data_9DSB
# 
_entry.id   9DSB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DSB         pdb_00009dsb 10.2210/pdb9dsb/pdb 
WWPDB D_1000288696 ?            ?                   
# 
_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       2025-05-28 
_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                        9DSB 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-26 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrzejj@anl.gov 
_pdbx_contact_author.name_first         Andrzej 
_pdbx_contact_author.name_last          Joachimiak 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2535-6209 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kim, Y.'                                                      1 ? 
'Maltseva, N.'                                                 2 ? 
'Endres, M.'                                                   3 ? 
'Kuhn, M.'                                                     4 ? 
'Joachimiak, A.'                                               5 ? 
'Center for Structural Biology of Infectious Diseases (CSBID)' 6 ? 
# 
_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 Spermin/spermidine N-Acetyltransferase from Enterococcus faecalis V583' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kim, Y.'                                                      1 ? 
primary 'Maltseva, N.'                                                 2 ? 
primary 'Endres, M.'                                                   3 ? 
primary 'Kuhn, M.'                                                     4 ? 
primary 'Joachimiak, A.'                                               5 ? 
primary 'Center for Structural Biology of Infectious Diseases (CSBID)' 6 ? 
# 
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 'Spermine/spermidine acetyltransferase' 17685.758 2   ? ? ? ? 
2 non-polymer syn 'ACETATE ION'                           59.044    1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                          35.453    11  ? ? ? ? 
4 non-polymer syn 'SODIUM ION'                            22.990    3   ? ? ? ? 
5 non-polymer nat 'POTASSIUM ION'                         39.098    1   ? ? ? ? 
6 water       nat water                                   18.015    162 ? ? ? ? 
# 
_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       
;SNAMEIHFEKVTSDNRKAVENLQVFAEQQAFIESMAENLKESDQFPEWESAGIYDGNQLIGYAMYGRWQDGRVWLDRFLI
DQRFQGQGYGKAACRLLMLKLIEKYQTNKLYLSVYDTNSSAIRLYQQLGFVFNGELDTNGERVMEWTHQNK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAMEIHFEKVTSDNRKAVENLQVFAEQQAFIESMAENLKESDQFPEWESAGIYDGNQLIGYAMYGRWQDGRVWLDRFLI
DQRFQGQGYGKAACRLLMLKLIEKYQTNKLYLSVYDTNSSAIRLYQQLGFVFNGELDTNGERVMEWTHQNK
;
_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 'ACETATE ION'   ACT 
3 'CHLORIDE ION'  CL  
4 'SODIUM ION'    NA  
5 'POTASSIUM ION' K   
6 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   MET n 
1 5   GLU n 
1 6   ILE n 
1 7   HIS n 
1 8   PHE n 
1 9   GLU n 
1 10  LYS n 
1 11  VAL n 
1 12  THR n 
1 13  SER n 
1 14  ASP n 
1 15  ASN n 
1 16  ARG n 
1 17  LYS n 
1 18  ALA n 
1 19  VAL n 
1 20  GLU n 
1 21  ASN n 
1 22  LEU n 
1 23  GLN n 
1 24  VAL n 
1 25  PHE n 
1 26  ALA n 
1 27  GLU n 
1 28  GLN n 
1 29  GLN n 
1 30  ALA n 
1 31  PHE n 
1 32  ILE n 
1 33  GLU n 
1 34  SER n 
1 35  MET n 
1 36  ALA n 
1 37  GLU n 
1 38  ASN n 
1 39  LEU n 
1 40  LYS n 
1 41  GLU n 
1 42  SER n 
1 43  ASP n 
1 44  GLN n 
1 45  PHE n 
1 46  PRO n 
1 47  GLU n 
1 48  TRP n 
1 49  GLU n 
1 50  SER n 
1 51  ALA n 
1 52  GLY n 
1 53  ILE n 
1 54  TYR n 
1 55  ASP n 
1 56  GLY n 
1 57  ASN n 
1 58  GLN n 
1 59  LEU n 
1 60  ILE n 
1 61  GLY n 
1 62  TYR n 
1 63  ALA n 
1 64  MET n 
1 65  TYR n 
1 66  GLY n 
1 67  ARG n 
1 68  TRP n 
1 69  GLN n 
1 70  ASP n 
1 71  GLY n 
1 72  ARG n 
1 73  VAL n 
1 74  TRP n 
1 75  LEU n 
1 76  ASP n 
1 77  ARG n 
1 78  PHE n 
1 79  LEU n 
1 80  ILE n 
1 81  ASP n 
1 82  GLN n 
1 83  ARG n 
1 84  PHE n 
1 85  GLN n 
1 86  GLY n 
1 87  GLN n 
1 88  GLY n 
1 89  TYR n 
1 90  GLY n 
1 91  LYS n 
1 92  ALA n 
1 93  ALA n 
1 94  CYS n 
1 95  ARG n 
1 96  LEU n 
1 97  LEU n 
1 98  MET n 
1 99  LEU n 
1 100 LYS n 
1 101 LEU n 
1 102 ILE n 
1 103 GLU n 
1 104 LYS n 
1 105 TYR n 
1 106 GLN n 
1 107 THR n 
1 108 ASN n 
1 109 LYS n 
1 110 LEU n 
1 111 TYR n 
1 112 LEU n 
1 113 SER n 
1 114 VAL n 
1 115 TYR n 
1 116 ASP n 
1 117 THR n 
1 118 ASN n 
1 119 SER n 
1 120 SER n 
1 121 ALA n 
1 122 ILE n 
1 123 ARG n 
1 124 LEU n 
1 125 TYR n 
1 126 GLN n 
1 127 GLN n 
1 128 LEU n 
1 129 GLY n 
1 130 PHE n 
1 131 VAL n 
1 132 PHE n 
1 133 ASN n 
1 134 GLY n 
1 135 GLU n 
1 136 LEU n 
1 137 ASP n 
1 138 THR n 
1 139 ASN n 
1 140 GLY n 
1 141 GLU n 
1 142 ARG n 
1 143 VAL n 
1 144 MET n 
1 145 GLU n 
1 146 TRP n 
1 147 THR n 
1 148 HIS n 
1 149 GLN n 
1 150 ASN n 
1 151 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   151 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EF_1086 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    V583 
_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      'Enterococcus faecalis V583' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     226185 
_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               'BL32 DE3' 
_entity_src_gen.pdbx_host_org_variant              gold 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMCSG53 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'   ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
K   non-polymer         . 'POTASSIUM ION' ? 'K 1'            39.098  
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 
NA  non-polymer         . 'SODIUM ION'    ? 'Na 1'           22.990  
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   SER 1   -2  ?   ?   ?   A . n 
A 1 2   ASN 2   -1  ?   ?   ?   A . n 
A 1 3   ALA 3   0   0   ALA ALA A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   GLU 5   2   2   GLU GLU A . n 
A 1 6   ILE 6   3   3   ILE ILE A . n 
A 1 7   HIS 7   4   4   HIS HIS A . n 
A 1 8   PHE 8   5   5   PHE PHE A . n 
A 1 9   GLU 9   6   6   GLU GLU A . n 
A 1 10  LYS 10  7   7   LYS LYS A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  THR 12  9   9   THR THR A . n 
A 1 13  SER 13  10  10  SER SER A . n 
A 1 14  ASP 14  11  11  ASP ASP A . n 
A 1 15  ASN 15  12  12  ASN ASN A . n 
A 1 16  ARG 16  13  13  ARG ARG A . n 
A 1 17  LYS 17  14  14  LYS LYS A . n 
A 1 18  ALA 18  15  15  ALA ALA A . n 
A 1 19  VAL 19  16  16  VAL VAL A . n 
A 1 20  GLU 20  17  17  GLU GLU A . n 
A 1 21  ASN 21  18  18  ASN ASN A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  GLN 23  20  20  GLN GLN A . n 
A 1 24  VAL 24  21  21  VAL VAL A . n 
A 1 25  PHE 25  22  22  PHE PHE A . n 
A 1 26  ALA 26  23  23  ALA ALA A . n 
A 1 27  GLU 27  24  24  GLU GLU A . n 
A 1 28  GLN 28  25  25  GLN GLN A . n 
A 1 29  GLN 29  26  26  GLN GLN A . n 
A 1 30  ALA 30  27  27  ALA ALA A . n 
A 1 31  PHE 31  28  28  PHE PHE A . n 
A 1 32  ILE 32  29  29  ILE ILE A . n 
A 1 33  GLU 33  30  30  GLU GLU A . n 
A 1 34  SER 34  31  31  SER SER A . n 
A 1 35  MET 35  32  32  MET MET A . n 
A 1 36  ALA 36  33  33  ALA ALA A . n 
A 1 37  GLU 37  34  34  GLU GLU A . n 
A 1 38  ASN 38  35  35  ASN ASN A . n 
A 1 39  LEU 39  36  36  LEU LEU A . n 
A 1 40  LYS 40  37  37  LYS LYS A . n 
A 1 41  GLU 41  38  38  GLU GLU A . n 
A 1 42  SER 42  39  39  SER SER A . n 
A 1 43  ASP 43  40  40  ASP ASP A . n 
A 1 44  GLN 44  41  41  GLN GLN A . n 
A 1 45  PHE 45  42  42  PHE PHE A . n 
A 1 46  PRO 46  43  43  PRO PRO A . n 
A 1 47  GLU 47  44  44  GLU GLU A . n 
A 1 48  TRP 48  45  45  TRP TRP A . n 
A 1 49  GLU 49  46  46  GLU GLU A . n 
A 1 50  SER 50  47  47  SER SER A . n 
A 1 51  ALA 51  48  48  ALA ALA A . n 
A 1 52  GLY 52  49  49  GLY GLY A . n 
A 1 53  ILE 53  50  50  ILE ILE A . n 
A 1 54  TYR 54  51  51  TYR TYR A . n 
A 1 55  ASP 55  52  52  ASP ASP A . n 
A 1 56  GLY 56  53  53  GLY GLY A . n 
A 1 57  ASN 57  54  54  ASN ASN A . n 
A 1 58  GLN 58  55  55  GLN GLN A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ILE 60  57  57  ILE ILE A . n 
A 1 61  GLY 61  58  58  GLY GLY A . n 
A 1 62  TYR 62  59  59  TYR TYR A . n 
A 1 63  ALA 63  60  60  ALA ALA A . n 
A 1 64  MET 64  61  61  MET MET A . n 
A 1 65  TYR 65  62  62  TYR TYR A . n 
A 1 66  GLY 66  63  63  GLY GLY A . n 
A 1 67  ARG 67  64  64  ARG ARG A . n 
A 1 68  TRP 68  65  65  TRP TRP A . n 
A 1 69  GLN 69  66  66  GLN GLN A . n 
A 1 70  ASP 70  67  67  ASP ASP A . n 
A 1 71  GLY 71  68  68  GLY GLY A . n 
A 1 72  ARG 72  69  69  ARG ARG A . n 
A 1 73  VAL 73  70  70  VAL VAL A . n 
A 1 74  TRP 74  71  71  TRP TRP A . n 
A 1 75  LEU 75  72  72  LEU LEU A . n 
A 1 76  ASP 76  73  73  ASP ASP A . n 
A 1 77  ARG 77  74  74  ARG ARG A . n 
A 1 78  PHE 78  75  75  PHE PHE A . n 
A 1 79  LEU 79  76  76  LEU LEU A . n 
A 1 80  ILE 80  77  77  ILE ILE A . n 
A 1 81  ASP 81  78  78  ASP ASP A . n 
A 1 82  GLN 82  79  79  GLN GLN A . n 
A 1 83  ARG 83  80  80  ARG ARG A . n 
A 1 84  PHE 84  81  81  PHE PHE A . n 
A 1 85  GLN 85  82  82  GLN GLN A . n 
A 1 86  GLY 86  83  83  GLY GLY A . n 
A 1 87  GLN 87  84  84  GLN GLN A . n 
A 1 88  GLY 88  85  85  GLY GLY A . n 
A 1 89  TYR 89  86  86  TYR TYR A . n 
A 1 90  GLY 90  87  87  GLY GLY A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  ALA 92  89  89  ALA ALA A . n 
A 1 93  ALA 93  90  90  ALA ALA A . n 
A 1 94  CYS 94  91  91  CYS CYS A . n 
A 1 95  ARG 95  92  92  ARG ARG A . n 
A 1 96  LEU 96  93  93  LEU LEU A . n 
A 1 97  LEU 97  94  94  LEU LEU A . n 
A 1 98  MET 98  95  95  MET MET A . n 
A 1 99  LEU 99  96  96  LEU LEU A . n 
A 1 100 LYS 100 97  97  LYS LYS A . n 
A 1 101 LEU 101 98  98  LEU LEU A . n 
A 1 102 ILE 102 99  99  ILE ILE A . n 
A 1 103 GLU 103 100 100 GLU GLU A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 TYR 105 102 102 TYR TYR A . n 
A 1 106 GLN 106 103 103 GLN GLN A . n 
A 1 107 THR 107 104 104 THR THR A . n 
A 1 108 ASN 108 105 105 ASN ASN A . n 
A 1 109 LYS 109 106 106 LYS LYS A . n 
A 1 110 LEU 110 107 107 LEU LEU A . n 
A 1 111 TYR 111 108 108 TYR TYR A . n 
A 1 112 LEU 112 109 109 LEU LEU A . n 
A 1 113 SER 113 110 110 SER SER A . n 
A 1 114 VAL 114 111 111 VAL VAL A . n 
A 1 115 TYR 115 112 112 TYR TYR A . n 
A 1 116 ASP 116 113 113 ASP ASP A . n 
A 1 117 THR 117 114 114 THR THR A . n 
A 1 118 ASN 118 115 115 ASN ASN A . n 
A 1 119 SER 119 116 116 SER SER A . n 
A 1 120 SER 120 117 117 SER SER A . n 
A 1 121 ALA 121 118 118 ALA ALA A . n 
A 1 122 ILE 122 119 119 ILE ILE A . n 
A 1 123 ARG 123 120 120 ARG ARG A . n 
A 1 124 LEU 124 121 121 LEU LEU A . n 
A 1 125 TYR 125 122 122 TYR TYR A . n 
A 1 126 GLN 126 123 123 GLN GLN A . n 
A 1 127 GLN 127 124 124 GLN GLN A . n 
A 1 128 LEU 128 125 125 LEU LEU A . n 
A 1 129 GLY 129 126 126 GLY GLY A . n 
A 1 130 PHE 130 127 127 PHE PHE A . n 
A 1 131 VAL 131 128 128 VAL VAL A . n 
A 1 132 PHE 132 129 129 PHE PHE A . n 
A 1 133 ASN 133 130 130 ASN ASN A . n 
A 1 134 GLY 134 131 131 GLY GLY A . n 
A 1 135 GLU 135 132 132 GLU GLU A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 ASP 137 134 134 ASP ASP A . n 
A 1 138 THR 138 135 135 THR THR A . n 
A 1 139 ASN 139 136 136 ASN ASN A . n 
A 1 140 GLY 140 137 137 GLY GLY A . n 
A 1 141 GLU 141 138 138 GLU GLU A . n 
A 1 142 ARG 142 139 139 ARG ARG A . n 
A 1 143 VAL 143 140 140 VAL VAL A . n 
A 1 144 MET 144 141 141 MET MET A . n 
A 1 145 GLU 145 142 142 GLU GLU A . n 
A 1 146 TRP 146 143 143 TRP TRP A . n 
A 1 147 THR 147 144 144 THR THR A . n 
A 1 148 HIS 148 145 145 HIS HIS A . n 
A 1 149 GLN 149 146 146 GLN GLN A . n 
A 1 150 ASN 150 147 ?   ?   ?   A . n 
A 1 151 LYS 151 148 ?   ?   ?   A . n 
B 1 1   SER 1   -2  ?   ?   ?   B . n 
B 1 2   ASN 2   -1  ?   ?   ?   B . n 
B 1 3   ALA 3   0   0   ALA ALA B . n 
B 1 4   MET 4   1   1   MET MET B . n 
B 1 5   GLU 5   2   2   GLU GLU B . n 
B 1 6   ILE 6   3   3   ILE ILE B . n 
B 1 7   HIS 7   4   4   HIS HIS B . n 
B 1 8   PHE 8   5   5   PHE PHE B . n 
B 1 9   GLU 9   6   6   GLU GLU B . n 
B 1 10  LYS 10  7   7   LYS LYS B . n 
B 1 11  VAL 11  8   8   VAL VAL B . n 
B 1 12  THR 12  9   9   THR THR B . n 
B 1 13  SER 13  10  10  SER SER B . n 
B 1 14  ASP 14  11  11  ASP ASP B . n 
B 1 15  ASN 15  12  12  ASN ASN B . n 
B 1 16  ARG 16  13  13  ARG ARG B . n 
B 1 17  LYS 17  14  14  LYS LYS B . n 
B 1 18  ALA 18  15  15  ALA ALA B . n 
B 1 19  VAL 19  16  16  VAL VAL B . n 
B 1 20  GLU 20  17  17  GLU GLU B . n 
B 1 21  ASN 21  18  18  ASN ASN B . n 
B 1 22  LEU 22  19  19  LEU LEU B . n 
B 1 23  GLN 23  20  20  GLN GLN B . n 
B 1 24  VAL 24  21  21  VAL VAL B . n 
B 1 25  PHE 25  22  22  PHE PHE B . n 
B 1 26  ALA 26  23  23  ALA ALA B . n 
B 1 27  GLU 27  24  24  GLU GLU B . n 
B 1 28  GLN 28  25  25  GLN GLN B . n 
B 1 29  GLN 29  26  26  GLN GLN B . n 
B 1 30  ALA 30  27  27  ALA ALA B . n 
B 1 31  PHE 31  28  28  PHE PHE B . n 
B 1 32  ILE 32  29  29  ILE ILE B . n 
B 1 33  GLU 33  30  30  GLU GLU B . n 
B 1 34  SER 34  31  31  SER SER B . n 
B 1 35  MET 35  32  32  MET MET B . n 
B 1 36  ALA 36  33  33  ALA ALA B . n 
B 1 37  GLU 37  34  34  GLU GLU B . n 
B 1 38  ASN 38  35  35  ASN ASN B . n 
B 1 39  LEU 39  36  36  LEU LEU B . n 
B 1 40  LYS 40  37  37  LYS LYS B . n 
B 1 41  GLU 41  38  38  GLU GLU B . n 
B 1 42  SER 42  39  39  SER SER B . n 
B 1 43  ASP 43  40  40  ASP ASP B . n 
B 1 44  GLN 44  41  41  GLN GLN B . n 
B 1 45  PHE 45  42  42  PHE PHE B . n 
B 1 46  PRO 46  43  43  PRO PRO B . n 
B 1 47  GLU 47  44  44  GLU GLU B . n 
B 1 48  TRP 48  45  45  TRP TRP B . n 
B 1 49  GLU 49  46  46  GLU GLU B . n 
B 1 50  SER 50  47  47  SER SER B . n 
B 1 51  ALA 51  48  48  ALA ALA B . n 
B 1 52  GLY 52  49  49  GLY GLY B . n 
B 1 53  ILE 53  50  50  ILE ILE B . n 
B 1 54  TYR 54  51  51  TYR TYR B . n 
B 1 55  ASP 55  52  52  ASP ASP B . n 
B 1 56  GLY 56  53  53  GLY GLY B . n 
B 1 57  ASN 57  54  54  ASN ASN B . n 
B 1 58  GLN 58  55  55  GLN GLN B . n 
B 1 59  LEU 59  56  56  LEU LEU B . n 
B 1 60  ILE 60  57  57  ILE ILE B . n 
B 1 61  GLY 61  58  58  GLY GLY B . n 
B 1 62  TYR 62  59  59  TYR TYR B . n 
B 1 63  ALA 63  60  60  ALA ALA B . n 
B 1 64  MET 64  61  61  MET MET B . n 
B 1 65  TYR 65  62  62  TYR TYR B . n 
B 1 66  GLY 66  63  63  GLY GLY B . n 
B 1 67  ARG 67  64  64  ARG ARG B . n 
B 1 68  TRP 68  65  65  TRP TRP B . n 
B 1 69  GLN 69  66  66  GLN GLN B . n 
B 1 70  ASP 70  67  67  ASP ASP B . n 
B 1 71  GLY 71  68  68  GLY GLY B . n 
B 1 72  ARG 72  69  69  ARG ARG B . n 
B 1 73  VAL 73  70  70  VAL VAL B . n 
B 1 74  TRP 74  71  71  TRP TRP B . n 
B 1 75  LEU 75  72  72  LEU LEU B . n 
B 1 76  ASP 76  73  73  ASP ASP B . n 
B 1 77  ARG 77  74  74  ARG ARG B . n 
B 1 78  PHE 78  75  75  PHE PHE B . n 
B 1 79  LEU 79  76  76  LEU LEU B . n 
B 1 80  ILE 80  77  77  ILE ILE B . n 
B 1 81  ASP 81  78  78  ASP ASP B . n 
B 1 82  GLN 82  79  79  GLN GLN B . n 
B 1 83  ARG 83  80  80  ARG ARG B . n 
B 1 84  PHE 84  81  81  PHE PHE B . n 
B 1 85  GLN 85  82  82  GLN GLN B . n 
B 1 86  GLY 86  83  83  GLY GLY B . n 
B 1 87  GLN 87  84  84  GLN GLN B . n 
B 1 88  GLY 88  85  85  GLY GLY B . n 
B 1 89  TYR 89  86  86  TYR TYR B . n 
B 1 90  GLY 90  87  87  GLY GLY B . n 
B 1 91  LYS 91  88  88  LYS LYS B . n 
B 1 92  ALA 92  89  89  ALA ALA B . n 
B 1 93  ALA 93  90  90  ALA ALA B . n 
B 1 94  CYS 94  91  91  CYS CYS B . n 
B 1 95  ARG 95  92  92  ARG ARG B . n 
B 1 96  LEU 96  93  93  LEU LEU B . n 
B 1 97  LEU 97  94  94  LEU LEU B . n 
B 1 98  MET 98  95  95  MET MET B . n 
B 1 99  LEU 99  96  96  LEU LEU B . n 
B 1 100 LYS 100 97  97  LYS LYS B . n 
B 1 101 LEU 101 98  98  LEU LEU B . n 
B 1 102 ILE 102 99  99  ILE ILE B . n 
B 1 103 GLU 103 100 100 GLU GLU B . n 
B 1 104 LYS 104 101 101 LYS LYS B . n 
B 1 105 TYR 105 102 102 TYR TYR B . n 
B 1 106 GLN 106 103 103 GLN GLN B . n 
B 1 107 THR 107 104 104 THR THR B . n 
B 1 108 ASN 108 105 105 ASN ASN B . n 
B 1 109 LYS 109 106 106 LYS LYS B . n 
B 1 110 LEU 110 107 107 LEU LEU B . n 
B 1 111 TYR 111 108 108 TYR TYR B . n 
B 1 112 LEU 112 109 109 LEU LEU B . n 
B 1 113 SER 113 110 110 SER SER B . n 
B 1 114 VAL 114 111 111 VAL VAL B . n 
B 1 115 TYR 115 112 112 TYR TYR B . n 
B 1 116 ASP 116 113 113 ASP ASP B . n 
B 1 117 THR 117 114 114 THR THR B . n 
B 1 118 ASN 118 115 115 ASN ASN B . n 
B 1 119 SER 119 116 116 SER SER B . n 
B 1 120 SER 120 117 117 SER SER B . n 
B 1 121 ALA 121 118 118 ALA ALA B . n 
B 1 122 ILE 122 119 119 ILE ILE B . n 
B 1 123 ARG 123 120 120 ARG ARG B . n 
B 1 124 LEU 124 121 121 LEU LEU B . n 
B 1 125 TYR 125 122 122 TYR TYR B . n 
B 1 126 GLN 126 123 123 GLN GLN B . n 
B 1 127 GLN 127 124 124 GLN GLN B . n 
B 1 128 LEU 128 125 125 LEU LEU B . n 
B 1 129 GLY 129 126 126 GLY GLY B . n 
B 1 130 PHE 130 127 127 PHE PHE B . n 
B 1 131 VAL 131 128 128 VAL VAL B . n 
B 1 132 PHE 132 129 129 PHE PHE B . n 
B 1 133 ASN 133 130 130 ASN ASN B . n 
B 1 134 GLY 134 131 131 GLY GLY B . n 
B 1 135 GLU 135 132 132 GLU GLU B . n 
B 1 136 LEU 136 133 133 LEU LEU B . n 
B 1 137 ASP 137 134 134 ASP ASP B . n 
B 1 138 THR 138 135 135 THR THR B . n 
B 1 139 ASN 139 136 136 ASN ASN B . n 
B 1 140 GLY 140 137 137 GLY GLY B . n 
B 1 141 GLU 141 138 138 GLU GLU B . n 
B 1 142 ARG 142 139 139 ARG ARG B . n 
B 1 143 VAL 143 140 140 VAL VAL B . n 
B 1 144 MET 144 141 141 MET MET B . n 
B 1 145 GLU 145 142 142 GLU GLU B . n 
B 1 146 TRP 146 143 143 TRP TRP B . n 
B 1 147 THR 147 144 144 THR THR B . n 
B 1 148 HIS 148 145 145 HIS HIS B . n 
B 1 149 GLN 149 146 ?   ?   ?   B . n 
B 1 150 ASN 150 147 ?   ?   ?   B . n 
B 1 151 LYS 151 148 ?   ?   ?   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 ACT 1  201 201 ACT ACT A . 
D 3 CL  1  202 2   CL  CL  A . 
E 3 CL  1  203 4   CL  CL  A . 
F 3 CL  1  204 10  CL  CL  A . 
G 3 CL  1  205 13  CL  CL  A . 
H 4 NA  1  206 3   NA  NA  A . 
I 5 K   1  207 1   K   K   A . 
J 3 CL  1  201 1   CL  CL  B . 
K 3 CL  1  202 3   CL  CL  B . 
L 3 CL  1  203 7   CL  CL  B . 
M 3 CL  1  204 8   CL  CL  B . 
N 3 CL  1  205 9   CL  CL  B . 
O 3 CL  1  206 11  CL  CL  B . 
P 3 CL  1  207 12  CL  CL  B . 
Q 4 NA  1  208 1   NA  NA  B . 
R 4 NA  1  209 2   NA  NA  B . 
S 6 HOH 1  301 193 HOH HOH A . 
S 6 HOH 2  302 188 HOH HOH A . 
S 6 HOH 3  303 233 HOH HOH A . 
S 6 HOH 4  304 158 HOH HOH A . 
S 6 HOH 5  305 91  HOH HOH A . 
S 6 HOH 6  306 65  HOH HOH A . 
S 6 HOH 7  307 31  HOH HOH A . 
S 6 HOH 8  308 45  HOH HOH A . 
S 6 HOH 9  309 199 HOH HOH A . 
S 6 HOH 10 310 63  HOH HOH A . 
S 6 HOH 11 311 145 HOH HOH A . 
S 6 HOH 12 312 106 HOH HOH A . 
S 6 HOH 13 313 212 HOH HOH A . 
S 6 HOH 14 314 35  HOH HOH A . 
S 6 HOH 15 315 217 HOH HOH A . 
S 6 HOH 16 316 114 HOH HOH A . 
S 6 HOH 17 317 70  HOH HOH A . 
S 6 HOH 18 318 29  HOH HOH A . 
S 6 HOH 19 319 9   HOH HOH A . 
S 6 HOH 20 320 60  HOH HOH A . 
S 6 HOH 21 321 19  HOH HOH A . 
S 6 HOH 22 322 130 HOH HOH A . 
S 6 HOH 23 323 175 HOH HOH A . 
S 6 HOH 24 324 202 HOH HOH A . 
S 6 HOH 25 325 163 HOH HOH A . 
S 6 HOH 26 326 194 HOH HOH A . 
S 6 HOH 27 327 237 HOH HOH A . 
S 6 HOH 28 328 165 HOH HOH A . 
S 6 HOH 29 329 51  HOH HOH A . 
S 6 HOH 30 330 166 HOH HOH A . 
S 6 HOH 31 331 57  HOH HOH A . 
S 6 HOH 32 332 215 HOH HOH A . 
S 6 HOH 33 333 61  HOH HOH A . 
S 6 HOH 34 334 30  HOH HOH A . 
S 6 HOH 35 335 148 HOH HOH A . 
S 6 HOH 36 336 67  HOH HOH A . 
S 6 HOH 37 337 46  HOH HOH A . 
S 6 HOH 38 338 3   HOH HOH A . 
S 6 HOH 39 339 16  HOH HOH A . 
S 6 HOH 40 340 187 HOH HOH A . 
S 6 HOH 41 341 154 HOH HOH A . 
S 6 HOH 42 342 44  HOH HOH A . 
S 6 HOH 43 343 197 HOH HOH A . 
S 6 HOH 44 344 97  HOH HOH A . 
S 6 HOH 45 345 83  HOH HOH A . 
S 6 HOH 46 346 143 HOH HOH A . 
S 6 HOH 47 347 22  HOH HOH A . 
S 6 HOH 48 348 180 HOH HOH A . 
S 6 HOH 49 349 94  HOH HOH A . 
S 6 HOH 50 350 174 HOH HOH A . 
S 6 HOH 51 351 203 HOH HOH A . 
S 6 HOH 52 352 127 HOH HOH A . 
S 6 HOH 53 353 205 HOH HOH A . 
S 6 HOH 54 354 117 HOH HOH A . 
S 6 HOH 55 355 184 HOH HOH A . 
S 6 HOH 56 356 66  HOH HOH A . 
S 6 HOH 57 357 20  HOH HOH A . 
S 6 HOH 58 358 213 HOH HOH A . 
S 6 HOH 59 359 176 HOH HOH A . 
S 6 HOH 60 360 54  HOH HOH A . 
S 6 HOH 61 361 24  HOH HOH A . 
S 6 HOH 62 362 59  HOH HOH A . 
S 6 HOH 63 363 115 HOH HOH A . 
S 6 HOH 64 364 214 HOH HOH A . 
S 6 HOH 65 365 10  HOH HOH A . 
S 6 HOH 66 366 85  HOH HOH A . 
S 6 HOH 67 367 224 HOH HOH A . 
S 6 HOH 68 368 152 HOH HOH A . 
S 6 HOH 69 369 118 HOH HOH A . 
S 6 HOH 70 370 164 HOH HOH A . 
S 6 HOH 71 371 228 HOH HOH A . 
S 6 HOH 72 372 144 HOH HOH A . 
S 6 HOH 73 373 235 HOH HOH A . 
S 6 HOH 74 374 159 HOH HOH A . 
S 6 HOH 75 375 55  HOH HOH A . 
T 6 HOH 1  301 225 HOH HOH B . 
T 6 HOH 2  302 119 HOH HOH B . 
T 6 HOH 3  303 33  HOH HOH B . 
T 6 HOH 4  304 28  HOH HOH B . 
T 6 HOH 5  305 32  HOH HOH B . 
T 6 HOH 6  306 25  HOH HOH B . 
T 6 HOH 7  307 92  HOH HOH B . 
T 6 HOH 8  308 8   HOH HOH B . 
T 6 HOH 9  309 238 HOH HOH B . 
T 6 HOH 10 310 71  HOH HOH B . 
T 6 HOH 11 311 201 HOH HOH B . 
T 6 HOH 12 312 21  HOH HOH B . 
T 6 HOH 13 313 15  HOH HOH B . 
T 6 HOH 14 314 140 HOH HOH B . 
T 6 HOH 15 315 39  HOH HOH B . 
T 6 HOH 16 316 12  HOH HOH B . 
T 6 HOH 17 317 207 HOH HOH B . 
T 6 HOH 18 318 52  HOH HOH B . 
T 6 HOH 19 319 86  HOH HOH B . 
T 6 HOH 20 320 98  HOH HOH B . 
T 6 HOH 21 321 48  HOH HOH B . 
T 6 HOH 22 322 75  HOH HOH B . 
T 6 HOH 23 323 218 HOH HOH B . 
T 6 HOH 24 324 122 HOH HOH B . 
T 6 HOH 25 325 11  HOH HOH B . 
T 6 HOH 26 326 123 HOH HOH B . 
T 6 HOH 27 327 157 HOH HOH B . 
T 6 HOH 28 328 84  HOH HOH B . 
T 6 HOH 29 329 178 HOH HOH B . 
T 6 HOH 30 330 200 HOH HOH B . 
T 6 HOH 31 331 190 HOH HOH B . 
T 6 HOH 32 332 204 HOH HOH B . 
T 6 HOH 33 333 62  HOH HOH B . 
T 6 HOH 34 334 27  HOH HOH B . 
T 6 HOH 35 335 87  HOH HOH B . 
T 6 HOH 36 336 196 HOH HOH B . 
T 6 HOH 37 337 192 HOH HOH B . 
T 6 HOH 38 338 239 HOH HOH B . 
T 6 HOH 39 339 95  HOH HOH B . 
T 6 HOH 40 340 56  HOH HOH B . 
T 6 HOH 41 341 195 HOH HOH B . 
T 6 HOH 42 342 112 HOH HOH B . 
T 6 HOH 43 343 128 HOH HOH B . 
T 6 HOH 44 344 110 HOH HOH B . 
T 6 HOH 45 345 198 HOH HOH B . 
T 6 HOH 46 346 90  HOH HOH B . 
T 6 HOH 47 347 216 HOH HOH B . 
T 6 HOH 48 348 226 HOH HOH B . 
T 6 HOH 49 349 206 HOH HOH B . 
T 6 HOH 50 350 147 HOH HOH B . 
T 6 HOH 51 351 74  HOH HOH B . 
T 6 HOH 52 352 211 HOH HOH B . 
T 6 HOH 53 353 183 HOH HOH B . 
T 6 HOH 54 354 151 HOH HOH B . 
T 6 HOH 55 355 186 HOH HOH B . 
T 6 HOH 56 356 185 HOH HOH B . 
T 6 HOH 57 357 42  HOH HOH B . 
T 6 HOH 58 358 222 HOH HOH B . 
T 6 HOH 59 359 160 HOH HOH B . 
T 6 HOH 60 360 23  HOH HOH B . 
T 6 HOH 61 361 64  HOH HOH B . 
T 6 HOH 62 362 156 HOH HOH B . 
T 6 HOH 63 363 155 HOH HOH B . 
T 6 HOH 64 364 168 HOH HOH B . 
T 6 HOH 65 365 210 HOH HOH B . 
T 6 HOH 66 366 81  HOH HOH B . 
T 6 HOH 67 367 209 HOH HOH B . 
T 6 HOH 68 368 189 HOH HOH B . 
T 6 HOH 69 369 236 HOH HOH B . 
T 6 HOH 70 370 102 HOH HOH B . 
T 6 HOH 71 371 234 HOH HOH B . 
T 6 HOH 72 372 131 HOH HOH B . 
T 6 HOH 73 373 220 HOH HOH B . 
T 6 HOH 74 374 93  HOH HOH B . 
T 6 HOH 75 375 191 HOH HOH B . 
T 6 HOH 76 376 221 HOH HOH B . 
T 6 HOH 77 377 38  HOH HOH B . 
T 6 HOH 78 378 223 HOH HOH B . 
T 6 HOH 79 379 229 HOH HOH B . 
T 6 HOH 80 380 170 HOH HOH B . 
T 6 HOH 81 381 126 HOH HOH B . 
T 6 HOH 82 382 53  HOH HOH B . 
T 6 HOH 83 383 232 HOH HOH B . 
T 6 HOH 84 384 138 HOH HOH B . 
T 6 HOH 85 385 231 HOH HOH B . 
T 6 HOH 86 386 230 HOH HOH B . 
T 6 HOH 87 387 219 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0430    1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2-5419 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .           5 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .           6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DSB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.296 
_cell.length_a_esd                 ? 
_cell.length_b                     90.296 
_cell.length_b_esd                 ? 
_cell.length_c                     34.775 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9DSB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                143 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 3' 
_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                   9DSB 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M sodium acetate pH 4.5, 3 M sodium Chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-01 
_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   0.97946 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DSB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     47864 
_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                           94.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.507 
_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                                0.052 
_reflns.pdbx_Rpim_I_all                                0.016 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       466493 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.050 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.50 1.53  ? ? ? ? ? ? 1758 ? ? ? ? ? ? ? ? ? ? ? 8.2  0.462 ? ? 0.716 0.240 ? 1  1 0.885 0.969 ? 70.0  ? 0.673 ? ? ? ? ? ? ? ? ? 
1.53 1.55  ? ? ? ? ? ? 1882 ? ? ? ? ? ? ? ? ? ? ? 8.2  0.474 ? ? 0.683 0.229 ? 2  1 0.913 0.977 ? 74.2  ? 0.642 ? ? ? ? ? ? ? ? ? 
1.55 1.58  ? ? ? ? ? ? 2013 ? ? ? ? ? ? ? ? ? ? ? 7.8  0.471 ? ? 0.658 0.225 ? 3  1 0.903 0.974 ? 78.1  ? 0.617 ? ? ? ? ? ? ? ? ? 
1.58 1.62  ? ? ? ? ? ? 2114 ? ? ? ? ? ? ? ? ? ? ? 8.6  0.494 ? ? 0.511 0.166 ? 4  1 0.952 0.988 ? 85.7  ? 0.482 ? ? ? ? ? ? ? ? ? 
1.62 1.65  ? ? ? ? ? ? 2358 ? ? ? ? ? ? ? ? ? ? ? 8.7  0.489 ? ? 0.485 0.158 ? 5  1 0.959 0.990 ? 91.9  ? 0.458 ? ? ? ? ? ? ? ? ? 
1.65 1.69  ? ? ? ? ? ? 2375 ? ? ? ? ? ? ? ? ? ? ? 9.1  0.479 ? ? 0.431 0.139 ? 6  1 0.962 0.990 ? 96.0  ? 0.407 ? ? ? ? ? ? ? ? ? 
1.69 1.73  ? ? ? ? ? ? 2581 ? ? ? ? ? ? ? ? ? ? ? 9.2  0.498 ? ? 0.370 0.119 ? 7  1 0.978 0.994 ? 98.9  ? 0.349 ? ? ? ? ? ? ? ? ? 
1.73 1.78  ? ? ? ? ? ? 2487 ? ? ? ? ? ? ? ? ? ? ? 9.7  0.494 ? ? 0.336 0.107 ? 8  1 0.984 0.996 ? 99.8  ? 0.318 ? ? ? ? ? ? ? ? ? 
1.78 1.83  ? ? ? ? ? ? 2543 ? ? ? ? ? ? ? ? ? ? ? 9.7  0.499 ? ? 0.273 0.087 ? 9  1 0.989 0.997 ? 99.7  ? 0.259 ? ? ? ? ? ? ? ? ? 
1.83 1.89  ? ? ? ? ? ? 2496 ? ? ? ? ? ? ? ? ? ? ? 9.1  0.514 ? ? 0.219 0.072 ? 10 1 0.992 0.998 ? 99.8  ? 0.207 ? ? ? ? ? ? ? ? ? 
1.89 1.96  ? ? ? ? ? ? 2547 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.497 ? ? 0.174 0.053 ? 11 1 0.996 0.999 ? 99.9  ? 0.166 ? ? ? ? ? ? ? ? ? 
1.96 2.04  ? ? ? ? ? ? 2532 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.500 ? ? 0.130 0.040 ? 12 1 0.997 0.999 ? 99.9  ? 0.123 ? ? ? ? ? ? ? ? ? 
2.04 2.13  ? ? ? ? ? ? 2489 ? ? ? ? ? ? ? ? ? ? ? 10.5 0.495 ? ? 0.096 0.029 ? 13 1 0.998 1.000 ? 99.6  ? 0.091 ? ? ? ? ? ? ? ? ? 
2.13 2.24  ? ? ? ? ? ? 2556 ? ? ? ? ? ? ? ? ? ? ? 10.4 0.478 ? ? 0.075 0.023 ? 14 1 0.999 1.000 ? 99.8  ? 0.071 ? ? ? ? ? ? ? ? ? 
2.24 2.38  ? ? ? ? ? ? 2508 ? ? ? ? ? ? ? ? ? ? ? 9.7  0.469 ? ? 0.061 0.019 ? 15 1 0.999 1.000 ? 99.6  ? 0.058 ? ? ? ? ? ? ? ? ? 
2.38 2.56  ? ? ? ? ? ? 2512 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.455 ? ? 0.049 0.015 ? 16 1 0.999 1.000 ? 99.8  ? 0.047 ? ? ? ? ? ? ? ? ? 
2.56 2.82  ? ? ? ? ? ? 2550 ? ? ? ? ? ? ? ? ? ? ? 10.9 0.463 ? ? 0.043 0.013 ? 17 1 0.999 1.000 ? 100.0 ? 0.041 ? ? ? ? ? ? ? ? ? 
2.82 3.23  ? ? ? ? ? ? 2527 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.467 ? ? 0.035 0.011 ? 18 1 1.000 1.000 ? 99.7  ? 0.033 ? ? ? ? ? ? ? ? ? 
3.23 4.07  ? ? ? ? ? ? 2518 ? ? ? ? ? ? ? ? ? ? ? 10.2 0.587 ? ? 0.033 0.010 ? 19 1 0.999 1.000 ? 99.2  ? 0.032 ? ? ? ? ? ? ? ? ? 
4.07 50.00 ? ? ? ? ? ? 2518 ? ? ? ? ? ? ? ? ? ? ? 10.8 0.782 ? ? 0.037 0.011 ? 20 1 0.999 1.000 ? 99.5  ? 0.035 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.34 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.34 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.69 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.637 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.968 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DSB 
_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                            1.50 
_refine.ls_d_res_low                             39.10 
_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                     45414 
_refine.ls_number_reflns_R_free                  2447 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.38 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16501 
_refine.ls_R_factor_R_free                       0.20358 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16288 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.019 
_refine.pdbx_overall_ESU_R_Free                  0.016 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.506 
_refine.overall_SU_ML                            0.059 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        39.10 
_refine_hist.number_atoms_solvent             162 
_refine_hist.number_atoms_total               2600 
_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        2419 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         19 
_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' ? 0.002  0.012  2589 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2377 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.964  1.823  3496 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.373  1.775  5446 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.251  5.000  313  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 3.963  5.000  18   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.626 10.000 466  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.049  0.200  349  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  3219 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  689  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.597  3.157  1229 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.595  3.157  1227 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.866  5.665  1549 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.864  5.665  1550 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.108  3.374  1360 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.107  3.374  1361 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.095  6.155  1948 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.587 33.13  3077 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.276 32.82  3047 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 1.289  3.000  4966 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.501 
_refine_ls_shell.d_res_low                        1.540 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             180 
_refine_ls_shell.number_reflns_R_work             2442 
_refine_ls_shell.percent_reflns_obs               70.03 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.236 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.334 
# 
_struct.entry_id                     9DSB 
_struct.title                        'Crystal Structure of Spermin/spermidine N-Acetyltransferase from Enterococcus faecalis V583' 
_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        9DSB 
_struct_keywords.text            
;GCN5-related N-acetyltransferase (GNAT), polyamine acetyltransferase, Structural Genomics, Center for Structural Biology of Infectious Diseases, CSBID, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 6 ? 
T N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q836M4_ENTFA 
_struct_ref.pdbx_db_accession          Q836M4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEIHFEKVTSDNRKAVENLQVFAEQQAFIESMAENLKESDQFPEWESAGIYDGNQLIGYAMYGRWQDGRVWLDRFLIDQR
FQGQGYGKAACRLLMLKLIEKYQTNKLYLSVYDTNSSAIRLYQQLGFVFNGELDTNGERVMEWTHQNK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DSB A 4 ? 151 ? Q836M4 1 ? 148 ? 1 148 
2 1 9DSB B 4 ? 151 ? Q836M4 1 ? 148 ? 1 148 
# 
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 9DSB SER A 1 ? UNP Q836M4 ? ? 'expression tag' -2 1 
1 9DSB ASN A 2 ? UNP Q836M4 ? ? 'expression tag' -1 2 
1 9DSB ALA A 3 ? UNP Q836M4 ? ? 'expression tag' 0  3 
2 9DSB SER B 1 ? UNP Q836M4 ? ? 'expression tag' -2 4 
2 9DSB ASN B 2 ? UNP Q836M4 ? ? 'expression tag' -1 5 
2 9DSB ALA B 3 ? UNP Q836M4 ? ? 'expression tag' 0  6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 15  ? ASN A 21  ? ASN A 12  ASN A 18  1 ? 7  
HELX_P HELX_P2  AA2 GLU A 27  ? PHE A 45  ? GLU A 24  PHE A 42  1 ? 19 
HELX_P HELX_P3  AA3 GLN A 82  ? GLN A 85  ? GLN A 79  GLN A 82  5 ? 4  
HELX_P HELX_P4  AA4 GLY A 88  ? TYR A 105 ? GLY A 85  TYR A 102 1 ? 18 
HELX_P HELX_P5  AA5 ASN A 118 ? LEU A 128 ? ASN A 115 LEU A 125 1 ? 11 
HELX_P HELX_P6  AA6 ASN B 15  ? ASN B 21  ? ASN B 12  ASN B 18  1 ? 7  
HELX_P HELX_P7  AA7 GLU B 27  ? PHE B 45  ? GLU B 24  PHE B 42  1 ? 19 
HELX_P HELX_P8  AA8 GLN B 82  ? GLN B 85  ? GLN B 79  GLN B 82  5 ? 4  
HELX_P HELX_P9  AA9 GLY B 88  ? TYR B 105 ? GLY B 85  TYR B 102 1 ? 18 
HELX_P HELX_P10 AB1 ASN B 118 ? GLY B 129 ? ASN B 115 GLY B 126 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 34  OG  ? ? ? 1_555 I K   . K  ? ? A SER 31  A K   207 1_555 ? ? ? ? ? ? ? 2.635 ? ? 
metalc2  metalc ? ? A SER 113 O   ? ? ? 1_555 H NA  . NA ? ? A SER 110 A NA  206 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc3  metalc ? ? A SER 113 OG  ? ? ? 1_555 H NA  . NA ? ? A SER 110 A NA  206 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc4  metalc ? ? A GLU 141 OE1 ? ? ? 1_555 H NA  . NA ? ? A GLU 138 A NA  206 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc5  metalc ? ? H NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? A NA  206 A HOH 361 1_555 ? ? ? ? ? ? ? 2.474 ? ? 
metalc6  metalc ? ? H NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? A NA  206 B HOH 311 1_555 ? ? ? ? ? ? ? 2.523 ? ? 
metalc7  metalc ? ? H NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? A NA  206 B HOH 321 1_555 ? ? ? ? ? ? ? 2.700 ? ? 
metalc8  metalc ? ? S HOH .   O   ? ? ? 1_555 R NA  . NA ? ? A HOH 348 B NA  209 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc9  metalc ? ? B SER 42  O   ? ? ? 1_555 Q NA  . NA ? ? B SER 39  B NA  208 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc10 metalc ? ? B PHE 45  O   ? ? ? 1_555 Q NA  . NA ? ? B PHE 42  B NA  208 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc11 metalc ? ? B TRP 48  O   ? ? ? 1_555 Q NA  . NA ? ? B TRP 45  B NA  208 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc12 metalc ? ? B SER 113 O   ? ? ? 1_555 R NA  . NA ? ? B SER 110 B NA  209 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
metalc13 metalc ? ? B SER 113 OG  ? ? ? 1_555 R NA  . NA ? ? B SER 110 B NA  209 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc14 metalc ? ? B GLU 141 OE1 ? ? ? 1_555 R NA  . NA ? ? B GLU 138 B NA  209 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc15 metalc ? ? Q NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? B NA  208 B HOH 349 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc16 metalc ? ? Q NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? B NA  208 B HOH 376 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc17 metalc ? ? R NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? B NA  209 B HOH 358 1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc18 metalc ? ? R NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? B NA  209 B HOH 360 1_555 ? ? ? ? ? ? ? 2.657 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 OG  ? A SER 113 ? A SER 110 ? 1_555 86.0  ? 
2  O   ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 OE1 ? A GLU 141 ? A GLU 138 ? 1_555 82.6  ? 
3  OG  ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 OE1 ? A GLU 141 ? A GLU 138 ? 1_555 86.3  ? 
4  O   ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? S HOH .   ? A HOH 361 ? 1_555 96.8  ? 
5  OG  ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? S HOH .   ? A HOH 361 ? 1_555 85.1  ? 
6  OE1 ? A GLU 141 ? A GLU 138 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? S HOH .   ? A HOH 361 ? 1_555 171.3 ? 
7  O   ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 311 ? 1_555 174.6 ? 
8  OG  ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 311 ? 1_555 88.9  ? 
9  OE1 ? A GLU 141 ? A GLU 138 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 311 ? 1_555 95.2  ? 
10 O   ? S HOH .   ? A HOH 361 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 311 ? 1_555 84.5  ? 
11 O   ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 321 ? 1_555 90.7  ? 
12 OG  ? A SER 113 ? A SER 110 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 321 ? 1_555 163.4 ? 
13 OE1 ? A GLU 141 ? A GLU 138 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 321 ? 1_555 77.2  ? 
14 O   ? S HOH .   ? A HOH 361 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 321 ? 1_555 111.5 ? 
15 O   ? T HOH .   ? B HOH 311 ? 1_555 NA ? H NA . ? A NA 206 ? 1_555 O   ? T HOH .   ? B HOH 321 ? 1_555 93.7  ? 
16 O   ? S HOH .   ? A HOH 348 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? B SER 113 ? B SER 110 ? 1_555 176.4 ? 
17 O   ? S HOH .   ? A HOH 348 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 OG  ? B SER 113 ? B SER 110 ? 1_555 101.2 ? 
18 O   ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 OG  ? B SER 113 ? B SER 110 ? 1_555 82.4  ? 
19 O   ? S HOH .   ? A HOH 348 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 OE1 ? B GLU 141 ? B GLU 138 ? 1_555 82.8  ? 
20 O   ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 OE1 ? B GLU 141 ? B GLU 138 ? 1_555 97.5  ? 
21 OG  ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 OE1 ? B GLU 141 ? B GLU 138 ? 1_555 81.4  ? 
22 O   ? S HOH .   ? A HOH 348 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 358 ? 1_555 60.3  ? 
23 O   ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 358 ? 1_555 116.2 ? 
24 OG  ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 358 ? 1_555 158.2 ? 
25 OE1 ? B GLU 141 ? B GLU 138 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 358 ? 1_555 84.6  ? 
26 O   ? S HOH .   ? A HOH 348 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 360 ? 1_555 99.8  ? 
27 O   ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 360 ? 1_555 80.6  ? 
28 OG  ? B SER 113 ? B SER 110 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 360 ? 1_555 87.8  ? 
29 OE1 ? B GLU 141 ? B GLU 138 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 360 ? 1_555 169.2 ? 
30 O   ? T HOH .   ? B HOH 358 ? 1_555 NA ? R NA . ? B NA 209 ? 1_555 O   ? T HOH .   ? B HOH 360 ? 1_555 105.9 ? 
31 O   ? B SER 42  ? B SER 39  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? B PHE 45  ? B PHE 42  ? 1_555 79.9  ? 
32 O   ? B SER 42  ? B SER 39  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? B TRP 48  ? B TRP 45  ? 1_555 102.6 ? 
33 O   ? B PHE 45  ? B PHE 42  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? B TRP 48  ? B TRP 45  ? 1_555 91.2  ? 
34 O   ? B SER 42  ? B SER 39  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 349 ? 1_555 104.5 ? 
35 O   ? B PHE 45  ? B PHE 42  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 349 ? 1_555 78.7  ? 
36 O   ? B TRP 48  ? B TRP 45  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 349 ? 1_555 148.8 ? 
37 O   ? B SER 42  ? B SER 39  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 376 ? 1_555 105.5 ? 
38 O   ? B PHE 45  ? B PHE 42  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 376 ? 1_555 162.2 ? 
39 O   ? B TRP 48  ? B TRP 45  ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 376 ? 1_555 103.7 ? 
40 O   ? T HOH .   ? B HOH 349 ? 1_555 NA ? Q NA . ? B NA 208 ? 1_555 O   ? T HOH .   ? B HOH 376 ? 1_555 83.6  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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 ILE A 6   ? LYS A 10  ? ILE A 3   LYS A 7   
AA1 2 TRP B 48  ? ASP B 55  ? TRP B 45  ASP B 52  
AA1 3 GLN B 58  ? ARG B 67  ? GLN B 55  ARG B 64  
AA1 4 VAL B 73  ? ILE B 80  ? VAL B 70  ILE B 77  
AA2 1 VAL A 131 ? LEU A 136 ? VAL A 128 LEU A 133 
AA2 2 ARG A 142 ? THR A 147 ? ARG A 139 THR A 144 
AA2 3 LYS A 109 ? VAL A 114 ? LYS A 106 VAL A 111 
AA2 4 VAL A 73  ? ILE A 80  ? VAL A 70  ILE A 77  
AA2 5 GLN A 58  ? ARG A 67  ? GLN A 55  ARG A 64  
AA2 6 TRP A 48  ? ASP A 55  ? TRP A 45  ASP A 52  
AA2 7 ILE B 6   ? LYS B 10  ? ILE B 3   LYS B 7   
AA3 1 LYS B 109 ? VAL B 114 ? LYS B 106 VAL B 111 
AA3 2 ARG B 142 ? THR B 147 ? ARG B 139 THR B 144 
AA3 3 VAL B 131 ? LEU B 136 ? VAL B 128 LEU B 133 
# 
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 HIS A 7   ? N HIS A 4   O TYR B 54  ? O TYR B 51  
AA1 2 3 N ILE B 53  ? N ILE B 50  O ILE B 60  ? O ILE B 57  
AA1 3 4 N GLY B 66  ? N GLY B 63  O TRP B 74  ? O TRP B 71  
AA2 1 2 N VAL A 131 ? N VAL A 128 O GLU A 145 ? O GLU A 142 
AA2 2 3 O MET A 144 ? O MET A 141 N LEU A 112 ? N LEU A 109 
AA2 3 4 O TYR A 111 ? O TYR A 108 N LEU A 75  ? N LEU A 72  
AA2 4 5 O LEU A 79  ? O LEU A 76  N TYR A 62  ? N TYR A 59  
AA2 5 6 O ILE A 60  ? O ILE A 57  N ILE A 53  ? N ILE A 50  
AA2 6 7 N GLY A 52  ? N GLY A 49  O GLU B 9   ? O GLU B 6   
AA3 1 2 N LEU B 112 ? N LEU B 109 O MET B 144 ? O MET B 141 
AA3 2 3 O GLU B 145 ? O GLU B 142 N VAL B 131 ? N VAL B 128 
# 
_pdbx_entry_details.entry_id                   9DSB 
_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_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 VAL A 21 ? ? -150.88 37.99  
2 1 PHE A 22 ? ? -93.70  33.35  
3 1 ALA A 23 ? ? -148.95 -13.29 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.initial_of_center     CSBID 
# 
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 SER -2  ? A SER 1   
2 1 Y 1 A ASN -1  ? A ASN 2   
3 1 Y 1 A ASN 147 ? A ASN 150 
4 1 Y 1 A LYS 148 ? A LYS 151 
5 1 Y 1 B SER -2  ? B SER 1   
6 1 Y 1 B ASN -1  ? B ASN 2   
7 1 Y 1 B GLN 146 ? B GLN 149 
8 1 Y 1 B ASN 147 ? B ASN 150 
9 1 Y 1 B LYS 148 ? B LYS 151 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
CL  CL   CL N N 81  
CYS N    N  N N 82  
CYS CA   C  N R 83  
CYS C    C  N N 84  
CYS O    O  N N 85  
CYS CB   C  N N 86  
CYS SG   S  N N 87  
CYS OXT  O  N N 88  
CYS H    H  N N 89  
CYS H2   H  N N 90  
CYS HA   H  N N 91  
CYS HB2  H  N N 92  
CYS HB3  H  N N 93  
CYS HG   H  N N 94  
CYS HXT  H  N N 95  
GLN N    N  N N 96  
GLN CA   C  N S 97  
GLN C    C  N N 98  
GLN O    O  N N 99  
GLN CB   C  N N 100 
GLN CG   C  N N 101 
GLN CD   C  N N 102 
GLN OE1  O  N N 103 
GLN NE2  N  N N 104 
GLN OXT  O  N N 105 
GLN H    H  N N 106 
GLN H2   H  N N 107 
GLN HA   H  N N 108 
GLN HB2  H  N N 109 
GLN HB3  H  N N 110 
GLN HG2  H  N N 111 
GLN HG3  H  N N 112 
GLN HE21 H  N N 113 
GLN HE22 H  N N 114 
GLN HXT  H  N N 115 
GLU N    N  N N 116 
GLU CA   C  N S 117 
GLU C    C  N N 118 
GLU O    O  N N 119 
GLU CB   C  N N 120 
GLU CG   C  N N 121 
GLU CD   C  N N 122 
GLU OE1  O  N N 123 
GLU OE2  O  N N 124 
GLU OXT  O  N N 125 
GLU H    H  N N 126 
GLU H2   H  N N 127 
GLU HA   H  N N 128 
GLU HB2  H  N N 129 
GLU HB3  H  N N 130 
GLU HG2  H  N N 131 
GLU HG3  H  N N 132 
GLU HE2  H  N N 133 
GLU HXT  H  N N 134 
GLY N    N  N N 135 
GLY CA   C  N N 136 
GLY C    C  N N 137 
GLY O    O  N N 138 
GLY OXT  O  N N 139 
GLY H    H  N N 140 
GLY H2   H  N N 141 
GLY HA2  H  N N 142 
GLY HA3  H  N N 143 
GLY HXT  H  N N 144 
HIS N    N  N N 145 
HIS CA   C  N S 146 
HIS C    C  N N 147 
HIS O    O  N N 148 
HIS CB   C  N N 149 
HIS CG   C  Y N 150 
HIS ND1  N  Y N 151 
HIS CD2  C  Y N 152 
HIS CE1  C  Y N 153 
HIS NE2  N  Y N 154 
HIS OXT  O  N N 155 
HIS H    H  N N 156 
HIS H2   H  N N 157 
HIS HA   H  N N 158 
HIS HB2  H  N N 159 
HIS HB3  H  N N 160 
HIS HD1  H  N N 161 
HIS HD2  H  N N 162 
HIS HE1  H  N N 163 
HIS HE2  H  N N 164 
HIS HXT  H  N N 165 
HOH O    O  N N 166 
HOH H1   H  N N 167 
HOH H2   H  N N 168 
ILE N    N  N N 169 
ILE CA   C  N S 170 
ILE C    C  N N 171 
ILE O    O  N N 172 
ILE CB   C  N S 173 
ILE CG1  C  N N 174 
ILE CG2  C  N N 175 
ILE CD1  C  N N 176 
ILE OXT  O  N N 177 
ILE H    H  N N 178 
ILE H2   H  N N 179 
ILE HA   H  N N 180 
ILE HB   H  N N 181 
ILE HG12 H  N N 182 
ILE HG13 H  N N 183 
ILE HG21 H  N N 184 
ILE HG22 H  N N 185 
ILE HG23 H  N N 186 
ILE HD11 H  N N 187 
ILE HD12 H  N N 188 
ILE HD13 H  N N 189 
ILE HXT  H  N N 190 
K   K    K  N N 191 
LEU N    N  N N 192 
LEU CA   C  N S 193 
LEU C    C  N N 194 
LEU O    O  N N 195 
LEU CB   C  N N 196 
LEU CG   C  N N 197 
LEU CD1  C  N N 198 
LEU CD2  C  N N 199 
LEU OXT  O  N N 200 
LEU H    H  N N 201 
LEU H2   H  N N 202 
LEU HA   H  N N 203 
LEU HB2  H  N N 204 
LEU HB3  H  N N 205 
LEU HG   H  N N 206 
LEU HD11 H  N N 207 
LEU HD12 H  N N 208 
LEU HD13 H  N N 209 
LEU HD21 H  N N 210 
LEU HD22 H  N N 211 
LEU HD23 H  N N 212 
LEU HXT  H  N N 213 
LYS N    N  N N 214 
LYS CA   C  N S 215 
LYS C    C  N N 216 
LYS O    O  N N 217 
LYS CB   C  N N 218 
LYS CG   C  N N 219 
LYS CD   C  N N 220 
LYS CE   C  N N 221 
LYS NZ   N  N N 222 
LYS OXT  O  N N 223 
LYS H    H  N N 224 
LYS H2   H  N N 225 
LYS HA   H  N N 226 
LYS HB2  H  N N 227 
LYS HB3  H  N N 228 
LYS HG2  H  N N 229 
LYS HG3  H  N N 230 
LYS HD2  H  N N 231 
LYS HD3  H  N N 232 
LYS HE2  H  N N 233 
LYS HE3  H  N N 234 
LYS HZ1  H  N N 235 
LYS HZ2  H  N N 236 
LYS HZ3  H  N N 237 
LYS HXT  H  N N 238 
MET N    N  N N 239 
MET CA   C  N S 240 
MET C    C  N N 241 
MET O    O  N N 242 
MET CB   C  N N 243 
MET CG   C  N N 244 
MET SD   S  N N 245 
MET CE   C  N N 246 
MET OXT  O  N N 247 
MET H    H  N N 248 
MET H2   H  N N 249 
MET HA   H  N N 250 
MET HB2  H  N N 251 
MET HB3  H  N N 252 
MET HG2  H  N N 253 
MET HG3  H  N N 254 
MET HE1  H  N N 255 
MET HE2  H  N N 256 
MET HE3  H  N N 257 
MET HXT  H  N N 258 
NA  NA   NA N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HIS N   CA   sing N N 135 
HIS N   H    sing N N 136 
HIS N   H2   sing N N 137 
HIS CA  C    sing N N 138 
HIS CA  CB   sing N N 139 
HIS CA  HA   sing N N 140 
HIS C   O    doub N N 141 
HIS C   OXT  sing N N 142 
HIS CB  CG   sing N N 143 
HIS CB  HB2  sing N N 144 
HIS CB  HB3  sing N N 145 
HIS CG  ND1  sing Y N 146 
HIS CG  CD2  doub Y N 147 
HIS ND1 CE1  doub Y N 148 
HIS ND1 HD1  sing N N 149 
HIS CD2 NE2  sing Y N 150 
HIS CD2 HD2  sing N N 151 
HIS CE1 NE2  sing Y N 152 
HIS CE1 HE1  sing N N 153 
HIS NE2 HE2  sing N N 154 
HIS OXT HXT  sing N N 155 
HOH O   H1   sing N N 156 
HOH O   H2   sing N N 157 
ILE N   CA   sing N N 158 
ILE N   H    sing N N 159 
ILE N   H2   sing N N 160 
ILE CA  C    sing N N 161 
ILE CA  CB   sing N N 162 
ILE CA  HA   sing N N 163 
ILE C   O    doub N N 164 
ILE C   OXT  sing N N 165 
ILE CB  CG1  sing N N 166 
ILE CB  CG2  sing N N 167 
ILE CB  HB   sing N N 168 
ILE CG1 CD1  sing N N 169 
ILE CG1 HG12 sing N N 170 
ILE CG1 HG13 sing N N 171 
ILE CG2 HG21 sing N N 172 
ILE CG2 HG22 sing N N 173 
ILE CG2 HG23 sing N N 174 
ILE CD1 HD11 sing N N 175 
ILE CD1 HD12 sing N N 176 
ILE CD1 HD13 sing N N 177 
ILE OXT HXT  sing N N 178 
LEU N   CA   sing N N 179 
LEU N   H    sing N N 180 
LEU N   H2   sing N N 181 
LEU CA  C    sing N N 182 
LEU CA  CB   sing N N 183 
LEU CA  HA   sing N N 184 
LEU C   O    doub N N 185 
LEU C   OXT  sing N N 186 
LEU CB  CG   sing N N 187 
LEU CB  HB2  sing N N 188 
LEU CB  HB3  sing N N 189 
LEU CG  CD1  sing N N 190 
LEU CG  CD2  sing N N 191 
LEU CG  HG   sing N N 192 
LEU CD1 HD11 sing N N 193 
LEU CD1 HD12 sing N N 194 
LEU CD1 HD13 sing N N 195 
LEU CD2 HD21 sing N N 196 
LEU CD2 HD22 sing N N 197 
LEU CD2 HD23 sing N N 198 
LEU OXT HXT  sing N N 199 
LYS N   CA   sing N N 200 
LYS N   H    sing N N 201 
LYS N   H2   sing N N 202 
LYS CA  C    sing N N 203 
LYS CA  CB   sing N N 204 
LYS CA  HA   sing N N 205 
LYS C   O    doub N N 206 
LYS C   OXT  sing N N 207 
LYS CB  CG   sing N N 208 
LYS CB  HB2  sing N N 209 
LYS CB  HB3  sing N N 210 
LYS CG  CD   sing N N 211 
LYS CG  HG2  sing N N 212 
LYS CG  HG3  sing N N 213 
LYS CD  CE   sing N N 214 
LYS CD  HD2  sing N N 215 
LYS CD  HD3  sing N N 216 
LYS CE  NZ   sing N N 217 
LYS CE  HE2  sing N N 218 
LYS CE  HE3  sing N N 219 
LYS NZ  HZ1  sing N N 220 
LYS NZ  HZ2  sing N N 221 
LYS NZ  HZ3  sing N N 222 
LYS OXT HXT  sing N N 223 
MET N   CA   sing N N 224 
MET N   H    sing N N 225 
MET N   H2   sing N N 226 
MET CA  C    sing N N 227 
MET CA  CB   sing N N 228 
MET CA  HA   sing N N 229 
MET C   O    doub N N 230 
MET C   OXT  sing N N 231 
MET CB  CG   sing N N 232 
MET CB  HB2  sing N N 233 
MET CB  HB3  sing N N 234 
MET CG  SD   sing N N 235 
MET CG  HG2  sing N N 236 
MET CG  HG3  sing N N 237 
MET SD  CE   sing N N 238 
MET CE  HE1  sing N N 239 
MET CE  HE2  sing N N 240 
MET CE  HE3  sing N N 241 
MET OXT HXT  sing N N 242 
PHE N   CA   sing N N 243 
PHE N   H    sing N N 244 
PHE N   H2   sing N N 245 
PHE CA  C    sing N N 246 
PHE CA  CB   sing N N 247 
PHE CA  HA   sing N N 248 
PHE C   O    doub N N 249 
PHE C   OXT  sing N N 250 
PHE CB  CG   sing N N 251 
PHE CB  HB2  sing N N 252 
PHE CB  HB3  sing N N 253 
PHE CG  CD1  doub Y N 254 
PHE CG  CD2  sing Y N 255 
PHE CD1 CE1  sing Y N 256 
PHE CD1 HD1  sing N N 257 
PHE CD2 CE2  doub Y N 258 
PHE CD2 HD2  sing N N 259 
PHE CE1 CZ   doub Y N 260 
PHE CE1 HE1  sing N N 261 
PHE CE2 CZ   sing Y N 262 
PHE CE2 HE2  sing N N 263 
PHE CZ  HZ   sing N N 264 
PHE OXT HXT  sing N N 265 
PRO N   CA   sing N N 266 
PRO N   CD   sing N N 267 
PRO N   H    sing N N 268 
PRO CA  C    sing N N 269 
PRO CA  CB   sing N N 270 
PRO CA  HA   sing N N 271 
PRO C   O    doub N N 272 
PRO C   OXT  sing N N 273 
PRO CB  CG   sing N N 274 
PRO CB  HB2  sing N N 275 
PRO CB  HB3  sing N N 276 
PRO CG  CD   sing N N 277 
PRO CG  HG2  sing N N 278 
PRO CG  HG3  sing N N 279 
PRO CD  HD2  sing N N 280 
PRO CD  HD3  sing N N 281 
PRO OXT HXT  sing N N 282 
SER N   CA   sing N N 283 
SER N   H    sing N N 284 
SER N   H2   sing N N 285 
SER CA  C    sing N N 286 
SER CA  CB   sing N N 287 
SER CA  HA   sing N N 288 
SER C   O    doub N N 289 
SER C   OXT  sing N N 290 
SER CB  OG   sing N N 291 
SER CB  HB2  sing N N 292 
SER CB  HB3  sing N N 293 
SER OG  HG   sing N N 294 
SER OXT HXT  sing N N 295 
THR N   CA   sing N N 296 
THR N   H    sing N N 297 
THR N   H2   sing N N 298 
THR CA  C    sing N N 299 
THR CA  CB   sing N N 300 
THR CA  HA   sing N N 301 
THR C   O    doub N N 302 
THR C   OXT  sing N N 303 
THR CB  OG1  sing N N 304 
THR CB  CG2  sing N N 305 
THR CB  HB   sing N N 306 
THR OG1 HG1  sing N N 307 
THR CG2 HG21 sing N N 308 
THR CG2 HG22 sing N N 309 
THR CG2 HG23 sing N N 310 
THR OXT HXT  sing N N 311 
TRP N   CA   sing N N 312 
TRP N   H    sing N N 313 
TRP N   H2   sing N N 314 
TRP CA  C    sing N N 315 
TRP CA  CB   sing N N 316 
TRP CA  HA   sing N N 317 
TRP C   O    doub N N 318 
TRP C   OXT  sing N N 319 
TRP CB  CG   sing N N 320 
TRP CB  HB2  sing N N 321 
TRP CB  HB3  sing N N 322 
TRP CG  CD1  doub Y N 323 
TRP CG  CD2  sing Y N 324 
TRP CD1 NE1  sing Y N 325 
TRP CD1 HD1  sing N N 326 
TRP CD2 CE2  doub Y N 327 
TRP CD2 CE3  sing Y N 328 
TRP NE1 CE2  sing Y N 329 
TRP NE1 HE1  sing N N 330 
TRP CE2 CZ2  sing Y N 331 
TRP CE3 CZ3  doub Y N 332 
TRP CE3 HE3  sing N N 333 
TRP CZ2 CH2  doub Y N 334 
TRP CZ2 HZ2  sing N N 335 
TRP CZ3 CH2  sing Y N 336 
TRP CZ3 HZ3  sing N N 337 
TRP CH2 HH2  sing N N 338 
TRP OXT HXT  sing N N 339 
TYR N   CA   sing N N 340 
TYR N   H    sing N N 341 
TYR N   H2   sing N N 342 
TYR CA  C    sing N N 343 
TYR CA  CB   sing N N 344 
TYR CA  HA   sing N N 345 
TYR C   O    doub N N 346 
TYR C   OXT  sing N N 347 
TYR CB  CG   sing N N 348 
TYR CB  HB2  sing N N 349 
TYR CB  HB3  sing N N 350 
TYR CG  CD1  doub Y N 351 
TYR CG  CD2  sing Y N 352 
TYR CD1 CE1  sing Y N 353 
TYR CD1 HD1  sing N N 354 
TYR CD2 CE2  doub Y N 355 
TYR CD2 HD2  sing N N 356 
TYR CE1 CZ   doub Y N 357 
TYR CE1 HE1  sing N N 358 
TYR CE2 CZ   sing Y N 359 
TYR CE2 HE2  sing N N 360 
TYR CZ  OH   sing N N 361 
TYR OH  HH   sing N N 362 
TYR OXT HXT  sing N N 363 
VAL N   CA   sing N N 364 
VAL N   H    sing N N 365 
VAL N   H2   sing N N 366 
VAL CA  C    sing N N 367 
VAL CA  CB   sing N N 368 
VAL CA  HA   sing N N 369 
VAL C   O    doub N N 370 
VAL C   OXT  sing N N 371 
VAL CB  CG1  sing N N 372 
VAL CB  CG2  sing N N 373 
VAL CB  HB   sing N N 374 
VAL CG1 HG11 sing N N 375 
VAL CG1 HG12 sing N N 376 
VAL CG1 HG13 sing N N 377 
VAL CG2 HG21 sing N N 378 
VAL CG2 HG22 sing N N 379 
VAL CG2 HG23 sing N N 380 
VAL OXT HXT  sing N N 381 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DSB 
_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]   0.011075 
_atom_sites.fract_transf_matrix[1][2]   0.006394 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012788 
_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]   0.028756 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
K  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 3   ? -16.969 -0.912  13.256  1.00 41.43 ? 0   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 3   ? -16.670 -2.313  13.645  1.00 40.75 ? 0   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 3   ? -15.657 -2.901  12.662  1.00 38.63 ? 0   ALA A C   1 
ATOM   4    O  O   . ALA A 1 3   ? -14.634 -2.269  12.395  1.00 38.62 ? 0   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 3   ? -17.960 -3.107  13.728  1.00 41.32 ? 0   ALA A CB  1 
ATOM   6    N  N   . MET A 1 4   ? -15.941 -4.094  12.120  1.00 36.68 ? 1   MET A N   1 
ATOM   7    C  CA  . MET A 1 4   ? -15.011 -4.778  11.238  1.00 34.63 ? 1   MET A CA  1 
ATOM   8    C  C   . MET A 1 4   ? -14.904 -4.026  9.913   1.00 31.61 ? 1   MET A C   1 
ATOM   9    O  O   . MET A 1 4   ? -15.854 -3.371  9.477   1.00 30.48 ? 1   MET A O   1 
ATOM   10   C  CB  . MET A 1 4   ? -15.448 -6.222  10.964  1.00 35.61 ? 1   MET A CB  1 
ATOM   11   C  CG  . MET A 1 4   ? -15.630 -7.084  12.212  1.00 37.37 ? 1   MET A CG  1 
ATOM   12   S  SD  . MET A 1 4   ? -15.822 -8.851  11.887  1.00 39.48 ? 1   MET A SD  1 
ATOM   13   C  CE  . MET A 1 4   ? -16.444 -8.853  10.203  1.00 37.38 ? 1   MET A CE  1 
ATOM   14   N  N   . GLU A 1 5   ? -13.719 -4.132  9.300   1.00 28.28 ? 2   GLU A N   1 
ATOM   15   C  CA  . GLU A 1 5   ? -13.404 -3.505  8.026   1.00 27.59 ? 2   GLU A CA  1 
ATOM   16   C  C   . GLU A 1 5   ? -12.729 -4.557  7.146   1.00 25.80 ? 2   GLU A C   1 
ATOM   17   O  O   . GLU A 1 5   ? -11.544 -4.455  6.843   1.00 24.73 ? 2   GLU A O   1 
ATOM   18   C  CB  . GLU A 1 5   ? -12.472 -2.301  8.205   1.00 27.50 ? 2   GLU A CB  1 
ATOM   19   C  CG  . GLU A 1 5   ? -13.028 -1.153  9.046   1.00 27.71 ? 2   GLU A CG  1 
ATOM   20   C  CD  . GLU A 1 5   ? -12.028 -0.024  9.274   1.00 27.40 ? 2   GLU A CD  1 
ATOM   21   O  OE1 . GLU A 1 5   ? -10.951 -0.076  8.650   1.00 28.99 ? 2   GLU A OE1 1 
ATOM   22   O  OE2 . GLU A 1 5   ? -12.300 0.912   10.063  1.00 27.68 ? 2   GLU A OE2 1 
ATOM   23   N  N   . ILE A 1 6   ? -13.495 -5.584  6.758   1.00 24.38 ? 3   ILE A N   1 
ATOM   24   C  CA  . ILE A 1 6   ? -12.941 -6.749  6.087   1.00 24.16 ? 3   ILE A CA  1 
ATOM   25   C  C   . ILE A 1 6   ? -12.668 -6.431  4.621   1.00 22.63 ? 3   ILE A C   1 
ATOM   26   O  O   . ILE A 1 6   ? -13.568 -6.043  3.882   1.00 23.34 ? 3   ILE A O   1 
ATOM   27   C  CB  . ILE A 1 6   ? -13.877 -7.961  6.220   1.00 25.19 ? 3   ILE A CB  1 
ATOM   28   C  CG1 . ILE A 1 6   ? -14.091 -8.341  7.676   1.00 26.84 ? 3   ILE A CG1 1 
ATOM   29   C  CG2 . ILE A 1 6   ? -13.370 -9.135  5.384   1.00 25.35 ? 3   ILE A CG2 1 
ATOM   30   C  CD1 . ILE A 1 6   ? -12.856 -8.845  8.393   1.00 28.13 ? 3   ILE A CD1 1 
ATOM   31   N  N   . HIS A 1 7   ? -11.415 -6.630  4.211   1.00 23.21 ? 4   HIS A N   1 
ATOM   32   C  CA  . HIS A 1 7   ? -11.036 -6.502  2.816   1.00 23.06 ? 4   HIS A CA  1 
ATOM   33   C  C   . HIS A 1 7   ? -9.899  -7.477  2.544   1.00 22.95 ? 4   HIS A C   1 
ATOM   34   O  O   . HIS A 1 7   ? -9.318  -8.021  3.479   1.00 23.50 ? 4   HIS A O   1 
ATOM   35   C  CB  . HIS A 1 7   ? -10.668 -5.050  2.486   1.00 23.08 ? 4   HIS A CB  1 
ATOM   36   C  CG  . HIS A 1 7   ? -9.501  -4.534  3.259   1.00 23.14 ? 4   HIS A CG  1 
ATOM   37   N  ND1 . HIS A 1 7   ? -8.268  -4.293  2.690   1.00 23.23 ? 4   HIS A ND1 1 
ATOM   38   C  CD2 . HIS A 1 7   ? -9.376  -4.214  4.552   1.00 23.07 ? 4   HIS A CD2 1 
ATOM   39   C  CE1 . HIS A 1 7   ? -7.434  -3.855  3.619   1.00 23.16 ? 4   HIS A CE1 1 
ATOM   40   N  NE2 . HIS A 1 7   ? -8.088  -3.797  4.756   1.00 23.04 ? 4   HIS A NE2 1 
ATOM   41   N  N   . PHE A 1 8   ? -9.601  -7.667  1.256   1.00 22.51 ? 5   PHE A N   1 
ATOM   42   C  CA  . PHE A 1 8   ? -8.595  -8.615  0.809   1.00 23.40 ? 5   PHE A CA  1 
ATOM   43   C  C   . PHE A 1 8   ? -7.547  -7.891  -0.026  1.00 22.62 ? 5   PHE A C   1 
ATOM   44   O  O   . PHE A 1 8   ? -7.868  -6.968  -0.769  1.00 23.97 ? 5   PHE A O   1 
ATOM   45   C  CB  . PHE A 1 8   ? -9.271  -9.718  -0.005  1.00 24.77 ? 5   PHE A CB  1 
ATOM   46   C  CG  . PHE A 1 8   ? -10.444 -10.347 0.731   1.00 26.73 ? 5   PHE A CG  1 
ATOM   47   C  CD1 . PHE A 1 8   ? -10.243 -11.409 1.604   1.00 27.87 ? 5   PHE A CD1 1 
ATOM   48   C  CD2 . PHE A 1 8   ? -11.734 -9.843  0.588   1.00 28.10 ? 5   PHE A CD2 1 
ATOM   49   C  CE1 . PHE A 1 8   ? -11.310 -11.971 2.290   1.00 29.38 ? 5   PHE A CE1 1 
ATOM   50   C  CE2 . PHE A 1 8   ? -12.794 -10.407 1.281   1.00 29.16 ? 5   PHE A CE2 1 
ATOM   51   C  CZ  . PHE A 1 8   ? -12.578 -11.468 2.128   1.00 29.62 ? 5   PHE A CZ  1 
ATOM   52   N  N   . GLU A 1 9   ? -6.296  -8.348  0.087   1.00 21.83 ? 6   GLU A N   1 
ATOM   53   C  CA  . GLU A 1 9   ? -5.196  -7.773  -0.667  1.00 22.72 ? 6   GLU A CA  1 
ATOM   54   C  C   . GLU A 1 9   ? -4.465  -8.879  -1.412  1.00 22.90 ? 6   GLU A C   1 
ATOM   55   O  O   . GLU A 1 9   ? -4.176  -9.913  -0.831  1.00 22.90 ? 6   GLU A O   1 
ATOM   56   C  CB  . GLU A 1 9   ? -4.204  -7.053  0.245   1.00 23.54 ? 6   GLU A CB  1 
ATOM   57   C  CG  . GLU A 1 9   ? -4.842  -5.937  1.065   1.00 24.26 ? 6   GLU A CG  1 
ATOM   58   C  CD  . GLU A 1 9   ? -3.874  -5.197  1.963   1.00 25.56 ? 6   GLU A CD  1 
ATOM   59   O  OE1 . GLU A 1 9   ? -2.659  -5.494  1.909   1.00 27.81 ? 6   GLU A OE1 1 
ATOM   60   O  OE2 . GLU A 1 9   ? -4.344  -4.304  2.700   1.00 27.21 ? 6   GLU A OE2 1 
ATOM   61   N  N   . LYS A 1 10  ? -4.163  -8.636  -2.691  1.00 24.69 ? 7   LYS A N   1 
ATOM   62   C  CA  . LYS A 1 10  ? -3.214  -9.452  -3.427  1.00 27.16 ? 7   LYS A CA  1 
ATOM   63   C  C   . LYS A 1 10  ? -1.939  -9.588  -2.600  1.00 25.98 ? 7   LYS A C   1 
ATOM   64   O  O   . LYS A 1 10  ? -1.541  -8.651  -1.910  1.00 26.52 ? 7   LYS A O   1 
ATOM   65   C  CB  . LYS A 1 10  ? -2.892  -8.786  -4.769  1.00 30.36 ? 7   LYS A CB  1 
ATOM   66   C  CG  . LYS A 1 10  ? -3.934  -9.007  -5.858  1.00 33.74 ? 7   LYS A CG  1 
ATOM   67   C  CD  . LYS A 1 10  ? -3.930  -10.414 -6.445  1.00 35.78 ? 7   LYS A CD  1 
ATOM   68   C  CE  . LYS A 1 10  ? -2.674  -10.721 -7.204  1.00 37.31 ? 7   LYS A CE  1 
ATOM   69   N  NZ  . LYS A 1 10  ? -2.647  -12.096 -7.707  1.00 39.04 ? 7   LYS A NZ  1 
ATOM   70   N  N   . VAL A 1 11  ? -1.308  -10.764 -2.664  1.00 26.41 ? 8   VAL A N   1 
ATOM   71   C  CA  . VAL A 1 11  ? -0.059  -10.979 -1.958  1.00 26.34 ? 8   VAL A CA  1 
ATOM   72   C  C   . VAL A 1 11  ? 1.070   -10.377 -2.792  1.00 28.32 ? 8   VAL A C   1 
ATOM   73   O  O   . VAL A 1 11  ? 1.193   -10.667 -3.982  1.00 30.06 ? 8   VAL A O   1 
ATOM   74   C  CB  . VAL A 1 11  ? 0.180   -12.470 -1.653  1.00 26.45 ? 8   VAL A CB  1 
ATOM   75   C  CG1 . VAL A 1 11  ? 1.499   -12.674 -0.926  1.00 26.18 ? 8   VAL A CG1 1 
ATOM   76   C  CG2 . VAL A 1 11  ? -0.953  -13.076 -0.838  1.00 26.31 ? 8   VAL A CG2 1 
ATOM   77   N  N   . THR A 1 12  ? 1.871   -9.517  -2.150  1.00 27.96 ? 9   THR A N   1 
ATOM   78   C  CA  . THR A 1 12  ? 3.014   -8.874  -2.774  1.00 28.51 ? 9   THR A CA  1 
ATOM   79   C  C   . THR A 1 12  ? 4.186   -8.967  -1.803  1.00 27.33 ? 9   THR A C   1 
ATOM   80   O  O   . THR A 1 12  ? 4.038   -9.496  -0.706  1.00 28.04 ? 9   THR A O   1 
ATOM   81   C  CB  . THR A 1 12  ? 2.699   -7.410  -3.093  1.00 28.83 ? 9   THR A CB  1 
ATOM   82   O  OG1 . THR A 1 12  ? 2.609   -6.760  -1.829  1.00 28.90 ? 9   THR A OG1 1 
ATOM   83   C  CG2 . THR A 1 12  ? 1.418   -7.211  -3.883  1.00 28.85 ? 9   THR A CG2 1 
ATOM   84   N  N   . SER A 1 13  ? 5.330   -8.389  -2.186  1.00 28.02 ? 10  SER A N   1 
ATOM   85   C  CA  . SER A 1 13  ? 6.465   -8.272  -1.286  1.00 27.00 ? 10  SER A CA  1 
ATOM   86   C  C   . SER A 1 13  ? 6.100   -7.483  -0.027  1.00 25.81 ? 10  SER A C   1 
ATOM   87   O  O   . SER A 1 13  ? 6.752   -7.639  1.002   1.00 26.88 ? 10  SER A O   1 
ATOM   88   C  CB  . SER A 1 13  ? 7.658   -7.676  -1.995  1.00 27.89 ? 10  SER A CB  1 
ATOM   89   O  OG  . SER A 1 13  ? 7.253   -6.675  -2.919  1.00 30.65 ? 10  SER A OG  1 
ATOM   90   N  N   . ASP A 1 14  ? 5.062   -6.639  -0.108  1.00 26.27 ? 11  ASP A N   1 
ATOM   91   C  CA  . ASP A 1 14  ? 4.676   -5.784  1.002   1.00 27.16 ? 11  ASP A CA  1 
ATOM   92   C  C   . ASP A 1 14  ? 4.022   -6.580  2.133   1.00 24.91 ? 11  ASP A C   1 
ATOM   93   O  O   . ASP A 1 14  ? 4.066   -6.129  3.278   1.00 26.32 ? 11  ASP A O   1 
ATOM   94   C  CB  . ASP A 1 14  ? 3.777   -4.643  0.543   1.00 29.08 ? 11  ASP A CB  1 
ATOM   95   C  CG  . ASP A 1 14  ? 4.433   -3.578  -0.329  1.00 31.79 ? 11  ASP A CG  1 
ATOM   96   O  OD1 . ASP A 1 14  ? 5.649   -3.689  -0.597  1.00 33.62 ? 11  ASP A OD1 1 
ATOM   97   O  OD2 . ASP A 1 14  ? 3.722   -2.631  -0.730  1.00 34.95 ? 11  ASP A OD2 1 
ATOM   98   N  N   . ASN A 1 15  ? 3.395   -7.731  1.822   1.00 22.74 ? 12  ASN A N   1 
ATOM   99   C  CA  . ASN A 1 15  ? 2.673   -8.495  2.834   1.00 22.18 ? 12  ASN A CA  1 
ATOM   100  C  C   . ASN A 1 15  ? 2.956   -10.005 2.824   1.00 22.42 ? 12  ASN A C   1 
ATOM   101  O  O   . ASN A 1 15  ? 2.430   -10.711 3.678   1.00 23.02 ? 12  ASN A O   1 
ATOM   102  C  CB  . ASN A 1 15  ? 1.167   -8.270  2.724   1.00 21.26 ? 12  ASN A CB  1 
