . SER B 96  ? 0.16234 0.14054 0.14521 -0.01217 0.06196  -0.01941 93  SER B N   
4357 C C   . SER B 96  ? 0.13725 0.11857 0.15405 -0.00972 0.02041  -0.00009 93  SER B C   
4358 O O   . SER B 96  ? 0.11195 0.12234 0.12559 -0.00750 0.01517  0.00941  93  SER B O   
4373 N N   . ARG B 97  ? 0.14786 0.11611 0.15101 -0.00624 0.02923  0.00193  94  ARG B N   
4374 C CA  . ARG B 97  ? 0.15067 0.11973 0.14713 0.00004  0.01732  -0.01096 94  ARG B CA  
4375 C C   . ARG B 97  ? 0.11310 0.12892 0.13552 -0.01281 0.00145  -0.03345 94  ARG B C   
4376 O O   . ARG B 97  ? 0.10778 0.17526 0.12337 -0.00782 0.00384  -0.01922 94  ARG B O   
4377 C CB  . ARG B 97  ? 0.17701 0.13969 0.17365 0.00923  0.00350  0.02129  94  ARG B CB  
4378 C CG  . ARG B 97  ? 0.17588 0.12188 0.18904 -0.00001 0.00123  0.00572  94  ARG B CG  
4379 C CD  . ARG B 97  ? 0.22117 0.14058 0.19759 -0.00789 0.02282  -0.00031 94  ARG B CD  
4380 N NE  . ARG B 97  ? 0.24034 0.19608 0.20208 0.01668  0.04668  0.02366  94  ARG B NE  
4381 C CZ  . ARG B 97  ? 0.21231 0.13933 0.18592 -0.00959 0.01455  0.01559  94  ARG B CZ  
4382 N NH1 . ARG B 97  ? 0.20547 0.16357 0.16042 -0.01384 0.02646  -0.00907 94  ARG B NH1 
4383 N NH2 . ARG B 97  ? 0.24465 0.18844 0.22201 -0.00186 0.00089  0.05564  94  ARG B NH2 
4397 N N   . ALA B 98  ? 0.15008 0.12633 0.12741 -0.00157 0.02033  -0.03576 95  ALA B N   
4398 C CA  . ALA B 98  ? 0.15708 0.11059 0.13298 -0.01009 0.03554  -0.01659 95  ALA B CA  
4399 C C   . ALA B 98  ? 0.14297 0.08655 0.11614 -0.03641 0.01189  -0.00740 95  ALA B C   
4400 O O   . ALA B 98  ? 0.15502 0.14834 0.11586 -0.01468 -0.00041 -0.01429 95  ALA B O   
4401 C CB  . ALA B 98  ? 0.16209 0.14049 0.15394 -0.01710 0.04220  -0.01358 95  ALA B CB  
4407 N N   . GLU B 99  ? 0.13776 0.11244 0.13152 -0.03270 0.01479  -0.00077 96  GLU B N   
4408 C CA  . GLU B 99  ? 0.14279 0.11497 0.13130 0.00355  0.00180  0.00023  96  GLU B CA  
4409 C C   . GLU B 99  ? 0.10372 0.10870 0.11087 -0.00449 -0.00427 0.00277  96  GLU B C   
4410 O O   . GLU B 99  ? 0.10034 0.12749 0.12271 -0.01034 -0.01167 -0.01677 96  GLU B O   
4411 C CB  . GLU B 99  ? 0.20242 0.14656 0.16027 -0.01402 0.04241  -0.00445 96  GLU B CB  
4412 C CG  . GLU B 99  ? 0.27062 0.27354 0.23921 0.00342  0.05079  0.00677  96  GLU B CG  
4413 C CD  . GLU B 99  ? 0.30983 0.36127 0.31243 0.00016  0.06354  -0.02131 96  GLU B CD  
4414 O OE1 . GLU B 99  ? 0.32934 0.36638 0.33344 0.00080  0.08548  -0.00660 96  GLU B OE1 
4415 O OE2 . GLU B 99  ? 0.33451 0.40240 0.34480 0.03012  0.07035  -0.03507 96  GLU B OE2 
4422 N N   . LEU B 100 ? 0.10565 0.12370 0.11894 0.00157  0.00926  0.01093  97  LEU B N   
4423 C CA  . LEU B 100 ? 0.11534 0.10930 0.13042 -0.02031 0.00091  0.02043  97  LEU B CA  
4424 C C   . LEU B 100 ? 0.11662 0.12955 0.12167 -0.02933 -0.02155 0.03645  97  LEU B C   
4425 O O   . LEU B 100 ? 0.13514 0.13414 0.10952 -0.00627 0.01248  0.00806  97  LEU B O   
4426 C CB  . LEU B 100 ? 0.10609 0.11045 0.13781 -0.03404 0.01012  0.02834  97  LEU B CB  
4427 C CG  . LEU B 100 ? 0.12941 0.10487 0.14457 -0.01166 0.01547  0.02906  97  LEU B CG  
4428 C CD1 . LEU B 100 ? 0.14687 0.12921 0.13904 0.01190  0.02615  0.01754  97  LEU B CD1 
4429 C CD2 . LEU B 100 ? 0.13618 0.17066 0.14079 -0.02528 0.00614  -0.01092 97  LEU B CD2 
4441 N N   . GLU B 101 ? 0.12613 0.09834 0.12640 -0.02002 -0.02475 0.03050  98  GLU B N   
4442 C CA  . GLU B 101 ? 0.12592 0.13982 0.13660 0.00309  -0.02203 0.02593  98  GLU B CA  
4443 C C   . GLU B 101 ? 0.12570 0.11631 0.12939 -0.01350 -0.03704 0.02213  98  GLU B C   
4444 O O   . GLU B 101 ? 0.12670 0.11520 0.11923 -0.02186 -0.03050 0.01340  98  GLU B O   
4445 C CB  . GLU B 101 ? 0.16281 0.17305 0.18270 0.03925  -0.00226 0.00379  98  GLU B CB  
4446 C CG  . GLU B 101 ? 0.18453 0.20797 0.22497 0.04129  -0.00638 -0.00574 98  GLU B CG  
4447 C CD  . GLU B 101 ? 0.20784 0.26092 0.26463 0.03847  -0.00578 0.03265  98  GLU B CD  
4448 O OE1 . GLU B 101 ? 0.19658 0.27884 0.32143 -0.03835 -0.05693 0.01323  98  GLU B OE1 
4449 O OE2 . GLU B 101 ? 0.24477 0.33080 0.25290 0.02902  0.00036  0.06256  98  GLU B OE2 
4456 N N   . ALA B 102 ? 0.14752 0.10702 0.11985 -0.00593 -0.01739 -0.00837 99  ALA B N   
4457 C CA  . ALA B 102 ? 0.15893 0.08410 0.12078 0.00964  0.00565  0.01620  99  ALA B CA  
4458 C C   . ALA B 102 ? 0.13281 0.07987 0.12605 -0.00336 -0.01905 -0.00716 99  ALA B C   
4459 O O   . ALA B 102 ? 0.15529 0.08446 0.13809 0.00135  0.00630  0.01445  99  ALA B O   
4460 C CB  . ALA B 102 ? 0.16954 0.11892 0.12718 0.05649  0.01322  0.01626  99  ALA B CB  