ATOM   103  C  CG  . ASN A 1 15  ? 0.606   -8.623  1.365   1.00 21.28 ? 12  ASN A CG  1 
ATOM   104  O  OD1 . ASN A 1 15  ? 1.327   -9.115  0.493   1.00 21.44 ? 12  ASN A OD1 1 
ATOM   105  N  ND2 . ASN A 1 15  ? -0.675  -8.357  1.151   1.00 21.81 ? 12  ASN A ND2 1 
ATOM   106  N  N   A ARG A 1 16  ? 3.774   -10.490 1.882   0.51 23.78 ? 13  ARG A N   1 
ATOM   107  N  N   B ARG A 1 16  ? 3.786   -10.499 1.895   0.49 22.78 ? 13  ARG A N   1 
ATOM   108  C  CA  A ARG A 1 16  ? 4.016   -11.919 1.715   0.51 24.45 ? 13  ARG A CA  1 
ATOM   109  C  CA  B ARG A 1 16  ? 3.967   -11.937 1.744   0.49 22.85 ? 13  ARG A CA  1 
ATOM   110  C  C   A ARG A 1 16  ? 4.554   -12.543 3.004   0.51 23.77 ? 13  ARG A C   1 
ATOM   111  C  C   B ARG A 1 16  ? 4.549   -12.552 3.018   0.49 22.95 ? 13  ARG A C   1 
ATOM   112  O  O   A ARG A 1 16  ? 4.162   -13.650 3.369   0.51 24.66 ? 13  ARG A O   1 
ATOM   113  O  O   B ARG A 1 16  ? 4.174   -13.661 3.393   0.49 23.67 ? 13  ARG A O   1 
ATOM   114  C  CB  A ARG A 1 16  ? 4.957   -12.130 0.520   0.51 26.43 ? 13  ARG A CB  1 
ATOM   115  C  CB  B ARG A 1 16  ? 4.859   -12.318 0.557   0.49 23.35 ? 13  ARG A CB  1 
ATOM   116  C  CG  A ARG A 1 16  ? 6.086   -13.140 0.676   0.51 28.03 ? 13  ARG A CG  1 
ATOM   117  C  CG  B ARG A 1 16  ? 6.219   -11.638 0.533   0.49 23.74 ? 13  ARG A CG  1 
ATOM   118  C  CD  A ARG A 1 16  ? 7.347   -12.566 0.050   0.51 29.68 ? 13  ARG A CD  1 
ATOM   119  C  CD  B ARG A 1 16  ? 7.275   -12.499 -0.125  0.49 24.33 ? 13  ARG A CD  1 
ATOM   120  N  NE  A ARG A 1 16  ? 7.242   -12.366 -1.401  0.51 30.74 ? 13  ARG A NE  1 
ATOM   121  N  NE  B ARG A 1 16  ? 8.356   -11.713 -0.730  0.49 24.17 ? 13  ARG A NE  1 
ATOM   122  C  CZ  A ARG A 1 16  ? 8.161   -11.764 -2.154  0.51 31.70 ? 13  ARG A CZ  1 
ATOM   123  C  CZ  B ARG A 1 16  ? 8.524   -11.636 -2.043  0.49 25.46 ? 13  ARG A CZ  1 
ATOM   124  N  NH1 A ARG A 1 16  ? 9.203   -11.176 -1.595  0.51 32.46 ? 13  ARG A NH1 1 
ATOM   125  N  NH1 B ARG A 1 16  ? 7.632   -12.196 -2.843  0.49 26.41 ? 13  ARG A NH1 1 
ATOM   126  N  NH2 A ARG A 1 16  ? 8.030   -11.735 -3.470  0.51 31.85 ? 13  ARG A NH2 1 
ATOM   127  N  NH2 B ARG A 1 16  ? 9.565   -11.003 -2.550  0.49 26.03 ? 13  ARG A NH2 1 
ATOM   128  N  N   . LYS A 1 17  ? 5.480   -11.846 3.674   1.00 23.79 ? 14  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 17  ? 6.130   -12.389 4.858   1.00 23.58 ? 14  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 17  ? 5.163   -12.377 6.040   1.00 22.99 ? 14  LYS A C   1 
ATOM   131  O  O   . LYS A 1 17  ? 5.216   -13.260 6.890   1.00 24.75 ? 14  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 17  ? 7.447   -11.662 5.147   1.00 23.69 ? 14  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 17  ? 8.484   -11.864 4.049   1.00 25.06 ? 14  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 17  ? 9.900   -11.414 4.391   1.00 25.70 ? 14  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 17  ? 10.848  -11.678 3.269   1.00 26.57 ? 14  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 17  ? 12.225  -11.325 3.624   1.00 27.12 ? 14  LYS A NZ  1 
ATOM   137  N  N   . ALA A 1 18  ? 4.251   -11.400 6.073   1.00 23.28 ? 15  ALA A N   1 
ATOM   138  C  CA  . ALA A 1 18  ? 3.214   -11.368 7.093   1.00 22.67 ? 15  ALA A CA  1 
ATOM   139  C  C   . ALA A 1 18  ? 2.273   -12.561 6.915   1.00 22.76 ? 15  ALA A C   1 
ATOM   140  O  O   . ALA A 1 18  ? 1.880   -13.196 7.890   1.00 23.11 ? 15  ALA A O   1 
ATOM   141  C  CB  . ALA A 1 18  ? 2.463   -10.054 7.039   1.00 23.24 ? 15  ALA A CB  1 
ATOM   142  N  N   . VAL A 1 19  ? 1.933   -12.859 5.655   1.00 22.15 ? 16  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 19  ? 1.086   -13.993 5.318   1.00 21.99 ? 16  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 19  ? 1.799   -15.287 5.707   1.00 22.93 ? 16  VAL A C   1 
ATOM   145  O  O   . VAL A 1 19  ? 1.188   -16.163 6.312   1.00 24.17 ? 16  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 19  ? 0.705   -13.973 3.825   1.00 22.34 ? 16  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 19  ? -0.017  -15.249 3.396   1.00 22.51 ? 16  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 19  ? -0.134  -12.746 3.485   1.00 22.31 ? 16  VAL A CG2 1 
ATOM   149  N  N   . GLU A 1 20  ? 3.095   -15.389 5.381   1.00 22.55 ? 17  GLU A N   1 
ATOM   150  C  CA  . GLU A 1 20  ? 3.866   -16.581 5.703   1.00 23.40 ? 17  GLU A CA  1 
ATOM   151  C  C   . GLU A 1 20  ? 3.916   -16.808 7.214   1.00 24.25 ? 17  GLU A C   1 
ATOM   152  O  O   . GLU A 1 20  ? 4.021   -17.949 7.655   1.00 25.86 ? 17  GLU A O   1 
ATOM   153  C  CB  . GLU A 1 20  ? 5.260   -16.504 5.082   1.00 23.07 ? 17  GLU A CB  1 
ATOM   154  C  CG  . GLU A 1 20  ? 5.236   -16.738 3.576   1.00 23.75 ? 17  GLU A CG  1 
ATOM   155  C  CD  . GLU A 1 20  ? 6.476   -16.293 2.830   1.00 24.11 ? 17  GLU A CD  1 
ATOM   156  O  OE1 . GLU A 1 20  ? 7.317   -15.559 3.406   1.00 25.13 ? 17  GLU A OE1 1 
ATOM   157  O  OE2 . GLU A 1 20  ? 6.583   -16.685 1.649   1.00 23.34 ? 17  GLU A OE2 1 
ATOM   158  N  N   . ASN A 1 21  ? 3.828   -15.726 7.998   1.00 25.35 ? 18  ASN A N   1 
ATOM   159  C  CA  . ASN A 1 21  ? 3.929   -15.811 9.446   1.00 27.25 ? 18  ASN A CA  1 
ATOM   160  C  C   . ASN A 1 21  ? 2.551   -15.796 10.114  1.00 28.23 ? 18  ASN A C   1 
ATOM   161  O  O   . ASN A 1 21  ? 2.464   -15.625 11.327  1.00 29.73 ? 18  ASN A O   1 
ATOM   162  C  CB  . ASN A 1 21  ? 4.839   -14.715 9.997   1.00 27.78 ? 18  ASN A CB  1 
ATOM   163  C  CG  . ASN A 1 21  ? 6.301   -15.031 9.779   1.00 28.27 ? 18  ASN A CG  1 
ATOM   164  O  OD1 . ASN A 1 21  ? 6.952   -15.583 10.673  1.00 30.51 ? 18  ASN A OD1 1 
ATOM   165  N  ND2 . ASN A 1 21  ? 6.820   -14.748 8.594   1.00 27.81 ? 18  ASN A ND2 1 
ATOM   166  N  N   . LEU A 1 22  ? 1.471   -15.997 9.346   1.00 28.87 ? 19  LEU A N   1 
ATOM   167  C  CA  . LEU A 1 22  ? 0.152   -16.163 9.941   1.00 30.77 ? 19  LEU A CA  1 
ATOM   168  C  C   . LEU A 1 22  ? 0.213   -17.277 10.983  1.00 31.79 ? 19  LEU A C   1 
ATOM   169  O  O   . LEU A 1 22  ? 0.721   -18.356 10.699  1.00 31.54 ? 19  LEU A O   1 
ATOM   170  C  CB  . LEU A 1 22  ? -0.909  -16.461 8.881   1.00 31.78 ? 19  LEU A CB  1 
ATOM   171  C  CG  . LEU A 1 22  ? -1.619  -15.247 8.270   1.00 33.82 ? 19  LEU A CG  1 
ATOM   172  C  CD1 . LEU A 1 22  ? -2.554  -15.684 7.163   1.00 34.31 ? 19  LEU A CD1 1 
ATOM   173  C  CD2 . LEU A 1 22  ? -2.395  -14.475 9.316   1.00 32.85 ? 19  LEU A CD2 1 
ATOM   174  N  N   . GLN A 1 23  ? -0.303  -16.998 12.186  1.00 33.58 ? 20  GLN A N   1 
ATOM   175  C  CA  . GLN A 1 23  ? -0.234  -17.937 13.294  1.00 35.06 ? 20  GLN A CA  1 
ATOM   176  C  C   . GLN A 1 23  ? -1.428  -18.886 13.205  1.00 34.79 ? 20  GLN A C   1 
ATOM   177  O  O   . GLN A 1 23  ? -2.563  -18.429 13.122  1.00 34.09 ? 20  GLN A O   1 
ATOM   178  C  CB  . GLN A 1 23  ? -0.185  -17.162 14.612  1.00 37.40 ? 20  GLN A CB  1 
ATOM   179  C  CG  . GLN A 1 23  ? 0.924   -16.115 14.676  1.00 39.24 ? 20  GLN A CG  1 
ATOM   180  C  CD  . GLN A 1 23  ? 1.110   -15.500 16.047  1.00 41.72 ? 20  GLN A CD  1 
ATOM   181  O  OE1 . GLN A 1 23  ? 0.434   -15.854 17.020  1.00 44.56 ? 20  GLN A OE1 1 
ATOM   182  N  NE2 . GLN A 1 23  ? 2.038   -14.559 16.137  1.00 43.10 ? 20  GLN A NE2 1 
ATOM   183  N  N   . VAL A 1 24  ? -1.160  -20.201 13.213  1.00 35.91 ? 21  VAL A N   1 
ATOM   184  C  CA  . VAL A 1 24  ? -2.189  -21.213 13.007  1.00 36.99 ? 21  VAL A CA  1 
ATOM   185  C  C   . VAL A 1 24  ? -1.828  -22.511 13.740  1.00 39.56 ? 21  VAL A C   1 
ATOM   186  O  O   . VAL A 1 24  ? -2.141  -23.596 13.254  1.00 39.57 ? 21  VAL A O   1 
ATOM   187  C  CB  . VAL A 1 24  ? -2.371  -21.453 11.492  1.00 36.77 ? 21  VAL A CB  1 
ATOM   188  C  CG1 . VAL A 1 24  ? -3.194  -20.362 10.814  1.00 35.94 ? 21  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A 1 24  ? -1.037  -21.631 10.772  1.00 36.87 ? 21  VAL A CG2 1 
ATOM   190  N  N   . PHE A 1 25  ? -1.244  -22.394 14.944  1.00 43.42 ? 22  PHE A N   1 
ATOM   191  C  CA  . PHE A 1 25  ? -0.577  -23.498 15.628  1.00 45.48 ? 22  PHE A CA  1 
ATOM   192  C  C   . PHE A 1 25  ? -1.512  -24.230 16.595  1.00 47.05 ? 22  PHE A C   1 
ATOM   193  O  O   . PHE A 1 25  ? -1.063  -24.708 17.636  1.00 49.85 ? 22  PHE A O   1 
ATOM   194  C  CB  . PHE A 1 25  ? 0.622   -23.036 16.471  1.00 47.56 ? 22  PHE A CB  1 
ATOM   195  C  CG  . PHE A 1 25  ? 1.353   -21.784 16.003  1.00 48.02 ? 22  PHE A CG  1 
ATOM   196  C  CD1 . PHE A 1 25  ? 1.643   -21.578 14.659  1.00 48.39 ? 22  PHE A CD1 1 
ATOM   197  C  CD2 . PHE A 1 25  ? 1.734   -20.803 16.916  1.00 48.65 ? 22  PHE A CD2 1 
ATOM   198  C  CE1 . PHE A 1 25  ? 2.297   -20.428 14.242  1.00 48.98 ? 22  PHE A CE1 1 
ATOM   199  C  CE2 . PHE A 1 25  ? 2.379   -19.651 16.493  1.00 48.76 ? 22  PHE A CE2 1 
ATOM   200  C  CZ  . PHE A 1 25  ? 2.663   -19.467 15.160  1.00 49.36 ? 22  PHE A CZ  1 
ATOM   201  N  N   . ALA A 1 26  ? -2.804  -24.319 16.269  1.00 47.66 ? 23  ALA A N   1 
ATOM   202  C  CA  . ALA A 1 26  ? -3.724  -25.146 17.037  1.00 47.22 ? 23  ALA A CA  1 
ATOM   203  C  C   . ALA A 1 26  ? -4.829  -25.697 16.141  1.00 45.97 ? 23  ALA A C   1 
ATOM   204  O  O   . ALA A 1 26  ? -5.547  -26.612 16.536  1.00 47.23 ? 23  ALA A O   1 
ATOM   205  C  CB  . ALA A 1 26  ? -4.303  -24.346 18.180  1.00 47.61 ? 23  ALA A CB  1 
ATOM   206  N  N   . GLU A 1 27  ? -4.940  -25.138 14.933  1.00 44.60 ? 24  GLU A N   1 
ATOM   207  C  CA  . GLU A 1 27  ? -6.031  -25.436 14.025  1.00 42.91 ? 24  GLU A CA  1 
ATOM   208  C  C   . GLU A 1 27  ? -5.759  -26.800 13.396  1.00 42.79 ? 24  GLU A C   1 
ATOM   209  O  O   . GLU A 1 27  ? -5.312  -26.888 12.254  1.00 43.74 ? 24  GLU A O   1 
ATOM   210  C  CB  . GLU A 1 27  ? -6.138  -24.310 12.994  1.00 42.25 ? 24  GLU A CB  1 
ATOM   211  C  CG  . GLU A 1 27  ? -5.869  -22.920 13.566  1.00 41.54 ? 24  GLU A CG  1 
ATOM   212  C  CD  . GLU A 1 27  ? -6.260  -21.756 12.674  1.00 41.20 ? 24  GLU A CD  1 
ATOM   213  O  OE1 . GLU A 1 27  ? -6.702  -21.987 11.530  1.00 42.13 ? 24  GLU A OE1 1 
ATOM   214  O  OE2 . GLU A 1 27  ? -6.112  -20.604 13.131  1.00 39.33 ? 24  GLU A OE2 1 
ATOM   215  N  N   . GLN A 1 28  ? -6.015  -27.859 14.170  1.00 42.31 ? 25  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? -5.705  -29.219 13.758  1.00 41.67 ? 25  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? -6.553  -29.578 12.542  1.00 39.10 ? 25  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? -6.052  -30.168 11.589  1.00 37.47 ? 25  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? -5.949  -30.175 14.925  1.00 44.49 ? 25  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? -5.120  -29.864 16.169  1.00 46.66 ? 25  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? -5.919  -29.957 17.451  1.00 48.10 ? 25  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? -6.019  -28.993 18.220  1.00 49.01 ? 25  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? -6.508  -31.121 17.691  1.00 48.79 ? 25  GLN A NE2 1 
ATOM   224  N  N   . GLN A 1 29  ? -7.838  -29.200 12.582  1.00 38.97 ? 26  GLN A N   1 
ATOM   225  C  CA  . GLN A 1 29  ? -8.749  -29.444 11.474  1.00 38.77 ? 26  GLN A CA  1 
ATOM   226  C  C   . GLN A 1 29  ? -8.336  -28.616 10.259  1.00 34.84 ? 26  GLN A C   1 
ATOM   227  O  O   . GLN A 1 29  ? -8.489  -29.071 9.127   1.00 34.37 ? 26  GLN A O   1 
ATOM   228  C  CB  . GLN A 1 29  ? -10.203 -29.177 11.869  1.00 41.40 ? 26  GLN A CB  1 
ATOM   229  C  CG  . GLN A 1 29  ? -10.908 -30.386 12.477  1.00 43.95 ? 26  GLN A CG  1 
ATOM   230  C  CD  . GLN A 1 29  ? -11.189 -31.485 11.473  1.00 46.99 ? 26  GLN A CD  1 
ATOM   231  O  OE1 . GLN A 1 29  ? -11.062 -31.301 10.257  1.00 50.63 ? 26  GLN A OE1 1 
ATOM   232  N  NE2 . GLN A 1 29  ? -11.587 -32.645 11.975  1.00 48.87 ? 26  GLN A NE2 1 
ATOM   233  N  N   . ALA A 1 30  ? -7.812  -27.408 10.495  1.00 33.68 ? 27  ALA A N   1 
ATOM   234  C  CA  . ALA A 1 30  ? -7.389  -26.541 9.407   1.00 31.52 ? 27  ALA A CA  1 
ATOM   235  C  C   . ALA A 1 30  ? -6.224  -27.173 8.650   1.00 29.20 ? 27  ALA A C   1 
ATOM   236  O  O   . ALA A 1 30  ? -6.194  -27.126 7.424   1.00 30.34 ? 27  ALA A O   1 
ATOM   237  C  CB  . ALA A 1 30  ? -7.020  -25.170 9.922   1.00 31.91 ? 27  ALA A CB  1 
ATOM   238  N  N   . PHE A 1 31  ? -5.261  -27.754 9.375   1.00 28.77 ? 28  PHE A N   1 
ATOM   239  C  CA  . PHE A 1 31  ? -4.072  -28.282 8.724   1.00 27.21 ? 28  PHE A CA  1 
ATOM   240  C  C   . PHE A 1 31  ? -4.424  -29.561 7.966   1.00 25.33 ? 28  PHE A C   1 
ATOM   241  O  O   . PHE A 1 31  ? -3.762  -29.886 6.984   1.00 24.90 ? 28  PHE A O   1 
ATOM   242  C  CB  . PHE A 1 31  ? -2.876  -28.558 9.640   1.00 30.16 ? 28  PHE A CB  1 
ATOM   243  C  CG  . PHE A 1 31  ? -1.562  -28.518 8.868   1.00 32.17 ? 28  PHE A CG  1 
ATOM   244  C  CD1 . PHE A 1 31  ? -1.017  -29.670 8.309   0.85 32.22 ? 28  PHE A CD1 1 
ATOM   245  C  CD2 . PHE A 1 31  ? -0.900  -27.312 8.659   0.55 32.81 ? 28  PHE A CD2 1 
ATOM   246  C  CE1 . PHE A 1 31  ? 0.170   -29.614 7.590   0.92 33.04 ? 28  PHE A CE1 1 
ATOM   247  C  CE2 . PHE A 1 31  ? 0.284   -27.265 7.938   0.74 33.23 ? 28  PHE A CE2 1 
ATOM   248  C  CZ  . PHE A 1 31  ? 0.813   -28.413 7.403   0.81 32.90 ? 28  PHE A CZ  1 
ATOM   249  N  N   . ILE A 1 32  ? -5.469  -30.274 8.415   1.00 24.90 ? 29  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 32  ? -6.005  -31.385 7.646   1.00 23.87 ? 29  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 32  ? -6.420  -30.868 6.271   1.00 22.75 ? 29  ILE A C   1 
ATOM   252  O  O   . ILE A 1 32  ? -6.109  -31.483 5.257   1.00 23.56 ? 29  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 32  ? -7.168  -32.090 8.373   1.00 25.47 ? 29  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 32  ? -6.689  -32.823 9.628   1.00 26.88 ? 29  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 32  ? -7.908  -33.035 7.425   1.00 26.00 ? 29  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 32  ? -7.809  -33.380 10.490  1.00 27.98 ? 29  ILE A CD1 1 
ATOM   257  N  N   . GLU A 1 33  ? -7.124  -29.729 6.249   1.00 22.59 ? 30  GLU A N   1 
ATOM   258  C  CA  . GLU A 1 33  ? -7.576  -29.139 4.999   1.00 22.53 ? 30  GLU A CA  1 
ATOM   259  C  C   . GLU A 1 33  ? -6.374  -28.655 4.191   1.00 21.46 ? 30  GLU A C   1 
ATOM   260  O  O   . GLU A 1 33  ? -6.368  -28.773 2.968   1.00 23.55 ? 30  GLU A O   1 
ATOM   261  C  CB  . GLU A 1 33  ? -8.575  -28.008 5.247   1.00 23.24 ? 30  GLU A CB  1 
ATOM   262  C  CG  . GLU A 1 33  ? -9.833  -28.456 5.986   1.00 24.51 ? 30  GLU A CG  1 
ATOM   263  C  CD  . GLU A 1 33  ? -10.670 -29.488 5.253   1.00 25.48 ? 30  GLU A CD  1 
ATOM   264  O  OE1 . GLU A 1 33  ? -10.447 -29.692 4.039   1.00 25.68 ? 30  GLU A OE1 1 
ATOM   265  O  OE2 . GLU A 1 33  ? -11.527 -30.122 5.910   1.00 26.67 ? 30  GLU A OE2 1 
ATOM   266  N  N   . SER A 1 34  ? -5.364  -28.102 4.871   1.00 22.28 ? 31  SER A N   1 
ATOM   267  C  CA  . SER A 1 34  ? -4.166  -27.637 4.191   1.00 21.56 ? 31  SER A CA  1 
ATOM   268  C  C   . SER A 1 34  ? -3.490  -28.787 3.453   1.00 20.44 ? 31  SER A C   1 
ATOM   269  O  O   . SER A 1 34  ? -3.073  -28.634 2.307   1.00 20.95 ? 31  SER A O   1 
ATOM   270  C  CB  . SER A 1 34  ? -3.195  -26.976 5.139   1.00 23.39 ? 31  SER A CB  1 
ATOM   271  O  OG  . SER A 1 34  ? -2.575  -25.850 4.522   1.00 26.40 ? 31  SER A OG  1 
ATOM   272  N  N   A MET A 1 35  ? -3.388  -29.938 4.122   0.55 20.45 ? 32  MET A N   1 
ATOM   273  N  N   B MET A 1 35  ? -3.373  -29.933 4.132   0.45 20.19 ? 32  MET A N   1 
ATOM   274  C  CA  A MET A 1 35  ? -2.712  -31.088 3.545   0.55 20.39 ? 32  MET A CA  1 
ATOM   275  C  CA  B MET A 1 35  ? -2.719  -31.102 3.566   0.45 19.96 ? 32  MET A CA  1 
ATOM   276  C  C   A MET A 1 35  ? -3.538  -31.648 2.389   0.55 19.97 ? 32  MET A C   1 
ATOM   277  C  C   B MET A 1 35  ? -3.538  -31.642 2.395   0.45 19.60 ? 32  MET A C   1 
ATOM   278  O  O   A MET A 1 35  ? -2.985  -32.013 1.356   0.55 20.57 ? 32  MET A O   1 
ATOM   279  O  O   B MET A 1 35  ? -2.980  -31.976 1.354   0.45 20.02 ? 32  MET A O   1 
ATOM   280  C  CB  A MET A 1 35  ? -2.452  -32.168 4.599   0.55 20.76 ? 32  MET A CB  1 
ATOM   281  C  CB  B MET A 1 35  ? -2.505  -32.187 4.628   0.45 20.09 ? 32  MET A CB  1 
ATOM   282  C  CG  A MET A 1 35  ? -1.600  -33.326 4.098   0.55 21.02 ? 32  MET A CG  1 
ATOM   283  C  CG  B MET A 1 35  ? -1.415  -31.853 5.632   0.45 20.10 ? 32  MET A CG  1 
ATOM   284  S  SD  A MET A 1 35  ? 0.011   -32.874 3.422   0.55 21.68 ? 32  MET A SD  1 
ATOM   285  S  SD  B MET A 1 35  ? 0.220   -31.673 4.887   0.45 20.63 ? 32  MET A SD  1 
ATOM   286  C  CE  A MET A 1 35  ? 0.740   -32.030 4.832   0.55 22.10 ? 32  MET A CE  1 
ATOM   287  C  CE  B MET A 1 35  ? 0.638   -33.403 4.644   0.45 20.78 ? 32  MET A CE  1 
ATOM   288  N  N   . ALA A 1 36  ? -4.864  -31.721 2.568   1.00 19.38 ? 33  ALA A N   1 
ATOM   289  C  CA  . ALA A 1 36  ? -5.739  -32.222 1.520   1.00 19.07 ? 33  ALA A CA  1 
ATOM   290  C  C   . ALA A 1 36  ? -5.575  -31.390 0.251   1.00 19.16 ? 33  ALA A C   1 
ATOM   291  O  O   . ALA A 1 36  ? -5.555  -31.922 -0.853  1.00 19.87 ? 33  ALA A O   1 
ATOM   292  C  CB  . ALA A 1 36  ? -7.171  -32.245 2.001   1.00 19.40 ? 33  ALA A CB  1 
ATOM   293  N  N   . GLU A 1 37  ? -5.441  -30.073 0.411   1.00 19.42 ? 34  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 37  ? -5.233  -29.201 -0.732  1.00 19.65 ? 34  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 37  ? -3.821  -29.408 -1.279  1.00 20.01 ? 34  GLU A C   1 
ATOM   296  O  O   . GLU A 1 37  ? -3.647  -29.470 -2.492  1.00 19.72 ? 34  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 37  ? -5.540  -27.746 -0.380  1.00 19.96 ? 34  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 37  ? -5.382  -26.791 -1.560  1.00 20.84 ? 34  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 37  ? -6.285  -27.035 -2.757  1.00 21.17 ? 34  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 37  ? -7.288  -27.752 -2.599  1.00 21.74 ? 34  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 37  ? -5.985  -26.511 -3.855  1.00 22.34 ? 34  GLU A OE2 1 
ATOM   302  N  N   . ASN A 1 38  ? -2.817  -29.510 -0.391  1.00 21.32 ? 35  ASN A N   1 
ATOM   303  C  CA  . ASN A 1 38  ? -1.455  -29.813 -0.812  1.00 21.20 ? 35  ASN A CA  1 
ATOM   304  C  C   . ASN A 1 38  ? -1.464  -31.017 -1.751  1.00 21.45 ? 35  ASN A C   1 
ATOM   305  O  O   . ASN A 1 38  ? -0.856  -30.981 -2.820  1.00 23.39 ? 35  ASN A O   1 
ATOM   306  C  CB  . ASN A 1 38  ? -0.506  -30.124 0.346   1.00 21.96 ? 35  ASN A CB  1 
ATOM   307  C  CG  . ASN A 1 38  ? -0.161  -28.922 1.191   1.00 23.19 ? 35  ASN A CG  1 
ATOM   308  O  OD1 . ASN A 1 38  ? -0.418  -27.779 0.797   1.00 23.85 ? 35  ASN A OD1 1 
ATOM   309  N  ND2 . ASN A 1 38  ? 0.444   -29.166 2.345   1.00 24.67 ? 35  ASN A ND2 1 
ATOM   310  N  N   . LEU A 1 39  ? -2.155  -32.080 -1.331  1.00 21.85 ? 36  LEU A N   1 
ATOM   311  C  CA  . LEU A 1 39  ? -2.175  -33.327 -2.080  1.00 22.70 ? 36  LEU A CA  1 
ATOM   312  C  C   . LEU A 1 39  ? -2.911  -33.117 -3.400  1.00 22.34 ? 36  LEU A C   1 
ATOM   313  O  O   . LEU A 1 39  ? -2.452  -33.550 -4.451  1.00 24.51 ? 36  LEU A O   1 
ATOM   314  C  CB  . LEU A 1 39  ? -2.803  -34.439 -1.244  1.00 22.69 ? 36  LEU A CB  1 
ATOM   315  C  CG  . LEU A 1 39  ? -1.997  -34.921 -0.033  1.00 22.99 ? 36  LEU A CG  1 
ATOM   316  C  CD1 . LEU A 1 39  ? -2.820  -35.927 0.760   1.00 22.97 ? 36  LEU A CD1 1 
ATOM   317  C  CD2 . LEU A 1 39  ? -0.668  -35.531 -0.441  1.00 24.29 ? 36  LEU A CD2 1 
ATOM   318  N  N   . LYS A 1 40  ? -4.037  -32.407 -3.350  1.00 22.93 ? 37  LYS A N   1 
ATOM   319  C  CA  . LYS A 1 40  ? -4.806  -32.133 -4.550  1.00 23.16 ? 37  LYS A CA  1 
ATOM   320  C  C   . LYS A 1 40  ? -3.965  -31.387 -5.585  1.00 24.66 ? 37  LYS A C   1 
ATOM   321  O  O   . LYS A 1 40  ? -4.022  -31.705 -6.771  1.00 25.19 ? 37  LYS A O   1 
ATOM   322  C  CB  . LYS A 1 40  ? -6.041  -31.321 -4.163  1.00 22.82 ? 37  LYS A CB  1 
ATOM   323  C  CG  . LYS A 1 40  ? -6.999  -31.063 -5.309  1.00 23.19 ? 37  LYS A CG  1 
ATOM   324  C  CD  . LYS A 1 40  ? -8.230  -30.286 -4.870  1.00 23.06 ? 37  LYS A CD  1 
ATOM   325  C  CE  . LYS A 1 40  ? -9.204  -30.134 -5.981  1.00 24.02 ? 37  LYS A CE  1 
ATOM   326  N  NZ  . LYS A 1 40  ? -10.353 -29.343 -5.535  1.00 24.24 ? 37  LYS A NZ  1 
ATOM   327  N  N   . GLU A 1 41  ? -3.193  -30.394 -5.127  1.00 24.58 ? 38  GLU A N   1 
ATOM   328  C  CA  . GLU A 1 41  ? -2.411  -29.553 -6.021  1.00 25.85 ? 38  GLU A CA  1 
ATOM   329  C  C   . GLU A 1 41  ? -1.288  -30.367 -6.661  1.00 27.10 ? 38  GLU A C   1 
ATOM   330  O  O   . GLU A 1 41  ? -0.982  -30.161 -7.833  1.00 28.18 ? 38  GLU A O   1 
ATOM   331  C  CB  . GLU A 1 41  ? -1.910  -28.309 -5.287  1.00 27.39 ? 38  GLU A CB  1 
ATOM   332  C  CG  . GLU A 1 41  ? -3.043  -27.342 -4.960  1.00 28.39 ? 38  GLU A CG  1 
ATOM   333  C  CD  . GLU A 1 41  ? -2.658  -26.085 -4.204  1.00 29.28 ? 38  GLU A CD  1 
ATOM   334  O  OE1 . GLU A 1 41  ? -1.448  -25.818 -4.043  1.00 31.09 ? 38  GLU A OE1 1 
ATOM   335  O  OE2 . GLU A 1 41  ? -3.591  -25.390 -3.753  1.00 30.17 ? 38  GLU A OE2 1 
ATOM   336  N  N   . SER A 1 42  ? -0.684  -31.288 -5.897  1.00 28.70 ? 39  SER A N   1 
ATOM   337  C  CA  . SER A 1 42  ? 0.349   -32.160 -6.438  1.00 29.26 ? 39  SER A CA  1 
ATOM   338  C  C   . SER A 1 42  ? -0.244  -33.117 -7.471  1.00 31.23 ? 39  SER A C   1 
ATOM   339  O  O   . SER A 1 42  ? 0.354   -33.333 -8.523  1.00 33.21 ? 39  SER A O   1 
ATOM   340  C  CB  . SER A 1 42  ? 1.093   -32.911 -5.354  1.00 28.61 ? 39  SER A CB  1 
ATOM   341  O  OG  . SER A 1 42  ? 0.336   -33.985 -4.813  1.00 27.97 ? 39  SER A OG  1 
ATOM   342  N  N   . ASP A 1 43  ? -1.422  -33.675 -7.161  1.00 32.17 ? 40  ASP A N   1 
ATOM   343  C  CA  . ASP A 1 43  ? -2.121  -34.603 -8.040  1.00 33.36 ? 40  ASP A CA  1 
ATOM   344  C  C   . ASP A 1 43  ? -2.539  -33.932 -9.352  1.00 35.51 ? 40  ASP A C   1 
ATOM   345  O  O   . ASP A 1 43  ? -2.724  -34.616 -10.356 1.00 36.18 ? 40  ASP A O   1 
ATOM   346  C  CB  . ASP A 1 43  ? -3.332  -35.206 -7.341  1.00 34.39 ? 40  ASP A CB  1 
ATOM   347  C  CG  . ASP A 1 43  ? -4.173  -36.179 -8.159  1.00 35.76 ? 40  ASP A CG  1 
ATOM   348  O  OD1 . ASP A 1 43  ? -3.709  -37.319 -8.383  1.00 37.71 ? 40  ASP A OD1 1 
ATOM   349  O  OD2 . ASP A 1 43  ? -5.285  -35.791 -8.576  1.00 36.36 ? 40  ASP A OD2 1 
ATOM   350  N  N   A GLN A 1 44  ? -2.709  -32.602 -9.334  0.66 35.59 ? 41  GLN A N   1 
ATOM   351  N  N   B GLN A 1 44  ? -2.668  -32.599 -9.335  0.34 36.17 ? 41  GLN A N   1 
ATOM   352  C  CA  A GLN A 1 44  ? -3.196  -31.870 -10.494 0.66 36.74 ? 41  GLN A CA  1 
ATOM   353  C  CA  B GLN A 1 44  ? -3.196  -31.860 -10.468 0.34 37.43 ? 41  GLN A CA  1 
ATOM   354  C  C   A GLN A 1 44  ? -2.154  -31.841 -11.609 0.66 37.79 ? 41  GLN A C   1 
ATOM   355  C  C   B GLN A 1 44  ? -2.167  -31.793 -11.598 0.34 37.79 ? 41  GLN A C   1 
ATOM   356  O  O   A GLN A 1 44  ? -2.506  -31.974 -12.779 0.66 38.61 ? 41  GLN A O   1 
ATOM   357  O  O   B GLN A 1 44  ? -2.540  -31.860 -12.767 0.34 38.23 ? 41  GLN A O   1 
ATOM   358  C  CB  A GLN A 1 44  ? -3.591  -30.432 -10.157 0.66 36.77 ? 41  GLN A CB  1 
ATOM   359  C  CB  B GLN A 1 44  ? -3.609  -30.452 -10.038 0.34 38.13 ? 41  GLN A CB  1 
ATOM   360  C  CG  A GLN A 1 44  ? -4.966  -30.298 -9.514  0.66 36.17 ? 41  GLN A CG  1 
ATOM   361  C  CG  B GLN A 1 44  ? -5.023  -30.071 -10.464 0.34 38.49 ? 41  GLN A CG  1 
ATOM   362  C  CD  A GLN A 1 44  ? -5.350  -28.858 -9.266  0.66 35.83 ? 41  GLN A CD  1 
ATOM   363  C  CD  B GLN A 1 44  ? -5.191  -28.588 -10.710 0.34 38.86 ? 41  GLN A CD  1 
ATOM   364  O  OE1 A GLN A 1 44  ? -5.298  -28.373 -8.131  0.66 33.92 ? 41  GLN A OE1 1 
ATOM   365  O  OE1 B GLN A 1 44  ? -4.714  -28.045 -11.713 0.34 38.64 ? 41  GLN A OE1 1 
ATOM   366  N  NE2 A GLN A 1 44  ? -5.708  -28.156 -10.332 0.66 37.29 ? 41  GLN A NE2 1 
ATOM   367  N  NE2 B GLN A 1 44  ? -5.891  -27.920 -9.803  0.34 39.68 ? 41  GLN A NE2 1 
ATOM   368  N  N   . PHE A 1 45  ? -0.880  -31.651 -11.247 1.00 38.06 ? 42  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 45  ? 0.173   -31.463 -12.238 1.00 40.10 ? 42  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 45  ? 1.191   -32.598 -12.163 1.00 39.63 ? 42  PHE A C   1 
ATOM   371  O  O   . PHE A 1 45  ? 1.663   -32.941 -11.082 1.00 38.27 ? 42  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 45  ? 0.839   -30.098 -12.049 1.00 41.12 ? 42  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 45  ? -0.139  -28.943 -12.205 1.00 41.95 ? 42  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 45  ? -0.514  -28.491 -13.467 1.00 43.06 ? 42  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 45  ? -0.699  -28.329 -11.091 1.00 41.91 ? 42  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 45  ? -1.418  -27.448 -13.608 1.00 42.94 ? 42  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 45  ? -1.598  -27.284 -11.237 1.00 42.54 ? 42  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 45  ? -1.955  -26.845 -12.492 1.00 43.31 ? 42  PHE A CZ  1 
ATOM   379  N  N   . PRO A 1 46  ? 1.601   -33.181 -13.315 1.00 43.67 ? 43  PRO A N   1 
ATOM   380  C  CA  . PRO A 1 46  ? 2.507   -34.324 -13.304 1.00 43.93 ? 43  PRO A CA  1 
ATOM   381  C  C   . PRO A 1 46  ? 3.950   -33.962 -12.958 1.00 43.31 ? 43  PRO A C   1 
ATOM   382  O  O   . PRO A 1 46  ? 4.742   -34.848 -12.644 1.00 42.82 ? 43  PRO A O   1 
ATOM   383  C  CB  . PRO A 1 46  ? 2.385   -34.913 -14.706 1.00 44.94 ? 43  PRO A CB  1 
ATOM   384  C  CG  . PRO A 1 46  ? 1.765   -33.825 -15.564 1.00 44.85 ? 43  PRO A CG  1 
ATOM   385  C  CD  . PRO A 1 46  ? 1.251   -32.730 -14.673 1.00 44.47 ? 43  PRO A CD  1 
ATOM   386  N  N   . GLU A 1 47  ? 4.273   -32.662 -13.023 1.00 43.37 ? 44  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 47  ? 5.564   -32.138 -12.601 1.00 42.53 ? 44  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 47  ? 5.786   -32.382 -11.109 1.00 39.71 ? 44  GLU A C   1 
ATOM   389  O  O   . GLU A 1 47  ? 6.930   -32.512 -10.674 1.00 38.91 ? 44  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 47  ? 5.658   -30.637 -12.895 1.00 44.03 ? 44  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 47  ? 4.660   -29.782 -12.115 1.00 44.57 ? 44  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 47  ? 4.711   -28.295 -12.416 1.00 45.55 ? 44  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 47  ? 4.279   -27.875 -13.512 1.00 45.06 ? 44  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 47  ? 5.194   -27.561 -11.532 1.00 46.11 ? 44  GLU A OE2 1 
ATOM   395  N  N   . TRP A 1 48  ? 4.687   -32.404 -10.337 1.00 37.17 ? 45  TRP A N   1 
ATOM   396  C  CA  . TRP A 1 48  ? 4.733   -32.519 -8.888  1.00 34.34 ? 45  TRP A CA  1 
ATOM   397  C  C   . TRP A 1 48  ? 4.409   -33.946 -8.464  1.00 32.21 ? 45  TRP A C   1 
ATOM   398  O  O   . TRP A 1 48  ? 3.618   -34.628 -9.113  1.00 31.97 ? 45  TRP A O   1 
ATOM   399  C  CB  . TRP A 1 48  ? 3.741   -31.545 -8.234  1.00 34.11 ? 45  TRP A CB  1 
ATOM   400  C  CG  . TRP A 1 48  ? 4.219   -30.120 -8.149  1.00 33.81 ? 45  TRP A CG  1 
ATOM   401  C  CD1 . TRP A 1 48  ? 5.501   -29.680 -7.989  1.00 34.18 ? 45  TRP A CD1 1 
ATOM   402  C  CD2 . TRP A 1 48  ? 3.394   -28.937 -8.205  1.00 33.24 ? 45  TRP A CD2 1 
ATOM   403  N  NE1 . TRP A 1 48  ? 5.533   -28.312 -7.946  1.00 34.25 ? 45  TRP A NE1 1 
ATOM   404  C  CE2 . TRP A 1 48  ? 4.259   -27.828 -8.077  1.00 34.11 ? 45  TRP A CE2 1 
ATOM   405  C  CE3 . TRP A 1 48  ? 2.021   -28.708 -8.353  1.00 33.56 ? 45  TRP A CE3 1 
ATOM   406  C  CZ2 . TRP A 1 48  ? 3.789   -26.518 -8.095  1.00 33.41 ? 45  TRP A CZ2 1 
ATOM   407  C  CZ3 . TRP A 1 48  ? 1.561   -27.410 -8.368  1.00 33.48 ? 45  TRP A CZ3 1 
ATOM   408  C  CH2 . TRP A 1 48  ? 2.434   -26.332 -8.240  1.00 34.26 ? 45  TRP A CH2 1 
ATOM   409  N  N   . GLU A 1 49  ? 5.004   -34.363 -7.344  1.00 30.26 ? 46  GLU A N   1 
ATOM   410  C  CA  . GLU A 1 49  ? 4.698   -35.653 -6.757  1.00 30.42 ? 46  GLU A CA  1 
ATOM   411  C  C   . GLU A 1 49  ? 4.778   -35.534 -5.237  1.00 26.62 ? 46  GLU A C   1 
ATOM   412  O  O   . GLU A 1 49  ? 5.707   -34.936 -4.703  1.00 24.89 ? 46  GLU A O   1 
ATOM   413  C  CB  . GLU A 1 49  ? 5.619   -36.718 -7.356  1.00 33.05 ? 46  GLU A CB  1 
ATOM   414  C  CG  . GLU A 1 49  ? 5.047   -38.131 -7.255  1.00 35.81 ? 46  GLU A CG  1 
ATOM   415  C  CD  . GLU A 1 49  ? 5.615   -39.131 -8.250  1.00 38.19 ? 46  GLU A CD  1 
ATOM   416  O  OE1 . GLU A 1 49  ? 6.324   -38.723 -9.198  1.00 40.35 ? 46  GLU A OE1 1 
ATOM   417  O  OE2 . GLU A 1 49  ? 5.346   -40.338 -8.068  1.00 41.70 ? 46  GLU A OE2 1 
ATOM   418  N  N   . SER A 1 50  ? 3.762   -36.090 -4.567  1.00 24.86 ? 47  SER A N   1 
ATOM   419  C  CA  . SER A 1 50  ? 3.727   -36.194 -3.120  1.00 24.56 ? 47  SER A CA  1 
ATOM   420  C  C   . SER A 1 50  ? 4.133   -37.607 -2.712  1.00 24.03 ? 47  SER A C   1 
ATOM   421  O  O   . SER A 1 50  ? 3.907   -38.559 -3.458  1.00 25.96 ? 47  SER A O   1 
ATOM   422  C  CB  . SER A 1 50  ? 2.351   -35.848 -2.592  1.00 24.91 ? 47  SER A CB  1 
ATOM   423  O  OG  . SER A 1 50  ? 2.075   -34.456 -2.690  1.00 25.67 ? 47  SER A OG  1 
ATOM   424  N  N   . ALA A 1 51  ? 4.706   -37.734 -1.511  1.00 22.88 ? 48  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 51  ? 5.081   -39.024 -0.963  1.00 22.99 ? 48  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 51  ? 4.834   -39.020 0.542   1.00 22.18 ? 48  ALA A C   1 
ATOM   427  O  O   . ALA A 1 51  ? 5.088   -38.022 1.211   1.00 22.36 ? 48  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 51  ? 6.535   -39.311 -1.280  1.00 23.31 ? 48  ALA A CB  1 
ATOM   429  N  N   . GLY A 1 52  ? 4.331   -40.142 1.065   1.00 22.26 ? 49  GLY A N   1 
ATOM   430  C  CA  . GLY A 1 52  ? 4.369   -40.387 2.495   1.00 21.41 ? 49  GLY A CA  1 
ATOM   431  C  C   . GLY A 1 52  ? 5.731   -40.949 2.896   1.00 21.76 ? 49  GLY A C   1 
ATOM   432  O  O   . GLY A 1 52  ? 6.308   -41.761 2.170   1.00 21.38 ? 49  GLY A O   1 
ATOM   433  N  N   . ILE A 1 53  ? 6.240   -40.485 4.043   1.00 21.61 ? 50  ILE A N   1 
ATOM   434  C  CA  . ILE A 1 53  ? 7.499   -40.958 4.596   1.00 21.53 ? 50  ILE A CA  1 
ATOM   435  C  C   . ILE A 1 53  ? 7.179   -41.953 5.705   1.00 21.13 ? 50  ILE A C   1 
ATOM   436  O  O   . ILE A 1 53  ? 6.418   -41.641 6.620   1.00 21.18 ? 50  ILE A O   1 
ATOM   437  C  CB  . ILE A 1 53  ? 8.356   -39.797 5.131   1.00 22.29 ? 50  ILE A CB  1 
ATOM   438  C  CG1 . ILE A 1 53  ? 8.555   -38.702 4.081   1.00 21.74 ? 50  ILE A CG1 1 
ATOM   439  C  CG2 . ILE A 1 53  ? 9.684   -40.327 5.670   1.00 22.73 ? 50  ILE A CG2 1 
ATOM   440  C  CD1 . ILE A 1 53  ? 9.329   -37.497 4.583   1.00 22.14 ? 50  ILE A CD1 1 
ATOM   441  N  N   . TYR A 1 54  ? 7.783   -43.142 5.618   1.00 21.11 ? 51  TYR A N   1 
ATOM   442  C  CA  . TYR A 1 54  ? 7.493   -44.228 6.537   1.00 21.77 ? 51  TYR A CA  1 
ATOM   443  C  C   . TYR A 1 54  ? 8.749   -44.679 7.273   1.00 21.97 ? 51  TYR A C   1 
ATOM   444  O  O   . TYR A 1 54  ? 9.846   -44.657 6.719   1.00 21.27 ? 51  TYR A O   1 
ATOM   445  C  CB  . TYR A 1 54  ? 6.899   -45.408 5.765   1.00 21.35 ? 51  TYR A CB  1 
ATOM   446  C  CG  . TYR A 1 54  ? 5.471   -45.166 5.304   1.00 21.72 ? 51  TYR A CG  1 
ATOM   447  C  CD1 . TYR A 1 54  ? 5.202   -44.496 4.116   1.00 22.31 ? 51  TYR A CD1 1 
ATOM   448  C  CD2 . TYR A 1 54  ? 4.393   -45.606 6.063   1.00 22.85 ? 51  TYR A CD2 1 
ATOM   449  C  CE1 . TYR A 1 54  ? 3.903   -44.254 3.705   1.00 22.87 ? 51  TYR A CE1 1 
ATOM   450  C  CE2 . TYR A 1 54  ? 3.090   -45.375 5.658   1.00 23.41 ? 51  TYR A CE2 1 
ATOM   451  C  CZ  . TYR A 1 54  ? 2.844   -44.703 4.473   1.00 23.34 ? 51  TYR A CZ  1 
ATOM   452  O  OH  . TYR A 1 54  ? 1.563   -44.480 4.062   1.00 25.37 ? 51  TYR A OH  1 
ATOM   453  N  N   . ASP A 1 55  ? 8.557   -45.075 8.537   1.00 22.89 ? 52  ASP A N   1 
ATOM   454  C  CA  . ASP A 1 55  ? 9.490   -45.934 9.241   1.00 24.51 ? 52  ASP A CA  1 
ATOM   455  C  C   . ASP A 1 55  ? 8.777   -47.265 9.449   1.00 24.76 ? 52  ASP A C   1 
ATOM   456  O  O   . ASP A 1 55  ? 7.910   -47.374 10.317  1.00 24.96 ? 52  ASP A O   1 
ATOM   457  C  CB  . ASP A 1 55  ? 9.959   -45.335 10.558  1.00 26.48 ? 52  ASP A CB  1 
ATOM   458  C  CG  . ASP A 1 55  ? 10.965  -46.189 11.319  1.00 28.54 ? 52  ASP A CG  1 
ATOM   459  O  OD1 . ASP A 1 55  ? 11.552  -47.101 10.698  1.00 29.08 ? 52  ASP A OD1 1 
ATOM   460  O  OD2 . ASP A 1 55  ? 11.143  -45.951 12.532  1.00 31.61 ? 52  ASP A OD2 1 
ATOM   461  N  N   . GLY A 1 56  ? 9.129   -48.257 8.623   1.00 25.12 ? 53  GLY A N   1 
ATOM   462  C  CA  . GLY A 1 56  ? 8.381   -49.499 8.556   1.00 26.08 ? 53  GLY A CA  1 
ATOM   463  C  C   . GLY A 1 56  ? 6.941   -49.242 8.117   1.00 27.02 ? 53  GLY A C   1 
ATOM   464  O  O   . GLY A 1 56  ? 6.711   -48.715 7.031   1.00 29.17 ? 53  GLY A O   1 
ATOM   465  N  N   . ASN A 1 57  ? 5.981   -49.584 8.985   1.00 28.23 ? 54  ASN A N   1 
ATOM   466  C  CA  . ASN A 1 57  ? 4.568   -49.410 8.678   1.00 28.81 ? 54  ASN A CA  1 
ATOM   467  C  C   . ASN A 1 57  ? 4.029   -48.095 9.239   1.00 29.01 ? 54  ASN A C   1 
ATOM   468  O  O   . ASN A 1 57  ? 2.868   -47.762 9.007   1.00 29.62 ? 54  ASN A O   1 
ATOM   469  C  CB  . ASN A 1 57  ? 3.728   -50.577 9.187   1.00 30.08 ? 54  ASN A CB  1 
ATOM   470  C  CG  . ASN A 1 57  ? 3.979   -51.834 8.392   1.00 31.52 ? 54  ASN A CG  1 
ATOM   471  O  OD1 . ASN A 1 57  ? 4.169   -51.764 7.172   1.00 33.31 ? 54  ASN A OD1 1 
ATOM   472  N  ND2 . ASN A 1 57  ? 3.998   -52.979 9.057   1.00 33.41 ? 54  ASN A ND2 1 
ATOM   473  N  N   . GLN A 1 58  ? 4.871   -47.345 9.963   1.00 28.85 ? 55  GLN A N   1 
ATOM   474  C  CA  . GLN A 1 58  ? 4.438   -46.110 10.597  1.00 28.61 ? 55  GLN A CA  1 
ATOM   475  C  C   . GLN A 1 58  ? 4.724   -44.929 9.674   1.00 27.48 ? 55  GLN A C   1 
ATOM   476  O  O   . GLN A 1 58  ? 5.878   -44.667 9.336   1.00 26.58 ? 55  GLN A O   1 
ATOM   477  C  CB  . GLN A 1 58  ? 5.140   -45.934 11.943  1.00 30.56 ? 55  GLN A CB  1 
ATOM   478  C  CG  . GLN A 1 58  ? 4.764   -44.664 12.701  1.00 32.52 ? 55  GLN A CG  1 
ATOM   479  C  CD  . GLN A 1 58  ? 3.287   -44.564 13.019  1.00 33.43 ? 55  GLN A CD  1 
ATOM   480  O  OE1 . GLN A 1 58  ? 2.676   -45.499 13.548  1.00 35.89 ? 55  GLN A OE1 1 
ATOM   481  N  NE2 . GLN A 1 58  ? 2.693   -43.423 12.698  1.00 34.04 ? 55  GLN A NE2 1 
ATOM   482  N  N   . LEU A 1 59  ? 3.664   -44.208 9.287   1.00 27.22 ? 56  LEU A N   1 
ATOM   483  C  CA  . LEU A 1 59  ? 3.816   -42.946 8.582   1.00 25.84 ? 56  LEU A CA  1 
ATOM   484  C  C   . LEU A 1 59  ? 4.391   -41.919 9.553   1.00 26.15 ? 56  LEU A C   1 
ATOM   485  O  O   . LEU A 1 59  ? 3.759   -41.620 10.569  1.00 27.42 ? 56  LEU A O   1 
ATOM   486  C  CB  . LEU A 1 59  ? 2.475   -42.473 8.024   1.00 26.07 ? 56  LEU A CB  1 
ATOM   487  C  CG  . LEU A 1 59  ? 2.507   -41.143 7.260   1.00 26.25 ? 56  LEU A CG  1 
ATOM   488  C  CD1 . LEU A 1 59  ? 3.159   -41.315 5.900   1.00 26.37 ? 56  LEU A CD1 1 
ATOM   489  C  CD2 . LEU A 1 59  ? 1.116   -40.558 7.118   1.00 27.30 ? 56  LEU A CD2 1 
ATOM   490  N  N   . ILE A 1 60  ? 5.569   -41.368 9.221   1.00 25.17 ? 57  ILE A N   1 
ATOM   491  C  CA  . ILE A 1 60  ? 6.247   -40.419 10.093  1.00 24.90 ? 57  ILE A CA  1 
ATOM   492  C  C   . ILE A 1 60  ? 6.315   -39.024 9.474   1.00 24.47 ? 57  ILE A C   1 
ATOM   493  O  O   . ILE A 1 60  ? 6.745   -38.090 10.144  1.00 24.91 ? 57  ILE A O   1 
ATOM   494  C  CB  . ILE A 1 60  ? 7.665   -40.897 10.446  1.00 25.12 ? 57  ILE A CB  1 
ATOM   495  C  CG1 . ILE A 1 60  ? 8.543   -41.063 9.200   1.00 25.97 ? 57  ILE A CG1 1 
ATOM   496  C  CG2 . ILE A 1 60  ? 7.606   -42.166 11.293  1.00 25.01 ? 57  ILE A CG2 1 
ATOM   497  C  CD1 . ILE A 1 60  ? 10.033  -41.140 9.493   1.00 26.07 ? 57  ILE A CD1 1 
ATOM   498  N  N   . GLY A 1 61  ? 5.954   -38.879 8.195   1.00 23.85 ? 58  GLY A N   1 
ATOM   499  C  CA  . GLY A 1 61  ? 6.081   -37.584 7.557   1.00 22.84 ? 58  GLY A CA  1 
ATOM   500  C  C   . GLY A 1 61  ? 5.573   -37.573 6.121   1.00 21.78 ? 58  GLY A C   1 
ATOM   501  O  O   . GLY A 1 61  ? 4.849   -38.470 5.688   1.00 21.12 ? 58  GLY A O   1 
ATOM   502  N  N   . TYR A 1 62  ? 5.966   -36.509 5.418   1.00 21.92 ? 59  TYR A N   1 
ATOM   503  C  CA  . TYR A 1 62  ? 5.452   -36.179 4.104   1.00 21.98 ? 59  TYR A CA  1 
ATOM   504  C  C   . TYR A 1 62  ? 6.481   -35.340 3.359   1.00 21.14 ? 59  TYR A C   1 
ATOM   505  O  O   . TYR A 1 62  ? 7.212   -34.556 3.969   1.00 21.08 ? 59  TYR A O   1 
ATOM   506  C  CB  . TYR A 1 62  ? 4.153   -35.392 4.272   1.00 22.96 ? 59  TYR A CB  1 
ATOM   507  C  CG  . TYR A 1 62  ? 3.655   -34.703 3.010   1.00 23.24 ? 59  TYR A CG  1 
ATOM   508  C  CD1 . TYR A 1 62  ? 3.045   -35.434 1.998   1.00 24.12 ? 59  TYR A CD1 1 
ATOM   509  C  CD2 . TYR A 1 62  ? 3.760   -33.325 2.846   1.00 24.02 ? 59  TYR A CD2 1 
ATOM   510  C  CE1 . TYR A 1 62  ? 2.568   -34.819 0.853   1.00 24.74 ? 59  TYR A CE1 1 
ATOM   511  C  CE2 . TYR A 1 62  ? 3.294   -32.700 1.700   1.00 24.40 ? 59  TYR A CE2 1 
ATOM   512  C  CZ  . TYR A 1 62  ? 2.687   -33.449 0.705   1.00 25.01 ? 59  TYR A CZ  1 
ATOM   513  O  OH  . TYR A 1 62  ? 2.217   -32.842 -0.424  1.00 27.09 ? 59  TYR A OH  1 
ATOM   514  N  N   . ALA A 1 63  ? 6.500   -35.493 2.035   1.00 20.69 ? 60  ALA A N   1 
ATOM   515  C  CA  . ALA A 1 63  ? 7.327   -34.658 1.187   1.00 21.08 ? 60  ALA A CA  1 
ATOM   516  C  C   . ALA A 1 63  ? 6.644   -34.452 -0.160  1.00 21.60 ? 60  ALA A C   1 
ATOM   517  O  O   . ALA A 1 63  ? 5.910   -35.316 -0.640  1.00 21.40 ? 60  ALA A O   1 
ATOM   518  C  CB  . ALA A 1 63  ? 8.703   -35.273 1.022   1.00 21.42 ? 60  ALA A CB  1 
ATOM   519  N  N   A MET A 1 64  ? 6.836   -33.261 -0.731  0.61 22.38 ? 61  MET A N   1 
ATOM   520  N  N   B MET A 1 64  ? 6.934   -33.296 -0.761  0.39 22.03 ? 61  MET A N   1 
ATOM   521  C  CA  A MET A 1 64  ? 6.485   -33.003 -2.116  0.61 23.37 ? 61  MET A CA  1 
ATOM   522  C  CA  B MET A 1 64  ? 6.484   -32.956 -2.097  0.39 22.67 ? 61  MET A CA  1 
ATOM   523  C  C   A MET A 1 64  ? 7.734   -32.508 -2.835  0.61 23.51 ? 61  MET A C   1 
ATOM   524  C  C   B MET A 1 64  ? 7.684   -32.417 -2.869  0.39 23.26 ? 61  MET A C   1 
ATOM   525  O  O   A MET A 1 64  ? 8.557   -31.803 -2.249  0.61 24.04 ? 61  MET A O   1 
ATOM   526  O  O   B MET A 1 64  ? 8.431   -31.589 -2.348  0.39 23.78 ? 61  MET A O   1 
ATOM   527  C  CB  A MET A 1 64  ? 5.372   -31.958 -2.259  0.61 24.38 ? 61  MET A CB  1 
ATOM   528  C  CB  B MET A 1 64  ? 5.378   -31.899 -2.039  0.39 23.17 ? 61  MET A CB  1 
ATOM   529  C  CG  A MET A 1 64  ? 4.853   -31.833 -3.682  0.61 25.54 ? 61  MET A CG  1 
ATOM   530  C  CG  B MET A 1 64  ? 4.860   -31.473 -3.390  0.39 23.38 ? 61  MET A CG  1 
ATOM   531  S  SD  A MET A 1 64  ? 3.732   -30.444 -3.932  0.61 29.02 ? 61  MET A SD  1 
ATOM   532  S  SD  B MET A 1 64  ? 3.509   -30.296 -3.195  0.39 24.69 ? 61  MET A SD  1 
ATOM   533  C  CE  A MET A 1 64  ? 2.467   -30.808 -2.710  0.61 29.35 ? 61  MET A CE  1 
ATOM   534  C  CE  B MET A 1 64  ? 3.219   -29.821 -4.905  0.39 25.58 ? 61  MET A CE  1 
ATOM   535  N  N   . TYR A 1 65  ? 7.856   -32.891 -4.109  1.00 23.53 ? 62  TYR A N   1 
ATOM   536  C  CA  . TYR A 1 65  ? 9.015   -32.544 -4.913  1.00 25.02 ? 62  TYR A CA  1 
ATOM   537  C  C   . TYR A 1 65  ? 8.635   -32.610 -6.387  1.00 26.00 ? 62  TYR A C   1 
ATOM   538  O  O   . TYR A 1 65  ? 7.512   -32.975 -6.725  1.00 27.26 ? 62  TYR A O   1 
ATOM   539  C  CB  . TYR A 1 65  ? 10.141  -33.531 -4.592  1.00 26.29 ? 62  TYR A CB  1 
ATOM   540  C  CG  . TYR A 1 65  ? 9.735   -34.983 -4.805  1.00 27.44 ? 62  TYR A CG  1 
ATOM   541  C  CD1 . TYR A 1 65  ? 9.751   -35.556 -6.072  1.00 28.77 ? 62  TYR A CD1 1 
ATOM   542  C  CD2 . TYR A 1 65  ? 9.326   -35.775 -3.740  1.00 28.02 ? 62  TYR A CD2 1 
ATOM   543  C  CE1 . TYR A 1 65  ? 9.381   -36.875 -6.272  1.00 29.90 ? 62  TYR A CE1 1 
ATOM   544  C  CE2 . TYR A 1 65  ? 8.949   -37.095 -3.926  1.00 30.63 ? 62  TYR A CE2 1 
ATOM   545  C  CZ  . TYR A 1 65  ? 8.975   -37.644 -5.197  1.00 30.75 ? 62  TYR A CZ  1 
ATOM   546  O  OH  . TYR A 1 65  ? 8.616   -38.940 -5.413  1.00 33.33 ? 62  TYR A OH  1 
ATOM   547  N  N   . GLY A 1 66  ? 9.594   -32.294 -7.262  1.00 28.08 ? 63  GLY A N   1 
ATOM   548  C  CA  . GLY A 1 66  ? 9.363   -32.452 -8.686  1.00 29.00 ? 63  GLY A CA  1 
ATOM   549  C  C   . GLY A 1 66  ? 10.288  -31.588 -9.534  1.00 30.25 ? 63  GLY A C   1 
ATOM   550  O  O   . GLY A 1 66  ? 10.915  -30.648 -9.045  1.00 29.66 ? 63  GLY A O   1 
ATOM   551  N  N   . ARG A 1 67  ? 10.337  -31.941 -10.821 1.00 34.52 ? 64  ARG A N   1 
ATOM   552  C  CA  . ARG A 1 67  ? 11.090  -31.211 -11.823 1.00 37.89 ? 64  ARG A CA  1 
ATOM   553  C  C   . ARG A 1 67  ? 10.246  -30.034 -12.298 1.00 40.90 ? 64  ARG A C   1 
ATOM   554  O  O   . ARG A 1 67  ? 9.185   -30.222 -12.894 1.00 41.36 ? 64  ARG A O   1 
ATOM   555  C  CB  . ARG A 1 67  ? 11.444  -32.152 -12.980 1.00 40.30 ? 64  ARG A CB  1 
ATOM   556  C  CG  . ARG A 1 67  ? 12.020  -31.467 -14.210 1.00 41.87 ? 64  ARG A CG  1 
ATOM   557  C  CD  . ARG A 1 67  ? 12.079  -32.414 -15.397 1.00 43.66 ? 64  ARG A CD  1 
ATOM   558  N  NE  . ARG A 1 67  ? 12.316  -31.709 -16.662 1.00 45.14 ? 64  ARG A NE  1 
ATOM   559  C  CZ  . ARG A 1 67  ? 11.447  -30.917 -17.292 1.00 47.36 ? 64  ARG A CZ  1 
ATOM   560  N  NH1 . ARG A 1 67  ? 10.223  -30.736 -16.818 1.00 47.84 ? 64  ARG A NH1 1 
ATOM   561  N  NH2 . ARG A 1 67  ? 11.806  -30.312 -18.413 1.00 47.80 ? 64  ARG A NH2 1 
ATOM   562  N  N   . TRP A 1 68  ? 10.727  -28.822 -12.010 1.00 44.58 ? 65  TRP A N   1 
ATOM   563  C  CA  . TRP A 1 68  ? 10.091  -27.611 -12.495 1.00 47.88 ? 65  TRP A CA  1 
ATOM   564  C  C   . TRP A 1 68  ? 10.542  -27.356 -13.935 1.00 51.41 ? 65  TRP A C   1 
ATOM   565  O  O   . TRP A 1 68  ? 11.539  -27.918 -14.385 1.00 52.06 ? 65  TRP A O   1 
ATOM   566  C  CB  . TRP A 1 68  ? 10.409  -26.443 -11.549 0.80 49.74 ? 65  TRP A CB  1 
ATOM   567  C  CG  . TRP A 1 68  ? 9.821   -25.128 -11.980 1.00 52.16 ? 65  TRP A CG  1 
ATOM   568  C  CD1 . TRP A 1 68  ? 10.471  -23.932 -12.044 1.00 53.37 ? 65  TRP A CD1 1 
ATOM   569  C  CD2 . TRP A 1 68  ? 8.471   -24.878 -12.433 1.00 53.51 ? 65  TRP A CD2 1 
ATOM   570  N  NE1 . TRP A 1 68  ? 9.631   -22.956 -12.506 0.98 54.10 ? 65  TRP A NE1 1 
ATOM   571  C  CE2 . TRP A 1 68  ? 8.401   -23.505 -12.754 1.00 53.68 ? 65  TRP A CE2 1 
ATOM   572  C  CE3 . TRP A 1 68  ? 7.329   -25.668 -12.606 0.89 54.13 ? 65  TRP A CE3 1 
ATOM   573  C  CZ2 . TRP A 1 68  ? 7.235   -22.915 -13.231 0.69 54.31 ? 65  TRP A CZ2 1 
ATOM   574  C  CZ3 . TRP A 1 68  ? 6.175   -25.080 -13.077 0.87 54.43 ? 65  TRP A CZ3 1 
ATOM   575  C  CH2 . TRP A 1 68  ? 6.133   -23.723 -13.392 0.85 54.39 ? 65  TRP A CH2 1 
ATOM   576  N  N   . GLN A 1 69  ? 9.784   -26.516 -14.651 1.00 54.54 ? 66  GLN A N   1 
ATOM   577  C  CA  . GLN A 1 69  ? 9.906   -26.340 -16.090 1.00 57.33 ? 66  GLN A CA  1 
ATOM   578  C  C   . GLN A 1 69  ? 11.327  -25.981 -16.520 1.00 57.64 ? 66  GLN A C   1 
ATOM   579  O  O   . GLN A 1 69  ? 11.731  -26.334 -17.627 1.00 60.19 ? 66  GLN A O   1 
ATOM   580  C  CB  . GLN A 1 69  ? 8.929   -25.266 -16.571 1.00 58.85 ? 66  GLN A CB  1 
ATOM   581  C  CG  . GLN A 1 69  ? 7.459   -25.618 -16.369 1.00 59.69 ? 66  GLN A CG  1 
ATOM   582  C  CD  . GLN A 1 69  ? 7.165   -27.089 -16.567 1.00 60.60 ? 66  GLN A CD  1 
ATOM   583  O  OE1 . GLN A 1 69  ? 7.263   -27.629 -17.675 1.00 61.42 ? 66  GLN A OE1 1 
ATOM   584  N  NE2 . GLN A 1 69  ? 6.811   -27.756 -15.479 1.00 61.02 ? 66  GLN A NE2 1 
ATOM   585  N  N   . ASP A 1 70  ? 12.078  -25.285 -15.656 1.00 56.65 ? 67  ASP A N   1 
ATOM   586  C  CA  . ASP A 1 70  ? 13.457  -24.928 -15.965 1.00 54.37 ? 67  ASP A CA  1 
ATOM   587  C  C   . ASP A 1 70  ? 14.355  -26.167 -15.994 1.00 52.11 ? 67  ASP A C   1 
ATOM   588  O  O   . ASP A 1 70  ? 15.505  -26.078 -16.417 1.00 53.01 ? 67  ASP A O   1 
ATOM   589  C  CB  . ASP A 1 70  ? 14.007  -23.860 -15.028 1.00 54.15 ? 67  ASP A CB  1 
ATOM   590  C  CG  . ASP A 1 70  ? 13.647  -24.000 -13.557 1.00 53.79 ? 67  ASP A CG  1 
ATOM   591  O  OD1 . ASP A 1 70  ? 13.539  -25.148 -13.083 1.00 54.41 ? 67  ASP A OD1 1 
ATOM   592  O  OD2 . ASP A 1 70  ? 13.501  -22.953 -12.896 1.00 53.75 ? 67  ASP A OD2 1 
ATOM   593  N  N   . GLY A 1 71  ? 13.835  -27.314 -15.538 1.00 49.50 ? 68  GLY A N   1 
ATOM   594  C  CA  . GLY A 1 71  ? 14.598  -28.552 -15.505 1.00 46.34 ? 68  GLY A CA  1 
ATOM   595  C  C   . GLY A 1 71  ? 15.256  -28.766 -14.144 1.00 42.49 ? 68  GLY A C   1 
ATOM   596  O  O   . GLY A 1 71  ? 15.854  -29.813 -13.901 1.00 42.82 ? 68  GLY A O   1 
ATOM   597  N  N   . ARG A 1 72  ? 15.140  -27.762 -13.264 1.00 37.81 ? 69  ARG A N   1 
ATOM   598  C  CA  . ARG A 1 72  ? 15.643  -27.864 -11.906 1.00 34.21 ? 69  ARG A CA  1 
ATOM   599  C  C   . ARG A 1 72  ? 14.694  -28.721 -11.077 1.00 31.61 ? 69  ARG A C   1 
ATOM   600  O  O   . ARG A 1 72  ? 13.477  -28.613 -11.213 1.00 31.30 ? 69  ARG A O   1 
ATOM   601  C  CB  . ARG A 1 72  ? 15.742  -26.501 -11.219 1.00 33.83 ? 69  ARG A CB  1 
ATOM   602  C  CG  . ARG A 1 72  ? 16.820  -25.587 -11.779 1.00 34.69 ? 69  ARG A CG  1 
ATOM   603  C  CD  . ARG A 1 72  ? 16.927  -24.330 -10.943 1.00 35.75 ? 69  ARG A CD  1 
ATOM   604  N  NE  . ARG A 1 72  ? 18.191  -23.629 -11.188 1.00 36.15 ? 69  ARG A NE  1 
ATOM   605  C  CZ  . ARG A 1 72  ? 18.643  -22.612 -10.464 1.00 36.96 ? 69  ARG A CZ  1 
ATOM   606  N  NH1 . ARG A 1 72  ? 17.944  -22.171 -9.433  1.00 37.02 ? 69  ARG A NH1 1 
ATOM   607  N  NH2 . ARG A 1 72  ? 19.802  -22.051 -10.760 1.00 37.36 ? 69  ARG A NH2 1 
ATOM   608  N  N   . VAL A 1 73  ? 15.279  -29.545 -10.204 1.00 29.48 ? 70  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 73  ? 14.523  -30.427 -9.336  1.00 28.75 ? 70  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 73  ? 14.489  -29.820 -7.939  1.00 27.01 ? 70  VAL A C   1 
ATOM   611  O  O   . VAL A 1 73  ? 15.537  -29.542 -7.360  1.00 27.42 ? 70  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 73  ? 15.115  -31.847 -9.303  1.00 28.99 ? 70  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 73  ? 14.511  -32.678 -8.178  1.00 28.98 ? 70  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 73  ? 14.950  -32.552 -10.643 1.00 29.80 ? 70  VAL A CG2 1 
ATOM   615  N  N   . TRP A 1 74  ? 13.266  -29.673 -7.414  1.00 26.10 ? 71  TRP A N   1 
ATOM   616  C  CA  . TRP A 1 74  ? 13.006  -28.970 -6.172  1.00 25.76 ? 71  TRP A CA  1 
ATOM   617  C  C   . TRP A 1 74  ? 12.392  -29.895 -5.125  1.00 24.13 ? 71  TRP A C   1 
ATOM   618  O  O   . TRP A 1 74  ? 11.507  -30.696 -5.436  1.00 24.86 ? 71  TRP A O   1 
ATOM   619  C  CB  . TRP A 1 74  ? 12.055  -27.798 -6.441  1.00 26.05 ? 71  TRP A CB  1 
ATOM   620  C  CG  . TRP A 1 74  ? 12.731  -26.604 -7.053  1.00 26.24 ? 71  TRP A CG  1 
ATOM   621  C  CD1 . TRP A 1 74  ? 13.107  -26.435 -8.353  1.00 26.80 ? 71  TRP A CD1 1 
ATOM   622  C  CD2 . TRP A 1 74  ? 13.111  -25.396 -6.361  1.00 26.39 ? 71  TRP A CD2 1 
ATOM   623  N  NE1 . TRP A 1 74  ? 13.702  -25.214 -8.517  1.00 27.63 ? 71  TRP A NE1 1 
ATOM   624  C  CE2 . TRP A 1 74  ? 13.715  -24.551 -7.317  1.00 26.79 ? 71  TRP A CE2 1 
ATOM   625  C  CE3 . TRP A 1 74  ? 12.997  -24.952 -5.039  1.00 26.71 ? 71  TRP A CE3 1 
ATOM   626  C  CZ2 . TRP A 1 74  ? 14.203  -23.289 -6.985  1.00 27.30 ? 71  TRP A CZ2 1 
ATOM   627  C  CZ3 . TRP A 1 74  ? 13.477  -23.702 -4.714  1.00 27.67 ? 71  TRP A CZ3 1 
ATOM   628  C  CH2 . TRP A 1 74  ? 14.072  -22.885 -5.675  1.00 27.06 ? 71  TRP A CH2 1 
ATOM   629  N  N   . LEU A 1 75  ? 12.846  -29.730 -3.877  1.00 23.32 ? 72  LEU A N   1 
ATOM   630  C  CA  . LEU A 1 75  ? 12.127  -30.213 -2.710  1.00 22.90 ? 72  LEU A CA  1 
ATOM   631  C  C   . LEU A 1 75  ? 11.172  -29.107 -2.263  1.00 22.61 ? 72  LEU A C   1 
ATOM   632  O  O   . LEU A 1 75  ? 11.599  -28.083 -1.738  1.00 22.98 ? 72  LEU A O   1 
ATOM   633  C  CB  . LEU A 1 75  ? 13.089  -30.609 -1.591  1.00 23.33 ? 72  LEU A CB  1 
ATOM   634  C  CG  . LEU A 1 75  ? 12.441  -31.130 -0.302  1.00 25.67 ? 72  LEU A CG  1 
ATOM   635  C  CD1 . LEU A 1 75  ? 11.555  -32.338 -0.573  1.00 26.60 ? 72  LEU A CD1 1 
ATOM   636  C  CD2 . LEU A 1 75  ? 13.479  -31.476 0.753   1.00 27.35 ? 72  LEU A CD2 1 
ATOM   637  N  N   . ASP A 1 76  ? 9.875   -29.329 -2.487  1.00 22.04 ? 73  ASP A N   1 
ATOM   638  C  CA  . ASP A 1 76  ? 8.879   -28.277 -2.365  1.00 21.95 ? 73  ASP A CA  1 
ATOM   639  C  C   . ASP A 1 76  ? 8.270   -28.253 -0.964  1.00 21.23 ? 73  ASP A C   1 
ATOM   640  O  O   . ASP A 1 76  ? 7.960   -27.182 -0.446  1.00 22.50 ? 73  ASP A O   1 
ATOM   641  C  CB  . ASP A 1 76  ? 7.821   -28.416 -3.442  1.00 22.00 ? 73  ASP A CB  1 
ATOM   642  C  CG  . ASP A 1 76  ? 8.329   -28.224 -4.861  1.00 22.62 ? 73  ASP A CG  1 
ATOM   643  O  OD1 . ASP A 1 76  ? 9.005   -27.203 -5.109  1.00 22.98 ? 73  ASP A OD1 1 
ATOM   644  O  OD2 . ASP A 1 76  ? 8.052   -29.105 -5.697  1.00 25.16 ? 73  ASP A OD2 1 
ATOM   645  N  N   . ARG A 1 77  ? 8.059   -29.440 -0.384  1.00 20.35 ? 74  ARG A N   1 
ATOM   646  C  CA  . ARG A 1 77  ? 7.565   -29.568 0.977   1.00 20.54 ? 74  ARG A CA  1 
ATOM   647  C  C   . ARG A 1 77  ? 8.254   -30.754 1.642   1.00 21.74 ? 74  ARG A C   1 
ATOM   648  O  O   . ARG A 1 77  ? 8.547   -31.735 0.973   1.00 22.36 ? 74  ARG A O   1 
ATOM   649  C  CB  . ARG A 1 77  ? 6.050   -29.816 0.998   1.00 20.20 ? 74  ARG A CB  1 
ATOM   650  C  CG  . ARG A 1 77  ? 5.216   -28.753 0.296   1.00 19.67 ? 74  ARG A CG  1 
ATOM   651  C  CD  . ARG A 1 77  ? 3.745   -29.132 0.265   1.00 19.30 ? 74  ARG A CD  1 
ATOM   652  N  NE  . ARG A 1 77  ? 2.930   -28.172 -0.486  1.00 18.74 ? 74  ARG A NE  1 
ATOM   653  C  CZ  . ARG A 1 77  ? 2.561   -26.964 -0.063  1.00 17.93 ? 74  ARG A CZ  1 
ATOM   654  N  NH1 . ARG A 1 77  ? 2.850   -26.551 1.161   1.00 18.50 ? 74  ARG A NH1 1 
ATOM   655  N  NH2 . ARG A 1 77  ? 1.858   -26.170 -0.854  1.00 17.99 ? 74  ARG A NH2 1 
ATOM   656  N  N   . PHE A 1 78  ? 8.485   -30.648 2.955   1.00 22.18 ? 75  PHE A N   1 
ATOM   657  C  CA  . PHE A 1 78  ? 9.158   -31.681 3.721   1.00 22.84 ? 75  PHE A CA  1 
ATOM   658  C  C   . PHE A 1 78  ? 8.770   -31.522 5.188   1.00 23.87 ? 75  PHE A C   1 
ATOM   659  O  O   . PHE A 1 78  ? 9.141   -30.533 5.823   1.00 25.12 ? 75  PHE A O   1 
ATOM   660  C  CB  . PHE A 1 78  ? 10.671  -31.592 3.517   1.00 22.90 ? 75  PHE A CB  1 
ATOM   661  C  CG  . PHE A 1 78  ? 11.421  -32.729 4.194   1.00 24.15 ? 75  PHE A CG  1 
ATOM   662  C  CD1 . PHE A 1 78  ? 11.576  -33.949 3.548   1.00 24.00 ? 75  PHE A CD1 1 
ATOM   663  C  CD2 . PHE A 1 78  ? 11.929  -32.591 5.482   1.00 25.90 ? 75  PHE A CD2 1 
ATOM   664  C  CE1 . PHE A 1 78  ? 12.243  -34.997 4.164   1.00 24.80 ? 75  PHE A CE1 1 
ATOM   665  C  CE2 . PHE A 1 78  ? 12.597  -33.642 6.093   1.00 27.14 ? 75  PHE A CE2 1 
ATOM   666  C  CZ  . PHE A 1 78  ? 12.748  -34.844 5.436   1.00 25.48 ? 75  PHE A CZ  1 
ATOM   667  N  N   . LEU A 1 79  ? 7.985   -32.485 5.689   1.00 23.96 ? 76  LEU A N   1 
ATOM   668  C  CA  . LEU A 1 79  ? 7.443   -32.441 7.036   1.00 25.16 ? 76  LEU A CA  1 
ATOM   669  C  C   . LEU A 1 79  ? 7.704   -33.770 7.735   1.00 25.43 ? 76  LEU A C   1 
ATOM   670  O  O   . LEU A 1 79  ? 7.497   -34.826 7.146   1.00 25.20 ? 76  LEU A O   1 
ATOM   671  C  CB  . LEU A 1 79  ? 5.938   -32.186 6.990   1.00 26.88 ? 76  LEU A CB  1 
ATOM   672  C  CG  . LEU A 1 79  ? 5.484   -30.880 6.334   1.00 28.21 ? 76  LEU A CG  1 
ATOM   673  C  CD1 . LEU A 1 79  ? 3.978   -30.879 6.169   1.00 29.08 ? 76  LEU A CD1 1 
ATOM   674  C  CD2 . LEU A 1 79  ? 5.923   -29.674 7.141   1.00 29.38 ? 76  LEU A CD2 1 
ATOM   675  N  N   . ILE A 1 80  ? 8.082   -33.689 9.014   1.00 26.63 ? 77  ILE A N   1 
ATOM   676  C  CA  . ILE A 1 80  ? 8.097   -34.842 9.898   1.00 27.19 ? 77  ILE A CA  1 
ATOM   677  C  C   . ILE A 1 80  ? 7.051   -34.618 10.986  1.00 27.95 ? 77  ILE A C   1 
ATOM   678  O  O   . ILE A 1 80  ? 6.985   -33.542 11.575  1.00 27.31 ? 77  ILE A O   1 
ATOM   679  C  CB  . ILE A 1 80  ? 9.504   -35.060 10.484  1.00 28.13 ? 77  ILE A CB  1 
ATOM   680  C  CG1 . ILE A 1 80  ? 10.531  -35.348 9.383   1.00 28.09 ? 77  ILE A CG1 1 
ATOM   681  C  CG2 . ILE A 1 80  ? 9.491   -36.149 11.557  1.00 28.63 ? 77  ILE A CG2 1 
ATOM   682  C  CD1 . ILE A 1 80  ? 10.258  -36.607 8.577   1.00 27.91 ? 77  ILE A CD1 1 
ATOM   683  N  N   . ASP A 1 81  ? 6.246   -35.656 11.237  1.00 29.43 ? 78  ASP A N   1 
ATOM   684  C  CA  . ASP A 1 81  ? 5.203   -35.636 12.249  1.00 29.85 ? 78  ASP A CA  1 
ATOM   685  C  C   . ASP A 1 81  ? 5.824   -35.355 13.616  1.00 31.74 ? 78  ASP A C   1 
ATOM   686  O  O   . ASP A 1 81  ? 6.887   -35.882 13.940  1.00 32.74 ? 78  ASP A O   1 
ATOM   687  C  CB  . ASP A 1 81  ? 4.444   -36.953 12.211  1.00 29.90 ? 78  ASP A CB  1 
ATOM   688  C  CG  . ASP A 1 81  ? 3.278   -37.102 13.174  1.00 30.38 ? 78  ASP A CG  1 
ATOM   689  O  OD1 . ASP A 1 81  ? 3.495   -36.930 14.392  1.00 31.16 ? 78  ASP A OD1 1 
ATOM   690  O  OD2 . ASP A 1 81  ? 2.174   -37.428 12.693  1.00 30.39 ? 78  ASP A OD2 1 
ATOM   691  N  N   . GLN A 1 82  ? 5.132   -34.533 14.415  1.00 34.69 ? 79  GLN A N   1 
ATOM   692  C  CA  . GLN A 1 82  ? 5.651   -34.039 15.682  1.00 37.79 ? 79  GLN A CA  1 
ATOM   693  C  C   . GLN A 1 82  ? 5.955   -35.188 16.641  1.00 38.90 ? 79  GLN A C   1 
ATOM   694  O  O   . GLN A 1 82  ? 6.888   -35.094 17.436  1.00 39.96 ? 79  GLN A O   1 
ATOM   695  C  CB  . GLN A 1 82  ? 4.652   -33.066 16.312  1.00 40.48 ? 79  GLN A CB  1 
ATOM   696  C  CG  . GLN A 1 82  ? 4.986   -32.646 17.741  1.00 43.39 ? 79  GLN A CG  1 
ATOM   697  C  CD  . GLN A 1 82  ? 6.253   -31.825 17.853  1.00 45.90 ? 79  GLN A CD  1 
ATOM   698  O  OE1 . GLN A 1 82  ? 7.329   -32.217 17.389  1.00 47.96 ? 79  GLN A OE1 1 
ATOM   699  N  NE2 . GLN A 1 82  ? 6.138   -30.665 18.480  1.00 48.38 ? 79  GLN A NE2 1 
ATOM   700  N  N   . ARG A 1 83  ? 5.174   -36.272 16.557  1.00 39.64 ? 80  ARG A N   1 
ATOM   701  C  CA  . ARG A 1 83  ? 5.347   -37.417 17.438  1.00 40.40 ? 80  ARG A CA  1 
ATOM   702  C  C   . ARG A 1 83  ? 6.689   -38.112 17.202  1.00 40.29 ? 80  ARG A C   1 
ATOM   703  O  O   . ARG A 1 83  ? 7.044   -39.008 17.965  1.00 40.69 ? 80  ARG A O   1 
ATOM   704  C  CB  . ARG A 1 83  ? 4.212   -38.427 17.237  1.00 41.62 ? 80  ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 83  ? 2.839   -37.963 17.701  1.00 42.35 ? 80  ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 83  ? 1.780   -38.964 17.279  1.00 43.12 ? 80  ARG A CD  1 
ATOM   707  N  NE  . ARG A 1 83  ? 1.667   -39.011 15.817  1.00 42.47 ? 80  ARG A NE  1 
ATOM   708  C  CZ  . ARG A 1 83  ? 1.101   -39.984 15.111  1.00 41.13 ? 80  ARG A CZ  1 
ATOM   709  N  NH1 . ARG A 1 83  ? 0.594   -41.047 15.715  1.00 41.85 ? 80  ARG A NH1 1 
ATOM   710  N  NH2 . ARG A 1 83  ? 1.059   -39.898 13.793  1.00 39.14 ? 80  ARG A NH2 1 
ATOM   711  N  N   . PHE A 1 84  ? 7.434   -37.707 16.162  1.00 38.56 ? 81  PHE A N   1 
ATOM   712  C  CA  . PHE A 1 84  ? 8.639   -38.423 15.770  1.00 39.40 ? 81  PHE A CA  1 
ATOM   713  C  C   . PHE A 1 84  ? 9.842   -37.495 15.589  1.00 39.98 ? 81  PHE A C   1 
ATOM   714  O  O   . PHE A 1 84  ? 10.880  -37.939 15.105  1.00 40.82 ? 81  PHE A O   1 
ATOM   715  C  CB  . PHE A 1 84  ? 8.331   -39.173 14.471  1.00 39.15 ? 81  PHE A CB  1 
ATOM   716  C  CG  . PHE A 1 84  ? 7.196   -40.184 14.562  1.00 38.46 ? 81  PHE A CG  1 
ATOM   717  C  CD1 . PHE A 1 84  ? 7.390   -41.430 15.154  1.00 38.03 ? 81  PHE A CD1 1 
ATOM   718  C  CD2 . PHE A 1 84  ? 5.944   -39.894 14.034  1.00 38.62 ? 81  PHE A CD2 1 
ATOM   719  C  CE1 . PHE A 1 84  ? 6.351   -42.344 15.232  1.00 37.96 ? 81  PHE A CE1 1 
ATOM   720  C  CE2 . PHE A 1 84  ? 4.911   -40.814 14.113  1.00 38.36 ? 81  PHE A CE2 1 
ATOM   721  C  CZ  . PHE A 1 84  ? 5.117   -42.037 14.707  1.00 38.43 ? 81  PHE A CZ  1 
ATOM   722  N  N   . GLN A 1 85  ? 9.728   -36.223 15.994  1.00 40.28 ? 82  GLN A N   1 
ATOM   723  C  CA  . GLN A 1 85  ? 10.801  -35.265 15.768  1.00 42.02 ? 82  GLN A CA  1 
ATOM   724  C  C   . GLN A 1 85  ? 11.874  -35.414 16.846  1.00 45.10 ? 82  GLN A C   1 
ATOM   725  O  O   . GLN A 1 85  ? 11.641  -36.022 17.889  1.00 47.01 ? 82  GLN A O   1 
ATOM   726  C  CB  . GLN A 1 85  ? 10.275  -33.832 15.702  1.00 41.66 ? 82  GLN A CB  1 
ATOM   727  C  CG  . GLN A 1 85  ? 9.414   -33.556 14.474  1.00 41.36 ? 82  GLN A CG  1 
ATOM   728  C  CD  . GLN A 1 85  ? 9.151   -32.086 14.240  1.00 41.53 ? 82  GLN A CD  1 
ATOM   729  O  OE1 . GLN A 1 85  ? 9.287   -31.580 13.121  1.00 41.96 ? 82  GLN A OE1 1 
ATOM   730  N  NE2 . GLN A 1 85  ? 8.751   -31.386 15.292  1.00 41.71 ? 82  GLN A NE2 1 
ATOM   731  N  N   . GLY A 1 86  ? 13.061  -34.865 16.557  1.00 46.95 ? 83  GLY A N   1 
ATOM   732  C  CA  . GLY A 1 86  ? 14.171  -34.844 17.497  1.00 48.59 ? 83  GLY A CA  1 
ATOM   733  C  C   . GLY A 1 86  ? 14.876  -36.195 17.611  1.00 49.46 ? 83  GLY A C   1 
ATOM   734  O  O   . GLY A 1 86  ? 15.667  -36.392 18.533  1.00 51.25 ? 83  GLY A O   1 
ATOM   735  N  N   . GLN A 1 87  ? 14.610  -37.104 16.661  1.00 49.69 ? 84  GLN A N   1 
ATOM   736  C  CA  . GLN A 1 87  ? 15.059  -38.486 16.758  1.00 49.22 ? 84  GLN A CA  1 
ATOM   737  C  C   . GLN A 1 87  ? 15.662  -38.967 15.436  1.00 46.58 ? 84  GLN A C   1 
ATOM   738  O  O   . GLN A 1 87  ? 15.667  -40.164 15.158  1.00 48.13 ? 84  GLN A O   1 
ATOM   739  C  CB  . GLN A 1 87  ? 13.876  -39.342 17.214  1.00 50.64 ? 84  GLN A CB  1 
ATOM   740  C  CG  . GLN A 1 87  ? 13.463  -39.101 18.663  1.00 52.70 ? 84  GLN A CG  1 
ATOM   741  C  CD  . GLN A 1 87  ? 11.980  -39.295 18.899  1.00 53.83 ? 84  GLN A CD  1 
ATOM   742  O  OE1 . GLN A 1 87  ? 11.428  -40.376 18.670  1.00 55.78 ? 84  GLN A OE1 1 
ATOM   743  N  NE2 . GLN A 1 87  ? 11.316  -38.241 19.354  1.00 54.40 ? 84  GLN A NE2 1 
ATOM   744  N  N   . GLY A 1 88  ? 16.179  -38.031 14.630  1.00 43.44 ? 85  GLY A N   1 
ATOM   745  C  CA  . GLY A 1 88  ? 17.034  -38.358 13.499  1.00 41.53 ? 85  GLY A CA  1 
ATOM   746  C  C   . GLY A 1 88  ? 16.267  -38.750 12.235  1.00 39.65 ? 85  GLY A C   1 
ATOM   747  O  O   . GLY A 1 88  ? 16.886  -39.153 11.253  1.00 38.53 ? 85  GLY A O   1 
ATOM   748  N  N   . TYR A 1 89  ? 14.935  -38.614 12.239  1.00 39.24 ? 86  TYR A N   1 
ATOM   749  C  CA  . TYR A 1 89  ? 14.131  -39.032 11.100  1.00 37.64 ? 86  TYR A CA  1 
ATOM   750  C  C   . TYR A 1 89  ? 14.288  -38.049 9.942   1.00 35.98 ? 86  TYR A C   1 
ATOM   751  O  O   . TYR A 1 89  ? 14.503  -38.468 8.807   1.00 36.34 ? 86  TYR A O   1 
ATOM   752  C  CB  . TYR A 1 89  ? 12.644  -39.154 11.436  1.00 37.71 ? 86  TYR A CB  1 
ATOM   753  C  CG  . TYR A 1 89  ? 12.204  -40.469 12.066  1.00 38.59 ? 86  TYR A CG  1 
ATOM   754  C  CD1 . TYR A 1 89  ? 12.774  -41.688 11.710  1.00 39.18 ? 86  TYR A CD1 1 
ATOM   755  C  CD2 . TYR A 1 89  ? 11.180  -40.485 13.001  1.00 38.46 ? 86  TYR A CD2 1 
ATOM   756  C  CE1 . TYR A 1 89  ? 12.350  -42.876 12.282  1.00 39.55 ? 86  TYR A CE1 1 
ATOM   757  C  CE2 . TYR A 1 89  ? 10.746  -41.664 13.582  1.00 38.91 ? 86  TYR A CE2 1 
ATOM   758  C  CZ  . TYR A 1 89  ? 11.331  -42.862 13.220  1.00 39.37 ? 86  TYR A CZ  1 
ATOM   759  O  OH  . TYR A 1 89  ? 10.882  -44.006 13.807  1.00 40.73 ? 86  TYR A OH  1 
ATOM   760  N  N   . GLY A 1 90  ? 14.146  -36.751 10.230  1.00 35.36 ? 87  GLY A N   1 
ATOM   761  C  CA  . GLY A 1 90  ? 14.245  -35.719 9.210   1.00 34.28 ? 87  GLY A CA  1 
ATOM   762  C  C   . GLY A 1 90  ? 15.497  -35.887 8.351   1.00 33.92 ? 87  GLY A C   1 
ATOM   763  O  O   . GLY A 1 90  ? 15.412  -35.960 7.129   1.00 34.63 ? 87  GLY A O   1 
ATOM   764  N  N   . LYS A 1 91  ? 16.659  -35.974 9.004   1.00 34.19 ? 88  LYS A N   1 
ATOM   765  C  CA  . LYS A 1 91  ? 17.931  -36.033 8.302   1.00 34.16 ? 88  LYS A CA  1 
ATOM   766  C  C   . LYS A 1 91  ? 18.025  -37.342 7.518   1.00 31.59 ? 88  LYS A C   1 
ATOM   767  O  O   . LYS A 1 91  ? 18.423  -37.349 6.356   1.00 30.55 ? 88  LYS A O   1 
ATOM   768  C  CB  . LYS A 1 91  ? 19.071  -35.862 9.310   1.00 36.64 ? 88  LYS A CB  1 
ATOM   769  C  CG  . LYS A 1 91  ? 20.412  -35.456 8.721   1.00 38.36 ? 88  LYS A CG  1 
ATOM   770  C  CD  . LYS A 1 91  ? 21.565  -35.528 9.717   1.00 39.99 ? 88  LYS A CD  1 
ATOM   771  C  CE  . LYS A 1 91  ? 21.345  -34.733 10.970  1.00 40.34 ? 88  LYS A CE  1 
ATOM   772  N  NZ  . LYS A 1 91  ? 22.449  -34.918 11.917  1.00 42.43 ? 88  LYS A NZ  1 
ATOM   773  N  N   . ALA A 1 92  ? 17.634  -38.451 8.154   1.00 31.89 ? 89  ALA A N   1 
ATOM   774  C  CA  . ALA A 1 92  ? 17.690  -39.756 7.511   1.00 30.58 ? 89  ALA A CA  1 
ATOM   775  C  C   . ALA A 1 92  ? 16.786  -39.785 6.280   1.00 29.63 ? 89  ALA A C   1 
ATOM   776  O  O   . ALA A 1 92  ? 17.221  -40.183 5.203   1.00 30.88 ? 89  ALA A O   1 
ATOM   777  C  CB  . ALA A 1 92  ? 17.319  -40.837 8.500   1.00 31.22 ? 89  ALA A CB  1 
ATOM   778  N  N   . ALA A 1 93  ? 15.533  -39.343 6.450   1.00 29.06 ? 90  ALA A N   1 
ATOM   779  C  CA  . ALA A 1 93  ? 14.568  -39.274 5.362   1.00 28.05 ? 90  ALA A CA  1 
ATOM   780  C  C   . ALA A 1 93  ? 15.002  -38.276 4.285   1.00 27.18 ? 90  ALA A C   1 
ATOM   781  O  O   . ALA A 1 93  ? 14.858  -38.550 3.098   1.00 27.47 ? 90  ALA A O   1 
ATOM   782  C  CB  . ALA A 1 93  ? 13.200  -38.930 5.913   1.00 28.25 ? 90  ALA A CB  1 
ATOM   783  N  N   . CYS A 1 94  ? 15.532  -37.114 4.682   1.00 27.65 ? 91  CYS A N   1 
ATOM   784  C  CA  . CYS A 1 94  ? 15.936  -36.114 3.706   1.00 28.26 ? 91  CYS A CA  1 
ATOM   785  C  C   . CYS A 1 94  ? 17.081  -36.640 2.835   1.00 27.70 ? 91  CYS A C   1 
ATOM   786  O  O   . CYS A 1 94  ? 17.072  -36.463 1.618   1.00 27.39 ? 91  CYS A O   1 
ATOM   787  C  CB  . CYS A 1 94  ? 16.323  -34.804 4.378   1.00 29.62 ? 91  CYS A CB  1 