4466 N N   . LEU B 103 ? 0.11555 0.09083 0.10979 0.00825  -0.02190 -0.00358 100 LEU B N   
4467 C CA  . LEU B 103 ? 0.11716 0.10219 0.10903 0.01506  -0.01682 -0.00980 100 LEU B CA  
4468 C C   . LEU B 103 ? 0.10438 0.09150 0.09603 0.01783  -0.02888 0.00839  100 LEU B C   
4469 O O   . LEU B 103 ? 0.13156 0.10133 0.09435 0.01346  0.00492  -0.00906 100 LEU B O   
4470 C CB  . LEU B 103 ? 0.10803 0.06872 0.13636 -0.02032 -0.03502 -0.00464 100 LEU B CB  
4471 C CG  . LEU B 103 ? 0.11282 0.11522 0.16976 -0.00036 -0.04292 -0.02074 100 LEU B CG  
4472 C CD1 . LEU B 103 ? 0.14823 0.15652 0.18658 -0.03842 -0.04042 0.00109  100 LEU B CD1 
4473 C CD2 . LEU B 103 ? 0.14611 0.17076 0.17888 0.00466  -0.05360 -0.01532 100 LEU B CD2 
4485 N N   . ARG B 104 ? 0.08679 0.11605 0.11131 0.01843  -0.02049 -0.01213 101 ARG B N   
4486 C CA  . ARG B 104 ? 0.10423 0.13068 0.13239 0.00278  -0.01742 -0.02571 101 ARG B CA  
4487 C C   . ARG B 104 ? 0.08949 0.08160 0.11593 0.00598  -0.03670 -0.00466 101 ARG B C   
4488 O O   . ARG B 104 ? 0.12616 0.10798 0.11713 0.01057  -0.01146 -0.00138 101 ARG B O   
4489 C CB  . ARG B 104 ? 0.12790 0.07482 0.14472 0.02633  -0.00773 0.01108  101 ARG B CB  
4490 C CG  . ARG B 104 ? 0.10797 0.12875 0.14265 0.00364  -0.01419 -0.00976 101 ARG B CG  
4491 C CD  . ARG B 104 ? 0.11536 0.12157 0.14548 -0.01066 -0.02714 0.03015  101 ARG B CD  
4492 N NE  . ARG B 104 ? 0.11591 0.10168 0.16407 0.00038  -0.02803 0.02660  101 ARG B NE  
4493 C CZ  . ARG B 104 ? 0.12223 0.14393 0.17070 0.03747  -0.00176 0.02711  101 ARG B CZ  
4494 N NH1 . ARG B 104 ? 0.15365 0.15874 0.16265 0.05257  0.02012  0.00168  101 ARG B NH1 
4495 N NH2 . ARG B 104 ? 0.10443 0.16198 0.16698 0.00947  0.00428  0.02252  101 ARG B NH2 
4509 N N   . SER B 105 ? 0.09837 0.10629 0.11848 -0.00881 -0.02230 0.00354  102 SER B N   
4510 C CA  . SER B 105 ? 0.12222 0.14693 0.15132 0.01029  -0.00417 -0.00834 102 SER B CA  
4511 C C   . SER B 105 ? 0.13062 0.10579 0.12980 -0.00266 -0.01715 -0.00013 102 SER B C   
4512 O O   . SER B 105 ? 0.12540 0.11258 0.15834 0.02352  -0.03180 -0.03313 102 SER B O   
4513 C CB  . SER B 105 ? 0.13231 0.14313 0.18886 0.01522  0.01363  0.03037  102 SER B CB  
4514 O OG  . SER B 105 ? 0.15817 0.15259 0.15800 0.00088  0.02676  0.03550  102 SER B OG  
4520 N N   . THR B 106 ? 0.15835 0.07049 0.12266 0.00947  0.00003  0.00803  103 THR B N   
4521 C CA  . THR B 106 ? 0.16775 0.06894 0.13487 0.03367  0.03156  0.02689  103 THR B CA  
4522 C C   . THR B 106 ? 0.15260 0.08425 0.13188 0.03911  0.02378  0.01233  103 THR B C   
4523 O O   . THR B 106 ? 0.16102 0.11378 0.14159 0.02109  0.04409  0.00769  103 THR B O   
4524 C CB  . THR B 106 ? 0.18668 0.12970 0.15167 0.05010  0.01808  0.02514  103 THR B CB  
4525 O OG1 . THR B 106 ? 0.22103 0.16620 0.11898 0.03393  0.04674  0.00326  103 THR B OG1 
4526 C CG2 . THR B 106 ? 0.20278 0.15751 0.19521 0.05626  0.01429  -0.00251 103 THR B CG2 
4534 N N   . PHE B 107 ? 0.14030 0.07090 0.12389 0.00534  0.02039  -0.00505 104 PHE B N   
4535 C CA  . PHE B 107 ? 0.12801 0.06933 0.14643 0.01203  0.02484  0.03267  104 PHE B CA  
4536 C C   . PHE B 107 ? 0.14183 0.06656 0.15099 0.03820  0.00179  0.01743  104 PHE B C   
4537 O O   . PHE B 107 ? 0.14056 0.17797 0.14177 0.01106  0.01240  0.01462  104 PHE B O   
4538 C CB  . PHE B 107 ? 0.10573 0.12482 0.14764 -0.00847 0.03339  0.00324  104 PHE B CB  
4539 C CG  . PHE B 107 ? 0.10084 0.13582 0.13327 0.01265  0.00197  0.02162  104 PHE B CG  
4540 C CD1 . PHE B 107 ? 0.13342 0.12882 0.14131 -0.02058 0.00889  -0.00134 104 PHE B CD1 
4541 C CD2 . PHE B 107 ? 0.11569 0.16876 0.14499 0.04483  -0.01064 -0.01253 104 PHE B CD2 
4542 C CE1 . PHE B 107 ? 0.14928 0.15161 0.15995 0.00762  0.00074  -0.01823 104 PHE B CE1 
4543 C CE2 . PHE B 107 ? 0.12136 0.18002 0.15270 0.04605  -0.00014 -0.00962 104 PHE B CE2 
4544 C CZ  . PHE B 107 ? 0.12810 0.18106 0.15809 0.01679  -0.00464 -0.00944 104 PHE B CZ  
4554 N N   . GLY B 108 ? 0.13982 0.06286 0.14759 0.02223  -0.00650 0.00527  105 GLY B N   
4555 C CA  . GLY B 108 ? 0.14299 0.11577 0.13955 -0.00926 -0.01140 -0.01204 105 GLY B CA  
4556 C C   . GLY B 108 ? 0.12879 0.11465 0.13331 -0.01199 -0.03253 -0.00934 105 GLY B C   
4557 O O   . GLY B 108 ? 0.15692 0.12609 0.13155 0.04580  -0.02039 -0.01028 105 GLY B O   
4561 N N   . VAL B 109 ? 0.12814 0.07081 0.13498 0.00799  -0.03396 -0.01015 106 VAL B N   
4562 C CA  . VAL B 109 ? 0.13584 0.06347 0.12812 0.02779  -0.00531 -0.00571 106 VAL B CA  
4563 C C   . VAL B 109 ? 0.11544 0.08343 0.11692 0.02895  0.01009  0.01097  106 VAL B C   
4564 O O   . VAL B 109 ? 0.14954 0.13234 0.13058 0.04455  0.04023  0.00384  106 VAL B O   
4565 C CB  . VAL B 109 ? 0.15308 0.05745 0.13054 0.01174  -0.02821 0.01728  106 VAL B CB  
4566 C CG1 . VAL B 109 ? 0.15631 0.12319 0.12996 -0.02205 0.01244  0.00260  106 VAL B CG1 
4567 C CG2 . VAL B 109 ? 0.17481 0.08787 0.14991 0.01868  -0.06684 0.02532  106 VAL B CG2 
4577 N N   . GLU B 110 ? 0.13408 0.09488 0.11172 0.02438  0.00217  0.00197  107 GLU B N   
4578 C CA  . GLU B 110 ? 0.12493 0.10670 0.12676 0.04246  -0.02277 0.04407  107 GLU B CA  
4579 C C   . GLU B 110 ? 0.11379 0.10969 0.14985 0.04434  -0.00546 0.05035  107 GLU B C   
4580 O O   . GLU B 110 ? 0.12850 0.08240 0.23337 0.01182  0.00046  0.05158  107 GLU B O   
4581 C CB  . GLU B 110 ? 0.17846 0.19130 0.15618 -0.00172 -0.03260 0.01761  107 GLU B CB  
4582 C CG  . GLU B 110 ? 0.24786 0.20678 0.21719 -0.00986 -0.01133 0.00067  107 GLU B CG  
4583 C CD  . GLU B 110 ? 0.29765 0.25614 0.27307 0.01239  -0.01757 -0.02184 107 GLU B CD  
4584 O OE1 . GLU B 110 ? 0.30119 0.31810 0.24788 0.02193  0.02785  -0.09577 107 GLU B OE1 
4585 O OE2 . GLU B 110 ? 0.34435 0.33544 0.33048 -0.01120 -0.05123 -0.01976 107 GLU B OE2 
4592 N N   . THR B 111 ? 0.12220 0.09776 0.11997 0.00042  -0.00948 -0.01582 108 THR B N   
4595 C C   . THR B 111 ? 0.08453 0.06235 0.10767 0.03046  -0.01522 0.01181  108 THR B C   
4596 O O   . THR B 111 ? 0.10802 0.09316 0.14948 0.04304  -0.01919 0.02891  108 THR B O   
4617 N N   . ILE B 112 ? 0.07235 0.10437 0.11239 0.01966  -0.00875 0.01440  109 ILE B N   
4618 C CA  . ILE B 112 ? 0.06739 0.11151 0.09863 -0.00709 -0.02683 0.01234  109 ILE B CA  
4619 C C   . ILE B 112 ? 0.09864 0.08411 0.10958 0.04309  -0.00833 0.02950  109 ILE B C   
4620 O O   . ILE B 112 ? 0.13524 0.08882 0.12164 0.03352  0.01211  0.03172  109 ILE B O   
4621 C CB  . ILE B 112 ? 0.08443 0.09917 0.10941 -0.01309 -0.03364 -0.00679 109 ILE B CB  
4622 C CG1 . ILE B 112 ? 0.12195 0.11586 0.11703 -0.00012 -0.00366 0.04083  109 ILE B CG1 
4623 C CG2 . ILE B 112 ? 0.09915 0.14940 0.12528 -0.00019 -0.01246 0.00992  109 ILE B CG2 
4624 C CD1 . ILE B 112 ? 0.12588 0.10951 0.11397 0.01208  0.01608  0.03858  109 ILE B CD1 
4636 N N   . PRO B 113 ? 0.09767 0.10090 0.10104 0.01952  0.00795  0.01279  110 PRO B N   
4637 C CA  . PRO B 113 ? 0.10010 0.06917 0.10646 -0.00283 0.00580  -0.02522 110 PRO B CA  
4638 C C   . PRO B 113 ? 0.11873 0.11182 0.10268 0.01511  0.00892  0.00181  110 PRO B C   
4639 O O   . PRO B 113 ? 0.11749 0.17443 0.08004 0.02255  0.00821  0.00422  110 PRO B O   
4640 C CB  . PRO B 113 ? 0.09565 0.14005 0.13689 -0.05356 0.01630  -0.02436 110 PRO B CB  
4641 C CG  . PRO B 113 ? 0.11622 0.13050 0.13578 -0.02611 0.00827  0.04782  110 PRO B CG  
4642 C CD  . PRO B 113 ? 0.12207 0.06868 0.12948 -0.02109 0.02246  0.02062  110 PRO B CD  
4650 N N   . THR B 114 ? 0.12070 0.12558 0.09699 0.00049  0.02115  0.00441  111 THR B N   
4651 C CA  . THR B 114 ? 0.11553 0.12174 0.11728 0.01870  0.00354  0.01585  111 THR B CA  
4652 C C   . THR B 114 ? 0.11939 0.12408 0.11558 0.02639  0.01665  0.02590  111 THR B C   
4653 O O   . THR B 114 ? 0.13645 0.11295 0.08372 0.00506  0.03185  -0.01587 111 THR B O   
4654 C CB  . THR B 114 ? 0.09899 0.12471 0.15593 0.03692  -0.01779 0.00112  111 THR B CB  
4655 O OG1 . THR B 114 ? 0.12545 0.18331 0.15146 0.01302  -0.01156 -0.00106 111 THR B OG1 
4656 C CG2 . THR B 114 ? 0.09824 0.11493 0.19577 -0.00587 -0.01143 -0.01997 111 THR B CG2 
4664 N N   . VAL B 115 ? 0.10443 0.06643 0.12756 0.02929  0.00674  0.00638  112 VAL B N   
4665 C CA  A VAL B 115 ? 0.10565 0.09645 0.13635 0.01960  -0.00340 -0.01540 112 VAL B CA  
4666 C CA  B VAL B 115 ? 0.10565 0.09645 0.13635 0.01960  -0.00340 -0.01540 112 VAL B CA  
4667 C C   . VAL B 115 ? 0.09947 0.10979 0.12180 -0.01928 -0.00808 -0.00861 112 VAL B C   
4668 O O   . VAL B 115 ? 0.11649 0.14124 0.10549 0.02680  -0.00112 -0.03048 112 VAL B O   
4669 C CB  A VAL B 115 ? 0.14465 0.13165 0.18635 0.01540  -0.00270 -0.01300 112 VAL B CB  
4670 C CB  B VAL B 115 ? 0.14465 0.13165 0.18635 0.01540  -0.00270 -0.01300 112 VAL B CB  
4671 C CG1 A VAL B 115 ? 0.15455 0.15065 0.20185 -0.00180 -0.01630 -0.02610 112 VAL B CG1 
4672 C CG1 B VAL B 115 ? 0.15455 0.15065 0.20185 -0.00180 -0.01630 -0.02610 112 VAL B CG1 
4673 C CG2 A VAL B 115 ? 0.18035 0.14975 0.20075 0.02550  0.00410  -0.01610 112 VAL B CG2 
4674 C CG2 B VAL B 115 ? 0.18035 0.14975 0.20075 0.02550  0.00410  -0.01610 112 VAL B CG2 
4691 N N   . ILE B 116 ? 0.09386 0.11685 0.10335 -0.02501 -0.01355 0.00858  113 ILE B N   