ATOM   788  S  SG  . CYS A 1 94  ? 16.403  -33.422 3.214   1.00 31.95 ? 91  CYS A SG  1 
ATOM   789  N  N   . ARG A 1 95  ? 18.066  -37.299 3.452   1.00 28.39 ? 92  ARG A N   1 
ATOM   790  C  CA  . ARG A 1 95  ? 19.195  -37.826 2.699   1.00 28.96 ? 92  ARG A CA  1 
ATOM   791  C  C   . ARG A 1 95  ? 18.701  -38.833 1.660   1.00 27.93 ? 92  ARG A C   1 
ATOM   792  O  O   . ARG A 1 95  ? 19.071  -38.767 0.491   1.00 27.46 ? 92  ARG A O   1 
ATOM   793  C  CB  . ARG A 1 95  ? 20.225  -38.480 3.623   1.00 31.79 ? 92  ARG A CB  1 
ATOM   794  C  CG  . ARG A 1 95  ? 21.633  -38.520 3.042   1.00 34.39 ? 92  ARG A CG  1 
ATOM   795  C  CD  . ARG A 1 95  ? 22.514  -39.564 3.712   1.00 36.70 ? 92  ARG A CD  1 
ATOM   796  N  NE  . ARG A 1 95  ? 22.068  -39.864 5.078   1.00 38.93 ? 92  ARG A NE  1 
ATOM   797  C  CZ  . ARG A 1 95  ? 22.474  -39.269 6.197   1.00 40.32 ? 92  ARG A CZ  1 
ATOM   798  N  NH1 . ARG A 1 95  ? 23.438  -38.363 6.180   1.00 40.17 ? 92  ARG A NH1 1 
ATOM   799  N  NH2 . ARG A 1 95  ? 21.900  -39.590 7.345   1.00 41.06 ? 92  ARG A NH2 1 
ATOM   800  N  N   . LEU A 1 96  ? 17.846  -39.761 2.092   1.00 27.90 ? 93  LEU A N   1 
ATOM   801  C  CA  . LEU A 1 96  ? 17.370  -40.814 1.208   1.00 28.79 ? 93  LEU A CA  1 
ATOM   802  C  C   . LEU A 1 96  ? 16.573  -40.203 0.059   1.00 27.28 ? 93  LEU A C   1 
ATOM   803  O  O   . LEU A 1 96  ? 16.763  -40.580 -1.095  1.00 27.59 ? 93  LEU A O   1 
ATOM   804  C  CB  . LEU A 1 96  ? 16.581  -41.863 1.991   1.00 29.98 ? 93  LEU A CB  1 
ATOM   805  C  CG  . LEU A 1 96  ? 17.384  -42.625 3.052   1.00 32.25 ? 93  LEU A CG  1 
ATOM   806  C  CD1 . LEU A 1 96  ? 16.525  -43.652 3.765   1.00 32.87 ? 93  LEU A CD1 1 
ATOM   807  C  CD2 . LEU A 1 96  ? 18.615  -43.292 2.451   1.00 32.96 ? 93  LEU A CD2 1 
ATOM   808  N  N   . LEU A 1 97  ? 15.724  -39.211 0.367   1.00 26.60 ? 94  LEU A N   1 
ATOM   809  C  CA  . LEU A 1 97  ? 14.951  -38.542 -0.666  1.00 27.57 ? 94  LEU A CA  1 
ATOM   810  C  C   . LEU A 1 97  ? 15.877  -37.896 -1.696  1.00 28.03 ? 94  LEU A C   1 
ATOM   811  O  O   . LEU A 1 97  ? 15.632  -38.007 -2.896  1.00 29.25 ? 94  LEU A O   1 
ATOM   812  C  CB  . LEU A 1 97  ? 13.989  -37.535 -0.043  1.00 27.15 ? 94  LEU A CB  1 
ATOM   813  C  CG  . LEU A 1 97  ? 13.121  -36.742 -1.025  1.00 27.94 ? 94  LEU A CG  1 
ATOM   814  C  CD1 . LEU A 1 97  ? 12.331  -37.637 -1.972  1.00 28.35 ? 94  LEU A CD1 1 
ATOM   815  C  CD2 . LEU A 1 97  ? 12.196  -35.839 -0.231  1.00 28.58 ? 94  LEU A CD2 1 
ATOM   816  N  N   A MET A 1 98  ? 16.940  -37.234 -1.219  0.81 27.04 ? 95  MET A N   1 
ATOM   817  N  N   B MET A 1 98  ? 16.947  -37.247 -1.223  0.19 28.48 ? 95  MET A N   1 
ATOM   818  C  CA  A MET A 1 98  ? 17.903  -36.578 -2.092  0.81 26.33 ? 95  MET A CA  1 
ATOM   819  C  CA  B MET A 1 98  ? 17.889  -36.584 -2.108  0.19 28.32 ? 95  MET A CA  1 
ATOM   820  C  C   A MET A 1 98  ? 18.489  -37.575 -3.095  0.81 26.29 ? 95  MET A C   1 
ATOM   821  C  C   B MET A 1 98  ? 18.483  -37.577 -3.104  0.19 27.71 ? 95  MET A C   1 
ATOM   822  O  O   A MET A 1 98  ? 18.573  -37.284 -4.287  0.81 26.77 ? 95  MET A O   1 
ATOM   823  O  O   B MET A 1 98  ? 18.566  -37.280 -4.294  0.19 28.35 ? 95  MET A O   1 
ATOM   824  C  CB  A MET A 1 98  ? 19.030  -35.940 -1.269  0.81 26.02 ? 95  MET A CB  1 
ATOM   825  C  CB  B MET A 1 98  ? 19.022  -35.922 -1.319  0.19 29.05 ? 95  MET A CB  1 
ATOM   826  C  CG  A MET A 1 98  ? 18.605  -34.728 -0.463  0.81 25.83 ? 95  MET A CG  1 
ATOM   827  C  CG  B MET A 1 98  ? 18.646  -34.588 -0.718  0.19 29.48 ? 95  MET A CG  1 
ATOM   828  S  SD  A MET A 1 98  ? 19.739  -34.328 0.885   0.81 26.13 ? 95  MET A SD  1 
ATOM   829  S  SD  B MET A 1 98  ? 20.101  -33.737 -0.082  0.19 30.44 ? 95  MET A SD  1 
ATOM   830  C  CE  A MET A 1 98  ? 21.209  -33.843 -0.032  0.81 25.90 ? 95  MET A CE  1 
ATOM   831  C  CE  B MET A 1 98  ? 20.493  -34.837 1.283   0.19 30.36 ? 95  MET A CE  1 
ATOM   832  N  N   . LEU A 1 99  ? 18.890  -38.754 -2.612  1.00 27.02 ? 96  LEU A N   1 
ATOM   833  C  CA  . LEU A 1 99  ? 19.536  -39.750 -3.458  1.00 27.78 ? 96  LEU A CA  1 
ATOM   834  C  C   . LEU A 1 99  ? 18.547  -40.308 -4.479  1.00 28.73 ? 96  LEU A C   1 
ATOM   835  O  O   . LEU A 1 99  ? 18.917  -40.574 -5.624  1.00 29.05 ? 96  LEU A O   1 
ATOM   836  C  CB  . LEU A 1 99  ? 20.144  -40.846 -2.587  1.00 28.14 ? 96  LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 99  ? 21.187  -40.375 -1.569  1.00 28.83 ? 96  LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 99  ? 21.861  -41.573 -0.934  1.00 29.93 ? 96  LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 99  ? 22.225  -39.430 -2.171  1.00 29.69 ? 96  LEU A CD2 1 
ATOM   840  N  N   . LYS A 1 100 ? 17.283  -40.450 -4.066  1.00 29.10 ? 97  LYS A N   1 
ATOM   841  C  CA  . LYS A 1 100 ? 16.251  -40.963 -4.950  1.00 30.62 ? 97  LYS A CA  1 
ATOM   842  C  C   . LYS A 1 100 ? 15.999  -39.986 -6.096  1.00 31.12 ? 97  LYS A C   1 
ATOM   843  O  O   . LYS A 1 100 ? 15.796  -40.402 -7.235  1.00 32.21 ? 97  LYS A O   1 
ATOM   844  C  CB  . LYS A 1 100 ? 14.991  -41.258 -4.135  1.00 32.36 ? 97  LYS A CB  1 
ATOM   845  C  CG  . LYS A 1 100 ? 15.036  -42.613 -3.454  1.00 33.47 ? 97  LYS A CG  1 
ATOM   846  C  CD  . LYS A 1 100 ? 13.898  -42.810 -2.463  1.00 35.30 ? 97  LYS A CD  1 
ATOM   847  C  CE  . LYS A 1 100 ? 13.423  -44.222 -2.393  1.00 37.27 ? 97  LYS A CE  1 
ATOM   848  N  NZ  . LYS A 1 100 ? 12.951  -44.739 -3.681  1.00 38.84 ? 97  LYS A NZ  1 
ATOM   849  N  N   . LEU A 1 101 ? 16.026  -38.688 -5.783  1.00 30.79 ? 98  LEU A N   1 
ATOM   850  C  CA  . LEU A 1 101 ? 15.774  -37.660 -6.779  1.00 30.99 ? 98  LEU A CA  1 
ATOM   851  C  C   . LEU A 1 101 ? 16.874  -37.642 -7.840  1.00 31.37 ? 98  LEU A C   1 
ATOM   852  O  O   . LEU A 1 101 ? 16.569  -37.620 -9.029  1.00 32.47 ? 98  LEU A O   1 
ATOM   853  C  CB  . LEU A 1 101 ? 15.591  -36.306 -6.094  1.00 30.67 ? 98  LEU A CB  1 
ATOM   854  C  CG  . LEU A 1 101 ? 14.230  -36.094 -5.425  1.00 31.08 ? 98  LEU A CG  1 
ATOM   855  C  CD1 . LEU A 1 101 ? 14.185  -34.823 -4.599  1.00 31.22 ? 98  LEU A CD1 1 
ATOM   856  C  CD2 . LEU A 1 101 ? 13.141  -36.078 -6.484  1.00 31.85 ? 98  LEU A CD2 1 
ATOM   857  N  N   . ILE A 1 102 ? 18.149  -37.679 -7.431  1.00 32.54 ? 99  ILE A N   1 
ATOM   858  C  CA  . ILE A 1 102 ? 19.236  -37.593 -8.400  1.00 33.42 ? 99  ILE A CA  1 
ATOM   859  C  C   . ILE A 1 102 ? 19.381  -38.906 -9.169  1.00 35.61 ? 99  ILE A C   1 
ATOM   860  O  O   . ILE A 1 102 ? 20.067  -38.943 -10.190 1.00 38.05 ? 99  ILE A O   1 
ATOM   861  C  CB  . ILE A 1 102 ? 20.566  -37.154 -7.755  1.00 33.48 ? 99  ILE A CB  1 
ATOM   862  C  CG1 . ILE A 1 102 ? 21.034  -38.101 -6.644  1.00 32.27 ? 99  ILE A CG1 1 
ATOM   863  C  CG2 . ILE A 1 102 ? 20.451  -35.710 -7.266  1.00 33.84 ? 99  ILE A CG2 1 
ATOM   864  C  CD1 . ILE A 1 102 ? 22.484  -37.911 -6.228  1.00 33.08 ? 99  ILE A CD1 1 
ATOM   865  N  N   . GLU A 1 103 ? 18.755  -39.984 -8.682  1.00 36.99 ? 100 GLU A N   1 
ATOM   866  C  CA  . GLU A 1 103 ? 18.721  -41.236 -9.423  1.00 38.93 ? 100 GLU A CA  1 
ATOM   867  C  C   . GLU A 1 103 ? 17.598  -41.179 -10.457 1.00 40.40 ? 100 GLU A C   1 
ATOM   868  O  O   . GLU A 1 103 ? 17.774  -41.626 -11.588 1.00 41.36 ? 100 GLU A O   1 
ATOM   869  C  CB  . GLU A 1 103 ? 18.568  -42.438 -8.490  1.00 40.82 ? 100 GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 103 ? 18.715  -43.777 -9.208  1.00 42.81 ? 100 GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 103 ? 18.719  -44.996 -8.302  1.00 44.40 ? 100 GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 103 ? 18.413  -44.863 -7.098  1.00 46.55 ? 100 GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 103 ? 19.046  -46.087 -8.808  1.00 45.64 ? 100 GLU A OE2 1 
ATOM   874  N  N   . LYS A 1 104 ? 16.450  -40.619 -10.057 1.00 40.43 ? 101 LYS A N   1 
ATOM   875  C  CA  . LYS A 1 104 ? 15.294  -40.513 -10.931 1.00 41.35 ? 101 LYS A CA  1 
ATOM   876  C  C   . LYS A 1 104 ? 15.621  -39.604 -12.117 1.00 40.69 ? 101 LYS A C   1 
ATOM   877  O  O   . LYS A 1 104 ? 15.409  -39.985 -13.265 1.00 41.84 ? 101 LYS A O   1 
ATOM   878  C  CB  . LYS A 1 104 ? 14.079  -40.003 -10.146 1.00 43.25 ? 101 LYS A CB  1 
ATOM   879  C  CG  . LYS A 1 104 ? 12.761  -40.030 -10.907 1.00 44.39 ? 101 LYS A CG  1 
ATOM   880  C  CD  . LYS A 1 104 ? 11.576  -39.480 -10.123 1.00 46.52 ? 101 LYS A CD  1 
ATOM   881  C  CE  . LYS A 1 104 ? 10.270  -39.699 -10.824 1.00 48.13 ? 101 LYS A CE  1 
ATOM   882  N  NZ  . LYS A 1 104 ? 10.262  -39.159 -12.187 1.00 48.97 ? 101 LYS A NZ  1 
ATOM   883  N  N   . TYR A 1 105 ? 16.144  -38.405 -11.833 1.00 38.57 ? 102 TYR A N   1 
ATOM   884  C  CA  . TYR A 1 105 ? 16.372  -37.404 -12.864 1.00 39.17 ? 102 TYR A CA  1 
ATOM   885  C  C   . TYR A 1 105 ? 17.847  -37.393 -13.266 1.00 39.97 ? 102 TYR A C   1 
ATOM   886  O  O   . TYR A 1 105 ? 18.703  -37.871 -12.526 1.00 39.44 ? 102 TYR A O   1 
ATOM   887  C  CB  . TYR A 1 105 ? 15.900  -36.037 -12.360 1.00 39.04 ? 102 TYR A CB  1 
ATOM   888  C  CG  . TYR A 1 105 ? 14.429  -35.964 -11.963 1.00 38.02 ? 102 TYR A CG  1 
ATOM   889  C  CD1 . TYR A 1 105 ? 13.428  -35.818 -12.919 1.00 39.91 ? 102 TYR A CD1 1 
ATOM   890  C  CD2 . TYR A 1 105 ? 14.039  -36.028 -10.629 1.00 37.58 ? 102 TYR A CD2 1 
ATOM   891  C  CE1 . TYR A 1 105 ? 12.090  -35.746 -12.561 1.00 38.69 ? 102 TYR A CE1 1 
ATOM   892  C  CE2 . TYR A 1 105 ? 12.705  -35.954 -10.259 1.00 38.05 ? 102 TYR A CE2 1 
ATOM   893  C  CZ  . TYR A 1 105 ? 11.726  -35.812 -11.227 1.00 38.88 ? 102 TYR A CZ  1 
ATOM   894  O  OH  . TYR A 1 105 ? 10.404  -35.731 -10.889 1.00 41.73 ? 102 TYR A OH  1 
ATOM   895  N  N   . GLN A 1 106 ? 18.123  -36.829 -14.450 1.00 42.50 ? 103 GLN A N   1 
ATOM   896  C  CA  . GLN A 1 106 ? 19.471  -36.742 -14.992 1.00 44.67 ? 103 GLN A CA  1 
ATOM   897  C  C   . GLN A 1 106 ? 20.385  -35.952 -14.058 1.00 44.98 ? 103 GLN A C   1 
ATOM   898  O  O   . GLN A 1 106 ? 21.477  -36.411 -13.727 1.00 46.20 ? 103 GLN A O   1 
ATOM   899  C  CB  . GLN A 1 106 ? 19.498  -36.075 -16.370 1.00 46.30 ? 103 GLN A CB  1 
ATOM   900  C  CG  . GLN A 1 106 ? 19.410  -37.050 -17.541 1.00 48.69 ? 103 GLN A CG  1 
ATOM   901  C  CD  . GLN A 1 106 ? 19.859  -36.443 -18.854 1.00 50.48 ? 103 GLN A CD  1 
ATOM   902  O  OE1 . GLN A 1 106 ? 20.116  -35.239 -18.954 1.00 52.67 ? 103 GLN A OE1 1 
ATOM   903  N  NE2 . GLN A 1 106 ? 19.955  -37.275 -19.881 1.00 50.44 ? 103 GLN A NE2 1 
ATOM   904  N  N   . THR A 1 107 ? 19.918  -34.766 -13.651 1.00 44.54 ? 104 THR A N   1 
ATOM   905  C  CA  . THR A 1 107 ? 20.724  -33.768 -12.960 1.00 43.78 ? 104 THR A CA  1 
ATOM   906  C  C   . THR A 1 107 ? 21.364  -34.346 -11.697 1.00 42.08 ? 104 THR A C   1 
ATOM   907  O  O   . THR A 1 107 ? 20.927  -35.372 -11.179 1.00 41.59 ? 104 THR A O   1 
ATOM   908  C  CB  . THR A 1 107 ? 19.829  -32.570 -12.637 1.00 43.56 ? 104 THR A CB  1 
ATOM   909  O  OG1 . THR A 1 107 ? 20.651  -31.543 -12.092 1.00 43.40 ? 104 THR A OG1 1 
ATOM   910  C  CG2 . THR A 1 107 ? 18.728  -32.906 -11.646 1.00 44.35 ? 104 THR A CG2 1 
ATOM   911  N  N   . ASN A 1 108 ? 22.408  -33.653 -11.219 1.00 40.25 ? 105 ASN A N   1 
ATOM   912  C  CA  . ASN A 1 108 ? 23.059  -33.949 -9.952  1.00 40.40 ? 105 ASN A CA  1 
ATOM   913  C  C   . ASN A 1 108 ? 22.924  -32.761 -8.999  1.00 36.93 ? 105 ASN A C   1 
ATOM   914  O  O   . ASN A 1 108 ? 23.695  -32.637 -8.048  1.00 37.59 ? 105 ASN A O   1 
ATOM   915  C  CB  . ASN A 1 108 ? 24.533  -34.288 -10.144 1.00 42.59 ? 105 ASN A CB  1 
ATOM   916  C  CG  . ASN A 1 108 ? 24.744  -35.552 -10.943 1.00 43.72 ? 105 ASN A CG  1 
ATOM   917  O  OD1 . ASN A 1 108 ? 25.421  -35.525 -11.976 1.00 45.07 ? 105 ASN A OD1 1 
ATOM   918  N  ND2 . ASN A 1 108 ? 24.193  -36.667 -10.482 1.00 45.29 ? 105 ASN A ND2 1 
ATOM   919  N  N   . LYS A 1 109 ? 21.945  -31.886 -9.259  1.00 33.35 ? 106 LYS A N   1 
ATOM   920  C  CA  . LYS A 1 109 ? 21.688  -30.735 -8.408  1.00 31.25 ? 106 LYS A CA  1 
ATOM   921  C  C   . LYS A 1 109 ? 20.238  -30.770 -7.929  1.00 29.30 ? 106 LYS A C   1 
ATOM   922  O  O   . LYS A 1 109 ? 19.337  -31.056 -8.715  1.00 30.13 ? 106 LYS A O   1 
ATOM   923  C  CB  . LYS A 1 109 ? 21.950  -29.420 -9.149  1.00 32.23 ? 106 LYS A CB  1 
ATOM   924  C  CG  . LYS A 1 109 ? 23.413  -29.016 -9.266  1.00 33.51 ? 106 LYS A CG  1 
ATOM   925  C  CD  . LYS A 1 109 ? 23.673  -27.990 -10.361 1.00 34.93 ? 106 LYS A CD  1 
ATOM   926  C  CE  . LYS A 1 109 ? 23.493  -28.583 -11.724 1.00 36.72 ? 106 LYS A CE  1 
ATOM   927  N  NZ  . LYS A 1 109 ? 23.933  -27.677 -12.786 1.00 38.10 ? 106 LYS A NZ  1 
ATOM   928  N  N   . LEU A 1 110 ? 20.042  -30.468 -6.637  1.00 27.67 ? 107 LEU A N   1 
ATOM   929  C  CA  . LEU A 1 110 ? 18.725  -30.301 -6.043  1.00 26.57 ? 107 LEU A CA  1 
ATOM   930  C  C   . LEU A 1 110 ? 18.593  -28.890 -5.479  1.00 25.35 ? 107 LEU A C   1 
ATOM   931  O  O   . LEU A 1 110 ? 19.584  -28.276 -5.079  1.00 25.92 ? 107 LEU A O   1 
ATOM   932  C  CB  . LEU A 1 110 ? 18.496  -31.322 -4.934  1.00 27.06 ? 107 LEU A CB  1 
ATOM   933  C  CG  . LEU A 1 110 ? 18.625  -32.790 -5.337  1.00 27.71 ? 107 LEU A CG  1 
ATOM   934  C  CD1 . LEU A 1 110 ? 18.412  -33.638 -4.104  1.00 28.05 ? 107 LEU A CD1 1 
ATOM   935  C  CD2 . LEU A 1 110 ? 17.660  -33.162 -6.448  1.00 28.70 ? 107 LEU A CD2 1 
ATOM   936  N  N   . TYR A 1 111 ? 17.343  -28.417 -5.412  1.00 24.88 ? 108 TYR A N   1 
ATOM   937  C  CA  . TYR A 1 111 ? 17.044  -27.055 -5.004  1.00 25.56 ? 108 TYR A CA  1 
ATOM   938  C  C   . TYR A 1 111 ? 15.946  -27.051 -3.945  1.00 24.48 ? 108 TYR A C   1 
ATOM   939  O  O   . TYR A 1 111 ? 15.022  -27.862 -3.986  1.00 24.77 ? 108 TYR A O   1 
ATOM   940  C  CB  . TYR A 1 111 ? 16.614  -26.226 -6.217  1.00 26.07 ? 108 TYR A CB  1 
ATOM   941  C  CG  . TYR A 1 111 ? 17.707  -26.073 -7.266  1.00 27.48 ? 108 TYR A CG  1 
ATOM   942  C  CD1 . TYR A 1 111 ? 17.863  -27.015 -8.276  1.00 28.61 ? 108 TYR A CD1 1 
ATOM   943  C  CD2 . TYR A 1 111 ? 18.590  -24.998 -7.241  1.00 27.53 ? 108 TYR A CD2 1 
ATOM   944  C  CE1 . TYR A 1 111 ? 18.854  -26.890 -9.234  1.00 30.24 ? 108 TYR A CE1 1 
ATOM   945  C  CE2 . TYR A 1 111 ? 19.587  -24.862 -8.194  1.00 28.85 ? 108 TYR A CE2 1 
ATOM   946  C  CZ  . TYR A 1 111 ? 19.717  -25.809 -9.195  1.00 30.26 ? 108 TYR A CZ  1 
ATOM   947  O  OH  . TYR A 1 111 ? 20.699  -25.678 -10.134 1.00 34.71 ? 108 TYR A OH  1 
ATOM   948  N  N   . LEU A 1 112 ? 16.065  -26.106 -3.009  1.00 23.85 ? 109 LEU A N   1 
ATOM   949  C  CA  . LEU A 1 112 ? 15.006  -25.786 -2.069  1.00 24.37 ? 109 LEU A CA  1 
ATOM   950  C  C   . LEU A 1 112 ? 15.151  -24.313 -1.690  1.00 24.18 ? 109 LEU A C   1 
ATOM   951  O  O   . LEU A 1 112 ? 16.163  -23.687 -1.993  1.00 24.86 ? 109 LEU A O   1 
ATOM   952  C  CB  . LEU A 1 112 ? 15.038  -26.722 -0.857  1.00 24.68 ? 109 LEU A CB  1 
ATOM   953  C  CG  . LEU A 1 112 ? 16.281  -26.659 0.040   1.00 25.63 ? 109 LEU A CG  1 
ATOM   954  C  CD1 . LEU A 1 112 ? 16.212  -25.540 1.072   1.00 25.45 ? 109 LEU A CD1 1 
ATOM   955  C  CD2 . LEU A 1 112 ? 16.517  -27.993 0.731   1.00 25.89 ? 109 LEU A CD2 1 
ATOM   956  N  N   . SER A 1 113 ? 14.115  -23.747 -1.066  1.00 24.68 ? 110 SER A N   1 
ATOM   957  C  CA  . SER A 1 113 ? 14.216  -22.397 -0.533  1.00 24.97 ? 110 SER A CA  1 
ATOM   958  C  C   . SER A 1 113 ? 13.664  -22.368 0.889   1.00 25.60 ? 110 SER A C   1 
ATOM   959  O  O   . SER A 1 113 ? 12.739  -23.116 1.218   1.00 25.96 ? 110 SER A O   1 
ATOM   960  C  CB  . SER A 1 113 ? 13.540  -21.385 -1.431  1.00 26.05 ? 110 SER A CB  1 
ATOM   961  O  OG  . SER A 1 113 ? 12.176  -21.715 -1.639  1.00 26.24 ? 110 SER A OG  1 
ATOM   962  N  N   . VAL A 1 114 ? 14.256  -21.504 1.723   1.00 27.64 ? 111 VAL A N   1 
ATOM   963  C  CA  . VAL A 1 114 ? 13.973  -21.481 3.148   1.00 29.00 ? 111 VAL A CA  1 
ATOM   964  C  C   . VAL A 1 114 ? 13.687  -20.042 3.578   1.00 29.46 ? 111 VAL A C   1 
ATOM   965  O  O   . VAL A 1 114 ? 14.123  -19.086 2.930   1.00 28.07 ? 111 VAL A O   1 
ATOM   966  C  CB  . VAL A 1 114 ? 15.164  -22.079 3.927   1.00 31.14 ? 111 VAL A CB  1 
ATOM   967  C  CG1 . VAL A 1 114 ? 16.239  -21.035 4.201   1.00 31.32 ? 111 VAL A CG1 1 
ATOM   968  C  CG2 . VAL A 1 114 ? 14.728  -22.748 5.226   1.00 31.95 ? 111 VAL A CG2 1 
ATOM   969  N  N   . TYR A 1 115 ? 12.974  -19.907 4.702   1.00 30.51 ? 112 TYR A N   1 
ATOM   970  C  CA  . TYR A 1 115 ? 12.721  -18.614 5.315   1.00 32.53 ? 112 TYR A CA  1 
ATOM   971  C  C   . TYR A 1 115 ? 13.953  -18.234 6.133   1.00 37.65 ? 112 TYR A C   1 
ATOM   972  O  O   . TYR A 1 115 ? 14.625  -19.103 6.681   1.00 39.30 ? 112 TYR A O   1 
ATOM   973  C  CB  . TYR A 1 115 ? 11.439  -18.668 6.154   1.00 31.07 ? 112 TYR A CB  1 
ATOM   974  C  CG  . TYR A 1 115 ? 10.899  -17.285 6.487   1.00 30.96 ? 112 TYR A CG  1 
ATOM   975  C  CD1 . TYR A 1 115 ? 10.146  -16.575 5.562   1.00 31.17 ? 112 TYR A CD1 1 
ATOM   976  C  CD2 . TYR A 1 115 ? 11.167  -16.682 7.710   1.00 31.28 ? 112 TYR A CD2 1 
ATOM   977  C  CE1 . TYR A 1 115 ? 9.659   -15.311 5.849   1.00 30.98 ? 112 TYR A CE1 1 
ATOM   978  C  CE2 . TYR A 1 115 ? 10.687  -15.415 8.010   1.00 32.08 ? 112 TYR A CE2 1 
ATOM   979  C  CZ  . TYR A 1 115 ? 9.934   -14.726 7.073   1.00 31.33 ? 112 TYR A CZ  1 
ATOM   980  O  OH  . TYR A 1 115 ? 9.459   -13.475 7.350   1.00 29.54 ? 112 TYR A OH  1 
ATOM   981  N  N   . ASP A 1 116 ? 14.218  -16.928 6.243   1.00 41.47 ? 113 ASP A N   1 
ATOM   982  C  CA  . ASP A 1 116 ? 15.487  -16.436 6.759   1.00 45.27 ? 113 ASP A CA  1 
ATOM   983  C  C   . ASP A 1 116 ? 15.601  -16.622 8.276   1.00 48.93 ? 113 ASP A C   1 
ATOM   984  O  O   . ASP A 1 116 ? 16.573  -16.154 8.868   1.00 50.93 ? 113 ASP A O   1 
ATOM   985  C  CB  . ASP A 1 116 ? 15.700  -14.989 6.337   1.00 47.95 ? 113 ASP A CB  1 
ATOM   986  C  CG  . ASP A 1 116 ? 17.090  -14.419 6.585   1.00 49.97 ? 113 ASP A CG  1 
ATOM   987  O  OD1 . ASP A 1 116 ? 18.072  -15.026 6.105   1.00 53.05 ? 113 ASP A OD1 1 
ATOM   988  O  OD2 . ASP A 1 116 ? 17.178  -13.368 7.251   1.00 51.36 ? 113 ASP A OD2 1 
ATOM   989  N  N   . THR A 1 117 ? 14.636  -17.311 8.909   1.00 50.84 ? 114 THR A N   1 
ATOM   990  C  CA  . THR A 1 117 ? 14.666  -17.518 10.353  1.00 53.40 ? 114 THR A CA  1 
ATOM   991  C  C   . THR A 1 117 ? 14.482  -18.991 10.731  1.00 54.83 ? 114 THR A C   1 
ATOM   992  O  O   . THR A 1 117 ? 14.483  -19.309 11.920  1.00 57.24 ? 114 THR A O   1 
ATOM   993  C  CB  . THR A 1 117 ? 13.598  -16.650 11.025  1.00 54.69 ? 114 THR A CB  1 
ATOM   994  O  OG1 . THR A 1 117 ? 12.326  -17.156 10.631  1.00 55.40 ? 114 THR A OG1 1 
ATOM   995  C  CG2 . THR A 1 117 ? 13.716  -15.180 10.660  1.00 53.88 ? 114 THR A CG2 1 
ATOM   996  N  N   . ASN A 1 118 ? 14.331  -19.891 9.749   1.00 53.59 ? 115 ASN A N   1 
ATOM   997  C  CA  . ASN A 1 118 ? 14.093  -21.299 10.040  1.00 54.10 ? 115 ASN A CA  1 
ATOM   998  C  C   . ASN A 1 118 ? 15.431  -21.997 10.280  1.00 54.51 ? 115 ASN A C   1 
ATOM   999  O  O   . ASN A 1 118 ? 15.899  -22.757 9.435   1.00 53.94 ? 115 ASN A O   1 
ATOM   1000 C  CB  . ASN A 1 118 ? 13.287  -21.972 8.933   1.00 53.86 ? 115 ASN A CB  1 
ATOM   1001 C  CG  . ASN A 1 118 ? 12.801  -23.353 9.313   1.00 54.31 ? 115 ASN A CG  1 
ATOM   1002 O  OD1 . ASN A 1 118 ? 13.137  -23.871 10.384  1.00 55.01 ? 115 ASN A OD1 1 
ATOM   1003 N  ND2 . ASN A 1 118 ? 12.018  -23.972 8.442   1.00 54.23 ? 115 ASN A ND2 1 
ATOM   1004 N  N   . SER A 1 119 ? 16.018  -21.754 11.457  1.00 54.86 ? 116 SER A N   1 
ATOM   1005 C  CA  . SER A 1 119 ? 17.359  -22.219 11.774  1.00 54.27 ? 116 SER A CA  1 
ATOM   1006 C  C   . SER A 1 119 ? 17.388  -23.737 11.950  1.00 54.52 ? 116 SER A C   1 
ATOM   1007 O  O   . SER A 1 119 ? 18.385  -24.375 11.619  1.00 53.65 ? 116 SER A O   1 
ATOM   1008 C  CB  . SER A 1 119 ? 17.893  -21.516 12.999  1.00 54.64 ? 116 SER A CB  1 
ATOM   1009 O  OG  . SER A 1 119 ? 17.885  -20.105 12.825  1.00 54.21 ? 116 SER A OG  1 
ATOM   1010 N  N   . SER A 1 120 ? 16.293  -24.307 12.470  1.00 55.16 ? 117 SER A N   1 
ATOM   1011 C  CA  . SER A 1 120 ? 16.193  -25.743 12.684  1.00 54.81 ? 117 SER A CA  1 
ATOM   1012 C  C   . SER A 1 120 ? 16.325  -26.494 11.358  1.00 52.56 ? 117 SER A C   1 
ATOM   1013 O  O   . SER A 1 120 ? 16.937  -27.561 11.310  1.00 52.50 ? 117 SER A O   1 
ATOM   1014 C  CB  . SER A 1 120 ? 14.903  -26.099 13.385  1.00 55.84 ? 117 SER A CB  1 
ATOM   1015 O  OG  . SER A 1 120 ? 14.769  -25.383 14.606  1.00 57.37 ? 117 SER A OG  1 
ATOM   1016 N  N   . ALA A 1 121 ? 15.757  -25.916 10.290  1.00 51.75 ? 118 ALA A N   1 
ATOM   1017 C  CA  . ALA A 1 121 ? 15.751  -26.534 8.973   1.00 49.57 ? 118 ALA A CA  1 
ATOM   1018 C  C   . ALA A 1 121 ? 17.057  -26.252 8.232   1.00 48.28 ? 118 ALA A C   1 
ATOM   1019 O  O   . ALA A 1 121 ? 17.609  -27.152 7.603   1.00 48.79 ? 118 ALA A O   1 
ATOM   1020 C  CB  . ALA A 1 121 ? 14.560  -26.045 8.179   1.00 49.50 ? 118 ALA A CB  1 
ATOM   1021 N  N   . ILE A 1 122 ? 17.539  -25.003 8.302   1.00 46.73 ? 119 ILE A N   1 
ATOM   1022 C  CA  . ILE A 1 122 ? 18.748  -24.601 7.597   1.00 46.13 ? 119 ILE A CA  1 
ATOM   1023 C  C   . ILE A 1 122 ? 19.903  -25.504 8.025   1.00 44.78 ? 119 ILE A C   1 
ATOM   1024 O  O   . ILE A 1 122 ? 20.660  -25.983 7.181   1.00 43.93 ? 119 ILE A O   1 
ATOM   1025 C  CB  . ILE A 1 122 ? 19.071  -23.109 7.824   1.00 45.44 ? 119 ILE A CB  1 
ATOM   1026 C  CG1 . ILE A 1 122 ? 17.990  -22.199 7.229   1.00 45.31 ? 119 ILE A CG1 1 
ATOM   1027 C  CG2 . ILE A 1 122 ? 20.457  -22.758 7.277   1.00 45.68 ? 119 ILE A CG2 1 
ATOM   1028 C  CD1 . ILE A 1 122 ? 18.155  -20.723 7.548   1.00 45.06 ? 119 ILE A CD1 1 
ATOM   1029 N  N   . ARG A 1 123 ? 20.019  -25.738 9.339   1.00 44.72 ? 120 ARG A N   1 
ATOM   1030 C  CA  . ARG A 1 123 ? 21.105  -26.532 9.895   1.00 45.20 ? 120 ARG A CA  1 
ATOM   1031 C  C   . ARG A 1 123 ? 21.051  -27.952 9.329   1.00 44.86 ? 120 ARG A C   1 
ATOM   1032 O  O   . ARG A 1 123 ? 22.087  -28.516 8.989   1.00 46.29 ? 120 ARG A O   1 
ATOM   1033 C  CB  . ARG A 1 123 ? 21.042  -26.558 11.428  1.00 46.84 ? 120 ARG A CB  1 
ATOM   1034 C  CG  . ARG A 1 123 ? 22.399  -26.468 12.111  1.00 48.88 ? 120 ARG A CG  1 
ATOM   1035 C  CD  . ARG A 1 123 ? 22.322  -26.780 13.601  1.00 50.53 ? 120 ARG A CD  1 
ATOM   1036 N  NE  . ARG A 1 123 ? 23.089  -25.839 14.427  1.00 52.45 ? 120 ARG A NE  1 
ATOM   1037 C  CZ  . ARG A 1 123 ? 23.366  -25.979 15.724  1.00 53.84 ? 120 ARG A CZ  1 
ATOM   1038 N  NH1 . ARG A 1 123 ? 23.104  -27.113 16.355  1.00 54.45 ? 120 ARG A NH1 1 
ATOM   1039 N  NH2 . ARG A 1 123 ? 23.936  -24.984 16.384  1.00 54.80 ? 120 ARG A NH2 1 
ATOM   1040 N  N   . LEU A 1 124 ? 19.836  -28.510 9.223   1.00 44.25 ? 121 LEU A N   1 
ATOM   1041 C  CA  . LEU A 1 124 ? 19.629  -29.856 8.706   1.00 43.41 ? 121 LEU A CA  1 
ATOM   1042 C  C   . LEU A 1 124 ? 20.131  -29.939 7.266   1.00 40.61 ? 121 LEU A C   1 
ATOM   1043 O  O   . LEU A 1 124 ? 20.882  -30.851 6.924   1.00 40.87 ? 121 LEU A O   1 
ATOM   1044 C  CB  . LEU A 1 124 ? 18.149  -30.227 8.817   1.00 45.04 ? 121 LEU A CB  1 
ATOM   1045 C  CG  . LEU A 1 124 ? 17.766  -31.669 8.460   1.00 46.53 ? 121 LEU A CG  1 
ATOM   1046 C  CD1 . LEU A 1 124 ? 16.557  -32.105 9.271   1.00 47.40 ? 121 LEU A CD1 1 
ATOM   1047 C  CD2 . LEU A 1 124 ? 17.472  -31.849 6.978   1.00 47.34 ? 121 LEU A CD2 1 
ATOM   1048 N  N   . TYR A 1 125 ? 19.712  -28.975 6.437   1.00 39.18 ? 122 TYR A N   1 
ATOM   1049 C  CA  . TYR A 1 125 ? 20.047  -28.961 5.022   1.00 36.43 ? 122 TYR A CA  1 
ATOM   1050 C  C   . TYR A 1 125 ? 21.539  -28.681 4.839   1.00 36.37 ? 122 TYR A C   1 
ATOM   1051 O  O   . TYR A 1 125 ? 22.163  -29.241 3.938   1.00 33.86 ? 122 TYR A O   1 
ATOM   1052 C  CB  . TYR A 1 125 ? 19.153  -27.943 4.304   1.00 35.03 ? 122 TYR A CB  1 
ATOM   1053 C  CG  . TYR A 1 125 ? 17.654  -28.204 4.406   1.00 34.40 ? 122 TYR A CG  1 
ATOM   1054 C  CD1 . TYR A 1 125 ? 17.138  -29.497 4.383   1.00 34.41 ? 122 TYR A CD1 1 
ATOM   1055 C  CD2 . TYR A 1 125 ? 16.753  -27.152 4.534   1.00 33.92 ? 122 TYR A CD2 1 
ATOM   1056 C  CE1 . TYR A 1 125 ? 15.774  -29.733 4.475   1.00 34.17 ? 122 TYR A CE1 1 
ATOM   1057 C  CE2 . TYR A 1 125 ? 15.388  -27.375 4.628   1.00 33.35 ? 122 TYR A CE2 1 
ATOM   1058 C  CZ  . TYR A 1 125 ? 14.896  -28.669 4.599   1.00 34.17 ? 122 TYR A CZ  1 
ATOM   1059 O  OH  . TYR A 1 125 ? 13.553  -28.891 4.694   1.00 36.46 ? 122 TYR A OH  1 
ATOM   1060 N  N   . GLN A 1 126 ? 22.109  -27.833 5.707   1.00 36.85 ? 123 GLN A N   1 
ATOM   1061 C  CA  . GLN A 1 126 ? 23.532  -27.525 5.656   1.00 37.78 ? 123 GLN A CA  1 
ATOM   1062 C  C   . GLN A 1 126 ? 24.356  -28.778 5.953   1.00 37.21 ? 123 GLN A C   1 
ATOM   1063 O  O   . GLN A 1 126 ? 25.340  -29.035 5.267   1.00 36.79 ? 123 GLN A O   1 
ATOM   1064 C  CB  . GLN A 1 126 ? 23.909  -26.371 6.588   1.00 39.29 ? 123 GLN A CB  1 
ATOM   1065 C  CG  . GLN A 1 126 ? 23.528  -24.994 6.050   1.00 40.56 ? 123 GLN A CG  1 
ATOM   1066 C  CD  . GLN A 1 126 ? 23.815  -23.872 7.025   1.00 42.23 ? 123 GLN A CD  1 
ATOM   1067 O  OE1 . GLN A 1 126 ? 23.590  -24.004 8.234   1.00 44.51 ? 123 GLN A OE1 1 
ATOM   1068 N  NE2 . GLN A 1 126 ? 24.323  -22.757 6.517   1.00 41.68 ? 123 GLN A NE2 1 
ATOM   1069 N  N   . GLN A 1 127 ? 23.945  -29.559 6.959   1.00 37.13 ? 124 GLN A N   1 
ATOM   1070 C  CA  . GLN A 1 127 ? 24.637  -30.792 7.311   1.00 37.39 ? 124 GLN A CA  1 
ATOM   1071 C  C   . GLN A 1 127 ? 24.571  -31.800 6.162   1.00 35.26 ? 124 GLN A C   1 
ATOM   1072 O  O   . GLN A 1 127 ? 25.430  -32.673 6.062   1.00 35.47 ? 124 GLN A O   1 
ATOM   1073 C  CB  . GLN A 1 127 ? 24.055  -31.421 8.577   1.00 39.56 ? 124 GLN A CB  1 
ATOM   1074 C  CG  . GLN A 1 127 ? 24.392  -30.664 9.857   1.00 42.01 ? 124 GLN A CG  1 
ATOM   1075 C  CD  . GLN A 1 127 ? 23.939  -31.376 11.113  1.00 44.81 ? 124 GLN A CD  1 
ATOM   1076 O  OE1 . GLN A 1 127 ? 23.554  -32.551 11.089  1.00 47.05 ? 124 GLN A OE1 1 
ATOM   1077 N  NE2 . GLN A 1 127 ? 24.000  -30.672 12.234  1.00 46.09 ? 124 GLN A NE2 1 
ATOM   1078 N  N   . LEU A 1 128 ? 23.546  -31.679 5.310   1.00 34.38 ? 125 LEU A N   1 
ATOM   1079 C  CA  . LEU A 1 128 ? 23.333  -32.596 4.202   1.00 32.31 ? 125 LEU A CA  1 
ATOM   1080 C  C   . LEU A 1 128 ? 23.944  -32.075 2.902   1.00 30.45 ? 125 LEU A C   1 
ATOM   1081 O  O   . LEU A 1 128 ? 23.813  -32.723 1.867   1.00 30.95 ? 125 LEU A O   1 
ATOM   1082 C  CB  . LEU A 1 128 ? 21.831  -32.841 4.067   1.00 33.30 ? 125 LEU A CB  1 
ATOM   1083 C  CG  . LEU A 1 128 ? 21.219  -33.734 5.150   1.00 34.72 ? 125 LEU A CG  1 
ATOM   1084 C  CD1 . LEU A 1 128 ? 19.729  -33.894 4.922   1.00 35.49 ? 125 LEU A CD1 1 
ATOM   1085 C  CD2 . LEU A 1 128 ? 21.904  -35.090 5.199   1.00 34.87 ? 125 LEU A CD2 1 
ATOM   1086 N  N   . GLY A 1 129 ? 24.601  -30.910 2.951   1.00 29.00 ? 126 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 129 ? 25.405  -30.442 1.834   1.00 28.91 ? 126 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 129 ? 24.761  -29.292 1.060   1.00 29.37 ? 126 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 129 ? 25.361  -28.792 0.111   1.00 30.16 ? 126 GLY A O   1 
ATOM   1090 N  N   . PHE A 1 130 ? 23.542  -28.885 1.446   1.00 27.46 ? 127 PHE A N   1 
ATOM   1091 C  CA  . PHE A 1 130 ? 22.892  -27.740 0.818   1.00 27.16 ? 127 PHE A CA  1 
ATOM   1092 C  C   . PHE A 1 130 ? 23.623  -26.459 1.222   1.00 28.23 ? 127 PHE A C   1 
ATOM   1093 O  O   . PHE A 1 130 ? 23.937  -26.272 2.395   1.00 30.74 ? 127 PHE A O   1 
ATOM   1094 C  CB  . PHE A 1 130 ? 21.409  -27.597 1.180   1.00 26.58 ? 127 PHE A CB  1 
ATOM   1095 C  CG  . PHE A 1 130 ? 20.463  -28.530 0.435   1.00 26.51 ? 127 PHE A CG  1 
ATOM   1096 C  CD1 . PHE A 1 130 ? 19.920  -28.163 -0.793  1.00 26.53 ? 127 PHE A CD1 1 
ATOM   1097 C  CD2 . PHE A 1 130 ? 20.138  -29.780 0.950   1.00 26.56 ? 127 PHE A CD2 1 
ATOM   1098 C  CE1 . PHE A 1 130 ? 19.063  -29.014 -1.477  1.00 26.25 ? 127 PHE A CE1 1 
ATOM   1099 C  CE2 . PHE A 1 130 ? 19.280  -30.625 0.263   1.00 26.37 ? 127 PHE A CE2 1 
ATOM   1100 C  CZ  . PHE A 1 130 ? 18.746  -30.244 -0.948  1.00 25.49 ? 127 PHE A CZ  1 
ATOM   1101 N  N   . VAL A 1 131 ? 23.860  -25.577 0.239   1.00 28.51 ? 128 VAL A N   1 
ATOM   1102 C  CA  . VAL A 1 131 ? 24.496  -24.288 0.473   1.00 29.69 ? 128 VAL A CA  1 
ATOM   1103 C  C   . VAL A 1 131 ? 23.637  -23.191 -0.153  1.00 29.76 ? 128 VAL A C   1 
ATOM   1104 O  O   . VAL A 1 131 ? 23.011  -23.398 -1.190  1.00 31.70 ? 128 VAL A O   1 
ATOM   1105 C  CB  . VAL A 1 131 ? 25.934  -24.228 -0.081  1.00 29.58 ? 128 VAL A CB  1 
ATOM   1106 C  CG1 . VAL A 1 131 ? 26.805  -25.331 0.506   1.00 29.11 ? 128 VAL A CG1 1 
ATOM   1107 C  CG2 . VAL A 1 131 ? 25.973  -24.271 -1.607  1.00 29.85 ? 128 VAL A CG2 1 
ATOM   1108 N  N   . PHE A 1 132 ? 23.653  -22.004 0.463   1.00 30.17 ? 129 PHE A N   1 
ATOM   1109 C  CA  . PHE A 1 132 ? 23.025  -20.833 -0.127  1.00 29.73 ? 129 PHE A CA  1 
ATOM   1110 C  C   . PHE A 1 132 ? 23.759  -20.473 -1.415  1.00 29.36 ? 129 PHE A C   1 
ATOM   1111 O  O   . PHE A 1 132 ? 24.987  -20.416 -1.426  1.00 29.78 ? 129 PHE A O   1 
ATOM   1112 C  CB  . PHE A 1 132 ? 23.036  -19.658 0.853   1.00 30.26 ? 129 PHE A CB  1 
ATOM   1113 C  CG  . PHE A 1 132 ? 22.095  -19.818 2.035   1.00 31.05 ? 129 PHE A CG  1 
ATOM   1114 C  CD1 . PHE A 1 132 ? 20.716  -19.789 1.850   1.00 30.29 ? 129 PHE A CD1 1 
ATOM   1115 C  CD2 . PHE A 1 132 ? 22.587  -19.968 3.327   1.00 31.07 ? 129 PHE A CD2 1 
ATOM   1116 C  CE1 . PHE A 1 132 ? 19.855  -19.927 2.925   1.00 31.38 ? 129 PHE A CE1 1 
ATOM   1117 C  CE2 . PHE A 1 132 ? 21.720  -20.105 4.400   1.00 32.68 ? 129 PHE A CE2 1 
ATOM   1118 C  CZ  . PHE A 1 132 ? 20.358  -20.078 4.198   1.00 32.13 ? 129 PHE A CZ  1 
ATOM   1119 N  N   . ASN A 1 133 ? 22.995  -20.242 -2.492  1.00 28.98 ? 130 ASN A N   1 
ATOM   1120 C  CA  . ASN A 1 133 ? 23.575  -20.035 -3.810  1.00 30.40 ? 130 ASN A CA  1 
ATOM   1121 C  C   . ASN A 1 133 ? 23.375  -18.599 -4.297  1.00 30.50 ? 130 ASN A C   1 
ATOM   1122 O  O   . ASN A 1 133 ? 23.646  -18.311 -5.462  1.00 31.37 ? 130 ASN A O   1 
ATOM   1123 C  CB  . ASN A 1 133 ? 23.027  -21.032 -4.823  1.00 31.29 ? 130 ASN A CB  1 
ATOM   1124 C  CG  . ASN A 1 133 ? 21.590  -20.761 -5.201  1.00 30.00 ? 130 ASN A CG  1 
ATOM   1125 O  OD1 . ASN A 1 133 ? 20.921  -19.908 -4.600  1.00 29.24 ? 130 ASN A OD1 1 
ATOM   1126 N  ND2 . ASN A 1 133 ? 21.110  -21.454 -6.221  1.00 30.13 ? 130 ASN A ND2 1 
ATOM   1127 N  N   . GLY A 1 134 ? 22.863  -17.719 -3.425  1.00 30.27 ? 131 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 134 ? 22.748  -16.301 -3.729  1.00 30.12 ? 131 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 134 ? 21.520  -15.961 -4.574  1.00 29.65 ? 131 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 134 ? 21.393  -14.829 -5.042  1.00 30.13 ? 131 GLY A O   1 
ATOM   1131 N  N   . GLU A 1 135 ? 20.611  -16.930 -4.748  1.00 28.96 ? 132 GLU A N   1 
ATOM   1132 C  CA  . GLU A 1 135 ? 19.367  -16.706 -5.469  1.00 29.03 ? 132 GLU A CA  1 
ATOM   1133 C  C   . GLU A 1 135 ? 18.221  -16.495 -4.484  1.00 27.84 ? 132 GLU A C   1 
ATOM   1134 O  O   . GLU A 1 135 ? 18.276  -16.956 -3.343  1.00 27.11 ? 132 GLU A O   1 
ATOM   1135 C  CB  . GLU A 1 135 ? 18.997  -17.888 -6.366  1.00 30.18 ? 132 GLU A CB  1 
ATOM   1136 C  CG  . GLU A 1 135 ? 19.729  -17.906 -7.705  1.00 31.58 ? 132 GLU A CG  1 
ATOM   1137 C  CD  . GLU A 1 135 ? 19.360  -19.086 -8.583  1.00 33.07 ? 132 GLU A CD  1 
ATOM   1138 O  OE1 . GLU A 1 135 ? 18.602  -19.947 -8.091  1.00 34.07 ? 132 GLU A OE1 1 
ATOM   1139 O  OE2 . GLU A 1 135 ? 19.815  -19.147 -9.746  1.00 33.89 ? 132 GLU A OE2 1 
ATOM   1140 N  N   . LEU A 1 136 ? 17.177  -15.810 -4.970  1.00 27.15 ? 133 LEU A N   1 
ATOM   1141 C  CA  . LEU A 1 136 ? 15.920  -15.658 -4.256  1.00 27.43 ? 133 LEU A CA  1 
ATOM   1142 C  C   . LEU A 1 136 ? 14.806  -16.335 -5.045  1.00 27.52 ? 133 LEU A C   1 
ATOM   1143 O  O   . LEU A 1 136 ? 14.720  -16.179 -6.261  1.00 28.18 ? 133 LEU A O   1 
ATOM   1144 C  CB  . LEU A 1 136 ? 15.602  -14.180 -4.056  1.00 28.38 ? 133 LEU A CB  1 
ATOM   1145 C  CG  . LEU A 1 136 ? 16.541  -13.423 -3.115  1.00 28.46 ? 133 LEU A CG  1 
ATOM   1146 C  CD1 . LEU A 1 136 ? 16.179  -11.947 -3.110  1.00 29.36 ? 133 LEU A CD1 1 
ATOM   1147 C  CD2 . LEU A 1 136 ? 16.511  -14.004 -1.708  1.00 28.04 ? 133 LEU A CD2 1 
ATOM   1148 N  N   . ASP A 1 137 ? 13.938  -17.050 -4.326  1.00 26.74 ? 134 ASP A N   1 
ATOM   1149 C  CA  . ASP A 1 137 ? 12.796  -17.707 -4.934  1.00 27.37 ? 134 ASP A CA  1 
ATOM   1150 C  C   . ASP A 1 137 ? 11.712  -16.659 -5.176  1.00 27.83 ? 134 ASP A C   1 
ATOM   1151 O  O   . ASP A 1 137 ? 11.840  -15.523 -4.727  1.00 26.59 ? 134 ASP A O   1 
ATOM   1152 C  CB  . ASP A 1 137 ? 12.345  -18.878 -4.076  1.00 26.35 ? 134 ASP A CB  1 
ATOM   1153 C  CG  . ASP A 1 137 ? 11.605  -19.989 -4.803  1.00 26.42 ? 134 ASP A CG  1 
ATOM   1154 O  OD1 . ASP A 1 137 ? 11.168  -19.760 -5.955  1.00 27.00 ? 134 ASP A OD1 1 
ATOM   1155 O  OD2 . ASP A 1 137 ? 11.492  -21.075 -4.214  1.00 26.84 ? 134 ASP A OD2 1 
ATOM   1156 N  N   . THR A 1 138 ? 10.647  -17.058 -5.884  1.00 28.89 ? 135 THR A N   1 
ATOM   1157 C  CA  . THR A 1 138 ? 9.565   -16.156 -6.262  1.00 29.15 ? 135 THR A CA  1 
ATOM   1158 C  C   . THR A 1 138 ? 8.777   -15.699 -5.033  1.00 28.78 ? 135 THR A C   1 
ATOM   1159 O  O   . THR A 1 138 ? 8.124   -14.658 -5.072  1.00 29.97 ? 135 THR A O   1 
ATOM   1160 C  CB  . THR A 1 138 ? 8.658   -16.843 -7.281  1.00 31.24 ? 135 THR A CB  1 
ATOM   1161 O  OG1 . THR A 1 138 ? 8.299   -18.092 -6.698  1.00 32.09 ? 135 THR A OG1 1 
ATOM   1162 C  CG2 . THR A 1 138 ? 9.351   -17.084 -8.610  1.00 31.96 ? 135 THR A CG2 1 
ATOM   1163 N  N   . ASN A 1 139 ? 8.862   -16.469 -3.943  1.00 27.27 ? 136 ASN A N   1 
ATOM   1164 C  CA  . ASN A 1 139 ? 8.214   -16.134 -2.685  1.00 27.90 ? 136 ASN A CA  1 
ATOM   1165 C  C   . ASN A 1 139 ? 9.166   -15.365 -1.769  1.00 29.29 ? 136 ASN A C   1 
ATOM   1166 O  O   . ASN A 1 139 ? 8.892   -15.227 -0.577  1.00 31.64 ? 136 ASN A O   1 
ATOM   1167 C  CB  . ASN A 1 139 ? 7.684   -17.388 -1.997  1.00 27.47 ? 136 ASN A CB  1 
ATOM   1168 C  CG  . ASN A 1 139 ? 8.769   -18.413 -1.765  1.00 26.89 ? 136 ASN A CG  1 
ATOM   1169 O  OD1 . ASN A 1 139 ? 9.954   -18.127 -1.974  1.00 25.36 ? 136 ASN A OD1 1 
ATOM   1170 N  ND2 . ASN A 1 139 ? 8.392   -19.607 -1.335  1.00 27.35 ? 136 ASN A ND2 1 
ATOM   1171 N  N   . GLY A 1 140 ? 10.295  -14.894 -2.320  1.00 29.04 ? 137 GLY A N   1 
ATOM   1172 C  CA  . GLY A 1 140 ? 11.245  -14.085 -1.578  1.00 27.88 ? 137 GLY A CA  1 
ATOM   1173 C  C   . GLY A 1 140 ? 12.165  -14.907 -0.676  1.00 26.59 ? 137 GLY A C   1 
ATOM   1174 O  O   . GLY A 1 140 ? 12.985  -14.334 0.033   1.00 26.34 ? 137 GLY A O   1 
ATOM   1175 N  N   . GLU A 1 141 ? 12.026  -16.239 -0.686  1.00 25.73 ? 138 GLU A N   1 
ATOM   1176 C  CA  . GLU A 1 141 ? 12.850  -17.089 0.161   1.00 25.65 ? 138 GLU A CA  1 
ATOM   1177 C  C   . GLU A 1 141 ? 14.231  -17.254 -0.469  1.00 26.18 ? 138 GLU A C   1 
ATOM   1178 O  O   . GLU A 1 141 ? 14.391  -17.182 -1.687  1.00 26.59 ? 138 GLU A O   1 
ATOM   1179 C  CB  . GLU A 1 141 ? 12.216  -18.456 0.431   1.00 25.22 ? 138 GLU A CB  1 
ATOM   1180 C  CG  . GLU A 1 141 ? 10.998  -18.393 1.350   1.00 25.51 ? 138 GLU A CG  1 
ATOM   1181 C  CD  . GLU A 1 141 ? 10.595  -19.735 1.930   1.00 26.77 ? 138 GLU A CD  1 
ATOM   1182 O  OE1 . GLU A 1 141 ? 10.525  -20.701 1.145   1.00 29.48 ? 138 GLU A OE1 1 
ATOM   1183 O  OE2 . GLU A 1 141 ? 10.347  -19.822 3.154   1.00 28.02 ? 138 GLU A OE2 1 
ATOM   1184 N  N   . ARG A 1 142 ? 15.221  -17.487 0.394   1.00 26.18 ? 139 ARG A N   1 
ATOM   1185 C  CA  . ARG A 1 142 ? 16.592  -17.702 -0.034  1.00 25.90 ? 139 ARG A CA  1 
ATOM   1186 C  C   . ARG A 1 142 ? 16.727  -19.138 -0.531  1.00 25.75 ? 139 ARG A C   1 
ATOM   1187 O  O   . ARG A 1 142 ? 16.268  -20.072 0.130   1.00 25.29 ? 139 ARG A O   1 
ATOM   1188 C  CB  . ARG A 1 142 ? 17.543  -17.439 1.135   1.00 28.17 ? 139 ARG A CB  1 
ATOM   1189 C  CG  . ARG A 1 142 ? 17.417  -16.051 1.745   1.00 29.57 ? 139 ARG A CG  1 
ATOM   1190 C  CD  . ARG A 1 142 ? 18.225  -15.958 3.026   1.00 31.84 ? 139 ARG A CD  1 
ATOM   1191 N  NE  . ARG A 1 142 ? 19.651  -16.101 2.721   1.00 33.55 ? 139 ARG A NE  1 
ATOM   1192 C  CZ  . ARG A 1 142 ? 20.611  -16.420 3.581   1.00 33.62 ? 139 ARG A CZ  1 
ATOM   1193 N  NH1 . ARG A 1 142 ? 20.323  -16.698 4.843   1.00 33.54 ? 139 ARG A NH1 1 
ATOM   1194 N  NH2 . ARG A 1 142 ? 21.864  -16.473 3.164   1.00 35.03 ? 139 ARG A NH2 1 
ATOM   1195 N  N   . VAL A 1 143 ? 17.339  -19.288 -1.710  1.00 24.74 ? 140 VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 143 ? 17.481  -20.580 -2.359  1.00 25.14 ? 140 VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 143 ? 18.733  -21.264 -1.820  1.00 25.97 ? 140 VAL A C   1 
ATOM   1198 O  O   . VAL A 1 143 ? 19.729  -20.611 -1.537  1.00 25.25 ? 140 VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 143 ? 17.526  -20.405 -3.890  1.00 25.56 ? 140 VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 143 ? 17.894  -21.690 -4.620  1.00 26.95 ? 140 VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 143 ? 16.219  -19.830 -4.423  1.00 25.40 ? 140 VAL A CG2 1 
ATOM   1202 N  N   . MET A 1 144 ? 18.644  -22.587 -1.659  1.00 26.13 ? 141 MET A N   1 
ATOM   1203 C  CA  . MET A 1 144 ? 19.792  -23.424 -1.358  1.00 26.72 ? 141 MET A CA  1 
ATOM   1204 C  C   . MET A 1 144 ? 19.917  -24.487 -2.443  1.00 27.76 ? 141 MET A C   1 
ATOM   1205 O  O   . MET A 1 144 ? 18.924  -24.865 -3.063  1.00 27.49 ? 141 MET A O   1 
ATOM   1206 C  CB  . MET A 1 144 ? 19.640  -24.144 -0.016  1.00 28.21 ? 141 MET A CB  1 
ATOM   1207 C  CG  . MET A 1 144 ? 19.544  -23.233 1.183   1.00 29.54 ? 141 MET A CG  1 
ATOM   1208 S  SD  . MET A 1 144 ? 19.416  -24.223 2.682   1.00 34.02 ? 141 MET A SD  1 
ATOM   1209 C  CE  . MET A 1 144 ? 18.922  -23.095 3.984   1.00 35.32 ? 141 MET A CE  1 
ATOM   1210 N  N   . GLU A 1 145 ? 21.147  -24.972 -2.633  1.00 28.52 ? 142 GLU A N   1 
ATOM   1211 C  CA  . GLU A 1 145 ? 21.472  -25.860 -3.734  1.00 29.66 ? 142 GLU A CA  1 
ATOM   1212 C  C   . GLU A 1 145 ? 22.431  -26.940 -3.245  1.00 29.71 ? 142 GLU A C   1 
ATOM   1213 O  O   . GLU A 1 145 ? 23.463  -26.635 -2.654  1.00 29.61 ? 142 GLU A O   1 
ATOM   1214 C  CB  . GLU A 1 145 ? 22.071  -25.029 -4.868  1.00 32.05 ? 142 GLU A CB  1 
ATOM   1215 C  CG  . GLU A 1 145 ? 22.279  -25.812 -6.161  1.00 33.33 ? 142 GLU A CG  1 
ATOM   1216 C  CD  . GLU A 1 145 ? 22.767  -24.985 -7.339  1.00 34.77 ? 142 GLU A CD  1 
ATOM   1217 O  OE1 . GLU A 1 145 ? 22.756  -23.737 -7.257  1.00 35.68 ? 142 GLU A OE1 1 
ATOM   1218 O  OE2 . GLU A 1 145 ? 23.173  -25.607 -8.345  1.00 36.01 ? 142 GLU A OE2 1 
ATOM   1219 N  N   . TRP A 1 146 ? 22.060  -28.200 -3.486  1.00 29.28 ? 143 TRP A N   1 
ATOM   1220 C  CA  . TRP A 1 146 ? 22.937  -29.332 -3.233  1.00 30.55 ? 143 TRP A CA  1 
ATOM   1221 C  C   . TRP A 1 146 ? 23.570  -29.767 -4.550  1.00 32.29 ? 143 TRP A C   1 
ATOM   1222 O  O   . TRP A 1 146 ? 22.869  -29.992 -5.535  1.00 30.04 ? 143 TRP A O   1 
ATOM   1223 C  CB  . TRP A 1 146 ? 22.164  -30.491 -2.585  1.00 30.92 ? 143 TRP A CB  1 
ATOM   1224 C  CG  . TRP A 1 146 ? 23.020  -31.668 -2.191  1.00 32.24 ? 143 TRP A CG  1 
ATOM   1225 C  CD1 . TRP A 1 146 ? 23.798  -31.793 -1.078  1.00 33.78 ? 143 TRP A CD1 1 
ATOM   1226 C  CD2 . TRP A 1 146 ? 23.149  -32.913 -2.905  1.00 33.07 ? 143 TRP A CD2 1 
ATOM   1227 N  NE1 . TRP A 1 146 ? 24.417  -33.014 -1.057  1.00 34.18 ? 143 TRP A NE1 1 
ATOM   1228 C  CE2 . TRP A 1 146 ? 24.039  -33.727 -2.164  1.00 33.04 ? 143 TRP A CE2 1 
ATOM   1229 C  CE3 . TRP A 1 146 ? 22.606  -33.415 -4.093  1.00 35.13 ? 143 TRP A CE3 1 
ATOM   1230 C  CZ2 . TRP A 1 146 ? 24.393  -35.011 -2.574  1.00 34.66 ? 143 TRP A CZ2 1 
ATOM   1231 C  CZ3 . TRP A 1 146 ? 22.955  -34.687 -4.494  1.00 36.31 ? 143 TRP A CZ3 1 
ATOM   1232 C  CH2 . TRP A 1 146 ? 23.835  -35.473 -3.745  1.00 35.79 ? 143 TRP A CH2 1 
ATOM   1233 N  N   . THR A 1 147 ? 24.902  -29.863 -4.552  1.00 34.50 ? 144 THR A N   1 
ATOM   1234 C  CA  . THR A 1 147 ? 25.638  -30.357 -5.701  1.00 38.24 ? 144 THR A CA  1 
ATOM   1235 C  C   . THR A 1 147 ? 26.353  -31.637 -5.283  1.00 42.22 ? 144 THR A C   1 
ATOM   1236 O  O   . THR A 1 147 ? 26.875  -31.735 -4.173  1.00 43.29 ? 144 THR A O   1 
ATOM   1237 C  CB  . THR A 1 147 ? 26.606  -29.292 -6.214  1.00 39.16 ? 144 THR A CB  1 
ATOM   1238 O  OG1 . THR A 1 147 ? 25.817  -28.125 -6.431  1.00 38.77 ? 144 THR A OG1 1 
ATOM   1239 C  CG2 . THR A 1 147 ? 27.289  -29.707 -7.505  1.00 40.61 ? 144 THR A CG2 1 
ATOM   1240 N  N   . HIS A 1 148 ? 26.377  -32.605 -6.202  1.00 45.55 ? 145 HIS A N   1 
ATOM   1241 C  CA  . HIS A 1 148 ? 26.777  -33.963 -5.881  1.00 47.09 ? 145 HIS A CA  1 
ATOM   1242 C  C   . HIS A 1 148 ? 28.267  -34.173 -6.147  1.00 47.51 ? 145 HIS A C   1 
ATOM   1243 O  O   . HIS A 1 148 ? 29.008  -34.532 -5.235  1.00 48.08 ? 145 HIS A O   1 
ATOM   1244 C  CB  . HIS A 1 148 ? 25.931  -34.960 -6.677  1.00 47.62 ? 145 HIS A CB  1 
ATOM   1245 C  CG  . HIS A 1 148 ? 26.343  -36.368 -6.433  1.00 49.82 ? 145 HIS A CG  1 
ATOM   1246 N  ND1 . HIS A 1 148 ? 26.820  -36.765 -5.204  1.00 50.73 ? 145 HIS A ND1 1 
ATOM   1247 C  CD2 . HIS A 1 148 ? 26.379  -37.447 -7.220  1.00 50.62 ? 145 HIS A CD2 1 
ATOM   1248 C  CE1 . HIS A 1 148 ? 27.132  -38.046 -5.256  1.00 50.75 ? 145 HIS A CE1 1 
ATOM   1249 N  NE2 . HIS A 1 148 ? 26.869  -38.484 -6.470  1.00 51.47 ? 145 HIS A NE2 1 
ATOM   1250 N  N   . GLN A 1 149 ? 28.678  -33.973 -7.406  1.00 48.04 ? 146 GLN A N   1 
ATOM   1251 C  CA  . GLN A 1 149 ? 30.013  -34.317 -7.873  1.00 47.44 ? 146 GLN A CA  1 
ATOM   1252 C  C   . GLN A 1 149 ? 30.146  -35.849 -7.934  1.00 46.89 ? 146 GLN A C   1 
ATOM   1253 O  O   . GLN A 1 149 ? 30.475  -36.348 -9.034  1.00 46.64 ? 146 GLN A O   1 
ATOM   1254 C  CB  . GLN A 1 149 ? 31.131  -33.741 -7.002  1.00 47.73 ? 146 GLN A CB  1 
ATOM   1255 C  CG  . GLN A 1 149 ? 31.134  -32.219 -6.904  0.53 48.07 ? 146 GLN A CG  1 
ATOM   1256 C  CD  . GLN A 1 149 ? 32.132  -31.691 -5.896  0.41 48.34 ? 146 GLN A CD  1 
ATOM   1257 O  OE1 . GLN A 1 149 ? 32.595  -32.409 -5.002  0.29 48.57 ? 146 GLN A OE1 1 
ATOM   1258 N  NE2 . GLN A 1 149 ? 32.462  -30.414 -6.021  0.38 48.78 ? 146 GLN A NE2 1 
ATOM   1259 N  N   . ALA B 1 3   ? 15.311  -50.703 15.139  1.00 42.00 ? 0   ALA B N   1 
ATOM   1260 C  CA  . ALA B 1 3   ? 15.704  -50.635 13.709  1.00 41.27 ? 0   ALA B CA  1 
ATOM   1261 C  C   . ALA B 1 3   ? 15.009  -49.449 13.045  1.00 40.53 ? 0   ALA B C   1 
ATOM   1262 O  O   . ALA B 1 3   ? 13.846  -49.171 13.336  1.00 43.31 ? 0   ALA B O   1 
ATOM   1263 C  CB  . ALA B 1 3   ? 15.365  -51.936 13.011  1.00 40.16 ? 0   ALA B CB  1 
ATOM   1264 N  N   . MET B 1 4   ? 15.740  -48.749 12.168  1.00 37.83 ? 1   MET B N   1 
ATOM   1265 C  CA  . MET B 1 4   ? 15.179  -47.665 11.379  1.00 35.30 ? 1   MET B CA  1 
ATOM   1266 C  C   . MET B 1 4   ? 15.033  -48.153 9.938   1.00 31.40 ? 1   MET B C   1 
ATOM   1267 O  O   . MET B 1 4   ? 16.001  -48.641 9.350   1.00 32.40 ? 1   MET B O   1 
ATOM   1268 C  CB  . MET B 1 4   ? 16.065  -46.414 11.457  1.00 37.67 ? 1   MET B CB  1 
ATOM   1269 C  CG  . MET B 1 4   ? 15.296  -45.105 11.340  1.00 39.07 ? 1   MET B CG  1 
ATOM   1270 S  SD  . MET B 1 4   ? 16.315  -43.614 11.360  1.00 41.24 ? 1   MET B SD  1 
ATOM   1271 C  CE  . MET B 1 4   ? 17.415  -43.945 9.977   1.00 41.99 ? 1   MET B CE  1 
ATOM   1272 N  N   . GLU B 1 5   ? 13.806  -48.061 9.404   1.00 27.37 ? 2   GLU B N   1 
ATOM   1273 C  CA  . GLU B 1 5   ? 13.466  -48.607 8.098   1.00 25.40 ? 2   GLU B CA  1 
ATOM   1274 C  C   . GLU B 1 5   ? 12.719  -47.557 7.280   1.00 24.85 ? 2   GLU B C   1 
ATOM   1275 O  O   . GLU B 1 5   ? 11.515  -47.669 7.086   1.00 25.05 ? 2   GLU B O   1 
ATOM   1276 C  CB  . GLU B 1 5   ? 12.588  -49.853 8.234   1.00 24.63 ? 2   GLU B CB  1 
ATOM   1277 C  CG  . GLU B 1 5   ? 13.263  -51.021 8.947   1.00 25.01 ? 2   GLU B CG  1 
ATOM   1278 C  CD  . GLU B 1 5   ? 12.315  -52.155 9.301   1.00 25.30 ? 2   GLU B CD  1 
ATOM   1279 O  OE1 . GLU B 1 5   ? 11.186  -52.191 8.767   1.00 25.66 ? 2   GLU B OE1 1 
ATOM   1280 O  OE2 . GLU B 1 5   ? 12.693  -52.985 10.150  1.00 26.40 ? 2   GLU B OE2 1 
ATOM   1281 N  N   . ILE B 1 6   ? 13.458  -46.561 6.774   1.00 24.48 ? 3   ILE B N   1 
ATOM   1282 C  CA  . ILE B 1 6   ? 12.862  -45.425 6.090   1.00 24.34 ? 3   ILE B CA  1 
ATOM   1283 C  C   . ILE B 1 6   ? 12.565  -45.800 4.642   1.00 22.61 ? 3   ILE B C   1 
ATOM   1284 O  O   . ILE B 1 6   ? 13.430  -46.330 3.950   1.00 23.32 ? 3   ILE B O   1 
ATOM   1285 C  CB  . ILE B 1 6   ? 13.786  -44.196 6.154   1.00 25.37 ? 3   ILE B CB  1 
ATOM   1286 C  CG1 . ILE B 1 6   ? 14.274  -43.912 7.575   1.00 27.93 ? 3   ILE B CG1 1 
ATOM   1287 C  CG2 . ILE B 1 6   ? 13.115  -42.979 5.517   1.00 25.87 ? 3   ILE B CG2 1 
ATOM   1288 C  CD1 . ILE B 1 6   ? 13.197  -43.465 8.541   1.00 29.60 ? 3   ILE B CD1 1 
ATOM   1289 N  N   . HIS B 1 7   ? 11.344  -45.497 4.190   1.00 23.11 ? 4   HIS B N   1 
ATOM   1290 C  CA  . HIS B 1 7   ? 10.974  -45.673 2.794   1.00 23.04 ? 4   HIS B CA  1 
ATOM   1291 C  C   . HIS B 1 7   ? 9.872   -44.679 2.434   1.00 23.42 ? 4   HIS B C   1 
ATOM   1292 O  O   . HIS B 1 7   ? 9.299   -44.041 3.312   1.00 23.45 ? 4   HIS B O   1 
ATOM   1293 C  CB  . HIS B 1 7   ? 10.603  -47.134 2.509   1.00 22.43 ? 4   HIS B CB  1 
ATOM   1294 C  CG  . HIS B 1 7   ? 9.420   -47.631 3.258   1.00 22.01 ? 4   HIS B CG  1 
ATOM   1295 N  ND1 . HIS B 1 7   ? 8.187   -47.748 2.656   1.00 23.05 ? 4   HIS B ND1 1 
ATOM   1296 C  CD2 . HIS B 1 7   ? 9.256   -48.021 4.527   1.00 21.99 ? 4   HIS B CD2 1 
ATOM   1297 C  CE1 . HIS B 1 7   ? 7.316   -48.215 3.538   1.00 23.50 ? 4   HIS B CE1 1 
ATOM   1298 N  NE2 . HIS B 1 7   ? 7.943   -48.389 4.680   1.00 22.43 ? 4   HIS B NE2 1 
ATOM   1299 N  N   . PHE B 1 8   ? 9.606   -44.565 1.129   1.00 23.96 ? 5   PHE B N   1 
ATOM   1300 C  CA  . PHE B 1 8   ? 8.692   -43.574 0.587   1.00 24.76 ? 5   PHE B CA  1 
ATOM   1301 C  C   . PHE B 1 8   ? 7.603   -44.279 -0.210  1.00 25.22 ? 5   PHE B C   1 
ATOM   1302 O  O   . PHE B 1 8   ? 7.901   -45.161 -1.013  1.00 25.65 ? 5   PHE B O   1 
ATOM   1303 C  CB  . PHE B 1 8   ? 9.444   -42.607 -0.328  1.00 25.31 ? 5   PHE B CB  1 
ATOM   1304 C  CG  . PHE B 1 8   ? 10.526  -41.832 0.405   1.00 26.63 ? 5   PHE B CG  1 
ATOM   1305 C  CD1 . PHE B 1 8   ? 11.798  -42.372 0.577   1.00 27.07 ? 5   PHE B CD1 1 
ATOM   1306 C  CD2 . PHE B 1 8   ? 10.252  -40.591 0.963   1.00 27.83 ? 5   PHE B CD2 1 
ATOM   1307 C  CE1 . PHE B 1 8   ? 12.771  -41.677 1.272   1.00 28.77 ? 5   PHE B CE1 1 
ATOM   1308 C  CE2 . PHE B 1 8   ? 11.236  -39.894 1.647   1.00 29.38 ? 5   PHE B CE2 1 
ATOM   1309 C  CZ  . PHE B 1 8   ? 12.487  -40.440 1.803   1.00 29.11 ? 5   PHE B CZ  1 
ATOM   1310 N  N   . GLU B 1 9   ? 6.350   -43.862 0.006   1.00 25.77 ? 6   GLU B N   1 
ATOM   1311 C  CA  . GLU B 1 9   ? 5.221   -44.403 -0.732  1.00 25.68 ? 6   GLU B CA  1 
ATOM   1312 C  C   . GLU B 1 9   ? 4.486   -43.264 -1.423  1.00 25.78 ? 6   GLU B C   1 
ATOM   1313 O  O   . GLU B 1 9   ? 4.294   -42.206 -0.832  1.00 25.87 ? 6   GLU B O   1 
ATOM   1314 C  CB  . GLU B 1 9   ? 4.241   -45.164 0.160   1.00 26.36 ? 6   GLU B CB  1 
ATOM   1315 C  CG  . GLU B 1 9   ? 4.878   -46.350 0.876   1.00 26.64 ? 6   GLU B CG  1 
ATOM   1316 C  CD  . GLU B 1 9   ? 3.898   -47.166 1.693   1.00 27.48 ? 6   GLU B CD  1 
ATOM   1317 O  OE1 . GLU B 1 9   ? 2.694   -46.837 1.666   1.00 27.94 ? 6   GLU B OE1 1 
ATOM   1318 O  OE2 . GLU B 1 9   ? 4.342   -48.137 2.345   1.00 28.47 ? 6   GLU B OE2 1 
ATOM   1319 N  N   . LYS B 1 10  ? 4.090   -43.504 -2.678  1.00 27.32 ? 7   LYS B N   1 
ATOM   1320 C  CA  . LYS B 1 10  ? 3.157   -42.648 -3.390  1.00 29.12 ? 7   LYS B CA  1 
ATOM   1321 C  C   . LYS B 1 10  ? 1.889   -42.497 -2.556  1.00 27.43 ? 7   LYS B C   1 
ATOM   1322 O  O   . LYS B 1 10  ? 1.499   -43.424 -1.846  1.00 26.11 ? 7   LYS B O   1 
ATOM   1323 C  CB  . LYS B 1 10  ? 2.758   -43.265 -4.736  1.00 32.47 ? 7   LYS B CB  1 
ATOM   1324 C  CG  . LYS B 1 10  ? 3.886   -43.457 -5.741  1.00 35.52 ? 7   LYS B CG  1 
ATOM   1325 C  CD  . LYS B 1 10  ? 3.500   -44.318 -6.938  1.00 37.50 ? 7   LYS B CD  1 
ATOM   1326 C  CE  . LYS B 1 10  ? 4.629   -44.525 -7.901  1.00 39.32 ? 7   LYS B CE  1 
ATOM   1327 N  NZ  . LYS B 1 10  ? 5.037   -43.279 -8.556  1.00 40.57 ? 7   LYS B NZ  1 
ATOM   1328 N  N   . VAL B 1 11  ? 1.248   -41.328 -2.662  1.00 27.76 ? 8   VAL B N   1 
ATOM   1329 C  CA  . VAL B 1 11  ? 0.021   -41.067 -1.931  1.00 28.00 ? 8   VAL B CA  1 
ATOM   1330 C  C   . VAL B 1 11  ? -1.158  -41.526 -2.788  1.00 29.15 ? 8   VAL B C   1 
ATOM   1331 O  O   . VAL B 1 11  ? -1.390  -40.989 -3.869  1.00 31.41 ? 8   VAL B O   1 
ATOM   1332 C  CB  . VAL B 1 11  ? -0.105  -39.587 -1.521  1.00 28.65 ? 8   VAL B CB  1 
ATOM   1333 C  CG1 . VAL B 1 11  ? -1.439  -39.321 -0.842  1.00 28.87 ? 8   VAL B CG1 1 
ATOM   1334 C  CG2 . VAL B 1 11  ? 1.040   -39.153 -0.615  1.00 28.65 ? 8   VAL B CG2 1 
ATOM   1335 N  N   . THR B 1 12  ? -1.876  -42.540 -2.287  1.00 28.00 ? 9   THR B N   1 
ATOM   1336 C  CA  . THR B 1 12  ? -3.067  -43.083 -2.922  1.00 28.72 ? 9   THR B CA  1 
ATOM   1337 C  C   . THR B 1 12  ? -4.188  -43.086 -1.886  1.00 27.57 ? 9   THR B C   1 
ATOM   1338 O  O   . THR B 1 12  ? -3.983  -42.643 -0.759  1.00 27.32 ? 9   THR B O   1 
ATOM   1339 C  CB  . THR B 1 12  ? -2.799  -44.500 -3.437  1.00 29.04 ? 9   THR B CB  1 
ATOM   1340 O  OG1 . THR B 1 12  ? -2.754  -45.359 -2.299  1.00 28.81 ? 9   THR B OG1 1 
ATOM   1341 C  CG2 . THR B 1 12  ? -1.509  -44.625 -4.228  1.00 29.92 ? 9   THR B CG2 1 
ATOM   1342 N  N   . SER B 1 13  ? -5.351  -43.646 -2.246  1.00 28.87 ? 10  SER B N   1 
ATOM   1343 C  CA  . SER B 1 13  ? -6.470  -43.704 -1.319  1.00 28.56 ? 10  SER B CA  1 
ATOM   1344 C  C   . SER B 1 13  ? -6.121  -44.561 -0.103  1.00 26.52 ? 10  SER B C   1 
ATOM   1345 O  O   . SER B 1 13  ? -6.712  -44.378 0.956   1.00 28.31 ? 10  SER B O   1 
ATOM   1346 C  CB  . SER B 1 13  ? -7.748  -44.162 -1.993  1.00 29.53 ? 10  SER B CB  1 
ATOM   1347 O  OG  . SER B 1 13  ? -7.809  -45.576 -2.113  1.00 31.60 ? 10  SER B OG  1 
ATOM   1348 N  N   . ASP B 1 14  ? -5.136  -45.462 -0.245  1.00 26.04 ? 11  ASP B N   1 
ATOM   1349 C  CA  . ASP B 1 14  ? -4.739  -46.338 0.845   1.00 25.88 ? 11  ASP B CA  1 
ATOM   1350 C  C   . ASP B 1 14  ? -4.181  -45.536 2.020   1.00 24.55 ? 11  ASP B C   1 
ATOM   1351 O  O   . ASP B 1 14  ? -4.403  -45.906 3.170   1.00 26.40 ? 11  ASP B O   1 
ATOM   1352 C  CB  . ASP B 1 14  ? -3.742  -47.388 0.378   1.00 27.08 ? 11  ASP B CB  1 
ATOM   1353 C  CG  . ASP B 1 14  ? -4.293  -48.456 -0.559  1.00 28.92 ? 11  ASP B CG  1 
ATOM   1354 O  OD1 . ASP B 1 14  ? -5.499  -48.405 -0.873  1.00 29.38 ? 11  ASP B OD1 1 
ATOM   1355 O  OD2 . ASP B 1 14  ? -3.502  -49.330 -0.974  1.00 31.86 ? 11  ASP B OD2 1 
ATOM   1356 N  N   . ASN B 1 15  ? -3.446  -44.449 1.744   1.00 23.94 ? 12  ASN B N   1 
ATOM   1357 C  CA  . ASN B 1 15  ? -2.768  -43.735 2.817   1.00 24.12 ? 12  ASN B CA  1 
ATOM   1358 C  C   . ASN B 1 15  ? -3.010  -42.222 2.809   1.00 23.74 ? 12  ASN B C   1 
ATOM   1359 O  O   . ASN B 1 15  ? -2.456  -41.523 3.652   1.00 23.01 ? 12  ASN B O   1 
ATOM   1360 C  CB  . ASN B 1 15  ? -1.270  -44.027 2.809   1.00 24.21 ? 12  ASN B CB  1 
ATOM   1361 C  CG  . ASN B 1 15  ? -0.595  -43.630 1.515   1.00 25.25 ? 12  ASN B CG  1 
ATOM   1362 O  OD1 . ASN B 1 15  ? -1.219  -43.030 0.632   1.00 24.88 ? 12  ASN B OD1 1 
ATOM   1363 N  ND2 . ASN B 1 15  ? 0.679   -43.967 1.375   1.00 25.98 ? 12  ASN B ND2 1 
ATOM   1364 N  N   A ARG B 1 16  ? -3.834  -41.721 1.882   0.58 24.26 ? 13  ARG B N   1 
ATOM   1365 N  N   B ARG B 1 16  ? -3.849  -41.713 1.897   0.42 23.79 ? 13  ARG B N   1 
ATOM   1366 C  CA  A ARG B 1 16  ? -3.999  -40.284 1.726   0.58 24.92 ? 13  ARG B CA  1 
ATOM   1367 C  CA  B ARG B 1 16  ? -3.972  -40.271 1.729   0.42 24.03 ? 13  ARG B CA  1 
ATOM   1368 C  C   A ARG B 1 16  ? -4.496  -39.663 3.029   0.58 23.72 ? 13  ARG B C   1 
ATOM   1369 C  C   B ARG B 1 16  ? -4.532  -39.630 2.999   0.42 23.38 ? 13  ARG B C   1 
ATOM   1370 O  O   A ARG B 1 16  ? -3.979  -38.642 3.467   0.58 24.59 ? 13  ARG B O   1 
ATOM   1371 O  O   B ARG B 1 16  ? -4.097  -38.549 3.380   0.42 23.98 ? 13  ARG B O   1 
ATOM   1372 C  CB  A ARG B 1 16  ? -4.920  -39.972 0.542   0.58 26.21 ? 13  ARG B CB  1 
ATOM   1373 C  CB  B ARG B 1 16  ? -4.791  -39.869 0.495   0.42 24.44 ? 13  ARG B CB  1 
ATOM   1374 C  CG  A ARG B 1 16  ? -5.298  -38.507 0.378   0.58 27.37 ? 13  ARG B CG  1 
ATOM   1375 C  CG  B ARG B 1 16  ? -6.268  -40.230 0.521   0.42 24.71 ? 13  ARG B CG  1 
ATOM   1376 C  CD  A ARG B 1 16  ? -5.342  -38.110 -1.090  0.58 28.94 ? 13  ARG B CD  1 
ATOM   1377 C  CD  B ARG B 1 16  ? -6.894  -40.080 -0.859  0.42 25.66 ? 13  ARG B CD  1 
ATOM   1378 N  NE  A ARG B 1 16  ? -5.990  -39.114 -1.943  0.58 31.93 ? 13  ARG B NE  1 
ATOM   1379 N  NE  B ARG B 1 16  ? -6.369  -38.924 -1.591  0.42 26.72 ? 13  ARG B NE  1 
ATOM   1380 C  CZ  A ARG B 1 16  ? -5.813  -39.233 -3.257  0.58 34.06 ? 13  ARG B CZ  1 
ATOM   1381 C  CZ  B ARG B 1 16  ? -5.899  -38.988 -2.831  0.42 28.34 ? 13  ARG B CZ  1 
ATOM   1382 N  NH1 A ARG B 1 16  ? -5.049  -38.374 -3.913  0.58 34.94 ? 13  ARG B NH1 1 
ATOM   1383 N  NH1 B ARG B 1 16  ? -6.035  -40.101 -3.531  0.42 29.17 ? 13  ARG B NH1 1 
ATOM   1384 N  NH2 A ARG B 1 16  ? -6.412  -40.211 -3.916  0.58 34.84 ? 13  ARG B NH2 1 
ATOM   1385 N  NH2 B ARG B 1 16  ? -5.322  -37.933 -3.378  0.42 27.98 ? 13  ARG B NH2 1 
ATOM   1386 N  N   . LYS B 1 17  ? -5.498  -40.284 3.656   1.00 23.53 ? 14  LYS B N   1 
ATOM   1387 C  CA  . LYS B 1 17  ? -6.088  -39.721 4.862   1.00 23.63 ? 14  LYS B CA  1 
ATOM   1388 C  C   . LYS B 1 17  ? -5.117  -39.808 6.038   1.00 23.30 ? 14  LYS B C   1 
ATOM   1389 O  O   . LYS B 1 17  ? -5.171  -38.974 6.938   1.00 24.83 ? 14  LYS B O   1 
ATOM   1390 C  CB  . LYS B 1 17  ? -7.448  -40.344 5.183   1.00 24.25 ? 14  LYS B CB  1 
ATOM   1391 C  CG  . LYS B 1 17  ? -8.494  -40.021 4.135   1.00 24.50 ? 14  LYS B CG  1 
ATOM   1392 C  CD  . LYS B 1 17  ? -9.912  -40.430 4.508   1.00 24.67 ? 14  LYS B CD  1 
ATOM   1393 C  CE  . LYS B 1 17  ? -10.830 -40.261 3.346   1.00 25.78 ? 14  LYS B CE  1 
ATOM   1394 N  NZ  . LYS B 1 17  ? -12.191 -40.704 3.659   1.00 26.49 ? 14  LYS B NZ  1 
ATOM   1395 N  N   . ALA B 1 18  ? -4.210  -40.790 6.017   1.00 23.78 ? 15  ALA B N   1 
ATOM   1396 C  CA  . ALA B 1 18  ? -3.144  -40.857 7.005   1.00 24.03 ? 15  ALA B CA  1 
ATOM   1397 C  C   . ALA B 1 18  ? -2.220  -39.646 6.864   1.00 23.70 ? 15  ALA B C   1 
ATOM   1398 O  O   . ALA B 1 18  ? -1.869  -39.013 7.858   1.00 25.16 ? 15  ALA B O   1 
ATOM   1399 C  CB  . ALA B 1 18  ? -2.375  -42.152 6.866   1.00 24.44 ? 15  ALA B CB  1 
ATOM   1400 N  N   . VAL B 1 19  ? -1.837  -39.329 5.619   1.00 22.94 ? 16  VAL B N   1 
ATOM   1401 C  CA  . VAL B 1 19  ? -0.995  -38.176 5.326   1.00 22.78 ? 16  VAL B CA  1 
ATOM   1402 C  C   . VAL B 1 19  ? -1.735  -36.886 5.689   1.00 22.70 ? 16  VAL B C   1 
ATOM   1403 O  O   . VAL B 1 19  ? -1.152  -35.982 6.279   1.00 23.29 ? 16  VAL B O   1 
ATOM   1404 C  CB  . VAL B 1 19  ? -0.535  -38.186 3.854   1.00 23.21 ? 16  VAL B CB  1 
ATOM   1405 C  CG1 . VAL B 1 19  ? 0.144   -36.877 3.452   1.00 23.67 ? 16  VAL B CG1 1 
ATOM   1406 C  CG2 . VAL B 1 19  ? 0.376   -39.375 3.559   1.00 23.38 ? 16  VAL B CG2 1 
ATOM   1407 N  N   . GLU B 1 20  ? -3.036  -36.813 5.382   1.00 21.96 ? 17  GLU B N   1 
ATOM   1408 C  CA  . GLU B 1 20  ? -3.804  -35.611 5.673   1.00 22.30 ? 17  GLU B CA  1 
ATOM   1409 C  C   . GLU B 1 20  ? -3.872  -35.355 7.179   1.00 22.66 ? 17  GLU B C   1 
ATOM   1410 O  O   . GLU B 1 20  ? -4.071  -34.215 7.592   1.00 24.81 ? 17  GLU B O   1 
ATOM   1411 C  CB  . GLU B 1 20  ? -5.189  -35.686 5.033   1.00 21.87 ? 17  GLU B CB  1 
ATOM   1412 C  CG  . GLU B 1 20  ? -5.132  -35.568 3.513   1.00 22.30 ? 17  GLU B CG  1 
ATOM   1413 C  CD  . GLU B 1 20  ? -6.418  -35.921 2.795   1.00 22.59 ? 17  GLU B CD  1 
ATOM   1414 O  OE1 . GLU B 1 20  ? -7.394  -36.365 3.449   1.00 24.13 ? 17  GLU B OE1 1 
ATOM   1415 O  OE2 . GLU B 1 20  ? -6.438  -35.747 1.557   1.00 24.07 ? 17  GLU B OE2 1 
ATOM   1416 N  N   . ASN B 1 21  ? -3.679  -36.405 7.988   1.00 24.31 ? 18  ASN B N   1 
ATOM   1417 C  CA  . ASN B 1 21  ? -3.807  -36.319 9.436   1.00 25.37 ? 18  ASN B CA  1 
ATOM   1418 C  C   . ASN B 1 21  ? -2.439  -36.251 10.123  1.00 26.05 ? 18  ASN B C   1 
ATOM   1419 O  O   . ASN B 1 21  ? -2.371  -36.308 11.347  1.00 27.01 ? 18  ASN B O   1 
ATOM   1420 C  CB  . ASN B 1 21  ? -4.663  -37.466 9.965   1.00 26.15 ? 18  ASN B CB  1 
ATOM   1421 C  CG  . ASN B 1 21  ? -6.137  -37.173 9.815   1.00 27.50 ? 18  ASN B CG  1 
ATOM   1422 O  OD1 . ASN B 1 21  ? -6.690  -36.388 10.594  1.00 28.98 ? 18  ASN B OD1 1 
ATOM   1423 N  ND2 . ASN B 1 21  ? -6.782  -37.766 8.822   1.00 27.50 ? 18  ASN B ND2 1 
ATOM   1424 N  N   . LEU B 1 22  ? -1.352  -36.084 9.359   1.00 27.21 ? 19  LEU B N   1 
ATOM   1425 C  CA  . LEU B 1 22  ? -0.030  -35.929 9.957   1.00 28.57 ? 19  LEU B CA  1 
ATOM   1426 C  C   . LEU B 1 22  ? -0.097  -34.873 11.061  1.00 28.93 ? 19  LEU B C   1 
ATOM   1427 O  O   . LEU B 1 22  ? -0.705  -33.817 10.874  1.00 28.35 ? 19  LEU B O   1 
ATOM   1428 C  CB  . LEU B 1 22  ? 1.013   -35.594 8.892   1.00 30.00 ? 19  LEU B CB  1 
ATOM   1429 C  CG  . LEU B 1 22  ? 1.638   -36.793 8.170   1.00 33.15 ? 19  LEU B CG  1 
ATOM   1430 C  CD1 . LEU B 1 22  ? 2.117   -36.424 6.782   1.00 34.01 ? 19  LEU B CD1 1 
ATOM   1431 C  CD2 . LEU B 1 22  ? 2.792   -37.358 8.973   1.00 32.44 ? 19  LEU B CD2 1 
ATOM   1432 N  N   . GLN B 1 23  ? 0.500   -35.189 12.219  1.00 30.54 ? 20  GLN B N   1 
ATOM   1433 C  CA  . GLN B 1 23  ? 0.444   -34.319 13.382  1.00 34.67 ? 20  GLN B CA  1 
ATOM   1434 C  C   . GLN B 1 23  ? 1.571   -33.296 13.273  1.00 35.05 ? 20  GLN B C   1 
ATOM   1435 O  O   . GLN B 1 23  ? 2.645   -33.470 13.844  1.00 34.73 ? 20  GLN B O   1 
ATOM   1436 C  CB  . GLN B 1 23  ? 0.471   -35.119 14.687  1.00 35.75 ? 20  GLN B CB  1 
ATOM   1437 C  CG  . GLN B 1 23  ? -0.681  -36.111 14.817  1.00 37.27 ? 20  GLN B CG  1 
ATOM   1438 C  CD  . GLN B 1 23  ? -0.723  -36.835 16.146  1.00 38.58 ? 20  GLN B CD  1 
ATOM   1439 O  OE1 . GLN B 1 23  ? -0.173  -36.381 17.156  1.00 41.61 ? 20  GLN B OE1 1 
ATOM   1440 N  NE2 . GLN B 1 23  ? -1.406  -37.971 16.164  1.00 38.94 ? 20  GLN B NE2 1 
ATOM   1441 N  N   . VAL B 1 24  ? 1.295   -32.236 12.506  1.00 36.67 ? 21  VAL B N   1 
ATOM   1442 C  CA  . VAL B 1 24  ? 2.254   -31.177 12.237  1.00 37.78 ? 21  VAL B CA  1 
ATOM   1443 C  C   . VAL B 1 24  ? 1.620   -29.828 12.575  1.00 38.82 ? 21  VAL B C   1 
ATOM   1444 O  O   . VAL B 1 24  ? 2.076   -28.799 12.088  1.00 39.45 ? 21  VAL B O   1 
ATOM   1445 C  CB  . VAL B 1 24  ? 2.714   -31.250 10.766  1.00 38.79 ? 21  VAL B CB  1 
ATOM   1446 C  CG1 . VAL B 1 24  ? 3.659   -32.418 10.523  1.00 38.64 ? 21  VAL B CG1 1 
ATOM   1447 C  CG2 . VAL B 1 24  ? 1.541   -31.321 9.796   1.00 40.08 ? 21  VAL B CG2 1 
ATOM   1448 N  N   . PHE B 1 25  ? 0.608   -29.851 13.456  1.00 38.83 ? 22  PHE B N   1 
ATOM   1449 C  CA  . PHE B 1 25  ? -0.223  -28.691 13.751  1.00 38.95 ? 22  PHE B CA  1 
ATOM   1450 C  C   . PHE B 1 25  ? 0.394   -27.833 14.858  1.00 39.50 ? 22  PHE B C   1 
ATOM   1451 O  O   . PHE B 1 25  ? -0.138  -26.766 15.171  1.00 40.10 ? 22  PHE B O   1 
ATOM   1452 C  CB  . PHE B 1 25  ? -1.636  -29.110 14.172  0.35 38.89 ? 22  PHE B CB  1 
ATOM   1453 C  CG  . PHE B 1 25  ? -1.697  -29.934 15.451  0.10 38.69 ? 22  PHE B CG  1 
ATOM   1454 C  CD1 . PHE B 1 25  ? -1.784  -29.321 16.696  0.43 38.52 ? 22  PHE B CD1 1 
ATOM   1455 C  CD2 . PHE B 1 25  ? -1.664  -31.323 15.403  0.10 38.60 ? 22  PHE B CD2 1 
ATOM   1456 C  CE1 . PHE B 1 25  ? -1.835  -30.077 17.857  0.48 38.45 ? 22  PHE B CE1 1 
ATOM   1457 C  CE2 . PHE B 1 25  ? -1.715  -32.074 16.567  0.17 38.32 ? 22  PHE B CE2 1 
ATOM   1458 C  CZ  . PHE B 1 25  ? -1.801  -31.450 17.789  0.10 38.40 ? 22  PHE B CZ  1 
ATOM   1459 N  N   . ALA B 1 26  ? 1.501   -28.297 15.456  1.00 39.12 ? 23  ALA B N   1 
ATOM   1460 C  CA  . ALA B 1 26  ? 2.140   -27.582 16.550  1.00 39.55 ? 23  ALA B CA  1 
ATOM   1461 C  C   . ALA B 1 26  ? 3.531   -27.082 16.157  1.00 39.00 ? 23  ALA B C   1 
ATOM   1462 O  O   . ALA B 1 26  ? 4.271   -26.597 17.010  1.00 39.45 ? 23  ALA B O   1 
ATOM   1463 C  CB  . ALA B 1 26  ? 2.203   -28.487 17.762  1.00 40.58 ? 23  ALA B CB  1 
ATOM   1464 N  N   . GLU B 1 27  ? 3.874   -27.177 14.866  1.00 37.92 ? 24  GLU B N   1 
ATOM   1465 C  CA  . GLU B 1 27  ? 5.202   -26.839 14.378  1.00 37.24 ? 24  GLU B CA  1 
ATOM   1466 C  C   . GLU B 1 27  ? 5.170   -25.468 13.703  1.00 37.18 ? 24  GLU B C   1 
ATOM   1467 O  O   . GLU B 1 27  ? 4.751   -25.358 12.553  1.00 37.66 ? 24  GLU B O   1 
ATOM   1468 C  CB  . GLU B 1 27  ? 5.645   -27.909 13.380  1.00 37.28 ? 24  GLU B CB  1 
ATOM   1469 C  CG  . GLU B 1 27  ? 5.574   -29.333 13.926  1.00 37.42 ? 24  GLU B CG  1 
ATOM   1470 C  CD  . GLU B 1 27  ? 5.923   -30.400 12.902  1.00 37.95 ? 24  GLU B CD  1 
ATOM   1471 O  OE1 . GLU B 1 27  ? 6.315   -30.037 11.772  1.00 39.20 ? 24  GLU B OE1 1 
ATOM   1472 O  OE2 . GLU B 1 27  ? 5.792   -31.598 13.237  1.00 38.10 ? 24  GLU B OE2 1 
ATOM   1473 N  N   . GLN B 1 28  ? 5.645   -24.435 14.414  1.00 38.32 ? 25  GLN B N   1 
ATOM   1474 C  CA  . GLN B 1 28  ? 5.516   -23.055 13.968  1.00 37.91 ? 25  GLN B CA  1 
ATOM   1475 C  C   . GLN B 1 28  ? 6.337   -22.795 12.706  1.00 34.89 ? 25  GLN B C   1 
ATOM   1476 O  O   . GLN B 1 28  ? 5.816   -22.247 11.739  1.00 32.49 ? 25  GLN B O   1 
ATOM   1477 C  CB  . GLN B 1 28  ? 5.945   -22.065 15.052  1.00 40.34 ? 25  GLN B CB  1 
ATOM   1478 C  CG  . GLN B 1 28  ? 4.997   -21.996 16.243  1.00 42.48 ? 25  GLN B CG  1 