4695 C C   . ILE B 116 ? 0.11625 0.10583 0.12481 -0.01000 -0.01238 -0.02018 113 ILE B C   
4696 O O   . ILE B 116 ? 0.15610 0.11600 0.11990 0.02379  -0.00140 -0.02888 113 ILE B O   
4742 N N   . ALA B 117 ? 0.12881 0.10517 0.10080 -0.02270 -0.00630 -0.00912 114 ALA B N   
4743 C CA  . ALA B 117 ? 0.13937 0.10589 0.09549 -0.02942 -0.02193 -0.01174 114 ALA B CA  
4744 C C   . ALA B 117 ? 0.16587 0.06758 0.10755 0.01872  0.00966  -0.01642 114 ALA B C   
4745 O O   . ALA B 117 ? 0.17199 0.06563 0.10897 0.03143  0.01285  -0.02215 114 ALA B O   
4746 C CB  . ALA B 117 ? 0.16497 0.13490 0.12344 -0.02283 0.02557  0.00684  114 ALA B CB  
4752 N N   . VAL B 118 ? 0.15968 0.10565 0.11422 0.01854  0.02529  -0.01171 115 VAL B N   
4753 C CA  . VAL B 118 ? 0.13838 0.12677 0.11371 -0.00280 0.02070  -0.01303 115 VAL B CA  
4754 C C   . VAL B 118 ? 0.12876 0.10922 0.13542 -0.01474 0.01903  -0.02933 115 VAL B C   
4755 O O   . VAL B 118 ? 0.15302 0.11980 0.15247 -0.00360 0.00755  0.01183  115 VAL B O   
4756 C CB  . VAL B 118 ? 0.11015 0.15076 0.14549 -0.02548 0.00644  -0.00232 115 VAL B CB  
4757 C CG1 . VAL B 118 ? 0.09342 0.17092 0.15313 -0.04694 0.03139  -0.01194 115 VAL B CG1 
4758 C CG2 . VAL B 118 ? 0.13145 0.23621 0.17131 -0.00728 -0.00982 -0.00158 115 VAL B CG2 
4768 N N   . ASN B 119 ? 0.14258 0.10776 0.12393 -0.00355 0.01854  -0.01012 116 ASN B N   
4769 C CA  . ASN B 119 ? 0.12034 0.14008 0.12865 0.01070  0.00069  0.01912  116 ASN B CA  
4770 C C   . ASN B 119 ? 0.12986 0.12686 0.12701 0.01466  -0.00653 0.02235  116 ASN B C   
4771 O O   . ASN B 119 ? 0.15509 0.14654 0.14151 -0.00201 0.00326  0.01897  116 ASN B O   
4772 C CB  . ASN B 119 ? 0.13903 0.14174 0.14929 -0.00138 0.00178  0.01031  116 ASN B CB  
4773 C CG  . ASN B 119 ? 0.15889 0.22151 0.18795 0.01309  0.00279  0.03318  116 ASN B CG  
4774 O OD1 . ASN B 119 ? 0.16728 0.21047 0.18992 0.06748  0.00486  0.03646  116 ASN B OD1 
4775 N ND2 . ASN B 119 ? 0.22052 0.38222 0.23852 0.01975  0.01144  0.03283  116 ASN B ND2 
4782 N N   . ALA B 120 ? 0.13456 0.14582 0.12657 0.02575  -0.00822 0.00866  117 ALA B N   
4783 C CA  . ALA B 120 ? 0.16051 0.11001 0.11959 0.03420  -0.00377 0.02398  117 ALA B CA  
4784 C C   . ALA B 120 ? 0.16705 0.15174 0.11408 0.02244  -0.01054 -0.01316 117 ALA B C   
4785 O O   . ALA B 120 ? 0.21230 0.22226 0.10711 -0.00086 0.02173  -0.01935 117 ALA B O   
4786 C CB  . ALA B 120 ? 0.20023 0.13652 0.12299 0.00032  0.03270  0.03628  117 ALA B CB  
4792 N N   . ASP B 121 ? 0.15022 0.17472 0.14260 0.03269  -0.00920 0.02625  118 ASP B N   
4793 C CA  . ASP B 121 ? 0.17202 0.17342 0.19590 0.05016  -0.02158 0.01740  118 ASP B CA  
4794 C C   . ASP B 121 ? 0.19797 0.15003 0.19086 0.07383  -0.02478 0.02257  118 ASP B C   
4795 O O   . ASP B 121 ? 0.23489 0.17511 0.20665 0.04297  0.02175  0.06181  118 ASP B O   
4796 C CB  . ASP B 121 ? 0.19954 0.21022 0.22471 0.02054  -0.03573 0.03393  118 ASP B CB  
4797 C CG  . ASP B 121 ? 0.22016 0.22225 0.27140 0.01280  -0.01159 0.05012  118 ASP B CG  
4798 O OD1 . ASP B 121 ? 0.22694 0.20278 0.27177 0.00626  -0.03763 0.04446  118 ASP B OD1 
4799 O OD2 . ASP B 121 ? 0.24849 0.25642 0.31321 0.01793  0.02984  0.06145  118 ASP B OD2 
4804 N N   . THR B 122 ? 0.19981 0.17845 0.17076 0.00531  -0.01359 0.01859  119 THR B N   
4805 C CA  . THR B 122 ? 0.19650 0.15615 0.16404 0.04089  -0.00045 0.03887  119 THR B CA  
4806 C C   . THR B 122 ? 0.20053 0.14399 0.15107 0.01920  0.00165  0.01513  119 THR B C   
4807 O O   . THR B 122 ? 0.22376 0.16397 0.15797 0.02646  0.02122  -0.00389 119 THR B O   
4808 C CB  . THR B 122 ? 0.18509 0.19118 0.17030 0.05888  -0.00881 0.04549  119 THR B CB  
4809 O OG1 . THR B 122 ? 0.18706 0.17155 0.19781 0.04830  0.00609  0.04646  119 THR B OG1 
4810 C CG2 . THR B 122 ? 0.19816 0.26477 0.17373 0.06044  -0.02464 0.00450  119 THR B CG2 
4818 N N   . GLY B 123 ? 0.20084 0.11231 0.14078 0.02731  0.00332  0.02729  120 GLY B N   
4819 C CA  . GLY B 123 ? 0.18838 0.11822 0.15278 0.01891  0.01460  0.04034  120 GLY B CA  
4820 C C   . GLY B 123 ? 0.13197 0.14123 0.14338 0.01446  -0.00895 0.00093  120 GLY B C   
4821 O O   . GLY B 123 ? 0.12356 0.12787 0.14915 0.01056  -0.00087 -0.00456 120 GLY B O   
4825 N N   . ALA B 124 ? 0.14105 0.18401 0.15015 0.02888  -0.00704 0.00323  121 ALA B N   
4826 C CA  . ALA B 124 ? 0.15673 0.08821 0.15310 0.00686  -0.00257 -0.00650 121 ALA B CA  
4827 C C   . ALA B 124 ? 0.14508 0.09764 0.14087 -0.04348 0.00210  -0.00943 121 ALA B C   
4828 O O   . ALA B 124 ? 0.15819 0.12171 0.14207 -0.04437 0.00329  -0.03017 121 ALA B O   