ATOM   1479 C  CD  . GLN B 1 28  ? 5.333   -20.871 17.199  1.00 44.21 ? 25  GLN B CD  1 
ATOM   1480 O  OE1 . GLN B 1 28  ? 5.594   -19.734 16.789  1.00 43.06 ? 25  GLN B OE1 1 
ATOM   1481 N  NE2 . GLN B 1 28  ? 5.340   -21.178 18.489  1.00 45.87 ? 25  GLN B NE2 1 
ATOM   1482 N  N   . GLN B 1 29  ? 7.626   -23.161 12.727  1.00 34.55 ? 26  GLN B N   1 
ATOM   1483 C  CA  . GLN B 1 29  ? 8.516   -22.861 11.615  1.00 32.95 ? 26  GLN B CA  1 
ATOM   1484 C  C   . GLN B 1 29  ? 8.099   -23.660 10.381  1.00 30.13 ? 26  GLN B C   1 
ATOM   1485 O  O   . GLN B 1 29  ? 8.190   -23.155 9.264   1.00 29.08 ? 26  GLN B O   1 
ATOM   1486 C  CB  . GLN B 1 29  ? 9.987   -23.106 11.964  1.00 35.01 ? 26  GLN B CB  1 
ATOM   1487 C  CG  . GLN B 1 29  ? 10.542  -22.185 13.049  1.00 37.44 ? 26  GLN B CG  1 
ATOM   1488 C  CD  . GLN B 1 29  ? 10.451  -20.708 12.725  1.00 38.21 ? 26  GLN B CD  1 
ATOM   1489 O  OE1 . GLN B 1 29  ? 9.902   -19.914 13.497  1.00 40.23 ? 26  GLN B OE1 1 
ATOM   1490 N  NE2 . GLN B 1 29  ? 11.006  -20.312 11.588  1.00 38.92 ? 26  GLN B NE2 1 
ATOM   1491 N  N   . ALA B 1 30  ? 7.619   -24.893 10.589  1.00 28.37 ? 27  ALA B N   1 
ATOM   1492 C  CA  . ALA B 1 30  ? 7.150   -25.729 9.494   1.00 27.09 ? 27  ALA B CA  1 
ATOM   1493 C  C   . ALA B 1 30  ? 5.996   -25.045 8.760   1.00 26.29 ? 27  ALA B C   1 
ATOM   1494 O  O   . ALA B 1 30  ? 5.897   -25.146 7.540   1.00 26.23 ? 27  ALA B O   1 
ATOM   1495 C  CB  . ALA B 1 30  ? 6.756   -27.105 10.001  1.00 27.06 ? 27  ALA B CB  1 
ATOM   1496 N  N   . PHE B 1 31  ? 5.134   -24.337 9.500   1.00 26.63 ? 28  PHE B N   1 
ATOM   1497 C  CA  . PHE B 1 31  ? 4.004   -23.647 8.896   1.00 25.91 ? 28  PHE B CA  1 
ATOM   1498 C  C   . PHE B 1 31  ? 4.465   -22.518 7.980   1.00 24.62 ? 28  PHE B C   1 
ATOM   1499 O  O   . PHE B 1 31  ? 3.878   -22.315 6.922   1.00 23.98 ? 28  PHE B O   1 
ATOM   1500 C  CB  . PHE B 1 31  ? 3.074   -23.031 9.941   1.00 28.49 ? 28  PHE B CB  1 
ATOM   1501 C  CG  . PHE B 1 31  ? 2.386   -24.049 10.832  1.00 30.88 ? 28  PHE B CG  1 
ATOM   1502 C  CD1 . PHE B 1 31  ? 1.888   -25.235 10.309  0.34 31.50 ? 28  PHE B CD1 1 
ATOM   1503 C  CD2 . PHE B 1 31  ? 2.255   -23.812 12.191  0.45 31.87 ? 28  PHE B CD2 1 
ATOM   1504 C  CE1 . PHE B 1 31  ? 1.265   -26.157 11.128  0.79 32.41 ? 28  PHE B CE1 1 
ATOM   1505 C  CE2 . PHE B 1 31  ? 1.632   -24.738 13.006  0.64 32.06 ? 28  PHE B CE2 1 
ATOM   1506 C  CZ  . PHE B 1 31  ? 1.142   -25.905 12.471  0.67 32.62 ? 28  PHE B CZ  1 
ATOM   1507 N  N   . ILE B 1 32  ? 5.505   -21.783 8.397   1.00 24.73 ? 29  ILE B N   1 
ATOM   1508 C  CA  . ILE B 1 32  ? 6.028   -20.688 7.596   1.00 23.66 ? 29  ILE B CA  1 
ATOM   1509 C  C   . ILE B 1 32  ? 6.425   -21.236 6.227   1.00 22.56 ? 29  ILE B C   1 
ATOM   1510 O  O   . ILE B 1 32  ? 6.064   -20.661 5.205   1.00 23.05 ? 29  ILE B O   1 
ATOM   1511 C  CB  . ILE B 1 32  ? 7.193   -19.969 8.303   1.00 24.97 ? 29  ILE B CB  1 
ATOM   1512 C  CG1 . ILE B 1 32  ? 6.766   -19.382 9.654   1.00 25.94 ? 29  ILE B CG1 1 
ATOM   1513 C  CG2 . ILE B 1 32  ? 7.804   -18.898 7.397   1.00 25.18 ? 29  ILE B CG2 1 
ATOM   1514 C  CD1 . ILE B 1 32  ? 7.905   -18.796 10.468  1.00 27.32 ? 29  ILE B CD1 1 
ATOM   1515 N  N   . GLU B 1 33  ? 7.162   -22.356 6.217   1.00 22.44 ? 30  GLU B N   1 
ATOM   1516 C  CA  . GLU B 1 33  ? 7.580   -22.976 4.970   1.00 22.20 ? 30  GLU B CA  1 
ATOM   1517 C  C   . GLU B 1 33  ? 6.371   -23.470 4.178   1.00 21.09 ? 30  GLU B C   1 
ATOM   1518 O  O   . GLU B 1 33  ? 6.346   -23.338 2.958   1.00 22.86 ? 30  GLU B O   1 
ATOM   1519 C  CB  . GLU B 1 33  ? 8.572   -24.111 5.217   1.00 22.95 ? 30  GLU B CB  1 
ATOM   1520 C  CG  . GLU B 1 33  ? 9.846   -23.641 5.908   1.00 24.44 ? 30  GLU B CG  1 
ATOM   1521 C  CD  . GLU B 1 33  ? 10.627  -22.572 5.162   1.00 25.34 ? 30  GLU B CD  1 
ATOM   1522 O  OE1 . GLU B 1 33  ? 10.335  -22.310 3.974   1.00 25.17 ? 30  GLU B OE1 1 
ATOM   1523 O  OE2 . GLU B 1 33  ? 11.535  -21.981 5.782   1.00 27.76 ? 30  GLU B OE2 1 
ATOM   1524 N  N   A SER B 1 34  ? 5.399   -24.073 4.868   0.89 21.51 ? 31  SER B N   1 
ATOM   1525 N  N   B SER B 1 34  ? 5.373   -24.023 4.878   0.11 21.24 ? 31  SER B N   1 
ATOM   1526 C  CA  A SER B 1 34  ? 4.199   -24.559 4.207   0.89 21.17 ? 31  SER B CA  1 
ATOM   1527 C  CA  B SER B 1 34  ? 4.150   -24.482 4.240   0.11 20.98 ? 31  SER B CA  1 
ATOM   1528 C  C   A SER B 1 34  ? 3.488   -23.405 3.504   0.89 20.63 ? 31  SER B C   1 
ATOM   1529 C  C   B SER B 1 34  ? 3.458   -23.318 3.534   0.11 20.53 ? 31  SER B C   1 
ATOM   1530 O  O   A SER B 1 34  ? 3.098   -23.532 2.346   0.89 21.60 ? 31  SER B O   1 
ATOM   1531 O  O   B SER B 1 34  ? 3.082   -23.430 2.370   0.11 20.80 ? 31  SER B O   1 
ATOM   1532 C  CB  A SER B 1 34  ? 3.280   -25.245 5.172   0.89 21.49 ? 31  SER B CB  1 
ATOM   1533 C  CB  B SER B 1 34  ? 3.226   -25.141 5.232   0.11 21.13 ? 31  SER B CB  1 
ATOM   1534 O  OG  A SER B 1 34  ? 3.899   -26.394 5.731   0.89 21.61 ? 31  SER B OG  1 
ATOM   1535 O  OG  B SER B 1 34  ? 2.005   -25.523 4.614   0.11 21.18 ? 31  SER B OG  1 
ATOM   1536 N  N   A MET B 1 35  ? 3.330   -22.280 4.211   0.89 21.37 ? 32  MET B N   1 
ATOM   1537 N  N   B MET B 1 35  ? 3.308   -22.198 4.249   0.11 20.15 ? 32  MET B N   1 
ATOM   1538 C  CA  A MET B 1 35  ? 2.650   -21.116 3.661   0.89 22.04 ? 32  MET B CA  1 
ATOM   1539 C  CA  B MET B 1 35  ? 2.638   -21.029 3.704   0.11 19.74 ? 32  MET B CA  1 
ATOM   1540 C  C   A MET B 1 35  ? 3.463   -20.510 2.519   0.89 20.62 ? 32  MET B C   1 
ATOM   1541 C  C   B MET B 1 35  ? 3.453   -20.446 2.550   0.11 20.18 ? 32  MET B C   1 
ATOM   1542 O  O   A MET B 1 35  ? 2.902   -20.119 1.502   0.89 21.25 ? 32  MET B O   1 
ATOM   1543 O  O   B MET B 1 35  ? 2.878   -20.014 1.556   0.11 20.39 ? 32  MET B O   1 
ATOM   1544 C  CB  A MET B 1 35  ? 2.389   -20.050 4.731   0.89 23.90 ? 32  MET B CB  1 
ATOM   1545 C  CB  B MET B 1 35  ? 2.400   -19.965 4.783   0.11 19.13 ? 32  MET B CB  1 
ATOM   1546 C  CG  A MET B 1 35  ? 1.632   -18.831 4.213   0.89 25.31 ? 32  MET B CG  1 
ATOM   1547 C  CG  B MET B 1 35  ? 1.307   -20.323 5.779   0.11 18.34 ? 32  MET B CG  1 
ATOM   1548 S  SD  A MET B 1 35  ? -0.046  -19.131 3.620   0.89 28.37 ? 32  MET B SD  1 
ATOM   1549 S  SD  B MET B 1 35  ? -0.321  -20.526 5.028   0.11 17.40 ? 32  MET B SD  1 
ATOM   1550 C  CE  A MET B 1 35  ? -0.831  -19.625 5.160   0.89 27.74 ? 32  MET B CE  1 
ATOM   1551 C  CE  B MET B 1 35  ? -0.514  -18.925 4.235   0.11 17.54 ? 32  MET B CE  1 
ATOM   1552 N  N   . ALA B 1 36  ? 4.788   -20.432 2.683   1.00 20.87 ? 33  ALA B N   1 
ATOM   1553 C  CA  . ALA B 1 36  ? 5.649   -19.904 1.636   1.00 20.46 ? 33  ALA B CA  1 
ATOM   1554 C  C   . ALA B 1 36  ? 5.492   -20.714 0.352   1.00 19.85 ? 33  ALA B C   1 
ATOM   1555 O  O   . ALA B 1 36  ? 5.454   -20.151 -0.740  1.00 19.68 ? 33  ALA B O   1 
ATOM   1556 C  CB  . ALA B 1 36  ? 7.080   -19.882 2.105   1.00 21.02 ? 33  ALA B CB  1 
ATOM   1557 N  N   . GLU B 1 37  ? 5.385   -22.038 0.501   1.00 19.98 ? 34  GLU B N   1 
ATOM   1558 C  CA  . GLU B 1 37  ? 5.219   -22.933 -0.633  1.00 20.67 ? 34  GLU B CA  1 
ATOM   1559 C  C   . GLU B 1 37  ? 3.828   -22.750 -1.241  1.00 20.21 ? 34  GLU B C   1 
ATOM   1560 O  O   . GLU B 1 37  ? 3.674   -22.854 -2.451  1.00 20.66 ? 34  GLU B O   1 
ATOM   1561 C  CB  . GLU B 1 37  ? 5.468   -24.389 -0.238  1.00 21.44 ? 34  GLU B CB  1 
ATOM   1562 C  CG  . GLU B 1 37  ? 5.285   -25.366 -1.396  1.00 22.06 ? 34  GLU B CG  1 
ATOM   1563 C  CD  . GLU B 1 37  ? 6.240   -25.176 -2.558  1.00 22.30 ? 34  GLU B CD  1 
ATOM   1564 O  OE1 . GLU B 1 37  ? 7.294   -24.530 -2.374  1.00 23.31 ? 34  GLU B OE1 1 
ATOM   1565 O  OE2 . GLU B 1 37  ? 5.924   -25.684 -3.655  1.00 23.16 ? 34  GLU B OE2 1 
ATOM   1566 N  N   . ASN B 1 38  ? 2.819   -22.477 -0.404  1.00 21.19 ? 35  ASN B N   1 
ATOM   1567 C  CA  . ASN B 1 38  ? 1.478   -22.191 -0.897  1.00 21.01 ? 35  ASN B CA  1 
ATOM   1568 C  C   . ASN B 1 38  ? 1.524   -20.992 -1.842  1.00 21.98 ? 35  ASN B C   1 
ATOM   1569 O  O   . ASN B 1 38  ? 0.939   -21.019 -2.923  1.00 23.24 ? 35  ASN B O   1 
ATOM   1570 C  CB  . ASN B 1 38  ? 0.491   -21.883 0.226   1.00 20.52 ? 35  ASN B CB  1 
ATOM   1571 C  CG  . ASN B 1 38  ? 0.211   -23.061 1.126   1.00 21.00 ? 35  ASN B CG  1 
ATOM   1572 O  OD1 . ASN B 1 38  ? 0.479   -24.213 0.758   1.00 20.64 ? 35  ASN B OD1 1 
ATOM   1573 N  ND2 . ASN B 1 38  ? -0.340  -22.790 2.302   1.00 21.55 ? 35  ASN B ND2 1 
ATOM   1574 N  N   . LEU B 1 39  ? 2.228   -19.941 -1.410  1.00 21.90 ? 36  LEU B N   1 
ATOM   1575 C  CA  . LEU B 1 39  ? 2.328   -18.700 -2.165  1.00 22.82 ? 36  LEU B CA  1 
ATOM   1576 C  C   . LEU B 1 39  ? 3.113   -18.917 -3.455  1.00 22.56 ? 36  LEU B C   1 
ATOM   1577 O  O   . LEU B 1 39  ? 2.797   -18.314 -4.477  1.00 24.06 ? 36  LEU B O   1 
ATOM   1578 C  CB  . LEU B 1 39  ? 2.964   -17.604 -1.313  1.00 23.64 ? 36  LEU B CB  1 
ATOM   1579 C  CG  . LEU B 1 39  ? 2.210   -17.208 -0.042  1.00 23.88 ? 36  LEU B CG  1 
ATOM   1580 C  CD1 . LEU B 1 39  ? 2.979   -16.127 0.704   1.00 24.21 ? 36  LEU B CD1 1 
ATOM   1581 C  CD2 . LEU B 1 39  ? 0.804   -16.743 -0.357  1.00 24.99 ? 36  LEU B CD2 1 
ATOM   1582 N  N   . LYS B 1 40  ? 4.154   -19.753 -3.402  1.00 22.08 ? 37  LYS B N   1 
ATOM   1583 C  CA  . LYS B 1 40  ? 4.950   -20.040 -4.583  1.00 23.04 ? 37  LYS B CA  1 
ATOM   1584 C  C   . LYS B 1 40  ? 4.083   -20.709 -5.646  1.00 24.47 ? 37  LYS B C   1 
ATOM   1585 O  O   . LYS B 1 40  ? 4.096   -20.300 -6.806  1.00 25.94 ? 37  LYS B O   1 
ATOM   1586 C  CB  . LYS B 1 40  ? 6.149   -20.925 -4.232  1.00 22.54 ? 37  LYS B CB  1 
ATOM   1587 C  CG  . LYS B 1 40  ? 7.013   -21.309 -5.424  1.00 22.71 ? 37  LYS B CG  1 
ATOM   1588 C  CD  . LYS B 1 40  ? 8.303   -22.025 -5.047  1.00 23.00 ? 37  LYS B CD  1 
ATOM   1589 C  CE  . LYS B 1 40  ? 9.087   -22.435 -6.252  1.00 23.07 ? 37  LYS B CE  1 
ATOM   1590 N  NZ  . LYS B 1 40  ? 10.328  -23.113 -5.881  1.00 22.20 ? 37  LYS B NZ  1 
ATOM   1591 N  N   . GLU B 1 41  ? 3.327   -21.730 -5.227  1.00 25.17 ? 38  GLU B N   1 
ATOM   1592 C  CA  . GLU B 1 41  ? 2.524   -22.529 -6.138  1.00 25.99 ? 38  GLU B CA  1 
ATOM   1593 C  C   . GLU B 1 41  ? 1.382   -21.682 -6.693  1.00 27.04 ? 38  GLU B C   1 
ATOM   1594 O  O   . GLU B 1 41  ? 1.069   -21.765 -7.878  1.00 27.99 ? 38  GLU B O   1 
ATOM   1595 C  CB  . GLU B 1 41  ? 2.021   -23.793 -5.439  1.00 27.58 ? 38  GLU B CB  1 
ATOM   1596 C  CG  . GLU B 1 41  ? 3.150   -24.732 -5.020  1.00 27.76 ? 38  GLU B CG  1 
ATOM   1597 C  CD  . GLU B 1 41  ? 2.703   -26.044 -4.398  1.00 28.43 ? 38  GLU B CD  1 
ATOM   1598 O  OE1 . GLU B 1 41  ? 1.490   -26.346 -4.435  1.00 29.76 ? 38  GLU B OE1 1 
ATOM   1599 O  OE2 . GLU B 1 41  ? 3.569   -26.759 -3.852  1.00 27.55 ? 38  GLU B OE2 1 
ATOM   1600 N  N   . SER B 1 42  ? 0.784   -20.857 -5.828  1.00 27.94 ? 39  SER B N   1 
ATOM   1601 C  CA  . SER B 1 42  ? -0.288  -19.964 -6.237  1.00 28.12 ? 39  SER B CA  1 
ATOM   1602 C  C   . SER B 1 42  ? 0.204   -18.981 -7.296  1.00 30.17 ? 39  SER B C   1 
ATOM   1603 O  O   . SER B 1 42  ? -0.467  -18.778 -8.308  1.00 30.51 ? 39  SER B O   1 
ATOM   1604 C  CB  . SER B 1 42  ? -0.872  -19.239 -5.057  1.00 27.66 ? 39  SER B CB  1 
ATOM   1605 O  OG  . SER B 1 42  ? -2.041  -18.535 -5.448  1.00 27.86 ? 39  SER B OG  1 
ATOM   1606 N  N   . ASP B 1 43  ? 1.375   -18.378 -7.051  1.00 31.61 ? 40  ASP B N   1 
ATOM   1607 C  CA  . ASP B 1 43  ? 1.932   -17.357 -7.927  1.00 34.14 ? 40  ASP B CA  1 
ATOM   1608 C  C   . ASP B 1 43  ? 2.351   -17.964 -9.264  1.00 37.00 ? 40  ASP B C   1 
ATOM   1609 O  O   . ASP B 1 43  ? 2.452   -17.253 -10.262 1.00 37.97 ? 40  ASP B O   1 
ATOM   1610 C  CB  . ASP B 1 43  ? 3.086   -16.628 -7.258  1.00 35.06 ? 40  ASP B CB  1 
ATOM   1611 C  CG  . ASP B 1 43  ? 2.713   -15.823 -6.022  1.00 35.86 ? 40  ASP B CG  1 
ATOM   1612 O  OD1 . ASP B 1 43  ? 1.515   -15.805 -5.674  1.00 37.63 ? 40  ASP B OD1 1 
ATOM   1613 O  OD2 . ASP B 1 43  ? 3.620   -15.231 -5.408  1.00 36.93 ? 40  ASP B OD2 1 
ATOM   1614 N  N   . GLN B 1 44  ? 2.592   -19.279 -9.277  1.00 39.66 ? 41  GLN B N   1 
ATOM   1615 C  CA  . GLN B 1 44  ? 3.066   -19.954 -10.471 1.00 43.27 ? 41  GLN B CA  1 
ATOM   1616 C  C   . GLN B 1 44  ? 1.952   -20.059 -11.513 1.00 43.92 ? 41  GLN B C   1 
ATOM   1617 O  O   . GLN B 1 44  ? 2.186   -19.784 -12.688 1.00 43.77 ? 41  GLN B O   1 
ATOM   1618 C  CB  . GLN B 1 44  ? 3.633   -21.330 -10.123 1.00 45.14 ? 41  GLN B CB  1 
ATOM   1619 C  CG  . GLN B 1 44  ? 4.443   -21.948 -11.256 1.00 46.75 ? 41  GLN B CG  1 
ATOM   1620 C  CD  . GLN B 1 44  ? 5.418   -20.965 -11.869 1.00 48.50 ? 41  GLN B CD  1 
ATOM   1621 O  OE1 . GLN B 1 44  ? 6.379   -20.527 -11.227 1.00 50.98 ? 41  GLN B OE1 1 
ATOM   1622 N  NE2 . GLN B 1 44  ? 5.178   -20.599 -13.121 1.00 49.22 ? 41  GLN B NE2 1 
ATOM   1623 N  N   . PHE B 1 45  ? 0.748   -20.457 -11.084 1.00 44.91 ? 42  PHE B N   1 
ATOM   1624 C  CA  . PHE B 1 45  ? -0.337  -20.729 -12.014 1.00 46.75 ? 42  PHE B CA  1 
ATOM   1625 C  C   . PHE B 1 45  ? -1.339  -19.579 -12.006 1.00 45.76 ? 42  PHE B C   1 
ATOM   1626 O  O   . PHE B 1 45  ? -1.782  -19.142 -10.946 1.00 43.60 ? 42  PHE B O   1 
ATOM   1627 C  CB  . PHE B 1 45  ? -1.006  -22.067 -11.692 1.00 48.54 ? 42  PHE B CB  1 
ATOM   1628 C  CG  . PHE B 1 45  ? -0.198  -23.262 -12.176 1.00 50.62 ? 42  PHE B CG  1 
ATOM   1629 C  CD1 . PHE B 1 45  ? -0.244  -23.660 -13.510 1.00 51.69 ? 42  PHE B CD1 1 
ATOM   1630 C  CD2 . PHE B 1 45  ? 0.618   -23.973 -11.302 1.00 51.89 ? 42  PHE B CD2 1 
ATOM   1631 C  CE1 . PHE B 1 45  ? 0.502   -24.742 -13.953 1.00 52.65 ? 42  PHE B CE1 1 
ATOM   1632 C  CE2 . PHE B 1 45  ? 1.359   -25.057 -11.749 1.00 52.55 ? 42  PHE B CE2 1 
ATOM   1633 C  CZ  . PHE B 1 45  ? 1.300   -25.439 -13.073 1.00 52.94 ? 42  PHE B CZ  1 
ATOM   1634 N  N   . PRO B 1 46  ? -1.726  -19.055 -13.192 1.00 47.67 ? 43  PRO B N   1 
ATOM   1635 C  CA  . PRO B 1 46  ? -2.653  -17.930 -13.280 1.00 47.76 ? 43  PRO B CA  1 
ATOM   1636 C  C   . PRO B 1 46  ? -4.091  -18.250 -12.876 1.00 46.86 ? 43  PRO B C   1 
ATOM   1637 O  O   . PRO B 1 46  ? -4.844  -17.339 -12.539 1.00 48.24 ? 43  PRO B O   1 
ATOM   1638 C  CB  . PRO B 1 46  ? -2.569  -17.499 -14.738 1.00 48.84 ? 43  PRO B CB  1 
ATOM   1639 C  CG  . PRO B 1 46  ? -2.128  -18.756 -15.447 1.00 48.69 ? 43  PRO B CG  1 
ATOM   1640 C  CD  . PRO B 1 46  ? -1.255  -19.513 -14.508 1.00 48.47 ? 43  PRO B CD  1 
ATOM   1641 N  N   . GLU B 1 47  ? -4.469  -19.535 -12.920 1.00 45.65 ? 44  GLU B N   1 
ATOM   1642 C  CA  . GLU B 1 47  ? -5.779  -19.968 -12.455 1.00 43.79 ? 44  GLU B CA  1 
ATOM   1643 C  C   . GLU B 1 47  ? -5.975  -19.531 -11.006 1.00 40.02 ? 44  GLU B C   1 
ATOM   1644 O  O   . GLU B 1 47  ? -7.056  -19.080 -10.628 1.00 38.85 ? 44  GLU B O   1 
ATOM   1645 C  CB  . GLU B 1 47  ? -5.991  -21.486 -12.433 1.00 45.55 ? 44  GLU B CB  1 
ATOM   1646 C  CG  . GLU B 1 47  ? -5.522  -22.226 -13.682 1.00 47.12 ? 44  GLU B CG  1 
ATOM   1647 C  CD  . GLU B 1 47  ? -4.091  -22.739 -13.650 1.00 47.90 ? 44  GLU B CD  1 
ATOM   1648 O  OE1 . GLU B 1 47  ? -3.812  -23.730 -12.937 1.00 47.12 ? 44  GLU B OE1 1 
ATOM   1649 O  OE2 . GLU B 1 47  ? -3.246  -22.133 -14.343 1.00 48.60 ? 44  GLU B OE2 1 
ATOM   1650 N  N   . TRP B 1 48  ? -4.911  -19.699 -10.210 1.00 36.48 ? 45  TRP B N   1 
ATOM   1651 C  CA  . TRP B 1 48  ? -4.963  -19.560 -8.766  1.00 34.26 ? 45  TRP B CA  1 
ATOM   1652 C  C   . TRP B 1 48  ? -4.623  -18.132 -8.364  1.00 32.76 ? 45  TRP B C   1 
ATOM   1653 O  O   . TRP B 1 48  ? -3.790  -17.492 -9.000  1.00 33.26 ? 45  TRP B O   1 
ATOM   1654 C  CB  . TRP B 1 48  ? -3.970  -20.528 -8.110  1.00 34.65 ? 45  TRP B CB  1 
ATOM   1655 C  CG  . TRP B 1 48  ? -4.169  -21.972 -8.482  1.00 35.60 ? 45  TRP B CG  1 
ATOM   1656 C  CD1 . TRP B 1 48  ? -5.264  -22.541 -9.064  1.00 36.64 ? 45  TRP B CD1 1 
ATOM   1657 C  CD2 . TRP B 1 48  ? -3.227  -23.045 -8.269  1.00 35.76 ? 45  TRP B CD2 1 
ATOM   1658 N  NE1 . TRP B 1 48  ? -5.064  -23.884 -9.241  1.00 37.67 ? 45  TRP B NE1 1 
ATOM   1659 C  CE2 . TRP B 1 48  ? -3.830  -24.223 -8.759  1.00 36.97 ? 45  TRP B CE2 1 
ATOM   1660 C  CE3 . TRP B 1 48  ? -1.942  -23.125 -7.720  1.00 36.26 ? 45  TRP B CE3 1 
ATOM   1661 C  CZ2 . TRP B 1 48  ? -3.192  -25.458 -8.710  1.00 36.18 ? 45  TRP B CZ2 1 
ATOM   1662 C  CZ3 . TRP B 1 48  ? -1.313  -24.348 -7.672  1.00 35.87 ? 45  TRP B CZ3 1 
ATOM   1663 C  CH2 . TRP B 1 48  ? -1.930  -25.497 -8.163  1.00 36.39 ? 45  TRP B CH2 1 
ATOM   1664 N  N   . GLU B 1 49  ? -5.252  -17.663 -7.283  1.00 31.32 ? 46  GLU B N   1 
ATOM   1665 C  CA  . GLU B 1 49  ? -4.896  -16.389 -6.687  1.00 30.89 ? 46  GLU B CA  1 
ATOM   1666 C  C   . GLU B 1 49  ? -4.863  -16.540 -5.169  1.00 27.70 ? 46  GLU B C   1 
ATOM   1667 O  O   . GLU B 1 49  ? -5.718  -17.202 -4.589  1.00 26.52 ? 46  GLU B O   1 
ATOM   1668 C  CB  . GLU B 1 49  ? -5.860  -15.278 -7.106  1.00 33.37 ? 46  GLU B CB  1 
ATOM   1669 C  CG  . GLU B 1 49  ? -5.383  -13.892 -6.681  1.00 36.72 ? 46  GLU B CG  1 
ATOM   1670 C  CD  . GLU B 1 49  ? -6.418  -12.789 -6.798  1.00 38.56 ? 46  GLU B CD  1 
ATOM   1671 O  OE1 . GLU B 1 49  ? -7.055  -12.671 -7.865  1.00 41.82 ? 46  GLU B OE1 1 
ATOM   1672 O  OE2 . GLU B 1 49  ? -6.579  -12.036 -5.815  1.00 42.50 ? 46  GLU B OE2 1 
ATOM   1673 N  N   . SER B 1 50  ? -3.853  -15.917 -4.550  1.00 27.44 ? 47  SER B N   1 
ATOM   1674 C  CA  . SER B 1 50  ? -3.735  -15.827 -3.104  1.00 26.06 ? 47  SER B CA  1 
ATOM   1675 C  C   . SER B 1 50  ? -4.052  -14.401 -2.661  1.00 25.01 ? 47  SER B C   1 
ATOM   1676 O  O   . SER B 1 50  ? -3.689  -13.440 -3.341  1.00 25.54 ? 47  SER B O   1 
ATOM   1677 C  CB  . SER B 1 50  ? -2.348  -16.229 -2.647  1.00 26.64 ? 47  SER B CB  1 
ATOM   1678 O  OG  . SER B 1 50  ? -2.168  -17.640 -2.651  1.00 27.09 ? 47  SER B OG  1 
ATOM   1679 N  N   . ALA B 1 51  ? -4.698  -14.274 -1.497  1.00 23.11 ? 48  ALA B N   1 
ATOM   1680 C  CA  . ALA B 1 51  ? -4.975  -12.974 -0.912  1.00 23.28 ? 48  ALA B CA  1 
ATOM   1681 C  C   . ALA B 1 51  ? -4.802  -13.040 0.603   1.00 22.59 ? 48  ALA B C   1 
ATOM   1682 O  O   . ALA B 1 51  ? -5.111  -14.059 1.221   1.00 23.61 ? 48  ALA B O   1 
ATOM   1683 C  CB  . ALA B 1 51  ? -6.375  -12.541 -1.281  1.00 24.17 ? 48  ALA B CB  1 
ATOM   1684 N  N   . GLY B 1 52  ? -4.295  -11.947 1.187   1.00 21.54 ? 49  GLY B N   1 
ATOM   1685 C  CA  . GLY B 1 52  ? -4.397  -11.738 2.620   1.00 20.39 ? 49  GLY B CA  1 
ATOM   1686 C  C   . GLY B 1 52  ? -5.788  -11.212 2.975   1.00 20.86 ? 49  GLY B C   1 
ATOM   1687 O  O   . GLY B 1 52  ? -6.357  -10.405 2.234   1.00 20.98 ? 49  GLY B O   1 
ATOM   1688 N  N   . ILE B 1 53  ? -6.326  -11.690 4.103   1.00 21.13 ? 50  ILE B N   1 
ATOM   1689 C  CA  . ILE B 1 53  ? -7.583  -11.210 4.653   1.00 21.76 ? 50  ILE B CA  1 
ATOM   1690 C  C   . ILE B 1 53  ? -7.256  -10.214 5.758   1.00 22.26 ? 50  ILE B C   1 
ATOM   1691 O  O   . ILE B 1 53  ? -6.492  -10.533 6.668   1.00 23.58 ? 50  ILE B O   1 
ATOM   1692 C  CB  . ILE B 1 53  ? -8.454  -12.362 5.192   1.00 21.49 ? 50  ILE B CB  1 
ATOM   1693 C  CG1 . ILE B 1 53  ? -8.630  -13.481 4.161   1.00 21.71 ? 50  ILE B CG1 1 
ATOM   1694 C  CG2 . ILE B 1 53  ? -9.796  -11.832 5.700   1.00 21.68 ? 50  ILE B CG2 1 
ATOM   1695 C  CD1 . ILE B 1 53  ? -9.509  -14.627 4.627   1.00 22.27 ? 50  ILE B CD1 1 
ATOM   1696 N  N   . TYR B 1 54  ? -7.852  -9.020  5.660   1.00 22.47 ? 51  TYR B N   1 
ATOM   1697 C  CA  . TYR B 1 54  ? -7.581  -7.921  6.570   1.00 23.47 ? 51  TYR B CA  1 
ATOM   1698 C  C   . TYR B 1 54  ? -8.850  -7.490  7.296   1.00 23.63 ? 51  TYR B C   1 
ATOM   1699 O  O   . TYR B 1 54  ? -9.944  -7.594  6.751   1.00 23.54 ? 51  TYR B O   1 
ATOM   1700 C  CB  . TYR B 1 54  ? -7.023  -6.737  5.778   1.00 23.60 ? 51  TYR B CB  1 
ATOM   1701 C  CG  . TYR B 1 54  ? -5.598  -6.987  5.314   1.00 24.21 ? 51  TYR B CG  1 
ATOM   1702 C  CD1 . TYR B 1 54  ? -5.344  -7.775  4.201   1.00 25.21 ? 51  TYR B CD1 1 
ATOM   1703 C  CD2 . TYR B 1 54  ? -4.515  -6.454  5.999   1.00 24.78 ? 51  TYR B CD2 1 
ATOM   1704 C  CE1 . TYR B 1 54  ? -4.049  -8.040  3.789   1.00 24.69 ? 51  TYR B CE1 1 
ATOM   1705 C  CE2 . TYR B 1 54  ? -3.215  -6.699  5.589   1.00 25.42 ? 51  TYR B CE2 1 
ATOM   1706 C  CZ  . TYR B 1 54  ? -2.980  -7.497  4.482   1.00 25.44 ? 51  TYR B CZ  1 
ATOM   1707 O  OH  . TYR B 1 54  ? -1.698  -7.741  4.076   1.00 25.76 ? 51  TYR B OH  1 
ATOM   1708 N  N   . ASP B 1 55  ? -8.671  -7.034  8.543   1.00 24.37 ? 52  ASP B N   1 
ATOM   1709 C  CA  . ASP B 1 55  ? -9.636  -6.183  9.217   1.00 25.60 ? 52  ASP B CA  1 
ATOM   1710 C  C   . ASP B 1 55  ? -8.962  -4.830  9.402   1.00 26.07 ? 52  ASP B C   1 
ATOM   1711 O  O   . ASP B 1 55  ? -8.146  -4.664  10.309  1.00 27.21 ? 52  ASP B O   1 
ATOM   1712 C  CB  . ASP B 1 55  ? -10.101 -6.756  10.547  1.00 26.72 ? 52  ASP B CB  1 
ATOM   1713 C  CG  . ASP B 1 55  ? -11.113 -5.901  11.301  1.00 28.21 ? 52  ASP B CG  1 
ATOM   1714 O  OD1 . ASP B 1 55  ? -11.515 -4.856  10.754  1.00 28.83 ? 52  ASP B OD1 1 
ATOM   1715 O  OD2 . ASP B 1 55  ? -11.491 -6.286  12.428  1.00 30.00 ? 52  ASP B OD2 1 
ATOM   1716 N  N   . GLY B 1 56  ? -9.294  -3.888  8.513   1.00 26.17 ? 53  GLY B N   1 
ATOM   1717 C  CA  . GLY B 1 56  ? -8.574  -2.634  8.427   1.00 26.53 ? 53  GLY B CA  1 
ATOM   1718 C  C   . GLY B 1 56  ? -7.119  -2.900  8.054   1.00 26.97 ? 53  GLY B C   1 
ATOM   1719 O  O   . GLY B 1 56  ? -6.845  -3.488  7.010   1.00 25.80 ? 53  GLY B O   1 
ATOM   1720 N  N   . ASN B 1 57  ? -6.202  -2.519  8.948   1.00 29.26 ? 54  ASN B N   1 
ATOM   1721 C  CA  . ASN B 1 57  ? -4.776  -2.628  8.685   1.00 30.02 ? 54  ASN B CA  1 
ATOM   1722 C  C   . ASN B 1 57  ? -4.203  -3.917  9.272   1.00 30.05 ? 54  ASN B C   1 
ATOM   1723 O  O   . ASN B 1 57  ? -3.004  -4.148  9.152   1.00 30.94 ? 54  ASN B O   1 
ATOM   1724 C  CB  . ASN B 1 57  ? -4.024  -1.418  9.224   1.00 32.38 ? 54  ASN B CB  1 
ATOM   1725 C  CG  . ASN B 1 57  ? -4.648  -0.127  8.753   1.00 33.94 ? 54  ASN B CG  1 
ATOM   1726 O  OD1 . ASN B 1 57  ? -4.853  0.051   7.547   1.00 37.19 ? 54  ASN B OD1 1 
ATOM   1727 N  ND2 . ASN B 1 57  ? -4.987  0.764   9.674   1.00 36.62 ? 54  ASN B ND2 1 
ATOM   1728 N  N   . GLN B 1 58  ? -5.048  -4.747  9.901   1.00 28.79 ? 55  GLN B N   1 
ATOM   1729 C  CA  . GLN B 1 58  ? -4.585  -5.965  10.552  1.00 28.36 ? 55  GLN B CA  1 
ATOM   1730 C  C   . GLN B 1 58  ? -4.806  -7.165  9.633   1.00 26.68 ? 55  GLN B C   1 
ATOM   1731 O  O   . GLN B 1 58  ? -5.941  -7.475  9.269   1.00 26.18 ? 55  GLN B O   1 
ATOM   1732 C  CB  . GLN B 1 58  ? -5.312  -6.153  11.885  1.00 30.17 ? 55  GLN B CB  1 
ATOM   1733 C  CG  . GLN B 1 58  ? -5.026  -7.474  12.593  1.00 31.91 ? 55  GLN B CG  1 
ATOM   1734 C  CD  . GLN B 1 58  ? -3.596  -7.610  13.072  1.00 32.87 ? 55  GLN B CD  1 
ATOM   1735 O  OE1 . GLN B 1 58  ? -3.113  -6.821  13.891  1.00 35.47 ? 55  GLN B OE1 1 
ATOM   1736 N  NE2 . GLN B 1 58  ? -2.905  -8.630  12.581  1.00 33.26 ? 55  GLN B NE2 1 
ATOM   1737 N  N   . LEU B 1 59  ? -3.712  -7.847  9.276   1.00 26.13 ? 56  LEU B N   1 
ATOM   1738 C  CA  . LEU B 1 59  ? -3.810  -9.124  8.589   1.00 25.15 ? 56  LEU B CA  1 
ATOM   1739 C  C   . LEU B 1 59  ? -4.404  -10.144 9.556   1.00 25.64 ? 56  LEU B C   1 
ATOM   1740 O  O   . LEU B 1 59  ? -3.838  -10.371 10.627  1.00 26.19 ? 56  LEU B O   1 
ATOM   1741 C  CB  . LEU B 1 59  ? -2.435  -9.570  8.101   1.00 25.20 ? 56  LEU B CB  1 
ATOM   1742 C  CG  . LEU B 1 59  ? -2.394  -10.913 7.364   1.00 24.06 ? 56  LEU B CG  1 
ATOM   1743 C  CD1 . LEU B 1 59  ? -2.967  -10.800 5.963   1.00 23.26 ? 56  LEU B CD1 1 
ATOM   1744 C  CD2 . LEU B 1 59  ? -0.977  -11.455 7.322   1.00 24.49 ? 56  LEU B CD2 1 
ATOM   1745 N  N   . ILE B 1 60  ? -5.526  -10.767 9.159   1.00 24.70 ? 57  ILE B N   1 
ATOM   1746 C  CA  . ILE B 1 60  ? -6.222  -11.709 10.026  1.00 25.33 ? 57  ILE B CA  1 
ATOM   1747 C  C   . ILE B 1 60  ? -6.306  -13.109 9.418   1.00 24.26 ? 57  ILE B C   1 
ATOM   1748 O  O   . ILE B 1 60  ? -6.733  -14.026 10.113  1.00 25.63 ? 57  ILE B O   1 
ATOM   1749 C  CB  . ILE B 1 60  ? -7.637  -11.212 10.373  1.00 27.12 ? 57  ILE B CB  1 
ATOM   1750 C  CG1 . ILE B 1 60  ? -8.529  -11.087 9.130   1.00 28.42 ? 57  ILE B CG1 1 
ATOM   1751 C  CG2 . ILE B 1 60  ? -7.570  -9.911  11.168  1.00 27.30 ? 57  ILE B CG2 1 
ATOM   1752 C  CD1 . ILE B 1 60  ? -10.010 -10.951 9.436   1.00 29.46 ? 57  ILE B CD1 1 
ATOM   1753 N  N   . GLY B 1 61  ? -5.968  -13.276 8.134   1.00 22.54 ? 58  GLY B N   1 
ATOM   1754 C  CA  . GLY B 1 61  ? -6.138  -14.573 7.502   1.00 22.06 ? 58  GLY B CA  1 
ATOM   1755 C  C   . GLY B 1 61  ? -5.650  -14.598 6.059   1.00 21.31 ? 58  GLY B C   1 
ATOM   1756 O  O   . GLY B 1 61  ? -5.043  -13.646 5.573   1.00 23.47 ? 58  GLY B O   1 
ATOM   1757 N  N   . TYR B 1 62  ? -5.887  -15.742 5.414   1.00 21.08 ? 59  TYR B N   1 
ATOM   1758 C  CA  . TYR B 1 62  ? -5.375  -16.032 4.088   1.00 20.90 ? 59  TYR B CA  1 
ATOM   1759 C  C   . TYR B 1 62  ? -6.423  -16.809 3.299   1.00 20.29 ? 59  TYR B C   1 
ATOM   1760 O  O   . TYR B 1 62  ? -7.097  -17.695 3.836   1.00 19.85 ? 59  TYR B O   1 
ATOM   1761 C  CB  . TYR B 1 62  ? -4.080  -16.838 4.209   1.00 21.31 ? 59  TYR B CB  1 
ATOM   1762 C  CG  . TYR B 1 62  ? -3.639  -17.549 2.939   1.00 20.11 ? 59  TYR B CG  1 
ATOM   1763 C  CD1 . TYR B 1 62  ? -3.013  -16.863 1.904   1.00 20.63 ? 59  TYR B CD1 1 
ATOM   1764 C  CD2 . TYR B 1 62  ? -3.803  -18.921 2.796   1.00 20.82 ? 59  TYR B CD2 1 
ATOM   1765 C  CE1 . TYR B 1 62  ? -2.594  -17.517 0.755   1.00 21.56 ? 59  TYR B CE1 1 
ATOM   1766 C  CE2 . TYR B 1 62  ? -3.393  -19.582 1.651   1.00 20.83 ? 59  TYR B CE2 1 
ATOM   1767 C  CZ  . TYR B 1 62  ? -2.778  -18.882 0.630   1.00 21.94 ? 59  TYR B CZ  1 
ATOM   1768 O  OH  . TYR B 1 62  ? -2.362  -19.557 -0.486  1.00 23.17 ? 59  TYR B OH  1 
ATOM   1769 N  N   . ALA B 1 63  ? -6.530  -16.484 2.009   1.00 20.39 ? 60  ALA B N   1 
ATOM   1770 C  CA  . ALA B 1 63  ? -7.373  -17.247 1.111   1.00 20.66 ? 60  ALA B CA  1 
ATOM   1771 C  C   . ALA B 1 63  ? -6.623  -17.567 -0.175  1.00 20.60 ? 60  ALA B C   1 
ATOM   1772 O  O   . ALA B 1 63  ? -5.715  -16.840 -0.579  1.00 21.20 ? 60  ALA B O   1 
ATOM   1773 C  CB  . ALA B 1 63  ? -8.657  -16.499 0.822   1.00 21.19 ? 60  ALA B CB  1 
ATOM   1774 N  N   A MET B 1 64  ? -7.004  -18.690 -0.786  0.75 21.08 ? 61  MET B N   1 
ATOM   1775 N  N   B MET B 1 64  ? -7.012  -18.688 -0.792  0.25 20.88 ? 61  MET B N   1 
ATOM   1776 C  CA  A MET B 1 64  ? -6.547  -19.064 -2.111  0.75 21.80 ? 61  MET B CA  1 
ATOM   1777 C  CA  B MET B 1 64  ? -6.544  -19.066 -2.114  0.25 21.20 ? 61  MET B CA  1 
ATOM   1778 C  C   A MET B 1 64  ? -7.746  -19.622 -2.873  0.75 21.92 ? 61  MET B C   1 
ATOM   1779 C  C   B MET B 1 64  ? -7.731  -19.641 -2.883  0.25 21.76 ? 61  MET B C   1 
ATOM   1780 O  O   A MET B 1 64  ? -8.501  -20.428 -2.330  0.75 23.94 ? 61  MET B O   1 
ATOM   1781 O  O   B MET B 1 64  ? -8.461  -20.478 -2.356  0.25 22.49 ? 61  MET B O   1 
ATOM   1782 C  CB  A MET B 1 64  ? -5.424  -20.103 -2.038  0.75 22.32 ? 61  MET B CB  1 
ATOM   1783 C  CB  B MET B 1 64  ? -5.410  -20.094 -2.038  0.25 21.18 ? 61  MET B CB  1 
ATOM   1784 C  CG  A MET B 1 64  ? -4.845  -20.471 -3.382  0.75 23.15 ? 61  MET B CG  1 
ATOM   1785 C  CG  B MET B 1 64  ? -4.508  -20.098 -3.260  0.25 20.99 ? 61  MET B CG  1 
ATOM   1786 S  SD  A MET B 1 64  ? -3.430  -21.582 -3.246  0.75 25.12 ? 61  MET B SD  1 
ATOM   1787 S  SD  B MET B 1 64  ? -5.205  -20.946 -4.692  0.25 21.08 ? 61  MET B SD  1 
ATOM   1788 C  CE  A MET B 1 64  ? -3.444  -22.272 -4.906  0.75 26.29 ? 61  MET B CE  1 
ATOM   1789 C  CE  B MET B 1 64  ? -4.593  -22.613 -4.412  0.25 20.67 ? 61  MET B CE  1 
ATOM   1790 N  N   . TYR B 1 65  ? -7.912  -19.171 -4.123  1.00 22.26 ? 62  TYR B N   1 
ATOM   1791 C  CA  . TYR B 1 65  ? -9.086  -19.495 -4.921  1.00 23.50 ? 62  TYR B CA  1 
ATOM   1792 C  C   . TYR B 1 65  ? -8.690  -19.520 -6.393  1.00 24.92 ? 62  TYR B C   1 
ATOM   1793 O  O   . TYR B 1 65  ? -7.685  -18.926 -6.785  1.00 25.51 ? 62  TYR B O   1 
ATOM   1794 C  CB  . TYR B 1 65  ? -10.202 -18.473 -4.670  1.00 24.97 ? 62  TYR B CB  1 
ATOM   1795 C  CG  . TYR B 1 65  ? -9.700  -17.036 -4.610  1.00 26.01 ? 62  TYR B CG  1 
ATOM   1796 C  CD1 . TYR B 1 65  ? -9.518  -16.280 -5.763  1.00 26.67 ? 62  TYR B CD1 1 
ATOM   1797 C  CD2 . TYR B 1 65  ? -9.378  -16.447 -3.394  1.00 26.89 ? 62  TYR B CD2 1 
ATOM   1798 C  CE1 . TYR B 1 65  ? -9.040  -14.980 -5.707  1.00 27.73 ? 62  TYR B CE1 1 
ATOM   1799 C  CE2 . TYR B 1 65  ? -8.903  -15.148 -3.322  1.00 28.37 ? 62  TYR B CE2 1 
ATOM   1800 C  CZ  . TYR B 1 65  ? -8.727  -14.415 -4.481  1.00 28.50 ? 62  TYR B CZ  1 
ATOM   1801 O  OH  . TYR B 1 65  ? -8.257  -13.137 -4.385  1.00 31.63 ? 62  TYR B OH  1 
ATOM   1802 N  N   . GLY B 1 66  ? -9.497  -20.197 -7.214  1.00 27.04 ? 63  GLY B N   1 
ATOM   1803 C  CA  . GLY B 1 66  ? -9.138  -20.344 -8.613  1.00 29.34 ? 63  GLY B CA  1 
ATOM   1804 C  C   . GLY B 1 66  ? -10.256 -20.968 -9.439  1.00 30.08 ? 63  GLY B C   1 
ATOM   1805 O  O   . GLY B 1 66  ? -11.020 -21.793 -8.947  1.00 29.29 ? 63  GLY B O   1 
ATOM   1806 N  N   . ARG B 1 67  ? -10.329 -20.537 -10.703 1.00 33.47 ? 64  ARG B N   1 
ATOM   1807 C  CA  . ARG B 1 67  ? -11.187 -21.150 -11.700 1.00 37.03 ? 64  ARG B CA  1 
ATOM   1808 C  C   . ARG B 1 67  ? -10.297 -21.974 -12.622 1.00 41.00 ? 64  ARG B C   1 
ATOM   1809 O  O   . ARG B 1 67  ? -9.526  -21.415 -13.400 1.00 42.79 ? 64  ARG B O   1 
ATOM   1810 C  CB  . ARG B 1 67  ? -11.942 -20.072 -12.485 1.00 38.44 ? 64  ARG B CB  1 
ATOM   1811 C  CG  . ARG B 1 67  ? -12.877 -20.608 -13.562 1.00 38.92 ? 64  ARG B CG  1 
ATOM   1812 C  CD  . ARG B 1 67  ? -13.058 -19.611 -14.702 1.00 40.01 ? 64  ARG B CD  1 
ATOM   1813 N  NE  . ARG B 1 67  ? -13.550 -20.219 -15.944 1.00 41.38 ? 64  ARG B NE  1 
ATOM   1814 C  CZ  . ARG B 1 67  ? -12.898 -21.106 -16.697 1.00 42.93 ? 64  ARG B CZ  1 
ATOM   1815 N  NH1 . ARG B 1 67  ? -11.698 -21.539 -16.349 1.00 43.59 ? 64  ARG B NH1 1 
ATOM   1816 N  NH2 . ARG B 1 67  ? -13.459 -21.575 -17.799 1.00 44.96 ? 64  ARG B NH2 1 
ATOM   1817 N  N   . TRP B 1 68  ? -10.396 -23.302 -12.505 1.00 44.05 ? 65  TRP B N   1 
ATOM   1818 C  CA  . TRP B 1 68  ? -9.499  -24.202 -13.212 1.00 47.77 ? 65  TRP B CA  1 
ATOM   1819 C  C   . TRP B 1 68  ? -10.023 -24.459 -14.621 1.00 50.99 ? 65  TRP B C   1 
ATOM   1820 O  O   . TRP B 1 68  ? -11.068 -23.933 -15.005 1.00 52.37 ? 65  TRP B O   1 
ATOM   1821 C  CB  . TRP B 1 68  ? -9.330  -25.500 -12.413 1.00 48.60 ? 65  TRP B CB  1 
ATOM   1822 C  CG  . TRP B 1 68  ? -8.875  -25.254 -11.001 1.00 48.59 ? 65  TRP B CG  1 
ATOM   1823 C  CD1 . TRP B 1 68  ? -8.143  -24.194 -10.551 1.00 48.36 ? 65  TRP B CD1 1 
ATOM   1824 C  CD2 . TRP B 1 68  ? -9.133  -26.085 -9.851  1.00 48.65 ? 65  TRP B CD2 1 
ATOM   1825 N  NE1 . TRP B 1 68  ? -7.929  -24.304 -9.204  1.00 47.90 ? 65  TRP B NE1 1 
ATOM   1826 C  CE2 . TRP B 1 68  ? -8.518  -25.451 -8.750  1.00 47.60 ? 65  TRP B CE2 1 
ATOM   1827 C  CE3 . TRP B 1 68  ? -9.816  -27.290 -9.645  1.00 48.71 ? 65  TRP B CE3 1 
ATOM   1828 C  CZ2 . TRP B 1 68  ? -8.566  -25.980 -7.467  1.00 46.22 ? 65  TRP B CZ2 1 
ATOM   1829 C  CZ3 . TRP B 1 68  ? -9.867  -27.811 -8.372  1.00 47.66 ? 65  TRP B CZ3 1 
ATOM   1830 C  CH2 . TRP B 1 68  ? -9.247  -27.161 -7.302  1.00 46.85 ? 65  TRP B CH2 1 
ATOM   1831 N  N   . GLN B 1 69  ? -9.283  -25.275 -15.383 1.00 52.88 ? 66  GLN B N   1 
ATOM   1832 C  CA  . GLN B 1 69  ? -9.578  -25.498 -16.790 0.41 54.17 ? 66  GLN B CA  1 
ATOM   1833 C  C   . GLN B 1 69  ? -10.970 -26.114 -16.938 0.78 54.64 ? 66  GLN B C   1 
ATOM   1834 O  O   . GLN B 1 69  ? -11.594 -25.971 -17.988 0.54 55.75 ? 66  GLN B O   1 
ATOM   1835 C  CB  . GLN B 1 69  ? -8.492  -26.341 -17.467 0.51 55.17 ? 66  GLN B CB  1 
ATOM   1836 C  CG  . GLN B 1 69  ? -8.905  -27.756 -17.867 0.65 55.83 ? 66  GLN B CG  1 
ATOM   1837 C  CD  . GLN B 1 69  ? -9.137  -28.693 -16.702 0.77 56.33 ? 66  GLN B CD  1 
ATOM   1838 O  OE1 . GLN B 1 69  ? -8.803  -28.392 -15.550 0.79 56.59 ? 66  GLN B OE1 1 
ATOM   1839 N  NE2 . GLN B 1 69  ? -9.703  -29.854 -16.998 0.84 56.96 ? 66  GLN B NE2 1 
ATOM   1840 N  N   . ASP B 1 70  ? -11.446 -26.797 -15.887 1.00 53.74 ? 67  ASP B N   1 
ATOM   1841 C  CA  . ASP B 1 70  ? -12.732 -27.475 -15.923 1.00 52.36 ? 67  ASP B CA  1 
ATOM   1842 C  C   . ASP B 1 70  ? -13.862 -26.450 -16.041 1.00 49.35 ? 67  ASP B C   1 
ATOM   1843 O  O   . ASP B 1 70  ? -14.878 -26.732 -16.672 1.00 48.85 ? 67  ASP B O   1 
ATOM   1844 C  CB  . ASP B 1 70  ? -12.879 -28.443 -14.755 1.00 53.47 ? 67  ASP B CB  1 
ATOM   1845 C  CG  . ASP B 1 70  ? -13.331 -27.849 -13.428 1.00 54.39 ? 67  ASP B CG  1 
ATOM   1846 O  OD1 . ASP B 1 70  ? -14.523 -27.496 -13.325 1.00 55.90 ? 67  ASP B OD1 1 
ATOM   1847 O  OD2 . ASP B 1 70  ? -12.492 -27.751 -12.508 1.00 54.70 ? 67  ASP B OD2 1 
ATOM   1848 N  N   . GLY B 1 71  ? -13.682 -25.268 -15.433 1.00 46.42 ? 68  GLY B N   1 
ATOM   1849 C  CA  . GLY B 1 71  ? -14.649 -24.185 -15.541 1.00 42.74 ? 68  GLY B CA  1 
ATOM   1850 C  C   . GLY B 1 71  ? -15.267 -23.804 -14.195 1.00 39.62 ? 68  GLY B C   1 
ATOM   1851 O  O   . GLY B 1 71  ? -15.970 -22.799 -14.107 1.00 38.22 ? 68  GLY B O   1 
ATOM   1852 N  N   . ARG B 1 72  ? -15.009 -24.612 -13.158 1.00 36.05 ? 69  ARG B N   1 
ATOM   1853 C  CA  . ARG B 1 72  ? -15.560 -24.374 -11.834 1.00 34.28 ? 69  ARG B CA  1 
ATOM   1854 C  C   . ARG B 1 72  ? -14.635 -23.470 -11.027 1.00 32.51 ? 69  ARG B C   1 
ATOM   1855 O  O   . ARG B 1 72  ? -13.415 -23.568 -11.128 1.00 32.49 ? 69  ARG B O   1 
ATOM   1856 C  CB  . ARG B 1 72  ? -15.733 -25.675 -11.048 1.00 35.06 ? 69  ARG B CB  1 
ATOM   1857 C  CG  . ARG B 1 72  ? -16.874 -26.547 -11.542 1.00 35.56 ? 69  ARG B CG  1 
ATOM   1858 C  CD  . ARG B 1 72  ? -16.868 -27.838 -10.760 1.00 36.26 ? 69  ARG B CD  1 
ATOM   1859 N  NE  . ARG B 1 72  ? -17.908 -28.772 -11.194 1.00 37.00 ? 69  ARG B NE  1 
ATOM   1860 C  CZ  . ARG B 1 72  ? -18.167 -29.924 -10.592 1.00 37.14 ? 69  ARG B CZ  1 
ATOM   1861 N  NH1 . ARG B 1 72  ? -17.464 -30.292 -9.533  1.00 37.56 ? 69  ARG B NH1 1 
ATOM   1862 N  NH2 . ARG B 1 72  ? -19.130 -30.704 -11.049 1.00 37.58 ? 69  ARG B NH2 1 
ATOM   1863 N  N   . VAL B 1 73  ? -15.249 -22.628 -10.191 1.00 30.41 ? 70  VAL B N   1 
ATOM   1864 C  CA  . VAL B 1 73  ? -14.530 -21.704 -9.333  1.00 28.83 ? 70  VAL B CA  1 
ATOM   1865 C  C   . VAL B 1 73  ? -14.481 -22.303 -7.934  1.00 26.72 ? 70  VAL B C   1 
ATOM   1866 O  O   . VAL B 1 73  ? -15.527 -22.575 -7.346  1.00 26.21 ? 70  VAL B O   1 
ATOM   1867 C  CB  . VAL B 1 73  ? -15.216 -20.326 -9.336  1.00 29.25 ? 70  VAL B CB  1 
ATOM   1868 C  CG1 . VAL B 1 73  ? -14.500 -19.326 -8.434  1.00 29.92 ? 70  VAL B CG1 1 
ATOM   1869 C  CG2 . VAL B 1 73  ? -15.346 -19.777 -10.749 1.00 30.32 ? 70  VAL B CG2 1 
ATOM   1870 N  N   . TRP B 1 74  ? -13.256 -22.483 -7.424  1.00 25.19 ? 71  TRP B N   1 
ATOM   1871 C  CA  . TRP B 1 74  ? -13.021 -23.146 -6.157  1.00 24.33 ? 71  TRP B CA  1 
ATOM   1872 C  C   . TRP B 1 74  ? -12.507 -22.179 -5.093  1.00 23.41 ? 71  TRP B C   1 
ATOM   1873 O  O   . TRP B 1 74  ? -11.753 -21.253 -5.390  1.00 24.73 ? 71  TRP B O   1 
ATOM   1874 C  CB  . TRP B 1 74  ? -12.003 -24.274 -6.361  1.00 24.13 ? 71  TRP B CB  1 
ATOM   1875 C  CG  . TRP B 1 74  ? -12.547 -25.477 -7.082  1.00 25.40 ? 71  TRP B CG  1 
ATOM   1876 C  CD1 . TRP B 1 74  ? -12.666 -25.667 -8.429  1.00 26.34 ? 71  TRP B CD1 1 
ATOM   1877 C  CD2 . TRP B 1 74  ? -13.027 -26.687 -6.460  1.00 25.23 ? 71  TRP B CD2 1 
ATOM   1878 N  NE1 . TRP B 1 74  ? -13.190 -26.907 -8.686  1.00 27.18 ? 71  TRP B NE1 1 
ATOM   1879 C  CE2 . TRP B 1 74  ? -13.426 -27.554 -7.500  1.00 26.29 ? 71  TRP B CE2 1 
ATOM   1880 C  CE3 . TRP B 1 74  ? -13.163 -27.113 -5.134  1.00 25.74 ? 71  TRP B CE3 1 
ATOM   1881 C  CZ2 . TRP B 1 74  ? -13.949 -28.820 -7.248  1.00 26.50 ? 71  TRP B CZ2 1 
ATOM   1882 C  CZ3 . TRP B 1 74  ? -13.680 -28.367 -4.887  1.00 26.93 ? 71  TRP B CZ3 1 
ATOM   1883 C  CH2 . TRP B 1 74  ? -14.061 -29.209 -5.931  1.00 26.76 ? 71  TRP B CH2 1 
ATOM   1884 N  N   . LEU B 1 75  ? -12.909 -22.449 -3.846  1.00 23.56 ? 72  LEU B N   1 
ATOM   1885 C  CA  . LEU B 1 75  ? -12.251 -21.928 -2.660  1.00 23.97 ? 72  LEU B CA  1 
ATOM   1886 C  C   . LEU B 1 75  ? -11.266 -22.991 -2.176  1.00 23.45 ? 72  LEU B C   1 
ATOM   1887 O  O   . LEU B 1 75  ? -11.682 -24.014 -1.644  1.00 24.42 ? 72  LEU B O   1 
ATOM   1888 C  CB  . LEU B 1 75  ? -13.309 -21.614 -1.604  1.00 26.01 ? 72  LEU B CB  1 
ATOM   1889 C  CG  . LEU B 1 75  ? -12.813 -21.091 -0.251  1.00 28.46 ? 72  LEU B CG  1 
ATOM   1890 C  CD1 . LEU B 1 75  ? -11.983 -19.819 -0.391  1.00 29.62 ? 72  LEU B CD1 1 
ATOM   1891 C  CD2 . LEU B 1 75  ? -14.005 -20.848 0.672   1.00 30.69 ? 72  LEU B CD2 1 
ATOM   1892 N  N   . ASP B 1 76  ? -9.968  -22.737 -2.378  1.00 22.66 ? 73  ASP B N   1 
ATOM   1893 C  CA  . ASP B 1 76  ? -8.934  -23.760 -2.270  1.00 22.56 ? 73  ASP B CA  1 
ATOM   1894 C  C   . ASP B 1 76  ? -8.311  -23.805 -0.876  1.00 21.17 ? 73  ASP B C   1 
ATOM   1895 O  O   . ASP B 1 76  ? -7.970  -24.879 -0.375  1.00 22.43 ? 73  ASP B O   1 
ATOM   1896 C  CB  . ASP B 1 76  ? -7.864  -23.552 -3.327  1.00 22.93 ? 73  ASP B CB  1 
ATOM   1897 C  CG  . ASP B 1 76  ? -8.376  -23.638 -4.754  1.00 24.36 ? 73  ASP B CG  1 
ATOM   1898 O  OD1 . ASP B 1 76  ? -9.200  -24.537 -5.011  1.00 25.16 ? 73  ASP B OD1 1 
ATOM   1899 O  OD2 . ASP B 1 76  ? -7.969  -22.797 -5.580  1.00 26.66 ? 73  ASP B OD2 1 
ATOM   1900 N  N   . ARG B 1 77  ? -8.104  -22.626 -0.286  1.00 20.80 ? 74  ARG B N   1 
ATOM   1901 C  CA  . ARG B 1 77  ? -7.482  -22.510 1.020   1.00 20.32 ? 74  ARG B CA  1 
ATOM   1902 C  C   . ARG B 1 77  ? -8.145  -21.339 1.738   1.00 20.89 ? 74  ARG B C   1 
ATOM   1903 O  O   . ARG B 1 77  ? -8.461  -20.336 1.109   1.00 20.62 ? 74  ARG B O   1 
ATOM   1904 C  CB  . ARG B 1 77  ? -5.971  -22.280 0.871   1.00 20.10 ? 74  ARG B CB  1 
ATOM   1905 C  CG  . ARG B 1 77  ? -5.197  -23.348 0.103   1.00 20.76 ? 74  ARG B CG  1 
ATOM   1906 C  CD  . ARG B 1 77  ? -3.709  -23.028 0.041   1.00 21.03 ? 74  ARG B CD  1 
ATOM   1907 N  NE  . ARG B 1 77  ? -2.881  -24.037 -0.629  1.00 21.52 ? 74  ARG B NE  1 
ATOM   1908 C  CZ  . ARG B 1 77  ? -2.463  -25.204 -0.136  1.00 22.05 ? 74  ARG B CZ  1 
ATOM   1909 N  NH1 . ARG B 1 77  ? -2.752  -25.587 1.097   1.00 22.62 ? 74  ARG B NH1 1 
ATOM   1910 N  NH2 . ARG B 1 77  ? -1.729  -26.006 -0.888  1.00 22.47 ? 74  ARG B NH2 1 
ATOM   1911 N  N   . PHE B 1 78  ? -8.403  -21.506 3.039   1.00 21.75 ? 75  PHE B N   1 
ATOM   1912 C  CA  . PHE B 1 78  ? -9.044  -20.478 3.838   1.00 22.57 ? 75  PHE B CA  1 
ATOM   1913 C  C   . PHE B 1 78  ? -8.639  -20.673 5.295   1.00 23.35 ? 75  PHE B C   1 
ATOM   1914 O  O   . PHE B 1 78  ? -8.930  -21.709 5.888   1.00 25.89 ? 75  PHE B O   1 
ATOM   1915 C  CB  . PHE B 1 78  ? -10.563 -20.530 3.654   1.00 23.10 ? 75  PHE B CB  1 
ATOM   1916 C  CG  . PHE B 1 78  ? -11.271 -19.379 4.350   1.00 24.56 ? 75  PHE B CG  1 
ATOM   1917 C  CD1 . PHE B 1 78  ? -11.392 -18.141 3.729   1.00 24.55 ? 75  PHE B CD1 1 
ATOM   1918 C  CD2 . PHE B 1 78  ? -11.795 -19.531 5.631   1.00 26.32 ? 75  PHE B CD2 1 
ATOM   1919 C  CE1 . PHE B 1 78  ? -12.021 -17.086 4.368   1.00 24.93 ? 75  PHE B CE1 1 
ATOM   1920 C  CE2 . PHE B 1 78  ? -12.428 -18.473 6.265   1.00 27.22 ? 75  PHE B CE2 1 
ATOM   1921 C  CZ  . PHE B 1 78  ? -12.540 -17.254 5.634   1.00 25.33 ? 75  PHE B CZ  1 
ATOM   1922 N  N   . LEU B 1 79  ? -7.950  -19.669 5.846   1.00 23.04 ? 76  LEU B N   1 
ATOM   1923 C  CA  . LEU B 1 79  ? -7.381  -19.739 7.182   1.00 24.66 ? 76  LEU B CA  1 
ATOM   1924 C  C   . LEU B 1 79  ? -7.619  -18.414 7.893   1.00 24.43 ? 76  LEU B C   1 
ATOM   1925 O  O   . LEU B 1 79  ? -7.417  -17.353 7.306   1.00 25.35 ? 76  LEU B O   1 
ATOM   1926 C  CB  . LEU B 1 79  ? -5.879  -20.017 7.143   1.00 26.40 ? 76  LEU B CB  1 
ATOM   1927 C  CG  . LEU B 1 79  ? -5.436  -21.373 6.593   1.00 27.53 ? 76  LEU B CG  1 
ATOM   1928 C  CD1 . LEU B 1 79  ? -3.928  -21.331 6.427   1.00 27.87 ? 76  LEU B CD1 1 
ATOM   1929 C  CD2 . LEU B 1 79  ? -5.846  -22.532 7.489   1.00 28.10 ? 76  LEU B CD2 1 
ATOM   1930 N  N   . ILE B 1 80  ? -8.000  -18.503 9.169   1.00 24.80 ? 77  ILE B N   1 
ATOM   1931 C  CA  . ILE B 1 80  ? -8.056  -17.347 10.046  1.00 25.01 ? 77  ILE B CA  1 
ATOM   1932 C  C   . ILE B 1 80  ? -6.994  -17.537 11.122  1.00 25.10 ? 77  ILE B C   1 
ATOM   1933 O  O   . ILE B 1 80  ? -6.934  -18.583 11.760  1.00 24.84 ? 77  ILE B O   1 
ATOM   1934 C  CB  . ILE B 1 80  ? -9.465  -17.173 10.643  1.00 25.56 ? 77  ILE B CB  1 
ATOM   1935 C  CG1 . ILE B 1 80  ? -10.511 -16.952 9.546   1.00 25.95 ? 77  ILE B CG1 1 
ATOM   1936 C  CG2 . ILE B 1 80  ? -9.488  -16.060 11.692  1.00 25.56 ? 77  ILE B CG2 1 
ATOM   1937 C  CD1 . ILE B 1 80  ? -10.358 -15.653 8.772   1.00 25.59 ? 77  ILE B CD1 1 
ATOM   1938 N  N   . ASP B 1 81  ? -6.165  -16.508 11.303  1.00 26.24 ? 78  ASP B N   1 
ATOM   1939 C  CA  . ASP B 1 81  ? -5.138  -16.490 12.328  1.00 27.30 ? 78  ASP B CA  1 
ATOM   1940 C  C   . ASP B 1 81  ? -5.762  -16.864 13.672  1.00 28.85 ? 78  ASP B C   1 
ATOM   1941 O  O   . ASP B 1 81  ? -6.828  -16.368 14.032  1.00 28.88 ? 78  ASP B O   1 
ATOM   1942 C  CB  . ASP B 1 81  ? -4.458  -15.131 12.350  1.00 27.51 ? 78  ASP B CB  1 
ATOM   1943 C  CG  . ASP B 1 81  ? -3.212  -15.004 13.212  1.00 29.23 ? 78  ASP B CG  1 
ATOM   1944 O  OD1 . ASP B 1 81  ? -3.334  -15.139 14.447  1.00 31.40 ? 78  ASP B OD1 1 
ATOM   1945 O  OD2 . ASP B 1 81  ? -2.134  -14.746 12.638  1.00 30.53 ? 78  ASP B OD2 1 
ATOM   1946 N  N   A GLN B 1 82  ? -5.083  -17.743 14.412  0.70 30.17 ? 79  GLN B N   1 
ATOM   1947 N  N   B GLN B 1 82  ? -5.053  -17.736 14.403  0.30 30.38 ? 79  GLN B N   1 
ATOM   1948 C  CA  A GLN B 1 82  ? -5.601  -18.285 15.658  0.70 31.99 ? 79  GLN B CA  1 
ATOM   1949 C  CA  B GLN B 1 82  ? -5.499  -18.284 15.675  0.30 32.29 ? 79  GLN B CA  1 
ATOM   1950 C  C   A GLN B 1 82  ? -5.793  -17.201 16.722  0.70 34.10 ? 79  GLN B C   1 
ATOM   1951 C  C   B GLN B 1 82  ? -5.823  -17.184 16.682  0.30 33.96 ? 79  GLN B C   1 
ATOM   1952 O  O   A GLN B 1 82  ? -6.529  -17.421 17.681  0.70 36.09 ? 79  GLN B O   1 
ATOM   1953 O  O   B GLN B 1 82  ? -6.675  -17.372 17.549  0.30 34.81 ? 79  GLN B O   1 
ATOM   1954 C  CB  A GLN B 1 82  ? -4.676  -19.402 16.140  0.70 32.24 ? 79  GLN B CB  1 
ATOM   1955 C  CB  B GLN B 1 82  ? -4.411  -19.198 16.235  0.30 32.66 ? 79  GLN B CB  1 
ATOM   1956 C  CG  A GLN B 1 82  ? -3.215  -18.982 16.275  0.70 32.20 ? 79  GLN B CG  1 
ATOM   1957 C  CG  B GLN B 1 82  ? -4.677  -20.680 16.002  0.30 32.86 ? 79  GLN B CG  1 
ATOM   1958 C  CD  A GLN B 1 82  ? -2.296  -20.142 16.580  0.70 32.72 ? 79  GLN B CD  1 
ATOM   1959 C  CD  B GLN B 1 82  ? -5.875  -21.169 16.783  0.30 33.49 ? 79  GLN B CD  1 
ATOM   1960 O  OE1 A GLN B 1 82  ? -2.701  -21.307 16.555  0.70 32.51 ? 79  GLN B OE1 1 
ATOM   1961 O  OE1 B GLN B 1 82  ? -6.897  -21.586 16.228  0.30 33.68 ? 79  GLN B OE1 1 
ATOM   1962 N  NE2 A GLN B 1 82  ? -1.041  -19.838 16.869  0.70 33.52 ? 79  GLN B NE2 1 
ATOM   1963 N  NE2 B GLN B 1 82  ? -5.764  -21.089 18.099  0.30 33.58 ? 79  GLN B NE2 1 
ATOM   1964 N  N   . ARG B 1 83  ? -5.135  -16.044 16.562  1.00 35.01 ? 80  ARG B N   1 
ATOM   1965 C  CA  . ARG B 1 83  ? -5.318  -14.927 17.479  1.00 37.02 ? 80  ARG B CA  1 
ATOM   1966 C  C   . ARG B 1 83  ? -6.732  -14.351 17.369  1.00 38.03 ? 80  ARG B C   1 
ATOM   1967 O  O   . ARG B 1 83  ? -7.275  -13.883 18.369  1.00 39.05 ? 80  ARG B O   1 
ATOM   1968 C  CB  . ARG B 1 83  ? -4.257  -13.846 17.233  1.00 38.55 ? 80  ARG B CB  1 
ATOM   1969 C  CG  . ARG B 1 83  ? -2.848  -14.236 17.658  1.00 39.85 ? 80  ARG B CG  1 
ATOM   1970 C  CD  . ARG B 1 83  ? -1.810  -13.242 17.158  1.00 41.19 ? 80  ARG B CD  1 
ATOM   1971 N  NE  . ARG B 1 83  ? -1.535  -13.413 15.727  1.00 42.74 ? 80  ARG B NE  1 
ATOM   1972 C  CZ  . ARG B 1 83  ? -0.965  -12.511 14.934  1.00 44.26 ? 80  ARG B CZ  1 
ATOM   1973 N  NH1 . ARG B 1 83  ? -0.644  -11.315 15.397  1.00 45.26 ? 80  ARG B NH1 1 
ATOM   1974 N  NH2 . ARG B 1 83  ? -0.733  -12.799 13.665  1.00 45.26 ? 80  ARG B NH2 1 
ATOM   1975 N  N   . PHE B 1 84  ? -7.327  -14.394 16.167  1.00 37.95 ? 81  PHE B N   1 
ATOM   1976 C  CA  . PHE B 1 84  ? -8.590  -13.715 15.909  1.00 39.31 ? 81  PHE B CA  1 
ATOM   1977 C  C   . PHE B 1 84  ? -9.704  -14.725 15.633  1.00 40.26 ? 81  PHE B C   1 
ATOM   1978 O  O   . PHE B 1 84  ? -10.667 -14.410 14.939  1.00 40.12 ? 81  PHE B O   1 
ATOM   1979 C  CB  . PHE B 1 84  ? -8.427  -12.747 14.732  1.00 39.50 ? 81  PHE B CB  1 
ATOM   1980 C  CG  . PHE B 1 84  ? -7.074  -12.050 14.676  1.00 38.91 ? 81  PHE B CG  1 
ATOM   1981 C  CD1 . PHE B 1 84  ? -6.724  -11.077 15.608  1.00 40.00 ? 81  PHE B CD1 1 
ATOM   1982 C  CD2 . PHE B 1 84  ? -6.162  -12.361 13.676  1.00 38.49 ? 81  PHE B CD2 1 
ATOM   1983 C  CE1 . PHE B 1 84  ? -5.486  -10.454 15.550  1.00 40.00 ? 81  PHE B CE1 1 
ATOM   1984 C  CE2 . PHE B 1 84  ? -4.926  -11.736 13.622  1.00 38.76 ? 81  PHE B CE2 1 
ATOM   1985 C  CZ  . PHE B 1 84  ? -4.590  -10.786 14.558  1.00 39.18 ? 81  PHE B CZ  1 
ATOM   1986 N  N   . GLN B 1 85  ? -9.582  -15.938 16.184  1.00 42.66 ? 82  GLN B N   1 
ATOM   1987 C  CA  . GLN B 1 85  ? -10.608 -16.951 15.998  1.00 44.67 ? 82  GLN B CA  1 
ATOM   1988 C  C   . GLN B 1 85  ? -11.724 -16.751 17.021  1.00 48.03 ? 82  GLN B C   1 
ATOM   1989 O  O   . GLN B 1 85  ? -11.495 -16.231 18.112  1.00 49.96 ? 82  GLN B O   1 
ATOM   1990 C  CB  . GLN B 1 85  ? -10.041 -18.370 16.059  1.00 45.77 ? 82  GLN B CB  1 
ATOM   1991 C  CG  . GLN B 1 85  ? -9.627  -18.919 14.697  1.00 46.29 ? 82  GLN B CG  1 
ATOM   1992 C  CD  . GLN B 1 85  ? -9.904  -20.399 14.556  1.00 48.15 ? 82  GLN B CD  1 
ATOM   1993 O  OE1 . GLN B 1 85  ? -10.961 -20.807 14.062  1.00 50.69 ? 82  GLN B OE1 1 
ATOM   1994 N  NE2 . GLN B 1 85  ? -8.975  -21.218 15.026  1.00 48.48 ? 82  GLN B NE2 1 
ATOM   1995 N  N   . GLY B 1 86  ? -12.938 -17.160 16.631  1.00 49.93 ? 83  GLY B N   1 
ATOM   1996 C  CA  . GLY B 1 86  ? -14.101 -17.133 17.504  1.00 51.31 ? 83  GLY B CA  1 
ATOM   1997 C  C   . GLY B 1 86  ? -14.668 -15.726 17.678  1.00 52.31 ? 83  GLY B C   1 
ATOM   1998 O  O   . GLY B 1 86  ? -15.254 -15.425 18.717  1.00 56.26 ? 83  GLY B O   1 
ATOM   1999 N  N   . GLN B 1 87  ? -14.499 -14.874 16.658  1.00 50.37 ? 84  GLN B N   1 
ATOM   2000 C  CA  . GLN B 1 87  ? -14.952 -13.492 16.723  1.00 49.21 ? 84  GLN B CA  1 
ATOM   2001 C  C   . GLN B 1 87  ? -15.776 -13.120 15.487  1.00 44.87 ? 84  GLN B C   1 
ATOM   2002 O  O   . GLN B 1 87  ? -16.069 -11.944 15.280  1.00 44.58 ? 84  GLN B O   1 
ATOM   2003 C  CB  . GLN B 1 87  ? -13.740 -12.577 16.907  1.00 50.49 ? 84  GLN B CB  1 
ATOM   2004 C  CG  . GLN B 1 87  ? -13.009 -12.783 18.231  1.00 52.51 ? 84  GLN B CG  1 
ATOM   2005 C  CD  . GLN B 1 87  ? -11.721 -11.994 18.345  1.00 53.85 ? 84  GLN B CD  1 
ATOM   2006 O  OE1 . GLN B 1 87  ? -11.325 -11.259 17.434  1.00 54.93 ? 84  GLN B OE1 1 
ATOM   2007 N  NE2 . GLN B 1 87  ? -11.049 -12.142 19.477  1.00 55.05 ? 84  GLN B NE2 1 
ATOM   2008 N  N   . GLY B 1 88  ? -16.157 -14.121 14.681  1.00 41.20 ? 85  GLY B N   1 
ATOM   2009 C  CA  . GLY B 1 88  ? -17.067 -13.924 13.562  1.00 39.13 ? 85  GLY B CA  1 
ATOM   2010 C  C   . GLY B 1 88  ? -16.355 -13.555 12.259  1.00 38.24 ? 85  GLY B C   1 
ATOM   2011 O  O   . GLY B 1 88  ? -17.019 -13.260 11.266  1.00 36.48 ? 85  GLY B O   1 
ATOM   2012 N  N   . TYR B 1 89  ? -15.015 -13.585 12.255  1.00 37.69 ? 86  TYR B N   1 
ATOM   2013 C  CA  . TYR B 1 89  ? -14.238 -13.199 11.084  1.00 37.37 ? 86  TYR B CA  1 
ATOM   2014 C  C   . TYR B 1 89  ? -14.340 -14.263 9.994   1.00 36.18 ? 86  TYR B C   1 
ATOM   2015 O  O   . TYR B 1 89  ? -14.254 -13.945 8.810   1.00 33.43 ? 86  TYR B O   1 
ATOM   2016 C  CB  . TYR B 1 89  ? -12.763 -12.977 11.422  1.00 38.07 ? 86  TYR B CB  1 
ATOM   2017 C  CG  . TYR B 1 89  ? -12.493 -11.727 12.244  1.00 38.73 ? 86  TYR B CG  1 
ATOM   2018 C  CD1 . TYR B 1 89  ? -12.533 -10.468 11.661  1.00 39.44 ? 86  TYR B CD1 1 
ATOM   2019 C  CD2 . TYR B 1 89  ? -12.185 -11.808 13.596  1.00 39.62 ? 86  TYR B CD2 1 
ATOM   2020 C  CE1 . TYR B 1 89  ? -12.287 -9.322  12.399  1.00 39.42 ? 86  TYR B CE1 1 
ATOM   2021 C  CE2 . TYR B 1 89  ? -11.929 -10.671 14.344  1.00 40.04 ? 86  TYR B CE2 1 
ATOM   2022 C  CZ  . TYR B 1 89  ? -11.984 -9.425  13.745  1.00 40.88 ? 86  TYR B CZ  1 
ATOM   2023 O  OH  . TYR B 1 89  ? -11.732 -8.307  14.484  1.00 42.61 ? 86  TYR B OH  1 
ATOM   2024 N  N   . GLY B 1 90  ? -14.500 -15.527 10.401  1.00 36.44 ? 87  GLY B N   1 
ATOM   2025 C  CA  . GLY B 1 90  ? -14.668 -16.621 9.460   1.00 36.19 ? 87  GLY B CA  1 
ATOM   2026 C  C   . GLY B 1 90  ? -15.863 -16.393 8.537   1.00 35.63 ? 87  GLY B C   1 
ATOM   2027 O  O   . GLY B 1 90  ? -15.713 -16.377 7.317   1.00 34.42 ? 87  GLY B O   1 
ATOM   2028 N  N   . LYS B 1 91  ? -17.045 -16.208 9.135   1.00 36.61 ? 88  LYS B N   1 
ATOM   2029 C  CA  . LYS B 1 91  ? -18.277 -16.039 8.381   1.00 36.09 ? 88  LYS B CA  1 
ATOM   2030 C  C   . LYS B 1 91  ? -18.203 -14.782 7.516   1.00 33.74 ? 88  LYS B C   1 
ATOM   2031 O  O   . LYS B 1 91  ? -18.479 -14.829 6.320   1.00 33.63 ? 88  LYS B O   1 
ATOM   2032 C  CB  . LYS B 1 91  ? -19.488 -16.014 9.324   1.00 38.22 ? 88  LYS B CB  1 
ATOM   2033 C  CG  . LYS B 1 91  ? -20.777 -15.465 8.717   1.00 39.85 ? 88  LYS B CG  1 
ATOM   2034 C  CD  . LYS B 1 91  ? -22.048 -15.799 9.489   1.00 42.14 ? 88  LYS B CD  1 
ATOM   2035 C  CE  . LYS B 1 91  ? -22.482 -17.218 9.288   1.00 43.84 ? 88  LYS B CE  1 
ATOM   2036 N  NZ  . LYS B 1 91  ? -23.731 -17.501 9.999   1.00 45.03 ? 88  LYS B NZ  1 
ATOM   2037 N  N   . ALA B 1 92  ? -17.840 -13.652 8.124   1.00 33.71 ? 89  ALA B N   1 
ATOM   2038 C  CA  . ALA B 1 92  ? -17.911 -12.375 7.431   1.00 32.94 ? 89  ALA B CA  1 
ATOM   2039 C  C   . ALA B 1 92  ? -16.957 -12.351 6.240   1.00 30.69 ? 89  ALA B C   1 
ATOM   2040 O  O   . ALA B 1 92  ? -17.344 -11.928 5.152   1.00 31.02 ? 89  ALA B O   1 
ATOM   2041 C  CB  . ALA B 1 92  ? -17.622 -11.254 8.392   1.00 34.03 ? 89  ALA B CB  1 
ATOM   2042 N  N   . ALA B 1 93  ? -15.718 -12.814 6.457   1.00 28.86 ? 90  ALA B N   1 
ATOM   2043 C  CA  . ALA B 1 93  ? -14.699 -12.810 5.418   1.00 28.12 ? 90  ALA B CA  1 
ATOM   2044 C  C   . ALA B 1 93  ? -15.055 -13.798 4.308   1.00 28.01 ? 90  ALA B C   1 
ATOM   2045 O  O   . ALA B 1 93  ? -14.918 -13.474 3.131   1.00 29.04 ? 90  ALA B O   1 
ATOM   2046 C  CB  . ALA B 1 93  ? -13.338 -13.109 6.010   1.00 28.13 ? 90  ALA B CB  1 
ATOM   2047 N  N   . CYS B 1 94  ? -15.522 -14.999 4.674   1.00 27.87 ? 91  CYS B N   1 
ATOM   2048 C  CA  . CYS B 1 94  ? -15.878 -15.995 3.676   1.00 28.11 ? 91  CYS B CA  1 
ATOM   2049 C  C   . CYS B 1 94  ? -17.052 -15.504 2.825   1.00 27.84 ? 91  CYS B C   1 
ATOM   2050 O  O   . CYS B 1 94  ? -17.025 -15.641 1.603   1.00 27.41 ? 91  CYS B O   1 
ATOM   2051 C  CB  . CYS B 1 94  ? -16.186 -17.345 4.310   1.00 28.72 ? 91  CYS B CB  1 
ATOM   2052 S  SG  . CYS B 1 94  ? -16.369 -18.665 3.086   1.00 30.42 ? 91  CYS B SG  1 
ATOM   2053 N  N   . ARG B 1 95  ? -18.074 -14.924 3.471   1.00 28.92 ? 92  ARG B N   1 
ATOM   2054 C  CA  . ARG B 1 95  ? -19.227 -14.386 2.763   1.00 30.35 ? 92  ARG B CA  1 
ATOM   2055 C  C   . ARG B 1 95  ? -18.773 -13.321 1.768   1.00 29.49 ? 92  ARG B C   1 
ATOM   2056 O  O   . ARG B 1 95  ? -19.154 -13.362 0.602   1.00 29.51 ? 92  ARG B O   1 
ATOM   2057 C  CB  . ARG B 1 95  ? -20.266 -13.828 3.740   1.00 33.08 ? 92  ARG B CB  1 
ATOM   2058 C  CG  . ARG B 1 95  ? -21.456 -13.141 3.080   1.00 35.33 ? 92  ARG B CG  1 
ATOM   2059 C  CD  . ARG B 1 95  ? -22.504 -12.755 4.112   1.00 37.25 ? 92  ARG B CD  1 
ATOM   2060 N  NE  . ARG B 1 95  ? -21.922 -11.849 5.110   1.00 39.51 ? 92  ARG B NE  1 
ATOM   2061 C  CZ  . ARG B 1 95  ? -22.373 -11.638 6.342   1.00 41.56 ? 92  ARG B CZ  1 
ATOM   2062 N  NH1 . ARG B 1 95  ? -23.513 -12.173 6.748   1.00 42.54 ? 92  ARG B NH1 1 
ATOM   2063 N  NH2 . ARG B 1 95  ? -21.672 -10.880 7.168   1.00 42.69 ? 92  ARG B NH2 1 
ATOM   2064 N  N   . LEU B 1 96  ? -17.935 -12.387 2.230   1.00 29.51 ? 93  LEU B N   1 
ATOM   2065 C  CA  . LEU B 1 96  ? -17.446 -11.322 1.366   1.00 30.46 ? 93  LEU B CA  1 
ATOM   2066 C  C   . LEU B 1 96  ? -16.638 -11.924 0.217   1.00 29.19 ? 93  LEU B C   1 
ATOM   2067 O  O   . LEU B 1 96  ? -16.776 -11.488 -0.923  1.00 27.71 ? 93  LEU B O   1 
ATOM   2068 C  CB  . LEU B 1 96  ? -16.653 -10.268 2.142   1.00 32.26 ? 93  LEU B CB  1 
ATOM   2069 C  CG  . LEU B 1 96  ? -17.477 -9.181  2.842   1.00 34.31 ? 93  LEU B CG  1 
ATOM   2070 C  CD1 . LEU B 1 96  ? -16.569 -8.283  3.660   1.00 35.70 ? 93  LEU B CD1 1 
ATOM   2071 C  CD2 . LEU B 1 96  ? -18.285 -8.344  1.859   1.00 34.97 ? 93  LEU B CD2 1 
ATOM   2072 N  N   . LEU B 1 97  ? -15.832 -12.958 0.507   1.00 28.29 ? 94  LEU B N   1 
ATOM   2073 C  CA  . LEU B 1 97  ? -15.011 -13.577 -0.523  1.00 30.03 ? 94  LEU B CA  1 
ATOM   2074 C  C   . LEU B 1 97  ? -15.889 -14.250 -1.577  1.00 30.56 ? 94  LEU B C   1 
ATOM   2075 O  O   . LEU B 1 97  ? -15.575 -14.198 -2.764  1.00 31.81 ? 94  LEU B O   1 
ATOM   2076 C  CB  . LEU B 1 97  ? -14.005 -14.568 0.057   1.00 30.49 ? 94  LEU B CB  1 
ATOM   2077 C  CG  . LEU B 1 97  ? -13.075 -15.228 -0.966  1.00 31.14 ? 94  LEU B CG  1 
ATOM   2078 C  CD1 . LEU B 1 97  ? -12.242 -14.207 -1.736  1.00 30.63 ? 94  LEU B CD1 1 
ATOM   2079 C  CD2 . LEU B 1 97  ? -12.187 -16.249 -0.275  1.00 32.07 ? 94  LEU B CD2 1 
ATOM   2080 N  N   A MET B 1 98  ? -16.976 -14.896 -1.135  0.79 29.37 ? 95  MET B N   1 
ATOM   2081 N  N   B MET B 1 98  ? -16.975 -14.894 -1.135  0.21 30.74 ? 95  MET B N   1 
ATOM   2082 C  CA  A MET B 1 98  ? -17.908 -15.539 -2.048  0.79 28.52 ? 95  MET B CA  1 
ATOM   2083 C  CA  B MET B 1 98  ? -17.904 -15.532 -2.052  0.21 31.10 ? 95  MET B CA  1 
ATOM   2084 C  C   A MET B 1 98  ? -18.471 -14.512 -3.032  0.79 28.83 ? 95  MET B C   1 
ATOM   2085 C  C   B MET B 1 98  ? -18.461 -14.508 -3.037  0.21 30.54 ? 95  MET B C   1 
ATOM   2086 O  O   A MET B 1 98  ? -18.519 -14.762 -4.235  0.79 28.07 ? 95  MET B O   1 
ATOM   2087 O  O   B MET B 1 98  ? -18.506 -14.768 -4.238  0.21 30.68 ? 95  MET B O   1 
ATOM   2088 C  CB  A MET B 1 98  ? -19.046 -16.219 -1.275  0.79 28.59 ? 95  MET B CB  1 
ATOM   2089 C  CB  B MET B 1 98  ? -19.060 -16.200 -1.302  0.21 31.93 ? 95  MET B CB  1 
ATOM   2090 C  CG  A MET B 1 98  ? -18.593 -17.400 -0.437  0.79 28.16 ? 95  MET B CG  1 
ATOM   2091 C  CG  B MET B 1 98  ? -18.777 -17.633 -0.910  0.21 32.67 ? 95  MET B CG  1 
ATOM   2092 S  SD  A MET B 1 98  ? -19.767 -17.846 0.858   0.79 28.60 ? 95  MET B SD  1 
ATOM   2093 S  SD  B MET B 1 98  ? -20.202 -18.401 -0.120  0.21 33.50 ? 95  MET B SD  1 
ATOM   2094 C  CE  A MET B 1 98  ? -21.183 -18.434 -0.083  0.79 29.02 ? 95  MET B CE  1 
ATOM   2095 C  CE  B MET B 1 98  ? -19.871 -17.693 1.496   0.21 33.36 ? 95  MET B CE  1 
ATOM   2096 N  N   . LEU B 1 99  ? -18.869 -13.342 -2.522  1.00 30.42 ? 96  LEU B N   1 
ATOM   2097 C  CA  . LEU B 1 99  ? -19.460 -12.305 -3.353  1.00 29.85 ? 96  LEU B CA  1 
ATOM   2098 C  C   . LEU B 1 99  ? -18.432 -11.758 -4.346  1.00 29.55 ? 96  LEU B C   1 
ATOM   2099 O  O   . LEU B 1 99  ? -18.775 -11.459 -5.490  1.00 29.56 ? 96  LEU B O   1 
ATOM   2100 C  CB  . LEU B 1 99  ? -20.053 -11.217 -2.457  1.00 30.70 ? 96  LEU B CB  1 
ATOM   2101 C  CG  . LEU B 1 99  ? -21.127 -11.684 -1.465  1.00 31.67 ? 96  LEU B CG  1 
ATOM   2102 C  CD1 . LEU B 1 99  ? -21.651 -10.519 -0.638  1.00 32.15 ? 96  LEU B CD1 1 
ATOM   2103 C  CD2 . LEU B 1 99  ? -22.286 -12.392 -2.154  1.00 33.96 ? 96  LEU B CD2 1 
ATOM   2104 N  N   . LYS B 1 100 ? -17.164 -11.660 -3.925  1.00 28.53 ? 97  LYS B N   1 
ATOM   2105 C  CA  . LYS B 1 100 ? -16.102 -11.218 -4.815  1.00 30.34 ? 97  LYS B CA  1 
ATOM   2106 C  C   . LYS B 1 100 ? -15.966 -12.147 -6.020  1.00 30.72 ? 97  LYS B C   1 
ATOM   2107 O  O   . LYS B 1 100 ? -15.804 -11.679 -7.145  1.00 31.92 ? 97  LYS B O   1 
ATOM   2108 C  CB  . LYS B 1 100 ? -14.761 -11.160 -4.081  1.00 31.76 ? 97  LYS B CB  1 
ATOM   2109 C  CG  . LYS B 1 100 ? -14.643 -10.036 -3.073  1.00 34.13 ? 97  LYS B CG  1 
ATOM   2110 C  CD  . LYS B 1 100 ? -13.311 -10.019 -2.334  1.00 35.85 ? 97  LYS B CD  1 
ATOM   2111 C  CE  . LYS B 1 100 ? -12.121 -9.807  -3.220  1.00 36.53 ? 97  LYS B CE  1 
ATOM   2112 N  NZ  . LYS B 1 100 ? -12.184 -8.529  -3.935  1.00 37.03 ? 97  LYS B NZ  1 
ATOM   2113 N  N   . LEU B 1 101 ? -16.019 -13.462 -5.780  1.00 30.47 ? 98  LEU B N   1 
ATOM   2114 C  CA  . LEU B 1 101 ? -15.681 -14.431 -6.810  1.00 31.51 ? 98  LEU B CA  1 
ATOM   2115 C  C   . LEU B 1 101 ? -16.798 -14.541 -7.849  1.00 33.39 ? 98  LEU B C   1 
ATOM   2116 O  O   . LEU B 1 101 ? -16.510 -14.661 -9.037  1.00 36.13 ? 98  LEU B O   1 
ATOM   2117 C  CB  . LEU B 1 101 ? -15.330 -15.777 -6.172  1.00 30.54 ? 98  LEU B CB  1 
ATOM   2118 C  CG  . LEU B 1 101 ? -14.132 -15.771 -5.213  1.00 32.01 ? 98  LEU B CG  1 
ATOM   2119 C  CD1 . LEU B 1 101 ? -13.786 -17.173 -4.744  1.00 30.95 ? 98  LEU B CD1 1 
ATOM   2120 C  CD2 . LEU B 1 101 ? -12.905 -15.110 -5.822  1.00 32.63 ? 98  LEU B CD2 1 
ATOM   2121 N  N   . ILE B 1 102 ? -18.066 -14.478 -7.426  1.00 35.67 ? 99  ILE B N   1 
ATOM   2122 C  CA  . ILE B 1 102 ? -19.170 -14.585 -8.376  1.00 37.30 ? 99  ILE B CA  1 
ATOM   2123 C  C   . ILE B 1 102 ? -19.268 -13.309 -9.214  1.00 39.27 ? 99  ILE B C   1 
ATOM   2124 O  O   . ILE B 1 102 ? -19.915 -13.308 -10.260 1.00 42.06 ? 99  ILE B O   1 
ATOM   2125 C  CB  . ILE B 1 102 ? -20.510 -14.934 -7.697  1.00 37.39 ? 99  ILE B CB  1 
ATOM   2126 C  CG1 . ILE B 1 102 ? -20.850 -13.991 -6.539  1.00 38.15 ? 99  ILE B CG1 1 
ATOM   2127 C  CG2 . ILE B 1 102 ? -20.519 -16.401 -7.261  1.00 37.65 ? 99  ILE B CG2 1 
ATOM   2128 C  CD1 . ILE B 1 102 ? -22.289 -14.085 -6.064  1.00 38.93 ? 99  ILE B CD1 1 
ATOM   2129 N  N   . GLU B 1 103 ? -18.635 -12.226 -8.749  1.00 40.49 ? 100 GLU B N   1 
ATOM   2130 C  CA  . GLU B 1 103 ? -18.512 -11.007 -9.532  1.00 43.01 ? 100 GLU B CA  1 
ATOM   2131 C  C   . GLU B 1 103 ? -17.338 -11.128 -10.503 1.00 46.17 ? 100 GLU B C   1 
ATOM   2132 O  O   . GLU B 1 103 ? -17.466 -10.782 -11.676 1.00 49.01 ? 100 GLU B O   1 
ATOM   2133 C  CB  . GLU B 1 103 ? -18.332 -9.811  -8.596  1.00 43.26 ? 100 GLU B CB  1 
ATOM   2134 C  CG  . GLU B 1 103 ? -18.121 -8.485  -9.320  1.00 44.22 ? 100 GLU B CG  1 
ATOM   2135 C  CD  . GLU B 1 103 ? -17.602 -7.368  -8.432  1.00 45.60 ? 100 GLU B CD  1 
ATOM   2136 O  OE1 . GLU B 1 103 ? -17.129 -7.646  -7.307  1.00 45.38 ? 100 GLU B OE1 1 
ATOM   2137 O  OE2 . GLU B 1 103 ? -17.684 -6.207  -8.877  1.00 46.42 ? 100 GLU B OE2 1 
ATOM   2138 N  N   . LYS B 1 104 ? -16.193 -11.602 -9.992  1.00 46.28 ? 101 LYS B N   1 
ATOM   2139 C  CA  . LYS B 1 104 ? -14.965 -11.700 -10.768 1.00 47.28 ? 101 LYS B CA  1 
ATOM   2140 C  C   . LYS B 1 104 ? -15.142 -12.665 -11.939 1.00 47.03 ? 101 LYS B C   1 
ATOM   2141 O  O   . LYS B 1 104 ? -14.567 -12.446 -13.003 1.00 46.61 ? 101 LYS B O   1 
ATOM   2142 C  CB  . LYS B 1 104 ? -13.796 -12.140 -9.878  1.00 48.87 ? 101 LYS B CB  1 
ATOM   2143 C  CG  . LYS B 1 104 ? -12.475 -12.362 -10.604 1.00 49.80 ? 101 LYS B CG  1 
ATOM   2144 C  CD  . LYS B 1 104 ? -11.310 -12.687 -9.677  0.82 51.19 ? 101 LYS B CD  1 
ATOM   2145 C  CE  . LYS B 1 104 ? -10.021 -12.826 -10.421 0.76 52.26 ? 101 LYS B CE  1 
ATOM   2146 N  NZ  . LYS B 1 104 ? -8.875  -12.784 -9.512  1.00 53.75 ? 101 LYS B NZ  1 
ATOM   2147 N  N   . TYR B 1 105 ? -15.927 -13.733 -11.730 1.00 46.60 ? 102 TYR B N   1 
ATOM   2148 C  CA  . TYR B 1 105 ? -16.167 -14.731 -12.762 1.00 47.02 ? 102 TYR B CA  1 
ATOM   2149 C  C   . TYR B 1 105 ? -17.626 -14.659 -13.208 1.00 48.65 ? 102 TYR B C   1 
ATOM   2150 O  O   . TYR B 1 105 ? -18.443 -13.987 -12.582 1.00 48.68 ? 102 TYR B O   1 
ATOM   2151 C  CB  . TYR B 1 105 ? -15.778 -16.121 -12.244 1.00 46.08 ? 102 TYR B CB  1 
ATOM   2152 C  CG  . TYR B 1 105 ? -14.350 -16.226 -11.721 1.00 45.14 ? 102 TYR B CG  1 
ATOM   2153 C  CD1 . TYR B 1 105 ? -13.273 -16.405 -12.584 1.00 46.27 ? 102 TYR B CD1 1 
ATOM   2154 C  CD2 . TYR B 1 105 ? -14.078 -16.153 -10.360 1.00 44.28 ? 102 TYR B CD2 1 
ATOM   2155 C  CE1 . TYR B 1 105 ? -11.975 -16.500 -12.108 1.00 46.57 ? 102 TYR B CE1 1 
ATOM   2156 C  CE2 . TYR B 1 105 ? -12.786 -16.248 -9.872  1.00 45.24 ? 102 TYR B CE2 1 
ATOM   2157 C  CZ  . TYR B 1 105 ? -11.730 -16.422 -10.748 1.00 46.15 ? 102 TYR B CZ  1 
ATOM   2158 O  OH  . TYR B 1 105 ? -10.461 -16.517 -10.256 1.00 46.86 ? 102 TYR B OH  1 
ATOM   2159 N  N   . GLN B 1 106 ? -17.937 -15.367 -14.301 1.00 51.15 ? 103 GLN B N   1 
ATOM   2160 C  CA  . GLN B 1 106 ? -19.268 -15.353 -14.890 1.00 52.93 ? 103 GLN B CA  1 
ATOM   2161 C  C   . GLN B 1 106 ? -20.225 -16.255 -14.110 1.00 52.31 ? 103 GLN B C   1 
ATOM   2162 O  O   . GLN B 1 106 ? -21.441 -16.094 -14.213 1.00 54.06 ? 103 GLN B O   1 
ATOM   2163 C  CB  . GLN B 1 106 ? -19.213 -15.807 -16.350 0.53 54.12 ? 103 GLN B CB  1 
ATOM   2164 C  CG  . GLN B 1 106 ? -18.586 -14.797 -17.305 0.52 54.94 ? 103 GLN B CG  1 
ATOM   2165 C  CD  . GLN B 1 106 ? -19.455 -13.581 -17.550 1.00 56.00 ? 103 GLN B CD  1 
ATOM   2166 O  OE1 . GLN B 1 106 ? -19.526 -12.663 -16.726 1.00 57.44 ? 103 GLN B OE1 1 
ATOM   2167 N  NE2 . GLN B 1 106 ? -20.109 -13.549 -18.703 1.00 56.40 ? 103 GLN B NE2 1 
ATOM   2168 N  N   . THR B 1 107 ? -19.675 -17.193 -13.329 1.00 50.87 ? 104 THR B N   1 
ATOM   2169 C  CA  . THR B 1 107 ? -20.459 -18.254 -12.713 1.00 48.01 ? 104 THR B CA  1 
ATOM   2170 C  C   . THR B 1 107 ? -21.351 -17.686 -11.609 1.00 44.91 ? 104 THR B C   1 
ATOM   2171 O  O   . THR B 1 107 ? -21.109 -16.592 -11.104 1.00 44.79 ? 104 THR B O   1 
ATOM   2172 C  CB  . THR B 1 107 ? -19.524 -19.325 -12.149 1.00 47.88 ? 104 THR B CB  1 
ATOM   2173 O  OG1 . THR B 1 107 ? -18.857 -18.686 -11.064 1.00 47.33 ? 104 THR B OG1 1 
ATOM   2174 C  CG2 . THR B 1 107 ? -18.532 -19.859 -13.168 1.00 48.40 ? 104 THR B CG2 1 
ATOM   2175 N  N   . ASN B 1 108 ? -22.381 -18.460 -11.247 1.00 42.42 ? 105 ASN B N   1 
ATOM   2176 C  CA  . ASN B 1 108 ? -23.166 -18.229 -10.044 1.00 41.07 ? 105 ASN B CA  1 
ATOM   2177 C  C   . ASN B 1 108 ? -22.969 -19.388 -9.064  1.00 37.30 ? 105 ASN B C   1 
ATOM   2178 O  O   . ASN B 1 108 ? -23.736 -19.537 -8.117  1.00 38.15 ? 105 ASN B O   1 
ATOM   2179 C  CB  . ASN B 1 108 ? -24.645 -18.031 -10.366 0.76 42.51 ? 105 ASN B CB  1 
ATOM   2180 C  CG  . ASN B 1 108 ? -24.932 -16.672 -10.960 0.61 44.14 ? 105 ASN B CG  1 
ATOM   2181 O  OD1 . ASN B 1 108 ? -25.447 -15.787 -10.266 1.00 45.93 ? 105 ASN B OD1 1 
ATOM   2182 N  ND2 . ASN B 1 108 ? -24.603 -16.479 -12.228 1.00 45.33 ? 105 ASN B ND2 1 
ATOM   2183 N  N   . LYS B 1 109 ? -21.930 -20.203 -9.284  1.00 33.60 ? 106 LYS B N   1 
ATOM   2184 C  CA  . LYS B 1 109 ? -21.654 -21.336 -8.416  1.00 32.24 ? 106 LYS B CA  1 
ATOM   2185 C  C   . LYS B 1 109 ? -20.226 -21.245 -7.883  1.00 30.53 ? 106 LYS B C   1 
ATOM   2186 O  O   . LYS B 1 109 ? -19.331 -20.776 -8.580  1.00 31.89 ? 106 LYS B O   1 
ATOM   2187 C  CB  . LYS B 1 109 ? -21.857 -22.662 -9.157  1.00 33.04 ? 106 LYS B CB  1 
ATOM   2188 C  CG  . LYS B 1 109 ? -23.306 -23.010 -9.465  1.00 34.22 ? 106 LYS B CG  1 
ATOM   2189 C  CD  . LYS B 1 109 ? -23.455 -24.280 -10.292 1.00 35.21 ? 106 LYS B CD  1 
ATOM   2190 C  CE  . LYS B 1 109 ? -24.877 -24.578 -10.639 1.00 36.18 ? 106 LYS B CE  1 
ATOM   2191 N  NZ  . LYS B 1 109 ? -24.951 -25.732 -11.538 1.00 38.10 ? 106 LYS B NZ  1 
ATOM   2192 N  N   . LEU B 1 110 ? -20.041 -21.705 -6.639  1.00 28.83 ? 107 LEU B N   1 
ATOM   2193 C  CA  . LEU B 1 110 ? -18.726 -21.848 -6.034  1.00 27.61 ? 107 LEU B CA  1 
ATOM   2194 C  C   . LEU B 1 110 ? -18.618 -23.227 -5.390  1.00 26.10 ? 107 LEU B C   1 
ATOM   2195 O  O   . LEU B 1 110 ? -19.598 -23.753 -4.861  1.00 26.23 ? 107 LEU B O   1 
ATOM   2196 C  CB  . LEU B 1 110 ? -18.470 -20.760 -4.995  1.00 28.21 ? 107 LEU B CB  1 
ATOM   2197 C  CG  . LEU B 1 110 ? -18.522 -19.315 -5.499  1.00 28.38 ? 107 LEU B CG  1 
ATOM   2198 C  CD1 . LEU B 1 110 ? -18.331 -18.400 -4.315  1.00 29.71 ? 107 LEU B CD1 1 
ATOM   2199 C  CD2 . LEU B 1 110 ? -17.491 -19.020 -6.575  1.00 28.87 ? 107 LEU B CD2 1 
ATOM   2200 N  N   . TYR B 1 111 ? -17.400 -23.780 -5.424  1.00 25.25 ? 108 TYR B N   1 
ATOM   2201 C  CA  . TYR B 1 111 ? -17.124 -25.119 -4.936  1.00 25.46 ? 108 TYR B CA  1 
ATOM   2202 C  C   . TYR B 1 111 ? -16.017 -25.077 -3.885  1.00 24.05 ? 108 TYR B C   1 
ATOM   2203 O  O   . TYR B 1 111 ? -15.115 -24.238 -3.936  1.00 23.47 ? 108 TYR B O   1 
ATOM   2204 C  CB  . TYR B 1 111 ? -16.715 -26.016 -6.109  1.00 25.46 ? 108 TYR B CB  1 
ATOM   2205 C  CG  . TYR B 1 111 ? -17.813 -26.256 -7.135  1.00 27.08 ? 108 TYR B CG  1 
ATOM   2206 C  CD1 . TYR B 1 111 ? -18.167 -25.275 -8.057  1.00 28.25 ? 108 TYR B CD1 1 
ATOM   2207 C  CD2 . TYR B 1 111 ? -18.497 -27.466 -7.184  1.00 27.82 ? 108 TYR B CD2 1 
ATOM   2208 C  CE1 . TYR B 1 111 ? -19.173 -25.488 -8.987  1.00 29.27 ? 108 TYR B CE1 1 
ATOM   2209 C  CE2 . TYR B 1 111 ? -19.490 -27.697 -8.122  1.00 29.04 ? 108 TYR B CE2 1 
ATOM   2210 C  CZ  . TYR B 1 111 ? -19.831 -26.704 -9.024  1.00 29.70 ? 108 TYR B CZ  1 
ATOM   2211 O  OH  . TYR B 1 111 ? -20.825 -26.939 -9.934  1.00 31.71 ? 108 TYR B OH  1 
ATOM   2212 N  N   . LEU B 1 112 ? -16.110 -26.010 -2.932  1.00 24.15 ? 109 LEU B N   1 
ATOM   2213 C  CA  . LEU B 1 112 ? -15.018 -26.350 -2.039  1.00 24.25 ? 109 LEU B CA  1 
ATOM   2214 C  C   . LEU B 1 112 ? -15.159 -27.825 -1.671  1.00 24.39 ? 109 LEU B C   1 
ATOM   2215 O  O   . LEU B 1 112 ? -16.149 -28.458 -2.012  1.00 23.86 ? 109 LEU B O   1 
ATOM   2216 C  CB  . LEU B 1 112 ? -14.974 -25.435 -0.812  1.00 25.19 ? 109 LEU B CB  1 
ATOM   2217 C  CG  . LEU B 1 112 ? -16.229 -25.370 0.065   1.00 25.73 ? 109 LEU B CG  1 
ATOM   2218 C  CD1 . LEU B 1 112 ? -16.384 -26.605 0.946   1.00 26.42 ? 109 LEU B CD1 1 
ATOM   2219 C  CD2 . LEU B 1 112 ? -16.217 -24.109 0.914   1.00 26.39 ? 109 LEU B CD2 1 
ATOM   2220 N  N   . SER B 1 113 ? -14.142 -28.379 -1.010  1.00 24.37 ? 110 SER B N   1 
ATOM   2221 C  CA  . SER B 1 113 ? -14.252 -29.727 -0.478  1.00 24.63 ? 110 SER B CA  1 
ATOM   2222 C  C   . SER B 1 113 ? -13.744 -29.738 0.959   1.00 25.80 ? 110 SER B C   1 
ATOM   2223 O  O   . SER B 1 113 ? -12.868 -28.947 1.313   1.00 26.58 ? 110 SER B O   1 
ATOM   2224 C  CB  . SER B 1 113 ? -13.538 -30.732 -1.350  1.00 25.27 ? 110 SER B CB  1 
ATOM   2225 O  OG  . SER B 1 113 ? -12.144 -30.486 -1.419  1.00 25.60 ? 110 SER B OG  1 
ATOM   2226 N  N   . VAL B 1 114 ? -14.312 -30.636 1.772   1.00 27.10 ? 111 VAL B N   1 
ATOM   2227 C  CA  . VAL B 1 114 ? -14.052 -30.665 3.202   1.00 28.08 ? 111 VAL B CA  1 
ATOM   2228 C  C   . VAL B 1 114 ? -13.811 -32.102 3.658   1.00 29.94 ? 111 VAL B C   1 
ATOM   2229 O  O   . VAL B 1 114 ? -14.355 -33.049 3.090   1.00 28.73 ? 111 VAL B O   1 
ATOM   2230 C  CB  . VAL B 1 114 ? -15.218 -30.035 3.989   1.00 29.30 ? 111 VAL B CB  1 
ATOM   2231 C  CG1 . VAL B 1 114 ? -15.186 -28.518 3.918   1.00 29.56 ? 111 VAL B CG1 1 
ATOM   2232 C  CG2 . VAL B 1 114 ? -16.571 -30.568 3.536   1.00 29.35 ? 111 VAL B CG2 1 
ATOM   2233 N  N   . TYR B 1 115 ? -13.001 -32.230 4.715   1.00 31.52 ? 112 TYR B N   1 
ATOM   2234 C  CA  . TYR B 1 115 ? -12.799 -33.495 5.398   1.00 34.06 ? 112 TYR B CA  1 
ATOM   2235 C  C   . TYR B 1 115 ? -14.017 -33.743 6.285   1.00 38.61 ? 112 TYR B C   1 
ATOM   2236 O  O   . TYR B 1 115 ? -14.597 -32.802 6.825   1.00 41.19 ? 112 TYR B O   1 
ATOM   2237 C  CB  . TYR B 1 115 ? -11.482 -33.466 6.179   1.00 33.06 ? 112 TYR B CB  1 
ATOM   2238 C  CG  . TYR B 1 115 ? -10.951 -34.849 6.536   1.00 32.47 ? 112 TYR B CG  1 
ATOM   2239 C  CD1 . TYR B 1 115 ? -10.121 -35.548 5.666   1.00 31.36 ? 112 TYR B CD1 1 
ATOM   2240 C  CD2 . TYR B 1 115 ? -11.295 -35.461 7.734   1.00 33.34 ? 112 TYR B CD2 1 
ATOM   2241 C  CE1 . TYR B 1 115 ? -9.636  -36.806 5.985   1.00 31.77 ? 112 TYR B CE1 1 
ATOM   2242 C  CE2 . TYR B 1 115 ? -10.822 -36.723 8.064   1.00 33.32 ? 112 TYR B CE2 1 
ATOM   2243 C  CZ  . TYR B 1 115 ? -9.995  -37.400 7.184   1.00 31.78 ? 112 TYR B CZ  1 
ATOM   2244 O  OH  . TYR B 1 115 ? -9.528  -38.642 7.507   1.00 32.13 ? 112 TYR B OH  1 
ATOM   2245 N  N   . ASP B 1 116 ? -14.385 -35.019 6.435   1.00 42.60 ? 113 ASP B N   1 
ATOM   2246 C  CA  . ASP B 1 116 ? -15.657 -35.393 7.036   1.00 45.04 ? 113 ASP B CA  1 
ATOM   2247 C  C   . ASP B 1 116 ? -15.724 -34.956 8.497   1.00 48.02 ? 113 ASP B C   1 
ATOM   2248 O  O   . ASP B 1 116 ? -16.747 -34.430 8.933   1.00 47.85 ? 113 ASP B O   1 
ATOM   2249 C  CB  . ASP B 1 116 ? -15.924 -36.879 6.866   1.00 46.60 ? 113 ASP B CB  1 
ATOM   2250 C  CG  . ASP B 1 116 ? -16.238 -37.309 5.441   1.00 47.20 ? 113 ASP B CG  1 
ATOM   2251 O  OD1 . ASP B 1 116 ? -16.281 -36.423 4.563   1.00 46.37 ? 113 ASP B OD1 1 
ATOM   2252 O  OD2 . ASP B 1 116 ? -16.441 -38.523 5.229   1.00 47.63 ? 113 ASP B OD2 1 
ATOM   2253 N  N   . THR B 1 117 ? -14.630 -35.166 9.240   1.00 51.04 ? 114 THR B N   1 
ATOM   2254 C  CA  . THR B 1 117 ? -14.597 -34.891 10.670  1.00 53.64 ? 114 THR B CA  1 
ATOM   2255 C  C   . THR B 1 117 ? -14.496 -33.388 10.937  1.00 54.80 ? 114 THR B C   1 
ATOM   2256 O  O   . THR B 1 117 ? -14.485 -32.978 12.097  1.00 56.01 ? 114 THR B O   1 
ATOM   2257 C  CB  . THR B 1 117 ? -13.442 -35.651 11.328  1.00 54.69 ? 114 THR B CB  1 
ATOM   2258 O  OG1 . THR B 1 117 ? -12.225 -35.139 10.791  1.00 55.10 ? 114 THR B OG1 1 
ATOM   2259 C  CG2 . THR B 1 117 ? -13.520 -37.151 11.103  1.00 54.20 ? 114 THR B CG2 1 
ATOM   2260 N  N   . ASN B 1 118 ? -14.412 -32.573 9.875   0.71 54.71 ? 115 ASN B N   1 
ATOM   2261 C  CA  . ASN B 1 118 ? -14.371 -31.125 10.011  0.45 53.96 ? 115 ASN B CA  1 
ATOM   2262 C  C   . ASN B 1 118 ? -15.789 -30.610 10.249  1.00 54.18 ? 115 ASN B C   1 
ATOM   2263 O  O   . ASN B 1 118 ? -16.513 -30.314 9.300   1.00 53.28 ? 115 ASN B O   1 
ATOM   2264 C  CB  . ASN B 1 118 ? -13.708 -30.480 8.797   0.51 54.50 ? 115 ASN B CB  1 
ATOM   2265 C  CG  . ASN B 1 118 ? -13.164 -29.101 9.088   0.68 55.26 ? 115 ASN B CG  1 
ATOM   2266 O  OD1 . ASN B 1 118 ? -13.441 -28.522 10.146  1.00 56.95 ? 115 ASN B OD1 1 
ATOM   2267 N  ND2 . ASN B 1 118 ? -12.399 -28.550 8.158   1.00 55.10 ? 115 ASN B ND2 1 
ATOM   2268 N  N   . SER B 1 119 ? -16.165 -30.496 11.529  1.00 53.39 ? 116 SER B N   1 
ATOM   2269 C  CA  . SER B 1 119 ? -17.527 -30.166 11.919  1.00 52.73 ? 116 SER B CA  1 
ATOM   2270 C  C   . SER B 1 119 ? -17.773 -28.661 11.819  1.00 51.29 ? 116 SER B C   1 
ATOM   2271 O  O   . SER B 1 119 ? -18.833 -28.240 11.358  0.61 50.24 ? 116 SER B O   1 
ATOM   2272 C  CB  . SER B 1 119 ? -17.822 -30.679 13.307  0.87 53.64 ? 116 SER B CB  1 
ATOM   2273 O  OG  . SER B 1 119 ? -17.582 -32.077 13.390  0.64 53.72 ? 116 SER B OG  1 
ATOM   2274 N  N   . SER B 1 120 ? -16.796 -27.860 12.264  1.00 50.36 ? 117 SER B N   1 
ATOM   2275 C  CA  . SER B 1 120 ? -16.906 -26.410 12.227  1.00 49.75 ? 117 SER B CA  1 
ATOM   2276 C  C   . SER B 1 120 ? -17.035 -25.923 10.786  0.58 48.62 ? 117 SER B C   1 
ATOM   2277 O  O   . SER B 1 120 ? -17.840 -25.037 10.508  0.79 48.38 ? 117 SER B O   1 
ATOM   2278 C  CB  . SER B 1 120 ? -15.738 -25.749 12.920  1.00 49.50 ? 117 SER B CB  1 
ATOM   2279 O  OG  . SER B 1 120 ? -15.707 -26.079 14.302  0.32 49.30 ? 117 SER B OG  1 
ATOM   2280 N  N   . ALA B 1 121 ? -16.245 -26.520 9.883   1.00 47.09 ? 118 ALA B N   1 
ATOM   2281 C  CA  . ALA B 1 121 ? -16.186 -26.083 8.497   1.00 45.73 ? 118 ALA B CA  1 
ATOM   2282 C  C   . ALA B 1 121 ? -17.497 -26.393 7.780   1.00 44.80 ? 118 ALA B C   1 
ATOM   2283 O  O   . ALA B 1 121 ? -18.035 -25.533 7.089   1.00 43.54 ? 118 ALA B O   1 
ATOM   2284 C  CB  . ALA B 1 121 ? -15.013 -26.725 7.792   0.36 45.74 ? 118 ALA B CB  1 
ATOM   2285 N  N   . ILE B 1 122 ? -17.997 -27.624 7.944   1.00 44.57 ? 119 ILE B N   1 
ATOM   2286 C  CA  . ILE B 1 122 ? -19.244 -28.031 7.313   1.00 44.62 ? 119 ILE B CA  1 
ATOM   2287 C  C   . ILE B 1 122 ? -20.373 -27.124 7.804   1.00 44.89 ? 119 ILE B C   1 
ATOM   2288 O  O   . ILE B 1 122 ? -21.155 -26.635 6.994   1.00 43.40 ? 119 ILE B O   1 
ATOM   2289 C  CB  . ILE B 1 122 ? -19.528 -29.528 7.549   1.00 44.13 ? 119 ILE B CB  1 
ATOM   2290 C  CG1 . ILE B 1 122 ? -18.490 -30.400 6.834   0.63 43.83 ? 119 ILE B CG1 1 
ATOM   2291 C  CG2 . ILE B 1 122 ? -20.951 -29.897 7.124   1.00 43.93 ? 119 ILE B CG2 1 
ATOM   2292 C  CD1 . ILE B 1 122 ? -18.520 -31.870 7.217   0.81 43.49 ? 119 ILE B CD1 1 
ATOM   2293 N  N   . ARG B 1 123 ? -20.432 -26.889 9.122   1.00 46.12 ? 120 ARG B N   1 
ATOM   2294 C  CA  . ARG B 1 123 ? -21.402 -25.977 9.709   1.00 46.34 ? 120 ARG B CA  1 
ATOM   2295 C  C   . ARG B 1 123 ? -21.263 -24.594 9.075   1.00 46.11 ? 120 ARG B C   1 
ATOM   2296 O  O   . ARG B 1 123 ? -22.227 -24.074 8.518   1.00 46.12 ? 120 ARG B O   1 
ATOM   2297 C  CB  . ARG B 1 123 ? -21.247 -25.892 11.232  1.00 47.47 ? 120 ARG B CB  1 
ATOM   2298 C  CG  . ARG B 1 123 ? -21.970 -27.000 11.986  1.00 48.69 ? 120 ARG B CG  1 
ATOM   2299 C  CD  . ARG B 1 123 ? -21.705 -26.989 13.487  1.00 50.56 ? 120 ARG B CD  1 
ATOM   2300 N  NE  . ARG B 1 123 ? -20.297 -27.250 13.812  1.00 52.33 ? 120 ARG B NE  1 
ATOM   2301 C  CZ  . ARG B 1 123 ? -19.811 -27.505 15.025  1.00 54.09 ? 120 ARG B CZ  1 
ATOM   2302 N  NH1 . ARG B 1 123 ? -20.619 -27.616 16.066  1.00 54.77 ? 120 ARG B NH1 1 
ATOM   2303 N  NH2 . ARG B 1 123 ? -18.511 -27.670 15.194  1.00 54.83 ? 120 ARG B NH2 1 
ATOM   2304 N  N   . LEU B 1 124 ? -20.051 -24.025 9.150   1.00 45.67 ? 121 LEU B N   1 
ATOM   2305 C  CA  . LEU B 1 124 ? -19.785 -22.673 8.681   1.00 44.58 ? 121 LEU B CA  1 
ATOM   2306 C  C   . LEU B 1 124 ? -20.234 -22.533 7.228   1.00 40.74 ? 121 LEU B C   1 
ATOM   2307 O  O   . LEU B 1 124 ? -20.953 -21.597 6.888   1.00 39.40 ? 121 LEU B O   1 
ATOM   2308 C  CB  . LEU B 1 124 ? -18.300 -22.336 8.828   1.00 46.28 ? 121 LEU B CB  1 
ATOM   2309 C  CG  . LEU B 1 124 ? -17.941 -20.870 9.097   1.00 47.26 ? 121 LEU B CG  1 
ATOM   2310 C  CD1 . LEU B 1 124 ? -16.443 -20.683 8.893   1.00 48.11 ? 121 LEU B CD1 1 
ATOM   2311 C  CD2 . LEU B 1 124 ? -18.718 -19.866 8.260   1.00 48.06 ? 121 LEU B CD2 1 
ATOM   2312 N  N   . TYR B 1 125 ? -19.795 -23.467 6.375   1.00 38.20 ? 122 TYR B N   1 
ATOM   2313 C  CA  . TYR B 1 125 ? -20.065 -23.384 4.949   1.00 35.98 ? 122 TYR B CA  1 
ATOM   2314 C  C   . TYR B 1 125 ? -21.559 -23.569 4.690   1.00 35.87 ? 122 TYR B C   1 
ATOM   2315 O  O   . TYR B 1 125 ? -22.122 -22.868 3.849   1.00 35.56 ? 122 TYR B O   1 
ATOM   2316 C  CB  . TYR B 1 125 ? -19.175 -24.379 4.197   0.88 34.64 ? 122 TYR B CB  1 
ATOM   2317 C  CG  . TYR B 1 125 ? -17.683 -24.097 4.320   0.60 33.52 ? 122 TYR B CG  1 
ATOM   2318 C  CD1 . TYR B 1 125 ? -17.202 -22.796 4.436   0.65 33.16 ? 122 TYR B CD1 1 
ATOM   2319 C  CD2 . TYR B 1 125 ? -16.754 -25.132 4.332   0.82 32.99 ? 122 TYR B CD2 1 
ATOM   2320 C  CE1 . TYR B 1 125 ? -15.847 -22.533 4.553   0.72 32.95 ? 122 TYR B CE1 1 
ATOM   2321 C  CE2 . TYR B 1 125 ? -15.395 -24.883 4.449   0.83 32.06 ? 122 TYR B CE2 1 
ATOM   2322 C  CZ  . TYR B 1 125 ? -14.941 -23.579 4.559   0.74 33.00 ? 122 TYR B CZ  1 
ATOM   2323 O  OH  . TYR B 1 125 ? -13.609 -23.307 4.677   0.99 33.98 ? 122 TYR B OH  1 
ATOM   2324 N  N   . GLN B 1 126 ? -22.198 -24.490 5.423   1.00 35.47 ? 123 GLN B N   1 
ATOM   2325 C  CA  . GLN B 1 126 ? -23.634 -24.701 5.300   1.00 35.94 ? 123 GLN B CA  1 
ATOM   2326 C  C   . GLN B 1 126 ? -24.392 -23.430 5.685   1.00 35.63 ? 123 GLN B C   1 
ATOM   2327 O  O   . GLN B 1 126 ? -25.348 -23.062 5.007   1.00 35.97 ? 123 GLN B O   1 
ATOM   2328 C  CB  . GLN B 1 126 ? -24.105 -25.906 6.115   1.00 36.83 ? 123 GLN B CB  1 
ATOM   2329 C  CG  . GLN B 1 126 ? -23.854 -27.246 5.428   1.00 37.17 ? 123 GLN B CG  1 
ATOM   2330 C  CD  . GLN B 1 126 ? -24.180 -28.449 6.288   1.00 37.77 ? 123 GLN B CD  1 
ATOM   2331 O  OE1 . GLN B 1 126 ? -24.357 -28.348 7.507   1.00 38.77 ? 123 GLN B OE1 1 
ATOM   2332 N  NE2 . GLN B 1 126 ? -24.243 -29.615 5.662   1.00 38.72 ? 123 GLN B NE2 1 
ATOM   2333 N  N   . GLN B 1 127 ? -23.952 -22.760 6.758   1.00 36.02 ? 124 GLN B N   1 
ATOM   2334 C  CA  . GLN B 1 127 ? -24.596 -21.543 7.238   1.00 37.39 ? 124 GLN B CA  1 
ATOM   2335 C  C   . GLN B 1 127 ? -24.536 -20.439 6.181   1.00 36.88 ? 124 GLN B C   1 
ATOM   2336 O  O   . GLN B 1 127 ? -25.404 -19.570 6.144   1.00 37.51 ? 124 GLN B O   1 
ATOM   2337 C  CB  . GLN B 1 127 ? -23.944 -21.063 8.535   1.00 38.46 ? 124 GLN B CB  1 
ATOM   2338 C  CG  . GLN B 1 127 ? -24.208 -21.970 9.733   1.00 40.87 ? 124 GLN B CG  1 
ATOM   2339 C  CD  . GLN B 1 127 ? -23.246 -21.754 10.882  1.00 43.30 ? 124 GLN B CD  1 
ATOM   2340 O  OE1 . GLN B 1 127 ? -22.436 -20.821 10.884  1.00 45.67 ? 124 GLN B OE1 1 
ATOM   2341 N  NE2 . GLN B 1 127 ? -23.330 -22.626 11.878  1.00 43.31 ? 124 GLN B NE2 1 
ATOM   2342 N  N   . LEU B 1 128 ? -23.506 -20.479 5.329   1.00 36.34 ? 125 LEU B N   1 
ATOM   2343 C  CA  . LEU B 1 128 ? -23.313 -19.491 4.281   1.00 35.37 ? 125 LEU B CA  1 
ATOM   2344 C  C   . LEU B 1 128 ? -24.016 -19.895 2.987   1.00 33.38 ? 125 LEU B C   1 
ATOM   2345 O  O   . LEU B 1 128 ? -24.140 -19.075 2.082   1.00 34.50 ? 125 LEU B O   1 
ATOM   2346 C  CB  . LEU B 1 128 ? -21.814 -19.305 4.059   1.00 36.18 ? 125 LEU B CB  1 
ATOM   2347 C  CG  . LEU B 1 128 ? -21.069 -18.550 5.163   1.00 38.30 ? 125 LEU B CG  1 
ATOM   2348 C  CD1 . LEU B 1 128 ? -19.569 -18.592 4.931   1.00 38.64 ? 125 LEU B CD1 1 
ATOM   2349 C  CD2 . LEU B 1 128 ? -21.556 -17.114 5.252   1.00 38.93 ? 125 LEU B CD2 1 
ATOM   2350 N  N   . GLY B 1 129 ? -24.445 -21.159 2.885   1.00 32.98 ? 126 GLY B N   1 
ATOM   2351 C  CA  . GLY B 1 129 ? -25.277 -21.585 1.772   1.00 30.89 ? 126 GLY B CA  1 
ATOM   2352 C  C   . GLY B 1 129 ? -24.697 -22.762 0.989   1.00 30.62 ? 126 GLY B C   1 
ATOM   2353 O  O   . GLY B 1 129 ? -25.315 -23.212 0.029   1.00 31.06 ? 126 GLY B O   1 
ATOM   2354 N  N   . PHE B 1 130 ? -23.513 -23.254 1.376   1.00 30.38 ? 127 PHE B N   1 
ATOM   2355 C  CA  . PHE B 1 130 ? -22.925 -24.406 0.705   1.00 30.15 ? 127 PHE B CA  1 
ATOM   2356 C  C   . PHE B 1 130 ? -23.717 -25.665 1.055   1.00 30.42 ? 127 PHE B C   1 
ATOM   2357 O  O   . PHE B 1 130 ? -24.210 -25.792 2.172   1.00 33.27 ? 127 PHE B O   1 
ATOM   2358 C  CB  . PHE B 1 130 ? -21.456 -24.611 1.085   1.00 29.96 ? 127 PHE B CB  1 
ATOM   2359 C  CG  . PHE B 1 130 ? -20.469 -23.680 0.393   1.00 28.56 ? 127 PHE B CG  1 
ATOM   2360 C  CD1 . PHE B 1 130 ? -19.887 -24.036 -0.819  1.00 28.31 ? 127 PHE B CD1 1 
ATOM   2361 C  CD2 . PHE B 1 130 ? -20.132 -22.449 0.949   1.00 28.66 ? 127 PHE B CD2 1 
ATOM   2362 C  CE1 . PHE B 1 130 ? -18.982 -23.195 -1.449  1.00 28.01 ? 127 PHE B CE1 1 
ATOM   2363 C  CE2 . PHE B 1 130 ? -19.223 -21.612 0.316   1.00 28.32 ? 127 PHE B CE2 1 
ATOM   2364 C  CZ  . PHE B 1 130 ? -18.656 -21.982 -0.884  1.00 27.76 ? 127 PHE B CZ  1 
ATOM   2365 N  N   . VAL B 1 131 ? -23.808 -26.599 0.097   1.00 30.72 ? 128 VAL B N   1 
ATOM   2366 C  CA  . VAL B 1 131 ? -24.430 -27.897 0.324   1.00 31.23 ? 128 VAL B CA  1 
ATOM   2367 C  C   . VAL B 1 131 ? -23.571 -28.987 -0.316  1.00 30.32 ? 128 VAL B C   1 
ATOM   2368 O  O   . VAL B 1 131 ? -23.017 -28.794 -1.396  1.00 30.98 ? 128 VAL B O   1 
ATOM   2369 C  CB  . VAL B 1 131 ? -25.872 -27.971 -0.217  1.00 30.94 ? 128 VAL B CB  1 
ATOM   2370 C  CG1 . VAL B 1 131 ? -26.822 -27.085 0.576   1.00 31.20 ? 128 VAL B CG1 1 
ATOM   2371 C  CG2 . VAL B 1 131 ? -25.954 -27.645 -1.706  1.00 31.75 ? 128 VAL B CG2 1 
ATOM   2372 N  N   . PHE B 1 132 ? -23.514 -30.154 0.336   1.00 31.55 ? 129 PHE B N   1 
ATOM   2373 C  CA  . PHE B 1 132 ? -22.894 -31.329 -0.257  1.00 30.33 ? 129 PHE B CA  1 
ATOM   2374 C  C   . PHE B 1 132 ? -23.626 -31.665 -1.553  1.00 30.31 ? 129 PHE B C   1 
ATOM   2375 O  O   . PHE B 1 132 ? -24.853 -31.776 -1.554  1.00 32.64 ? 129 PHE B O   1 
ATOM   2376 C  CB  . PHE B 1 132 ? -22.918 -32.509 0.718   1.00 31.55 ? 129 PHE B CB  1 
ATOM   2377 C  CG  . PHE B 1 132 ? -21.941 -32.371 1.875   1.00 33.42 ? 129 PHE B CG  1 
ATOM   2378 C  CD1 . PHE B 1 132 ? -20.570 -32.401 1.647   1.00 31.99 ? 129 PHE B CD1 1 
ATOM   2379 C  CD2 . PHE B 1 132 ? -22.390 -32.239 3.184   1.00 33.97 ? 129 PHE B CD2 1 
ATOM   2380 C  CE1 . PHE B 1 132 ? -19.674 -32.284 2.697   1.00 33.59 ? 129 PHE B CE1 1 
ATOM   2381 C  CE2 . PHE B 1 132 ? -21.488 -32.126 4.232   1.00 34.41 ? 129 PHE B CE2 1 
ATOM   2382 C  CZ  . PHE B 1 132 ? -20.135 -32.147 3.985   1.00 33.41 ? 129 PHE B CZ  1 
ATOM   2383 N  N   . ASN B 1 133 ? -22.865 -31.824 -2.644  1.00 29.99 ? 130 ASN B N   1 
ATOM   2384 C  CA  . ASN B 1 133 ? -23.442 -32.063 -3.959  1.00 31.39 ? 130 ASN B CA  1 
ATOM   2385 C  C   . ASN B 1 133 ? -23.263 -33.520 -4.395  1.00 31.48 ? 130 ASN B C   1 
ATOM   2386 O  O   . ASN B 1 133 ? -23.553 -33.845 -5.546  1.00 32.82 ? 130 ASN B O   1 
ATOM   2387 C  CB  . ASN B 1 133 ? -22.882 -31.104 -5.004  1.00 33.03 ? 130 ASN B CB  1 
ATOM   2388 C  CG  . ASN B 1 133 ? -21.421 -31.341 -5.296  1.00 33.40 ? 130 ASN B CG  1 
ATOM   2389 O  OD1 . ASN B 1 133 ? -20.789 -32.209 -4.681  1.00 33.17 ? 130 ASN B OD1 1 
ATOM   2390 N  ND2 . ASN B 1 133 ? -20.874 -30.592 -6.241  1.00 34.96 ? 130 ASN B ND2 1 
ATOM   2391 N  N   . GLY B 1 134 ? -22.763 -34.378 -3.493  1.00 30.47 ? 131 GLY B N   1 
ATOM   2392 C  CA  . GLY B 1 134 ? -22.653 -35.808 -3.747  1.00 29.77 ? 131 GLY B CA  1 
ATOM   2393 C  C   . GLY B 1 134 ? -21.399 -36.177 -4.541  1.00 29.81 ? 131 GLY B C   1 
ATOM   2394 O  O   . GLY B 1 134 ? -21.218 -37.340 -4.899  1.00 29.89 ? 131 GLY B O   1 
ATOM   2395 N  N   . GLU B 1 135 ? -20.526 -35.193 -4.798  1.00 28.22 ? 132 GLU B N   1 
ATOM   2396 C  CA  . GLU B 1 135 ? -19.293 -35.433 -5.532  1.00 27.66 ? 132 GLU B CA  1 
ATOM   2397 C  C   . GLU B 1 135 ? -18.146 -35.673 -4.555  1.00 26.33 ? 132 GLU B C   1 
ATOM   2398 O  O   . GLU B 1 135 ? -18.195 -35.236 -3.404  1.00 24.48 ? 132 GLU B O   1 
ATOM   2399 C  CB  . GLU B 1 135 ? -18.958 -34.248 -6.437  1.00 28.49 ? 132 GLU B CB  1 
ATOM   2400 C  CG  . GLU B 1 135 ? -20.022 -33.976 -7.497  1.00 30.82 ? 132 GLU B CG  1 
ATOM   2401 C  CD  . GLU B 1 135 ? -19.815 -32.689 -8.273  1.00 31.81 ? 132 GLU B CD  1 
ATOM   2402 O  OE1 . GLU B 1 135 ? -18.929 -31.894 -7.891  1.00 33.90 ? 132 GLU B OE1 1 
ATOM   2403 O  OE2 . GLU B 1 135 ? -20.545 -32.484 -9.265  1.00 33.84 ? 132 GLU B OE2 1 
ATOM   2404 N  N   . LEU B 1 136 ? -17.119 -36.383 -5.039  1.00 25.84 ? 133 LEU B N   1 
ATOM   2405 C  CA  . LEU B 1 136 ? -15.850 -36.522 -4.344  1.00 25.46 ? 133 LEU B CA  1 
ATOM   2406 C  C   . LEU B 1 136 ? -14.791 -35.745 -5.113  1.00 26.55 ? 133 LEU B C   1 
ATOM   2407 O  O   . LEU B 1 136 ? -14.783 -35.754 -6.343  1.00 28.03 ? 133 LEU B O   1 
ATOM   2408 C  CB  . LEU B 1 136 ? -15.452 -37.988 -4.219  1.00 25.01 ? 133 LEU B CB  1 
ATOM   2409 C  CG  . LEU B 1 136 ? -16.276 -38.811 -3.228  1.00 25.16 ? 133 LEU B CG  1 
ATOM   2410 C  CD1 . LEU B 1 136 ? -15.954 -40.273 -3.414  1.00 25.64 ? 133 LEU B CD1 1 
ATOM   2411 C  CD2 . LEU B 1 136 ? -16.014 -38.369 -1.798  1.00 25.27 ? 133 LEU B CD2 1 
ATOM   2412 N  N   . ASP B 1 137 ? -13.901 -35.081 -4.367  1.00 26.37 ? 134 ASP B N   1 
ATOM   2413 C  CA  . ASP B 1 137 ? -12.771 -34.379 -4.945  1.00 27.46 ? 134 ASP B CA  1 
ATOM   2414 C  C   . ASP B 1 137 ? -11.683 -35.401 -5.263  1.00 27.77 ? 134 ASP B C   1 
ATOM   2415 O  O   . ASP B 1 137 ? -11.867 -36.584 -4.995  1.00 28.06 ? 134 ASP B O   1 
ATOM   2416 C  CB  . ASP B 1 137 ? -12.309 -33.278 -4.006  1.00 26.84 ? 134 ASP B CB  1 
ATOM   2417 C  CG  . ASP B 1 137 ? -11.751 -32.043 -4.690  1.00 27.38 ? 134 ASP B CG  1 
ATOM   2418 O  OD1 . ASP B 1 137 ? -11.522 -32.109 -5.917  1.00 28.61 ? 134 ASP B OD1 1 
ATOM   2419 O  OD2 . ASP B 1 137 ? -11.577 -31.031 -3.990  1.00 27.72 ? 134 ASP B OD2 1 
ATOM   2420 N  N   . THR B 1 138 ? -10.542 -34.941 -5.797  1.00 29.25 ? 135 THR B N   1 
ATOM   2421 C  CA  . THR B 1 138 ? -9.483  -35.841 -6.236  1.00 29.88 ? 135 THR B CA  1 
ATOM   2422 C  C   . THR B 1 138 ? -8.731  -36.391 -5.023  1.00 29.26 ? 135 THR B C   1 
ATOM   2423 O  O   . THR B 1 138 ? -7.995  -37.367 -5.144  1.00 30.34 ? 135 THR B O   1 
ATOM   2424 C  CB  . THR B 1 138 ? -8.518  -35.148 -7.200  1.00 31.01 ? 135 THR B CB  1 
ATOM   2425 O  OG1 . THR B 1 138 ? -7.632  -34.372 -6.399  1.00 31.25 ? 135 THR B OG1 1 
ATOM   2426 C  CG2 . THR B 1 138 ? -9.219  -34.282 -8.232  1.00 31.68 ? 135 THR B CG2 1 
ATOM   2427 N  N   . ASN B 1 139 ? -8.928  -35.757 -3.861  1.00 27.90 ? 136 ASN B N   1 
ATOM   2428 C  CA  . ASN B 1 139 ? -8.246  -36.133 -2.634  1.00 26.86 ? 136 ASN B CA  1 
ATOM   2429 C  C   . ASN B 1 139 ? -9.169  -36.933 -1.716  1.00 26.62 ? 136 ASN B C   1 
ATOM   2430 O  O   . ASN B 1 139 ? -8.808  -37.199 -0.573  1.00 28.59 ? 136 ASN B O   1 
ATOM   2431 C  CB  . ASN B 1 139 ? -7.688  -34.897 -1.936  1.00 26.07 ? 136 ASN B CB  1 
ATOM   2432 C  CG  . ASN B 1 139 ? -8.754  -33.863 -1.662  1.00 25.44 ? 136 ASN B CG  1 
ATOM   2433 O  OD1 . ASN B 1 139 ? -9.954  -34.159 -1.735  1.00 23.77 ? 136 ASN B OD1 1 
ATOM   2434 N  ND2 . ASN B 1 139 ? -8.340  -32.650 -1.336  1.00 25.77 ? 136 ASN B ND2 1 
ATOM   2435 N  N   . GLY B 1 140 ? -10.367 -37.284 -2.209  1.00 25.97 ? 137 GLY B N   1 
ATOM   2436 C  CA  . GLY B 1 140 ? -11.331 -38.061 -1.450  1.00 25.67 ? 137 GLY B CA  1 
ATOM   2437 C  C   . GLY B 1 140 ? -12.217 -37.217 -0.535  1.00 25.43 ? 137 GLY B C   1 
ATOM   2438 O  O   . GLY B 1 140 ? -13.021 -37.766 0.211   1.00 27.11 ? 137 GLY B O   1 
ATOM   2439 N  N   . GLU B 1 141 ? -12.075 -35.885 -0.584  1.00 24.52 ? 138 GLU B N   1 
ATOM   2440 C  CA  . GLU B 1 141 ? -12.914 -35.006 0.219   1.00 24.60 ? 138 GLU B CA  1 
ATOM   2441 C  C   . GLU B 1 141 ? -14.278 -34.846 -0.455  1.00 25.09 ? 138 GLU B C   1 
ATOM   2442 O  O   . GLU B 1 141 ? -14.384 -34.883 -1.680  1.00 26.15 ? 138 GLU B O   1 
ATOM   2443 C  CB  . GLU B 1 141 ? -12.281 -33.636 0.461   1.00 24.80 ? 138 GLU B CB  1 
ATOM   2444 C  CG  . GLU B 1 141 ? -11.064 -33.685 1.380   1.00 25.14 ? 138 GLU B CG  1 
ATOM   2445 C  CD  . GLU B 1 141 ? -10.610 -32.313 1.833   1.00 25.28 ? 138 GLU B CD  1 
ATOM   2446 O  OE1 . GLU B 1 141 ? -10.388 -31.463 0.943   1.00 26.26 ? 138 GLU B OE1 1 
ATOM   2447 O  OE2 . GLU B 1 141 ? -10.483 -32.083 3.055   1.00 26.13 ? 138 GLU B OE2 1 
ATOM   2448 N  N   . ARG B 1 142 ? -15.314 -34.652 0.369   1.00 25.04 ? 139 ARG B N   1 
ATOM   2449 C  CA  . ARG B 1 142 ? -16.669 -34.435 -0.113  1.00 25.27 ? 139 ARG B CA  1 
ATOM   2450 C  C   . ARG B 1 142 ? -16.820 -32.991 -0.577  1.00 24.96 ? 139 ARG B C   1 
ATOM   2451 O  O   . ARG B 1 142 ? -16.463 -32.054 0.138   1.00 25.88 ? 139 ARG B O   1 
ATOM   2452 C  CB  . ARG B 1 142 ? -17.698 -34.768 0.970   1.00 26.50 ? 139 ARG B CB  1 
ATOM   2453 C  CG  . ARG B 1 142 ? -17.902 -36.269 1.105   1.00 27.77 ? 139 ARG B CG  1 
ATOM   2454 C  CD  . ARG B 1 142 ? -18.589 -36.646 2.405   1.00 29.41 ? 139 ARG B CD  1 
ATOM   2455 N  NE  . ARG B 1 142 ? -19.904 -36.022 2.567   1.00 31.22 ? 139 ARG B NE  1 
ATOM   2456 C  CZ  . ARG B 1 142 ? -20.548 -35.865 3.722   1.00 32.85 ? 139 ARG B CZ  1 
ATOM   2457 N  NH1 . ARG B 1 142 ? -19.966 -36.167 4.872   1.00 34.77 ? 139 ARG B NH1 1 
ATOM   2458 N  NH2 . ARG B 1 142 ? -21.776 -35.380 3.727   1.00 33.91 ? 139 ARG B NH2 1 
ATOM   2459 N  N   . VAL B 1 143 ? -17.346 -32.834 -1.794  1.00 24.55 ? 140 VAL B N   1 
ATOM   2460 C  CA  . VAL B 1 143 ? -17.503 -31.527 -2.404  1.00 24.30 ? 140 VAL B CA  1 
ATOM   2461 C  C   . VAL B 1 143 ? -18.775 -30.880 -1.860  1.00 25.44 ? 140 VAL B C   1 
ATOM   2462 O  O   . VAL B 1 143 ? -19.808 -31.531 -1.740  1.00 27.01 ? 140 VAL B O   1 
ATOM   2463 C  CB  . VAL B 1 143 ? -17.537 -31.640 -3.941  1.00 25.12 ? 140 VAL B CB  1 
ATOM   2464 C  CG1 . VAL B 1 143 ? -17.672 -30.276 -4.607  1.00 25.43 ? 140 VAL B CG1 1 
ATOM   2465 C  CG2 . VAL B 1 143 ? -16.324 -32.382 -4.490  1.00 26.21 ? 140 VAL B CG2 1 
ATOM   2466 N  N   . MET B 1 144 ? -18.659 -29.596 -1.509  1.00 25.01 ? 141 MET B N   1 
ATOM   2467 C  CA  . MET B 1 144 ? -19.801 -28.747 -1.220  1.00 25.48 ? 141 MET B CA  1 
ATOM   2468 C  C   . MET B 1 144 ? -19.898 -27.678 -2.302  1.00 26.63 ? 141 MET B C   1 
ATOM   2469 O  O   . MET B 1 144 ? -18.887 -27.277 -2.872  1.00 26.32 ? 141 MET B O   1 
ATOM   2470 C  CB  . MET B 1 144 ? -19.665 -28.072 0.146   1.00 25.59 ? 141 MET B CB  1 
ATOM   2471 C  CG  . MET B 1 144 ? -19.319 -29.039 1.246   1.00 26.32 ? 141 MET B CG  1 
ATOM   2472 S  SD  . MET B 1 144 ? -19.451 -28.327 2.892   1.00 27.95 ? 141 MET B SD  1 
ATOM   2473 C  CE  . MET B 1 144 ? -21.240 -28.176 2.999   1.00 28.08 ? 141 MET B CE  1 
ATOM   2474 N  N   . GLU B 1 145 ? -21.127 -27.213 -2.549  1.00 27.60 ? 142 GLU B N   1 
ATOM   2475 C  CA  . GLU B 1 145 ? -21.415 -26.296 -3.637  1.00 29.40 ? 142 GLU B CA  1 
ATOM   2476 C  C   . GLU B 1 145 ? -22.373 -25.213 -3.150  1.00 29.27 ? 142 GLU B C   1 
ATOM   2477 O  O   . GLU B 1 145 ? -23.326 -25.505 -2.435  1.00 29.64 ? 142 GLU B O   1 
ATOM   2478 C  CB  . GLU B 1 145 ? -22.040 -27.088 -4.783  1.00 31.48 ? 142 GLU B CB  1 
ATOM   2479 C  CG  . GLU B 1 145 ? -22.271 -26.271 -6.049  1.00 33.42 ? 142 GLU B CG  1 
ATOM   2480 C  CD  . GLU B 1 145 ? -23.132 -26.993 -7.068  1.00 36.05 ? 142 GLU B CD  1 
ATOM   2481 O  OE1 . GLU B 1 145 ? -22.924 -28.207 -7.273  1.00 38.07 ? 142 GLU B OE1 1 
ATOM   2482 O  OE2 . GLU B 1 145 ? -24.004 -26.329 -7.664  1.00 38.53 ? 142 GLU B OE2 1 
ATOM   2483 N  N   . TRP B 1 146 ? -22.094 -23.969 -3.550  1.00 28.58 ? 143 TRP B N   1 
ATOM   2484 C  CA  . TRP B 1 146 ? -22.999 -22.859 -3.320  1.00 29.37 ? 143 TRP B CA  1 
ATOM   2485 C  C   . TRP B 1 146 ? -23.502 -22.354 -4.669  1.00 31.32 ? 143 TRP B C   1 
ATOM   2486 O  O   . TRP B 1 146 ? -22.706 -21.895 -5.485  1.00 31.71 ? 143 TRP B O   1 
ATOM   2487 C  CB  . TRP B 1 146 ? -22.299 -21.745 -2.531  1.00 29.67 ? 143 TRP B CB  1 
ATOM   2488 C  CG  . TRP B 1 146 ? -23.145 -20.515 -2.342  1.00 30.25 ? 143 TRP B CG  1 
ATOM   2489 C  CD1 . TRP B 1 146 ? -24.272 -20.397 -1.585  1.00 30.96 ? 143 TRP B CD1 1 
ATOM   2490 C  CD2 . TRP B 1 146 ? -22.905 -19.212 -2.912  1.00 30.21 ? 143 TRP B CD2 1 
ATOM   2491 N  NE1 . TRP B 1 146 ? -24.761 -19.118 -1.654  1.00 31.57 ? 143 TRP B NE1 1 
ATOM   2492 C  CE2 . TRP B 1 146 ? -23.941 -18.369 -2.454  1.00 30.87 ? 143 TRP B CE2 1 
ATOM   2493 C  CE3 . TRP B 1 146 ? -21.914 -18.678 -3.749  1.00 30.13 ? 143 TRP B CE3 1 
ATOM   2494 C  CZ2 . TRP B 1 146 ? -24.013 -17.025 -2.814  1.00 31.87 ? 143 TRP B CZ2 1 
ATOM   2495 C  CZ3 . TRP B 1 146 ? -21.989 -17.350 -4.102  1.00 30.26 ? 143 TRP B CZ3 1 
ATOM   2496 C  CH2 . TRP B 1 146 ? -23.022 -16.536 -3.635  1.00 31.03 ? 143 TRP B CH2 1 
ATOM   2497 N  N   . THR B 1 147 ? -24.814 -22.484 -4.900  1.00 34.25 ? 144 THR B N   1 
ATOM   2498 C  CA  . THR B 1 147 ? -25.443 -21.935 -6.087  1.00 36.26 ? 144 THR B CA  1 
ATOM   2499 C  C   . THR B 1 147 ? -26.134 -20.630 -5.706  1.00 37.53 ? 144 THR B C   1 
ATOM   2500 O  O   . THR B 1 147 ? -27.049 -20.628 -4.879  1.00 39.26 ? 144 THR B O   1 
ATOM   2501 C  CB  . THR B 1 147 ? -26.441 -22.930 -6.678  1.00 38.56 ? 144 THR B CB  1 
ATOM   2502 O  OG1 . THR B 1 147 ? -25.698 -24.093 -7.028  1.00 39.66 ? 144 THR B OG1 1 
ATOM   2503 C  CG2 . THR B 1 147 ? -27.146 -22.377 -7.905  1.00 39.30 ? 144 THR B CG2 1 
ATOM   2504 N  N   A HIS B 1 148 ? -25.703 -19.529 -6.331  0.50 37.69 ? 145 HIS B N   1 
ATOM   2505 N  N   B HIS B 1 148 ? -25.699 -19.533 -6.337  0.50 36.25 ? 145 HIS B N   1 
ATOM   2506 C  CA  A HIS B 1 148 ? -26.316 -18.232 -6.105  0.50 39.14 ? 145 HIS B CA  1 
ATOM   2507 C  CA  B HIS B 1 148 ? -26.302 -18.228 -6.132  0.50 37.08 ? 145 HIS B CA  1 
ATOM   2508 C  C   A HIS B 1 148 ? -27.638 -18.155 -6.877  0.50 39.85 ? 145 HIS B C   1 
ATOM   2509 C  C   B HIS B 1 148 ? -27.551 -18.107 -7.013  0.50 37.26 ? 145 HIS B C   1 
ATOM   2510 O  O   A HIS B 1 148 ? -27.558 -18.227 -8.126  0.50 40.26 ? 145 HIS B O   1 
ATOM   2511 O  O   B HIS B 1 148 ? -27.392 -18.380 -8.225  0.50 35.92 ? 145 HIS B O   1 
ATOM   2512 C  CB  A HIS B 1 148 ? -25.375 -17.099 -6.526  0.50 39.59 ? 145 HIS B CB  1 
ATOM   2513 C  CB  B HIS B 1 148 ? -25.294 -17.117 -6.441  0.50 37.01 ? 145 HIS B CB  1 
ATOM   2514 C  CG  A HIS B 1 148 ? -26.021 -15.760 -6.435  0.50 41.03 ? 145 HIS B CG  1 
ATOM   2515 C  CG  B HIS B 1 148 ? -25.909 -15.760 -6.491  0.50 38.15 ? 145 HIS B CG  1 
ATOM   2516 N  ND1 A HIS B 1 148 ? -26.889 -15.450 -5.410  0.50 42.11 ? 145 HIS B ND1 1 
ATOM   2517 N  ND1 B HIS B 1 148 ? -26.153 -15.086 -7.667  0.50 38.84 ? 145 HIS B ND1 1 
ATOM   2518 C  CD2 A HIS B 1 148 ? -25.958 -14.672 -7.214  0.50 42.00 ? 145 HIS B CD2 1 
ATOM   2519 C  CD2 B HIS B 1 148 ? -26.327 -14.959 -5.507  0.50 39.17 ? 145 HIS B CD2 1 
ATOM   2520 C  CE1 A HIS B 1 148 ? -27.327 -14.212 -5.572  0.50 41.90 ? 145 HIS B CE1 1 
ATOM   2521 C  CE1 B HIS B 1 148 ? -26.704 -13.914 -7.389  0.50 39.45 ? 145 HIS B CE1 1 
ATOM   2522 N  NE2 A HIS B 1 148 ? -26.774 -13.720 -6.661  0.50 42.78 ? 145 HIS B NE2 1 
ATOM   2523 N  NE2 B HIS B 1 148 ? -26.823 -13.819 -6.082  0.50 40.03 ? 145 HIS B NE2 1 
HETATM 2524 C  C   . ACT C 2 .   ? 6.913   -24.963 -7.438  1.00 25.42 ? 201 ACT A C   1 
HETATM 2525 O  O   . ACT C 2 .   ? 7.745   -25.576 -8.157  1.00 27.51 ? 201 ACT A O   1 
HETATM 2526 O  OXT . ACT C 2 .   ? 6.797   -25.144 -6.210  1.00 22.61 ? 201 ACT A OXT 1 
HETATM 2527 C  CH3 . ACT C 2 .   ? 6.003   -23.912 -8.100  1.00 26.12 ? 201 ACT A CH3 1 
HETATM 2528 CL CL  . CL  D 3 .   ? 24.119  -15.847 -0.581  1.00 49.38 ? 202 CL  A CL  1 
HETATM 2529 CL CL  . CL  E 3 .   ? -11.805 -6.374  -0.886  1.00 32.39 ? 203 CL  A CL  1 
HETATM 2530 CL CL  . CL  F 3 .   ? 25.206  -22.339 3.703   0.85 30.84 ? 204 CL  A CL  1 
HETATM 2531 CL CL  . CL  G 3 .   ? 15.849  -35.134 14.722  1.00 43.10 ? 205 CL  A CL  1 
HETATM 2532 NA NA  . NA  H 4 .   ? 10.806  -22.931 -0.139  1.00 29.61 ? 206 NA  A NA  1 
HETATM 2533 K  K   . K   I 5 .   ? -4.137  -23.912 3.657   1.00 29.40 ? 207 K   A K   1 
HETATM 2534 CL CL  . CL  J 3 .   ? -13.182 -17.646 12.703  1.00 42.74 ? 201 CL  B CL  1 
HETATM 2535 CL CL  . CL  K 3 .   ? 11.818  -45.963 -0.553  1.00 35.07 ? 202 CL  B CL  1 
HETATM 2536 CL CL  . CL  L 3 .   ? -5.741  -43.580 -5.444  0.80 39.64 ? 203 CL  B CL  1 
HETATM 2537 CL CL  . CL  M 3 .   ? -7.089  -24.156 4.068   0.75 24.49 ? 204 CL  B CL  1 
HETATM 2538 CL CL  . CL  N 3 .   ? 8.911   -24.144 15.209  0.85 44.38 ? 205 CL  B CL  1 
HETATM 2539 CL CL  . CL  O 3 .   ? -25.633 -30.036 2.702   0.80 28.53 ? 206 CL  B CL  1 
HETATM 2540 CL CL  . CL  P 3 .   ? 0.334   -6.925  6.348   1.00 32.50 ? 207 CL  B CL  1 
HETATM 2541 NA NA  . NA  Q 4 .   ? -1.627  -17.263 -9.704  1.00 23.97 ? 208 NA  B NA  1 
HETATM 2542 NA NA  . NA  R 4 .   ? -10.731 -29.316 0.216   1.00 29.54 ? 209 NA  B NA  1 
HETATM 2543 O  O   . HOH S 6 .   ? 21.287  -39.567 9.649   1.00 30.21 ? 301 HOH A O   1 
HETATM 2544 O  O   . HOH S 6 .   ? 13.331  -23.411 -10.560 1.00 26.34 ? 302 HOH A O   1 
HETATM 2545 O  O   . HOH S 6 .   ? 9.126   -28.429 -18.943 1.00 35.44 ? 303 HOH A O   1 
HETATM 2546 O  O   . HOH S 6 .   ? -3.103  -2.757  4.147   1.00 35.68 ? 304 HOH A O   1 
HETATM 2547 O  O   . HOH S 6 .   ? 26.292  -27.244 3.835   1.00 27.41 ? 305 HOH A O   1 
HETATM 2548 O  O   . HOH S 6 .   ? 26.433  -29.243 -2.084  1.00 44.35 ? 306 HOH A O   1 
HETATM 2549 O  O   . HOH S 6 .   ? 9.487   -15.205 2.237   1.00 25.38 ? 307 HOH A O   1 
HETATM 2550 O  O   . HOH S 6 .   ? -8.553  -21.051 10.114  1.00 37.45 ? 308 HOH A O   1 
HETATM 2551 O  O   . HOH S 6 .   ? 16.020  -42.206 16.628  1.00 41.58 ? 309 HOH A O   1 
HETATM 2552 O  O   . HOH S 6 .   ? 8.693   -28.722 -8.138  1.00 21.03 ? 310 HOH A O   1 
HETATM 2553 O  O   . HOH S 6 .   ? 14.910  -16.687 3.483   1.00 27.13 ? 311 HOH A O   1 
HETATM 2554 O  O   . HOH S 6 .   ? 2.650   -19.523 9.383   1.00 25.78 ? 312 HOH A O   1 
HETATM 2555 O  O   . HOH S 6 .   ? -2.385  -25.507 11.482  1.00 45.31 ? 313 HOH A O   1 
HETATM 2556 O  O   . HOH S 6 .   ? 13.191  -37.197 14.107  1.00 26.74 ? 314 HOH A O   1 
HETATM 2557 O  O   . HOH S 6 .   ? 13.282  -46.558 13.930  1.00 39.12 ? 315 HOH A O   1 
HETATM 2558 O  O   . HOH S 6 .   ? 7.987   -26.079 1.952   1.00 32.82 ? 316 HOH A O   1 
HETATM 2559 O  O   . HOH S 6 .   ? 14.694  -42.668 -8.030  1.00 32.89 ? 317 HOH A O   1 
HETATM 2560 O  O   . HOH S 6 .   ? -9.561  -27.120 -3.793  1.00 12.64 ? 318 HOH A O   1 
HETATM 2561 O  O   . HOH S 6 .   ? 7.840   -4.771  0.414   1.00 22.82 ? 319 HOH A O   1 
HETATM 2562 O  O   . HOH S 6 .   ? -8.583  0.843   9.393   1.00 36.57 ? 320 HOH A O   1 
HETATM 2563 O  O   . HOH S 6 .   ? 7.950   -47.750 12.953  1.00 31.24 ? 321 HOH A O   1 
HETATM 2564 O  O   . HOH S 6 .   ? 24.245  -24.531 -10.547 1.00 34.45 ? 322 HOH A O   1 
HETATM 2565 O  O   . HOH S 6 .   ? 8.933   -9.606  0.821   1.00 25.98 ? 323 HOH A O   1 
HETATM 2566 O  O   . HOH S 6 .   ? 26.704  -34.168 4.192   1.00 38.26 ? 324 HOH A O   1 
HETATM 2567 O  O   . HOH S 6 .   ? -1.435  -38.805 -8.314  1.00 38.37 ? 325 HOH A O   1 
HETATM 2568 O  O   . HOH S 6 .   ? -5.019  -32.745 -13.488 1.00 42.15 ? 326 HOH A O   1 
HETATM 2569 O  O   . HOH S 6 .   ? 12.608  -13.325 -6.156  1.00 34.93 ? 327 HOH A O   1 
HETATM 2570 O  O   . HOH S 6 .   ? 25.885  -26.512 -4.226  1.00 39.42 ? 328 HOH A O   1 
HETATM 2571 O  O   . HOH S 6 .   ? 18.136  -29.747 -10.802 1.00 36.68 ? 329 HOH A O   1 
HETATM 2572 O  O   . HOH S 6 .   ? 19.610  -39.297 11.559  1.00 32.94 ? 330 HOH A O   1 
HETATM 2573 O  O   . HOH S 6 .   ? 12.924  -11.618 0.457   1.00 23.63 ? 331 HOH A O   1 
HETATM 2574 O  O   . HOH S 6 .   ? 9.514   -27.811 5.682   1.00 36.87 ? 332 HOH A O   1 
HETATM 2575 O  O   . HOH S 6 .   ? 11.763  -26.812 5.004   1.00 42.33 ? 333 HOH A O   1 
HETATM 2576 O  O   . HOH S 6 .   ? 1.128   -12.333 10.414  1.00 25.85 ? 334 HOH A O   1 
HETATM 2577 O  O   . HOH S 6 .   ? 21.226  -16.484 0.466   1.00 33.30 ? 335 HOH A O   1 
HETATM 2578 O  O   . HOH S 6 .   ? -3.737  -31.696 11.876  1.00 25.58 ? 336 HOH A O   1 
HETATM 2579 O  O   . HOH S 6 .   ? -1.050  -23.368 -2.769  1.00 20.12 ? 337 HOH A O   1 
HETATM 2580 O  O   . HOH S 6 .   ? -0.423  -45.459 5.776   1.00 18.16 ? 338 HOH A O   1 
HETATM 2581 O  O   . HOH S 6 .   ? 20.380  -17.871 -1.345  1.00 17.88 ? 339 HOH A O   1 
HETATM 2582 O  O   . HOH S 6 .   ? 11.710  -31.970 11.701  1.00 34.60 ? 340 HOH A O   1 
HETATM 2583 O  O   . HOH S 6 .   ? 3.263   -4.090  5.091   1.00 37.42 ? 341 HOH A O   1 
HETATM 2584 O  O   . HOH S 6 .   ? 8.651   -31.005 10.384  1.00 33.26 ? 342 HOH A O   1 
HETATM 2585 O  O   . HOH S 6 .   ? 22.593  -18.509 -9.310  1.00 42.35 ? 343 HOH A O   1 
HETATM 2586 O  O   . HOH S 6 .   ? -1.735  -5.811  -2.476  1.00 29.21 ? 344 HOH A O   1 
HETATM 2587 O  O   . HOH S 6 .   ? 26.545  -34.589 0.164   1.00 41.15 ? 345 HOH A O   1 
HETATM 2588 O  O   . HOH S 6 .   ? 6.170   -9.009  3.632   1.00 25.89 ? 346 HOH A O   1 
HETATM 2589 O  O   . HOH S 6 .   ? 0.955   -36.475 -6.224  1.00 30.13 ? 347 HOH A O   1 
HETATM 2590 O  O   . HOH S 6 .   ? -8.580  -29.612 -0.736  1.00 14.11 ? 348 HOH A O   1 
HETATM 2591 O  O   . HOH S 6 .   ? 17.521  -14.322 -7.478  1.00 28.09 ? 349 HOH A O   1 
HETATM 2592 O  O   . HOH S 6 .   ? 4.126   -28.135 3.282   1.00 29.31 ? 350 HOH A O   1 
HETATM 2593 O  O   . HOH S 6 .   ? -0.556  -4.694  3.823   1.00 37.56 ? 351 HOH A O   1 
HETATM 2594 O  O   . HOH S 6 .   ? 13.540  -13.962 3.852   1.00 54.27 ? 352 HOH A O   1 
HETATM 2595 O  O   . HOH S 6 .   ? 5.014   -11.773 -4.151  1.00 33.11 ? 353 HOH A O   1 
HETATM 2596 O  O   . HOH S 6 .   ? 12.813  -19.728 -8.414  1.00 35.88 ? 354 HOH A O   1 
HETATM 2597 O  O   . HOH S 6 .   ? 21.031  -39.535 -13.346 1.00 39.23 ? 355 HOH A O   1 
HETATM 2598 O  O   . HOH S 6 .   ? -0.122  -35.880 -11.058 1.00 45.53 ? 356 HOH A O   1 
HETATM 2599 O  O   . HOH S 6 .   ? 7.589   -27.897 3.801   1.00 35.50 ? 357 HOH A O   1 
HETATM 2600 O  O   . HOH S 6 .   ? 1.154   -48.332 6.593   1.00 42.78 ? 358 HOH A O   1 
HETATM 2601 O  O   . HOH S 6 .   ? 5.495   -7.243  -5.314  1.00 40.11 ? 359 HOH A O   1 
HETATM 2602 O  O   . HOH S 6 .   ? -0.351  -42.929 13.464  1.00 35.84 ? 360 HOH A O   1 
HETATM 2603 O  O   . HOH S 6 .   ? 11.289  -24.866 -1.603  1.00 22.18 ? 361 HOH A O   1 
HETATM 2604 O  O   . HOH S 6 .   ? 5.472   -50.565 4.629   1.00 29.50 ? 362 HOH A O   1 
HETATM 2605 O  O   . HOH S 6 .   ? 9.738   -29.411 8.660   1.00 41.48 ? 363 HOH A O   1 
HETATM 2606 O  O   . HOH S 6 .   ? 12.048  -24.763 -20.294 1.00 48.57 ? 364 HOH A O   1 
HETATM 2607 O  O   . HOH S 6 .   ? -16.617 -5.331  6.764   1.00 18.76 ? 365 HOH A O   1 
HETATM 2608 O  O   . HOH S 6 .   ? 20.181  -28.049 -12.115 1.00 40.48 ? 366 HOH A O   1 
HETATM 2609 O  O   . HOH S 6 .   ? 10.643  -26.754 7.812   1.00 33.68 ? 367 HOH A O   1 
HETATM 2610 O  O   . HOH S 6 .   ? 24.459  -19.824 7.710   1.00 42.27 ? 368 HOH A O   1 
HETATM 2611 O  O   . HOH S 6 .   ? -4.351  -5.514  -3.207  1.00 26.67 ? 369 HOH A O   1 
HETATM 2612 O  O   . HOH S 6 .   ? -1.802  -36.606 -3.783  1.00 37.07 ? 370 HOH A O   1 
HETATM 2613 O  O   . HOH S 6 .   ? 12.851  -29.698 7.764   1.00 36.95 ? 371 HOH A O   1 
HETATM 2614 O  O   . HOH S 6 .   ? 5.522   -8.261  5.817   1.00 24.18 ? 372 HOH A O   1 
HETATM 2615 O  O   . HOH S 6 .   ? 2.764   -48.804 12.723  1.00 46.12 ? 373 HOH A O   1 
HETATM 2616 O  O   . HOH S 6 .   ? 10.148  -42.818 -4.212  1.00 36.66 ? 374 HOH A O   1 
HETATM 2617 O  O   . HOH S 6 .   ? 16.610  -33.382 -14.798 1.00 40.63 ? 375 HOH A O   1 
HETATM 2618 O  O   . HOH T 6 .   ? -0.720  -15.342 -5.751  1.00 26.46 ? 301 HOH B O   1 
HETATM 2619 O  O   . HOH T 6 .   ? 11.848  -49.561 12.099  1.00 28.04 ? 302 HOH B O   1 
HETATM 2620 O  O   . HOH T 6 .   ? 0.879   -28.212 -3.040  1.00 21.01 ? 303 HOH B O   1 
HETATM 2621 O  O   . HOH T 6 .   ? -1.009  -39.478 10.063  1.00 31.23 ? 304 HOH B O   1 
HETATM 2622 O  O   . HOH T 6 .   ? -9.394  -37.406 1.784   1.00 28.10 ? 305 HOH B O   1 
HETATM 2623 O  O   . HOH T 6 .   ? -19.955 -38.905 -6.340  1.00 21.18 ? 306 HOH B O   1 
HETATM 2624 O  O   . HOH T 6 .   ? -11.862 -31.777 -8.345  1.00 40.48 ? 307 HOH B O   1 
HETATM 2625 O  O   . HOH T 6 .   ? -7.814  -47.313 -0.323  1.00 19.73 ? 308 HOH B O   1 
HETATM 2626 O  O   . HOH T 6 .   ? -11.184 -6.158  -3.630  1.00 46.15 ? 309 HOH B O   1 
HETATM 2627 O  O   . HOH T 6 .   ? -26.543 -24.816 2.773   1.00 27.70 ? 310 HOH B O   1 
HETATM 2628 O  O   . HOH T 6 .   ? 8.854   -22.550 -1.692  1.00 26.99 ? 311 HOH B O   1 
HETATM 2629 O  O   . HOH T 6 .   ? -0.035  -26.143 3.096   1.00 22.42 ? 312 HOH B O   1 
HETATM 2630 O  O   . HOH T 6 .   ? -20.338 -34.212 -2.278  1.00 23.58 ? 313 HOH B O   1 
HETATM 2631 O  O   . HOH T 6 .   ? -6.695  -43.117 3.275   1.00 36.79 ? 314 HOH B O   1 
HETATM 2632 O  O   . HOH T 6 .   ? -20.931 -10.294 -6.480  1.00 27.83 ? 315 HOH B O   1 
HETATM 2633 O  O   . HOH T 6 .   ? -8.372  -3.877  12.828  1.00 40.16 ? 316 HOH B O   1 
HETATM 2634 O  O   . HOH T 6 .   ? -5.813  -35.248 12.821  1.00 41.40 ? 317 HOH B O   1 
HETATM 2635 O  O   . HOH T 6 .   ? -18.098 -22.306 -10.363 1.00 26.41 ? 318 HOH B O   1 
HETATM 2636 O  O   . HOH T 6 .   ? -15.333 -5.572  -9.939  1.00 40.53 ? 319 HOH B O   1 
HETATM 2637 O  O   . HOH T 6 .   ? -9.872  -22.816 8.114   1.00 43.23 ? 320 HOH B O   1 
HETATM 2638 O  O   . HOH T 6 .   ? 9.237   -23.634 1.943   1.00 35.46 ? 321 HOH B O   1 
HETATM 2639 O  O   . HOH T 6 .   ? 0.312   -9.219  14.038  1.00 36.18 ? 322 HOH B O   1 
HETATM 2640 O  O   . HOH T 6 .   ? -23.535 -35.226 5.747   1.00 41.22 ? 323 HOH B O   1 
HETATM 2641 O  O   . HOH T 6 .   ? 1.868   -39.786 -4.770  1.00 23.35 ? 324 HOH B O   1 
HETATM 2642 O  O   . HOH T 6 .   ? 16.456  -46.823 7.424   1.00 21.08 ? 325 HOH B O   1 
HETATM 2643 O  O   . HOH T 6 .   ? 0.032   -47.192 1.763   1.00 26.84 ? 326 HOH B O   1 
HETATM 2644 O  O   . HOH T 6 .   ? -1.684  -12.213 11.212  1.00 31.17 ? 327 HOH B O   1 
HETATM 2645 O  O   . HOH T 6 .   ? 5.902   -18.614 -7.902  1.00 29.56 ? 328 HOH B O   1 
HETATM 2646 O  O   . HOH T 6 .   ? -0.379  -36.991 19.790  1.00 39.29 ? 329 HOH B O   1 
HETATM 2647 O  O   . HOH T 6 .   ? -12.031 -26.867 2.841   1.00 30.62 ? 330 HOH B O   1 
HETATM 2648 O  O   . HOH T 6 .   ? -14.762 -8.979  -7.134  1.00 31.91 ? 331 HOH B O   1 
HETATM 2649 O  O   . HOH T 6 .   ? -20.693 -30.259 11.484  1.00 37.05 ? 332 HOH B O   1 
HETATM 2650 O  O   . HOH T 6 .   ? -16.863 -17.112 11.737  1.00 33.21 ? 333 HOH B O   1 
HETATM 2651 O  O   . HOH T 6 .   ? 9.821   -24.938 -3.433  1.00 33.97 ? 334 HOH B O   1 
HETATM 2652 O  O   . HOH T 6 .   ? -5.634  -35.560 -4.781  1.00 25.40 ? 335 HOH B O   1 
HETATM 2653 O  O   . HOH T 6 .   ? -0.500  -46.769 -1.480  1.00 37.56 ? 336 HOH B O   1 
HETATM 2654 O  O   . HOH T 6 .   ? -9.614  -19.736 -15.626 1.00 42.63 ? 337 HOH B O   1 
HETATM 2655 O  O   . HOH T 6 .   ? -11.762 -25.385 4.907   1.00 42.24 ? 338 HOH B O   1 
HETATM 2656 O  O   . HOH T 6 .   ? -6.190  -32.989 -8.347  1.00 31.04 ? 339 HOH B O   1 
HETATM 2657 O  O   . HOH T 6 .   ? -12.823 -4.919  14.464  1.00 35.32 ? 340 HOH B O   1 
HETATM 2658 O  O   . HOH T 6 .   ? -20.623 -25.807 -12.483 1.00 34.95 ? 341 HOH B O   1 
HETATM 2659 O  O   . HOH T 6 .   ? -8.574  -39.803 -6.423  1.00 38.39 ? 342 HOH B O   1 
HETATM 2660 O  O   . HOH T 6 .   ? -11.002 -2.226  11.612  1.00 34.47 ? 343 HOH B O   1 
HETATM 2661 O  O   . HOH T 6 .   ? 7.425   -27.220 6.324   1.00 33.02 ? 344 HOH B O   1 
HETATM 2662 O  O   . HOH T 6 .   ? -11.381 -39.338 -5.558  1.00 37.56 ? 345 HOH B O   1 
HETATM 2663 O  O   . HOH T 6 .   ? -26.262 -23.827 -2.601  1.00 36.85 ? 346 HOH B O   1 
HETATM 2664 O  O   . HOH T 6 .   ? -14.308 -7.073  -5.202  1.00 42.33 ? 347 HOH B O   1 
HETATM 2665 O  O   . HOH T 6 .   ? -13.513 -38.751 5.295   1.00 33.84 ? 348 HOH B O   1 
HETATM 2666 O  O   . HOH T 6 .   ? -0.144  -16.799 -11.414 1.00 34.57 ? 349 HOH B O   1 
HETATM 2667 O  O   . HOH T 6 .   ? -14.639 -30.948 -9.830  1.00 29.84 ? 350 HOH B O   1 
HETATM 2668 O  O   . HOH T 6 .   ? -23.885 -16.165 1.934   1.00 37.29 ? 351 HOH B O   1 
HETATM 2669 O  O   . HOH T 6 .   ? 10.289  -21.290 8.386   1.00 41.17 ? 352 HOH B O   1 
HETATM 2670 O  O   . HOH T 6 .   ? -2.220  -38.775 12.951  1.00 30.87 ? 353 HOH B O   1 
HETATM 2671 O  O   . HOH T 6 .   ? -21.413 -35.644 0.063   1.00 31.55 ? 354 HOH B O   1 
HETATM 2672 O  O   . HOH T 6 .   ? 5.905   -17.576 -11.266 1.00 33.87 ? 355 HOH B O   1 
HETATM 2673 O  O   . HOH T 6 .   ? -21.918 -11.078 -10.341 1.00 37.21 ? 356 HOH B O   1 
HETATM 2674 O  O   . HOH T 6 .   ? -6.945  -0.841  11.335  1.00 42.08 ? 357 HOH B O   1 
HETATM 2675 O  O   . HOH T 6 .   ? -8.948  -28.853 1.397   1.00 31.51 ? 358 HOH B O   1 
HETATM 2676 O  O   . HOH T 6 .   ? 5.572   -45.734 -4.074  1.00 39.46 ? 359 HOH B O   1 
HETATM 2677 O  O   . HOH T 6 .   ? -11.436 -27.039 -0.957  1.00 19.41 ? 360 HOH B O   1 
HETATM 2678 O  O   . HOH T 6 .   ? -0.871  -6.916  9.734   1.00 24.64 ? 361 HOH B O   1 
HETATM 2679 O  O   . HOH T 6 .   ? -22.887 -13.851 -10.502 1.00 34.69 ? 362 HOH B O   1 
HETATM 2680 O  O   . HOH T 6 .   ? -25.327 -26.158 -4.792  1.00 34.81 ? 363 HOH B O   1 
HETATM 2681 O  O   . HOH T 6 .   ? -27.240 -14.517 -2.493  1.00 32.78 ? 364 HOH B O   1 
HETATM 2682 O  O   . HOH T 6 .   ? -12.106 -37.034 3.096   1.00 30.41 ? 365 HOH B O   1 
HETATM 2683 O  O   . HOH T 6 .   ? -27.125 -18.360 1.444   1.00 55.01 ? 366 HOH B O   1 
HETATM 2684 O  O   . HOH T 6 .   ? -1.888  -3.251  6.357   1.00 44.42 ? 367 HOH B O   1 
HETATM 2685 O  O   . HOH T 6 .   ? 8.537   -53.353 10.025  1.00 23.72 ? 368 HOH B O   1 
HETATM 2686 O  O   . HOH T 6 .   ? -27.962 -19.515 4.190   1.00 43.34 ? 369 HOH B O   1 
HETATM 2687 O  O   . HOH T 6 .   ? -28.611 -17.476 -3.538  1.00 42.45 ? 370 HOH B O   1 
HETATM 2688 O  O   . HOH T 6 .   ? 8.643   -26.342 13.363  1.00 32.04 ? 371 HOH B O   1 
HETATM 2689 O  O   . HOH T 6 .   ? -5.345  -44.071 5.772   1.00 37.02 ? 372 HOH B O   1 
HETATM 2690 O  O   . HOH T 6 .   ? -14.771 -7.198  -1.888  1.00 36.01 ? 373 HOH B O   1 
HETATM 2691 O  O   . HOH T 6 .   ? -0.672  -5.130  11.671  1.00 37.59 ? 374 HOH B O   1 
HETATM 2692 O  O   . HOH T 6 .   ? -9.844  -24.752 2.663   1.00 34.53 ? 375 HOH B O   1 
HETATM 2693 O  O   . HOH T 6 .   ? -1.043  -15.207 -8.982  1.00 28.79 ? 376 HOH B O   1 
HETATM 2694 O  O   . HOH T 6 .   ? -3.333  -45.639 6.638   1.00 25.43 ? 377 HOH B O   1 
HETATM 2695 O  O   . HOH T 6 .   ? -10.451 -25.349 7.971   1.00 29.41 ? 378 HOH B O   1 
HETATM 2696 O  O   . HOH T 6 .   ? -21.070 -37.829 -8.732  1.00 35.38 ? 379 HOH B O   1 
HETATM 2697 O  O   . HOH T 6 .   ? 9.161   -51.284 12.005  1.00 37.17 ? 380 HOH B O   1 
HETATM 2698 O  O   . HOH T 6 .   ? 14.268  -47.128 0.076   1.00 29.07 ? 381 HOH B O   1 
HETATM 2699 O  O   . HOH T 6 .   ? -19.825 -23.348 -12.956 1.00 43.62 ? 382 HOH B O   1 
HETATM 2700 O  O   . HOH T 6 .   ? -12.765 -22.132 8.668   1.00 40.70 ? 383 HOH B O   1 
HETATM 2701 O  O   . HOH T 6 .   ? 16.851  -46.259 1.352   1.00 35.83 ? 384 HOH B O   1 
HETATM 2702 O  O   . HOH T 6 .   ? -15.384 -5.295  -3.934  1.00 36.03 ? 385 HOH B O   1 
HETATM 2703 O  O   . HOH T 6 .   ? 0.944   -9.032  10.309  1.00 29.84 ? 386 HOH B O   1 
HETATM 2704 O  O   . HOH T 6 .   ? 6.531   -15.220 -10.132 1.00 34.09 ? 387 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 3   ? 0.3937 0.4015 0.7787 0.0318  0.0329  -0.0899 0   ALA A N   
2    C  CA  . ALA A 3   ? 0.3836 0.3967 0.7676 0.0161  0.0293  -0.0927 0   ALA A CA  
3    C  C   . ALA A 3   ? 0.3655 0.3481 0.7540 0.0119  0.0204  -0.0916 0   ALA A C   
4    O  O   . ALA A 3   ? 0.3750 0.3421 0.7500 -0.0036 0.0102  -0.1231 0   ALA A O   
5    C  CB  . ALA A 3   ? 0.3911 0.4123 0.7664 0.0057  0.0329  -0.0940 0   ALA A CB  
6    N  N   . MET A 4   ? 0.3345 0.3284 0.7306 0.0143  0.0094  -0.0656 1   MET A N   
7    C  CA  . MET A 4   ? 0.3030 0.2992 0.7135 0.0204  0.0032  -0.0445 1   MET A CA  
8    C  C   . MET A 4   ? 0.2536 0.2719 0.6752 0.0383  -0.0080 -0.0455 1   MET A C   
9    O  O   . MET A 4   ? 0.1989 0.2941 0.6650 0.0322  0.0000  -0.0595 1   MET A O   
10   C  CB  . MET A 4   ? 0.3111 0.2970 0.7449 0.0314  0.0157  -0.0509 1   MET A CB  
11   C  CG  . MET A 4   ? 0.3244 0.3331 0.7622 0.0374  0.0216  -0.0464 1   MET A CG  
12   S  SD  . MET A 4   ? 0.3413 0.3449 0.8138 0.0315  0.0298  -0.0531 1   MET A SD  
13   C  CE  . MET A 4   ? 0.3229 0.3011 0.7960 0.0244  0.0228  -0.0614 1   MET A CE  
14   N  N   . GLU A 5   ? 0.2346 0.2108 0.6290 0.0351  -0.0118 -0.0376 2   GLU A N   
15   C  CA  . GLU A 5   ? 0.2325 0.2046 0.6111 0.0293  -0.0245 -0.0354 2   GLU A CA  
16   C  C   . GLU A 5   ? 0.2075 0.1777 0.5949 0.0117  -0.0072 -0.0251 2   GLU A C   
17   O  O   . GLU A 5   ? 0.2053 0.1490 0.5851 -0.0100 -0.0114 -0.0387 2   GLU A O   
18   C  CB  . GLU A 5   ? 0.2384 0.1989 0.6075 0.0306  -0.0344 -0.0352 2   GLU A CB  
19   C  CG  . GLU A 5   ? 0.2491 0.1960 0.6075 0.0354  -0.0485 -0.0355 2   GLU A CG  
20   C  CD  . GLU A 5   ? 0.2506 0.1886 0.6017 0.0438  -0.0593 -0.0426 2   GLU A CD  
21   O  OE1 . GLU A 5   ? 0.2516 0.2293 0.6204 0.0304  -0.0682 -0.0332 2   GLU A OE1 
22   O  OE2 . GLU A 5   ? 0.2675 0.1795 0.6046 0.0414  -0.0693 -0.0465 2   GLU A OE2 
23   N  N   . ILE A 6   ? 0.1828 0.1603 0.5830 0.0242  0.0003  -0.0174 3   ILE A N   
24   C  CA  . ILE A 6   ? 0.1865 0.1600 0.5712 0.0223  0.0092  -0.0068 3   ILE A CA  
25   C  C   . ILE A 6   ? 0.1620 0.1404 0.5572 0.0221  -0.0037 0.0005  3   ILE A C   
26   O  O   . ILE A 6   ? 0.1585 0.1635 0.5648 0.0433  -0.0040 0.0085  3   ILE A O   
27   C  CB  . ILE A 6   ? 0.2077 0.1669 0.5822 0.0196  0.0248  0.0017  3   ILE A CB  
28   C  CG1 . ILE A 6   ? 0.2249 0.2072 0.5875 0.0101  0.0258  0.0107  3   ILE A CG1 
29   C  CG2 . ILE A 6   ? 0.2025 0.1751 0.5855 0.0387  0.0275  0.0023  3   ILE A CG2 
30   C  CD1 . ILE A 6   ? 0.2282 0.2479 0.5926 -0.0052 0.0247  0.0169  3   ILE A CD1 
31   N  N   . HIS A 7   ? 0.1669 0.1643 0.5505 0.0158  -0.0015 0.0089  4   HIS A N   
32   C  CA  . HIS A 7   ? 0.1698 0.1596 0.5466 0.0169  -0.0002 0.0038  4   HIS A CA  
33   C  C   . HIS A 7   ? 0.1725 0.1547 0.5446 0.0177  -0.0061 0.0065  4   HIS A C   
34   O  O   . HIS A 7   ? 0.1921 0.1561 0.5445 0.0218  -0.0140 0.0041  4   HIS A O   
35   C  CB  . HIS A 7   ? 0.1837 0.1433 0.5499 0.0308  -0.0012 -0.0005 4   HIS A CB  
36   C  CG  . HIS A 7   ? 0.1809 0.1468 0.5514 0.0215  0.0063  -0.0097 4   HIS A CG  
37   N  ND1 . HIS A 7   ? 0.1711 0.1573 0.5540 0.0119  -0.0015 -0.0092 4   HIS A ND1 
38   C  CD2 . HIS A 7   ? 0.1810 0.1452 0.5502 0.0166  0.0036  -0.0162 4   HIS A CD2 
39   C  CE1 . HIS A 7   ? 0.1872 0.1448 0.5477 0.0079  0.0053  -0.0123 4   HIS A CE1 
40   N  NE2 . HIS A 7   ? 0.1792 0.1492 0.5467 0.0057  0.0104  -0.0127 4   HIS A NE2 
41   N  N   . PHE A 8   ? 0.1620 0.1491 0.5439 0.0141  -0.0064 0.0049  5   PHE A N   
42   C  CA  . PHE A 8   ? 0.1750 0.1571 0.5570 0.0180  0.0001  0.0097  5   PHE A CA  
43   C  C   . PHE A 8   ? 0.1528 0.1529 0.5535 0.0268  -0.0034 0.0125  5   PHE A C   
44   O  O   . PHE A 8   ? 0.1779 0.1669 0.5657 0.0491  -0.0025 0.0076  5   PHE A O   
45   C  CB  . PHE A 8   ? 0.2097 0.1613 0.5699 0.0067  -0.0080 0.0139  5   PHE A CB  
46   C  CG  . PHE A 8   ? 0.2212 0.2046 0.5897 -0.0076 -0.0068 0.0279  5   PHE A CG  
47   C  CD1 . PHE A 8   ? 0.2452 0.2103 0.6031 -0.0203 -0.0141 0.0337  5   PHE A CD1 
48   C  CD2 . PHE A 8   ? 0.2292 0.2338 0.6044 -0.0093 -0.0031 0.0322  5   PHE A CD2 
49   C  CE1 . PHE A 8   ? 0.2671 0.2474 0.6018 -0.0204 -0.0049 0.0387  5   PHE A CE1 
50   C  CE2 . PHE A 8   ? 0.2529 0.2486 0.6063 -0.0257 -0.0108 0.0401  5   PHE A CE2 
51   C  CZ  . PHE A 8   ? 0.2731 0.2415 0.6104 -0.0226 -0.0143 0.0386  5   PHE A CZ  
52   N  N   . GLU A 9   ? 0.1658 0.1128 0.5507 0.0432  -0.0068 0.0181  6   GLU A N   
53   C  CA  . GLU A 9   ? 0.1744 0.1327 0.5560 0.0239  -0.0137 0.0241  6   GLU A CA  
54   C  C   . GLU A 9   ? 0.1600 0.1536 0.5563 0.0271  -0.0223 0.0205  6   GLU A C   
55   O  O   . GLU A 9   ? 0.2022 0.1191 0.5486 0.0184  -0.0071 0.0078  6   GLU A O   
56   C  CB  . GLU A 9   ? 0.1781 0.1509 0.5653 0.0144  -0.0101 0.0242  6   GLU A CB  
57   C  CG  . GLU A 9   ? 0.1942 0.1495 0.5778 0.0087  -0.0021 0.0214  6   GLU A CG  
58   C  CD  . GLU A 9   ? 0.2026 0.1805 0.5879 0.0086  -0.0061 0.0126  6   GLU A CD  
59   O  OE1 . GLU A 9   ? 0.2082 0.2346 0.6137 -0.0011 -0.0042 0.0127  6   GLU A OE1 
60   O  OE2 . GLU A 9   ? 0.2191 0.2066 0.6080 -0.0040 0.0157  -0.0037 6   GLU A OE2 
61   N  N   . LYS A 10  ? 0.1750 0.1994 0.5637 0.0368  -0.0343 0.0111  7   LYS A N   
62   C  CA  . LYS A 10  ? 0.2191 0.2174 0.5952 0.0378  -0.0314 -0.0072 7   LYS A CA  
63   C  C   . LYS A 10  ? 0.1973 0.1837 0.6059 0.0361  -0.0326 -0.0149 7   LYS A C   
64   O  O   . LYS A 10  ? 0.2034 0.1859 0.6181 0.0107  -0.0346 -0.0105 7   LYS A O   
65   C  CB  . LYS A 10  ? 0.2675 0.2710 0.6149 0.0416  -0.0288 -0.0025 7   LYS A CB  
66   C  CG  . LYS A 10  ? 0.3230 0.3193 0.6396 0.0416  -0.0386 -0.0079 7   LYS A CG  
67   C  CD  . LYS A 10  ? 0.3686 0.3225 0.6681 0.0343  -0.0362 -0.0040 7   LYS A CD  
68   C  CE  . LYS A 10  ? 0.3836 0.3500 0.6841 0.0345  -0.0325 -0.0009 7   LYS A CE  
69   N  NZ  . LYS A 10  ? 0.4263 0.3618 0.6953 0.0385  -0.0271 -0.0027 7   LYS A NZ  
70   N  N   . VAL A 11  ? 0.1932 0.1912 0.6188 0.0347  -0.0367 -0.0288 8   VAL A N   
71   C  CA  . VAL A 11  ? 0.1873 0.1870 0.6263 0.0223  -0.0349 -0.0287 8   VAL A CA  
72   C  C   . VAL A 11  ? 0.2383 0.2028 0.6349 0.0011  -0.0185 -0.0308 8   VAL A C   
73   O  O   . VAL A 11  ? 0.2708 0.2317 0.6395 -0.0105 -0.0006 -0.0482 8   VAL A O   
74   C  CB  . VAL A 11  ? 0.1841 0.1889 0.6320 0.0243  -0.0453 -0.0269 8   VAL A CB  
75   C  CG1 . VAL A 11  ? 0.1749 0.1803 0.6394 0.0170  -0.0515 -0.0243 8   VAL A CG1 
76   C  CG2 . VAL A 11  ? 0.1829 0.1862 0.6306 0.0219  -0.0465 -0.0251 8   VAL A CG2 
77   N  N   . THR A 12  ? 0.2171 0.1986 0.6464 -0.0131 -0.0124 -0.0099 9   THR A N   
78   C  CA  . THR A 12  ? 0.2223 0.2117 0.6491 -0.0014 0.0000  0.0018  9   THR A CA  
79   C  C   . THR A 12  ? 0.2019 0.1893 0.6472 -0.0067 -0.0056 0.0088  9   THR A C   
80   O  O   . THR A 12  ? 0.2059 0.2120 0.6472 0.0078  -0.0122 -0.0050 9   THR A O   
81   C  CB  . THR A 12  ? 0.2264 0.2155 0.6535 0.0017  0.0116  0.0157  9   THR A CB  
82   O  OG1 . THR A 12  ? 0.2305 0.2049 0.6627 0.0072  0.0130  0.0153  9   THR A OG1 
83   C  CG2 . THR A 12  ? 0.2347 0.2101 0.6511 -0.0068 0.0130  0.0246  9   THR A CG2 
84   N  N   . SER A 13  ? 0.2204 0.2041 0.6399 -0.0040 0.0037  0.0265  10  SER A N   
85   C  CA  . SER A 13  ? 0.1925 0.1944 0.6388 -0.0144 0.0079  0.0300  10  SER A CA  
86   C  C   . SER A 13  ? 0.1890 0.1656 0.6258 -0.0135 -0.0034 0.0312  10  SER A C   
87   O  O   . SER A 13  ? 0.2136 0.1877 0.6197 0.0006  -0.0077 0.0295  10  SER A O   
88   C  CB  . SER A 13  ? 0.2046 0.2025 0.6525 -0.0335 0.0016  0.0375  10  SER A CB  
89   O  OG  . SER A 13  ? 0.2378 0.2763 0.6503 -0.0267 0.0019  0.0522  10  SER A OG  
90   N  N   . ASP A 14  ? 0.1786 0.1888 0.6304 -0.0105 0.0021  0.0144  11  ASP A N   
91   C  CA  . ASP A 14  ? 0.2231 0.1760 0.6326 -0.0116 -0.0078 0.0025  11  ASP A CA  
92   C  C   . ASP A 14  ? 0.1995 0.1411 0.6056 -0.0243 -0.0142 -0.0119 11  ASP A C   
93   O  O   . ASP A 14  ? 0.2163 0.1738 0.6097 -0.0343 -0.0068 -0.0249 11  ASP A O   
94   C  CB  . ASP A 14  ? 0.2378 0.2029 0.6643 0.0086  -0.0044 0.0007  11  ASP A CB  
95   C  CG  . ASP A 14  ? 0.2892 0.2267 0.6917 0.0027  -0.0005 0.0066  11  ASP A CG  
96   O  OD1 . ASP A 14  ? 0.2972 0.2658 0.7144 -0.0342 -0.0006 0.0064  11  ASP A OD1 
97   O  OD2 . ASP A 14  ? 0.3278 0.2589 0.7411 0.0180  -0.0092 0.0189  11  ASP A OD2 
98   N  N   . ASN A 15  ? 0.1531 0.1324 0.5785 -0.0219 -0.0086 0.0048  12  ASN A N   
99   C  CA  . ASN A 15  ? 0.1602 0.1237 0.5588 -0.0124 -0.0114 0.0019  12  ASN A CA  
100  C  C   . ASN A 15  ? 0.1669 0.1219 0.5630 -0.0116 -0.0090 0.0082  12  ASN A C   
101  O  O   . ASN A 15  ? 0.1854 0.1403 0.5486 -0.0089 -0.0037 0.0173  12  ASN A O   
102  C  CB  . ASN A 15  ? 0.1544 0.1146 0.5384 -0.0052 -0.0059 0.0010  12  ASN A CB  
103  C  CG  . ASN A 15  ? 0.1306 0.1477 0.5300 0.0059  -0.0041 0.0014  12  ASN A CG  
104  O  OD1 . ASN A 15  ? 0.1164 0.1716 0.5266 0.0161  -0.0120 -0.0052 12  ASN A OD1 
105  N  ND2 . ASN A 15  ? 0.1299 0.1762 0.5224 -0.0010 -0.0178 -0.0032 12  ASN A ND2 
106  N  N   A ARG A 16  ? 0.1869 0.1434 0.5732 -0.0159 -0.0083 0.0036  13  ARG A N   
107  N  N   B ARG A 16  ? 0.1730 0.1241 0.5682 -0.0194 -0.0087 0.0051  13  ARG A N   
108  C  CA  A ARG A 16  ? 0.2024 0.1456 0.5808 -0.0097 -0.0123 0.0069  13  ARG A CA  
109  C  CA  B ARG A 16  ? 0.1758 0.1229 0.5694 -0.0178 -0.0101 0.0092  13  ARG A CA  
110  C  C   A ARG A 16  ? 0.1865 0.1358 0.5809 -0.0155 -0.0168 0.0035  13  ARG A C   
111  C  C   B ARG A 16  ? 0.1746 0.1227 0.5745 -0.0168 -0.0135 0.0075  13  ARG A C   
112  O  O   A ARG A 16  ? 0.2122 0.1376 0.5869 -0.0202 -0.0170 0.0028  13  ARG A O   
113  O  O   B ARG A 16  ? 0.1983 0.1236 0.5774 -0.0216 -0.0143 0.0056  13  ARG A O   
114  C  CB  A ARG A 16  ? 0.2387 0.1796 0.5859 -0.0006 -0.0098 0.0151  13  ARG A CB  
115  C  CB  B ARG A 16  ? 0.1872 0.1327 0.5673 -0.0130 -0.0109 0.0169  13  ARG A CB  
116  C  CG  A ARG A 16  ? 0.2600 0.2088 0.5960 0.0129  -0.0135 0.0203  13  ARG A CG  
117  C  CG  B ARG A 16  ? 0.1969 0.1377 0.5672 -0.0243 -0.0123 0.0205  13  ARG A CG  
118  C  CD  A ARG A 16  ? 0.2881 0.2378 0.6019 -0.0033 -0.0124 0.0282  13  ARG A CD  
119  C  CD  B ARG A 16  ? 0.2093 0.1526 0.5623 -0.0255 -0.0084 0.0237  13  ARG A CD  
120  N  NE  A ARG A 16  ? 0.3095 0.2541 0.6041 -0.0039 -0.0185 0.0423  13  ARG A NE  
121  N  NE  B ARG A 16  ? 0.2133 0.1508 0.5538 -0.0260 -0.0106 0.0360  13  ARG A NE  
122  C  CZ  A ARG A 16  ? 0.3328 0.2603 0.6111 -0.0069 -0.0228 0.0543  13  ARG A CZ  
123  C  CZ  B ARG A 16  ? 0.2415 0.1693 0.5563 -0.0189 -0.0237 0.0433  13  ARG A CZ  
124  N  NH1 A ARG A 16  ? 0.3504 0.2652 0.6176 -0.0084 -0.0296 0.0544  13  ARG A NH1 
125  N  NH1 B ARG A 16  ? 0.2694 0.1825 0.5516 -0.0136 -0.0333 0.0456  13  ARG A NH1 
126  N  NH2 A ARG A 16  ? 0.3436 0.2574 0.6092 -0.0073 -0.0229 0.0621  13  ARG A NH2 
127  N  NH2 B ARG A 16  ? 0.2635 0.1765 0.5487 -0.0140 -0.0169 0.0562  13  ARG A NH2 
128  N  N   . LYS A 17  ? 0.1902 0.1319 0.5817 -0.0150 -0.0230 0.0048  14  LYS A N   
129  C  CA  . LYS A 17  ? 0.1764 0.1414 0.5781 -0.0071 -0.0228 0.0046  14  LYS A CA  
130  C  C   . LYS A 17  ? 0.1623 0.1334 0.5777 -0.0108 -0.0209 0.0092  14  LYS A C   
131  O  O   . LYS A 17  ? 0.1908 0.1745 0.5749 0.0179  -0.0308 0.0179  14  LYS A O   
132  C  CB  . LYS A 17  ? 0.1734 0.1408 0.5859 -0.0093 -0.0132 0.0018  14  LYS A CB  
133  C  CG  . LYS A 17  ? 0.1782 0.1731 0.6008 -0.0135 0.0007  -0.0034 14  LYS A CG  
134  C  CD  . LYS A 17  ? 0.1818 0.1808 0.6137 -0.0191 0.0071  -0.0079 14  LYS A CD  
135  C  CE  . LYS A 17  ? 0.2001 0.1850 0.6241 -0.0202 0.0186  -0.0126 14  LYS A CE  
136  N  NZ  . LYS A 17  ? 0.1998 0.1967 0.6338 -0.0246 0.0219  -0.0104 14  LYS A NZ  
137  N  N   . ALA A 18  ? 0.1792 0.1345 0.5708 -0.0046 -0.0146 0.0132  15  ALA A N   
138  C  CA  . ALA A 18  ? 0.1569 0.1381 0.5661 -0.0065 -0.0167 0.0087  15  ALA A CA  
139  C  C   . ALA A 18  ? 0.1566 0.1539 0.5542 -0.0175 -0.0155 0.0082  15  ALA A C   
140  O  O   . ALA A 18  ? 0.1584 0.1635 0.5561 -0.0122 -0.0278 0.0140  15  ALA A O   
141  C  CB  . ALA A 18  ? 0.1745 0.1411 0.5672 0.0003  -0.0140 0.0053  15  ALA A CB  
142  N  N   . VAL A 19  ? 0.1353 0.1512 0.5548 -0.0188 -0.0245 0.0039  16  VAL A N   
143  C  CA  . VAL A 19  ? 0.1216 0.1572 0.5564 -0.0146 -0.0253 0.0062  16  VAL A CA  
144  C  C   . VAL A 19  ? 0.1545 0.1493 0.5672 -0.0107 -0.0283 0.0089  16  VAL A C   
145  O  O   . VAL A 19  ? 0.1715 0.1619 0.5847 -0.0033 -0.0247 0.0256  16  VAL A O   
146  C  CB  . VAL A 19  ? 0.1266 0.1679 0.5542 -0.0115 -0.0228 0.0031  16  VAL A CB  
147  C  CG1 . VAL A 19  ? 0.1348 0.1664 0.5540 -0.0112 -0.0196 0.0017  16  VAL A CG1 
148  C  CG2 . VAL A 19  ? 0.1249 0.1739 0.5486 -0.0063 -0.0195 -0.0019 16  VAL A CG2 
149  N  N   . GLU A 20  ? 0.1584 0.1257 0.5723 -0.0032 -0.0327 0.0168  17  GLU A N   
150  C  CA  . GLU A 20  ? 0.1803 0.1366 0.5719 0.0073  -0.0376 0.0159  17  GLU A CA  
151  C  C   . GLU A 20  ? 0.1924 0.1517 0.5769 0.0032  -0.0474 0.0191  17  GLU A C   
152  O  O   . GLU A 20  ? 0.2332 0.1631 0.5861 -0.0066 -0.0486 0.0343  17  GLU A O   
153  C  CB  . GLU A 20  ? 0.1787 0.1302 0.5676 0.0063  -0.0369 0.0068  17  GLU A CB  
154  C  CG  . GLU A 20  ? 0.1835 0.1443 0.5744 0.0080  -0.0327 0.0007  17  GLU A CG  
155  C  CD  . GLU A 20  ? 0.1812 0.1557 0.5792 0.0024  -0.0288 -0.0105 17  GLU A CD  
156  O  OE1 . GLU A 20  ? 0.1731 0.1698 0.6120 -0.0065 -0.0299 -0.0099 17  GLU A OE1 
157  O  OE2 . GLU A 20  ? 0.1805 0.1249 0.5814 0.0180  -0.0106 -0.0232 17  GLU A OE2 
158  N  N   . ASN A 21  ? 0.2126 0.1670 0.5836 0.0043  -0.0526 0.0150  18  ASN A N   
159  C  CA  . ASN A 21  ? 0.2420 0.1971 0.5963 0.0028  -0.0560 0.0106  18  ASN A CA  
160  C  C   . ASN A 21  ? 0.2577 0.2040 0.6108 0.0079  -0.0470 0.0032  18  ASN A C   
161  O  O   . ASN A 21  ? 0.2786 0.2431 0.6077 -0.0039 -0.0500 0.0002  18  ASN A O   
162  C  CB  . ASN A 21  ? 0.2436 0.2109 0.6008 -0.0069 -0.0631 0.0190  18  ASN A CB  
163  C  CG  . ASN A 21  ? 0.2401 0.2346 0.5994 -0.0100 -0.0713 0.0249  18  ASN A CG  
164  O  OD1 . ASN A 21  ? 0.2800 0.2801 0.5990 -0.0069 -0.0761 0.0317  18  ASN A OD1 
165  N  ND2 . ASN A 21  ? 0.2431 0.2112 0.6023 -0.0284 -0.0764 0.0256  18  ASN A ND2 