4829 C CB  . ALA B 124 ? 0.16470 0.16459 0.14993 0.01911  -0.00647 -0.00091 121 ALA B CB  
4835 N N   . VAL B 125 ? 0.16019 0.10806 0.12677 -0.01321 0.01588  0.00158  122 VAL B N   
4836 C CA  . VAL B 125 ? 0.14738 0.10866 0.12666 -0.01943 0.00239  -0.00175 122 VAL B CA  
4837 C C   . VAL B 125 ? 0.16441 0.13062 0.13321 0.00204  0.02254  -0.00433 122 VAL B C   
4838 O O   . VAL B 125 ? 0.20873 0.16474 0.18014 -0.00117 0.05727  0.00035  122 VAL B O   
4839 C CB  . VAL B 125 ? 0.14417 0.08362 0.11607 -0.03950 -0.01907 0.01166  122 VAL B CB  
4840 C CG1 . VAL B 125 ? 0.17872 0.10987 0.12147 -0.02519 -0.04706 -0.00075 122 VAL B CG1 
4841 C CG2 . VAL B 125 ? 0.14773 0.20568 0.12860 -0.04851 0.00320  0.03151  122 VAL B CG2 
4851 N N   . VAL B 126 ? 0.15702 0.11823 0.13817 0.02693  0.03114  0.02294  123 VAL B N   
4852 C CA  . VAL B 126 ? 0.16582 0.14724 0.15349 0.04887  0.02735  0.00396  123 VAL B CA  
4853 C C   . VAL B 126 ? 0.15134 0.12473 0.12548 -0.00323 0.03019  -0.00718 123 VAL B C   
4854 O O   . VAL B 126 ? 0.16957 0.16460 0.13687 0.03336  0.03678  -0.03270 123 VAL B O   
4855 C CB  . VAL B 126 ? 0.17124 0.16658 0.16426 0.02773  0.00073  0.02443  123 VAL B CB  
4856 C CG1 . VAL B 126 ? 0.19092 0.20999 0.19153 -0.00104 0.01340  0.00457  123 VAL B CG1 
4857 C CG2 . VAL B 126 ? 0.17585 0.20918 0.19897 -0.01438 0.01136  0.00713  123 VAL B CG2 
4867 N N   . SER B 127 ? 0.16382 0.09326 0.12824 0.00743  0.05088  0.00288  124 SER B N   
4868 C CA  . SER B 127 ? 0.14694 0.11883 0.12397 -0.00660 0.04987  0.01117  124 SER B CA  
4869 C C   . SER B 127 ? 0.14282 0.12108 0.10869 -0.01934 0.01417  -0.02590 124 SER B C   
4870 O O   . SER B 127 ? 0.14254 0.11175 0.10369 -0.02212 0.02200  -0.00131 124 SER B O   
4871 C CB  . SER B 127 ? 0.12154 0.08793 0.15031 0.01813  0.02990  0.02614  124 SER B CB  
4872 O OG  . SER B 127 ? 0.14223 0.08782 0.15274 0.01240  0.01258  0.01004  124 SER B OG  
4878 N N   . THR B 128 ? 0.15713 0.15547 0.11120 -0.03392 0.02230  -0.01813 125 THR B N   
4879 C CA  . THR B 128 ? 0.15552 0.15147 0.13737 -0.02902 0.00563  -0.03909 125 THR B CA  
4880 C C   . THR B 128 ? 0.13949 0.12800 0.14263 -0.01803 0.01084  -0.02868 125 THR B C   
4881 O O   . THR B 128 ? 0.13953 0.13281 0.17078 0.01733  0.02948  0.00335  125 THR B O   
4882 C CB  . THR B 128 ? 0.18027 0.14215 0.16508 -0.03608 -0.00645 -0.04615 125 THR B CB  
4883 O OG1 . THR B 128 ? 0.24057 0.19329 0.16512 -0.09016 0.00721  -0.06547 125 THR B OG1 
4884 C CG2 . THR B 128 ? 0.18082 0.15665 0.17969 -0.05895 0.02169  -0.00691 125 THR B CG2 
4892 N N   . LYS B 129 ? 0.14230 0.13912 0.10730 -0.00757 -0.01268 -0.01929 126 LYS B N   
4893 C CA  . LYS B 129 ? 0.18382 0.11202 0.12554 0.00432  0.00455  -0.03618 126 LYS B CA  
4894 C C   . LYS B 129 ? 0.15267 0.12797 0.10663 -0.02155 0.01403  -0.02564 126 LYS B C   
4895 O O   . LYS B 129 ? 0.17461 0.15831 0.11344 -0.02271 0.01630  0.01260  126 LYS B O   
4896 C CB  . LYS B 129 ? 0.24473 0.13978 0.17017 0.01392  0.01080  -0.02575 126 LYS B CB  
4897 C CG  . LYS B 129 ? 0.33019 0.24001 0.24520 -0.00259 0.06433  -0.02549 126 LYS B CG  
4898 C CD  . LYS B 129 ? 0.42114 0.41808 0.35320 -0.01634 0.08204  -0.02172 126 LYS B CD  
4899 C CE  . LYS B 129 ? 0.48649 0.53337 0.44690 -0.01317 0.10030  -0.01384 126 LYS B CE  
4900 N NZ  . LYS B 129 ? 0.50959 0.59729 0.48965 -0.00978 0.10341  -0.01283 126 LYS B NZ  
4914 N N   . GLY B 130 ? 0.12278 0.10615 0.11819 0.00764  -0.00891 -0.01054 127 GLY B N   
4915 C CA  . GLY B 130 ? 0.12772 0.13508 0.12590 -0.02480 0.00649  -0.02884 127 GLY B CA  
4916 C C   . GLY B 130 ? 0.12886 0.12894 0.12567 0.00435  0.01075  0.01617  127 GLY B C   
4917 O O   . GLY B 130 ? 0.14952 0.12038 0.14253 -0.02178 0.03518  -0.00178 127 GLY B O   
4921 N N   . ARG B 131 ? 0.14895 0.09919 0.14065 0.00288  0.02796  0.01688  128 ARG B N   
4922 C CA  . ARG B 131 ? 0.14354 0.12578 0.15998 -0.01331 0.02975  0.01260  128 ARG B CA  
4923 C C   . ARG B 131 ? 0.15072 0.15547 0.16814 -0.00351 0.01817  0.01971  128 ARG B C   
4924 O O   . ARG B 131 ? 0.20009 0.17522 0.14033 -0.01055 0.03374  -0.00265 128 ARG B O   
4925 C CB  . ARG B 131 ? 0.13531 0.17950 0.16243 0.06034  0.02342  0.01878  128 ARG B CB  
4926 C CG  . ARG B 131 ? 0.15021 0.18317 0.15225 0.07003  0.02562  0.00453  128 ARG B CG  
4927 C CD  . ARG B 131 ? 0.15928 0.17383 0.15029 0.04034  0.01148  0.00170  128 ARG B CD  
4928 N NE  . ARG B 131 ? 0.18407 0.16422 0.14814 0.01092  0.01510  0.03795  128 ARG B NE  
4929 C CZ  . ARG B 131 ? 0.19692 0.18194 0.13617 0.02590  0.01099  0.02884  128 ARG B CZ  