166  N  N   . LEU A 22  ? 0.2497 0.2081 0.6391 0.0171  -0.0390 0.0024  19  LEU A N   
167  C  CA  . LEU A 22  ? 0.2715 0.2317 0.6659 0.0319  -0.0245 0.0004  19  LEU A CA  
168  C  C   . LEU A 22  ? 0.2897 0.2389 0.6790 0.0306  -0.0218 -0.0060 19  LEU A C   
169  O  O   . LEU A 22  ? 0.2967 0.2104 0.6910 0.0321  -0.0271 0.0094  19  LEU A O   
170  C  CB  . LEU A 22  ? 0.2769 0.2546 0.6758 0.0314  -0.0216 0.0040  19  LEU A CB  
171  C  CG  . LEU A 22  ? 0.3105 0.2853 0.6889 0.0499  -0.0190 0.0057  19  LEU A CG  
172  C  CD1 . LEU A 22  ? 0.2825 0.3193 0.7016 0.0467  -0.0231 -0.0014 19  LEU A CD1 
173  C  CD2 . LEU A 22  ? 0.2984 0.2559 0.6936 0.0696  -0.0178 0.0218  19  LEU A CD2 
174  N  N   . GLN A 23  ? 0.3226 0.2559 0.6974 0.0297  -0.0157 -0.0207 20  GLN A N   
175  C  CA  . GLN A 23  ? 0.3405 0.2759 0.7158 0.0146  -0.0091 -0.0189 20  GLN A CA  
176  C  C   . GLN A 23  ? 0.3392 0.2581 0.7244 0.0182  -0.0080 -0.0122 20  GLN A C   
177  O  O   . GLN A 23  ? 0.3253 0.2385 0.7313 0.0081  -0.0104 -0.0168 20  GLN A O   
178  C  CB  . GLN A 23  ? 0.3753 0.3176 0.7279 0.0001  -0.0074 -0.0293 20  GLN A CB  
179  C  CG  . GLN A 23  ? 0.3971 0.3467 0.7470 -0.0136 -0.0088 -0.0302 20  GLN A CG  
180  C  CD  . GLN A 23  ? 0.4332 0.3931 0.7586 -0.0200 -0.0114 -0.0341 20  GLN A CD  
181  O  OE1 . GLN A 23  ? 0.4412 0.4793 0.7723 -0.0151 -0.0069 -0.0314 20  GLN A OE1 
182  N  NE2 . GLN A 23  ? 0.4295 0.4362 0.7719 -0.0306 -0.0164 -0.0427 20  GLN A NE2 
183  N  N   . VAL A 24  ? 0.3631 0.2579 0.7432 0.0159  -0.0055 -0.0118 21  VAL A N   
184  C  CA  . VAL A 24  ? 0.3809 0.2735 0.7509 0.0060  -0.0138 -0.0125 21  VAL A CA  
185  C  C   . VAL A 24  ? 0.4272 0.3176 0.7583 0.0304  -0.0278 0.0005  21  VAL A C   
186  O  O   . VAL A 24  ? 0.4045 0.3480 0.7508 -0.0196 -0.0409 0.0021  21  VAL A O   
187  C  CB  . VAL A 24  ? 0.3788 0.2695 0.7487 -0.0006 -0.0109 -0.0088 21  VAL A CB  
188  C  CG1 . VAL A 24  ? 0.3561 0.2646 0.7446 -0.0078 0.0012  -0.0060 21  VAL A CG1 
189  C  CG2 . VAL A 24  ? 0.3891 0.2612 0.7504 0.0055  -0.0094 -0.0128 21  VAL A CG2 
190  N  N   . PHE A 25  ? 0.4803 0.4011 0.7681 0.0258  -0.0252 -0.0060 22  PHE A N   
191  C  CA  . PHE A 25  ? 0.5178 0.4342 0.7760 0.0388  -0.0224 0.0084  22  PHE A CA  
192  C  C   . PHE A 25  ? 0.5344 0.4709 0.7823 0.0536  -0.0016 0.0101  22  PHE A C   
193  O  O   . PHE A 25  ? 0.5872 0.5085 0.7980 0.0685  0.0036  0.0323  22  PHE A O   
194  C  CB  . PHE A 25  ? 0.5480 0.4787 0.7803 0.0244  -0.0248 -0.0018 22  PHE A CB  
195  C  CG  . PHE A 25  ? 0.5570 0.4898 0.7776 0.0180  -0.0149 -0.0078 22  PHE A CG  
196  C  CD1 . PHE A 25  ? 0.5602 0.4987 0.7796 0.0144  -0.0045 -0.0141 22  PHE A CD1 
197  C  CD2 . PHE A 25  ? 0.5598 0.5187 0.7696 0.0142  -0.0110 -0.0190 22  PHE A CD2 
198  C  CE1 . PHE A 25  ? 0.5676 0.5108 0.7825 0.0114  -0.0045 -0.0037 22  PHE A CE1 
199  C  CE2 . PHE A 25  ? 0.5629 0.5230 0.7665 0.0219  -0.0075 -0.0157 22  PHE A CE2 
200  C  CZ  . PHE A 25  ? 0.5748 0.5292 0.7712 0.0200  -0.0069 -0.0124 22  PHE A CZ  
201  N  N   . ALA A 26  ? 0.5450 0.4843 0.7813 0.0328  0.0108  0.0059  23  ALA A N   
202  C  CA  . ALA A 26  ? 0.5528 0.4616 0.7796 0.0357  0.0148  -0.0012 23  ALA A CA  
203  C  C   . ALA A 26  ? 0.5569 0.4287 0.7609 0.0340  0.0237  -0.0023 23  ALA A C   
204  O  O   . ALA A 26  ? 0.5834 0.4356 0.7752 0.0182  0.0173  0.0071  23  ALA A O   
205  C  CB  . ALA A 26  ? 0.5559 0.4647 0.7880 0.0383  0.0137  -0.0015 23  ALA A CB  
206  N  N   . GLU A 27  ? 0.5451 0.4118 0.7376 0.0358  0.0394  -0.0139 24  GLU A N   
207  C  CA  . GLU A 27  ? 0.5162 0.3823 0.7318 0.0579  0.0424  -0.0110 24  GLU A CA  
208  C  C   . GLU A 27  ? 0.5158 0.3756 0.7343 0.0722  0.0572  0.0000  24  GLU A C   
209  O  O   . GLU A 27  ? 0.5404 0.3861 0.7351 0.0805  0.0503  -0.0055 24  GLU A O   
210  C  CB  . GLU A 27  ? 0.4939 0.3822 0.7291 0.0571  0.0271  -0.0174 24  GLU A CB  
211  C  CG  . GLU A 27  ? 0.4689 0.3814 0.7279 0.0580  0.0161  -0.0173 24  GLU A CG  
212  C  CD  . GLU A 27  ? 0.4548 0.3856 0.7250 0.0438  -0.0011 -0.0206 24  GLU A CD  
213  O  OE1 . GLU A 27  ? 0.4421 0.4226 0.7360 0.0186  -0.0004 -0.0214 24  GLU A OE1 
214  O  OE2 . GLU A 27  ? 0.4072 0.3687 0.7182 0.0727  -0.0260 -0.0108 24  GLU A OE2 
215  N  N   . GLN A 28  ? 0.4925 0.3813 0.7335 0.0762  0.0746  0.0057  25  GLN A N   
216  C  CA  . GLN A 28  ? 0.4871 0.3613 0.7347 0.0611  0.0745  0.0299  25  GLN A CA  
217  C  C   . GLN A 28  ? 0.4304 0.3328 0.7223 0.0755  0.0875  0.0401  25  GLN A C   
218  O  O   . GLN A 28  ? 0.4289 0.2929 0.7017 0.0794  0.0903  0.0638  25  GLN A O   
219  C  CB  . GLN A 28  ? 0.5329 0.4135 0.7440 0.0468  0.0663  0.0346  25  GLN A CB  
220  C  CG  . GLN A 28  ? 0.5647 0.4452 0.7627 0.0338  0.0570  0.0311  25  GLN A CG  
221  C  CD  . GLN A 28  ? 0.5740 0.4782 0.7754 0.0262  0.0617  0.0287  25  GLN A CD  
222  O  OE1 . GLN A 28  ? 0.5890 0.4968 0.7762 0.0132  0.0566  0.0158  25  GLN A OE1 
223  N  NE2 . GLN A 28  ? 0.5757 0.4938 0.7841 0.0201  0.0600  0.0391  25  GLN A NE2 
224  N  N   . GLN A 29  ? 0.4168 0.3376 0.7260 0.0865  0.0902  0.0241  26  GLN A N   
225  C  CA  . GLN A 29  ? 0.3875 0.3531 0.7324 0.0940  0.0896  0.0215  26  GLN A CA  
226  C  C   . GLN A 29  ? 0.3169 0.2988 0.7080 0.0891  0.0787  0.0054  26  GLN A C   
227  O  O   . GLN A 29  ? 0.2923 0.3093 0.7042 0.1083  0.0716  0.0116  26  GLN A O   
228  C  CB  . GLN A 29  ? 0.4025 0.4071 0.7633 0.0919  0.0987  0.0268  26  GLN A CB  
229  C  CG  . GLN A 29  ? 0.4484 0.4336 0.7876 0.0893  0.1023  0.0403  26  GLN A CG  
230  C  CD  . GLN A 29  ? 0.4960 0.4814 0.8077 0.0861  0.0972  0.0290  26  GLN A CD  
231  O  OE1 . GLN A 29  ? 0.5600 0.5351 0.8283 0.0942  0.0884  0.0342  26  GLN A OE1 
232  N  NE2 . GLN A 29  ? 0.5253 0.5068 0.8244 0.0823  0.0954  0.0383  26  GLN A NE2 
233  N  N   . ALA A 30  ? 0.2933 0.3121 0.6739 0.0619  0.0809  0.0035  27  ALA A N   
234  C  CA  . ALA A 30  ? 0.2844 0.2604 0.6527 0.0542  0.0760  -0.0104 27  ALA A CA  
235  C  C   . ALA A 30  ? 0.2575 0.2262 0.6254 0.0340  0.0629  -0.0124 27  ALA A C   
236  O  O   . ALA A 30  ? 0.3027 0.2242 0.6259 0.0231  0.0531  -0.0279 27  ALA A O   
237  C  CB  . ALA A 30  ? 0.2819 0.2737 0.6567 0.0549  0.0707  -0.0204 27  ALA A CB  
238  N  N   . PHE A 31  ? 0.2569 0.2285 0.6077 0.0267  0.0672  -0.0139 28  PHE A N   
239  C  CA  . PHE A 31  ? 0.2217 0.2182 0.5936 0.0244  0.0547  -0.0078 28  PHE A CA  
240  C  C   . PHE A 31  ? 0.1936 0.2022 0.5665 0.0201  0.0656  -0.0026 28  PHE A C   
241  O  O   . PHE A 31  ? 0.2157 0.1698 0.5606 0.0364  0.0547  0.0007  28  PHE A O   
242  C  CB  . PHE A 31  ? 0.2599 0.2796 0.6062 0.0236  0.0411  -0.0012 28  PHE A CB  
243  C  CG  . PHE A 31  ? 0.2712 0.3267 0.6243 0.0326  0.0543  0.0052  28  PHE A CG  
244  C  CD1 . PHE A 31  ? 0.2588 0.3330 0.6324 0.0242  0.0547  0.0079  28  PHE A CD1 
245  C  CD2 . PHE A 31  ? 0.2771 0.3375 0.6320 0.0264  0.0627  0.0050  28  PHE A CD2 
246  C  CE1 . PHE A 31  ? 0.2769 0.3439 0.6343 0.0247  0.0643  0.0000  28  PHE A CE1 
247  C  CE2 . PHE A 31  ? 0.2774 0.3522 0.6327 0.0261  0.0626  0.0079  28  PHE A CE2 
248  C  CZ  . PHE A 31  ? 0.2731 0.3409 0.6360 0.0258  0.0581  0.0131  28  PHE A CZ  
249  N  N   . ILE A 32  ? 0.2076 0.1920 0.5462 0.0260  0.0797  -0.0036 29  ILE A N   
250  C  CA  . ILE A 32  ? 0.1940 0.1757 0.5371 0.0312  0.0781  -0.0036 29  ILE A CA  
251  C  C   . ILE A 32  ? 0.1875 0.1506 0.5261 0.0354  0.0704  -0.0102 29  ILE A C   
252  O  O   . ILE A 32  ? 0.2136 0.1624 0.5191 0.0192  0.0576  -0.0188 29  ILE A O   
253  C  CB  . ILE A 32  ? 0.2186 0.2000 0.5490 0.0137  0.0866  -0.0047 29  ILE A CB  
254  C  CG1 . ILE A 32  ? 0.2401 0.2276 0.5534 0.0044  0.0848  -0.0060 29  ILE A CG1 
255  C  CG2 . ILE A 32  ? 0.2218 0.2128 0.5532 0.0037  0.0893  -0.0047 29  ILE A CG2 
256  C  CD1 . ILE A 32  ? 0.2573 0.2489 0.5567 0.0039  0.0894  -0.0038 29  ILE A CD1 
257  N  N   . GLU A 33  ? 0.1997 0.1466 0.5118 0.0393  0.0601  -0.0172 30  GLU A N   
258  C  CA  . GLU A 33  ? 0.2036 0.1414 0.5107 0.0291  0.0455  -0.0149 30  GLU A CA  
259  C  C   . GLU A 33  ? 0.1912 0.1257 0.4982 0.0273  0.0352  -0.0195 30  GLU A C   
260  O  O   . GLU A 33  ? 0.2228 0.1700 0.5020 0.0186  0.0330  -0.0159 30  GLU A O   
261  C  CB  . GLU A 33  ? 0.2028 0.1526 0.5275 0.0366  0.0452  0.0002  30  GLU A CB  
262  C  CG  . GLU A 33  ? 0.2139 0.1756 0.5415 0.0345  0.0450  0.0131  30  GLU A CG  
263  C  CD  . GLU A 33  ? 0.2111 0.1993 0.5576 0.0170  0.0445  0.0177  30  GLU A CD  
264  O  OE1 . GLU A 33  ? 0.2133 0.2054 0.5570 0.0045  0.0364  0.0117  30  GLU A OE1 
265  O  OE2 . GLU A 33  ? 0.2083 0.2234 0.5816 0.0293  0.0520  0.0299  30  GLU A OE2 
266  N  N   . SER A 34  ? 0.2063 0.1463 0.4936 0.0274  0.0237  -0.0117 31  SER A N   
267  C  CA  . SER A 34  ? 0.1921 0.1307 0.4964 0.0067  0.0101  -0.0119 31  SER A CA  
268  C  C   . SER A 34  ? 0.1628 0.1256 0.4880 0.0033  0.0095  -0.0043 31  SER A C   
269  O  O   . SER A 34  ? 0.1793 0.1314 0.4851 -0.0007 0.0045  -0.0038 31  SER A O   
270  C  CB  . SER A 34  ? 0.2332 0.1482 0.5069 -0.0135 0.0086  -0.0224 31  SER A CB  
271  O  OG  . SER A 34  ? 0.2826 0.1849 0.5354 -0.0368 0.0133  -0.0101 31  SER A OG  
272  N  N   A MET A 35  ? 0.1566 0.1268 0.4936 0.0056  0.0122  -0.0005 32  MET A N   
273  N  N   B MET A 35  ? 0.1585 0.1231 0.4855 0.0072  0.0096  -0.0054 32  MET A N   
274  C  CA  A MET A 35  ? 0.1442 0.1322 0.4980 0.0079  0.0116  -0.0006 32  MET A CA  
275  C  CA  B MET A 35  ? 0.1480 0.1262 0.4842 0.0096  0.0075  -0.0055 32  MET A CA  
276  C  C   A MET A 35  ? 0.1314 0.1368 0.4902 0.0057  0.0157  -0.0035 32  MET A C   
277  C  C   B MET A 35  ? 0.1317 0.1310 0.4818 0.0063  0.0129  -0.0071 32  MET A C   
278  O  O   A MET A 35  ? 0.1406 0.1519 0.4890 0.0071  0.0167  -0.0109 32  MET A O   
279  O  O   B MET A 35  ? 0.1377 0.1423 0.4804 0.0077  0.0136  -0.0124 32  MET A O   
280  C  CB  A MET A 35  ? 0.1428 0.1380 0.5078 0.0005  0.0077  0.0052  32  MET A CB  
281  C  CB  B MET A 35  ? 0.1508 0.1282 0.4841 0.0069  0.0009  -0.0047 32  MET A CB  
282  C  CG  A MET A 35  ? 0.1392 0.1409 0.5183 0.0072  0.0023  0.0091  32  MET A CG  
283  C  CG  B MET A 35  ? 0.1537 0.1247 0.4853 0.0132  -0.0055 -0.0029 32  MET A CG  
284  S  SD  A MET A 35  ? 0.1371 0.1518 0.5348 0.0085  0.0010  0.0148  32  MET A SD  
285  S  SD  B MET A 35  ? 0.1525 0.1424 0.4887 0.0298  -0.0117 -0.0020 32  MET A SD  
286  C  CE  A MET A 35  ? 0.1274 0.1770 0.5353 0.0136  -0.0029 0.0126  32  MET A CE  
287  C  CE  B MET A 35  ? 0.1617 0.1389 0.4887 0.0227  -0.0095 -0.0015 32  MET A CE  
288  N  N   . ALA A 36  ? 0.1311 0.1221 0.4829 0.0016  0.0158  -0.0133 33  ALA A N   
289  C  CA  . ALA A 36  ? 0.1308 0.1158 0.4777 0.0052  0.0125  -0.0114 33  ALA A CA  
290  C  C   . ALA A 36  ? 0.1332 0.1180 0.4768 0.0047  0.0166  -0.0162 33  ALA A C   
291  O  O   . ALA A 36  ? 0.1511 0.1191 0.4846 -0.0036 0.0172  -0.0313 33  ALA A O   
292  C  CB  . ALA A 36  ? 0.1342 0.1192 0.4836 -0.0028 0.0130  -0.0073 33  ALA A CB  
293  N  N   . GLU A 37  ? 0.1502 0.1166 0.4710 0.0075  0.0154  -0.0092 34  GLU A N   
294  C  CA  . GLU A 37  ? 0.1515 0.1217 0.4733 0.0045  0.0077  0.0030  34  GLU A CA  
295  C  C   . GLU A 37  ? 0.1583 0.1283 0.4734 0.0158  0.0157  0.0069  34  GLU A C   
296  O  O   . GLU A 37  ? 0.1483 0.1389 0.4618 0.0285  0.0137  0.0114  34  GLU A O   
297  C  CB  . GLU A 37  ? 0.1517 0.1288 0.4779 0.0141  0.0043  0.0020  34  GLU A CB  
298  C  CG  . GLU A 37  ? 0.1570 0.1545 0.4802 0.0161  0.0020  0.0124  34  GLU A CG  
299  C  CD  . GLU A 37  ? 0.1667 0.1555 0.4820 0.0134  0.0019  0.0114  34  GLU A CD  
300  O  OE1 . GLU A 37  ? 0.1642 0.1742 0.4874 0.0163  -0.0038 0.0135  34  GLU A OE1 
301  O  OE2 . GLU A 37  ? 0.1767 0.1782 0.4937 0.0085  0.0007  0.0258  34  GLU A OE2 
302  N  N   . ASN A 38  ? 0.1646 0.1574 0.4878 0.0159  0.0240  0.0187  35  ASN A N   
303  C  CA  . ASN A 38  ? 0.1561 0.1567 0.4925 0.0113  0.0234  0.0230  35  ASN A CA  
304  C  C   . ASN A 38  ? 0.1543 0.1632 0.4973 0.0219  0.0350  0.0159  35  ASN A C   
305  O  O   . ASN A 38  ? 0.2066 0.1890 0.4929 0.0221  0.0250  0.0175  35  ASN A O   
306  C  CB  . ASN A 38  ? 0.1556 0.1797 0.4988 0.0232  0.0261  0.0311  35  ASN A CB  
307  C  CG  . ASN A 38  ? 0.1613 0.2214 0.4981 0.0091  0.0186  0.0313  35  ASN A CG  
308  O  OD1 . ASN A 38  ? 0.1655 0.2255 0.5151 0.0275  0.0332  0.0361  35  ASN A OD1 
309  N  ND2 . ASN A 38  ? 0.1876 0.2515 0.4980 0.0086  0.0157  0.0324  35  ASN A ND2 
310  N  N   . LEU A 39  ? 0.1723 0.1519 0.5060 0.0245  0.0365  0.0153  36  LEU A N   
311  C  CA  . LEU A 39  ? 0.1938 0.1527 0.5160 0.0087  0.0340  0.0110  36  LEU A CA  
312  C  C   . LEU A 39  ? 0.1742 0.1474 0.5272 0.0142  0.0328  0.0054  36  LEU A C   
313  O  O   . LEU A 39  ? 0.2238 0.1600 0.5473 0.0293  0.0406  -0.0200 36  LEU A O   
314  C  CB  . LEU A 39  ? 0.1902 0.1553 0.5163 0.0084  0.0375  0.0113  36  LEU A CB  
315  C  CG  . LEU A 39  ? 0.2039 0.1482 0.5213 0.0105  0.0366  0.0094  36  LEU A CG  
316  C  CD1 . LEU A 39  ? 0.1992 0.1479 0.5256 0.0228  0.0463  0.0105  36  LEU A CD1 
317  C  CD2 . LEU A 39  ? 0.2053 0.1905 0.5269 0.0135  0.0342  0.0110  36  LEU A CD2 
318  N  N   . LYS A 40  ? 0.1811 0.1573 0.5326 0.0189  0.0221  0.0012  37  LYS A N   
319  C  CA  . LYS A 40  ? 0.1632 0.1762 0.5404 0.0078  0.0194  0.0043  37  LYS A CA  
320  C  C   . LYS A 40  ? 0.1814 0.2102 0.5454 0.0187  0.0284  0.0083  37  LYS A C   
321  O  O   . LYS A 40  ? 0.2031 0.2059 0.5481 0.0204  0.0252  0.0176  37  LYS A O   
322  C  CB  . LYS A 40  ? 0.1649 0.1629 0.5390 0.0060  0.0160  0.0040  37  LYS A CB  
323  C  CG  . LYS A 40  ? 0.1657 0.1745 0.5406 -0.0035 0.0083  -0.0016 37  LYS A CG  
324  C  CD  . LYS A 40  ? 0.1649 0.1737 0.5373 -0.0059 0.0035  -0.0009 37  LYS A CD  
325  C  CE  . LYS A 40  ? 0.1777 0.1913 0.5437 -0.0161 0.0003  -0.0001 37  LYS A CE  
326  N  NZ  . LYS A 40  ? 0.1769 0.2027 0.5414 -0.0143 -0.0057 -0.0009 37  LYS A NZ  
327  N  N   . GLU A 41  ? 0.1591 0.2149 0.5598 0.0187  0.0367  0.0121  38  GLU A N   
328  C  CA  . GLU A 41  ? 0.1593 0.2494 0.5732 0.0247  0.0344  0.0226  38  GLU A CA  
329  C  C   . GLU A 41  ? 0.1622 0.2937 0.5736 0.0285  0.0484  0.0238  38  GLU A C   
330  O  O   . GLU A 41  ? 0.1904 0.3185 0.5617 0.0452  0.0376  0.0219  38  GLU A O   
331  C  CB  . GLU A 41  ? 0.1591 0.2898 0.5915 -0.0021 0.0274  0.0164  38  GLU A CB  
332  C  CG  . GLU A 41  ? 0.1745 0.2872 0.6167 0.0012  0.0219  0.0089  38  GLU A CG  
333  C  CD  . GLU A 41  ? 0.1626 0.3140 0.6359 -0.0108 0.0154  0.0012  38  GLU A CD  
334  O  OE1 . GLU A 41  ? 0.1621 0.3607 0.6583 -0.0316 0.0116  -0.0046 38  GLU A OE1 
335  O  OE2 . GLU A 41  ? 0.1715 0.3160 0.6585 -0.0113 0.0303  0.0039  38  GLU A OE2 
336  N  N   . SER A 42  ? 0.1905 0.3179 0.5819 0.0307  0.0446  0.0331  39  SER A N   
337  C  CA  . SER A 42  ? 0.1876 0.3354 0.5887 0.0333  0.0477  0.0302  39  SER A CA  
338  C  C   . SER A 42  ? 0.2223 0.3631 0.6010 0.0572  0.0389  0.0101  39  SER A C   
339  O  O   . SER A 42  ? 0.2397 0.4157 0.6062 0.0649  0.0448  0.0182  39  SER A O   
340  C  CB  . SER A 42  ? 0.1831 0.3203 0.5835 0.0175  0.0512  0.0427  39  SER A CB  
341  O  OG  . SER A 42  ? 0.1700 0.3206 0.5721 0.0171  0.0460  0.0490  39  SER A OG  
342  N  N   . ASP A 43  ? 0.2303 0.3697 0.6221 0.0549  0.0330  -0.0095 40  ASP A N   
343  C  CA  . ASP A 43  ? 0.2550 0.3693 0.6431 0.0759  0.0276  -0.0415 40  ASP A CA  
344  C  C   . ASP A 43  ? 0.2975 0.4008 0.6508 0.0591  0.0111  -0.0478 40  ASP A C   
345  O  O   . ASP A 43  ? 0.3169 0.4142 0.6434 0.0325  -0.0061 -0.0500 40  ASP A O   
346  C  CB  . ASP A 43  ? 0.2839 0.3679 0.6549 0.0683  0.0387  -0.0451 40  ASP A CB  
347  C  CG  . ASP A 43  ? 0.3030 0.3823 0.6732 0.0711  0.0366  -0.0546 40  ASP A CG  
348  O  OD1 . ASP A 43  ? 0.3405 0.3908 0.7015 0.0833  0.0281  -0.0440 40  ASP A OD1 
349  O  OD2 . ASP A 43  ? 0.3158 0.3754 0.6902 0.0646  0.0351  -0.0516 40  ASP A OD2 
350  N  N   A GLN A 44  ? 0.2822 0.4036 0.6663 0.0677  -0.0060 -0.0488 41  GLN A N   
351  N  N   B GLN A 44  ? 0.2998 0.4063 0.6681 0.0613  0.0068  -0.0472 41  GLN A N   
352  C  CA  A GLN A 44  ? 0.3051 0.4126 0.6782 0.0665  -0.0140 -0.0509 41  GLN A CA  
353  C  CA  B GLN A 44  ? 0.3196 0.4224 0.6799 0.0608  0.0037  -0.0455 41  GLN A CA  
354  C  C   A GLN A 44  ? 0.3130 0.4368 0.6859 0.0555  -0.0122 -0.0461 41  GLN A C   
355  C  C   B GLN A 44  ? 0.3132 0.4359 0.6865 0.0549  -0.0006 -0.0436 41  GLN A C   
356  O  O   A GLN A 44  ? 0.3168 0.4552 0.6948 0.0688  -0.0348 -0.0392 41  GLN A O   
357  O  O   B GLN A 44  ? 0.3154 0.4444 0.6924 0.0637  -0.0121 -0.0396 41  GLN A O   
358  C  CB  A GLN A 44  ? 0.3034 0.4118 0.6817 0.0656  -0.0187 -0.0586 41  GLN A CB  
359  C  CB  B GLN A 44  ? 0.3353 0.4265 0.6870 0.0607  0.0108  -0.0508 41  GLN A CB  
360  C  CG  A GLN A 44  ? 0.2996 0.3942 0.6802 0.0718  -0.0274 -0.0667 41  GLN A CG  
361  C  CG  B GLN A 44  ? 0.3422 0.4285 0.6915 0.0651  0.0111  -0.0532 41  GLN A CG  
362  C  CD  A GLN A 44  ? 0.2807 0.3976 0.6828 0.0855  -0.0360 -0.0726 41  GLN A CD  
363  C  CD  B GLN A 44  ? 0.3503 0.4306 0.6954 0.0706  0.0170  -0.0574 41  GLN A CD  
364  O  OE1 A GLN A 44  ? 0.2213 0.3877 0.6797 0.0875  -0.0579 -0.0719 41  GLN A OE1 
365  O  OE1 B GLN A 44  ? 0.3383 0.4318 0.6978 0.0701  0.0260  -0.0591 41  GLN A OE1 
366  N  NE2 A GLN A 44  ? 0.3240 0.4079 0.6847 0.0734  -0.0367 -0.0780 41  GLN A NE2 
367  N  NE2 B GLN A 44  ? 0.3678 0.4425 0.6974 0.0729  0.0192  -0.0636 41  GLN A NE2 
368  N  N   . PHE A 45  ? 0.3095 0.4416 0.6951 0.0578  -0.0024 -0.0405 42  PHE A N   
369  C  CA  . PHE A 45  ? 0.3564 0.4585 0.7086 0.0363  0.0159  -0.0391 42  PHE A CA  
370  C  C   . PHE A 45  ? 0.3392 0.4580 0.7083 0.0264  0.0308  -0.0423 42  PHE A C   
371  O  O   . PHE A 45  ? 0.3165 0.4543 0.6830 0.0022  0.0420  -0.0470 42  PHE A O   
372  C  CB  . PHE A 45  ? 0.3731 0.4574 0.7316 0.0352  0.0109  -0.0367 42  PHE A CB  
373  C  CG  . PHE A 45  ? 0.3911 0.4478 0.7548 0.0364  0.0189  -0.0367 42  PHE A CG  
374  C  CD1 . PHE A 45  ? 0.4059 0.4627 0.7675 0.0257  0.0185  -0.0392 42  PHE A CD1 
375  C  CD2 . PHE A 45  ? 0.4004 0.4335 0.7583 0.0331  0.0259  -0.0402 42  PHE A CD2 
376  C  CE1 . PHE A 45  ? 0.4013 0.4563 0.7738 0.0251  0.0312  -0.0507 42  PHE A CE1 
377  C  CE2 . PHE A 45  ? 0.4041 0.4440 0.7679 0.0382  0.0258  -0.0408 42  PHE A CE2 
378  C  CZ  . PHE A 45  ? 0.4162 0.4557 0.7736 0.0296  0.0305  -0.0480 42  PHE A CZ  
379  N  N   . PRO A 46  ? 0.4141 0.5247 0.7205 -0.0084 0.0292  -0.0439 43  PRO A N   
380  C  CA  . PRO A 46  ? 0.4328 0.5069 0.7293 -0.0091 0.0323  -0.0526 43  PRO A CA  
381  C  C   . PRO A 46  ? 0.4320 0.4835 0.7299 -0.0063 0.0273  -0.0485 43  PRO A C   
382  O  O   . PRO A 46  ? 0.4732 0.4225 0.7312 0.0052  0.0558  -0.0707 43  PRO A O   
383  C  CB  . PRO A 46  ? 0.4407 0.5384 0.7282 -0.0166 0.0265  -0.0499 43  PRO A CB  
384  C  CG  . PRO A 46  ? 0.4397 0.5335 0.7309 -0.0052 0.0290  -0.0485 43  PRO A CG  
385  C  CD  . PRO A 46  ? 0.4300 0.5287 0.7310 -0.0045 0.0239  -0.0425 43  PRO A CD  
386  N  N   . GLU A 47  ? 0.4430 0.4711 0.7337 -0.0170 0.0158  -0.0400 44  GLU A N   
387  C  CA  . GLU A 47  ? 0.4300 0.4614 0.7242 -0.0065 0.0007  -0.0278 44  GLU A CA  
388  C  C   . GLU A 47  ? 0.3642 0.4282 0.7162 -0.0138 0.0000  -0.0093 44  GLU A C   
389  O  O   . GLU A 47  ? 0.3537 0.4138 0.7107 -0.0490 0.0008  -0.0211 44  GLU A O   
390  C  CB  . GLU A 47  ? 0.4730 0.4575 0.7422 0.0022  -0.0095 -0.0268 44  GLU A CB  
391  C  CG  . GLU A 47  ? 0.5144 0.4317 0.7470 0.0111  -0.0112 -0.0384 44  GLU A CG  
392  C  CD  . GLU A 47  ? 0.5581 0.4246 0.7479 0.0181  -0.0155 -0.0464 44  GLU A CD  
393  O  OE1 . GLU A 47  ? 0.5680 0.3852 0.7587 0.0503  -0.0276 -0.0419 44  GLU A OE1 
394  O  OE2 . GLU A 47  ? 0.5664 0.4326 0.7529 0.0069  -0.0171 -0.0623 44  GLU A OE2 
395  N  N   . TRP A 48  ? 0.3267 0.3938 0.6914 -0.0527 -0.0127 0.0015  45  TRP A N   
396  C  CA  . TRP A 48  ? 0.2882 0.3384 0.6780 -0.0565 -0.0206 0.0082  45  TRP A CA  
397  C  C   . TRP A 48  ? 0.2591 0.3156 0.6490 -0.0447 -0.0109 -0.0046 45  TRP A C   
398  O  O   . TRP A 48  ? 0.2477 0.3123 0.6546 -0.0370 -0.0151 -0.0022 45  TRP A O   
399  C  CB  . TRP A 48  ? 0.2874 0.3299 0.6788 -0.0569 -0.0277 0.0025  45  TRP A CB  
400  C  CG  . TRP A 48  ? 0.2603 0.3366 0.6877 -0.0674 -0.0415 -0.0007 45  TRP A CG  
401  C  CD1 . TRP A 48  ? 0.2613 0.3363 0.7010 -0.0633 -0.0503 -0.0046 45  TRP A CD1 
402  C  CD2 . TRP A 48  ? 0.2506 0.3294 0.6830 -0.0661 -0.0338 -0.0050 45  TRP A CD2 
403  N  NE1 . TRP A 48  ? 0.2653 0.3372 0.6987 -0.0765 -0.0506 0.0007  45  TRP A NE1 
404  C  CE2 . TRP A 48  ? 0.2723 0.3338 0.6899 -0.0673 -0.0368 -0.0086 45  TRP A CE2 
405  C  CE3 . TRP A 48  ? 0.2494 0.3481 0.6773 -0.0626 -0.0303 -0.0136 45  TRP A CE3 
406  C  CZ2 . TRP A 48  ? 0.2691 0.3265 0.6734 -0.0595 -0.0313 -0.0168 45  TRP A CZ2 
407  C  CZ3 . TRP A 48  ? 0.2387 0.3517 0.6818 -0.0563 -0.0224 -0.0095 45  TRP A CZ3 
408  C  CH2 . TRP A 48  ? 0.2717 0.3494 0.6803 -0.0613 -0.0204 -0.0195 45  TRP A CH2 
409  N  N   . GLU A 49  ? 0.2451 0.2713 0.6333 -0.0415 0.0007  -0.0064 46  GLU A N   
410  C  CA  . GLU A 49  ? 0.2702 0.2621 0.6232 -0.0117 0.0006  -0.0049 46  GLU A CA  
411  C  C   . GLU A 49  ? 0.2171 0.1950 0.5993 -0.0146 0.0050  -0.0079 46  GLU A C   
412  O  O   . GLU A 49  ? 0.1849 0.1753 0.5855 0.0010  0.0336  -0.0154 46  GLU A O   
413  C  CB  . GLU A 49  ? 0.3091 0.2957 0.6506 0.0040  0.0019  -0.0137 46  GLU A CB  
414  C  CG  . GLU A 49  ? 0.3573 0.3187 0.6845 -0.0034 -0.0031 -0.0055 46  GLU A CG  
415  C  CD  . GLU A 49  ? 0.3931 0.3530 0.7046 0.0048  0.0041  -0.0169 46  GLU A CD  
416  O  OE1 . GLU A 49  ? 0.4345 0.3776 0.7210 -0.0010 -0.0033 0.0033  46  GLU A OE1 
417  O  OE2 . GLU A 49  ? 0.4554 0.3818 0.7471 -0.0090 0.0048  -0.0063 46  GLU A OE2 
418  N  N   . SER A 50  ? 0.2187 0.1549 0.5710 -0.0300 -0.0042 -0.0089 47  SER A N   
419  C  CA  . SER A 50  ? 0.2182 0.1513 0.5635 -0.0179 -0.0197 -0.0030 47  SER A CA  
420  C  C   . SER A 50  ? 0.2071 0.1561 0.5497 -0.0109 -0.0247 -0.0106 47  SER A C   
421  O  O   . SER A 50  ? 0.2852 0.1419 0.5589 -0.0018 -0.0218 -0.0085 47  SER A O   
422  C  CB  . SER A 50  ? 0.2203 0.1592 0.5667 -0.0035 -0.0266 0.0112  47  SER A CB  
423  O  OG  . SER A 50  ? 0.2246 0.1772 0.5735 0.0395  -0.0382 0.0248  47  SER A OG  
424  N  N   . ALA A 51  ? 0.1863 0.1418 0.5411 -0.0123 -0.0189 -0.0154 48  ALA A N   
425  C  CA  . ALA A 51  ? 0.1805 0.1545 0.5382 -0.0076 -0.0140 -0.0112 48  ALA A CA  
426  C  C   . ALA A 51  ? 0.1665 0.1379 0.5380 -0.0114 -0.0024 -0.0065 48  ALA A C   
427  O  O   . ALA A 51  ? 0.1552 0.1366 0.5577 -0.0276 -0.0070 -0.0057 48  ALA A O   
428  C  CB  . ALA A 51  ? 0.1895 0.1589 0.5372 0.0106  -0.0141 -0.0169 48  ALA A CB  
429  N  N   . GLY A 52  ? 0.1714 0.1349 0.5393 -0.0083 0.0014  -0.0063 49  GLY A N   
430  C  CA  . GLY A 52  ? 0.1512 0.1344 0.5276 0.0025  0.0050  -0.0036 49  GLY A CA  
431  C  C   . GLY A 52  ? 0.1552 0.1417 0.5298 0.0082  0.0012  -0.0083 49  GLY A C   
432  O  O   . GLY A 52  ? 0.1381 0.1347 0.5392 0.0013  0.0029  -0.0081 49  GLY A O   
433  N  N   . ILE A 53  ? 0.1502 0.1441 0.5265 0.0071  0.0043  -0.0093 50  ILE A N   
434  C  CA  . ILE A 53  ? 0.1514 0.1494 0.5172 0.0000  0.0122  0.0012  50  ILE A CA  
435  C  C   . ILE A 53  ? 0.1505 0.1343 0.5181 0.0041  0.0198  0.0054  50  ILE A C   
436  O  O   . ILE A 53  ? 0.1601 0.1167 0.5279 0.0240  0.0226  -0.0130 50  ILE A O   
437  C  CB  . ILE A 53  ? 0.1722 0.1570 0.5174 -0.0113 0.0145  0.0017  50  ILE A CB  
438  C  CG1 . ILE A 53  ? 0.1661 0.1431 0.5167 -0.0050 0.0072  0.0049  50  ILE A CG1 
439  C  CG2 . ILE A 53  ? 0.1680 0.1758 0.5195 -0.0126 0.0158  -0.0048 50  ILE A CG2 
440  C  CD1 . ILE A 53  ? 0.1765 0.1489 0.5157 -0.0142 0.0071  0.0059  50  ILE A CD1 
441  N  N   . TYR A 54  ? 0.1467 0.1348 0.5205 0.0052  0.0288  0.0142  51  TYR A N   
442  C  CA  . TYR A 54  ? 0.1670 0.1453 0.5146 0.0015  0.0299  0.0220  51  TYR A CA  
443  C  C   . TYR A 54  ? 0.1693 0.1486 0.5166 0.0178  0.0385  0.0238  51  TYR A C   
444  O  O   . TYR A 54  ? 0.1497 0.1502 0.5083 0.0524  0.0273  0.0286  51  TYR A O   
445  C  CB  . TYR A 54  ? 0.1633 0.1319 0.5159 -0.0124 0.0354  0.0255  51  TYR A CB  
446  C  CG  . TYR A 54  ? 0.1683 0.1452 0.5117 -0.0129 0.0329  0.0306  51  TYR A CG  
447  C  CD1 . TYR A 54  ? 0.1823 0.1520 0.5132 -0.0191 0.0335  0.0299  51  TYR A CD1 
448  C  CD2 . TYR A 54  ? 0.1898 0.1608 0.5175 -0.0242 0.0387  0.0346  51  TYR A CD2 
449  C  CE1 . TYR A 54  ? 0.1857 0.1717 0.5114 -0.0170 0.0328  0.0293  51  TYR A CE1 
450  C  CE2 . TYR A 54  ? 0.1868 0.1870 0.5156 -0.0221 0.0381  0.0326  51  TYR A CE2 
451  C  CZ  . TYR A 54  ? 0.1926 0.1771 0.5169 -0.0232 0.0363  0.0351  51  TYR A CZ  
452  O  OH  . TYR A 54  ? 0.1996 0.2364 0.5278 -0.0183 0.0382  0.0361  51  TYR A OH  
453  N  N   . ASP A 55  ? 0.2056 0.1363 0.5279 0.0254  0.0396  0.0254  52  ASP A N   
454  C  CA  . ASP A 55  ? 0.2228 0.1678 0.5405 0.0279  0.0304  0.0260  52  ASP A CA  
455  C  C   . ASP A 55  ? 0.2279 0.1580 0.5547 0.0361  0.0402  0.0328  52  ASP A C   
456  O  O   . ASP A 55  ? 0.2339 0.1579 0.5566 0.0418  0.0441  0.0199  52  ASP A O   
457  C  CB  . ASP A 55  ? 0.2695 0.1900 0.5464 0.0346  0.0252  0.0269  52  ASP A CB  
458  C  CG  . ASP A 55  ? 0.3093 0.2222 0.5526 0.0486  0.0104  0.0296  52  ASP A CG  
459  O  OD1 . ASP A 55  ? 0.3038 0.2412 0.5597 0.0601  0.0016  0.0308  52  ASP A OD1 
460  O  OD2 . ASP A 55  ? 0.3806 0.2634 0.5570 0.0470  0.0009  0.0397  52  ASP A OD2 
461  N  N   . GLY A 56  ? 0.2281 0.1622 0.5641 0.0293  0.0382  0.0312  53  GLY A N   
462  C  CA  . GLY A 56  ? 0.2484 0.1613 0.5809 0.0261  0.0521  0.0354  53  GLY A CA  
463  C  C   . GLY A 56  ? 0.2503 0.1752 0.6010 0.0251  0.0501  0.0361  53  GLY A C   
464  O  O   . GLY A 56  ? 0.2854 0.2250 0.5979 0.0256  0.0508  0.0343  53  GLY A O   
465  N  N   . ASN A 57  ? 0.2696 0.1731 0.6296 0.0173  0.0623  0.0293  54  ASN A N   
466  C  CA  . ASN A 57  ? 0.2536 0.1827 0.6583 0.0092  0.0718  0.0153  54  ASN A CA  
467  C  C   . ASN A 57  ? 0.2482 0.1910 0.6629 0.0185  0.0666  0.0150  54  ASN A C   
468  O  O   . ASN A 57  ? 0.2355 0.2137 0.6761 0.0014  0.0712  0.0034  54  ASN A O   
469  C  CB  . ASN A 57  ? 0.2730 0.1864 0.6835 0.0037  0.0731  0.0151  54  ASN A CB  
470  C  CG  . ASN A 57  ? 0.2824 0.2187 0.6962 0.0043  0.0756  -0.0071 54  ASN A CG  
471  O  OD1 . ASN A 57  ? 0.3063 0.2427 0.7165 -0.0019 0.0689  -0.0103 54  ASN A OD1 
472  N  ND2 . ASN A 57  ? 0.3172 0.2455 0.7066 -0.0181 0.0692  0.0051  54  ASN A ND2 
473  N  N   . GLN A 58  ? 0.2437 0.1922 0.6603 0.0188  0.0666  0.0211  55  GLN A N   
474  C  CA  . GLN A 58  ? 0.2191 0.2150 0.6528 0.0363  0.0737  0.0171  55  GLN A CA  
475  C  C   . GLN A 58  ? 0.2045 0.2052 0.6343 0.0314  0.0707  0.0053  55  GLN A C   
476  O  O   . GLN A 58  ? 0.2055 0.1795 0.6249 0.0137  0.0690  -0.0108 55  GLN A O   
477  C  CB  . GLN A 58  ? 0.2414 0.2578 0.6616 0.0389  0.0789  0.0239  55  GLN A CB  
478  C  CG  . GLN A 58  ? 0.2848 0.2793 0.6712 0.0430  0.0851  0.0248  55  GLN A CG  
479  C  CD  . GLN A 58  ? 0.2922 0.2885 0.6892 0.0505  0.0948  0.0295  55  GLN A CD  
480  O  OE1 . GLN A 58  ? 0.3376 0.3213 0.7045 0.0526  0.1093  0.0509  55  GLN A OE1 
481  N  NE2 . GLN A 58  ? 0.2810 0.3189 0.6934 0.0678  0.1028  0.0352  55  GLN A NE2 
482  N  N   . LEU A 59  ? 0.2062 0.2098 0.6180 0.0283  0.0663  0.0031  56  LEU A N   
483  C  CA  . LEU A 59  ? 0.1874 0.1937 0.6006 0.0274  0.0470  -0.0040 56  LEU A CA  
484  C  C   . LEU A 59  ? 0.2113 0.1967 0.5855 0.0172  0.0521  -0.0057 56  LEU A C   
485  O  O   . LEU A 59  ? 0.2354 0.2191 0.5872 0.0223  0.0585  -0.0076 56  LEU A O   
486  C  CB  . LEU A 59  ? 0.1984 0.1911 0.6009 0.0272  0.0326  -0.0028 56  LEU A CB  
487  C  CG  . LEU A 59  ? 0.2016 0.1988 0.5967 0.0312  0.0198  -0.0015 56  LEU A CG  
488  C  CD1 . LEU A 59  ? 0.1899 0.2138 0.5982 0.0160  0.0162  0.0023  56  LEU A CD1 
489  C  CD2 . LEU A 59  ? 0.1996 0.2344 0.6029 0.0295  0.0132  -0.0012 56  LEU A CD2 
490  N  N   . ILE A 60  ? 0.2037 0.1929 0.5596 0.0154  0.0310  -0.0100 57  ILE A N   
491  C  CA  . ILE A 60  ? 0.2306 0.1663 0.5491 0.0065  0.0304  -0.0099 57  ILE A CA  
492  C  C   . ILE A 60  ? 0.2375 0.1582 0.5338 0.0036  0.0237  -0.0127 57  ILE A C   
493  O  O   . ILE A 60  ? 0.2649 0.1498 0.5318 0.0133  0.0328  -0.0193 57  ILE A O   
494  C  CB  . ILE A 60  ? 0.2302 0.1742 0.5498 0.0146  0.0284  -0.0196 57  ILE A CB  
495  C  CG1 . ILE A 60  ? 0.2334 0.1983 0.5550 0.0133  0.0321  -0.0242 57  ILE A CG1 
496  C  CG2 . ILE A 60  ? 0.2250 0.1720 0.5533 0.0149  0.0284  -0.0141 57  ILE A CG2 
497  C  CD1 . ILE A 60  ? 0.2356 0.1955 0.5592 0.0156  0.0322  -0.0304 57  ILE A CD1 
498  N  N   . GLY A 61  ? 0.2224 0.1547 0.5289 -0.0038 0.0360  0.0009  58  GLY A N   
499  C  CA  . GLY A 61  ? 0.1929 0.1528 0.5220 0.0099  0.0350  0.0027  58  GLY A CA  
500  C  C   . GLY A 61  ? 0.1812 0.1322 0.5138 0.0035  0.0397  0.0106  58  GLY A C   
501  O  O   . GLY A 61  ? 0.1743 0.1254 0.5025 -0.0005 0.0575  0.0204  58  GLY A O   
502  N  N   . TYR A 62  ? 0.1805 0.1356 0.5166 0.0037  0.0321  0.0218  59  TYR A N   
503  C  CA  . TYR A 62  ? 0.1798 0.1382 0.5169 -0.0034 0.0287  0.0245  59  TYR A CA  
504  C  C   . TYR A 62  ? 0.1629 0.1315 0.5087 -0.0003 0.0256  0.0177  59  TYR A C   
505  O  O   . TYR A 62  ? 0.1614 0.1269 0.5125 -0.0053 0.0266  0.0213  59  TYR A O   
506  C  CB  . TYR A 62  ? 0.1819 0.1602 0.5303 -0.0001 0.0307  0.0347  59  TYR A CB  
507  C  CG  . TYR A 62  ? 0.1794 0.1633 0.5402 0.0055  0.0291  0.0502  59  TYR A CG  
508  C  CD1 . TYR A 62  ? 0.1887 0.1817 0.5460 0.0055  0.0209  0.0528  59  TYR A CD1 
509  C  CD2 . TYR A 62  ? 0.1931 0.1676 0.5516 0.0012  0.0248  0.0436  59  TYR A CD2 
510  C  CE1 . TYR A 62  ? 0.1970 0.1950 0.5480 -0.0014 0.0202  0.0613  59  TYR A CE1 
511  C  CE2 . TYR A 62  ? 0.2076 0.1654 0.5540 0.0084  0.0228  0.0496  59  TYR A CE2 
512  C  CZ  . TYR A 62  ? 0.2018 0.1939 0.5545 0.0032  0.0182  0.0563  59  TYR A CZ  
513  O  OH  . TYR A 62  ? 0.2229 0.2421 0.5643 0.0030  0.0161  0.0637  59  TYR A OH  
514  N  N   . ALA A 63  ? 0.1489 0.1266 0.5106 0.0098  0.0314  0.0056  60  ALA A N   
515  C  CA  . ALA A 63  ? 0.1407 0.1453 0.5147 0.0165  0.0340  0.0038  60  ALA A CA  
516  C  C   . ALA A 63  ? 0.1495 0.1468 0.5242 0.0151  0.0269  -0.0060 60  ALA A C   
517  O  O   . ALA A 63  ? 0.1511 0.1331 0.5286 0.0147  0.0332  -0.0080 60  ALA A O   
518  C  CB  . ALA A 63  ? 0.1360 0.1647 0.5131 0.0145  0.0386  0.0084  60  ALA A CB  
519  N  N   A MET A 64  ? 0.1671 0.1496 0.5336 -0.0030 0.0262  -0.0076 61  MET A N   
520  N  N   B MET A 64  ? 0.1598 0.1512 0.5260 0.0116  0.0296  -0.0081 61  MET A N   
521  C  CA  A MET A 64  ? 0.1889 0.1553 0.5436 0.0000  0.0243  -0.0073 61  MET A CA  
522  C  CA  B MET A 64  ? 0.1732 0.1581 0.5298 0.0202  0.0303  -0.0111 61  MET A CA  
523  C  C   A MET A 64  ? 0.1893 0.1523 0.5517 -0.0031 0.0261  -0.0091 61  MET A C   
524  C  C   B MET A 64  ? 0.1809 0.1565 0.5460 0.0057  0.0305  -0.0108 61  MET A C   
525  O  O   A MET A 64  ? 0.2058 0.1543 0.5530 -0.0106 0.0223  -0.0163 61  MET A O   
526  O  O   B MET A 64  ? 0.1981 0.1562 0.5489 -0.0051 0.0336  -0.0165 61  MET A O   
527  C  CB  A MET A 64  ? 0.1875 0.1843 0.5543 0.0090  0.0239  0.0040  61  MET A CB  
528  C  CB  B MET A 64  ? 0.1709 0.1859 0.5236 0.0342  0.0334  -0.0084 61  MET A CB  
529  C  CG  A MET A 64  ? 0.2048 0.2050 0.5605 0.0244  0.0265  0.0115  61  MET A CG  
530  C  CG  B MET A 64  ? 0.1715 0.1989 0.5178 0.0572  0.0391  -0.0091 61  MET A CG  
531  S  SD  A MET A 64  ? 0.2568 0.2617 0.5838 0.0731  0.0161  0.0267  61  MET A SD  
532  S  SD  B MET A 64  ? 0.1947 0.2417 0.5014 0.0910  0.0433  -0.0090 61  MET A SD  
533  C  CE  A MET A 64  ? 0.2755 0.2636 0.5759 0.0524  0.0130  0.0292  61  MET A CE  
534  C  CE  B MET A 64  ? 0.2153 0.2528 0.5036 0.0847  0.0379  -0.0061 61  MET A CE  
535  N  N   . TYR A 65  ? 0.1943 0.1411 0.5585 -0.0014 0.0256  -0.0101 62  TYR A N   
536  C  CA  . TYR A 65  ? 0.2003 0.1655 0.5846 -0.0142 0.0271  -0.0024 62  TYR A CA  
537  C  C   . TYR A 65  ? 0.2145 0.1817 0.5917 -0.0257 0.0328  0.0131  62  TYR A C   
538  O  O   . TYR A 65  ? 0.2220 0.2115 0.6020 -0.0409 0.0245  0.0361  62  TYR A O   
539  C  CB  . TYR A 65  ? 0.2204 0.1793 0.5991 -0.0030 0.0172  -0.0027 62  TYR A CB  
540  C  CG  . TYR A 65  ? 0.2356 0.1852 0.6217 0.0083  0.0046  -0.0174 62  TYR A CG  
541  C  CD1 . TYR A 65  ? 0.2431 0.2215 0.6286 0.0113  -0.0073 -0.0174 62  TYR A CD1 
542  C  CD2 . TYR A 65  ? 0.2288 0.2025 0.6333 0.0072  0.0116  -0.0106 62  TYR A CD2 
543  C  CE1 . TYR A 65  ? 0.2788 0.2157 0.6415 0.0145  -0.0019 -0.0120 62  TYR A CE1 
544  C  CE2 . TYR A 65  ? 0.3023 0.2142 0.6470 -0.0009 -0.0020 -0.0154 62  TYR A CE2 
545  C  CZ  . TYR A 65  ? 0.3126 0.2089 0.6467 0.0037  -0.0032 -0.0157 62  TYR A CZ  
546  O  OH  . TYR A 65  ? 0.3648 0.2306 0.6708 -0.0357 -0.0186 -0.0232 62  TYR A OH  
547  N  N   . GLY A 66  ? 0.2227 0.2321 0.6118 -0.0257 0.0369  0.0131  63  GLY A N   
548  C  CA  . GLY A 66  ? 0.2386 0.2465 0.6167 -0.0436 0.0452  0.0042  63  GLY A CA  
549  C  C   . GLY A 66  ? 0.2263 0.2831 0.6398 -0.0559 0.0501  0.0025  63  GLY A C   
550  O  O   . GLY A 66  ? 0.2480 0.2676 0.6111 -0.0654 0.0752  0.0188  63  GLY A O   
551  N  N   . ARG A 67  ? 0.2768 0.3677 0.6670 -0.0654 0.0348  -0.0032 64  ARG A N   
552  C  CA  . ARG A 67  ? 0.3061 0.4284 0.7050 -0.0746 0.0236  0.0107  64  ARG A CA  
553  C  C   . ARG A 67  ? 0.3260 0.4823 0.7457 -0.0667 -0.0004 0.0210  64  ARG A C   
554  O  O   . ARG A 67  ? 0.3034 0.5046 0.7634 -0.0825 0.0075  0.0140  64  ARG A O   
555  C  CB  . ARG A 67  ? 0.3478 0.4664 0.7167 -0.0529 0.0163  0.0070  64  ARG A CB  
556  C  CG  . ARG A 67  ? 0.3779 0.4884 0.7245 -0.0405 0.0111  0.0142  64  ARG A CG  
557  C  CD  . ARG A 67  ? 0.4121 0.5090 0.7377 -0.0271 0.0011  0.0073  64  ARG A CD  
558  N  NE  . ARG A 67  ? 0.4457 0.5221 0.7472 -0.0111 -0.0096 0.0119  64  ARG A NE  
559  C  CZ  . ARG A 67  ? 0.4809 0.5548 0.7635 -0.0032 -0.0227 0.0192  64  ARG A CZ  
560  N  NH1 . ARG A 67  ? 0.4861 0.5574 0.7742 0.0075  -0.0325 0.0102  64  ARG A NH1 
561  N  NH2 . ARG A 67  ? 0.4887 0.5582 0.7691 -0.0071 -0.0260 0.0258  64  ARG A NH2 
562  N  N   . TRP A 68  ? 0.3744 0.5214 0.7980 -0.0738 -0.0125 0.0067  65  TRP A N   
563  C  CA  . TRP A 68  ? 0.4179 0.5627 0.8384 -0.0607 -0.0231 0.0199  65  TRP A CA  
564  C  C   . TRP A 68  ? 0.4715 0.6287 0.8530 -0.0718 -0.0259 0.0153  65  TRP A C   
565  O  O   . TRP A 68  ? 0.4681 0.6518 0.8581 -0.0991 -0.0046 0.0116  65  TRP A O   
566  C  CB  . TRP A 68  ? 0.4569 0.5677 0.8651 -0.0536 -0.0278 0.0187  65  TRP A CB  
567  C  CG  . TRP A 68  ? 0.5016 0.5775 0.9027 -0.0426 -0.0391 0.0257  65  TRP A CG  
568  C  CD1 . TRP A 68  ? 0.5173 0.5833 0.9272 -0.0358 -0.0410 0.0290  65  TRP A CD1 
569  C  CD2 . TRP A 68  ? 0.5247 0.5799 0.9283 -0.0302 -0.0541 0.0338  65  TRP A CD2 
570  N  NE1 . TRP A 68  ? 0.5293 0.5943 0.9320 -0.0284 -0.0528 0.0288  65  TRP A NE1 
571  C  CE2 . TRP A 68  ? 0.5295 0.5750 0.9348 -0.0319 -0.0519 0.0269  65  TRP A CE2 
572  C  CE3 . TRP A 68  ? 0.5351 0.5835 0.9378 -0.0338 -0.0551 0.0376  65  TRP A CE3 
573  C  CZ2 . TRP A 68  ? 0.5419 0.5818 0.9396 -0.0283 -0.0575 0.0280  65  TRP A CZ2 
574  C  CZ3 . TRP A 68  ? 0.5460 0.5841 0.9380 -0.0284 -0.0578 0.0370  65  TRP A CZ3 
575  C  CH2 . TRP A 68  ? 0.5472 0.5789 0.9402 -0.0296 -0.0612 0.0287  65  TRP A CH2 
576  N  N   . GLN A 69  ? 0.5249 0.6808 0.8665 -0.0539 -0.0277 0.0224  66  GLN A N   
577  C  CA  . GLN A 69  ? 0.5739 0.7226 0.8815 -0.0535 -0.0216 0.0202  66  GLN A CA  
578  C  C   . GLN A 69  ? 0.5932 0.7201 0.8765 -0.0552 -0.0064 -0.0017 66  GLN A C   
579  O  O   . GLN A 69  ? 0.6342 0.7683 0.8841 -0.0511 0.0033  -0.0250 66  GLN A O   
580  C  CB  . GLN A 69  ? 0.5955 0.7440 0.8964 -0.0458 -0.0289 0.0346  66  GLN A CB  
581  C  CG  . GLN A 69  ? 0.5925 0.7743 0.9009 -0.0384 -0.0287 0.0447  66  GLN A CG  
582  C  CD  . GLN A 69  ? 0.6092 0.7824 0.9107 -0.0330 -0.0331 0.0502  66  GLN A CD  
583  O  OE1 . GLN A 69  ? 0.6176 0.8111 0.9047 -0.0143 -0.0194 0.0588  66  GLN A OE1 
584  N  NE2 . GLN A 69  ? 0.6135 0.7895 0.9154 -0.0293 -0.0366 0.0557  66  GLN A NE2 
585  N  N   . ASP A 70  ? 0.6260 0.6600 0.8663 -0.0524 0.0047  -0.0135 67  ASP A N   
586  C  CA  . ASP A 70  ? 0.6185 0.6034 0.8438 -0.0261 0.0117  -0.0207 67  ASP A CA  
587  C  C   . ASP A 70  ? 0.6091 0.5623 0.8084 -0.0406 0.0382  -0.0254 67  ASP A C   
588  O  O   . ASP A 70  ? 0.6216 0.5926 0.7997 -0.0326 0.0521  -0.0293 67  ASP A O   
589  C  CB  . ASP A 70  ? 0.6212 0.5880 0.8481 -0.0187 -0.0050 -0.0199 67  ASP A CB  
590  C  CG  . ASP A 70  ? 0.6236 0.5761 0.8440 -0.0041 -0.0192 -0.0297 67  ASP A CG  
591  O  OD1 . ASP A 70  ? 0.6363 0.5783 0.8526 -0.0032 -0.0277 -0.0359 67  ASP A OD1 
592  O  OD2 . ASP A 70  ? 0.6315 0.5585 0.8519 0.0085  -0.0335 -0.0312 67  ASP A OD2 
593  N  N   . GLY A 71  ? 0.5894 0.5164 0.7747 -0.0158 0.0519  -0.0460 68  GLY A N   
594  C  CA  . GLY A 71  ? 0.5612 0.4665 0.7330 -0.0370 0.0597  -0.0537 68  GLY A CA  
595  C  C   . GLY A 71  ? 0.5149 0.3902 0.7091 -0.0348 0.0777  -0.0608 68  GLY A C   
596  O  O   . GLY A 71  ? 0.5316 0.3864 0.7088 -0.0294 0.0959  -0.0763 68  GLY A O   
597  N  N   . ARG A 72  ? 0.4336 0.3147 0.6882 -0.0496 0.0773  -0.0359 69  ARG A N   
598  C  CA  . ARG A 72  ? 0.3684 0.2628 0.6685 -0.0457 0.0792  -0.0328 69  ARG A CA  
599  C  C   . ARG A 72  ? 0.3171 0.2332 0.6506 -0.0219 0.0689  -0.0323 69  ARG A C   
600  O  O   . ARG A 72  ? 0.3194 0.2192 0.6506 0.0005  0.0481  -0.0178 69  ARG A O   
601  C  CB  . ARG A 72  ? 0.3706 0.2382 0.6765 -0.0507 0.0836  -0.0221 69  ARG A CB  
602  C  CG  . ARG A 72  ? 0.3775 0.2558 0.6846 -0.0604 0.0877  -0.0273 69  ARG A CG  
603  C  CD  . ARG A 72  ? 0.3926 0.2744 0.6913 -0.0611 0.0883  -0.0395 69  ARG A CD  
604  N  NE  . ARG A 72  ? 0.4094 0.2654 0.6986 -0.0718 0.1016  -0.0449 69  ARG A NE  
605  C  CZ  . ARG A 72  ? 0.4312 0.2718 0.7010 -0.0709 0.1036  -0.0582 69  ARG A CZ  
606  N  NH1 . ARG A 72  ? 0.4333 0.2655 0.7077 -0.0652 0.1055  -0.0644 69  ARG A NH1 
607  N  NH2 . ARG A 72  ? 0.4372 0.2840 0.6983 -0.0697 0.1141  -0.0453 69  ARG A NH2 
608  N  N   . VAL A 73  ? 0.2729 0.2078 0.6394 -0.0150 0.0683  -0.0455 70  VAL A N   
609  C  CA  . VAL A 73  ? 0.2557 0.2063 0.6300 -0.0109 0.0619  -0.0519 70  VAL A CA  
610  C  C   . VAL A 73  ? 0.2127 0.1938 0.6198 -0.0055 0.0534  -0.0509 70  VAL A C   
611  O  O   . VAL A 73  ? 0.2017 0.2170 0.6229 0.0169  0.0506  -0.0496 70  VAL A O   
612  C  CB  . VAL A 73  ? 0.2681 0.2000 0.6333 -0.0116 0.0682  -0.0592 70  VAL A CB  
613  C  CG1 . VAL A 73  ? 0.2758 0.1858 0.6392 -0.0275 0.0744  -0.0593 70  VAL A CG1 
614  C  CG2 . VAL A 73  ? 0.2743 0.2247 0.6334 -0.0110 0.0674  -0.0630 70  VAL A CG2 
615  N  N   . TRP A 74  ? 0.1887 0.1902 0.6128 -0.0084 0.0356  -0.0463 71  TRP A N   
616  C  CA  . TRP A 74  ? 0.1924 0.1868 0.5992 -0.0033 0.0226  -0.0403 71  TRP A CA  
617  C  C   . TRP A 74  ? 0.1634 0.1682 0.5852 -0.0217 0.0151  -0.0496 71  TRP A C   
618  O  O   . TRP A 74  ? 0.1828 0.1718 0.5897 -0.0312 0.0188  -0.0645 71  TRP A O   
619  C  CB  . TRP A 74  ? 0.1939 0.1952 0.6004 0.0105  0.0273  -0.0399 71  TRP A CB  
620  C  CG  . TRP A 74  ? 0.1904 0.2050 0.6015 0.0118  0.0248  -0.0281 71  TRP A CG  
621  C  CD1 . TRP A 74  ? 0.2041 0.2102 0.6036 0.0265  0.0227  -0.0266 71  TRP A CD1 
622  C  CD2 . TRP A 74  ? 0.1990 0.2004 0.6031 0.0155  0.0158  -0.0266 71  TRP A CD2 
623  N  NE1 . TRP A 74  ? 0.2197 0.2189 0.6111 0.0123  0.0210  -0.0296 71  TRP A NE1 
624  C  CE2 . TRP A 74  ? 0.2051 0.2046 0.6081 0.0071  0.0201  -0.0308 71  TRP A CE2 
625  C  CE3 . TRP A 74  ? 0.2023 0.2108 0.6015 0.0068  0.0165  -0.0256 71  TRP A CE3 
626  C  CZ2 . TRP A 74  ? 0.2278 0.1993 0.6101 -0.0013 0.0169  -0.0236 71  TRP A CZ2 
627  C  CZ3 . TRP A 74  ? 0.2323 0.2116 0.6072 -0.0016 0.0144  -0.0202 71  TRP A CZ3 
628  C  CH2 . TRP A 74  ? 0.2193 0.1994 0.6091 -0.0099 0.0201  -0.0214 71  TRP A CH2 
629  N  N   . LEU A 75  ? 0.1472 0.1642 0.5747 -0.0162 0.0185  -0.0440 72  LEU A N   
630  C  CA  . LEU A 75  ? 0.1503 0.1511 0.5685 -0.0012 0.0161  -0.0407 72  LEU A CA  
631  C  C   . LEU A 75  ? 0.1464 0.1538 0.5588 0.0009  0.0088  -0.0406 72  LEU A C   
632  O  O   . LEU A 75  ? 0.1503 0.1692 0.5534 -0.0095 0.0059  -0.0406 72  LEU A O   
633  C  CB  . LEU A 75  ? 0.1515 0.1564 0.5784 0.0079  0.0177  -0.0328 72  LEU A CB  
634  C  CG  . LEU A 75  ? 0.1896 0.1958 0.5900 0.0114  0.0234  -0.0276 72  LEU A CG  
635  C  CD1 . LEU A 75  ? 0.2070 0.2027 0.6009 0.0075  0.0174  -0.0262 72  LEU A CD1 
636  C  CD2 . LEU A 75  ? 0.2095 0.2386 0.5911 -0.0074 0.0203  -0.0270 72  LEU A CD2 
637  N  N   . ASP A 76  ? 0.1438 0.1451 0.5482 -0.0055 0.0081  -0.0280 73  ASP A N   
638  C  CA  . ASP A 76  ? 0.1579 0.1318 0.5444 -0.0067 0.0092  -0.0374 73  ASP A CA  
639  C  C   . ASP A 76  ? 0.1447 0.1263 0.5354 -0.0072 0.0133  -0.0298 73  ASP A C   
640  O  O   . ASP A 76  ? 0.1755 0.1306 0.5486 -0.0010 -0.0078 -0.0378 73  ASP A O   
641  C  CB  . ASP A 76  ? 0.1480 0.1391 0.5488 -0.0140 0.0107  -0.0378 73  ASP A CB  
642  C  CG  . ASP A 76  ? 0.1733 0.1322 0.5539 -0.0134 0.0099  -0.0384 73  ASP A CG  
643  O  OD1 . ASP A 76  ? 0.1873 0.1429 0.5428 -0.0276 0.0175  -0.0503 73  ASP A OD1 
644  O  OD2 . ASP A 76  ? 0.2101 0.1846 0.5613 -0.0011 -0.0221 -0.0483 73  ASP A OD2 
645  N  N   . ARG A 77  ? 0.1370 0.1162 0.5198 0.0166  0.0080  -0.0221 74  ARG A N   
646  C  CA  . ARG A 77  ? 0.1495 0.1186 0.5120 0.0120  0.0076  -0.0163 74  ARG A CA  
647  C  C   . ARG A 77  ? 0.1664 0.1375 0.5220 0.0107  0.0021  -0.0080 74  ARG A C   
648  O  O   . ARG A 77  ? 0.1885 0.1295 0.5315 0.0188  0.0077  -0.0034 74  ARG A O   
649  C  CB  . ARG A 77  ? 0.1445 0.1341 0.4888 0.0199  -0.0030 -0.0067 74  ARG A CB  
650  C  CG  . ARG A 77  ? 0.1372 0.1447 0.4652 0.0235  -0.0016 -0.0100 74  ARG A CG  
651  C  CD  . ARG A 77  ? 0.1443 0.1406 0.4482 0.0138  -0.0021 -0.0116 74  ARG A CD  
652  N  NE  . ARG A 77  ? 0.1462 0.1412 0.4245 0.0076  -0.0054 -0.0158 74  ARG A NE  
653  C  CZ  . ARG A 77  ? 0.1473 0.1335 0.4005 0.0048  -0.0173 -0.0204 74  ARG A CZ  
654  N  NH1 . ARG A 77  ? 0.1649 0.1376 0.4001 0.0043  -0.0179 -0.0266 74  ARG A NH1 
655  N  NH2 . ARG A 77  ? 0.1554 0.1265 0.4015 0.0132  -0.0088 -0.0199 74  ARG A NH2 
656  N  N   . PHE A 78  ? 0.1719 0.1423 0.5283 0.0018  0.0025  -0.0004 75  PHE A N   
657  C  CA  . PHE A 78  ? 0.1828 0.1398 0.5452 -0.0008 0.0073  0.0021  75  PHE A CA  
658  C  C   . PHE A 78  ? 0.2020 0.1514 0.5534 -0.0097 -0.0004 0.0095  75  PHE A C   
659  O  O   . PHE A 78  ? 0.2507 0.1466 0.5570 -0.0217 0.0053  0.0195  75  PHE A O   
660  C  CB  . PHE A 78  ? 0.1858 0.1362 0.5480 -0.0005 0.0126  -0.0014 75  PHE A CB  
661  C  CG  . PHE A 78  ? 0.1935 0.1656 0.5583 0.0130  0.0018  0.0013  75  PHE A CG  
662  C  CD1 . PHE A 78  ? 0.1847 0.1560 0.5711 0.0058  0.0124  0.0036  75  PHE A CD1 
663  C  CD2 . PHE A 78  ? 0.2350 0.1798 0.5690 0.0132  0.0050  -0.0129 75  PHE A CD2 
664  C  CE1 . PHE A 78  ? 0.2046 0.1648 0.5729 0.0115  0.0007  0.0054  75  PHE A CE1 
665  C  CE2 . PHE A 78  ? 0.2590 0.1967 0.5755 0.0182  -0.0043 -0.0053 75  PHE A CE2 
666  C  CZ  . PHE A 78  ? 0.2217 0.1693 0.5771 0.0163  -0.0025 0.0053  75  PHE A CZ  
667  N  N   . LEU A 79  ? 0.1941 0.1518 0.5642 -0.0158 -0.0027 0.0076  76  LEU A N   
668  C  CA  . LEU A 79  ? 0.2170 0.1659 0.5730 0.0022  -0.0060 -0.0023 76  LEU A CA  
669  C  C   . LEU A 79  ? 0.2250 0.1667 0.5745 0.0132  -0.0028 0.0004  76  LEU A C   
670  O  O   . LEU A 79  ? 0.2347 0.1564 0.5662 0.0013  0.0065  0.0065  76  LEU A O   
671  C  CB  . LEU A 79  ? 0.2240 0.2072 0.5899 0.0140  -0.0082 -0.0045 76  LEU A CB  
672  C  CG  . LEU A 79  ? 0.2597 0.2085 0.6033 0.0098  -0.0132 -0.0046 76  LEU A CG  
673  C  CD1 . LEU A 79  ? 0.2634 0.2330 0.6085 -0.0047 -0.0165 -0.0130 76  LEU A CD1 
674  C  CD2 . LEU A 79  ? 0.2855 0.2183 0.6125 0.0188  -0.0128 -0.0117 76  LEU A CD2 
675  N  N   . ILE A 80  ? 0.2562 0.1699 0.5856 0.0152  -0.0035 0.0051  77  ILE A N   
676  C  CA  . ILE A 80  ? 0.2681 0.1705 0.5943 0.0243  0.0097  0.0045  77  ILE A CA  
677  C  C   . ILE A 80  ? 0.2898 0.1725 0.5994 0.0186  0.0199  0.0027  77  ILE A C   
678  O  O   . ILE A 80  ? 0.2880 0.1570 0.5925 0.0143  0.0139  0.0176  77  ILE A O   
679  C  CB  . ILE A 80  ? 0.2717 0.1935 0.6033 0.0283  0.0078  -0.0035 77  ILE A CB  
680  C  CG1 . ILE A 80  ? 0.2621 0.1976 0.6075 0.0244  0.0060  -0.0087 77  ILE A CG1 
681  C  CG2 . ILE A 80  ? 0.2714 0.2145 0.6018 0.0445  0.0019  0.0000  77  ILE A CG2 
682  C  CD1 . ILE A 80  ? 0.2576 0.1925 0.6102 0.0209  0.0044  -0.0071 77  ILE A CD1 
683  N  N   . ASP A 81  ? 0.3161 0.1908 0.6111 0.0047  0.0368  -0.0016 78  ASP A N   
684  C  CA  . ASP A 81  ? 0.3295 0.1748 0.6297 0.0177  0.0511  -0.0079 78  ASP A CA  
685  C  C   . ASP A 81  ? 0.3679 0.2019 0.6360 0.0293  0.0461  -0.0124 78  ASP A C   
686  O  O   . ASP A 81  ? 0.3851 0.2195 0.6392 0.0342  0.0348  -0.0063 78  ASP A O   
687  C  CB  . ASP A 81  ? 0.3266 0.1741 0.6351 0.0129  0.0672  -0.0029 78  ASP A CB  
688  C  CG  . ASP A 81  ? 0.3291 0.1831 0.6420 0.0272  0.0758  -0.0203 78  ASP A CG  
689  O  OD1 . ASP A 81  ? 0.3471 0.1938 0.6429 0.0137  0.0778  -0.0153 78  ASP A OD1 
690  O  OD2 . ASP A 81  ? 0.3090 0.1922 0.6534 0.0221  0.0987  -0.0279 78  ASP A OD2 
691  N  N   . GLN A 82  ? 0.4224 0.2475 0.6482 0.0449  0.0479  -0.0234 79  GLN A N   
692  C  CA  . GLN A 82  ? 0.4864 0.2867 0.6627 0.0538  0.0347  -0.0288 79  GLN A CA  
693  C  C   . GLN A 82  ? 0.5160 0.2960 0.6661 0.0749  0.0309  -0.0242 79  GLN A C   
694  O  O   . GLN A 82  ? 0.5425 0.3087 0.6670 0.0990  0.0225  -0.0324 79  GLN A O   
695  C  CB  . GLN A 82  ? 0.5214 0.3311 0.6856 0.0555  0.0441  -0.0558 79  GLN A CB  
696  C  CG  . GLN A 82  ? 0.5579 0.3800 0.7106 0.0411  0.0340  -0.0633 79  GLN A CG  
697  C  CD  . GLN A 82  ? 0.5758 0.4219 0.7460 0.0333  0.0302  -0.0772 79  GLN A CD  
698  O  OE1 . GLN A 82  ? 0.5720 0.4802 0.7701 0.0196  0.0429  -0.0818 79  GLN A OE1 
699  N  NE2 . GLN A 82  ? 0.6213 0.4490 0.7679 0.0243  0.0295  -0.1029 79  GLN A NE2 
700  N  N   . ARG A 83  ? 0.5519 0.2925 0.6614 0.0675  0.0276  0.0034  80  ARG A N   
701  C  CA  . ARG A 83  ? 0.5657 0.3029 0.6663 0.0700  0.0234  0.0189  80  ARG A CA  
702  C  C   . ARG A 83  ? 0.5676 0.3055 0.6578 0.0874  0.0100  0.0349  80  ARG A C   
703  O  O   . ARG A 83  ? 0.5772 0.2976 0.6711 0.0935  0.0103  0.0518  80  ARG A O   
704  C  CB  . ARG A 83  ? 0.5964 0.3095 0.6752 0.0461  0.0321  0.0215  80  ARG A CB  
705  C  CG  . ARG A 83  ? 0.5922 0.3367 0.6799 0.0094  0.0403  0.0217  80  ARG A CG  
706  C  CD  . ARG A 83  ? 0.6117 0.3437 0.6830 -0.0097 0.0454  0.0210  80  ARG A CD  
707  N  NE  . ARG A 83  ? 0.6050 0.3258 0.6827 -0.0431 0.0544  0.0205  80  ARG A NE  
708  C  CZ  . ARG A 83  ? 0.6066 0.2547 0.7014 -0.0631 0.0637  0.0379  80  ARG A CZ  
709  N  NH1 . ARG A 83  ? 0.5981 0.2807 0.7111 -0.0766 0.0728  0.0419  80  ARG A NH1 
710  N  NH2 . ARG A 83  ? 0.5876 0.2067 0.6928 -0.0773 0.0634  0.0295  80  ARG A NH2 
711  N  N   . PHE A 84  ? 0.5331 0.2818 0.6501 0.0945  -0.0003 0.0465  81  PHE A N   
712  C  CA  . PHE A 84  ? 0.5277 0.3111 0.6580 0.1016  -0.0094 0.0314  81  PHE A CA  
713  C  C   . PHE A 84  ? 0.4944 0.3566 0.6678 0.1070  -0.0125 0.0204  81  PHE A C   
714  O  O   . PHE A 84  ? 0.4992 0.3750 0.6765 0.1156  -0.0145 0.0073  81  PHE A O   
715  C  CB  . PHE A 84  ? 0.5294 0.3042 0.6539 0.1042  -0.0130 0.0352  81  PHE A CB  
716  C  CG  . PHE A 84  ? 0.5259 0.2864 0.6488 0.1050  -0.0166 0.0372  81  PHE A CG  
717  C  CD1 . PHE A 84  ? 0.5218 0.2743 0.6490 0.1098  -0.0156 0.0266  81  PHE A CD1 
718  C  CD2 . PHE A 84  ? 0.5288 0.2938 0.6445 0.0950  -0.0195 0.0308  81  PHE A CD2 
719  C  CE1 . PHE A 84  ? 0.5180 0.2759 0.6482 0.1130  -0.0118 0.0324  81  PHE A CE1 
720  C  CE2 . PHE A 84  ? 0.5277 0.2851 0.6446 0.1008  -0.0153 0.0355  81  PHE A CE2 
721  C  CZ  . PHE A 84  ? 0.5241 0.2906 0.6453 0.1045  -0.0182 0.0346  81  PHE A CZ  
722  N  N   . GLN A 85  ? 0.4794 0.3782 0.6728 0.1144  -0.0195 0.0115  82  GLN A N   
723  C  CA  . GLN A 85  ? 0.4982 0.4043 0.6937 0.1028  -0.0245 0.0118  82  GLN A CA  
724  C  C   . GLN A 85  ? 0.5166 0.4787 0.7183 0.1011  -0.0346 0.0104  82  GLN A C   
725  O  O   . GLN A 85  ? 0.5268 0.5352 0.7240 0.1067  -0.0340 0.0275  82  GLN A O   
726  C  CB  . GLN A 85  ? 0.5006 0.3924 0.6897 0.0820  -0.0357 0.0200  82  GLN A CB  
727  C  CG  . GLN A 85  ? 0.4969 0.3855 0.6890 0.0771  -0.0378 0.0193  82  GLN A CG  
728  C  CD  . GLN A 85  ? 0.5059 0.3853 0.6867 0.0693  -0.0355 0.0177  82  GLN A CD  
729  O  OE1 . GLN A 85  ? 0.5097 0.3923 0.6920 0.0607  -0.0350 0.0231  82  GLN A OE1 
730  N  NE2 . GLN A 85  ? 0.5146 0.3812 0.6889 0.0806  -0.0410 0.0167  82  GLN A NE2 
731  N  N   . GLY A 86  ? 0.5229 0.5100 0.7508 0.0999  -0.0335 0.0002  83  GLY A N   
732  C  CA  . GLY A 86  ? 0.5363 0.5467 0.7629 0.0995  -0.0364 -0.0022 83  GLY A CA  
733  C  C   . GLY A 86  ? 0.5380 0.5660 0.7750 0.1073  -0.0307 -0.0012 83  GLY A C   
734  O  O   . GLY A 86  ? 0.5362 0.6268 0.7839 0.1234  -0.0282 -0.0043 83  GLY A O   
735  N  N   . GLN A 87  ? 0.5303 0.5772 0.7804 0.0775  -0.0261 -0.0064 84  GLN A N   
736  C  CA  . GLN A 87  ? 0.5117 0.5691 0.7892 0.0716  -0.0133 -0.0041 84  GLN A CA  
737  C  C   . GLN A 87  ? 0.4766 0.5191 0.7739 0.0485  -0.0138 0.0036  84  GLN A C   
738  O  O   . GLN A 87  ? 0.5145 0.5283 0.7858 0.0389  -0.0096 -0.0081 84  GLN A O   
739  C  CB  . GLN A 87  ? 0.5116 0.5994 0.8128 0.0683  0.0024  -0.0073 84  GLN A CB  
740  C  CG  . GLN A 87  ? 0.5471 0.6251 0.8300 0.0713  0.0084  -0.0208 84  GLN A CG  
741  C  CD  . GLN A 87  ? 0.5544 0.6385 0.8521 0.0716  0.0299  -0.0244 84  GLN A CD  
742  O  OE1 . GLN A 87  ? 0.6051 0.6448 0.8693 0.0705  0.0329  -0.0329 84  GLN A OE1 
743  N  NE2 . GLN A 87  ? 0.5673 0.6381 0.8612 0.0676  0.0344  -0.0356 84  GLN A NE2 
744  N  N   . GLY A 88  ? 0.4225 0.4703 0.7577 0.0498  -0.0218 -0.0028 85  GLY A N   
745  C  CA  . GLY A 88  ? 0.3772 0.4499 0.7506 0.0355  -0.0195 0.0082  85  GLY A CA  
746  C  C   . GLY A 88  ? 0.3439 0.4212 0.7414 0.0250  -0.0089 0.0050  85  GLY A C   
747  O  O   . GLY A 88  ? 0.3354 0.3936 0.7349 0.0113  -0.0011 0.0080  85  GLY A O   
748  N  N   . TYR A 89  ? 0.3399 0.4214 0.7293 0.0171  -0.0031 0.0051  86  TYR A N   
749  C  CA  . TYR A 89  ? 0.3012 0.4009 0.7278 0.0186  0.0015  0.0070  86  TYR A CA  
750  C  C   . TYR A 89  ? 0.2735 0.3801 0.7131 0.0294  -0.0090 0.0008  86  TYR A C   
751  O  O   . TYR A 89  ? 0.2616 0.4143 0.7046 0.0367  -0.0109 -0.0001 86  TYR A O   
752  C  CB  . TYR A 89  ? 0.3065 0.3870 0.7390 0.0306  0.0074  0.0074  86  TYR A CB  
753  C  CG  . TYR A 89  ? 0.3478 0.3670 0.7513 0.0412  0.0164  0.0044  86  TYR A CG  
754  C  CD1 . TYR A 89  ? 0.3591 0.3715 0.7578 0.0444  0.0263  0.0019  86  TYR A CD1 
755  C  CD2 . TYR A 89  ? 0.3588 0.3523 0.7500 0.0563  0.0262  0.0034  86  TYR A CD2 
756  C  CE1 . TYR A 89  ? 0.3860 0.3637 0.7530 0.0419  0.0323  -0.0028 86  TYR A CE1 
757  C  CE2 . TYR A 89  ? 0.3838 0.3443 0.7502 0.0502  0.0232  0.0040  86  TYR A CE2 
758  C  CZ  . TYR A 89  ? 0.3870 0.3546 0.7543 0.0526  0.0275  0.0000  86  TYR A CZ  
759  O  OH  . TYR A 89  ? 0.4489 0.3392 0.7594 0.0537  0.0191  0.0094  86  TYR A OH  
760  N  N   . GLY A 90  ? 0.2728 0.3702 0.7004 0.0148  -0.0080 0.0055  87  GLY A N   
761  C  CA  . GLY A 90  ? 0.2659 0.3356 0.7010 0.0238  -0.0165 0.0013  87  GLY A CA  
762  C  C   . GLY A 90  ? 0.2615 0.3238 0.7036 0.0196  -0.0172 0.0066  87  GLY A C   
763  O  O   . GLY A 90  ? 0.2865 0.3201 0.7092 0.0243  -0.0133 0.0239  87  GLY A O   
764  N  N   . LYS A 91  ? 0.2587 0.3259 0.7144 0.0207  -0.0098 -0.0041 88  LYS A N   
765  C  CA  . LYS A 91  ? 0.2523 0.3276 0.7179 0.0189  -0.0149 0.0039  88  LYS A CA  
766  C  C   . LYS A 91  ? 0.2143 0.2797 0.7060 0.0195  -0.0063 0.0239  88  LYS A C   
767  O  O   . LYS A 91  ? 0.1912 0.2556 0.7138 0.0060  -0.0033 0.0245  88  LYS A O   
768  C  CB  . LYS A 91  ? 0.2813 0.3772 0.7334 0.0153  -0.0246 -0.0055 88  LYS A CB  
769  C  CG  . LYS A 91  ? 0.2899 0.4229 0.7445 0.0099  -0.0266 -0.0068 88  LYS A CG  
770  C  CD  . LYS A 91  ? 0.2997 0.4630 0.7567 0.0089  -0.0346 -0.0074 88  LYS A CD  
771  C  CE  . LYS A 91  ? 0.2889 0.4846 0.7593 0.0078  -0.0331 -0.0091 88  LYS A CE  
772  N  NZ  . LYS A 91  ? 0.3477 0.5061 0.7583 0.0069  -0.0468 -0.0004 88  LYS A NZ  
773  N  N   . ALA A 92  ? 0.2375 0.2766 0.6974 0.0399  -0.0026 0.0228  89  ALA A N   
774  C  CA  . ALA A 92  ? 0.2202 0.2522 0.6892 0.0492  0.0010  0.0256  89  ALA A CA  
775  C  C   . ALA A 92  ? 0.2166 0.2290 0.6802 0.0474  0.0074  0.0135  89  ALA A C   
776  O  O   . ALA A 92  ? 0.2517 0.2288 0.6928 0.0468  0.0056  0.0040  89  ALA A O   
777  C  CB  . ALA A 92  ? 0.2381 0.2619 0.6862 0.0674  0.0034  0.0289  89  ALA A CB  
778  N  N   . ALA A 93  ? 0.2090 0.2245 0.6704 0.0349  0.0079  0.0065  90  ALA A N   
779  C  CA  . ALA A 93  ? 0.1987 0.2052 0.6617 0.0156  0.0090  -0.0012 90  ALA A CA  
780  C  C   . ALA A 93  ? 0.1762 0.1926 0.6637 0.0145  0.0065  0.0075  90  ALA A C   
781  O  O   . ALA A 93  ? 0.1933 0.1868 0.6636 0.0098  0.0133  0.0165  90  ALA A O   
782  C  CB  . ALA A 93  ? 0.1986 0.2145 0.6600 0.0025  0.0129  0.0062  90  ALA A CB  
783  N  N   . CYS A 94  ? 0.1742 0.2084 0.6679 0.0129  0.0121  0.0125  91  CYS A N   
784  C  CA  . CYS A 94  ? 0.2016 0.1938 0.6784 0.0089  0.0167  0.0060  91  CYS A CA  
785  C  C   . CYS A 94  ? 0.1884 0.1902 0.6737 -0.0047 0.0229  0.0060  91  CYS A C   
786  O  O   . CYS A 94  ? 0.1704 0.1998 0.6703 -0.0036 0.0322  0.0084  91  CYS A O   
787  C  CB  . CYS A 94  ? 0.2293 0.2081 0.6878 0.0020  0.0135  0.0055  91  CYS A CB  
788  S  SG  . CYS A 94  ? 0.2941 0.2089 0.7109 -0.0133 0.0188  0.0112  91  CYS A SG  
789  N  N   . ARG A 95  ? 0.1957 0.2051 0.6779 -0.0002 0.0304  0.0009  92  ARG A N   
790  C  CA  . ARG A 95  ? 0.2038 0.2125 0.6840 0.0162  0.0300  -0.0001 92  ARG A CA  
791  C  C   . ARG A 95  ? 0.1988 0.1800 0.6821 0.0319  0.0429  0.0038  92  ARG A C   
792  O  O   . ARG A 95  ? 0.2143 0.1413 0.6875 0.0216  0.0387  0.0337  92  ARG A O   
793  C  CB  . ARG A 95  ? 0.2475 0.2672 0.6929 0.0340  0.0161  -0.0001 92  ARG A CB  
794  C  CG  . ARG A 95  ? 0.2723 0.3274 0.7066 0.0377  0.0221  -0.0083 92  ARG A CG  
795  C  CD  . ARG A 95  ? 0.3107 0.3686 0.7150 0.0532  0.0179  -0.0025 92  ARG A CD  
796  N  NE  . ARG A 95  ? 0.3320 0.4232 0.7239 0.0461  0.0191  -0.0015 92  ARG A NE  
797  C  CZ  . ARG A 95  ? 0.3656 0.4378 0.7283 0.0575  0.0045  0.0036  92  ARG A CZ  
798  N  NH1 . ARG A 95  ? 0.3573 0.4289 0.7400 0.0712  -0.0006 0.0097  92  ARG A NH1 
799  N  NH2 . ARG A 95  ? 0.3833 0.4457 0.7308 0.0504  0.0056  0.0037  92  ARG A NH2 
800  N  N   . LEU A 96  ? 0.1973 0.1787 0.6840 0.0307  0.0497  -0.0076 93  LEU A N   
801  C  CA  . LEU A 96  ? 0.2254 0.1835 0.6848 0.0266  0.0528  -0.0204 93  LEU A CA  
802  C  C   . LEU A 96  ? 0.1927 0.1573 0.6864 0.0302  0.0384  -0.0326 93  LEU A C   
803  O  O   . LEU A 96  ? 0.2016 0.1388 0.7076 0.0516  0.0241  -0.0391 93  LEU A O   
804  C  CB  . LEU A 96  ? 0.2407 0.2027 0.6955 0.0289  0.0705  -0.0182 93  LEU A CB  
805  C  CG  . LEU A 96  ? 0.2866 0.2345 0.7042 0.0303  0.0780  -0.0070 93  LEU A CG  
806  C  CD1 . LEU A 96  ? 0.3096 0.2321 0.7069 0.0375  0.0886  0.0007  93  LEU A CD1 
807  C  CD2 . LEU A 96  ? 0.2932 0.2546 0.7044 0.0367  0.0822  -0.0040 93  LEU A CD2 
808  N  N   . LEU A 97  ? 0.1752 0.1640 0.6713 0.0271  0.0219  -0.0344 94  LEU A N   
809  C  CA  . LEU A 97  ? 0.1879 0.2067 0.6527 -0.0134 0.0108  -0.0275 94  LEU A CA  
810  C  C   . LEU A 97  ? 0.1807 0.2482 0.6357 -0.0184 0.0036  -0.0299 94  LEU A C   
811  O  O   . LEU A 97  ? 0.2043 0.2737 0.6333 -0.0284 -0.0055 -0.0159 94  LEU A O   
812  C  CB  . LEU A 97  ? 0.1688 0.2053 0.6574 -0.0183 0.0111  -0.0184 94  LEU A CB  
813  C  CG  . LEU A 97  ? 0.1869 0.2051 0.6692 0.0011  0.0043  -0.0216 94  LEU A CG  
814  C  CD1 . LEU A 97  ? 0.1860 0.2205 0.6703 0.0133  -0.0024 -0.0234 94  LEU A CD1 
815  C  CD2 . LEU A 97  ? 0.1914 0.2172 0.6770 0.0174  -0.0002 -0.0197 94  LEU A CD2 
816  N  N   A MET A 98  ? 0.1744 0.2099 0.6431 -0.0068 0.0144  -0.0291 95  MET A N   
817  N  N   B MET A 98  ? 0.1907 0.2415 0.6497 -0.0191 0.0001  -0.0257 95  MET A N   
818  C  CA  A MET A 98  ? 0.1569 0.1965 0.6468 0.0062  0.0145  -0.0310 95  MET A CA  
819  C  CA  B MET A 98  ? 0.1908 0.2307 0.6542 -0.0079 0.0013  -0.0234 95  MET A CA  
820  C  C   A MET A 98  ? 0.1640 0.1854 0.6494 0.0179  0.0100  -0.0271 95  MET A C   
821  C  C   B MET A 98  ? 0.1897 0.2019 0.6613 0.0061  -0.0011 -0.0172 95  MET A C   
822  O  O   A MET A 98  ? 0.1919 0.1812 0.6441 0.0384  0.0125  -0.0299 95  MET A O   
823  O  O   B MET A 98  ? 0.2024 0.2103 0.6641 0.0068  0.0012  -0.0209 95  MET A O   
824  C  CB  A MET A 98  ? 0.1464 0.1914 0.6509 0.0106  0.0139  -0.0316 95  MET A CB  
825  C  CB  B MET A 98  ? 0.1959 0.2477 0.6602 -0.0119 -0.0060 -0.0188 95  MET A CB  
826  C  CG  A MET A 98  ? 0.1471 0.1788 0.6555 0.0136  0.0169  -0.0228 95  MET A CG  
827  C  CG  B MET A 98  ? 0.2044 0.2524 0.6632 -0.0098 -0.0082 -0.0169 95  MET A CG  
828  S  SD  A MET A 98  ? 0.1634 0.1756 0.6534 0.0192  0.0282  -0.0171 95  MET A SD  
829  S  SD  B MET A 98  ? 0.2158 0.2716 0.6690 -0.0158 -0.0178 -0.0101 95  MET A SD  
830  C  CE  A MET A 98  ? 0.1525 0.1754 0.6561 0.0458  0.0387  -0.0247 95  MET A CE  
831  C  CE  B MET A 98  ? 0.2129 0.2696 0.6709 -0.0139 -0.0172 -0.0088 95  MET A CE  
832  N  N   . LEU A 99  ? 0.1816 0.1821 0.6627 0.0185  0.0087  -0.0325 96  LEU A N   
833  C  CA  . LEU A 99  ? 0.2080 0.1805 0.6669 0.0315  0.0014  -0.0315 96  LEU A CA  
834  C  C   . LEU A 99  ? 0.2379 0.1796 0.6739 0.0394  -0.0123 -0.0349 96  LEU A C   
835  O  O   . LEU A 99  ? 0.2565 0.1742 0.6730 0.0336  -0.0100 -0.0132 96  LEU A O   
836  C  CB  . LEU A 99  ? 0.2103 0.1898 0.6688 0.0361  -0.0044 -0.0298 96  LEU A CB  
837  C  CG  . LEU A 99  ? 0.2157 0.2058 0.6738 0.0209  0.0028  -0.0367 96  LEU A CG  
838  C  CD1 . LEU A 99  ? 0.2346 0.2226 0.6797 0.0264  -0.0018 -0.0308 96  LEU A CD1 
839  C  CD2 . LEU A 99  ? 0.2415 0.2082 0.6782 0.0121  0.0075  -0.0374 96  LEU A CD2 
840  N  N   . LYS A 100 ? 0.2500 0.1679 0.6875 0.0430  -0.0246 -0.0322 97  LYS A N   
841  C  CA  . LYS A 100 ? 0.2748 0.1856 0.7028 0.0329  -0.0328 -0.0385 97  LYS A CA  
842  C  C   . LYS A 100 ? 0.2725 0.2007 0.7091 0.0368  -0.0430 -0.0376 97  LYS A C   
843  O  O   . LYS A 100 ? 0.2810 0.2298 0.7127 0.0364  -0.0509 -0.0350 97  LYS A O   
844  C  CB  . LYS A 100 ? 0.2955 0.2278 0.7061 0.0268  -0.0251 -0.0400 97  LYS A CB  
845  C  CG  . LYS A 100 ? 0.3280 0.2339 0.7096 0.0135  -0.0193 -0.0404 97  LYS A CG  
846  C  CD  . LYS A 100 ? 0.3451 0.2821 0.7139 0.0155  -0.0138 -0.0470 97  LYS A CD  
847  C  CE  . LYS A 100 ? 0.4003 0.2962 0.7192 0.0015  -0.0184 -0.0504 97  LYS A CE  
848  N  NZ  . LYS A 100 ? 0.4313 0.3226 0.7216 0.0049  -0.0188 -0.0535 97  LYS A NZ  
849  N  N   . LEU A 101 ? 0.2513 0.1908 0.7278 0.0353  -0.0457 -0.0239 98  LEU A N   
850  C  CA  . LEU A 101 ? 0.2422 0.1988 0.7365 0.0347  -0.0369 -0.0207 98  LEU A CA  
851  C  C   . LEU A 101 ? 0.2252 0.2175 0.7489 0.0381  -0.0419 -0.0208 98  LEU A C   
852  O  O   . LEU A 101 ? 0.2179 0.2661 0.7495 0.0169  -0.0383 -0.0210 98  LEU A O   
853  C  CB  . LEU A 101 ? 0.2346 0.1924 0.7382 0.0374  -0.0208 -0.0125 98  LEU A CB  
854  C  CG  . LEU A 101 ? 0.2445 0.1938 0.7423 0.0379  -0.0142 0.0019  98  LEU A CG  
855  C  CD1 . LEU A 101 ? 0.2542 0.1915 0.7403 0.0378  -0.0137 0.0052  98  LEU A CD1 
856  C  CD2 . LEU A 101 ? 0.2552 0.2095 0.7453 0.0236  -0.0152 0.0043  98  LEU A CD2 
857  N  N   . ILE A 102 ? 0.2346 0.2283 0.7733 0.0393  -0.0494 -0.0260 99  ILE A N   
858  C  CA  . ILE A 102 ? 0.2306 0.2488 0.7903 0.0314  -0.0459 -0.0311 99  ILE A CA  
859  C  C   . ILE A 102 ? 0.2604 0.2894 0.8030 0.0514  -0.0579 -0.0523 99  ILE A C   
860  O  O   . ILE A 102 ? 0.3166 0.3285 0.8003 0.0425  -0.0686 -0.0371 99  ILE A O   
861  C  CB  . ILE A 102 ? 0.2271 0.2522 0.7927 0.0327  -0.0394 -0.0362 99  ILE A CB  
862  C  CG1 . ILE A 102 ? 0.2018 0.2274 0.7969 0.0390  -0.0420 -0.0396 99  ILE A CG1 
863  C  CG2 . ILE A 102 ? 0.2415 0.2495 0.7948 0.0293  -0.0325 -0.0320 99  ILE A CG2 
864  C  CD1 . ILE A 102 ? 0.2052 0.2514 0.8001 0.0474  -0.0372 -0.0413 99  ILE A CD1 
865  N  N   . GLU A 103 ? 0.2769 0.3080 0.8203 0.0518  -0.0599 -0.0553 100 GLU A N   
866  C  CA  . GLU A 103 ? 0.3066 0.3241 0.8481 0.0469  -0.0744 -0.0662 100 GLU A CA  
867  C  C   . GLU A 103 ? 0.3377 0.3320 0.8650 0.0656  -0.0903 -0.0811 100 GLU A C   
868  O  O   . GLU A 103 ? 0.3478 0.3494 0.8742 0.0740  -0.0843 -0.0993 100 GLU A O   
869  C  CB  . GLU A 103 ? 0.3352 0.3554 0.8604 0.0495  -0.0789 -0.0451 100 GLU A CB  
870  C  CG  . GLU A 103 ? 0.3705 0.3824 0.8737 0.0379  -0.0780 -0.0422 100 GLU A CG  
871  C  CD  . GLU A 103 ? 0.3837 0.4090 0.8940 0.0314  -0.0760 -0.0187 100 GLU A CD  
872  O  OE1 . GLU A 103 ? 0.4110 0.4535 0.9041 0.0406  -0.0661 0.0076  100 GLU A OE1 
873  O  OE2 . GLU A 103 ? 0.4199 0.4118 0.9023 0.0175  -0.0801 -0.0052 100 GLU A OE2 
874  N  N   . LYS A 104 ? 0.3306 0.3159 0.8896 0.0598  -0.1008 -0.0877 101 LYS A N   
875  C  CA  . LYS A 104 ? 0.3472 0.3182 0.9057 0.0523  -0.1126 -0.0900 101 LYS A CA  
876  C  C   . LYS A 104 ? 0.3133 0.3288 0.9036 0.0637  -0.1077 -0.0957 101 LYS A C   
877  O  O   . LYS A 104 ? 0.3304 0.3453 0.9140 0.0666  -0.0945 -0.1197 101 LYS A O   
878  C  CB  . LYS A 104 ? 0.3725 0.3507 0.9199 0.0489  -0.1042 -0.0761 101 LYS A CB  
879  C  CG  . LYS A 104 ? 0.3964 0.3554 0.9345 0.0404  -0.1163 -0.0612 101 LYS A CG  
880  C  CD  . LYS A 104 ? 0.4295 0.3909 0.9469 0.0382  -0.1016 -0.0511 101 LYS A CD  
881  C  CE  . LYS A 104 ? 0.4569 0.4237 0.9479 0.0476  -0.1159 -0.0393 101 LYS A CE  
882  N  NZ  . LYS A 104 ? 0.4896 0.4180 0.9530 0.0477  -0.1137 -0.0343 101 LYS A NZ  
883  N  N   . TYR A 105 ? 0.2570 0.3050 0.9034 0.0905  -0.1017 -0.0843 102 TYR A N   
884  C  CA  . TYR A 105 ? 0.2522 0.3323 0.9038 0.0859  -0.0950 -0.0788 102 TYR A CA  
885  C  C   . TYR A 105 ? 0.2674 0.3500 0.9013 0.1045  -0.0689 -0.0818 102 TYR A C   
886  O  O   . TYR A 105 ? 0.2273 0.3729 0.8982 0.1282  -0.0385 -0.0883 102 TYR A O   
887  C  CB  . TYR A 105 ? 0.2575 0.3139 0.9117 0.0856  -0.1004 -0.0657 102 TYR A CB  
888  C  CG  . TYR A 105 ? 0.2457 0.2778 0.9210 0.0826  -0.1131 -0.0639 102 TYR A CG  
889  C  CD1 . TYR A 105 ? 0.2721 0.3151 0.9288 0.0808  -0.1211 -0.0636 102 TYR A CD1 
890  C  CD2 . TYR A 105 ? 0.2689 0.2380 0.9206 0.0789  -0.1172 -0.0662 102 TYR A CD2 
891  C  CE1 . TYR A 105 ? 0.2516 0.2830 0.9354 0.0698  -0.1317 -0.0618 102 TYR A CE1 
892  C  CE2 . TYR A 105 ? 0.2733 0.2467 0.9253 0.0692  -0.1218 -0.0455 102 TYR A CE2 
893  C  CZ  . TYR A 105 ? 0.2612 0.2742 0.9416 0.0570  -0.1295 -0.0481 102 TYR A CZ  
894  O  OH  . TYR A 105 ? 0.2760 0.3426 0.9668 0.0721  -0.1241 -0.0336 102 TYR A OH  
895  N  N   . GLN A 106 ? 0.3123 0.3987 0.9036 0.1131  -0.0404 -0.0936 103 GLN A N   
896  C  CA  . GLN A 106 ? 0.3698 0.4263 0.9010 0.1197  -0.0017 -0.1060 103 GLN A CA  
897  C  C   . GLN A 106 ? 0.3998 0.4282 0.8811 0.1199  0.0117  -0.1188 103 GLN A C   
898  O  O   . GLN A 106 ? 0.4207 0.4583 0.8761 0.1392  -0.0103 -0.1371 103 GLN A O   
899  C  CB  . GLN A 106 ? 0.4063 0.4404 0.9122 0.1231  0.0077  -0.0988 103 GLN A CB  
900  C  CG  . GLN A 106 ? 0.4559 0.4745 0.9195 0.1144  0.0141  -0.1011 103 GLN A CG  
901  C  CD  . GLN A 106 ? 0.4829 0.4925 0.9422 0.1001  0.0214  -0.0924 103 GLN A CD  
902  O  OE1 . GLN A 106 ? 0.5106 0.5155 0.9752 0.0712  0.0247  -0.0847 103 GLN A OE1 
903  N  NE2 . GLN A 106 ? 0.4722 0.4955 0.9485 0.1008  0.0197  -0.0955 103 GLN A NE2 
904  N  N   . THR A 107 ? 0.4139 0.4202 0.8582 0.1090  0.0415  -0.1166 104 THR A N   
905  C  CA  . THR A 107 ? 0.4130 0.4209 0.8294 0.0975  0.0551  -0.1087 104 THR A CA  
906  C  C   . THR A 107 ? 0.4201 0.3751 0.8036 0.0932  0.0792  -0.0886 104 THR A C   
907  O  O   . THR A 107 ? 0.4696 0.3080 0.8025 0.1001  0.0874  -0.1124 104 THR A O   
908  C  CB  . THR A 107 ? 0.4007 0.4194 0.8348 0.0929  0.0502  -0.1180 104 THR A CB  
909  O  OG1 . THR A 107 ? 0.3851 0.4338 0.8298 0.0814  0.0539  -0.1287 104 THR A OG1 
910  C  CG2 . THR A 107 ? 0.4233 0.4307 0.8310 0.0703  0.0530  -0.1249 104 THR A CG2 
911  N  N   . ASN A 108 ? 0.4048 0.3550 0.7694 0.0893  0.0940  -0.0730 105 ASN A N   
912  C  CA  . ASN A 108 ? 0.4053 0.3797 0.7500 0.0822  0.1077  -0.0563 105 ASN A CA  
913  C  C   . ASN A 108 ? 0.3278 0.3592 0.7159 0.0731  0.1056  -0.0427 105 ASN A C   
914  O  O   . ASN A 108 ? 0.3288 0.3853 0.7138 0.0730  0.1091  -0.0462 105 ASN A O   
915  C  CB  . ASN A 108 ? 0.4189 0.4301 0.7690 0.0824  0.1075  -0.0371 105 ASN A CB  
916  C  CG  . ASN A 108 ? 0.4621 0.4207 0.7783 0.0804  0.1156  -0.0258 105 ASN A CG  
917  O  OD1 . ASN A 108 ? 0.4729 0.4502 0.7891 0.0813  0.1275  -0.0072 105 ASN A OD1 
918  N  ND2 . ASN A 108 ? 0.4870 0.4492 0.7844 0.0554  0.1190  -0.0131 105 ASN A ND2 
919  N  N   . LYS A 109 ? 0.2522 0.3407 0.6741 0.0377  0.1185  -0.0466 106 LYS A N   
920  C  CA  . LYS A 109 ? 0.2241 0.3100 0.6532 0.0276  0.1183  -0.0349 106 LYS A CA  
921  C  C   . LYS A 109 ? 0.2090 0.2682 0.6359 0.0177  0.1009  -0.0392 106 LYS A C   
922  O  O   . LYS A 109 ? 0.2243 0.2936 0.6267 0.0346  0.1027  -0.0502 106 LYS A O   
923  C  CB  . LYS A 109 ? 0.2391 0.3335 0.6519 0.0361  0.1287  -0.0237 106 LYS A CB  
924  C  CG  . LYS A 109 ? 0.2574 0.3505 0.6652 0.0188  0.1225  -0.0192 106 LYS A CG  
925  C  CD  . LYS A 109 ? 0.2866 0.3742 0.6664 0.0198  0.1277  -0.0210 106 LYS A CD  
926  C  CE  . LYS A 109 ? 0.3254 0.3916 0.6779 0.0223  0.1184  -0.0259 106 LYS A CE  
927  N  NZ  . LYS A 109 ? 0.3632 0.4055 0.6785 0.0247  0.1203  -0.0251 106 LYS A NZ  
928  N  N   . LEU A 110 ? 0.1946 0.2265 0.6300 -0.0008 0.0826  -0.0365 107 LEU A N   
929  C  CA  . LEU A 110 ? 0.1810 0.1994 0.6290 -0.0020 0.0700  -0.0330 107 LEU A CA  
930  C  C   . LEU A 110 ? 0.1541 0.1874 0.6214 -0.0052 0.0649  -0.0239 107 LEU A C   
931  O  O   . LEU A 110 ? 0.1486 0.2043 0.6318 -0.0039 0.0553  -0.0305 107 LEU A O   
932  C  CB  . LEU A 110 ? 0.1799 0.2170 0.6312 -0.0113 0.0716  -0.0295 107 LEU A CB  
933  C  CG  . LEU A 110 ? 0.1847 0.2224 0.6455 -0.0153 0.0662  -0.0328 107 LEU A CG  
934  C  CD1 . LEU A 110 ? 0.1887 0.2257 0.6513 -0.0125 0.0622  -0.0237 107 LEU A CD1 
935  C  CD2 . LEU A 110 ? 0.2069 0.2345 0.6488 -0.0100 0.0653  -0.0356 107 LEU A CD2 
936  N  N   . TYR A 111 ? 0.1428 0.1873 0.6150 -0.0136 0.0538  -0.0266 108 TYR A N   
937  C  CA  . TYR A 111 ? 0.1761 0.1770 0.6178 -0.0170 0.0495  -0.0130 108 TYR A CA  
938  C  C   . TYR A 111 ? 0.1498 0.1692 0.6112 -0.0105 0.0368  -0.0158 108 TYR A C   
939  O  O   . TYR A 111 ? 0.1761 0.1629 0.6020 -0.0226 0.0281  -0.0098 108 TYR A O   
940  C  CB  . TYR A 111 ? 0.1924 0.1733 0.6246 -0.0112 0.0582  -0.0065 108 TYR A CB  
941  C  CG  . TYR A 111 ? 0.2129 0.1943 0.6366 -0.0293 0.0718  0.0017  108 TYR A CG  
942  C  CD1 . TYR A 111 ? 0.2288 0.2165 0.6416 -0.0251 0.0797  -0.0018 108 TYR A CD1 
943  C  CD2 . TYR A 111 ? 0.2157 0.1910 0.6391 -0.0300 0.0850  0.0118  108 TYR A CD2 
944  C  CE1 . TYR A 111 ? 0.2540 0.2480 0.6468 -0.0311 0.0923  0.0008  108 TYR A CE1 
945  C  CE2 . TYR A 111 ? 0.2505 0.2064 0.6390 -0.0350 0.0945  0.0186  108 TYR A CE2 
946  C  CZ  . TYR A 111 ? 0.2562 0.2474 0.6460 -0.0365 0.0979  0.0079  108 TYR A CZ  
947  O  OH  . TYR A 111 ? 0.3309 0.3335 0.6544 -0.0467 0.1226  0.0108  108 TYR A OH  
948  N  N   . LEU A 112 ? 0.1294 0.1644 0.6123 -0.0138 0.0264  -0.0171 109 LEU A N   
949  C  CA  . LEU A 112 ? 0.1642 0.1478 0.6139 0.0005  0.0404  -0.0099 109 LEU A CA  
950  C  C   . LEU A 112 ? 0.1492 0.1469 0.6224 -0.0091 0.0324  -0.0009 109 LEU A C   
951  O  O   . LEU A 112 ? 0.1565 0.1583 0.6296 -0.0255 0.0271  -0.0010 109 LEU A O   
952  C  CB  . LEU A 112 ? 0.1885 0.1303 0.6188 -0.0023 0.0447  -0.0250 109 LEU A CB  
953  C  CG  . LEU A 112 ? 0.1888 0.1550 0.6297 -0.0079 0.0491  -0.0275 109 LEU A CG  
954  C  CD1 . LEU A 112 ? 0.1783 0.1560 0.6326 -0.0096 0.0514  -0.0281 109 LEU A CD1 
955  C  CD2 . LEU A 112 ? 0.1947 0.1524 0.6365 -0.0203 0.0499  -0.0289 109 LEU A CD2 
956  N  N   . SER A 113 ? 0.1574 0.1500 0.6302 0.0055  0.0267  0.0047  110 SER A N   
957  C  CA  . SER A 113 ? 0.1586 0.1580 0.6320 0.0070  0.0138  -0.0025 110 SER A CA  
958  C  C   . SER A 113 ? 0.1667 0.1714 0.6346 -0.0007 0.0029  -0.0081 110 SER A C   
959  O  O   . SER A 113 ? 0.1764 0.1842 0.6255 -0.0149 0.0055  -0.0220 110 SER A O   
960  C  CB  . SER A 113 ? 0.1871 0.1714 0.6312 0.0004  0.0129  0.0038  110 SER A CB  
961  O  OG  . SER A 113 ? 0.1791 0.1923 0.6253 0.0160  0.0217  -0.0057 110 SER A OG  
962  N  N   . VAL A 114 ? 0.2023 0.1944 0.6533 -0.0002 -0.0179 -0.0144 111 VAL A N   
963  C  CA  . VAL A 114 ? 0.2163 0.2183 0.6673 0.0076  -0.0274 -0.0214 111 VAL A CA  
964  C  C   . VAL A 114 ? 0.2185 0.2164 0.6841 0.0196  -0.0428 -0.0194 111 VAL A C   
965  O  O   . VAL A 114 ? 0.1915 0.1978 0.6769 0.0434  -0.0458 -0.0200 111 VAL A O   
966  C  CB  . VAL A 114 ? 0.2534 0.2527 0.6767 0.0136  -0.0325 -0.0097 111 VAL A CB  
967  C  CG1 . VAL A 114 ? 0.2546 0.2515 0.6838 0.0187  -0.0335 -0.0137 111 VAL A CG1 
968  C  CG2 . VAL A 114 ? 0.2693 0.2647 0.6800 0.0072  -0.0312 -0.0097 111 VAL A CG2 
969  N  N   . TYR A 115 ? 0.2320 0.2335 0.6935 0.0250  -0.0575 -0.0373 112 TYR A N   
970  C  CA  . TYR A 115 ? 0.2531 0.2654 0.7173 0.0347  -0.0760 -0.0577 112 TYR A CA  
971  C  C   . TYR A 115 ? 0.3143 0.3701 0.7459 0.0368  -0.1196 -0.0846 112 TYR A C   
972  O  O   . TYR A 115 ? 0.3153 0.4102 0.7675 0.0537  -0.1584 -0.1152 112 TYR A O   
973  C  CB  . TYR A 115 ? 0.2463 0.2274 0.7067 0.0520  -0.0796 -0.0530 112 TYR A CB  
974  C  CG  . TYR A 115 ? 0.2506 0.2182 0.7073 0.0536  -0.0772 -0.0356 112 TYR A CG  
975  C  CD1 . TYR A 115 ? 0.2528 0.2296 0.7017 0.0326  -0.0782 -0.0260 112 TYR A CD1 
976  C  CD2 . TYR A 115 ? 0.2672 0.2206 0.7005 0.0672  -0.0898 -0.0251 112 TYR A CD2 
977  C  CE1 . TYR A 115 ? 0.2482 0.2237 0.7049 0.0363  -0.0767 -0.0141 112 TYR A CE1 
978  C  CE2 . TYR A 115 ? 0.2846 0.2299 0.7042 0.0684  -0.0765 -0.0274 112 TYR A CE2 
979  C  CZ  . TYR A 115 ? 0.2645 0.2233 0.7025 0.0451  -0.0787 -0.0106 112 TYR A CZ  
980  O  OH  . TYR A 115 ? 0.2277 0.2007 0.6939 0.0271  -0.0849 0.0203  112 TYR A OH  
981  N  N   . ASP A 116 ? 0.3768 0.4066 0.7923 0.0335  -0.1192 -0.0984 113 ASP A N   
982  C  CA  . ASP A 116 ? 0.4057 0.4945 0.8196 0.0266  -0.1362 -0.1071 113 ASP A CA  
983  C  C   . ASP A 116 ? 0.4682 0.5562 0.8347 0.0596  -0.1417 -0.1021 113 ASP A C   
984  O  O   . ASP A 116 ? 0.5043 0.5886 0.8422 0.0403  -0.1567 -0.1008 113 ASP A O   
985  C  CB  . ASP A 116 ? 0.4654 0.5164 0.8400 0.0304  -0.1175 -0.0955 113 ASP A CB  
986  C  CG  . ASP A 116 ? 0.4784 0.5547 0.8652 0.0254  -0.1101 -0.0930 113 ASP A CG  
987  O  OD1 . ASP A 116 ? 0.5443 0.5859 0.8852 0.0508  -0.0776 -0.0951 113 ASP A OD1 
988  O  OD2 . ASP A 116 ? 0.5213 0.5481 0.8819 0.0103  -0.0967 -0.0813 113 ASP A OD2 
989  N  N   . THR A 117 ? 0.5031 0.5854 0.8429 0.0953  -0.1327 -0.1000 114 THR A N   
990  C  CA  . THR A 117 ? 0.5555 0.6234 0.8500 0.1412  -0.1341 -0.1087 114 THR A CA  
991  C  C   . THR A 117 ? 0.5872 0.6334 0.8625 0.1743  -0.1371 -0.1089 114 THR A C   
992  O  O   . THR A 117 ? 0.6332 0.6768 0.8648 0.1861  -0.1386 -0.1112 114 THR A O   
993  C  CB  . THR A 117 ? 0.5794 0.6469 0.8515 0.1524  -0.1317 -0.1090 114 THR A CB  
994  O  OG1 . THR A 117 ? 0.5783 0.6713 0.8551 0.1538  -0.1260 -0.1013 114 THR A OG1 
995  C  CG2 . THR A 117 ? 0.5699 0.6295 0.8475 0.1702  -0.1323 -0.1190 114 THR A CG2 
996  N  N   . ASN A 118 ? 0.5684 0.6015 0.8662 0.2020  -0.1357 -0.1214 115 ASN A N   
997  C  CA  . ASN A 118 ? 0.5802 0.6116 0.8636 0.2107  -0.1409 -0.1101 115 ASN A CA  
998  C  C   . ASN A 118 ? 0.5950 0.6108 0.8652 0.2242  -0.1489 -0.1172 115 ASN A C   
999  O  O   . ASN A 118 ? 0.5884 0.5727 0.8882 0.2657  -0.1537 -0.1022 115 ASN A O   
1000 C  CB  . ASN A 118 ? 0.5688 0.6168 0.8607 0.2103  -0.1392 -0.1086 115 ASN A CB  
1001 C  CG  . ASN A 118 ? 0.5674 0.6350 0.8609 0.2155  -0.1307 -0.1078 115 ASN A CG  
1002 O  OD1 . ASN A 118 ? 0.5816 0.6563 0.8521 0.2144  -0.1234 -0.0993 115 ASN A OD1 
1003 N  ND2 . ASN A 118 ? 0.5776 0.6295 0.8532 0.2296  -0.1297 -0.1167 115 ASN A ND2 
1004 N  N   . SER A 119 ? 0.6062 0.6157 0.8625 0.2265  -0.1517 -0.1148 116 SER A N   
1005 C  CA  . SER A 119 ? 0.6128 0.5874 0.8618 0.2234  -0.1617 -0.1129 116 SER A CA  
1006 C  C   . SER A 119 ? 0.6226 0.5856 0.8631 0.2190  -0.1560 -0.1195 116 SER A C   
1007 O  O   . SER A 119 ? 0.6408 0.5457 0.8516 0.2234  -0.1612 -0.1192 116 SER A O   
1008 C  CB  . SER A 119 ? 0.6011 0.6076 0.8672 0.2221  -0.1648 -0.1116 116 SER A CB  
1009 O  OG  . SER A 119 ? 0.5765 0.6148 0.8684 0.2151  -0.1689 -0.1148 116 SER A OG  
1010 N  N   . SER A 120 ? 0.6700 0.5597 0.8658 0.2006  -0.1506 -0.1179 117 SER A N   
1011 C  CA  . SER A 120 ? 0.6605 0.5616 0.8601 0.2128  -0.1520 -0.1224 117 SER A CA  
1012 C  C   . SER A 120 ? 0.6513 0.4772 0.8685 0.2332  -0.1523 -0.1178 117 SER A C   
1013 O  O   . SER A 120 ? 0.6488 0.4780 0.8678 0.2424  -0.1645 -0.0981 117 SER A O   
1014 C  CB  . SER A 120 ? 0.6554 0.5980 0.8679 0.1950  -0.1590 -0.1248 117 SER A CB  
1015 O  OG  . SER A 120 ? 0.6685 0.6449 0.8661 0.1792  -0.1675 -0.1315 117 SER A OG  
1016 N  N   . ALA A 121 ? 0.6332 0.4768 0.8561 0.2250  -0.1479 -0.1248 118 ALA A N   
1017 C  CA  . ALA A 121 ? 0.6002 0.4349 0.8483 0.2164  -0.1431 -0.1205 118 ALA A CA  
1018 C  C   . ALA A 121 ? 0.5823 0.4093 0.8429 0.1972  -0.1434 -0.1251 118 ALA A C   
1019 O  O   . ALA A 121 ? 0.5903 0.4165 0.8470 0.1856  -0.1177 -0.1341 118 ALA A O   
1020 C  CB  . ALA A 121 ? 0.5853 0.4420 0.8533 0.2178  -0.1404 -0.1237 118 ALA A CB  
1021 N  N   . ILE A 122 ? 0.5590 0.3885 0.8280 0.1959  -0.1428 -0.1186 119 ILE A N   
1022 C  CA  . ILE A 122 ? 0.5647 0.3646 0.8235 0.1768  -0.1453 -0.1160 119 ILE A CA  
1023 C  C   . ILE A 122 ? 0.5593 0.3265 0.8155 0.1595  -0.1492 -0.1135 119 ILE A C   
1024 O  O   . ILE A 122 ? 0.5585 0.2897 0.8206 0.1546  -0.1551 -0.1140 119 ILE A O   
1025 C  CB  . ILE A 122 ? 0.5512 0.3547 0.8204 0.1862  -0.1343 -0.1193 119 ILE A CB  
1026 C  CG1 . ILE A 122 ? 0.5408 0.3643 0.8164 0.1857  -0.1271 -0.1205 119 ILE A CG1 
1027 C  CG2 . ILE A 122 ? 0.5542 0.3513 0.8299 0.1869  -0.1334 -0.1187 119 ILE A CG2 
1028 C  CD1 . ILE A 122 ? 0.5373 0.3629 0.8117 0.1831  -0.1246 -0.1219 119 ILE A CD1 
1029 N  N   . ARG A 123 ? 0.5695 0.3190 0.8105 0.1356  -0.1513 -0.1046 120 ARG A N   
1030 C  CA  . ARG A 123 ? 0.5468 0.3643 0.8060 0.1180  -0.1609 -0.0950 120 ARG A CA  
1031 C  C   . ARG A 123 ? 0.5427 0.3633 0.7982 0.1004  -0.1559 -0.0914 120 ARG A C   
1032 O  O   . ARG A 123 ? 0.5653 0.3968 0.7966 0.0957  -0.1604 -0.1085 120 ARG A O   
1033 C  CB  . ARG A 123 ? 0.5703 0.3970 0.8123 0.1137  -0.1560 -0.0927 120 ARG A CB  
1034 C  CG  . ARG A 123 ? 0.5910 0.4438 0.8222 0.0943  -0.1589 -0.0901 120 ARG A CG  
1035 C  CD  . ARG A 123 ? 0.6198 0.4685 0.8317 0.0891  -0.1546 -0.0861 120 ARG A CD  
1036 N  NE  . ARG A 123 ? 0.6481 0.4972 0.8473 0.0715  -0.1464 -0.0929 120 ARG A NE  
1037 C  CZ  . ARG A 123 ? 0.6718 0.5208 0.8530 0.0596  -0.1491 -0.0845 120 ARG A CZ  
1038 N  NH1 . ARG A 123 ? 0.6860 0.5283 0.8542 0.0570  -0.1488 -0.0762 120 ARG A NH1 
1039 N  NH2 . ARG A 123 ? 0.6737 0.5483 0.8600 0.0394  -0.1505 -0.0892 120 ARG A NH2 
1040 N  N   . LEU A 124 ? 0.5427 0.3484 0.7901 0.0799  -0.1312 -0.0798 121 LEU A N   
1041 C  CA  . LEU A 124 ? 0.5069 0.3617 0.7806 0.0720  -0.1151 -0.0823 121 LEU A CA  
1042 C  C   . LEU A 124 ? 0.4462 0.3252 0.7715 0.0670  -0.1078 -0.0824 121 LEU A C   
1043 O  O   . LEU A 124 ? 0.4556 0.3226 0.7746 0.0634  -0.0963 -0.0831 121 LEU A O   
1044 C  CB  . LEU A 124 ? 0.5236 0.4008 0.7868 0.0591  -0.1122 -0.0800 121 LEU A CB  
1045 C  CG  . LEU A 124 ? 0.5465 0.4306 0.7907 0.0428  -0.1087 -0.0893 121 LEU A CG  
1046 C  CD1 . LEU A 124 ? 0.5573 0.4479 0.7959 0.0377  -0.1034 -0.0892 121 LEU A CD1 
1047 C  CD2 . LEU A 124 ? 0.5625 0.4447 0.7912 0.0440  -0.1071 -0.0885 121 LEU A CD2 
1048 N  N   . TYR A 125 ? 0.3988 0.3227 0.7671 0.0499  -0.0909 -0.0746 122 TYR A N   
1049 C  CA  . TYR A 125 ? 0.3425 0.2775 0.7640 0.0504  -0.0923 -0.0669 122 TYR A CA  
1050 C  C   . TYR A 125 ? 0.3354 0.2809 0.7653 0.0454  -0.1021 -0.0677 122 TYR A C   
1051 O  O   . TYR A 125 ? 0.2859 0.2344 0.7662 0.0300  -0.1169 -0.0642 122 TYR A O   
1052 C  CB  . TYR A 125 ? 0.3183 0.2438 0.7687 0.0485  -0.0755 -0.0688 122 TYR A CB  
1053 C  CG  . TYR A 125 ? 0.3163 0.2277 0.7629 0.0534  -0.0745 -0.0667 122 TYR A CG  
1054 C  CD1 . TYR A 125 ? 0.3177 0.2182 0.7713 0.0635  -0.0647 -0.0686 122 TYR A CD1 
1055 C  CD2 . TYR A 125 ? 0.3029 0.2255 0.7602 0.0502  -0.0651 -0.0715 122 TYR A CD2 
1056 C  CE1 . TYR A 125 ? 0.3264 0.1994 0.7725 0.0499  -0.0647 -0.0767 122 TYR A CE1 
1057 C  CE2 . TYR A 125 ? 0.3012 0.2074 0.7583 0.0532  -0.0661 -0.0707 122 TYR A CE2 
1058 C  CZ  . TYR A 125 ? 0.3096 0.2162 0.7722 0.0513  -0.0590 -0.0628 122 TYR A CZ  
1059 O  OH  . TYR A 125 ? 0.3197 0.2787 0.7868 0.0355  -0.0585 -0.0404 122 TYR A OH  
1060 N  N   . GLN A 126 ? 0.3376 0.2847 0.7775 0.0416  -0.1086 -0.0666 123 GLN A N   
1061 C  CA  . GLN A 126 ? 0.3442 0.3074 0.7838 0.0533  -0.1090 -0.0647 123 GLN A CA  
1062 C  C   . GLN A 126 ? 0.3409 0.2990 0.7737 0.0423  -0.1112 -0.0541 123 GLN A C   
1063 O  O   . GLN A 126 ? 0.3127 0.3142 0.7708 0.0517  -0.1224 -0.0392 123 GLN A O   
1064 C  CB  . GLN A 126 ? 0.3782 0.3231 0.7916 0.0595  -0.1127 -0.0757 123 GLN A CB  
1065 C  CG  . GLN A 126 ? 0.4111 0.3319 0.7978 0.0671  -0.1153 -0.0747 123 GLN A CG  
1066 C  CD  . GLN A 126 ? 0.4415 0.3666 0.7963 0.0695  -0.1155 -0.0888 123 GLN A CD  
1067 O  OE1 . GLN A 126 ? 0.4877 0.4069 0.7964 0.0850  -0.1102 -0.0890 123 GLN A OE1 
1068 N  NE2 . GLN A 126 ? 0.4241 0.3633 0.7960 0.0671  -0.1216 -0.0979 123 GLN A NE2 
1069 N  N   . GLN A 127 ? 0.3405 0.2961 0.7739 0.0426  -0.1088 -0.0451 124 GLN A N   
1070 C  CA  . GLN A 127 ? 0.3485 0.2942 0.7778 0.0352  -0.1004 -0.0292 124 GLN A CA  
1071 C  C   . GLN A 127 ? 0.3097 0.2562 0.7736 0.0363  -0.0886 -0.0172 124 GLN A C   
1072 O  O   . GLN A 127 ? 0.3286 0.2370 0.7818 0.0361  -0.0942 -0.0331 124 GLN A O   
1073 C  CB  . GLN A 127 ? 0.3921 0.3224 0.7885 0.0373  -0.0932 -0.0251 124 GLN A CB  
1074 C  CG  . GLN A 127 ? 0.4278 0.3674 0.8007 0.0286  -0.0840 -0.0301 124 GLN A CG  
1075 C  CD  . GLN A 127 ? 0.4779 0.4122 0.8123 0.0153  -0.0703 -0.0263 124 GLN A CD  
1076 O  OE1 . GLN A 127 ? 0.5098 0.4483 0.8296 -0.0198 -0.0554 -0.0398 124 GLN A OE1 
1077 N  NE2 . GLN A 127 ? 0.5081 0.4252 0.8179 0.0169  -0.0696 -0.0239 124 GLN A NE2 
1078 N  N   . LEU A 128 ? 0.2949 0.2537 0.7576 0.0147  -0.0746 -0.0094 125 LEU A N   
1079 C  CA  . LEU A 128 ? 0.2405 0.2363 0.7505 -0.0173 -0.0592 0.0004  125 LEU A CA  
1080 C  C   . LEU A 128 ? 0.2201 0.1987 0.7378 -0.0064 -0.0516 -0.0097 125 LEU A C   
1081 O  O   . LEU A 128 ? 0.2516 0.1937 0.7305 -0.0034 -0.0476 -0.0052 125 LEU A O   
1082 C  CB  . LEU A 128 ? 0.2414 0.2679 0.7559 -0.0334 -0.0571 0.0083  125 LEU A CB  
1083 C  CG  . LEU A 128 ? 0.2362 0.3151 0.7675 -0.0656 -0.0432 0.0071  125 LEU A CG  
1084 C  CD1 . LEU A 128 ? 0.2326 0.3388 0.7770 -0.0811 -0.0356 0.0046  125 LEU A CD1 
1085 C  CD2 . LEU A 128 ? 0.2534 0.2958 0.7757 -0.0884 -0.0376 0.0093  125 LEU A CD2 
1086 N  N   . GLY A 129 ? 0.1777 0.1946 0.7296 0.0039  -0.0517 -0.0163 126 GLY A N   
1087 C  CA  . GLY A 129 ? 0.1692 0.2054 0.7237 0.0101  -0.0438 -0.0168 126 GLY A CA  
1088 C  C   . GLY A 129 ? 0.1817 0.2094 0.7247 0.0130  -0.0397 -0.0136 126 GLY A C   
1089 O  O   . GLY A 129 ? 0.1795 0.2317 0.7345 -0.0047 -0.0409 -0.0085 126 GLY A O   
1090 N  N   . PHE A 130 ? 0.1697 0.1659 0.7077 0.0011  -0.0458 -0.0277 127 PHE A N   
1091 C  CA  . PHE A 130 ? 0.1677 0.1653 0.6988 0.0082  -0.0438 -0.0314 127 PHE A CA  
1092 C  C   . PHE A 130 ? 0.1709 0.1915 0.7100 -0.0023 -0.0555 -0.0444 127 PHE A C   
1093 O  O   . PHE A 130 ? 0.2002 0.2545 0.7131 0.0207  -0.0601 -0.0527 127 PHE A O   
1094 C  CB  . PHE A 130 ? 0.1718 0.1518 0.6863 0.0036  -0.0369 -0.0302 127 PHE A CB  
1095 C  CG  . PHE A 130 ? 0.1758 0.1666 0.6647 0.0064  -0.0407 -0.0301 127 PHE A CG  
1096 C  CD1 . PHE A 130 ? 0.1810 0.1682 0.6586 0.0103  -0.0406 -0.0341 127 PHE A CD1 
1097 C  CD2 . PHE A 130 ? 0.1903 0.1651 0.6535 0.0050  -0.0323 -0.0344 127 PHE A CD2 
1098 C  CE1 . PHE A 130 ? 0.1721 0.1700 0.6552 0.0105  -0.0388 -0.0287 127 PHE A CE1 
1099 C  CE2 . PHE A 130 ? 0.1809 0.1717 0.6493 -0.0019 -0.0309 -0.0287 127 PHE A CE2 
1100 C  CZ  . PHE A 130 ? 0.1592 0.1596 0.6497 0.0080  -0.0434 -0.0371 127 PHE A CZ  
1101 N  N   . VAL A 131 ? 0.1881 0.1718 0.7230 -0.0109 -0.0542 -0.0425 128 VAL A N   
1102 C  CA  . VAL A 131 ? 0.2161 0.1737 0.7380 -0.0187 -0.0568 -0.0441 128 VAL A CA  
1103 C  C   . VAL A 131 ? 0.2108 0.1708 0.7491 -0.0095 -0.0586 -0.0509 128 VAL A C   
1104 O  O   . VAL A 131 ? 0.2446 0.1986 0.7612 -0.0085 -0.0588 -0.0351 128 VAL A O   
1105 C  CB  . VAL A 131 ? 0.2239 0.1643 0.7355 -0.0330 -0.0475 -0.0450 128 VAL A CB  
1106 C  CG1 . VAL A 131 ? 0.2111 0.1528 0.7421 -0.0334 -0.0472 -0.0518 128 VAL A CG1 
1107 C  CG2 . VAL A 131 ? 0.2337 0.1696 0.7308 -0.0411 -0.0352 -0.0430 128 VAL A CG2 
1108 N  N   . PHE A 132 ? 0.2161 0.1843 0.7458 -0.0151 -0.0561 -0.0503 129 PHE A N   
1109 C  CA  . PHE A 132 ? 0.1952 0.1957 0.7385 0.0000  -0.0367 -0.0490 129 PHE A CA  
1110 C  C   . PHE A 132 ? 0.1714 0.1970 0.7469 -0.0032 -0.0166 -0.0361 129 PHE A C   
1111 O  O   . PHE A 132 ? 0.1617 0.2167 0.7529 -0.0118 -0.0051 -0.0314 129 PHE A O   
1112 C  CB  . PHE A 132 ? 0.2100 0.1976 0.7421 -0.0020 -0.0599 -0.0557 129 PHE A CB  
1113 C  CG  . PHE A 132 ? 0.2481 0.2069 0.7246 0.0085  -0.0756 -0.0554 129 PHE A CG  
1114 C  CD1 . PHE A 132 ? 0.2458 0.1926 0.7123 0.0040  -0.0902 -0.0568 129 PHE A CD1 
1115 C  CD2 . PHE A 132 ? 0.2400 0.2137 0.7265 0.0071  -0.0926 -0.0622 129 PHE A CD2 
1116 C  CE1 . PHE A 132 ? 0.2501 0.2308 0.7111 0.0111  -0.1013 -0.0579 129 PHE A CE1 
1117 C  CE2 . PHE A 132 ? 0.2598 0.2572 0.7248 0.0091  -0.0870 -0.0563 129 PHE A CE2 
1118 C  CZ  . PHE A 132 ? 0.2589 0.2434 0.7185 0.0232  -0.0963 -0.0521 129 PHE A CZ  
1119 N  N   . ASN A 133 ? 0.1892 0.1830 0.7289 -0.0087 0.0079  -0.0267 130 ASN A N   
1120 C  CA  . ASN A 133 ? 0.2242 0.2007 0.7300 -0.0168 0.0432  -0.0174 130 ASN A CA  
1121 C  C   . ASN A 133 ? 0.2415 0.1931 0.7240 -0.0393 0.0486  -0.0131 130 ASN A C   
1122 O  O   . ASN A 133 ? 0.2546 0.2011 0.7361 -0.0477 0.0591  -0.0235 130 ASN A O   
1123 C  CB  . ASN A 133 ? 0.2478 0.2207 0.7202 -0.0177 0.0606  -0.0163 130 ASN A CB  
1124 C  CG  . ASN A 133 ? 0.2397 0.1872 0.7126 -0.0195 0.0767  -0.0216 130 ASN A CG  
1125 O  OD1 . ASN A 133 ? 0.2466 0.1496 0.7144 -0.0158 0.0890  -0.0052 130 ASN A OD1 
1126 N  ND2 . ASN A 133 ? 0.2564 0.1735 0.7147 -0.0246 0.0818  -0.0209 130 ASN A ND2 
1127 N  N   . GLY A 134 ? 0.2368 0.2055 0.7075 -0.0284 0.0398  -0.0040 131 GLY A N   
1128 C  CA  . GLY A 134 ? 0.2387 0.2083 0.6974 -0.0395 0.0305  0.0043  131 GLY A CA  
1129 C  C   . GLY A 134 ? 0.2374 0.1974 0.6914 -0.0417 0.0311  0.0081  131 GLY A C   
1130 O  O   . GLY A 134 ? 0.2418 0.2068 0.6960 -0.0498 0.0286  0.0189  131 GLY A O   
1131 N  N   . GLU A 135 ? 0.2243 0.2019 0.6740 -0.0430 0.0420  0.0170  132 GLU A N   
1132 C  CA  . GLU A 135 ? 0.2489 0.1924 0.6614 -0.0456 0.0341  0.0143  132 GLU A CA  
1133 C  C   . GLU A 135 ? 0.2316 0.1860 0.6398 -0.0395 0.0181  0.0128  132 GLU A C   
1134 O  O   . GLU A 135 ? 0.2082 0.1889 0.6328 -0.0292 0.0077  0.0156  132 GLU A O   
1135 C  CB  . GLU A 135 ? 0.2644 0.2149 0.6671 -0.0546 0.0483  0.0036  132 GLU A CB  
1136 C  CG  . GLU A 135 ? 0.2892 0.2378 0.6728 -0.0594 0.0604  0.0028  132 GLU A CG  
1137 C  CD  . GLU A 135 ? 0.3146 0.2656 0.6762 -0.0616 0.0593  -0.0072 132 GLU A CD  
1138 O  OE1 . GLU A 135 ? 0.3262 0.2756 0.6925 -0.0753 0.0584  -0.0112 132 GLU A OE1 
1139 O  OE2 . GLU A 135 ? 0.3478 0.2621 0.6777 -0.0588 0.0555  -0.0203 132 GLU A OE2 
1140 N  N   . LEU A 136 ? 0.2299 0.1693 0.6321 -0.0348 0.0192  0.0059  133 LEU A N   
1141 C  CA  . LEU A 136 ? 0.2278 0.1855 0.6285 -0.0395 0.0118  0.0050  133 LEU A CA  
1142 C  C   . LEU A 136 ? 0.2285 0.1947 0.6224 -0.0261 0.0008  0.0034  133 LEU A C   
1143 O  O   . LEU A 136 ? 0.2342 0.2227 0.6135 -0.0295 -0.0038 0.0009  133 LEU A O   
1144 C  CB  . LEU A 136 ? 0.2512 0.1954 0.6314 -0.0325 0.0130  -0.0002 133 LEU A CB  
1145 C  CG  . LEU A 136 ? 0.2471 0.2036 0.6305 -0.0400 0.0103  0.0008  133 LEU A CG  
1146 C  CD1 . LEU A 136 ? 0.2731 0.2070 0.6353 -0.0320 0.0119  -0.0057 133 LEU A CD1 
1147 C  CD2 . LEU A 136 ? 0.2295 0.2081 0.6276 -0.0395 0.0073  -0.0029 133 LEU A CD2 
1148 N  N   . ASP A 137 ? 0.2167 0.1707 0.6286 -0.0144 -0.0030 0.0096  134 ASP A N   
1149 C  CA  . ASP A 137 ? 0.2077 0.1913 0.6409 -0.0156 -0.0054 0.0169  134 ASP A CA  
1150 C  C   . ASP A 137 ? 0.2162 0.1910 0.6500 -0.0157 -0.0119 0.0224  134 ASP A C   
1151 O  O   . ASP A 137 ? 0.1943 0.1603 0.6554 -0.0242 -0.0129 0.0431  134 ASP A O   
1152 C  CB  . ASP A 137 ? 0.1931 0.1674 0.6406 -0.0105 -0.0151 0.0092  134 ASP A CB  
1153 C  CG  . ASP A 137 ? 0.1773 0.1887 0.6376 -0.0169 -0.0190 0.0093  134 ASP A CG  
1154 O  OD1 . ASP A 137 ? 0.1892 0.2025 0.6341 -0.0356 -0.0250 0.0074  134 ASP A OD1 
1155 O  OD2 . ASP A 137 ? 0.1888 0.1859 0.6448 0.0142  -0.0156 0.0081  134 ASP A OD2 
1156 N  N   . THR A 138 ? 0.2199 0.2106 0.6669 -0.0231 -0.0205 0.0287  135 THR A N   
1157 C  CA  . THR A 138 ? 0.2269 0.2068 0.6736 -0.0090 -0.0173 0.0236  135 THR A CA  
1158 C  C   . THR A 138 ? 0.2055 0.2137 0.6740 0.0013  -0.0194 0.0243  135 THR A C   
1159 O  O   . THR A 138 ? 0.2169 0.2308 0.6909 0.0216  -0.0224 0.0264  135 THR A O   
1160 C  CB  . THR A 138 ? 0.2687 0.2433 0.6746 -0.0133 -0.0267 0.0309  135 THR A CB  
1161 O  OG1 . THR A 138 ? 0.2831 0.2435 0.6925 -0.0504 -0.0351 0.0248  135 THR A OG1 
1162 C  CG2 . THR A 138 ? 0.2825 0.2556 0.6760 -0.0059 -0.0326 0.0312  135 THR A CG2 
1163 N  N   . ASN A 139 ? 0.1690 0.2068 0.6602 -0.0072 -0.0156 0.0151  136 ASN A N   
1164 C  CA  . ASN A 139 ? 0.1776 0.2255 0.6567 0.0027  0.0003  0.0079  136 ASN A CA  
1165 C  C   . ASN A 139 ? 0.1897 0.2623 0.6606 -0.0052 -0.0041 0.0000  136 ASN A C   
1166 O  O   . ASN A 139 ? 0.2080 0.3108 0.6831 0.0119  0.0111  -0.0055 136 ASN A O   
1167 C  CB  . ASN A 139 ? 0.1770 0.2251 0.6415 -0.0123 0.0111  -0.0003 136 ASN A CB  
1168 C  CG  . ASN A 139 ? 0.1762 0.2213 0.6241 -0.0126 0.0241  0.0035  136 ASN A CG  
1169 O  OD1 . ASN A 139 ? 0.1700 0.1932 0.6001 -0.0107 0.0228  -0.0121 136 ASN A OD1 
1170 N  ND2 . ASN A 139 ? 0.1863 0.2327 0.6199 -0.0255 0.0278  0.0107  136 ASN A ND2 
1171 N  N   . GLY A 140 ? 0.1997 0.2487 0.6549 -0.0130 -0.0158 -0.0055 137 GLY A N   
1172 C  CA  . GLY A 140 ? 0.1909 0.2159 0.6525 -0.0015 -0.0261 -0.0015 137 GLY A CA  
1173 C  C   . GLY A 140 ? 0.1854 0.1814 0.6432 -0.0100 -0.0320 -0.0170 137 GLY A C   
1174 O  O   . GLY A 140 ? 0.1723 0.1687 0.6596 -0.0325 -0.0204 -0.0217 137 GLY A O   
1175 N  N   . GLU A 141 ? 0.1665 0.1724 0.6386 0.0043  -0.0318 -0.0202 138 GLU A N   
1176 C  CA  . GLU A 141 ? 0.1731 0.1726 0.6288 -0.0031 -0.0235 -0.0159 138 GLU A CA  
1177 C  C   . GLU A 141 ? 0.1848 0.1853 0.6243 -0.0164 -0.0146 -0.0182 138 GLU A C   
1178 O  O   . GLU A 141 ? 0.1649 0.2190 0.6261 -0.0282 -0.0053 -0.0187 138 GLU A O   
1179 C  CB  . GLU A 141 ? 0.1643 0.1680 0.6258 0.0006  -0.0197 -0.0162 138 GLU A CB  
1180 C  CG  . GLU A 141 ? 0.1626 0.1790 0.6277 -0.0101 -0.0235 -0.0164 138 GLU A CG  
1181 C  CD  . GLU A 141 ? 0.1996 0.1851 0.6324 -0.0085 -0.0172 -0.0162 138 GLU A CD  
1182 O  OE1 . GLU A 141 ? 0.2388 0.2271 0.6540 -0.0066 -0.0145 -0.0335 138 GLU A OE1 
1183 O  OE2 . GLU A 141 ? 0.2337 0.1980 0.6327 -0.0076 -0.0257 -0.0265 138 GLU A OE2 
1184 N  N   . ARG A 142 ? 0.1967 0.1708 0.6271 -0.0042 -0.0122 -0.0191 139 ARG A N   
1185 C  CA  . ARG A 142 ? 0.2026 0.1528 0.6284 -0.0022 -0.0137 -0.0243 139 ARG A CA  
1186 C  C   . ARG A 142 ? 0.2077 0.1421 0.6285 -0.0139 -0.0049 -0.0190 139 ARG A C   
1187 O  O   . ARG A 142 ? 0.1814 0.1503 0.6291 -0.0210 -0.0099 -0.0257 139 ARG A O   
1188 C  CB  . ARG A 142 ? 0.2387 0.1951 0.6362 -0.0003 -0.0259 -0.0307 139 ARG A CB  
1189 C  CG  . ARG A 142 ? 0.2691 0.2095 0.6447 0.0063  -0.0316 -0.0391 139 ARG A CG  
1190 C  CD  . ARG A 142 ? 0.3250 0.2324 0.6525 0.0154  -0.0368 -0.0375 139 ARG A CD  
1191 N  NE  . ARG A 142 ? 0.3417 0.2637 0.6690 0.0254  -0.0438 -0.0356 139 ARG A NE  
1192 C  CZ  . ARG A 142 ? 0.3557 0.2390 0.6827 0.0541  -0.0525 -0.0344 139 ARG A CZ  
1193 N  NH1 . ARG A 142 ? 0.3530 0.2335 0.6877 0.0669  -0.0538 -0.0421 139 ARG A NH1 
1194 N  NH2 . ARG A 142 ? 0.3837 0.2576 0.6897 0.0595  -0.0400 -0.0343 139 ARG A NH2 
1195 N  N   . VAL A 143 ? 0.1820 0.1246 0.6334 -0.0148 0.0043  -0.0131 140 VAL A N   
1196 C  CA  . VAL A 143 ? 0.1858 0.1272 0.6421 -0.0173 0.0024  -0.0088 140 VAL A CA  
1197 C  C   . VAL A 143 ? 0.1954 0.1286 0.6625 -0.0128 -0.0072 -0.0144 140 VAL A C   
1198 O  O   . VAL A 143 ? 0.1708 0.1217 0.6670 0.0044  -0.0141 -0.0147 140 VAL A O   
1199 C  CB  . VAL A 143 ? 0.1891 0.1430 0.6386 -0.0259 0.0142  -0.0016 140 VAL A CB  
1200 C  CG1 . VAL A 143 ? 0.2257 0.1562 0.6420 -0.0268 0.0118  -0.0052 140 VAL A CG1 
1201 C  CG2 . VAL A 143 ? 0.1925 0.1355 0.6368 -0.0262 0.0159  0.0031  140 VAL A CG2 
1202 N  N   . MET A 144 ? 0.1867 0.1249 0.6810 -0.0224 -0.0170 -0.0203 141 MET A N   
1203 C  CA  . MET A 144 ? 0.1733 0.1415 0.7004 -0.0195 -0.0250 -0.0176 141 MET A CA  
1204 C  C   . MET A 144 ? 0.1927 0.1589 0.7029 -0.0034 -0.0249 -0.0162 141 MET A C   
1205 O  O   . MET A 144 ? 0.1872 0.1649 0.6921 0.0288  -0.0193 -0.0209 141 MET A O   
1206 C  CB  . MET A 144 ? 0.1792 0.1790 0.7135 -0.0017 -0.0365 -0.0131 141 MET A CB  
1207 C  CG  . MET A 144 ? 0.2019 0.1862 0.7342 -0.0243 -0.0486 -0.0226 141 MET A CG  
1208 S  SD  . MET A 144 ? 0.2606 0.2712 0.7605 -0.0120 -0.0751 -0.0094 141 MET A SD  
1209 C  CE  . MET A 144 ? 0.2749 0.3044 0.7625 -0.0030 -0.0683 -0.0009 141 MET A CE  
1210 N  N   . GLU A 145 ? 0.1975 0.1680 0.7181 0.0049  -0.0275 -0.0226 142 GLU A N   
1211 C  CA  . GLU A 145 ? 0.1948 0.2024 0.7296 0.0185  -0.0162 -0.0093 142 GLU A CA  
1212 C  C   . GLU A 145 ? 0.1891 0.2045 0.7351 0.0116  -0.0226 -0.0005 142 GLU A C   
1213 O  O   . GLU A 145 ? 0.1823 0.2044 0.7381 -0.0069 -0.0162 0.0019  142 GLU A O   
1214 C  CB  . GLU A 145 ? 0.2325 0.2366 0.7485 0.0103  -0.0012 -0.0041 142 GLU A CB  
1215 C  CG  . GLU A 145 ? 0.2444 0.2655 0.7563 0.0070  0.0086  -0.0123 142 GLU A CG  
1216 C  CD  . GLU A 145 ? 0.2618 0.2919 0.7671 0.0091  0.0218  -0.0067 142 GLU A CD  
1217 O  OE1 . GLU A 145 ? 0.2620 0.3018 0.7915 0.0173  0.0255  -0.0198 142 GLU A OE1 
1218 O  OE2 . GLU A 145 ? 0.2545 0.3498 0.7638 -0.0020 0.0215  -0.0108 142 GLU A OE2 
1219 N  N   . TRP A 146 ? 0.1700 0.2095 0.7331 -0.0011 -0.0193 0.0042  143 TRP A N   
1220 C  CA  . TRP A 146 ? 0.1852 0.2298 0.7455 0.0145  -0.0223 0.0030  143 TRP A CA  
1221 C  C   . TRP A 146 ? 0.2293 0.2509 0.7467 0.0126  -0.0084 0.0067  143 TRP A C   
1222 O  O   . TRP A 146 ? 0.1923 0.2198 0.7292 0.0318  0.0013  0.0109  143 TRP A O   
1223 C  CB  . TRP A 146 ? 0.2005 0.2246 0.7494 0.0084  -0.0380 -0.0003 143 TRP A CB  
1224 C  CG  . TRP A 146 ? 0.2192 0.2430 0.7625 0.0189  -0.0594 -0.0102 143 TRP A CG  
1225 C  CD1 . TRP A 146 ? 0.2634 0.2497 0.7702 0.0434  -0.0660 -0.0084 143 TRP A CD1 
1226 C  CD2 . TRP A 146 ? 0.2404 0.2356 0.7802 0.0490  -0.0672 -0.0151 143 TRP A CD2 
1227 N  NE1 . TRP A 146 ? 0.2732 0.2518 0.7736 0.0404  -0.0745 -0.0137 143 TRP A NE1 
1228 C  CE2 . TRP A 146 ? 0.2517 0.2238 0.7795 0.0445  -0.0747 -0.0209 143 TRP A CE2 
1229 C  CE3 . TRP A 146 ? 0.3056 0.2500 0.7789 0.0792  -0.0710 -0.0209 143 TRP A CE3 
1230 C  CZ2 . TRP A 146 ? 0.2779 0.2476 0.7912 0.0575  -0.0813 -0.0355 143 TRP A CZ2 
1231 C  CZ3 . TRP A 146 ? 0.3364 0.2515 0.7916 0.0768  -0.0758 -0.0313 143 TRP A CZ3 
1232 C  CH2 . TRP A 146 ? 0.3184 0.2513 0.7901 0.0799  -0.0742 -0.0426 143 TRP A CH2 
1233 N  N   . THR A 147 ? 0.2388 0.2971 0.7746 0.0154  0.0086  0.0022  144 THR A N   
1234 C  CA  . THR A 147 ? 0.3148 0.3463 0.7916 0.0376  0.0228  -0.0113 144 THR A CA  
1235 C  C   . THR A 147 ? 0.4138 0.3778 0.8123 0.0661  0.0108  0.0056  144 THR A C   
1236 O  O   . THR A 147 ? 0.4488 0.3874 0.8086 0.0897  0.0127  0.0151  144 THR A O   
1237 C  CB  . THR A 147 ? 0.3029 0.3884 0.7966 0.0425  0.0427  -0.0081 144 THR A CB  
1238 O  OG1 . THR A 147 ? 0.2683 0.4033 0.8013 0.0527  0.0573  -0.0086 144 THR A OG1 
1239 C  CG2 . THR A 147 ? 0.3206 0.4226 0.7997 0.0376  0.0452  -0.0151 144 THR A CG2 
1240 N  N   . HIS A 148 ? 0.4981 0.4036 0.8290 0.0645  0.0007  -0.0008 145 HIS A N   
1241 C  CA  . HIS A 148 ? 0.5264 0.4167 0.8458 0.0735  -0.0113 0.0174  145 HIS A CA  
1242 C  C   . HIS A 148 ? 0.5181 0.4564 0.8305 0.0509  -0.0141 0.0092  145 HIS A C   
1243 O  O   . HIS A 148 ? 0.4999 0.4854 0.8413 0.0526  -0.0140 0.0045  145 HIS A O   
1244 C  CB  . HIS A 148 ? 0.5566 0.3958 0.8567 0.0883  -0.0270 0.0234  145 HIS A CB  
1245 C  CG  . HIS A 148 ? 0.5997 0.4099 0.8830 0.1071  -0.0399 0.0452  145 HIS A CG  
1246 N  ND1 . HIS A 148 ? 0.6186 0.4186 0.8903 0.0951  -0.0440 0.0476  145 HIS A ND1 
1247 C  CD2 . HIS A 148 ? 0.6197 0.4223 0.8813 0.0998  -0.0449 0.0467  145 HIS A CD2 
1248 C  CE1 . HIS A 148 ? 0.6201 0.4161 0.8917 0.1113  -0.0495 0.0598  145 HIS A CE1 
1249 N  NE2 . HIS A 148 ? 0.6346 0.4263 0.8946 0.1167  -0.0459 0.0560  145 HIS A NE2 
1250 N  N   . GLN A 149 ? 0.5092 0.4942 0.8218 0.0423  -0.0137 -0.0075 146 GLN A N   
1251 C  CA  . GLN A 149 ? 0.5087 0.4802 0.8134 0.0493  -0.0271 -0.0153 146 GLN A CA  
1252 C  C   . GLN A 149 ? 0.4949 0.4799 0.8067 0.0507  -0.0243 -0.0345 146 GLN A C   
1253 O  O   . GLN A 149 ? 0.5040 0.4684 0.7995 0.0607  -0.0298 -0.0324 146 GLN A O   
1254 C  CB  . GLN A 149 ? 0.5086 0.4873 0.8176 0.0403  -0.0327 -0.0150 146 GLN A CB  
1255 C  CG  . GLN A 149 ? 0.5161 0.4898 0.8204 0.0364  -0.0369 -0.0135 146 GLN A CG  
1256 C  CD  . GLN A 149 ? 0.5230 0.4913 0.8225 0.0325  -0.0406 -0.0112 146 GLN A CD  
1257 O  OE1 . GLN A 149 ? 0.5274 0.4950 0.8228 0.0267  -0.0430 -0.0074 146 GLN A OE1 
1258 N  NE2 . GLN A 149 ? 0.5357 0.4913 0.8260 0.0325  -0.0404 -0.0111 146 GLN A NE2 
1259 N  N   . ALA B 3   ? 0.4766 0.3796 0.7394 0.0676  0.0147  0.0831  0   ALA B N   
1260 C  CA  . ALA B 3   ? 0.4533 0.3730 0.7415 0.0703  0.0128  0.0756  0   ALA B CA  
1261 C  C   . ALA B 3   ? 0.4243 0.3820 0.7335 0.0688  0.0029  0.0668  0   ALA B C   
1262 O  O   . ALA B 3   ? 0.4483 0.4273 0.7698 0.0894  0.0159  0.0477  0   ALA B O   
1263 C  CB  . ALA B 3   ? 0.4385 0.3460 0.7410 0.0935  0.0192  0.0797  0   ALA B CB  
1264 N  N   . MET B 4   ? 0.3682 0.3560 0.7130 0.0403  -0.0131 0.0402  1   MET B N   
1265 C  CA  . MET B 4   ? 0.3365 0.3157 0.6890 0.0367  -0.0062 0.0143  1   MET B CA  
1266 C  C   . MET B 4   ? 0.2662 0.2721 0.6546 0.0328  -0.0168 0.0136  1   MET B C   
1267 O  O   . MET B 4   ? 0.2453 0.3349 0.6506 0.0105  -0.0259 -0.0094 1   MET B O   
1268 C  CB  . MET B 4   ? 0.3723 0.3367 0.7222 0.0187  0.0080  0.0113  1   MET B CB  
1269 C  CG  . MET B 4   ? 0.3920 0.3464 0.7459 0.0274  0.0214  0.0146  1   MET B CG  
1270 S  SD  . MET B 4   ? 0.4438 0.3479 0.7750 0.0196  0.0501  -0.0021 1   MET B SD  
1271 C  CE  . MET B 4   ? 0.4528 0.3668 0.7756 0.0017  0.0539  0.0169  1   MET B CE  
1272 N  N   . GLU B 5   ? 0.2447 0.1964 0.5989 0.0352  -0.0068 0.0143  2   GLU B N   
1273 C  CA  . GLU B 5   ? 0.2215 0.1606 0.5828 0.0277  -0.0071 0.0202  2   GLU B CA  
1274 C  C   . GLU B 5   ? 0.2134 0.1530 0.5778 0.0190  -0.0080 0.0218  2   GLU B C   
1275 O  O   . GLU B 5   ? 0.2118 0.1623 0.5775 0.0362  0.0025  0.0312  2   GLU B O   
1276 C  CB  . GLU B 5   ? 0.2278 0.1408 0.5670 0.0329  -0.0159 0.0204  2   GLU B CB  
1277 C  CG  . GLU B 5   ? 0.2508 0.1398 0.5595 0.0357  -0.0182 0.0206  2   GLU B CG  
1278 C  CD  . GLU B 5   ? 0.2626 0.1485 0.5500 0.0294  -0.0276 0.0218  2   GLU B CD  
1279 O  OE1 . GLU B 5   ? 0.2586 0.1702 0.5461 0.0322  -0.0335 0.0231  2   GLU B OE1 
1280 O  OE2 . GLU B 5   ? 0.3179 0.1270 0.5579 0.0349  -0.0206 0.0198  2   GLU B OE2 
1281 N  N   . ILE B 6   ? 0.1985 0.1460 0.5856 0.0268  -0.0067 0.0244  3   ILE B N   
1282 C  CA  . ILE B 6   ? 0.1937 0.1533 0.5775 0.0231  -0.0094 0.0216  3   ILE B CA  
1283 C  C   . ILE B 6   ? 0.1656 0.1258 0.5676 0.0147  -0.0055 0.0078  3   ILE B C   
1284 O  O   . ILE B 6   ? 0.1505 0.1659 0.5697 0.0168  -0.0045 0.0085  3   ILE B O   
1285 C  CB  . ILE B 6   ? 0.1972 0.1698 0.5968 0.0167  -0.0213 0.0178  3   ILE B CB  
1286 C  CG1 . ILE B 6   ? 0.2397 0.2209 0.6007 0.0087  -0.0219 0.0137  3   ILE B CG1 
1287 C  CG2 . ILE B 6   ? 0.2043 0.1798 0.5988 0.0198  -0.0234 0.0258  3   ILE B CG2 
1288 C  CD1 . ILE B 6   ? 0.2607 0.2563 0.6075 0.0105  -0.0187 0.0136  3   ILE B CD1 
1289 N  N   . HIS B 7   ? 0.1691 0.1466 0.5623 0.0295  0.0012  -0.0028 4   HIS B N   
1290 C  CA  . HIS B 7   ? 0.1627 0.1485 0.5642 0.0341  -0.0034 -0.0006 4   HIS B CA  
1291 C  C   . HIS B 7   ? 0.1567 0.1704 0.5627 0.0346  0.0030  0.0100  4   HIS B C   
1292 O  O   . HIS B 7   ? 0.1540 0.1793 0.5575 0.0270  0.0235  0.0249  4   HIS B O   
1293 C  CB  . HIS B 7   ? 0.1583 0.1294 0.5642 0.0535  0.0003  0.0016  4   HIS B CB  
1294 C  CG  . HIS B 7   ? 0.1588 0.1086 0.5686 0.0419  -0.0121 0.0028  4   HIS B CG  
1295 N  ND1 . HIS B 7   ? 0.1381 0.1543 0.5831 0.0305  -0.0037 -0.0016 4   HIS B ND1 
1296 C  CD2 . HIS B 7   ? 0.1488 0.1155 0.5713 0.0496  -0.0104 0.0080  4   HIS B CD2 
1297 C  CE1 . HIS B 7   ? 0.1770 0.1429 0.5727 0.0249  -0.0085 0.0049  4   HIS B CE1 
1298 N  NE2 . HIS B 7   ? 0.1535 0.1225 0.5759 0.0308  -0.0205 0.0032  4   HIS B NE2 
1299 N  N   . PHE B 8   ? 0.1452 0.1992 0.5660 0.0224  0.0009  0.0081  5   PHE B N   
1300 C  CA  . PHE B 8   ? 0.1700 0.1975 0.5731 0.0106  -0.0138 0.0080  5   PHE B CA  
1301 C  C   . PHE B 8   ? 0.1774 0.2080 0.5729 0.0021  -0.0163 0.0058  5   PHE B C   
1302 O  O   . PHE B 8   ? 0.1885 0.2099 0.5759 0.0277  -0.0115 0.0046  5   PHE B O   
1303 C  CB  . PHE B 8   ? 0.1701 0.2079 0.5835 -0.0082 -0.0065 -0.0073 5   PHE B CB  
1304 C  CG  . PHE B 8   ? 0.1630 0.2412 0.6072 -0.0323 0.0028  -0.0193 5   PHE B CG  
1305 C  CD1 . PHE B 8   ? 0.1693 0.2378 0.6212 -0.0309 -0.0001 -0.0257 5   PHE B CD1 
1306 C  CD2 . PHE B 8   ? 0.1812 0.2564 0.6198 -0.0426 0.0068  -0.0245 5   PHE B CD2 
1307 C  CE1 . PHE B 8   ? 0.1836 0.2760 0.6332 -0.0461 0.0026  -0.0287 5   PHE B CE1 
1308 C  CE2 . PHE B 8   ? 0.2062 0.2828 0.6273 -0.0620 0.0014  -0.0295 5   PHE B CE2 
1309 C  CZ  . PHE B 8   ? 0.2013 0.2680 0.6366 -0.0625 0.0074  -0.0302 5   PHE B CZ  
1310 N  N   . GLU B 9   ? 0.2009 0.2024 0.5759 0.0201  -0.0100 -0.0031 6   GLU B N   
1311 C  CA  . GLU B 9   ? 0.2011 0.1907 0.5840 -0.0089 -0.0021 0.0007  6   GLU B CA  
1312 C  C   . GLU B 9   ? 0.1842 0.2008 0.5945 -0.0003 0.0026  -0.0060 6   GLU B C   
1313 O  O   . GLU B 9   ? 0.1893 0.1911 0.6024 0.0241  -0.0073 -0.0042 6   GLU B O   
1314 C  CB  . GLU B 9   ? 0.2124 0.2072 0.5820 -0.0198 -0.0086 0.0064  6   GLU B CB  
1315 C  CG  . GLU B 9   ? 0.2383 0.1938 0.5799 -0.0322 -0.0059 0.0090  6   GLU B CG  
1316 C  CD  . GLU B 9   ? 0.2512 0.2144 0.5785 -0.0379 -0.0071 0.0156  6   GLU B CD  
1317 O  OE1 . GLU B 9   ? 0.2498 0.2298 0.5818 -0.0535 -0.0026 0.0097  6   GLU B OE1 
1318 O  OE2 . GLU B 9   ? 0.2630 0.2379 0.5806 -0.0278 -0.0042 0.0405  6   GLU B OE2 
1319 N  N   . LYS B 10  ? 0.2043 0.2316 0.6018 0.0100  0.0156  -0.0047 7   LYS B N   
1320 C  CA  . LYS B 10  ? 0.2482 0.2399 0.6181 0.0126  0.0132  0.0095  7   LYS B CA  
1321 C  C   . LYS B 10  ? 0.2272 0.1982 0.6168 0.0190  0.0131  0.0121  7   LYS B C   
1322 O  O   . LYS B 10  ? 0.2029 0.1710 0.6181 0.0138  0.0104  0.0024  7   LYS B O   
1323 C  CB  . LYS B 10  ? 0.2938 0.3044 0.6354 0.0028  0.0087  0.0059  7   LYS B CB  
1324 C  CG  . LYS B 10  ? 0.3487 0.3474 0.6532 0.0001  0.0238  0.0108  7   LYS B CG  
1325 C  CD  . LYS B 10  ? 0.3840 0.3714 0.6692 -0.0209 0.0200  0.0120  7   LYS B CD  
1326 C  CE  . LYS B 10  ? 0.4179 0.3938 0.6819 -0.0282 0.0319  0.0190  7   LYS B CE  
1327 N  NZ  . LYS B 10  ? 0.4413 0.4030 0.6971 -0.0437 0.0322  0.0253  7   LYS B NZ  
1328 N  N   . VAL B 11  ? 0.2256 0.2009 0.6280 0.0189  0.0181  0.0152  8   VAL B N   
1329 C  CA  . VAL B 11  ? 0.2329 0.1963 0.6345 0.0094  0.0243  0.0157  8   VAL B CA  
1330 C  C   . VAL B 11  ? 0.2635 0.2105 0.6337 0.0156  0.0055  0.0246  8   VAL B C   
1331 O  O   . VAL B 11  ? 0.3055 0.2475 0.6404 0.0016  -0.0082 0.0393  8   VAL B O   
1332 C  CB  . VAL B 11  ? 0.2422 0.2047 0.6415 0.0145  0.0370  0.0074  8   VAL B CB  
1333 C  CG1 . VAL B 11  ? 0.2389 0.2091 0.6490 -0.0014 0.0470  0.0046  8   VAL B CG1 
1334 C  CG2 . VAL B 11  ? 0.2490 0.1992 0.6403 0.0050  0.0391  0.0084  8   VAL B CG2 
1335 N  N   . THR B 12  ? 0.2328 0.1969 0.6340 0.0188  0.0103  0.0135  9   THR B N   
1336 C  CA  . THR B 12  ? 0.2501 0.2072 0.6337 0.0178  0.0051  0.0122  9   THR B CA  
1337 C  C   . THR B 12  ? 0.2179 0.1896 0.6399 0.0226  0.0085  0.0105  9   THR B C   
1338 O  O   . THR B 12  ? 0.2210 0.1747 0.6420 0.0247  0.0159  0.0330  9   THR B O   
1339 C  CB  . THR B 12  ? 0.2509 0.2186 0.6338 0.0302  0.0066  0.0017  9   THR B CB  
1340 O  OG1 . THR B 12  ? 0.2463 0.2192 0.6290 0.0363  0.0170  0.0137  9   THR B OG1 
1341 C  CG2 . THR B 12  ? 0.2626 0.2375 0.6366 0.0285  0.0090  -0.0125 9   THR B CG2 
1342 N  N   . SER B 13  ? 0.2336 0.2215 0.6418 0.0135  0.0113  -0.0028 10  SER B N   
1343 C  CA  . SER B 13  ? 0.2106 0.2279 0.6464 0.0017  0.0082  -0.0018 10  SER B CA  
1344 C  C   . SER B 13  ? 0.1805 0.1993 0.6278 -0.0017 0.0151  -0.0082 10  SER B C   
1345 O  O   . SER B 13  ? 0.1851 0.2603 0.6301 0.0034  0.0227  -0.0014 10  SER B O   
1346 C  CB  . SER B 13  ? 0.2151 0.2435 0.6632 -0.0124 0.0188  -0.0092 10  SER B CB  
1347 O  OG  . SER B 13  ? 0.2657 0.2527 0.6822 -0.0128 0.0213  -0.0090 10  SER B OG  
1348 N  N   . ASP B 14  ? 0.1792 0.1977 0.6123 -0.0035 0.0120  0.0010  11  ASP B N   
1349 C  CA  . ASP B 14  ? 0.1983 0.1826 0.6022 -0.0111 0.0160  0.0027  11  ASP B CA  
1350 C  C   . ASP B 14  ? 0.1924 0.1575 0.5826 -0.0260 0.0194  0.0139  11  ASP B C   
1351 O  O   . ASP B 14  ? 0.2427 0.1911 0.5691 -0.0404 -0.0046 0.0179  11  ASP B O   
1352 C  CB  . ASP B 14  ? 0.2104 0.1919 0.6266 -0.0057 0.0186  -0.0004 11  ASP B CB  
1353 C  CG  . ASP B 14  ? 0.2529 0.2047 0.6410 -0.0068 0.0261  -0.0036 11  ASP B CG  
1354 O  OD1 . ASP B 14  ? 0.2508 0.2236 0.6419 -0.0364 0.0349  0.0006  11  ASP B OD1 
1355 O  OD2 . ASP B 14  ? 0.2842 0.2431 0.6829 0.0114  0.0472  -0.0062 11  ASP B OD2 
1356 N  N   . ASN B 15  ? 0.1833 0.1495 0.5768 -0.0242 0.0118  0.0063  12  ASN B N   
1357 C  CA  . ASN B 15  ? 0.1824 0.1677 0.5660 -0.0110 0.0165  0.0132  12  ASN B CA  
1358 C  C   . ASN B 15  ? 0.1781 0.1649 0.5589 -0.0095 0.0183  0.0196  12  ASN B C   
1359 O  O   . ASN B 15  ? 0.1592 0.1682 0.5468 -0.0215 0.0142  0.0173  12  ASN B O   
1360 C  CB  . ASN B 15  ? 0.1840 0.1637 0.5719 -0.0012 0.0146  0.0143  12  ASN B CB  
1361 C  CG  . ASN B 15  ? 0.1805 0.1992 0.5796 0.0116  0.0195  0.0099  12  ASN B CG  
1362 O  OD1 . ASN B 15  ? 0.1779 0.1827 0.5845 0.0171  0.0309  0.0202  12  ASN B OD1 
1363 N  ND2 . ASN B 15  ? 0.1699 0.2285 0.5885 -0.0036 0.0316  0.0118  12  ASN B ND2 
1364 N  N   A ARG B 16  ? 0.1909 0.1653 0.5653 -0.0129 0.0224  0.0287  13  ARG B N   
1365 N  N   B ARG B 16  ? 0.1802 0.1589 0.5648 -0.0049 0.0231  0.0262  13  ARG B N   
1366 C  CA  A ARG B 16  ? 0.2075 0.1660 0.5732 -0.0059 0.0319  0.0287  13  ARG B CA  
1367 C  CA  B ARG B 16  ? 0.1851 0.1592 0.5684 0.0064  0.0296  0.0267  13  ARG B CA  
1368 C  C   A ARG B 16  ? 0.1830 0.1429 0.5753 -0.0032 0.0411  0.0286  13  ARG B C   
1369 C  C   B ARG B 16  ? 0.1742 0.1411 0.5728 0.0014  0.0401  0.0266  13  ARG B C   
1370 O  O   A ARG B 16  ? 0.2016 0.1563 0.5761 -0.0097 0.0467  0.0152  13  ARG B O   
1371 O  O   B ARG B 16  ? 0.1846 0.1525 0.5738 -0.0061 0.0465  0.0162  13  ARG B O   
1372 C  CB  A ARG B 16  ? 0.2280 0.1848 0.5828 0.0037  0.0294  0.0327  13  ARG B CB  
1373 C  CB  B ARG B 16  ? 0.1900 0.1643 0.5741 0.0269  0.0276  0.0294  13  ARG B CB  
1374 C  CG  A ARG B 16  ? 0.2556 0.1886 0.5958 0.0033  0.0301  0.0412  13  ARG B CG  
1375 C  CG  B ARG B 16  ? 0.1893 0.1702 0.5791 0.0366  0.0251  0.0348  13  ARG B CG  
1376 C  CD  A ARG B 16  ? 0.2836 0.2098 0.6061 0.0119  0.0306  0.0542  13  ARG B CD  
1377 C  CD  B ARG B 16  ? 0.2096 0.1833 0.5818 0.0507  0.0236  0.0367  13  ARG B CD  
1378 N  NE  A ARG B 16  ? 0.3257 0.2712 0.6162 0.0188  0.0190  0.0514  13  ARG B NE  
1379 N  NE  B ARG B 16  ? 0.2329 0.1988 0.5835 0.0619  0.0273  0.0462  13  ARG B NE  
1380 C  CZ  A ARG B 16  ? 0.3564 0.3039 0.6337 0.0196  0.0207  0.0515  13  ARG B CZ  
1381 C  CZ  B ARG B 16  ? 0.2774 0.2096 0.5898 0.0669  0.0259  0.0431  13  ARG B CZ  
1382 N  NH1 A ARG B 16  ? 0.3542 0.3284 0.6447 0.0224  0.0265  0.0558  13  ARG B NH1 
1383 N  NH1 B ARG B 16  ? 0.3002 0.2114 0.5966 0.0646  0.0226  0.0412  13  ARG B NH1 
1384 N  NH2 A ARG B 16  ? 0.3625 0.3140 0.6473 0.0154  0.0161  0.0524  13  ARG B NH2 
1385 N  NH2 B ARG B 16  ? 0.2805 0.1882 0.5944 0.0738  0.0255  0.0333  13  ARG B NH2 
1386 N  N   . LYS B 17  ? 0.1932 0.1211 0.5796 -0.0097 0.0432  0.0258  14  LYS B N   
1387 C  CA  . LYS B 17  ? 0.1929 0.1270 0.5776 -0.0098 0.0455  0.0261  14  LYS B CA  
1388 C  C   . LYS B 17  ? 0.1836 0.1271 0.5745 -0.0155 0.0461  0.0275  14  LYS B C   
1389 O  O   . LYS B 17  ? 0.2030 0.1723 0.5678 0.0118  0.0538  0.0216  14  LYS B O   
1390 C  CB  . LYS B 17  ? 0.1899 0.1417 0.5899 -0.0122 0.0409  0.0223  14  LYS B CB  
1391 C  CG  . LYS B 17  ? 0.1861 0.1405 0.6042 -0.0023 0.0319  0.0200  14  LYS B CG  
1392 C  CD  . LYS B 17  ? 0.1830 0.1352 0.6191 -0.0087 0.0227  0.0179  14  LYS B CD  
1393 C  CE  . LYS B 17  ? 0.1909 0.1586 0.6301 -0.0336 0.0127  0.0232  14  LYS B CE  
1394 N  NZ  . LYS B 17  ? 0.1851 0.1796 0.6418 -0.0330 0.0160  0.0202  14  LYS B NZ  
1395 N  N   . ALA B 18  ? 0.2122 0.1168 0.5745 -0.0122 0.0368  0.0227  15  ALA B N   
1396 C  CA  . ALA B 18  ? 0.2040 0.1295 0.5793 -0.0082 0.0319  0.0232  15  ALA B CA  
1397 C  C   . ALA B 18  ? 0.2033 0.1336 0.5635 -0.0116 0.0332  0.0298  15  ALA B C   
1398 O  O   . ALA B 18  ? 0.2337 0.1520 0.5700 -0.0037 0.0453  0.0272  15  ALA B O   
1399 C  CB  . ALA B 18  ? 0.2049 0.1428 0.5809 0.0039  0.0250  0.0179  15  ALA B CB  
1400 N  N   . VAL B 19  ? 0.1788 0.1366 0.5559 -0.0081 0.0406  0.0350  16  VAL B N   
1401 C  CA  . VAL B 19  ? 0.1723 0.1393 0.5539 -0.0037 0.0410  0.0369  16  VAL B CA  
1402 C  C   . VAL B 19  ? 0.1721 0.1433 0.5469 -0.0040 0.0454  0.0371  16  VAL B C   
1403 O  O   . VAL B 19  ? 0.1741 0.1465 0.5641 0.0057  0.0531  0.0206  16  VAL B O   
1404 C  CB  . VAL B 19  ? 0.1874 0.1375 0.5569 0.0092  0.0344  0.0302  16  VAL B CB  
1405 C  CG1 . VAL B 19  ? 0.2047 0.1345 0.5599 0.0073  0.0321  0.0249  16  VAL B CG1 
1406 C  CG2 . VAL B 19  ? 0.1843 0.1439 0.5602 0.0103  0.0305  0.0276  16  VAL B CG2 
1407 N  N   . GLU B 20  ? 0.1743 0.1266 0.5334 -0.0047 0.0422  0.0370  17  GLU B N   
1408 C  CA  . GLU B 20  ? 0.1789 0.1464 0.5220 0.0039  0.0461  0.0349  17  GLU B CA  
1409 C  C   . GLU B 20  ? 0.1761 0.1490 0.5357 -0.0041 0.0437  0.0166  17  GLU B C   
1410 O  O   . GLU B 20  ? 0.2068 0.1671 0.5688 0.0045  0.0323  -0.0029 17  GLU B O   
1411 C  CB  . GLU B 20  ? 0.1858 0.1559 0.4890 0.0020  0.0488  0.0551  17  GLU B CB  
1412 C  CG  . GLU B 20  ? 0.2033 0.1676 0.4762 0.0066  0.0502  0.0718  17  GLU B CG  
1413 C  CD  . GLU B 20  ? 0.2126 0.1803 0.4652 0.0004  0.0479  0.0799  17  GLU B CD  
1414 O  OE1 . GLU B 20  ? 0.2177 0.2152 0.4837 -0.0076 0.0472  0.0793  17  GLU B OE1 
1415 O  OE2 . GLU B 20  ? 0.2516 0.1931 0.4697 0.0138  0.0385  0.0882  17  GLU B OE2 
1416 N  N   . ASN B 21  ? 0.2033 0.1635 0.5566 -0.0085 0.0400  0.0121  18  ASN B N   
1417 C  CA  . ASN B 21  ? 0.2306 0.1636 0.5696 -0.0113 0.0445  0.0053  18  ASN B CA  
1418 C  C   . ASN B 21  ? 0.2484 0.1611 0.5804 -0.0131 0.0345  0.0055  18  ASN B C   
1419 O  O   . ASN B 21  ? 0.2797 0.1650 0.5815 -0.0214 0.0340  0.0205  18  ASN B O   
1420 C  CB  . ASN B 21  ? 0.2303 0.1802 0.5829 -0.0146 0.0537  0.0020  18  ASN B CB  
1421 C  CG  . ASN B 21  ? 0.2340 0.2093 0.6013 -0.0145 0.0491  0.0015  18  ASN B CG  
1422 O  OD1 . ASN B 21  ? 0.2472 0.2416 0.6121 -0.0015 0.0586  0.0019  18  ASN B OD1 
1423 N  ND2 . ASN B 21  ? 0.2235 0.2084 0.6128 -0.0220 0.0431  0.0044  18  ASN B ND2 
1424 N  N   . LEU B 22  ? 0.2553 0.1758 0.6026 -0.0235 0.0298  -0.0019 19  LEU B N   
1425 C  CA  . LEU B 22  ? 0.2800 0.1815 0.6239 -0.0202 0.0169  -0.0029 19  LEU B CA  
1426 C  C   . LEU B 22  ? 0.2807 0.1701 0.6483 -0.0094 0.0165  -0.0016 19  LEU B C   
1427 O  O   . LEU B 22  ? 0.2485 0.1573 0.6713 -0.0057 0.0110  -0.0367 19  LEU B O   
1428 C  CB  . LEU B 22  ? 0.3169 0.1969 0.6257 -0.0340 0.0214  -0.0010 19  LEU B CB  
1429 C  CG  . LEU B 22  ? 0.3615 0.2696 0.6281 -0.0182 0.0315  -0.0103 19  LEU B CG  
1430 C  CD1 . LEU B 22  ? 0.3671 0.2902 0.6346 -0.0372 0.0385  -0.0014 19  LEU B CD1 
1431 C  CD2 . LEU B 22  ? 0.3644 0.2430 0.6252 -0.0001 0.0349  -0.0123 19  LEU B CD2 
1432 N  N   . GLN B 23  ? 0.3113 0.1823 0.6665 -0.0036 0.0107  0.0049  20  GLN B N   
1433 C  CA  . GLN B 23  ? 0.3713 0.2585 0.6874 0.0022  0.0015  -0.0019 20  GLN B CA  
1434 C  C   . GLN B 23  ? 0.3680 0.2676 0.6960 0.0081  -0.0104 -0.0107 20  GLN B C   
1435 O  O   . GLN B 23  ? 0.3639 0.2608 0.6946 0.0551  -0.0080 -0.0174 20  GLN B O   
1436 C  CB  . GLN B 23  ? 0.3858 0.2688 0.7038 -0.0124 0.0096  0.0069  20  GLN B CB  
1437 C  CG  . GLN B 23  ? 0.3836 0.3140 0.7184 -0.0250 0.0168  0.0070  20  GLN B CG  
1438 C  CD  . GLN B 23  ? 0.4051 0.3285 0.7322 -0.0416 0.0225  0.0134  20  GLN B CD  
1439 O  OE1 . GLN B 23  ? 0.4381 0.3966 0.7462 -0.0261 0.0175  0.0014  20  GLN B OE1 
1440 N  NE2 . GLN B 23  ? 0.3965 0.3433 0.7397 -0.0494 0.0317  0.0133  20  GLN B NE2 
1441 N  N   . VAL B 24  ? 0.3995 0.2791 0.7145 0.0248  -0.0192 -0.0144 21  VAL B N   
1442 C  CA  . VAL B 24  ? 0.4056 0.2981 0.7315 0.0263  -0.0180 -0.0062 21  VAL B CA  
1443 C  C   . VAL B 24  ? 0.4272 0.3087 0.7388 0.0411  -0.0165 -0.0063 21  VAL B C   
1444 O  O   . VAL B 24  ? 0.4602 0.2772 0.7613 0.0745  -0.0150 0.0046  21  VAL B O   
1445 C  CB  . VAL B 24  ? 0.4155 0.3236 0.7345 0.0107  -0.0277 -0.0119 21  VAL B CB  
1446 C  CG1 . VAL B 24  ? 0.4344 0.2954 0.7381 0.0054  -0.0300 -0.0133 21  VAL B CG1 
1447 C  CG2 . VAL B 24  ? 0.4397 0.3448 0.7380 0.0105  -0.0324 -0.0138 21  VAL B CG2 
1448 N  N   . PHE B 25  ? 0.4257 0.3175 0.7320 0.0564  -0.0169 -0.0073 22  PHE B N   
1449 C  CA  . PHE B 25  ? 0.4078 0.3481 0.7237 0.0654  -0.0120 0.0006  22  PHE B CA  
1450 C  C   . PHE B 25  ? 0.4231 0.3650 0.7125 0.0767  -0.0209 0.0027  22  PHE B C   
1451 O  O   . PHE B 25  ? 0.4063 0.3982 0.7191 0.0828  0.0038  -0.0177 22  PHE B O   
1452 C  CB  . PHE B 25  ? 0.4048 0.3488 0.7240 0.0692  -0.0111 0.0061  22  PHE B CB  
1453 C  CG  . PHE B 25  ? 0.3970 0.3465 0.7262 0.0706  -0.0082 0.0097  22  PHE B CG  
1454 C  CD1 . PHE B 25  ? 0.3872 0.3510 0.7252 0.0739  -0.0054 0.0140  22  PHE B CD1 
1455 C  CD2 . PHE B 25  ? 0.3947 0.3465 0.7254 0.0694  -0.0085 0.0114  22  PHE B CD2 
1456 C  CE1 . PHE B 25  ? 0.3891 0.3453 0.7264 0.0771  -0.0055 0.0128  22  PHE B CE1 
1457 C  CE2 . PHE B 25  ? 0.3902 0.3391 0.7264 0.0707  -0.0097 0.0129  22  PHE B CE2 
1458 C  CZ  . PHE B 25  ? 0.3893 0.3443 0.7252 0.0729  -0.0074 0.0137  22  PHE B CZ  
1459 N  N   . ALA B 26  ? 0.4227 0.3673 0.6962 0.0747  -0.0343 0.0098  23  ALA B N   
1460 C  CA  . ALA B 26  ? 0.4497 0.3707 0.6822 0.0760  -0.0470 0.0256  23  ALA B CA  
1461 C  C   . ALA B 26  ? 0.4631 0.3555 0.6630 0.0627  -0.0531 0.0335  23  ALA B C   
1462 O  O   . ALA B 26  ? 0.4712 0.3443 0.6832 0.0332  -0.0541 0.0263  23  ALA B O   
1463 C  CB  . ALA B 26  ? 0.4704 0.3830 0.6884 0.0668  -0.0486 0.0311  23  ALA B CB  
1464 N  N   . GLU B 27  ? 0.4697 0.3208 0.6503 0.0786  -0.0526 0.0441  24  GLU B N   
1465 C  CA  . GLU B 27  ? 0.4783 0.2854 0.6509 0.0716  -0.0484 0.0396  24  GLU B CA  
1466 C  C   . GLU B 27  ? 0.4800 0.2690 0.6634 0.0810  -0.0448 0.0235  24  GLU B C   
1467 O  O   . GLU B 27  ? 0.5005 0.2695 0.6607 0.0846  -0.0300 0.0038  24  GLU B O   
1468 C  CB  . GLU B 27  ? 0.4921 0.2617 0.6626 0.0638  -0.0381 0.0448  24  GLU B CB  
1469 C  CG  . GLU B 27  ? 0.5028 0.2488 0.6699 0.0645  -0.0346 0.0407  24  GLU B CG  
1470 C  CD  . GLU B 27  ? 0.5387 0.2230 0.6801 0.0298  -0.0257 0.0429  24  GLU B CD  
1471 O  OE1 . GLU B 27  ? 0.5576 0.2437 0.6879 0.0038  -0.0209 0.0339  24  GLU B OE1 
1472 O  OE2 . GLU B 27  ? 0.5461 0.2012 0.7002 0.0340  -0.0093 0.0246  24  GLU B OE2 
1473 N  N   . GLN B 28  ? 0.4725 0.3217 0.6617 0.0744  -0.0482 0.0064  25  GLN B N   
1474 C  CA  . GLN B 28  ? 0.4646 0.3153 0.6604 0.0610  -0.0388 -0.0037 25  GLN B CA  
1475 C  C   . GLN B 28  ? 0.3882 0.2913 0.6461 0.0583  -0.0481 -0.0119 25  GLN B C   
1476 O  O   . GLN B 28  ? 0.3530 0.2504 0.6310 0.0765  -0.0468 -0.0246 25  GLN B O   
1477 C  CB  . GLN B 28  ? 0.5084 0.3424 0.6816 0.0659  -0.0298 -0.0118 25  GLN B CB  
1478 C  CG  . GLN B 28  ? 0.5459 0.3631 0.7048 0.0808  -0.0139 -0.0040 25  GLN B CG  
1479 C  CD  . GLN B 28  ? 0.5716 0.3920 0.7160 0.0900  -0.0122 -0.0111 25  GLN B CD  
1480 O  OE1 . GLN B 28  ? 0.5499 0.3478 0.7382 0.1322  -0.0057 -0.0260 25  GLN B OE1 
1481 N  NE2 . GLN B 28  ? 0.5838 0.4394 0.7197 0.0946  -0.0080 0.0012  25  GLN B NE2 
1482 N  N   . GLN B 29  ? 0.3678 0.3054 0.6395 0.0473  -0.0488 -0.0004 26  GLN B N   
1483 C  CA  . GLN B 29  ? 0.3272 0.2898 0.6349 0.0387  -0.0488 -0.0050 26  GLN B CA  
1484 C  C   . GLN B 29  ? 0.2853 0.2459 0.6136 0.0284  -0.0363 0.0101  26  GLN B C   
1485 O  O   . GLN B 29  ? 0.2602 0.2294 0.6152 0.0211  -0.0332 0.0177  26  GLN B O   
1486 C  CB  . GLN B 29  ? 0.3393 0.3400 0.6508 0.0346  -0.0602 -0.0160 26  GLN B CB  
1487 C  CG  . GLN B 29  ? 0.3762 0.3809 0.6651 0.0234  -0.0608 -0.0313 26  GLN B CG  
1488 C  CD  . GLN B 29  ? 0.3905 0.3872 0.6740 0.0307  -0.0615 -0.0444 26  GLN B CD  
1489 O  OE1 . GLN B 29  ? 0.4306 0.4142 0.6838 0.0203  -0.0553 -0.0699 26  GLN B OE1 
1490 N  NE2 . GLN B 29  ? 0.4084 0.3969 0.6731 0.0257  -0.0598 -0.0536 26  GLN B NE2 
1491 N  N   . ALA B 30  ? 0.2648 0.2268 0.5862 0.0317  -0.0344 0.0070  27  ALA B N   
1492 C  CA  . ALA B 30  ? 0.2644 0.1885 0.5761 0.0276  -0.0264 0.0078  27  ALA B CA  
1493 C  C   . ALA B 30  ? 0.2563 0.1759 0.5665 0.0215  -0.0210 0.0052  27  ALA B C   
1494 O  O   . ALA B 30  ? 0.2654 0.1662 0.5648 0.0247  -0.0069 0.0071  27  ALA B O   
1495 C  CB  . ALA B 30  ? 0.2592 0.1967 0.5721 0.0247  -0.0269 0.0120  27  ALA B CB  
1496 N  N   . PHE B 31  ? 0.2624 0.1879 0.5615 0.0016  -0.0120 0.0051  28  PHE B N   
1497 C  CA  . PHE B 31  ? 0.2514 0.1746 0.5584 0.0005  -0.0128 0.0037  28  PHE B CA  
1498 C  C   . PHE B 31  ? 0.2171 0.1716 0.5466 0.0080  -0.0195 0.0067  28  PHE B C   
1499 O  O   . PHE B 31  ? 0.2221 0.1402 0.5488 0.0294  -0.0162 0.0007  28  PHE B O   
1500 C  CB  . PHE B 31  ? 0.2986 0.2210 0.5627 -0.0062 0.0025  -0.0030 28  PHE B CB  
1501 C  CG  . PHE B 31  ? 0.3518 0.2537 0.5677 -0.0018 0.0155  0.0078  28  PHE B CG  
1502 C  CD1 . PHE B 31  ? 0.3718 0.2525 0.5726 -0.0121 0.0173  0.0105  28  PHE B CD1 
1503 C  CD2 . PHE B 31  ? 0.3787 0.2596 0.5725 -0.0095 0.0149  0.0096  28  PHE B CD2 
1504 C  CE1 . PHE B 31  ? 0.4129 0.2435 0.5749 -0.0109 0.0196  0.0151  28  PHE B CE1 
1505 C  CE2 . PHE B 31  ? 0.3944 0.2469 0.5767 -0.0095 0.0139  0.0134  28  PHE B CE2 
1506 C  CZ  . PHE B 31  ? 0.4135 0.2500 0.5758 -0.0155 0.0152  0.0134  28  PHE B CZ  
1507 N  N   . ILE B 32  ? 0.2158 0.1754 0.5482 0.0165  -0.0296 0.0060  29  ILE B N   
1508 C  CA  . ILE B 32  ? 0.1922 0.1593 0.5472 0.0244  -0.0292 0.0020  29  ILE B CA  
1509 C  C   . ILE B 32  ? 0.1848 0.1403 0.5320 0.0224  -0.0342 0.0096  29  ILE B C   
1510 O  O   . ILE B 32  ? 0.1864 0.1501 0.5392 0.0273  -0.0395 0.0048  29  ILE B O   
1511 C  CB  . ILE B 32  ? 0.2153 0.1741 0.5592 0.0152  -0.0359 0.0023  29  ILE B CB  
1512 C  CG1 . ILE B 32  ? 0.2308 0.1847 0.5700 0.0126  -0.0349 -0.0003 29  ILE B CG1 
1513 C  CG2 . ILE B 32  ? 0.2188 0.1675 0.5703 0.0088  -0.0377 -0.0020 29  ILE B CG2 
1514 C  CD1 . ILE B 32  ? 0.2467 0.2146 0.5767 0.0112  -0.0401 0.0005  29  ILE B CD1 
1515 N  N   . GLU B 33  ? 0.1837 0.1463 0.5227 0.0256  -0.0335 0.0122  30  GLU B N   
1516 C  CA  . GLU B 33  ? 0.1809 0.1463 0.5162 0.0166  -0.0278 0.0184  30  GLU B CA  
1517 C  C   . GLU B 33  ? 0.1682 0.1358 0.4972 0.0191  -0.0215 0.0224  30  GLU B C   
1518 O  O   . GLU B 33  ? 0.1939 0.1767 0.4981 0.0237  -0.0175 0.0281  30  GLU B O   
1519 C  CB  . GLU B 33  ? 0.1922 0.1470 0.5326 0.0188  -0.0303 0.0193  30  GLU B CB  
1520 C  CG  . GLU B 33  ? 0.2027 0.1739 0.5517 0.0227  -0.0419 0.0122  30  GLU B CG  
1521 C  CD  . GLU B 33  ? 0.2016 0.1937 0.5673 0.0036  -0.0450 0.0096  30  GLU B CD  
1522 O  OE1 . GLU B 33  ? 0.1650 0.2129 0.5781 0.0036  -0.0607 0.0207  30  GLU B OE1 
1523 O  OE2 . GLU B 33  ? 0.2156 0.2381 0.6007 -0.0099 -0.0559 0.0071  30  GLU B OE2 
1524 N  N   A SER B 34  ? 0.1877 0.1447 0.4847 0.0129  -0.0206 0.0207  31  SER B N   
1525 N  N   B SER B 34  ? 0.1718 0.1358 0.4994 0.0179  -0.0194 0.0186  31  SER B N   
1526 C  CA  A SER B 34  ? 0.1776 0.1468 0.4797 0.0055  -0.0165 0.0256  31  SER B CA  
1527 C  CA  B SER B 34  ? 0.1683 0.1300 0.4988 0.0171  -0.0170 0.0170  31  SER B CA  
1528 C  C   A SER B 34  ? 0.1681 0.1417 0.4740 0.0002  -0.0235 0.0199  31  SER B C   
1529 C  C   B SER B 34  ? 0.1634 0.1190 0.4973 0.0142  -0.0156 0.0121  31  SER B C   
1530 O  O   A SER B 34  ? 0.1937 0.1665 0.4604 -0.0049 -0.0111 0.0244  31  SER B O   
1531 O  O   B SER B 34  ? 0.1680 0.1244 0.4977 0.0137  -0.0147 0.0132  31  SER B O   
1532 C  CB  A SER B 34  ? 0.1992 0.1367 0.4805 -0.0045 -0.0196 0.0346  31  SER B CB  
1533 C  CB  B SER B 34  ? 0.1706 0.1328 0.4993 0.0155  -0.0173 0.0177  31  SER B CB  
1534 O  OG  A SER B 34  ? 0.1949 0.1418 0.4842 0.0010  -0.0207 0.0391  31  SER B OG  
1535 O  OG  B SER B 34  ? 0.1671 0.1379 0.4997 0.0196  -0.0176 0.0180  31  SER B OG  
1536 N  N   A MET B 35  ? 0.1748 0.1478 0.4891 0.0002  -0.0287 0.0088  32  MET B N   
1537 N  N   B MET B 35  ? 0.1582 0.1097 0.4976 0.0132  -0.0160 0.0134  32  MET B N   
1538 C  CA  A MET B 35  ? 0.1808 0.1542 0.5022 0.0096  -0.0255 0.0088  32  MET B CA  
1539 C  CA  B MET B 35  ? 0.1540 0.1004 0.4954 0.0112  -0.0135 0.0087  32  MET B CA  
1540 C  C   A MET B 35  ? 0.1546 0.1318 0.4969 -0.0031 -0.0252 0.0017  32  MET B C   
1541 C  C   B MET B 35  ? 0.1546 0.1177 0.4943 0.0043  -0.0147 0.0120  32  MET B C   
1542 O  O   A MET B 35  ? 0.1823 0.1357 0.4890 -0.0140 -0.0188 -0.0039 32  MET B O   
1543 O  O   B MET B 35  ? 0.1588 0.1227 0.4931 0.0022  -0.0138 0.0115  32  MET B O   
1544 C  CB  A MET B 35  ? 0.2059 0.1786 0.5234 0.0012  -0.0261 0.0025  32  MET B CB  
1545 C  CB  B MET B 35  ? 0.1481 0.0795 0.4989 0.0133  -0.0131 0.0090  32  MET B CB  
1546 C  CG  A MET B 35  ? 0.2084 0.2043 0.5490 0.0116  -0.0246 0.0147  32  MET B CG  
1547 C  CG  B MET B 35  ? 0.1407 0.0573 0.4985 0.0174  -0.0130 0.0061  32  MET B CG  
1548 S  SD  A MET B 35  ? 0.2233 0.2606 0.5939 0.0123  -0.0393 0.0184  32  MET B SD  
1549 S  SD  B MET B 35  ? 0.1344 0.0269 0.4995 0.0239  -0.0090 0.0019  32  MET B SD  
1550 C  CE  A MET B 35  ? 0.1957 0.2727 0.5856 -0.0174 -0.0381 0.0237  32  MET B CE  
1551 C  CE  B MET B 35  ? 0.1383 0.0281 0.4998 0.0239  -0.0095 0.0029  32  MET B CE  
1552 N  N   . ALA B 36  ? 0.1559 0.1452 0.4916 -0.0027 -0.0150 0.0171  33  ALA B N   
1553 C  CA  . ALA B 36  ? 0.1528 0.1362 0.4881 -0.0052 -0.0137 0.0221  33  ALA B CA  
1554 C  C   . ALA B 36  ? 0.1403 0.1378 0.4758 0.0035  -0.0102 0.0301  33  ALA B C   
1555 O  O   . ALA B 36  ? 0.1473 0.1226 0.4775 -0.0073 0.0010  0.0442  33  ALA B O   
1556 C  CB  . ALA B 36  ? 0.1571 0.1520 0.4895 0.0079  -0.0157 0.0222  33  ALA B CB  
1557 N  N   . GLU B 37  ? 0.1558 0.1305 0.4726 -0.0021 -0.0161 0.0161  34  GLU B N   
1558 C  CA  . GLU B 37  ? 0.1656 0.1460 0.4737 -0.0062 -0.0172 0.0076  34  GLU B CA  
1559 C  C   . GLU B 37  ? 0.1570 0.1390 0.4719 -0.0065 -0.0149 0.0030  34  GLU B C   
1560 O  O   . GLU B 37  ? 0.1659 0.1505 0.4685 -0.0009 -0.0136 -0.0230 34  GLU B O   
1561 C  CB  . GLU B 37  ? 0.1824 0.1537 0.4785 0.0057  -0.0191 0.0099  34  GLU B CB  
1562 C  CG  . GLU B 37  ? 0.1929 0.1633 0.4819 0.0076  -0.0205 0.0031  34  GLU B CG  
1563 C  CD  . GLU B 37  ? 0.2018 0.1615 0.4839 0.0049  -0.0210 0.0078  34  GLU B CD  
1564 O  OE1 . GLU B 37  ? 0.1984 0.1936 0.4936 0.0035  -0.0062 0.0070  34  GLU B OE1 
1565 O  OE2 . GLU B 37  ? 0.2044 0.1792 0.4961 -0.0039 -0.0297 -0.0019 34  GLU B OE2 
1566 N  N   . ASN B 38  ? 0.1623 0.1590 0.4839 -0.0097 -0.0176 -0.0045 35  ASN B N   
1567 C  CA  . ASN B 38  ? 0.1444 0.1577 0.4960 -0.0182 -0.0088 -0.0078 35  ASN B CA  
1568 C  C   . ASN B 38  ? 0.1550 0.1804 0.4997 -0.0088 -0.0192 0.0015  35  ASN B C   
1569 O  O   . ASN B 38  ? 0.1554 0.2215 0.5060 -0.0202 -0.0247 -0.0123 35  ASN B O   
1570 C  CB  . ASN B 38  ? 0.1341 0.1505 0.4947 -0.0119 -0.0040 -0.0073 35  ASN B CB  
1571 C  CG  . ASN B 38  ? 0.1445 0.1581 0.4953 -0.0196 0.0103  -0.0062 35  ASN B CG  
1572 O  OD1 . ASN B 38  ? 0.1669 0.1157 0.5014 -0.0393 0.0039  0.0194  35  ASN B OD1 
1573 N  ND2 . ASN B 38  ? 0.1507 0.1701 0.4978 -0.0306 0.0128  0.0014  35  ASN B ND2 
1574 N  N   . LEU B 39  ? 0.1523 0.1668 0.5128 -0.0062 -0.0168 0.0063  36  LEU B N   
1575 C  CA  . LEU B 39  ? 0.1737 0.1726 0.5205 0.0080  -0.0127 0.0097  36  LEU B CA  
1576 C  C   . LEU B 39  ? 0.1740 0.1627 0.5203 0.0061  -0.0100 0.0079  36  LEU B C   
1577 O  O   . LEU B 39  ? 0.1922 0.1946 0.5272 0.0388  -0.0157 0.0155  36  LEU B O   
1578 C  CB  . LEU B 39  ? 0.1753 0.1928 0.5298 0.0137  -0.0232 0.0021  36  LEU B CB  
1579 C  CG  . LEU B 39  ? 0.1798 0.1899 0.5375 0.0203  -0.0257 0.0021  36  LEU B CG  
1580 C  CD1 . LEU B 39  ? 0.1803 0.1915 0.5477 0.0235  -0.0320 0.0011  36  LEU B CD1 
1581 C  CD2 . LEU B 39  ? 0.1812 0.2271 0.5409 0.0255  -0.0302 -0.0034 36  LEU B CD2 
1582 N  N   . LYS B 40  ? 0.1695 0.1578 0.5116 0.0021  0.0009  0.0011  37  LYS B N   
1583 C  CA  . LYS B 40  ? 0.1897 0.1697 0.5159 -0.0164 0.0068  -0.0138 37  LYS B CA  
1584 C  C   . LYS B 40  ? 0.2071 0.2024 0.5199 -0.0045 0.0040  -0.0108 37  LYS B C   
1585 O  O   . LYS B 40  ? 0.2293 0.2343 0.5218 -0.0053 0.0091  -0.0087 37  LYS B O   
1586 C  CB  . LYS B 40  ? 0.1815 0.1621 0.5126 -0.0199 0.0103  -0.0298 37  LYS B CB  
1587 C  CG  . LYS B 40  ? 0.1871 0.1610 0.5145 -0.0230 0.0171  -0.0293 37  LYS B CG  
1588 C  CD  . LYS B 40  ? 0.1901 0.1682 0.5153 -0.0149 0.0208  -0.0298 37  LYS B CD  
1589 C  CE  . LYS B 40  ? 0.1909 0.1667 0.5188 -0.0180 0.0238  -0.0277 37  LYS B CE  
1590 N  NZ  . LYS B 40  ? 0.1750 0.1512 0.5170 -0.0270 0.0289  -0.0324 37  LYS B NZ  
1591 N  N   . GLU B 41  ? 0.2063 0.2122 0.5375 -0.0068 0.0075  -0.0099 38  GLU B N   
1592 C  CA  . GLU B 41  ? 0.2044 0.2310 0.5521 -0.0024 0.0035  -0.0076 38  GLU B CA  
1593 C  C   . GLU B 41  ? 0.2043 0.2622 0.5606 0.0000  -0.0073 -0.0097 38  GLU B C   
1594 O  O   . GLU B 41  ? 0.2212 0.2894 0.5527 0.0347  -0.0002 0.0013  38  GLU B O   
1595 C  CB  . GLU B 41  ? 0.2201 0.2623 0.5655 -0.0124 0.0092  0.0058  38  GLU B CB  
1596 C  CG  . GLU B 41  ? 0.2250 0.2504 0.5791 -0.0155 0.0115  0.0173  38  GLU B CG  
1597 C  CD  . GLU B 41  ? 0.2274 0.2588 0.5938 -0.0210 0.0125  0.0252  38  GLU B CD  
1598 O  OE1 . GLU B 41  ? 0.2295 0.2871 0.6141 -0.0368 0.0080  0.0403  38  GLU B OE1 