4930 N NH1 . ARG B 131 ? 0.21931 0.17277 0.15114 0.03528  0.00531  0.03028  128 ARG B NH1 
4931 N NH2 . ARG B 131 ? 0.19248 0.23690 0.12694 0.05163  0.00832  -0.00838 128 ARG B NH2 
4945 N N   . GLU B 132 ? 0.17392 0.12890 0.16695 -0.00579 0.00815  0.04539  129 GLU B N   
4946 C CA  A GLU B 132 ? 0.21465 0.16305 0.20155 -0.00030 0.01830  0.03070  129 GLU B CA  
4947 C CA  B GLU B 132 ? 0.21465 0.16305 0.20155 -0.00030 0.01830  0.03070  129 GLU B CA  
4948 C C   . GLU B 132 ? 0.19034 0.13104 0.17250 0.01859  0.01140  0.01700  129 GLU B C   
4949 O O   . GLU B 132 ? 0.22547 0.14108 0.16741 0.01210  0.03765  0.02123  129 GLU B O   
4950 C CB  A GLU B 132 ? 0.31485 0.28225 0.30205 0.00750  0.02820  0.00920  129 GLU B CB  
4951 C CB  B GLU B 132 ? 0.31485 0.28225 0.30205 0.00750  0.02820  0.00920  129 GLU B CB  
4952 C CG  A GLU B 132 ? 0.43065 0.42115 0.40885 0.00330  0.06230  -0.00050 129 GLU B CG  
4953 C CG  B GLU B 132 ? 0.43065 0.42115 0.40885 0.00330  0.06230  -0.00050 129 GLU B CG  
4954 C CD  A GLU B 132 ? 0.51285 0.56055 0.49695 0.00270  0.08770  0.00290  129 GLU B CD  
4955 C CD  B GLU B 132 ? 0.51285 0.56055 0.49695 0.00270  0.08770  0.00290  129 GLU B CD  
4956 O OE1 A GLU B 132 ? 0.53775 0.59865 0.52785 0.00700  0.08580  0.00800  129 GLU B OE1 
4957 O OE1 B GLU B 132 ? 0.53775 0.59865 0.52785 0.00700  0.08580  0.00800  129 GLU B OE1 
4958 O OE2 A GLU B 132 ? 0.54565 0.62135 0.54125 -0.00070 0.10360  0.00310  129 GLU B OE2 
4959 O OE2 B GLU B 132 ? 0.54565 0.62135 0.54125 -0.00070 0.10360  0.00310  129 GLU B OE2 
4970 N N   . ARG B 133 ? 0.13090 0.17310 0.14047 0.01274  0.01218  -0.00896 130 ARG B N   
4971 C CA  . ARG B 133 ? 0.13855 0.15519 0.14880 0.00563  0.02869  -0.03678 130 ARG B CA  
4972 C C   . ARG B 133 ? 0.14152 0.13393 0.11585 -0.03480 0.02104  -0.04326 130 ARG B C   
4973 O O   . ARG B 133 ? 0.15824 0.17699 0.14753 -0.03052 0.05701  -0.00693 130 ARG B O   
4974 C CB  . ARG B 133 ? 0.18114 0.19599 0.19980 -0.03934 0.02335  -0.03510 130 ARG B CB  
4975 C CG  . ARG B 133 ? 0.21980 0.29623 0.26343 -0.04441 0.00887  -0.04767 130 ARG B CG  
4976 C CD  . ARG B 133 ? 0.28319 0.35799 0.31291 -0.02582 0.00519  -0.05876 130 ARG B CD  
4977 N NE  . ARG B 133 ? 0.32155 0.35603 0.32824 -0.02457 0.03529  -0.06707 130 ARG B NE  
4978 C CZ  . ARG B 133 ? 0.36623 0.42263 0.34788 -0.00306 0.03656  -0.03213 130 ARG B CZ  
4979 N NH1 . ARG B 133 ? 0.40593 0.43986 0.36099 0.03158  0.03141  -0.03915 130 ARG B NH1 
4980 N NH2 . ARG B 133 ? 0.38227 0.44677 0.36732 -0.01497 0.05747  -0.01019 130 ARG B NH2 
4994 N N   . LEU B 134 ? 0.11699 0.14770 0.11012 -0.03075 0.00384  -0.03804 131 LEU B N   
4995 C CA  . LEU B 134 ? 0.11851 0.12167 0.10406 -0.04897 0.00330  -0.03321 131 LEU B CA  
4996 C C   . LEU B 134 ? 0.12833 0.12729 0.11920 -0.02127 0.01547  -0.01919 131 LEU B C   
4997 O O   . LEU B 134 ? 0.16152 0.16488 0.12530 -0.03660 0.04003  0.00958  131 LEU B O   
4998 C CB  . LEU B 134 ? 0.11743 0.14094 0.09232 0.01458  -0.00412 -0.02552 131 LEU B CB  
4999 C CG  . LEU B 134 ? 0.13383 0.13440 0.09902 0.01203  -0.00133 -0.01454 131 LEU B CG  
5000 C CD1 . LEU B 134 ? 0.15198 0.20614 0.11108 -0.01338 -0.00544 -0.02078 131 LEU B CD1 
5001 C CD2 . LEU B 134 ? 0.16631 0.18856 0.11084 -0.00819 0.05142  -0.02072 131 LEU B CD2 
5013 N N   . LEU B 135 ? 0.15820 0.16046 0.12213 0.01128  0.03645  -0.01689 132 LEU B N   
5014 C CA  . LEU B 135 ? 0.14582 0.15995 0.13047 0.02601  0.03333  0.03635  132 LEU B CA  
5015 C C   . LEU B 135 ? 0.16455 0.16651 0.14615 0.01912  0.05777  0.01675  132 LEU B C   
5016 O O   . LEU B 135 ? 0.19946 0.21326 0.19393 -0.00828 0.07499  0.04077  132 LEU B O   
5017 C CB  . LEU B 135 ? 0.11858 0.18884 0.15728 0.02254  0.01273  0.03365  132 LEU B CB  
5018 C CG  . LEU B 135 ? 0.15513 0.19364 0.16865 0.02188  0.01519  0.01957  132 LEU B CG  
5019 C CD1 . LEU B 135 ? 0.18530 0.23382 0.16690 0.01118  0.03384  0.01840  132 LEU B CD1 
5020 C CD2 . LEU B 135 ? 0.19028 0.19885 0.18087 0.01634  0.00911  -0.01876 132 LEU B CD2 
5032 N N   . THR B 136 ? 0.14627 0.19076 0.14030 0.04849  0.03593  0.00387  133 THR B N   
5033 C CA  . THR B 136 ? 0.15881 0.23008 0.14796 0.06836  0.03181  0.01042  133 THR B CA  
5034 C C   . THR B 136 ? 0.14602 0.25370 0.14929 0.03856  0.02886  -0.00264 133 THR B C   
5035 O O   . THR B 136 ? 0.16927 0.26444 0.13081 0.03088  0.02601  0.00144  133 THR B O   
5036 C CB  . THR B 136 ? 0.17358 0.29053 0.16700 0.07607  0.02357  -0.03673 133 THR B CB  
5037 O OG1 . THR B 136 ? 0.19112 0.32517 0.18812 0.05937  0.00181  -0.08386 133 THR B OG1 
5038 C CG2 . THR B 136 ? 0.18770 0.32853 0.17465 0.07706  0.02989  -0.03293 133 THR B CG2 
5046 N N   . ASP B 137 ? 0.12092 0.21672 0.13744 0.00663  0.04032  0.00712  134 ASP B N   
5047 C CA  . ASP B 137 ? 0.12124 0.21048 0.13771 0.02469  0.04344  0.02042  134 ASP B CA  
5048 C C   . ASP B 137 ? 0.14147 0.19298 0.13473 0.01782  0.03619  0.02500  134 ASP B C   
5049 O O   . ASP B 137 ? 0.14385 0.21041 0.10616 0.01970  0.04304  0.02503  134 ASP B O   
5050 C CB  . ASP B 137 ? 0.11467 0.19460 0.12976 -0.00096 0.04157  -0.00313 134 ASP B CB  
5051 C CG  . ASP B 137 ? 0.11447 0.17019 0.13058 -0.01119 0.04048  -0.00877 134 ASP B CG  
5052 O OD1 . ASP B 137 ? 0.11636 0.16013 0.13111 0.00046  0.03617  0.00554  134 ASP B OD1 
5053 O OD2 . ASP B 137 ? 0.13145 0.19673 0.12932 -0.02135 0.03957  0.01193  134 ASP B OD2 
5058 N N   . PRO B 138 ? 0.16042 0.18492 0.16169 0.01723  0.03209  0.01921  135 PRO B N   
5059 C CA  . PRO B 138 ? 0.16496 0.16427 0.16388 0.04741  0.01743  -0.00573 135 PRO B CA  
5060 C C   . PRO B 138 ? 0.18104 0.17549 0.16246 0.07211  0.03377  -0.01791 135 PRO B C   
5061 O O   . PRO B 138 ? 0.20601 0.18311 0.14812 0.03517  0.04599  -0.01972 135 PRO B O   
5062 C CB  . PRO B 138 ? 0.19435 0.19718 0.17049 0.01885  0.03681  -0.00012 135 PRO B CB  
5063 C CG  . PRO B 138 ? 0.21105 0.18625 0.16962 -0.00322 0.03257  0.02376  135 PRO B CG  
5064 C CD  . PRO B 138 ? 0.18521 0.16178 0.17374 -0.00449 0.02291  0.03104  135 PRO B CD  
5072 N N   . GLU B 139 ? 0.20480 0.16793 0.20218 0.01609  0.05316  -0.00137 136 GLU B N   
5073 C CA  . GLU B 139 ? 0.24520 0.21542 0.25425 0.03533  0.06051  -0.02436 136 GLU B CA  
5074 C C   . GLU B 139 ? 0.19392 0.17155 0.18164 0.02017  0.03415  -0.02872 136 GLU B C   
5075 O O   . GLU B 139 ? 0.21748 0.20106 0.20340 0.06551  0.01834  -0.06288 136 GLU B O   
5076 C CB  . GLU B 139 ? 0.38010 0.33840 0.36897 0.01820  0.07306  -0.03105 136 GLU B CB  
5077 C CG  . GLU B 139 ? 0.50802 0.50123 0.49737 -0.00016 0.10680  -0.02157 136 GLU B CG  
5078 C CD  . GLU B 139 ? 0.63127 0.67880 0.60783 -0.01703 0.12843  0.00432  136 GLU B CD  
5079 O OE1 . GLU B 139 ? 0.70635 0.78379 0.69443 -0.01982 0.16732  0.01537  136 GLU B OE1 
5080 O OE2 . GLU B 139 ? 0.65700 0.69405 0.63559 -0.01664 0.11856  0.00267  136 GLU B OE2 
5087 N N   . GLY B 140 ? 0.18177 0.17873 0.12854 0.00388  0.04487  -0.01542 137 GLY B N   
5088 C CA  . GLY B 140 ? 0.15531 0.17854 0.11262 0.02577  0.03707  -0.00813 137 GLY B CA  
5089 C C   . GLY B 140 ? 0.13070 0.17747 0.10903 0.01232  0.01446  0.00428  137 GLY B C   
5090 O O   . GLY B 140 ? 0.14359 0.17418 0.10627 -0.00104 0.01259  -0.01023 137 GLY B O   
5094 N N   . LYS B 141 ? 0.12540 0.15345 0.11800 0.01232  0.02295  -0.01232 138 LYS B N   
5095 C CA  . LYS B 141 ? 0.13335 0.14159 0.13327 0.00821  0.04503  0.00543  138 LYS B CA  
5096 C C   . LYS B 141 ? 0.12527 0.15077 0.11721 0.00688  0.04839  0.00994  138 LYS B C   
5097 O O   . LYS B 141 ? 0.12406 0.16719 0.11659 0.02646  0.02529  0.00972  138 LYS B O   
5098 C CB  . LYS B 141 ? 0.12630 0.15972 0.14276 -0.01007 0.02996  -0.02805 138 LYS B CB  
5099 C CG  . LYS B 141 ? 0.16628 0.16310 0.15266 -0.01531 0.05110  -0.02800 138 LYS B CG  
5100 C CD  . LYS B 141 ? 0.20695 0.19627 0.14721 -0.02581 0.07201  0.02676  138 LYS B CD  
5101 C CE  . LYS B 141 ? 0.25282 0.24843 0.17906 -0.04231 0.08213  0.03875  138 LYS B CE  
5102 N NZ  . LYS B 141 ? 0.29833 0.30641 0.23914 -0.03126 0.09180  0.02893  138 LYS B NZ  
5116 N N   . ASN B 142 ? 0.12451 0.14689 0.12539 -0.00723 0.03604  -0.00426 139 ASN B N   
5117 C CA  . ASN B 142 ? 0.11689 0.16203 0.10970 -0.00808 0.02343  -0.02293 139 ASN B CA  
5118 C C   . ASN B 142 ? 0.13622 0.16599 0.11989 -0.01880 0.03510  -0.00082 139 ASN B C   
5119 O O   . ASN B 142 ? 0.14717 0.19715 0.12651 -0.03654 0.04333  -0.01792 139 ASN B O   
5120 C CB  . ASN B 142 ? 0.14431 0.14625 0.11312 0.00093  0.03976  -0.03306 139 ASN B CB  
5121 C CG  . ASN B 142 ? 0.19365 0.18760 0.12941 -0.00306 0.05229  -0.02967 139 ASN B CG  
5122 O OD1 . ASN B 142 ? 0.22684 0.23984 0.13887 0.03224  0.08754  -0.00529 139 ASN B OD1 
5123 N ND2 . ASN B 142 ? 0.17951 0.14011 0.12228 0.00004  0.02322  -0.02956 139 ASN B ND2 
5130 N N   . PHE B 143 ? 0.12788 0.13995 0.11421 -0.01975 0.02430  -0.01695 140 PHE B N   
5131 C CA  . PHE B 143 ? 0.13461 0.14151 0.12685 -0.03331 0.03164  0.00103  140 PHE B CA  
5132 C C   . PHE B 143 ? 0.15669 0.18055 0.14262 -0.00744 0.02218  0.01681  140 PHE B C   
5133 O O   . PHE B 143 ? 0.16821 0.20303 0.14495 0.04183  0.03868  0.02907  140 PHE B O   
5134 C CB  . PHE B 143 ? 0.14903 0.18519 0.14361 -0.03419 0.05687  -0.00669 140 PHE B CB  
5135 C CG  . PHE B 143 ? 0.15143 0.17642 0.14810 -0.03444 0.04619  -0.00225 140 PHE B CG  
5136 C CD1 . PHE B 143 ? 0.17136 0.21384 0.14783 -0.03146 0.02983  -0.01943 140 PHE B CD1 
5137 C CD2 . PHE B 143 ? 0.16534 0.17651 0.16826 -0.05034 0.04721  -0.03284 140 PHE B CD2 
5138 C CE1 . PHE B 143 ? 0.18807 0.21938 0.14939 -0.06195 0.01929  -0.00442 140 PHE B CE1 
5139 C CE2 . PHE B 143 ? 0.18415 0.20191 0.15848 -0.03726 0.04185  -0.04706 140 PHE B CE2 
5140 C CZ  . PHE B 143 ? 0.19592 0.20913 0.13861 -0.05388 0.04293  -0.02945 140 PHE B CZ  
5150 N N   . PRO B 144 ? 0.17367 0.17809 0.13864 -0.00592 0.02640  -0.00287 141 PRO B N   
5151 C CA  . PRO B 144 ? 0.16874 0.18479 0.11208 -0.01537 0.03253  -0.01334 141 PRO B CA  
5152 C C   . PRO B 144 ? 0.15936 0.17723 0.11477 -0.01343 0.03884  -0.02270 141 PRO B C   
5153 O O   . PRO B 144 ? 0.17996 0.18346 0.13759 -0.02142 0.07025  -0.01697 141 PRO B O   
5154 C CB  . PRO B 144 ? 0.20034 0.21981 0.13252 -0.01731 0.05797  0.00508  141 PRO B CB  
5155 C CG  . PRO B 144 ? 0.22212 0.19681 0.16821 -0.01643 0.04545  0.03192  141 PRO B CG  
5156 C CD  . PRO B 144 ? 0.21199 0.22798 0.16649 0.02482  0.03053  -0.00285 141 PRO B CD  
5164 N N   . TRP B 145 ? 0.17250 0.21893 0.12317 -0.01519 0.05037  0.00604  142 TRP B N   
5165 C CA  . TRP B 145 ? 0.17374 0.22448 0.12598 -0.03879 0.04800  -0.03243 142 TRP B CA  
5166 C C   . TRP B 145 ? 0.20134 0.22792 0.16730 -0.02685 0.06804  -0.01347 142 TRP B C   
5167 O O   . TRP B 145 ? 0.21190 0.20907 0.19968 -0.05393 0.05062  -0.01318 142 TRP B O   
5168 C CB  . TRP B 145 ? 0.15098 0.23781 0.13963 -0.02912 0.03522  -0.03758 142 TRP B CB  
5169 C CG  . TRP B 145 ? 0.12687 0.19033 0.15370 -0.01215 0.01906  0.01537  142 TRP B CG  
5170 C CD1 . TRP B 145 ? 0.15187 0.16087 0.16642 -0.02759 0.02543  0.01203  142 TRP B CD1 
5171 C CD2 . TRP B 145 ? 0.11733 0.18908 0.16954 -0.00456 0.02078  0.01353  142 TRP B CD2 
5172 N NE1 . TRP B 145 ? 0.14662 0.15527 0.15701 -0.01360 0.00351  0.01817  142 TRP B NE1 
5173 C CE2 . TRP B 145 ? 0.12901 0.16759 0.16006 0.01119  0.00315  0.01518  142 TRP B CE2 
5174 C CE3 . TRP B 145 ? 0.12167 0.17888 0.17722 -0.00117 0.01872  0.00681  142 TRP B CE3 
5175 C CZ2 . TRP B 145 ? 0.14255 0.19537 0.18319 0.02434  0.00862  0.02796  142 TRP B CZ2 
5176 C CZ3 . TRP B 145 ? 0.14973 0.21333 0.18663 0.02001  0.00979  0.01129  142 TRP B CZ3 
5177 C CH2 . TRP B 145 ? 0.13523 0.19597 0.17969 0.02143  0.00220  0.04451  142 TRP B CH2 
5188 N N   . SER B 146 ? 0.22999 0.19506 0.18728 -0.01146 0.07851  -0.00954 143 SER B N   
5189 C CA  . SER B 146 ? 0.30381 0.26724 0.28452 -0.03259 0.04600  -0.03750 143 SER B CA  
5190 C C   . SER B 146 ? 0.43183 0.36797 0.41649 0.00665  0.02716  -0.03327 143 SER B C   
5191 O O   . SER B 146 ? 0.42607 0.31822 0.40987 0.00315  0.02778  -0.06430 143 SER B O   
5192 C CB  . SER B 146 ? 0.30079 0.24187 0.30101 -0.01248 0.03699  -0.02078 143 SER B CB  
5193 O OG  . SER B 146 ? 0.29725 0.27563 0.31746 -0.01039 0.04468  0.03549  143 SER B OG  
5199 N N   . ASP B 147 ? 0.56235 0.50919 0.55054 0.00642  0.02031  -0.02169 144 ASP B N   
5200 C CA  . ASP B 147 ? 0.69231 0.70140 0.67667 0.00972  0.04309  -0.00579 144 ASP B CA  
5201 C C   . ASP B 147 ? 0.71801 0.75843 0.70034 0.00253  0.03360  -0.00605 144 ASP B C   
5202 O O   . ASP B 147 ? 0.72848 0.76733 0.70708 0.00526  0.04043  -0.00854 144 ASP B O   
5203 C CB  . ASP B 147 ? 0.78182 0.82353 0.76357 0.00275  0.07130  -0.00386 144 ASP B CB  
5204 C CG  . ASP B 147 ? 0.86341 0.93190 0.83978 -0.00229 0.09497  -0.00290 144 ASP B CG  
5205 O OD1 . ASP B 147 ? 0.88846 0.97712 0.86410 -0.00078 0.10413  -0.00400 144 ASP B OD1 
5206 O OD2 . ASP B 147 ? 0.88593 0.96083 0.86098 -0.00497 0.09806  0.00101  144 ASP B OD2 
5207 O OXT . ASP B 147 ? 0.72526 0.77808 0.70752 -0.00261 0.03537  -0.00564 144 ASP B OXT 
5212 C C1  . GOL C .   ? 0.30491 0.31931 0.30727 -0.04979 0.08453  -0.03961 201 GOL A C1  
5213 O O1  . GOL C .   ? 0.30530 0.36303 0.33616 -0.05120 0.09970  -0.01971 201 GOL A O1  
5214 C C2  . GOL C .   ? 0.34808 0.35830 0.31414 -0.01627 0.07874  -0.02965 201 GOL A C2  
5215 O O2  . GOL C .   ? 0.32391 0.32083 0.31631 -0.02603 0.09670  -0.03887 201 GOL A O2  
5216 C C3  . GOL C .   ? 0.33644 0.36154 0.32391 -0.00978 0.03836  -0.03740 201 GOL A C3  
5217 O O3  . GOL C .   ? 0.29260 0.33159 0.33082 0.03199  0.02521  -0.01391 201 GOL A O3  
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