1599 O  OE2 . GLU B 41  ? 0.2175 0.2251 0.6040 -0.0350 0.0160  0.0222  38  GLU B OE2 
1600 N  N   . SER B 42  ? 0.2014 0.2840 0.5759 -0.0016 -0.0009 -0.0109 39  SER B N   
1601 C  CA  . SER B 42  ? 0.1969 0.2804 0.5909 -0.0090 -0.0062 -0.0137 39  SER B CA  
1602 C  C   . SER B 42  ? 0.2281 0.3228 0.5953 0.0065  0.0035  -0.0018 39  SER B C   
1603 O  O   . SER B 42  ? 0.2258 0.3537 0.5794 0.0119  0.0191  -0.0149 39  SER B O   
1604 C  CB  . SER B 42  ? 0.1977 0.2594 0.5938 -0.0283 -0.0100 -0.0151 39  SER B CB  
1605 O  OG  . SER B 42  ? 0.2068 0.2504 0.6013 -0.0218 -0.0145 -0.0139 39  SER B OG  
1606 N  N   . ASP B 43  ? 0.2312 0.3420 0.6276 0.0031  0.0001  0.0099  40  ASP B N   
1607 C  CA  . ASP B 43  ? 0.2692 0.3799 0.6478 0.0163  0.0029  0.0345  40  ASP B CA  
1608 C  C   . ASP B 43  ? 0.3112 0.4366 0.6578 0.0053  -0.0018 0.0252  40  ASP B C   
1609 O  O   . ASP B 43  ? 0.3287 0.4701 0.6436 -0.0213 -0.0006 0.0166  40  ASP B O   
1610 C  CB  . ASP B 43  ? 0.2817 0.3828 0.6673 0.0155  -0.0026 0.0420  40  ASP B CB  
1611 C  CG  . ASP B 43  ? 0.2903 0.3820 0.6901 0.0258  0.0023  0.0429  40  ASP B CG  
1612 O  OD1 . ASP B 43  ? 0.2955 0.3955 0.7386 0.0226  -0.0007 0.0325  40  ASP B OD1 
1613 O  OD2 . ASP B 43  ? 0.2918 0.3977 0.7133 0.0134  -0.0099 0.0637  40  ASP B OD2 
1614 N  N   . GLN B 44  ? 0.3430 0.4731 0.6908 0.0255  0.0045  0.0133  41  GLN B N   
1615 C  CA  . GLN B 44  ? 0.3896 0.5361 0.7184 0.0301  0.0102  0.0056  41  GLN B CA  
1616 C  C   . GLN B 44  ? 0.3922 0.5454 0.7310 0.0280  0.0111  0.0155  41  GLN B C   
1617 O  O   . GLN B 44  ? 0.3721 0.5521 0.7386 0.0379  0.0411  0.0179  41  GLN B O   
1618 C  CB  . GLN B 44  ? 0.4187 0.5550 0.7413 0.0379  0.0041  0.0006  41  GLN B CB  
1619 C  CG  . GLN B 44  ? 0.4413 0.5733 0.7615 0.0527  0.0021  -0.0090 41  GLN B CG  
1620 C  CD  . GLN B 44  ? 0.4662 0.5952 0.7812 0.0520  0.0014  -0.0052 41  GLN B CD  
1621 O  OE1 . GLN B 44  ? 0.5008 0.6261 0.8099 0.0423  -0.0154 -0.0173 41  GLN B OE1 
1622 N  NE2 . GLN B 44  ? 0.4871 0.6004 0.7824 0.0688  -0.0053 -0.0100 41  GLN B NE2 
1623 N  N   . PHE B 45  ? 0.3978 0.5551 0.7535 0.0256  0.0124  0.0211  42  PHE B N   
1624 C  CA  . PHE B 45  ? 0.4262 0.5804 0.7696 0.0184  -0.0004 0.0267  42  PHE B CA  
1625 C  C   . PHE B 45  ? 0.3978 0.5754 0.7653 0.0048  0.0006  0.0373  42  PHE B C   
1626 O  O   . PHE B 45  ? 0.3316 0.5791 0.7459 -0.0002 -0.0055 0.0530  42  PHE B O   
1627 C  CB  . PHE B 45  ? 0.4561 0.5895 0.7985 0.0131  0.0015  0.0251  42  PHE B CB  
1628 C  CG  . PHE B 45  ? 0.4825 0.6085 0.8320 0.0340  -0.0056 0.0253  42  PHE B CG  
1629 C  CD1 . PHE B 45  ? 0.4993 0.6249 0.8397 0.0353  -0.0134 0.0267  42  PHE B CD1 
1630 C  CD2 . PHE B 45  ? 0.5053 0.6248 0.8412 0.0410  -0.0156 0.0257  42  PHE B CD2 
1631 C  CE1 . PHE B 45  ? 0.5207 0.6312 0.8486 0.0399  -0.0158 0.0249  42  PHE B CE1 
1632 C  CE2 . PHE B 45  ? 0.5084 0.6358 0.8524 0.0463  -0.0181 0.0223  42  PHE B CE2 
1633 C  CZ  . PHE B 45  ? 0.5142 0.6409 0.8563 0.0437  -0.0182 0.0257  42  PHE B CZ  
1634 N  N   . PRO B 46  ? 0.4386 0.5985 0.7741 -0.0110 0.0047  0.0372  43  PRO B N   
1635 C  CA  . PRO B 46  ? 0.4548 0.5807 0.7792 -0.0086 0.0102  0.0408  43  PRO B CA  
1636 C  C   . PRO B 46  ? 0.4530 0.5451 0.7820 0.0015  0.0133  0.0268  43  PRO B C   
1637 O  O   . PRO B 46  ? 0.5170 0.5294 0.7864 0.0315  -0.0099 0.0385  43  PRO B O   
1638 C  CB  . PRO B 46  ? 0.4625 0.6094 0.7835 -0.0110 0.0100  0.0407  43  PRO B CB  
1639 C  CG  . PRO B 46  ? 0.4586 0.6081 0.7830 -0.0111 0.0051  0.0473  43  PRO B CG  
1640 C  CD  . PRO B 46  ? 0.4497 0.6044 0.7873 -0.0064 0.0103  0.0382  43  PRO B CD  
1641 N  N   . GLU B 47  ? 0.4350 0.5224 0.7771 -0.0090 0.0335  0.0207  44  GLU B N   
1642 C  CA  . GLU B 47  ? 0.4074 0.4829 0.7731 0.0111  0.0432  0.0039  44  GLU B CA  
1643 C  C   . GLU B 47  ? 0.3578 0.4053 0.7575 0.0049  0.0299  0.0065  44  GLU B C   
1644 O  O   . GLU B 47  ? 0.3191 0.4034 0.7536 -0.0307 0.0284  0.0140  44  GLU B O   
1645 C  CB  . GLU B 47  ? 0.4331 0.4943 0.8032 0.0013  0.0710  -0.0100 44  GLU B CB  
1646 C  CG  . GLU B 47  ? 0.4554 0.5174 0.8173 0.0072  0.0940  -0.0140 44  GLU B CG  
1647 C  CD  . GLU B 47  ? 0.4712 0.5178 0.8308 0.0261  0.1116  -0.0114 44  GLU B CD  
1648 O  OE1 . GLU B 47  ? 0.4521 0.4954 0.8427 0.0628  0.1294  -0.0252 44  GLU B OE1 
1649 O  OE2 . GLU B 47  ? 0.4643 0.5309 0.8511 0.0140  0.1265  -0.0190 44  GLU B OE2 
1650 N  N   . TRP B 48  ? 0.3158 0.3447 0.7256 -0.0288 0.0309  0.0000  45  TRP B N   
1651 C  CA  . TRP B 48  ? 0.3106 0.2852 0.7058 -0.0275 0.0357  0.0023  45  TRP B CA  
1652 C  C   . TRP B 48  ? 0.3116 0.2680 0.6650 -0.0091 0.0265  0.0180  45  TRP B C   
1653 O  O   . TRP B 48  ? 0.3119 0.2949 0.6569 0.0069  0.0431  0.0127  45  TRP B O   
1654 C  CB  . TRP B 48  ? 0.3286 0.2692 0.7186 -0.0267 0.0339  0.0055  45  TRP B CB  
1655 C  CG  . TRP B 48  ? 0.3287 0.2707 0.7531 -0.0388 0.0300  -0.0029 45  TRP B CG  
1656 C  CD1 . TRP B 48  ? 0.3512 0.2731 0.7677 -0.0339 0.0248  -0.0020 45  TRP B CD1 
1657 C  CD2 . TRP B 48  ? 0.3615 0.2318 0.7654 -0.0463 0.0250  -0.0036 45  TRP B CD2 
1658 N  NE1 . TRP B 48  ? 0.3623 0.2793 0.7896 -0.0408 0.0229  -0.0180 45  TRP B NE1 
1659 C  CE2 . TRP B 48  ? 0.3647 0.2609 0.7789 -0.0495 0.0153  -0.0155 45  TRP B CE2 
1660 C  CE3 . TRP B 48  ? 0.3699 0.2409 0.7667 -0.0506 0.0200  -0.0046 45  TRP B CE3 
1661 C  CZ2 . TRP B 48  ? 0.3754 0.2225 0.7765 -0.0659 0.0193  -0.0096 45  TRP B CZ2 
1662 C  CZ3 . TRP B 48  ? 0.3655 0.2263 0.7710 -0.0550 0.0190  -0.0151 45  TRP B CZ3 
1663 C  CH2 . TRP B 48  ? 0.3886 0.2255 0.7685 -0.0656 0.0157  -0.0097 45  TRP B CH2 
1664 N  N   . GLU B 49  ? 0.2997 0.2509 0.6391 -0.0091 0.0248  0.0323  46  GLU B N   
1665 C  CA  . GLU B 49  ? 0.3050 0.2410 0.6276 0.0053  0.0231  0.0311  46  GLU B CA  
1666 C  C   . GLU B 49  ? 0.2566 0.1910 0.6049 -0.0086 0.0245  0.0317  46  GLU B C   
1667 O  O   . GLU B 49  ? 0.2207 0.1949 0.5920 0.0011  0.0130  0.0277  46  GLU B O   
1668 C  CB  . GLU B 49  ? 0.3519 0.2666 0.6493 0.0193  0.0193  0.0478  46  GLU B CB  
1669 C  CG  . GLU B 49  ? 0.4211 0.3030 0.6709 0.0063  0.0225  0.0348  46  GLU B CG  
1670 C  CD  . GLU B 49  ? 0.4635 0.3116 0.6899 0.0208  0.0250  0.0479  46  GLU B CD  
1671 O  OE1 . GLU B 49  ? 0.5208 0.3764 0.6917 0.0144  0.0255  0.0562  46  GLU B OE1 
1672 O  OE2 . GLU B 49  ? 0.5556 0.3398 0.7192 0.0135  0.0389  0.0404  46  GLU B OE2 
1673 N  N   . SER B 50  ? 0.2630 0.1978 0.5815 -0.0230 0.0239  0.0214  47  SER B N   
1674 C  CA  . SER B 50  ? 0.2577 0.1616 0.5705 -0.0141 0.0259  0.0176  47  SER B CA  
1675 C  C   . SER B 50  ? 0.2370 0.1561 0.5570 -0.0121 0.0284  0.0231  47  SER B C   
1676 O  O   . SER B 50  ? 0.2795 0.1196 0.5712 -0.0091 0.0390  0.0086  47  SER B O   
1677 C  CB  . SER B 50  ? 0.2737 0.1604 0.5779 0.0083  0.0227  0.0090  47  SER B CB  
1678 O  OG  . SER B 50  ? 0.2867 0.1626 0.5800 0.0322  0.0234  0.0011  47  SER B OG  
1679 N  N   . ALA B 51  ? 0.2105 0.1245 0.5429 -0.0203 0.0150  0.0187  48  ALA B N   
1680 C  CA  . ALA B 51  ? 0.2007 0.1432 0.5404 -0.0010 0.0129  0.0123  48  ALA B CA  
1681 C  C   . ALA B 51  ? 0.1930 0.1242 0.5407 -0.0055 0.0035  0.0005  48  ALA B C   
1682 O  O   . ALA B 51  ? 0.2079 0.1238 0.5653 0.0051  0.0082  0.0080  48  ALA B O   
1683 C  CB  . ALA B 51  ? 0.2108 0.1626 0.5447 0.0095  0.0087  0.0184  48  ALA B CB  
1684 N  N   . GLY B 52  ? 0.1770 0.1134 0.5277 0.0067  0.0068  -0.0033 49  GLY B N   
1685 C  CA  . GLY B 52  ? 0.1529 0.1072 0.5146 0.0094  0.0017  -0.0080 49  GLY B CA  
1686 C  C   . GLY B 52  ? 0.1578 0.1170 0.5175 0.0268  -0.0039 -0.0051 49  GLY B C   
1687 O  O   . GLY B 52  ? 0.1640 0.1340 0.4992 0.0158  -0.0093 -0.0079 49  GLY B O   
1688 N  N   . ILE B 53  ? 0.1522 0.1201 0.5306 0.0125  -0.0079 -0.0053 50  ILE B N   
1689 C  CA  . ILE B 53  ? 0.1510 0.1348 0.5410 0.0113  -0.0122 -0.0148 50  ILE B CA  
1690 C  C   . ILE B 53  ? 0.1579 0.1392 0.5484 0.0100  -0.0131 -0.0196 50  ILE B C   
1691 O  O   . ILE B 53  ? 0.2050 0.1464 0.5443 0.0107  -0.0169 -0.0010 50  ILE B O   
1692 C  CB  . ILE B 53  ? 0.1483 0.1227 0.5456 0.0154  -0.0182 -0.0216 50  ILE B CB  
1693 C  CG1 . ILE B 53  ? 0.1522 0.1286 0.5439 0.0303  -0.0161 -0.0291 50  ILE B CG1 
1694 C  CG2 . ILE B 53  ? 0.1447 0.1317 0.5471 0.0191  -0.0199 -0.0243 50  ILE B CG2 
1695 C  CD1 . ILE B 53  ? 0.1590 0.1419 0.5453 0.0268  -0.0115 -0.0243 50  ILE B CD1 
1696 N  N   . TYR B 54  ? 0.1492 0.1389 0.5653 0.0091  -0.0129 -0.0233 51  TYR B N   
1697 C  CA  . TYR B 54  ? 0.1659 0.1537 0.5720 0.0024  -0.0012 -0.0286 51  TYR B CA  
1698 C  C   . TYR B 54  ? 0.1769 0.1416 0.5792 0.0125  -0.0007 -0.0329 51  TYR B C   
1699 O  O   . TYR B 54  ? 0.1697 0.1378 0.5867 0.0227  -0.0058 -0.0374 51  TYR B O   
1700 C  CB  . TYR B 54  ? 0.1605 0.1593 0.5767 0.0039  0.0179  -0.0235 51  TYR B CB  
1701 C  CG  . TYR B 54  ? 0.1699 0.1683 0.5814 0.0156  0.0288  -0.0216 51  TYR B CG  
1702 C  CD1 . TYR B 54  ? 0.1968 0.1728 0.5880 0.0118  0.0376  -0.0234 51  TYR B CD1 
1703 C  CD2 . TYR B 54  ? 0.1843 0.1680 0.5888 0.0074  0.0332  -0.0233 51  TYR B CD2 
1704 C  CE1 . TYR B 54  ? 0.1826 0.1658 0.5896 -0.0012 0.0424  -0.0177 51  TYR B CE1 
1705 C  CE2 . TYR B 54  ? 0.1781 0.1942 0.5934 -0.0032 0.0340  -0.0230 51  TYR B CE2 
1706 C  CZ  . TYR B 54  ? 0.1859 0.1843 0.5964 0.0028  0.0386  -0.0204 51  TYR B CZ  
1707 O  OH  . TYR B 54  ? 0.1813 0.1913 0.6059 -0.0121 0.0454  0.0028  51  TYR B OH  
1708 N  N   . ASP B 55  ? 0.1939 0.1381 0.5938 0.0036  -0.0046 -0.0331 52  ASP B N   
1709 C  CA  . ASP B 55  ? 0.2094 0.1615 0.6016 0.0112  0.0033  -0.0303 52  ASP B CA  
1710 C  C   . ASP B 55  ? 0.2097 0.1696 0.6112 0.0063  -0.0026 -0.0381 52  ASP B C   
1711 O  O   . ASP B 55  ? 0.2345 0.1850 0.6143 -0.0236 -0.0015 -0.0231 52  ASP B O   
1712 C  CB  . ASP B 55  ? 0.2306 0.1825 0.6018 0.0147  0.0089  -0.0301 52  ASP B CB  
1713 C  CG  . ASP B 55  ? 0.2692 0.2012 0.6013 0.0192  0.0204  -0.0342 52  ASP B CG  
1714 O  OD1 . ASP B 55  ? 0.2635 0.2284 0.6034 0.0233  0.0088  -0.0253 52  ASP B OD1 
1715 O  OD2 . ASP B 55  ? 0.3128 0.2245 0.6024 0.0165  0.0287  -0.0273 52  ASP B OD2 
1716 N  N   . GLY B 56  ? 0.2152 0.1649 0.6140 0.0103  0.0007  -0.0431 53  GLY B N   
1717 C  CA  . GLY B 56  ? 0.2262 0.1552 0.6266 0.0202  -0.0035 -0.0525 53  GLY B CA  
1718 C  C   . GLY B 56  ? 0.2220 0.1643 0.6383 0.0229  -0.0056 -0.0522 53  GLY B C   
1719 O  O   . GLY B 56  ? 0.1791 0.1635 0.6374 0.0566  0.0048  -0.0411 53  GLY B O   
1720 N  N   . ASN B 57  ? 0.2683 0.1890 0.6545 0.0293  -0.0200 -0.0559 54  ASN B N   
1721 C  CA  . ASN B 57  ? 0.2678 0.2044 0.6681 0.0084  -0.0247 -0.0525 54  ASN B CA  
1722 C  C   . ASN B 57  ? 0.2731 0.2091 0.6592 0.0127  -0.0277 -0.0546 54  ASN B C   
1723 O  O   . ASN B 57  ? 0.2678 0.2248 0.6827 0.0175  -0.0425 -0.0433 54  ASN B O   
1724 C  CB  . ASN B 57  ? 0.3131 0.2287 0.6885 -0.0088 -0.0217 -0.0641 54  ASN B CB  
1725 C  CG  . ASN B 57  ? 0.3364 0.2515 0.7014 0.0067  -0.0184 -0.0563 54  ASN B CG  
1726 O  OD1 . ASN B 57  ? 0.3774 0.3280 0.7077 -0.0048 0.0040  -0.0581 54  ASN B OD1 
1727 N  ND2 . ASN B 57  ? 0.3772 0.3119 0.7021 0.0093  -0.0148 -0.0715 54  ASN B ND2 
1728 N  N   . GLN B 58  ? 0.2667 0.1907 0.6362 0.0138  -0.0404 -0.0626 55  GLN B N   
1729 C  CA  . GLN B 58  ? 0.2520 0.2075 0.6178 0.0167  -0.0493 -0.0572 55  GLN B CA  
1730 C  C   . GLN B 58  ? 0.2159 0.2003 0.5974 0.0186  -0.0509 -0.0475 55  GLN B C   
1731 O  O   . GLN B 58  ? 0.2161 0.1924 0.5862 0.0058  -0.0572 -0.0322 55  GLN B O   
1732 C  CB  . GLN B 58  ? 0.2756 0.2436 0.6269 0.0173  -0.0467 -0.0604 55  GLN B CB  
1733 C  CG  . GLN B 58  ? 0.3092 0.2727 0.6303 0.0329  -0.0502 -0.0570 55  GLN B CG  
1734 C  CD  . GLN B 58  ? 0.3209 0.2843 0.6437 0.0476  -0.0539 -0.0555 55  GLN B CD  
1735 O  OE1 . GLN B 58  ? 0.3445 0.3528 0.6501 0.0324  -0.0678 -0.0645 55  GLN B OE1 
1736 N  NE2 . GLN B 58  ? 0.2988 0.3126 0.6521 0.0710  -0.0539 -0.0491 55  GLN B NE2 
1737 N  N   . LEU B 59  ? 0.2239 0.1904 0.5782 0.0139  -0.0477 -0.0433 56  LEU B N   
1738 C  CA  . LEU B 59  ? 0.2076 0.1871 0.5609 0.0331  -0.0435 -0.0412 56  LEU B CA  
1739 C  C   . LEU B 59  ? 0.2315 0.1860 0.5564 0.0275  -0.0421 -0.0440 56  LEU B C   
1740 O  O   . LEU B 59  ? 0.2452 0.1906 0.5592 0.0238  -0.0544 -0.0391 56  LEU B O   
1741 C  CB  . LEU B 59  ? 0.2087 0.1991 0.5498 0.0274  -0.0415 -0.0398 56  LEU B CB  
1742 C  CG  . LEU B 59  ? 0.2008 0.1817 0.5314 0.0342  -0.0418 -0.0282 56  LEU B CG  
1743 C  CD1 . LEU B 59  ? 0.1752 0.1746 0.5336 0.0232  -0.0456 -0.0328 56  LEU B CD1 
1744 C  CD2 . LEU B 59  ? 0.1997 0.2016 0.5291 0.0297  -0.0417 -0.0303 56  LEU B CD2 
1745 N  N   . ILE B 60  ? 0.2144 0.1721 0.5520 0.0341  -0.0266 -0.0430 57  ILE B N   
1746 C  CA  . ILE B 60  ? 0.2419 0.1663 0.5543 0.0175  -0.0238 -0.0427 57  ILE B CA  
1747 C  C   . ILE B 60  ? 0.2263 0.1523 0.5429 0.0233  -0.0211 -0.0348 57  ILE B C   
1748 O  O   . ILE B 60  ? 0.2544 0.1816 0.5378 0.0198  -0.0299 -0.0222 57  ILE B O   
1749 C  CB  . ILE B 60  ? 0.2565 0.2101 0.5637 0.0306  -0.0150 -0.0446 57  ILE B CB  
1750 C  CG1 . ILE B 60  ? 0.2673 0.2403 0.5719 0.0295  -0.0236 -0.0434 57  ILE B CG1 
1751 C  CG2 . ILE B 60  ? 0.2599 0.2055 0.5716 0.0361  -0.0139 -0.0503 57  ILE B CG2 
1752 C  CD1 . ILE B 60  ? 0.2759 0.2613 0.5819 0.0182  -0.0213 -0.0378 57  ILE B CD1 
1753 N  N   . GLY B 61  ? 0.2078 0.1128 0.5356 0.0050  -0.0240 -0.0386 58  GLY B N   
1754 C  CA  . GLY B 61  ? 0.1862 0.1191 0.5326 0.0010  -0.0140 -0.0378 58  GLY B CA  
1755 C  C   . GLY B 61  ? 0.1722 0.1126 0.5247 -0.0059 -0.0083 -0.0293 58  GLY B C   
1756 O  O   . GLY B 61  ? 0.2135 0.1294 0.5489 -0.0290 -0.0189 -0.0201 58  GLY B O   
1757 N  N   . TYR B 62  ? 0.1779 0.1203 0.5028 -0.0107 0.0002  -0.0244 59  TYR B N   
1758 C  CA  . TYR B 62  ? 0.1651 0.1322 0.4966 -0.0100 0.0049  -0.0131 59  TYR B CA  
1759 C  C   . TYR B 62  ? 0.1557 0.1228 0.4922 -0.0159 0.0151  -0.0043 59  TYR B C   
1760 O  O   . TYR B 62  ? 0.1343 0.1248 0.4949 -0.0194 0.0219  -0.0176 59  TYR B O   
1761 C  CB  . TYR B 62  ? 0.1598 0.1544 0.4952 -0.0155 -0.0080 -0.0133 59  TYR B CB  
1762 C  CG  . TYR B 62  ? 0.1357 0.1381 0.4901 -0.0052 -0.0135 -0.0154 59  TYR B CG  
1763 C  CD1 . TYR B 62  ? 0.1509 0.1476 0.4854 -0.0004 -0.0107 -0.0129 59  TYR B CD1 
1764 C  CD2 . TYR B 62  ? 0.1581 0.1407 0.4921 -0.0090 -0.0179 -0.0153 59  TYR B CD2 
1765 C  CE1 . TYR B 62  ? 0.1730 0.1583 0.4877 -0.0071 -0.0073 -0.0147 59  TYR B CE1 
1766 C  CE2 . TYR B 62  ? 0.1658 0.1366 0.4888 -0.0041 -0.0135 -0.0174 59  TYR B CE2 
1767 C  CZ  . TYR B 62  ? 0.1820 0.1621 0.4893 -0.0092 -0.0149 -0.0252 59  TYR B CZ  
1768 O  OH  . TYR B 62  ? 0.1861 0.1976 0.4965 -0.0064 -0.0128 -0.0266 59  TYR B OH  
1769 N  N   . ALA B 63  ? 0.1453 0.1305 0.4988 -0.0120 0.0082  0.0076  60  ALA B N   
1770 C  CA  . ALA B 63  ? 0.1404 0.1364 0.5081 -0.0028 0.0057  0.0098  60  ALA B CA  
1771 C  C   . ALA B 63  ? 0.1290 0.1381 0.5156 -0.0031 0.0039  0.0163  60  ALA B C   
1772 O  O   . ALA B 63  ? 0.1489 0.1290 0.5275 -0.0058 0.0061  0.0263  60  ALA B O   
1773 C  CB  . ALA B 63  ? 0.1412 0.1505 0.5131 0.0020  0.0035  0.0172  60  ALA B CB  
1774 N  N   A MET B 64  ? 0.1447 0.1365 0.5194 -0.0089 0.0024  0.0154  61  MET B N   
1775 N  N   B MET B 64  ? 0.1388 0.1359 0.5183 -0.0009 0.0056  0.0183  61  MET B N   
1776 C  CA  A MET B 64  ? 0.1646 0.1359 0.5275 -0.0063 0.0001  0.0120  61  MET B CA  
1777 C  CA  B MET B 64  ? 0.1459 0.1379 0.5217 0.0058  0.0069  0.0211  61  MET B CA  
1778 C  C   A MET B 64  ? 0.1667 0.1351 0.5307 -0.0028 -0.0022 0.0151  61  MET B C   
1779 C  C   B MET B 64  ? 0.1552 0.1426 0.5289 0.0024  0.0042  0.0207  61  MET B C   
1780 O  O   A MET B 64  ? 0.1971 0.1637 0.5487 -0.0232 -0.0022 0.0227  61  MET B O   
1781 O  O   B MET B 64  ? 0.1669 0.1518 0.5355 -0.0041 0.0033  0.0245  61  MET B O   
1782 C  CB  A MET B 64  ? 0.1559 0.1557 0.5362 -0.0049 -0.0093 -0.0035 61  MET B CB  
1783 C  CB  B MET B 64  ? 0.1400 0.1458 0.5187 0.0076  0.0063  0.0194  61  MET B CB  
1784 C  CG  A MET B 64  ? 0.1788 0.1586 0.5421 0.0071  -0.0173 -0.0214 61  MET B CG  
1785 C  CG  B MET B 64  ? 0.1393 0.1419 0.5162 0.0171  0.0058  0.0180  61  MET B CG  
1786 S  SD  A MET B 64  ? 0.2181 0.1718 0.5643 0.0361  -0.0175 -0.0382 61  MET B SD  
1787 S  SD  B MET B 64  ? 0.1431 0.1464 0.5115 0.0345  0.0059  0.0187  61  MET B SD  
1788 C  CE  A MET B 64  ? 0.2371 0.1944 0.5671 0.0414  -0.0176 -0.0426 61  MET B CE  
1789 C  CE  B MET B 64  ? 0.1307 0.1402 0.5143 0.0250  0.0111  0.0202  61  MET B CE  
1790 N  N   . TYR B 65  ? 0.1675 0.1457 0.5326 0.0021  0.0085  0.0226  62  TYR B N   
1791 C  CA  . TYR B 65  ? 0.1688 0.1727 0.5514 -0.0055 0.0099  0.0271  62  TYR B CA  
1792 C  C   . TYR B 65  ? 0.1939 0.2012 0.5516 -0.0141 0.0071  0.0210  62  TYR B C   
1793 O  O   . TYR B 65  ? 0.1755 0.2419 0.5515 -0.0155 0.0079  0.0075  62  TYR B O   
1794 C  CB  . TYR B 65  ? 0.1931 0.1883 0.5674 0.0119  0.0226  0.0349  62  TYR B CB  
1795 C  CG  . TYR B 65  ? 0.2096 0.1885 0.5900 0.0177  0.0373  0.0530  62  TYR B CG  
1796 C  CD1 . TYR B 65  ? 0.2209 0.1883 0.6042 0.0221  0.0462  0.0617  62  TYR B CD1 
1797 C  CD2 . TYR B 65  ? 0.2262 0.1933 0.6020 0.0170  0.0417  0.0498  62  TYR B CD2 
1798 C  CE1 . TYR B 65  ? 0.2563 0.1815 0.6156 0.0215  0.0485  0.0681  62  TYR B CE1 
1799 C  CE2 . TYR B 65  ? 0.2627 0.2013 0.6139 0.0093  0.0491  0.0625  62  TYR B CE2 
1800 C  CZ  . TYR B 65  ? 0.2832 0.1775 0.6222 0.0086  0.0487  0.0721  62  TYR B CZ  
1801 O  OH  . TYR B 65  ? 0.3395 0.2060 0.6563 -0.0303 0.0640  0.0684  62  TYR B OH  
1802 N  N   . GLY B 66  ? 0.2145 0.2567 0.5558 -0.0145 -0.0010 0.0165  63  GLY B N   
1803 C  CA  . GLY B 66  ? 0.2630 0.2842 0.5677 -0.0258 -0.0079 0.0165  63  GLY B CA  
1804 C  C   . GLY B 66  ? 0.2564 0.2973 0.5888 -0.0256 -0.0155 0.0211  63  GLY B C   
1805 O  O   . GLY B 66  ? 0.2418 0.2979 0.5731 -0.0217 -0.0151 0.0258  63  GLY B O   
1806 N  N   . ARG B 67  ? 0.3233 0.3380 0.6103 -0.0264 -0.0162 0.0217  64  ARG B N   
1807 C  CA  . ARG B 67  ? 0.3577 0.3998 0.6492 -0.0471 -0.0306 0.0080  64  ARG B CA  
1808 C  C   . ARG B 67  ? 0.4146 0.4684 0.6746 -0.0374 -0.0148 -0.0021 64  ARG B C   
1809 O  O   . ARG B 67  ? 0.4450 0.4925 0.6880 -0.0624 -0.0117 0.0011  64  ARG B O   
1810 C  CB  . ARG B 67  ? 0.3858 0.4152 0.6593 -0.0495 -0.0385 0.0144  64  ARG B CB  
1811 C  CG  . ARG B 67  ? 0.3849 0.4145 0.6790 -0.0725 -0.0447 0.0095  64  ARG B CG  
1812 C  CD  . ARG B 67  ? 0.4022 0.4303 0.6877 -0.0811 -0.0435 0.0139  64  ARG B CD  
1813 N  NE  . ARG B 67  ? 0.4150 0.4560 0.7010 -0.0868 -0.0543 0.0127  64  ARG B NE  
1814 C  CZ  . ARG B 67  ? 0.4242 0.4905 0.7164 -0.0770 -0.0502 -0.0009 64  ARG B CZ  
1815 N  NH1 . ARG B 67  ? 0.4279 0.5011 0.7273 -0.0775 -0.0458 0.0033  64  ARG B NH1 
1816 N  NH2 . ARG B 67  ? 0.4717 0.5156 0.7207 -0.0645 -0.0521 -0.0085 64  ARG B NH2 
1817 N  N   . TRP B 68  ? 0.4611 0.4941 0.7184 -0.0276 -0.0133 0.0071  65  TRP B N   
1818 C  CA  . TRP B 68  ? 0.5121 0.5494 0.7533 0.0024  -0.0192 -0.0054 65  TRP B CA  
1819 C  C   . TRP B 68  ? 0.5622 0.5994 0.7756 0.0104  -0.0281 -0.0116 65  TRP B C   
1820 O  O   . TRP B 68  ? 0.5408 0.6492 0.7995 0.0161  -0.0140 -0.0096 65  TRP B O   
1821 C  CB  . TRP B 68  ? 0.5277 0.5685 0.7505 -0.0007 -0.0292 0.0034  65  TRP B CB  
1822 C  CG  . TRP B 68  ? 0.5212 0.5752 0.7494 0.0037  -0.0362 0.0109  65  TRP B CG  
1823 C  CD1 . TRP B 68  ? 0.5040 0.5757 0.7575 0.0045  -0.0400 0.0169  65  TRP B CD1 
1824 C  CD2 . TRP B 68  ? 0.5121 0.5806 0.7555 0.0016  -0.0374 0.0164  65  TRP B CD2 
1825 N  NE1 . TRP B 68  ? 0.4839 0.5717 0.7644 0.0035  -0.0557 0.0171  65  TRP B NE1 
1826 C  CE2 . TRP B 68  ? 0.4859 0.5727 0.7497 0.0100  -0.0407 0.0207  65  TRP B CE2 
1827 C  CE3 . TRP B 68  ? 0.5323 0.5727 0.7457 0.0126  -0.0408 0.0185  65  TRP B CE3 
1828 C  CZ2 . TRP B 68  ? 0.4657 0.5479 0.7423 0.0235  -0.0397 0.0172  65  TRP B CZ2 
1829 C  CZ3 . TRP B 68  ? 0.5136 0.5616 0.7354 0.0160  -0.0365 0.0205  65  TRP B CZ3 
1830 C  CH2 . TRP B 68  ? 0.4880 0.5579 0.7341 0.0108  -0.0343 0.0215  65  TRP B CH2 
1831 N  N   . GLN B 69  ? 0.5875 0.6198 0.8019 0.0228  -0.0283 -0.0218 66  GLN B N   
1832 C  CA  . GLN B 69  ? 0.6150 0.6310 0.8121 0.0193  -0.0354 -0.0176 66  GLN B CA  
1833 C  C   . GLN B 69  ? 0.6140 0.6397 0.8220 0.0131  -0.0508 -0.0120 66  GLN B C   
1834 O  O   . GLN B 69  ? 0.6461 0.6523 0.8197 0.0070  -0.0602 -0.0066 66  GLN B O   
1835 C  CB  . GLN B 69  ? 0.6374 0.6357 0.8231 0.0297  -0.0281 -0.0203 66  GLN B CB  
1836 C  CG  . GLN B 69  ? 0.6596 0.6333 0.8282 0.0319  -0.0254 -0.0226 66  GLN B CG  
1837 C  CD  . GLN B 69  ? 0.6790 0.6321 0.8290 0.0359  -0.0244 -0.0215 66  GLN B CD  
1838 O  OE1 . GLN B 69  ? 0.6955 0.6323 0.8223 0.0428  -0.0200 -0.0263 66  GLN B OE1 
1839 N  NE2 . GLN B 69  ? 0.6984 0.6279 0.8379 0.0417  -0.0274 -0.0236 66  GLN B NE2 
1840 N  N   . ASP B 70  ? 0.5940 0.6185 0.8291 0.0002  -0.0603 -0.0140 67  ASP B N   
1841 C  CA  . ASP B 70  ? 0.5772 0.5884 0.8236 0.0099  -0.0677 -0.0185 67  ASP B CA  
1842 C  C   . ASP B 70  ? 0.5408 0.5378 0.7964 -0.0098 -0.0738 -0.0180 67  ASP B C   
1843 O  O   . ASP B 70  ? 0.5065 0.5467 0.8029 0.0038  -0.0765 -0.0054 67  ASP B O   
1844 C  CB  . ASP B 70  ? 0.5991 0.6035 0.8290 0.0070  -0.0664 -0.0236 67  ASP B CB  
1845 C  CG  . ASP B 70  ? 0.6019 0.6306 0.8340 0.0113  -0.0656 -0.0270 67  ASP B CG  
1846 O  OD1 . ASP B 70  ? 0.6188 0.6458 0.8592 0.0247  -0.0567 -0.0281 67  ASP B OD1 
1847 O  OD2 . ASP B 70  ? 0.6010 0.6435 0.8335 0.0209  -0.0740 -0.0323 67  ASP B OD2 
1848 N  N   . GLY B 71  ? 0.4900 0.4860 0.7875 -0.0110 -0.0688 0.0159  68  GLY B N   
1849 C  CA  . GLY B 71  ? 0.4479 0.4354 0.7406 -0.0282 -0.0645 0.0252  68  GLY B CA  
1850 C  C   . GLY B 71  ? 0.4113 0.3755 0.7185 -0.0309 -0.0721 0.0338  68  GLY B C   
1851 O  O   . GLY B 71  ? 0.3915 0.3507 0.7099 -0.0357 -0.0737 0.0574  68  GLY B O   
1852 N  N   . ARG B 72  ? 0.3724 0.3050 0.6921 -0.0437 -0.0676 0.0224  69  ARG B N   
1853 C  CA  . ARG B 72  ? 0.3451 0.2808 0.6763 -0.0452 -0.0667 0.0181  69  ARG B CA  
1854 C  C   . ARG B 72  ? 0.3270 0.2534 0.6546 -0.0331 -0.0609 0.0235  69  ARG B C   
1855 O  O   . ARG B 72  ? 0.3297 0.2476 0.6571 -0.0289 -0.0551 0.0263  69  ARG B O   
1856 C  CB  . ARG B 72  ? 0.3567 0.2944 0.6808 -0.0412 -0.0646 0.0216  69  ARG B CB  
1857 C  CG  . ARG B 72  ? 0.3636 0.3027 0.6844 -0.0457 -0.0611 0.0168  69  ARG B CG  
1858 C  CD  . ARG B 72  ? 0.3754 0.3116 0.6907 -0.0426 -0.0528 0.0238  69  ARG B CD  
1859 N  NE  . ARG B 72  ? 0.3987 0.3109 0.6962 -0.0417 -0.0602 0.0162  69  ARG B NE  
1860 C  CZ  . ARG B 72  ? 0.4110 0.2969 0.7032 -0.0342 -0.0531 0.0225  69  ARG B CZ  
1861 N  NH1 . ARG B 72  ? 0.4277 0.2944 0.7047 -0.0485 -0.0496 0.0199  69  ARG B NH1 
1862 N  NH2 . ARG B 72  ? 0.4082 0.3138 0.7058 -0.0287 -0.0585 0.0265  69  ARG B NH2 
1863 N  N   . VAL B 73  ? 0.3002 0.2196 0.6353 -0.0351 -0.0730 0.0209  70  VAL B N   
1864 C  CA  . VAL B 73  ? 0.2633 0.2177 0.6144 -0.0351 -0.0684 0.0332  70  VAL B CA  
1865 C  C   . VAL B 73  ? 0.2148 0.2055 0.5949 -0.0196 -0.0641 0.0206  70  VAL B C   
1866 O  O   . VAL B 73  ? 0.2171 0.1960 0.5826 -0.0229 -0.0661 0.0171  70  VAL B O   
1867 C  CB  . VAL B 73  ? 0.2685 0.2211 0.6214 -0.0350 -0.0766 0.0376  70  VAL B CB  
1868 C  CG1 . VAL B 73  ? 0.2925 0.2141 0.6301 -0.0520 -0.0787 0.0387  70  VAL B CG1 
1869 C  CG2 . VAL B 73  ? 0.2903 0.2392 0.6221 -0.0311 -0.0751 0.0467  70  VAL B CG2 
1870 N  N   . TRP B 74  ? 0.1986 0.1813 0.5772 -0.0128 -0.0551 0.0179  71  TRP B N   
1871 C  CA  . TRP B 74  ? 0.1790 0.1750 0.5701 -0.0044 -0.0398 0.0219  71  TRP B CA  
1872 C  C   . TRP B 74  ? 0.1654 0.1685 0.5555 0.0019  -0.0308 0.0280  71  TRP B C   
1873 O  O   . TRP B 74  ? 0.1820 0.2080 0.5495 -0.0205 -0.0300 0.0321  71  TRP B O   
1874 C  CB  . TRP B 74  ? 0.1634 0.1802 0.5732 0.0025  -0.0421 0.0316  71  TRP B CB  
1875 C  CG  . TRP B 74  ? 0.1711 0.2083 0.5854 -0.0093 -0.0438 0.0247  71  TRP B CG  
1876 C  CD1 . TRP B 74  ? 0.1863 0.2202 0.5942 -0.0099 -0.0404 0.0282  71  TRP B CD1 
1877 C  CD2 . TRP B 74  ? 0.1642 0.1998 0.5946 0.0056  -0.0400 0.0323  71  TRP B CD2 
1878 N  NE1 . TRP B 74  ? 0.2069 0.2221 0.6035 -0.0161 -0.0428 0.0282  71  TRP B NE1 
1879 C  CE2 . TRP B 74  ? 0.1825 0.2158 0.6006 -0.0012 -0.0439 0.0329  71  TRP B CE2 
1880 C  CE3 . TRP B 74  ? 0.1571 0.2191 0.6016 0.0044  -0.0299 0.0321  71  TRP B CE3 
1881 C  CZ2 . TRP B 74  ? 0.1804 0.2208 0.6054 -0.0066 -0.0339 0.0272  71  TRP B CZ2 
1882 C  CZ3 . TRP B 74  ? 0.1862 0.2257 0.6112 -0.0092 -0.0334 0.0247  71  TRP B CZ3 
1883 C  CH2 . TRP B 74  ? 0.1919 0.2171 0.6077 -0.0134 -0.0325 0.0254  71  TRP B CH2 
1884 N  N   . LEU B 75  ? 0.1562 0.1843 0.5546 0.0125  -0.0244 0.0227  72  LEU B N   
1885 C  CA  . LEU B 75  ? 0.1723 0.1788 0.5594 0.0150  -0.0154 0.0178  72  LEU B CA  
1886 C  C   . LEU B 75  ? 0.1740 0.1670 0.5497 0.0182  -0.0078 0.0117  72  LEU B C   
1887 O  O   . LEU B 75  ? 0.1805 0.1831 0.5642 -0.0023 0.0027  0.0046  72  LEU B O   
1888 C  CB  . LEU B 75  ? 0.2049 0.2070 0.5761 0.0201  -0.0022 0.0123  72  LEU B CB  
1889 C  CG  . LEU B 75  ? 0.2389 0.2458 0.5967 0.0130  0.0001  0.0007  72  LEU B CG  
1890 C  CD1 . LEU B 75  ? 0.2691 0.2543 0.6019 0.0023  0.0084  -0.0002 72  LEU B CD1 
1891 C  CD2 . LEU B 75  ? 0.2753 0.2853 0.6052 0.0205  0.0089  -0.0086 72  LEU B CD2 
1892 N  N   . ASP B 76  ? 0.1721 0.1490 0.5399 0.0031  -0.0138 0.0057  73  ASP B N   
1893 C  CA  . ASP B 76  ? 0.1824 0.1418 0.5330 0.0043  -0.0154 0.0100  73  ASP B CA  
1894 C  C   . ASP B 76  ? 0.1656 0.1193 0.5193 -0.0127 -0.0195 0.0020  73  ASP B C   
1895 O  O   . ASP B 76  ? 0.2096 0.1270 0.5156 -0.0234 -0.0177 0.0124  73  ASP B O   
1896 C  CB  . ASP B 76  ? 0.1723 0.1551 0.5438 0.0156  -0.0174 0.0084  73  ASP B CB  
1897 C  CG  . ASP B 76  ? 0.1960 0.1749 0.5545 0.0219  -0.0128 0.0086  73  ASP B CG  
1898 O  OD1 . ASP B 76  ? 0.2164 0.1696 0.5697 0.0199  -0.0163 0.0123  73  ASP B OD1 
1899 O  OD2 . ASP B 76  ? 0.2453 0.1992 0.5682 0.0173  -0.0073 0.0137  73  ASP B OD2 
1900 N  N   . ARG B 77  ? 0.1664 0.1190 0.5047 -0.0037 -0.0123 -0.0023 74  ARG B N   
1901 C  CA  . ARG B 77  ? 0.1451 0.1222 0.5044 -0.0053 -0.0106 0.0024  74  ARG B CA  
1902 C  C   . ARG B 77  ? 0.1451 0.1399 0.5085 -0.0116 -0.0005 -0.0076 74  ARG B C   
1903 O  O   . ARG B 77  ? 0.1159 0.1696 0.4979 -0.0198 -0.0007 0.0080  74  ARG B O   
1904 C  CB  . ARG B 77  ? 0.1430 0.1206 0.4998 -0.0028 -0.0044 0.0012  74  ARG B CB  
1905 C  CG  . ARG B 77  ? 0.1424 0.1506 0.4956 0.0071  -0.0005 0.0087  74  ARG B CG  
1906 C  CD  . ARG B 77  ? 0.1500 0.1499 0.4989 -0.0047 -0.0069 0.0129  74  ARG B CD  
1907 N  NE  . ARG B 77  ? 0.1444 0.1714 0.5019 -0.0042 -0.0061 0.0081  74  ARG B NE  
1908 C  CZ  . ARG B 77  ? 0.1643 0.1715 0.5020 -0.0009 -0.0109 0.0091  74  ARG B CZ  
1909 N  NH1 . ARG B 77  ? 0.1755 0.1791 0.5048 0.0077  -0.0139 0.0189  74  ARG B NH1 
1910 N  NH2 . ARG B 77  ? 0.1677 0.1784 0.5075 0.0016  -0.0172 0.0037  74  ARG B NH2 
1911 N  N   . PHE B 78  ? 0.1605 0.1514 0.5145 -0.0014 -0.0018 -0.0147 75  PHE B N   
1912 C  CA  . PHE B 78  ? 0.1617 0.1585 0.5373 0.0115  0.0076  -0.0145 75  PHE B CA  
1913 C  C   . PHE B 78  ? 0.1853 0.1660 0.5356 0.0102  0.0197  -0.0177 75  PHE B C   
1914 O  O   . PHE B 78  ? 0.2461 0.1945 0.5430 -0.0010 0.0178  -0.0068 75  PHE B O   
1915 C  CB  . PHE B 78  ? 0.1624 0.1612 0.5542 0.0211  0.0068  -0.0129 75  PHE B CB  
1916 C  CG  . PHE B 78  ? 0.1762 0.1795 0.5772 0.0322  0.0153  -0.0147 75  PHE B CG  
1917 C  CD1 . PHE B 78  ? 0.1649 0.1731 0.5946 0.0183  0.0075  -0.0150 75  PHE B CD1 
1918 C  CD2 . PHE B 78  ? 0.2158 0.1925 0.5916 0.0325  0.0182  -0.0044 75  PHE B CD2 
1919 C  CE1 . PHE B 78  ? 0.1648 0.1827 0.5994 0.0293  0.0112  -0.0155 75  PHE B CE1 
1920 C  CE2 . PHE B 78  ? 0.2326 0.1999 0.6015 0.0413  0.0197  -0.0069 75  PHE B CE2 
1921 C  CZ  . PHE B 78  ? 0.1797 0.1774 0.6052 0.0447  0.0117  -0.0132 75  PHE B CZ  
1922 N  N   . LEU B 79  ? 0.1952 0.1431 0.5369 0.0040  0.0258  -0.0097 76  LEU B N   
1923 C  CA  . LEU B 79  ? 0.2300 0.1674 0.5392 0.0213  0.0253  -0.0021 76  LEU B CA  
1924 C  C   . LEU B 79  ? 0.2197 0.1725 0.5359 0.0239  0.0203  -0.0073 76  LEU B C   
1925 O  O   . LEU B 79  ? 0.2442 0.1896 0.5293 0.0165  0.0094  0.0038  76  LEU B O   
1926 C  CB  . LEU B 79  ? 0.2405 0.2104 0.5521 0.0277  0.0282  0.0004  76  LEU B CB  
1927 C  CG  . LEU B 79  ? 0.2655 0.2194 0.5611 0.0282  0.0297  -0.0010 76  LEU B CG  
1928 C  CD1 . LEU B 79  ? 0.2626 0.2368 0.5592 0.0233  0.0304  0.0012  76  LEU B CD1 
1929 C  CD2 . LEU B 79  ? 0.2893 0.2132 0.5652 0.0411  0.0277  0.0022  76  LEU B CD2 
1930 N  N   . ILE B 80  ? 0.2222 0.1777 0.5422 0.0348  0.0106  -0.0057 77  ILE B N   
1931 C  CA  . ILE B 80  ? 0.2120 0.1922 0.5460 0.0379  -0.0010 -0.0086 77  ILE B CA  
1932 C  C   . ILE B 80  ? 0.2174 0.1815 0.5546 0.0334  -0.0080 0.0044  77  ILE B C   
1933 O  O   . ILE B 80  ? 0.2017 0.1856 0.5564 0.0062  -0.0021 0.0138  77  ILE B O   
1934 C  CB  . ILE B 80  ? 0.2046 0.2142 0.5522 0.0527  -0.0073 -0.0124 77  ILE B CB  
1935 C  CG1 . ILE B 80  ? 0.1927 0.2370 0.5563 0.0514  -0.0073 -0.0117 77  ILE B CG1 
1936 C  CG2 . ILE B 80  ? 0.1916 0.2346 0.5450 0.0659  0.0000  -0.0129 77  ILE B CG2 
1937 C  CD1 . ILE B 80  ? 0.1769 0.2407 0.5544 0.0451  -0.0111 -0.0119 77  ILE B CD1 
1938 N  N   . ASP B 81  ? 0.2460 0.1847 0.5662 0.0206  -0.0209 0.0119  78  ASP B N   
1939 C  CA  . ASP B 81  ? 0.2708 0.1845 0.5817 0.0275  -0.0309 0.0158  78  ASP B CA  
1940 C  C   . ASP B 81  ? 0.3006 0.2054 0.5900 0.0280  -0.0262 0.0136  78  ASP B C   
1941 O  O   . ASP B 81  ? 0.3156 0.1992 0.5824 0.0436  -0.0302 0.0208  78  ASP B O   
1942 C  CB  . ASP B 81  ? 0.2713 0.1870 0.5869 0.0177  -0.0364 0.0186  78  ASP B CB  
1943 C  CG  . ASP B 81  ? 0.2912 0.2251 0.5941 0.0128  -0.0408 0.0302  78  ASP B CG  
1944 O  OD1 . ASP B 81  ? 0.3436 0.2487 0.6006 0.0027  -0.0382 0.0400  78  ASP B OD1 
1945 O  OD2 . ASP B 81  ? 0.2942 0.2497 0.6161 -0.0123 -0.0430 0.0296  78  ASP B OD2 
1946 N  N   A GLN B 82  ? 0.3244 0.2221 0.5998 0.0280  -0.0354 0.0162  79  GLN B N   
1947 N  N   B GLN B 82  ? 0.3296 0.2288 0.5956 0.0305  -0.0330 0.0175  79  GLN B N   
1948 C  CA  A GLN B 82  ? 0.3529 0.2448 0.6176 0.0274  -0.0322 0.0154  79  GLN B CA  
1949 C  CA  B GLN B 82  ? 0.3623 0.2584 0.6061 0.0240  -0.0276 0.0150  79  GLN B CA  
1950 C  C   A GLN B 82  ? 0.3964 0.2779 0.6211 0.0306  -0.0281 0.0068  79  GLN B C   
1951 C  C   B GLN B 82  ? 0.3972 0.2767 0.6163 0.0327  -0.0273 0.0070  79  GLN B C   
1952 O  O   A GLN B 82  ? 0.4426 0.3110 0.6174 0.0307  -0.0229 0.0067  79  GLN B O   
1953 O  O   B GLN B 82  ? 0.4171 0.2901 0.6153 0.0336  -0.0242 0.0072  79  GLN B O   
1954 C  CB  A GLN B 82  ? 0.3482 0.2488 0.6280 0.0234  -0.0369 0.0217  79  GLN B CB  
1955 C  CB  B GLN B 82  ? 0.3611 0.2734 0.6064 0.0194  -0.0291 0.0209  79  GLN B CB  
1956 C  CG  A GLN B 82  ? 0.3432 0.2393 0.6408 0.0257  -0.0381 0.0268  79  GLN B CG  
1957 C  CG  B GLN B 82  ? 0.3612 0.2792 0.6079 0.0088  -0.0286 0.0213  79  GLN B CG  
1958 C  CD  A GLN B 82  ? 0.3326 0.2543 0.6560 0.0267  -0.0386 0.0326  79  GLN B CD  
1959 C  CD  B GLN B 82  ? 0.3691 0.2943 0.6090 -0.0024 -0.0276 0.0235  79  GLN B CD  
1960 O  OE1 A GLN B 82  ? 0.3480 0.2247 0.6623 0.0561  -0.0386 0.0388  79  GLN B OE1 
1961 O  OE1 B GLN B 82  ? 0.3683 0.3022 0.6092 -0.0082 -0.0300 0.0297  79  GLN B OE1 
1962 N  NE2 A GLN B 82  ? 0.3333 0.2754 0.6648 0.0333  -0.0437 0.0342  79  GLN B NE2 
1963 N  NE2 B GLN B 82  ? 0.3707 0.2966 0.6083 -0.0103 -0.0270 0.0241  79  GLN B NE2 
1964 N  N   . ARG B 83  ? 0.4288 0.2715 0.6299 0.0341  -0.0283 0.0016  80  ARG B N   
1965 C  CA  . ARG B 83  ? 0.4596 0.3043 0.6424 0.0463  -0.0242 -0.0147 80  ARG B CA  
1966 C  C   . ARG B 83  ? 0.4785 0.3181 0.6483 0.0782  -0.0207 -0.0134 80  ARG B C   
1967 O  O   . ARG B 83  ? 0.4988 0.3318 0.6532 0.1016  -0.0285 -0.0254 80  ARG B O   
1968 C  CB  . ARG B 83  ? 0.4904 0.3167 0.6574 0.0295  -0.0195 -0.0141 80  ARG B CB  
1969 C  CG  . ARG B 83  ? 0.4895 0.3577 0.6669 0.0100  -0.0201 -0.0153 80  ARG B CG  
1970 C  CD  . ARG B 83  ? 0.5084 0.3822 0.6743 -0.0016 -0.0187 -0.0197 80  ARG B CD  
1971 N  NE  . ARG B 83  ? 0.5227 0.4191 0.6821 -0.0157 -0.0168 -0.0215 80  ARG B NE  
1972 C  CZ  . ARG B 83  ? 0.5434 0.4447 0.6936 -0.0381 -0.0071 -0.0301 80  ARG B CZ  
1973 N  NH1 . ARG B 83  ? 0.5504 0.4600 0.7092 -0.0448 -0.0005 -0.0337 80  ARG B NH1 
1974 N  NH2 . ARG B 83  ? 0.5555 0.4674 0.6968 -0.0415 -0.0031 -0.0303 80  ARG B NH2 
1975 N  N   . PHE B 84  ? 0.4743 0.3143 0.6531 0.0902  -0.0201 -0.0159 81  PHE B N   
1976 C  CA  . PHE B 84  ? 0.4816 0.3381 0.6739 0.0976  -0.0210 -0.0001 81  PHE B CA  
1977 C  C   . PHE B 84  ? 0.4717 0.3654 0.6926 0.1013  -0.0216 0.0098  81  PHE B C   
1978 O  O   . PHE B 84  ? 0.4892 0.3343 0.7005 0.1143  -0.0236 0.0151  81  PHE B O   
1979 C  CB  . PHE B 84  ? 0.4735 0.3527 0.6745 0.0858  -0.0187 0.0023  81  PHE B CB  
1980 C  CG  . PHE B 84  ? 0.4693 0.3307 0.6782 0.0819  -0.0233 0.0012  81  PHE B CG  
1981 C  CD1 . PHE B 84  ? 0.4694 0.3714 0.6788 0.0664  -0.0242 -0.0038 81  PHE B CD1 
1982 C  CD2 . PHE B 84  ? 0.4665 0.3194 0.6763 0.0720  -0.0235 0.0095  81  PHE B CD2 
1983 C  CE1 . PHE B 84  ? 0.4779 0.3624 0.6795 0.0610  -0.0207 0.0013  81  PHE B CE1 
1984 C  CE2 . PHE B 84  ? 0.4613 0.3302 0.6810 0.0780  -0.0298 0.0093  81  PHE B CE2 
1985 C  CZ  . PHE B 84  ? 0.4642 0.3456 0.6787 0.0742  -0.0284 0.0022  81  PHE B CZ  
1986 N  N   . GLN B 85  ? 0.5003 0.4068 0.7137 0.1076  -0.0227 0.0398  82  GLN B N   
1987 C  CA  . GLN B 85  ? 0.5178 0.4405 0.7388 0.1020  -0.0145 0.0394  82  GLN B CA  
1988 C  C   . GLN B 85  ? 0.5549 0.5180 0.7518 0.0983  0.0033  0.0412  82  GLN B C   
1989 O  O   . GLN B 85  ? 0.5790 0.5723 0.7466 0.0922  -0.0007 0.0399  82  GLN B O   
1990 C  CB  . GLN B 85  ? 0.5436 0.4365 0.7589 0.0920  -0.0065 0.0372  82  GLN B CB  
1991 C  CG  . GLN B 85  ? 0.5443 0.4463 0.7680 0.0948  -0.0023 0.0355  82  GLN B CG  
1992 C  CD  . GLN B 85  ? 0.5741 0.4633 0.7918 0.0885  -0.0088 0.0296  82  GLN B CD  
1993 O  OE1 . GLN B 85  ? 0.5837 0.5180 0.8242 0.0850  -0.0146 0.0251  82  GLN B OE1 
1994 N  NE2 . GLN B 85  ? 0.5742 0.4738 0.7940 0.0944  -0.0009 0.0342  82  GLN B NE2 
1995 N  N   . GLY B 86  ? 0.5567 0.5658 0.7745 0.1044  0.0121  0.0444  83  GLY B N   
1996 C  CA  . GLY B 86  ? 0.5748 0.5933 0.7813 0.1138  0.0222  0.0455  83  GLY B CA  
1997 C  C   . GLY B 86  ? 0.5823 0.6126 0.7927 0.1216  0.0289  0.0396  83  GLY B C   
1998 O  O   . GLY B 86  ? 0.6376 0.6869 0.8129 0.1341  0.0420  0.0331  83  GLY B O   
1999 N  N   . GLN B 87  ? 0.5427 0.5902 0.7808 0.1146  0.0206  0.0342  84  GLN B N   
2000 C  CA  . GLN B 87  ? 0.5138 0.5763 0.7793 0.1063  0.0117  0.0231  84  GLN B CA  
2001 C  C   . GLN B 87  ? 0.4356 0.5000 0.7690 0.0862  0.0127  0.0149  84  GLN B C   
2002 O  O   . GLN B 87  ? 0.4049 0.5073 0.7814 0.0888  0.0248  0.0203  84  GLN B O   
2003 C  CB  . GLN B 87  ? 0.5248 0.5974 0.7960 0.1060  0.0036  0.0142  84  GLN B CB  
2004 C  CG  . GLN B 87  ? 0.5641 0.6274 0.8036 0.1100  -0.0030 0.0171  84  GLN B CG  
2005 C  CD  . GLN B 87  ? 0.5806 0.6475 0.8177 0.1039  -0.0125 0.0216  84  GLN B CD  
2006 O  OE1 . GLN B 87  ? 0.6048 0.6699 0.8122 0.1039  -0.0067 0.0206  84  GLN B OE1 
2007 N  NE2 . GLN B 87  ? 0.6088 0.6600 0.8227 0.0991  -0.0237 0.0267  84  GLN B NE2 
2008 N  N   . GLY B 88  ? 0.3825 0.4358 0.7470 0.0728  0.0115  0.0321  85  GLY B N   
2009 C  CA  . GLY B 88  ? 0.3347 0.4126 0.7392 0.0490  0.0100  0.0217  85  GLY B CA  
2010 C  C   . GLY B 88  ? 0.3290 0.3975 0.7263 0.0353  -0.0035 0.0233  85  GLY B C   
2011 O  O   . GLY B 88  ? 0.3030 0.3739 0.7088 0.0098  -0.0051 0.0246  85  GLY B O   
2012 N  N   . TYR B 89  ? 0.3222 0.3831 0.7264 0.0238  -0.0144 0.0192  86  TYR B N   
2013 C  CA  . TYR B 89  ? 0.3127 0.3735 0.7337 0.0187  -0.0185 0.0170  86  TYR B CA  
2014 C  C   . TYR B 89  ? 0.2860 0.3670 0.7217 0.0300  -0.0010 0.0161  86  TYR B C   
2015 O  O   . TYR B 89  ? 0.2089 0.3694 0.6917 0.0419  -0.0024 0.0136  86  TYR B O   
2016 C  CB  . TYR B 89  ? 0.3279 0.3605 0.7580 0.0210  -0.0361 0.0167  86  TYR B CB  
2017 C  CG  . TYR B 89  ? 0.3522 0.3404 0.7790 0.0217  -0.0555 0.0221  86  TYR B CG  
2018 C  CD1 . TYR B 89  ? 0.3715 0.3406 0.7863 0.0190  -0.0637 0.0206  86  TYR B CD1 
2019 C  CD2 . TYR B 89  ? 0.3795 0.3345 0.7910 0.0308  -0.0749 0.0240  86  TYR B CD2 
2020 C  CE1 . TYR B 89  ? 0.3957 0.3010 0.8008 0.0040  -0.0756 0.0362  86  TYR B CE1 
2021 C  CE2 . TYR B 89  ? 0.4058 0.3081 0.8074 0.0249  -0.0774 0.0329  86  TYR B CE2 
2022 C  CZ  . TYR B 89  ? 0.4307 0.3080 0.8144 0.0120  -0.0847 0.0327  86  TYR B CZ  
2023 O  OH  . TYR B 89  ? 0.4863 0.2892 0.8434 0.0188  -0.1007 0.0370  86  TYR B OH  
2024 N  N   . GLY B 90  ? 0.2862 0.3690 0.7294 0.0316  0.0053  0.0113  87  GLY B N   
2025 C  CA  . GLY B 90  ? 0.2835 0.3525 0.7390 0.0335  0.0076  0.0141  87  GLY B CA  
2026 C  C   . GLY B 90  ? 0.2586 0.3482 0.7468 0.0331  0.0122  0.0099  87  GLY B C   
2027 O  O   . GLY B 90  ? 0.2141 0.3461 0.7474 0.0426  0.0145  0.0112  87  GLY B O   
2028 N  N   . LYS B 91  ? 0.2722 0.3594 0.7593 0.0316  0.0165  0.0077  88  LYS B N   
2029 C  CA  . LYS B 91  ? 0.2603 0.3464 0.7642 0.0193  0.0142  0.0042  88  LYS B CA  
2030 C  C   . LYS B 91  ? 0.2250 0.2999 0.7568 0.0106  0.0105  -0.0123 88  LYS B C   
2031 O  O   . LYS B 91  ? 0.2243 0.2874 0.7660 0.0079  0.0031  -0.0011 88  LYS B O   
2032 C  CB  . LYS B 91  ? 0.3016 0.3758 0.7747 0.0048  0.0302  0.0020  88  LYS B CB  
2033 C  CG  . LYS B 91  ? 0.3331 0.3944 0.7865 0.0034  0.0161  0.0098  88  LYS B CG  
2034 C  CD  . LYS B 91  ? 0.3652 0.4358 0.8000 -0.0067 0.0320  0.0100  88  LYS B CD  
2035 C  CE  . LYS B 91  ? 0.3895 0.4633 0.8129 -0.0280 0.0320  0.0108  88  LYS B CE  
2036 N  NZ  . LYS B 91  ? 0.3930 0.4964 0.8214 -0.0300 0.0366  0.0149  88  LYS B NZ  
2037 N  N   . ALA B 92  ? 0.2282 0.3060 0.7464 0.0183  -0.0086 -0.0015 89  ALA B N   
2038 C  CA  . ALA B 92  ? 0.2364 0.2813 0.7339 0.0106  -0.0073 -0.0031 89  ALA B CA  
2039 C  C   . ALA B 92  ? 0.2176 0.2361 0.7122 0.0099  -0.0150 0.0105  89  ALA B C   
2040 O  O   . ALA B 92  ? 0.2184 0.2371 0.7230 0.0211  -0.0112 0.0157  89  ALA B O   
2041 C  CB  . ALA B 92  ? 0.2652 0.2880 0.7395 0.0204  -0.0075 -0.0054 89  ALA B CB  
2042 N  N   . ALA B 93  ? 0.2086 0.2049 0.6829 -0.0089 -0.0152 0.0225  90  ALA B N   
2043 C  CA  . ALA B 93  ? 0.2113 0.1881 0.6688 -0.0135 -0.0141 0.0328  90  ALA B CA  
2044 C  C   . ALA B 93  ? 0.2158 0.1882 0.6603 -0.0108 -0.0118 0.0266  90  ALA B C   
2045 O  O   . ALA B 93  ? 0.2524 0.1951 0.6557 -0.0326 -0.0103 0.0247  90  ALA B O   
2046 C  CB  . ALA B 93  ? 0.2116 0.1856 0.6715 -0.0323 -0.0204 0.0317  90  ALA B CB  
2047 N  N   . CYS B 94  ? 0.2292 0.1730 0.6564 0.0199  -0.0120 0.0240  91  CYS B N   
2048 C  CA  . CYS B 94  ? 0.2404 0.1597 0.6680 0.0144  -0.0164 0.0310  91  CYS B CA  
2049 C  C   . CYS B 94  ? 0.2260 0.1608 0.6710 0.0262  -0.0095 0.0292  91  CYS B C   
2050 O  O   . CYS B 94  ? 0.2116 0.1626 0.6672 0.0548  -0.0023 0.0189  91  CYS B O   
2051 C  CB  . CYS B 94  ? 0.2584 0.1617 0.6712 0.0195  -0.0227 0.0293  91  CYS B CB  
2052 S  SG  . CYS B 94  ? 0.3079 0.1651 0.6827 0.0316  -0.0530 0.0223  91  CYS B SG  
2053 N  N   . ARG B 95  ? 0.2309 0.1808 0.6869 0.0304  -0.0127 0.0306  92  ARG B N   
2054 C  CA  . ARG B 95  ? 0.2371 0.2154 0.7003 0.0300  -0.0220 0.0227  92  ARG B CA  
2055 C  C   . ARG B 95  ? 0.2298 0.1858 0.7050 0.0360  -0.0377 0.0249  92  ARG B C   
2056 O  O   . ARG B 95  ? 0.2278 0.1792 0.7140 0.0291  -0.0411 0.0116  92  ARG B O   
2057 C  CB  . ARG B 95  ? 0.2708 0.2676 0.7183 0.0449  -0.0087 0.0127  92  ARG B CB  
2058 C  CG  . ARG B 95  ? 0.2860 0.3215 0.7346 0.0585  -0.0118 0.0043  92  ARG B CG  
2059 C  CD  . ARG B 95  ? 0.3108 0.3549 0.7494 0.0691  -0.0028 -0.0026 92  ARG B CD  
2060 N  NE  . ARG B 95  ? 0.3378 0.4001 0.7630 0.0571  0.0006  -0.0120 92  ARG B NE  
2061 C  CZ  . ARG B 95  ? 0.3728 0.4356 0.7705 0.0526  0.0033  -0.0212 92  ARG B CZ  
2062 N  NH1 . ARG B 95  ? 0.3578 0.4788 0.7795 0.0644  0.0060  -0.0150 92  ARG B NH1 
2063 N  NH2 . ARG B 95  ? 0.3768 0.4692 0.7759 0.0535  -0.0056 -0.0281 92  ARG B NH2 
2064 N  N   . LEU B 96  ? 0.2334 0.1740 0.7137 0.0251  -0.0305 0.0344  93  LEU B N   
2065 C  CA  . LEU B 96  ? 0.2467 0.1886 0.7219 0.0077  -0.0287 0.0321  93  LEU B CA  
2066 C  C   . LEU B 96  ? 0.2146 0.1630 0.7314 0.0101  -0.0142 0.0366  93  LEU B C   
2067 O  O   . LEU B 96  ? 0.1820 0.1279 0.7427 0.0250  0.0014  0.0308  93  LEU B O   
2068 C  CB  . LEU B 96  ? 0.2648 0.2276 0.7332 0.0021  -0.0510 0.0250  93  LEU B CB  
2069 C  CG  . LEU B 96  ? 0.2978 0.2549 0.7508 0.0002  -0.0598 0.0160  93  LEU B CG  
2070 C  CD1 . LEU B 96  ? 0.3352 0.2649 0.7563 0.0023  -0.0669 0.0026  93  LEU B CD1 
2071 C  CD2 . LEU B 96  ? 0.3153 0.2608 0.7524 -0.0044 -0.0657 0.0198  93  LEU B CD2 
2072 N  N   . LEU B 97  ? 0.2070 0.1426 0.7250 -0.0031 0.0006  0.0369  94  LEU B N   
2073 C  CA  . LEU B 97  ? 0.2385 0.1903 0.7122 -0.0246 0.0093  0.0260  94  LEU B CA  
2074 C  C   . LEU B 97  ? 0.2406 0.2295 0.6907 -0.0252 0.0174  0.0280  94  LEU B C   
2075 O  O   . LEU B 97  ? 0.2849 0.2362 0.6876 -0.0265 0.0237  0.0217  94  LEU B O   
2076 C  CB  . LEU B 97  ? 0.2369 0.1917 0.7298 -0.0191 0.0068  0.0143  94  LEU B CB  
2077 C  CG  . LEU B 97  ? 0.2337 0.2086 0.7408 0.0058  0.0049  0.0162  94  LEU B CG  
2078 C  CD1 . LEU B 97  ? 0.2122 0.2134 0.7379 0.0127  0.0012  0.0110  94  LEU B CD1 
2079 C  CD2 . LEU B 97  ? 0.2354 0.2296 0.7533 0.0271  0.0078  0.0154  94  LEU B CD2 
2080 N  N   A MET B 98  ? 0.2439 0.1885 0.6833 -0.0329 0.0082  0.0181  95  MET B N   
2081 N  N   B MET B 98  ? 0.2456 0.2251 0.6973 -0.0225 0.0186  0.0207  95  MET B N   
2082 C  CA  A MET B 98  ? 0.2236 0.1793 0.6805 -0.0386 0.0185  0.0171  95  MET B CA  
2083 C  CA  B MET B 98  ? 0.2508 0.2313 0.6994 -0.0110 0.0154  0.0121  95  MET B CA  
2084 C  C   A MET B 98  ? 0.2225 0.1883 0.6845 -0.0167 0.0132  0.0088  95  MET B C   
2085 C  C   B MET B 98  ? 0.2411 0.2178 0.7013 -0.0019 0.0187  0.0065  95  MET B C   
2086 O  O   A MET B 98  ? 0.2292 0.1588 0.6783 0.0000  0.0179  -0.0044 95  MET B O   
2087 O  O   B MET B 98  ? 0.2454 0.2163 0.7040 0.0006  0.0181  0.0049  95  MET B O   
2088 C  CB  A MET B 98  ? 0.2339 0.1770 0.6753 -0.0519 0.0155  0.0203  95  MET B CB  
2089 C  CB  B MET B 98  ? 0.2609 0.2513 0.7007 -0.0129 0.0178  0.0103  95  MET B CB  
2090 C  CG  A MET B 98  ? 0.2424 0.1566 0.6708 -0.0573 0.0108  0.0099  95  MET B CG  
2091 C  CG  B MET B 98  ? 0.2800 0.2577 0.7036 -0.0032 0.0114  0.0057  95  MET B CG  
2092 S  SD  A MET B 98  ? 0.2492 0.1798 0.6575 -0.0553 0.0055  0.0060  95  MET B SD  
2093 S  SD  B MET B 98  ? 0.2885 0.2806 0.7037 -0.0023 0.0142  -0.0021 95  MET B SD  
2094 C  CE  A MET B 98  ? 0.2420 0.2019 0.6585 -0.0483 0.0094  0.0016  95  MET B CE  
2095 C  CE  B MET B 98  ? 0.2847 0.2785 0.7040 0.0011  0.0133  -0.0009 95  MET B CE  
2096 N  N   . LEU B 99  ? 0.2403 0.2165 0.6990 0.0021  0.0194  0.0091  96  LEU B N   
2097 C  CA  . LEU B 99  ? 0.2196 0.2082 0.7064 0.0304  0.0275  0.0056  96  LEU B CA  
2098 C  C   . LEU B 99  ? 0.2185 0.1946 0.7093 0.0428  0.0277  0.0161  96  LEU B C   
2099 O  O   . LEU B 99  ? 0.2061 0.2026 0.7141 0.0274  0.0158  0.0146  96  LEU B O   
2100 C  CB  . LEU B 99  ? 0.2245 0.2328 0.7089 0.0439  0.0299  -0.0018 96  LEU B CB  
2101 C  CG  . LEU B 99  ? 0.2247 0.2636 0.7149 0.0414  0.0343  -0.0034 96  LEU B CG  
2102 C  CD1 . LEU B 99  ? 0.2230 0.2781 0.7203 0.0559  0.0363  -0.0060 96  LEU B CD1 
2103 C  CD2 . LEU B 99  ? 0.2627 0.3058 0.7215 0.0304  0.0253  -0.0033 96  LEU B CD2 
2104 N  N   . LYS B 100 ? 0.2171 0.1478 0.7191 0.0681  0.0391  0.0245  97  LYS B N   
2105 C  CA  . LYS B 100 ? 0.2539 0.1735 0.7251 0.0505  0.0408  0.0348  97  LYS B CA  
2106 C  C   . LYS B 100 ? 0.2489 0.1871 0.7310 0.0504  0.0471  0.0418  97  LYS B C   
2107 O  O   . LYS B 100 ? 0.2959 0.1861 0.7308 0.0545  0.0360  0.0491  97  LYS B O   
2108 C  CB  . LYS B 100 ? 0.2623 0.2242 0.7199 0.0443  0.0409  0.0266  97  LYS B CB  
2109 C  CG  . LYS B 100 ? 0.2992 0.2847 0.7127 0.0270  0.0349  0.0150  97  LYS B CG  
2110 C  CD  . LYS B 100 ? 0.3067 0.3390 0.7165 0.0156  0.0336  0.0072  97  LYS B CD  
2111 C  CE  . LYS B 100 ? 0.3053 0.3663 0.7163 0.0225  0.0374  0.0016  97  LYS B CE  
2112 N  NZ  . LYS B 100 ? 0.3121 0.3818 0.7130 0.0219  0.0306  0.0019  97  LYS B NZ  
2113 N  N   . LEU B 101 ? 0.2073 0.1946 0.7558 0.0456  0.0403  0.0645  98  LEU B N   
2114 C  CA  . LEU B 101 ? 0.2094 0.2143 0.7732 0.0462  0.0403  0.0626  98  LEU B CA  
2115 C  C   . LEU B 101 ? 0.2371 0.2509 0.7806 0.0601  0.0441  0.0661  98  LEU B C   
2116 O  O   . LEU B 101 ? 0.2930 0.2930 0.7866 0.0330  0.0519  0.0803  98  LEU B O   
2117 C  CB  . LEU B 101 ? 0.1626 0.2133 0.7845 0.0628  0.0280  0.0541  98  LEU B CB  
2118 C  CG  . LEU B 101 ? 0.1788 0.2417 0.7958 0.0482  0.0218  0.0408  98  LEU B CG  
2119 C  CD1 . LEU B 101 ? 0.1392 0.2376 0.7992 0.0481  0.0227  0.0343  98  LEU B CD1 
2120 C  CD2 . LEU B 101 ? 0.1956 0.2481 0.7960 0.0434  0.0283  0.0476  98  LEU B CD2 
2121 N  N   . ILE B 102 ? 0.2452 0.3030 0.8068 0.0587  0.0428  0.0675  99  ILE B N   
2122 C  CA  . ILE B 102 ? 0.2587 0.3378 0.8205 0.0533  0.0394  0.0606  99  ILE B CA  
2123 C  C   . ILE B 102 ? 0.2780 0.3767 0.8373 0.0732  0.0510  0.0781  99  ILE B C   
2124 O  O   . ILE B 102 ? 0.3378 0.4297 0.8306 0.0604  0.0722  0.0636  99  ILE B O   
2125 C  CB  . ILE B 102 ? 0.2717 0.3375 0.8111 0.0498  0.0371  0.0635  99  ILE B CB  
2126 C  CG1 . ILE B 102 ? 0.2939 0.3442 0.8113 0.0507  0.0357  0.0577  99  ILE B CG1 
2127 C  CG2 . ILE B 102 ? 0.2769 0.3405 0.8130 0.0366  0.0249  0.0620  99  ILE B CG2 
2128 C  CD1 . ILE B 102 ? 0.3060 0.3605 0.8124 0.0527  0.0372  0.0568  99  ILE B CD1 
2129 N  N   . GLU B 103 ? 0.3111 0.3687 0.8584 0.0817  0.0525  0.0747  100 GLU B N   
2130 C  CA  . GLU B 103 ? 0.3626 0.3813 0.8900 0.0824  0.0595  0.0775  100 GLU B CA  
2131 C  C   . GLU B 103 ? 0.4273 0.4115 0.9152 0.0796  0.0895  0.0855  100 GLU B C   
2132 O  O   . GLU B 103 ? 0.4603 0.4781 0.9236 0.0713  0.0817  0.0855  100 GLU B O   
2133 C  CB  . GLU B 103 ? 0.3701 0.3768 0.8966 0.1028  0.0580  0.0626  100 GLU B CB  
2134 C  CG  . GLU B 103 ? 0.3956 0.3769 0.9073 0.1054  0.0517  0.0515  100 GLU B CG  
2135 C  CD  . GLU B 103 ? 0.4324 0.3839 0.9162 0.1047  0.0435  0.0326  100 GLU B CD  
2136 O  OE1 . GLU B 103 ? 0.4400 0.3687 0.9155 0.1248  0.0391  0.0141  100 GLU B OE1 
2137 O  OE2 . GLU B 103 ? 0.4388 0.3882 0.9366 0.1049  0.0293  0.0272  100 GLU B OE2 
2138 N  N   . LYS B 104 ? 0.4378 0.3722 0.9485 0.0767  0.0943  0.0924  101 LYS B N   
2139 C  CA  . LYS B 104 ? 0.4734 0.3636 0.9593 0.0575  0.1125  0.1024  101 LYS B CA  
2140 C  C   . LYS B 104 ? 0.4934 0.3389 0.9543 0.0749  0.1244  0.1102  101 LYS B C   
2141 O  O   . LYS B 104 ? 0.5315 0.2700 0.9692 0.0748  0.1427  0.1391  101 LYS B O   
2142 C  CB  . LYS B 104 ? 0.4755 0.3986 0.9826 0.0546  0.1019  0.0870  101 LYS B CB  
2143 C  CG  . LYS B 104 ? 0.4782 0.4160 0.9976 0.0531  0.0990  0.0805  101 LYS B CG  
2144 C  CD  . LYS B 104 ? 0.4813 0.4516 1.0120 0.0534  0.0927  0.0719  101 LYS B CD  
2145 C  CE  . LYS B 104 ? 0.4883 0.4746 1.0228 0.0783  0.0887  0.0607  101 LYS B CE  
2146 N  NZ  . LYS B 104 ? 0.5102 0.5035 1.0286 0.0851  0.0786  0.0567  101 LYS B NZ  
2147 N  N   . TYR B 105 ? 0.4872 0.3348 0.9483 0.0756  0.1126  0.1141  102 TYR B N   
2148 C  CA  . TYR B 105 ? 0.4800 0.3638 0.9427 0.0675  0.0994  0.1130  102 TYR B CA  
2149 C  C   . TYR B 105 ? 0.4937 0.4191 0.9356 0.0671  0.0830  0.1133  102 TYR B C   
2150 O  O   . TYR B 105 ? 0.4881 0.4313 0.9300 0.0985  0.0702  0.1286  102 TYR B O   
2151 C  CB  . TYR B 105 ? 0.4536 0.3431 0.9538 0.0666  0.1025  0.0954  102 TYR B CB  
2152 C  CG  . TYR B 105 ? 0.4446 0.3108 0.9596 0.0578  0.1044  0.0940  102 TYR B CG  
2153 C  CD1 . TYR B 105 ? 0.4585 0.3333 0.9662 0.0552  0.1070  0.0989  102 TYR B CD1 
2154 C  CD2 . TYR B 105 ? 0.4290 0.2873 0.9662 0.0536  0.1052  0.0861  102 TYR B CD2 
2155 C  CE1 . TYR B 105 ? 0.4557 0.3399 0.9736 0.0378  0.1057  0.0921  102 TYR B CE1 
2156 C  CE2 . TYR B 105 ? 0.4458 0.2977 0.9752 0.0504  0.1000  0.0754  102 TYR B CE2 
2157 C  CZ  . TYR B 105 ? 0.4456 0.3286 0.9794 0.0393  0.1056  0.0806  102 TYR B CZ  
2158 O  OH  . TYR B 105 ? 0.4465 0.3259 1.0078 0.0534  0.1026  0.0720  102 TYR B OH  
2159 N  N   . GLN B 106 ? 0.5165 0.4917 0.9351 0.0548  0.0552  0.1143  103 GLN B N   
2160 C  CA  . GLN B 106 ? 0.5403 0.5366 0.9340 0.0554  0.0297  0.1148  103 GLN B CA  
2161 C  C   . GLN B 106 ? 0.5366 0.5363 0.9146 0.0482  0.0025  0.1232  103 GLN B C   
2162 O  O   . GLN B 106 ? 0.5489 0.5808 0.9241 0.0497  0.0115  0.1229  103 GLN B O   
2163 C  CB  . GLN B 106 ? 0.5541 0.5631 0.9390 0.0587  0.0319  0.1005  103 GLN B CB  
2164 C  CG  . GLN B 106 ? 0.5598 0.5887 0.9388 0.0546  0.0381  0.0948  103 GLN B CG  
2165 C  CD  . GLN B 106 ? 0.5643 0.6113 0.9519 0.0685  0.0356  0.0811  103 GLN B CD  
2166 O  OE1 . GLN B 106 ? 0.5810 0.6367 0.9646 0.0709  0.0357  0.0661  103 GLN B OE1 
2167 N  NE2 . GLN B 106 ? 0.5654 0.6260 0.9513 0.0694  0.0361  0.0775  103 GLN B NE2 
2168 N  N   . THR B 107 ? 0.5191 0.5119 0.9017 0.0311  -0.0202 0.1114  104 THR B N   
2169 C  CA  . THR B 107 ? 0.4763 0.4816 0.8662 0.0377  -0.0395 0.0977  104 THR B CA  
2170 C  C   . THR B 107 ? 0.4413 0.4238 0.8411 0.0433  -0.0667 0.0828  104 THR B C   
2171 O  O   . THR B 107 ? 0.4832 0.3789 0.8396 0.0613  -0.0990 0.0999  104 THR B O   
2172 C  CB  . THR B 107 ? 0.4653 0.4898 0.8639 0.0304  -0.0436 0.1069  104 THR B CB  
2173 O  OG1 . THR B 107 ? 0.4444 0.4956 0.8581 0.0066  -0.0467 0.1203  104 THR B OG1 
2174 C  CG2 . THR B 107 ? 0.4711 0.5016 0.8663 0.0193  -0.0372 0.1016  104 THR B CG2 
2175 N  N   . ASN B 108 ? 0.3994 0.4115 0.8005 0.0596  -0.0683 0.0626  105 ASN B N   
2176 C  CA  . ASN B 108 ? 0.3632 0.4131 0.7841 0.0557  -0.0707 0.0449  105 ASN B CA  
2177 C  C   . ASN B 108 ? 0.2909 0.3683 0.7578 0.0425  -0.0654 0.0217  105 ASN B C   
2178 O  O   . ASN B 108 ? 0.3117 0.3732 0.7644 0.0218  -0.0659 0.0240  105 ASN B O   
2179 C  CB  . ASN B 108 ? 0.3712 0.4546 0.7893 0.0719  -0.0668 0.0347  105 ASN B CB  
2180 C  CG  . ASN B 108 ? 0.4140 0.4680 0.7950 0.0766  -0.0600 0.0370  105 ASN B CG  
2181 O  OD1 . ASN B 108 ? 0.4350 0.5111 0.7990 0.0870  -0.0516 0.0239  105 ASN B OD1 
2182 N  ND2 . ASN B 108 ? 0.4330 0.4930 0.7962 0.0778  -0.0571 0.0281  105 ASN B ND2 
2183 N  N   . LYS B 109 ? 0.2305 0.3292 0.7167 0.0050  -0.0869 0.0198  106 LYS B N   
2184 C  CA  . LYS B 109 ? 0.2190 0.3109 0.6948 -0.0014 -0.0815 0.0108  106 LYS B CA  
2185 C  C   . LYS B 109 ? 0.2097 0.2810 0.6689 -0.0030 -0.0672 0.0152  106 LYS B C   
2186 O  O   . LYS B 109 ? 0.2460 0.3046 0.6609 0.0041  -0.0562 0.0382  106 LYS B O   
2187 C  CB  . LYS B 109 ? 0.2408 0.3138 0.7005 0.0080  -0.0875 0.0006  106 LYS B CB  
2188 C  CG  . LYS B 109 ? 0.2629 0.3219 0.7154 -0.0184 -0.0910 -0.0068 106 LYS B CG  
2189 C  CD  . LYS B 109 ? 0.2742 0.3373 0.7264 -0.0159 -0.0962 -0.0175 106 LYS B CD  
2190 C  CE  . LYS B 109 ? 0.2797 0.3573 0.7376 -0.0254 -0.0963 -0.0264 106 LYS B CE  
2191 N  NZ  . LYS B 109 ? 0.3108 0.3892 0.7477 -0.0246 -0.0950 -0.0334 106 LYS B NZ  
2192 N  N   . LEU B 110 ? 0.2085 0.2310 0.6555 -0.0077 -0.0518 0.0105  107 LEU B N   
2193 C  CA  . LEU B 110 ? 0.1953 0.2048 0.6490 -0.0135 -0.0399 0.0047  107 LEU B CA  
2194 C  C   . LEU B 110 ? 0.1600 0.1948 0.6370 -0.0215 -0.0309 0.0007  107 LEU B C   
2195 O  O   . LEU B 110 ? 0.1500 0.2007 0.6457 -0.0201 -0.0290 0.0000  107 LEU B O   
2196 C  CB  . LEU B 110 ? 0.2140 0.2008 0.6567 -0.0257 -0.0419 0.0037  107 LEU B CB  
2197 C  CG  . LEU B 110 ? 0.2098 0.2005 0.6681 -0.0174 -0.0407 0.0083  107 LEU B CG  
2198 C  CD1 . LEU B 110 ? 0.2294 0.2285 0.6707 -0.0145 -0.0420 -0.0001 107 LEU B CD1 
2199 C  CD2 . LEU B 110 ? 0.2239 0.2033 0.6694 -0.0120 -0.0383 0.0124  107 LEU B CD2 
2200 N  N   . TYR B 111 ? 0.1525 0.1851 0.6215 -0.0243 -0.0222 0.0055  108 TYR B N   
2201 C  CA  . TYR B 111 ? 0.1681 0.1863 0.6129 -0.0242 -0.0209 0.0044  108 TYR B CA  
2202 C  C   . TYR B 111 ? 0.1433 0.1654 0.6051 -0.0327 -0.0129 0.0131  108 TYR B C   
2203 O  O   . TYR B 111 ? 0.1441 0.1644 0.5832 -0.0349 -0.0148 0.0150  108 TYR B O   
2204 C  CB  . TYR B 111 ? 0.1700 0.1795 0.6176 -0.0136 -0.0228 -0.0003 108 TYR B CB  
2205 C  CG  . TYR B 111 ? 0.1952 0.2074 0.6263 -0.0131 -0.0414 -0.0067 108 TYR B CG  
2206 C  CD1 . TYR B 111 ? 0.2086 0.2351 0.6294 -0.0138 -0.0506 -0.0027 108 TYR B CD1 
2207 C  CD2 . TYR B 111 ? 0.1913 0.2262 0.6393 -0.0222 -0.0516 -0.0125 108 TYR B CD2 
2208 C  CE1 . TYR B 111 ? 0.2155 0.2580 0.6383 -0.0113 -0.0602 -0.0064 108 TYR B CE1 
2209 C  CE2 . TYR B 111 ? 0.2027 0.2521 0.6483 -0.0251 -0.0598 -0.0140 108 TYR B CE2 
2210 C  CZ  . TYR B 111 ? 0.2084 0.2713 0.6486 -0.0193 -0.0658 -0.0145 108 TYR B CZ  
2211 O  OH  . TYR B 111 ? 0.2036 0.3279 0.6732 -0.0265 -0.0713 -0.0284 108 TYR B OH  
2212 N  N   . LEU B 112 ? 0.1466 0.1656 0.6053 -0.0236 -0.0080 0.0175  109 LEU B N   
2213 C  CA  . LEU B 112 ? 0.1636 0.1439 0.6138 0.0000  -0.0082 0.0129  109 LEU B CA  
2214 C  C   . LEU B 112 ? 0.1567 0.1459 0.6240 -0.0094 -0.0044 0.0109  109 LEU B C   
2215 O  O   . LEU B 112 ? 0.1243 0.1380 0.6442 -0.0151 0.0123  0.0305  109 LEU B O   
2216 C  CB  . LEU B 112 ? 0.1945 0.1515 0.6111 0.0160  -0.0112 0.0187  109 LEU B CB  
2217 C  CG  . LEU B 112 ? 0.2056 0.1567 0.6154 0.0171  -0.0093 0.0255  109 LEU B CG  
2218 C  CD1 . LEU B 112 ? 0.2258 0.1638 0.6141 0.0258  -0.0126 0.0264  109 LEU B CD1 
2219 C  CD2 . LEU B 112 ? 0.2157 0.1706 0.6162 0.0326  -0.0145 0.0289  109 LEU B CD2 
2220 N  N   . SER B 113 ? 0.1593 0.1327 0.6336 0.0048  0.0033  0.0136  110 SER B N   
2221 C  CA  . SER B 113 ? 0.1650 0.1388 0.6320 0.0096  0.0132  0.0206  110 SER B CA  
2222 C  C   . SER B 113 ? 0.1828 0.1651 0.6322 -0.0121 0.0232  0.0287  110 SER B C   
2223 O  O   . SER B 113 ? 0.1872 0.1849 0.6377 -0.0313 0.0226  0.0395  110 SER B O   
2224 C  CB  . SER B 113 ? 0.1951 0.1321 0.6329 0.0045  0.0209  0.0091  110 SER B CB  
2225 O  OG  . SER B 113 ? 0.1794 0.1633 0.6299 0.0386  0.0191  0.0151  110 SER B OG  
2226 N  N   . VAL B 114 ? 0.1937 0.1888 0.6471 -0.0235 0.0352  0.0436  111 VAL B N   
2227 C  CA  . VAL B 114 ? 0.2006 0.2136 0.6525 -0.0249 0.0439  0.0536  111 VAL B CA  
2228 C  C   . VAL B 114 ? 0.2390 0.2273 0.6710 -0.0184 0.0468  0.0652  111 VAL B C   
2229 O  O   . VAL B 114 ? 0.2128 0.2263 0.6524 -0.0355 0.0509  0.0805  111 VAL B O   
2230 C  CB  . VAL B 114 ? 0.2076 0.2494 0.6563 -0.0105 0.0356  0.0531  111 VAL B CB  
2231 C  CG1 . VAL B 114 ? 0.2154 0.2488 0.6586 -0.0241 0.0368  0.0500  111 VAL B CG1 
2232 C  CG2 . VAL B 114 ? 0.1953 0.2660 0.6538 -0.0009 0.0305  0.0600  111 VAL B CG2 
2233 N  N   . TYR B 115 ? 0.2493 0.2546 0.6935 -0.0053 0.0484  0.0844  112 TYR B N   
2234 C  CA  . TYR B 115 ? 0.2890 0.2824 0.7225 -0.0193 0.0651  0.1103  112 TYR B CA  
2235 C  C   . TYR B 115 ? 0.3291 0.3752 0.7626 0.0022  0.0964  0.1229  112 TYR B C   
2236 O  O   . TYR B 115 ? 0.3829 0.4002 0.7820 0.0040  0.1228  0.1235  112 TYR B O   
2237 C  CB  . TYR B 115 ? 0.2855 0.2638 0.7065 -0.0126 0.0654  0.1067  112 TYR B CB  
2238 C  CG  . TYR B 115 ? 0.2740 0.2641 0.6953 -0.0192 0.0658  0.1081  112 TYR B CG  
2239 C  CD1 . TYR B 115 ? 0.2384 0.2699 0.6831 -0.0490 0.0627  0.0995  112 TYR B CD1 
2240 C  CD2 . TYR B 115 ? 0.2984 0.2733 0.6948 -0.0193 0.0734  0.0997  112 TYR B CD2 
2241 C  CE1 . TYR B 115 ? 0.2467 0.2805 0.6799 -0.0413 0.0605  0.0942  112 TYR B CE1 
2242 C  CE2 . TYR B 115 ? 0.2943 0.2830 0.6885 -0.0221 0.0683  0.1045  112 TYR B CE2 
2243 C  CZ  . TYR B 115 ? 0.2610 0.2625 0.6840 -0.0408 0.0628  0.1003  112 TYR B CZ  
2244 O  OH  . TYR B 115 ? 0.2769 0.2624 0.6814 -0.0327 0.0661  0.0853  112 TYR B OH  
2245 N  N   . ASP B 116 ? 0.3810 0.4118 0.8257 -0.0185 0.0821  0.1286  113 ASP B N   
2246 C  CA  . ASP B 116 ? 0.3952 0.4655 0.8503 -0.0070 0.1009  0.1359  113 ASP B CA  
2247 C  C   . ASP B 116 ? 0.4191 0.5437 0.8614 0.0422  0.1041  0.1331  113 ASP B C   
2248 O  O   . ASP B 116 ? 0.3999 0.5380 0.8800 0.0570  0.1054  0.1492  113 ASP B O   
2249 C  CB  . ASP B 116 ? 0.4311 0.4589 0.8803 -0.0138 0.0790  0.1265  113 ASP B CB  
2250 C  CG  . ASP B 116 ? 0.4533 0.4438 0.8962 -0.0339 0.0587  0.1305  113 ASP B CG  
2251 O  OD1 . ASP B 116 ? 0.4372 0.4097 0.9149 -0.0510 0.0498  0.1233  113 ASP B OD1 
2252 O  OD2 . ASP B 116 ? 0.4531 0.4188 0.9378 -0.0096 0.0454  0.1349  113 ASP B OD2 
2253 N  N   . THR B 117 ? 0.4506 0.6199 0.8688 0.0929  0.0994  0.1391  114 THR B N   
2254 C  CA  . THR B 117 ? 0.4873 0.6828 0.8677 0.1285  0.0973  0.1470  114 THR B CA  
2255 C  C   . THR B 117 ? 0.5088 0.7062 0.8669 0.1575  0.1016  0.1333  114 THR B C   
2256 O  O   . THR B 117 ? 0.5209 0.7539 0.8531 0.1728  0.1138  0.1382  114 THR B O   
2257 C  CB  . THR B 117 ? 0.5019 0.7014 0.8744 0.1407  0.0962  0.1516  114 THR B CB  
2258 O  OG1 . THR B 117 ? 0.4969 0.7173 0.8791 0.1354  0.0801  0.1557  114 THR B OG1 
2259 C  CG2 . THR B 117 ? 0.4921 0.6909 0.8764 0.1580  0.0948  0.1594  114 THR B CG2 
2260 N  N   . ASN B 118 ? 0.4973 0.7224 0.8589 0.1741  0.1076  0.1398  115 ASN B N   
2261 C  CA  . ASN B 118 ? 0.4687 0.7269 0.8544 0.1990  0.1105  0.1326  115 ASN B CA  
2262 C  C   . ASN B 118 ? 0.4651 0.7402 0.8532 0.2103  0.1005  0.1359  115 ASN B C   
2263 O  O   . ASN B 118 ? 0.4326 0.7427 0.8490 0.2134  0.1083  0.1343  115 ASN B O   
2264 C  CB  . ASN B 118 ? 0.4805 0.7383 0.8518 0.1995  0.1164  0.1296  115 ASN B CB  
2265 C  CG  . ASN B 118 ? 0.4908 0.7543 0.8544 0.1983  0.1191  0.1262  115 ASN B CG  
2266 O  OD1 . ASN B 118 ? 0.5152 0.7886 0.8597 0.2091  0.1206  0.1237  115 ASN B OD1 
2267 N  ND2 . ASN B 118 ? 0.4926 0.7515 0.8494 0.2017  0.1198  0.1249  115 ASN B ND2 
2268 N  N   . SER B 119 ? 0.4448 0.7304 0.8532 0.2207  0.0918  0.1372  116 SER B N   
2269 C  CA  . SER B 119 ? 0.4556 0.6966 0.8511 0.2182  0.0971  0.1350  116 SER B CA  
2270 C  C   . SER B 119 ? 0.4185 0.6864 0.8437 0.2226  0.0880  0.1354  116 SER B C   
2271 O  O   . SER B 119 ? 0.4179 0.6452 0.8458 0.2500  0.1079  0.1234  116 SER B O   
2272 C  CB  . SER B 119 ? 0.4773 0.7050 0.8557 0.2116  0.0941  0.1421  116 SER B CB  
2273 O  OG  . SER B 119 ? 0.4793 0.7057 0.8562 0.2189  0.0902  0.1474  116 SER B OG  
2274 N  N   . SER B 120 ? 0.4250 0.6462 0.8423 0.2202  0.0963  0.1341  117 SER B N   
2275 C  CA  . SER B 120 ? 0.4133 0.6456 0.8314 0.2054  0.1021  0.1332  117 SER B CA  
2276 C  C   . SER B 120 ? 0.3871 0.6402 0.8201 0.1900  0.1104  0.1315  117 SER B C   
2277 O  O   . SER B 120 ? 0.3789 0.6424 0.8166 0.1933  0.1210  0.1211  117 SER B O   
2278 C  CB  . SER B 120 ? 0.4091 0.6384 0.8332 0.2063  0.1092  0.1278  117 SER B CB  
2279 O  OG  . SER B 120 ? 0.4056 0.6372 0.8303 0.2135  0.1053  0.1308  117 SER B OG  
2280 N  N   . ALA B 121 ? 0.3459 0.6366 0.8065 0.1710  0.1086  0.1389  118 ALA B N   
2281 C  CA  . ALA B 121 ? 0.3191 0.6218 0.7966 0.1501  0.1059  0.1391  118 ALA B CA  
2282 C  C   . ALA B 121 ? 0.3038 0.6042 0.7940 0.1339  0.1105  0.1423  118 ALA B C   
2283 O  O   . ALA B 121 ? 0.2613 0.5922 0.8006 0.1337  0.1149  0.1418  118 ALA B O   
2284 C  CB  . ALA B 121 ? 0.3204 0.6202 0.7970 0.1513  0.1084  0.1406  118 ALA B CB  
2285 N  N   . ILE B 122 ? 0.2972 0.6095 0.7865 0.1134  0.1065  0.1383  119 ILE B N   
2286 C  CA  . ILE B 122 ? 0.3253 0.5779 0.7920 0.1137  0.0906  0.1407  119 ILE B CA  
2287 C  C   . ILE B 122 ? 0.3419 0.5780 0.7857 0.1216  0.0961  0.1367  119 ILE B C   
2288 O  O   . ILE B 122 ? 0.2880 0.5666 0.7943 0.1269  0.1082  0.1159  119 ILE B O   
2289 C  CB  . ILE B 122 ? 0.3122 0.5677 0.7967 0.1019  0.0776  0.1494  119 ILE B CB  
2290 C  CG1 . ILE B 122 ? 0.3179 0.5529 0.7943 0.1001  0.0792  0.1540  119 ILE B CG1 
2291 C  CG2 . ILE B 122 ? 0.3058 0.5576 0.8057 0.1116  0.0785  0.1544  119 ILE B CG2 
2292 C  CD1 . ILE B 122 ? 0.3107 0.5474 0.7941 0.0977  0.0799  0.1582  119 ILE B CD1 
2293 N  N   . ARG B 123 ? 0.3925 0.5656 0.7940 0.1486  0.1049  0.1213  120 ARG B N   
2294 C  CA  . ARG B 123 ? 0.4129 0.5550 0.7928 0.1531  0.1142  0.1214  120 ARG B CA  
2295 C  C   . ARG B 123 ? 0.4196 0.5396 0.7927 0.1413  0.1246  0.1089  120 ARG B C   
2296 O  O   . ARG B 123 ? 0.4202 0.5390 0.7931 0.1318  0.1271  0.1153  120 ARG B O   
2297 C  CB  . ARG B 123 ? 0.4363 0.5679 0.7992 0.1869  0.1084  0.1156  120 ARG B CB  
2298 C  CG  . ARG B 123 ? 0.4657 0.5804 0.8039 0.1879  0.1012  0.1245  120 ARG B CG  
2299 C  CD  . ARG B 123 ? 0.5007 0.6106 0.8096 0.1952  0.0860  0.1290  120 ARG B CD  
2300 N  NE  . ARG B 123 ? 0.5195 0.6435 0.8251 0.1941  0.0736  0.1389  120 ARG B NE  
2301 C  CZ  . ARG B 123 ? 0.5494 0.6736 0.8320 0.2013  0.0579  0.1436  120 ARG B CZ  
2302 N  NH1 . ARG B 123 ? 0.5599 0.6842 0.8369 0.2012  0.0537  0.1423  120 ARG B NH1 
2303 N  NH2 . ARG B 123 ? 0.5665 0.6877 0.8289 0.2017  0.0438  0.1559  120 ARG B NH2 
2304 N  N   . LEU B 124 ? 0.4405 0.5020 0.7925 0.1220  0.1146  0.0982  121 LEU B N   
2305 C  CA  . LEU B 124 ? 0.4313 0.4917 0.7708 0.1109  0.1217  0.0842  121 LEU B CA  
2306 C  C   . LEU B 124 ? 0.3792 0.4169 0.7516 0.1032  0.1307  0.0791  121 LEU B C   
2307 O  O   . LEU B 124 ? 0.3686 0.3886 0.7396 0.1052  0.1490  0.0696  121 LEU B O   
2308 C  CB  . LEU B 124 ? 0.4455 0.5293 0.7836 0.1067  0.1084  0.0806  121 LEU B CB  
2309 C  CG  . LEU B 124 ? 0.4599 0.5432 0.7926 0.1033  0.0990  0.0805  121 LEU B CG  
2310 C  CD1 . LEU B 124 ? 0.4682 0.5646 0.7949 0.1021  0.0960  0.0790  121 LEU B CD1 
2311 C  CD2 . LEU B 124 ? 0.4837 0.5503 0.7921 0.0956  0.0902  0.0845  121 LEU B CD2 
2312 N  N   . TYR B 125 ? 0.3358 0.3735 0.7421 0.0784  0.1312  0.0817  122 TYR B N   
2313 C  CA  . TYR B 125 ? 0.2996 0.3354 0.7319 0.0659  0.1452  0.0803  122 TYR B CA  
2314 C  C   . TYR B 125 ? 0.2980 0.3283 0.7365 0.0553  0.1547  0.0810  122 TYR B C   
2315 O  O   . TYR B 125 ? 0.2859 0.3133 0.7516 0.0571  0.1542  0.0906  122 TYR B O   
2316 C  CB  . TYR B 125 ? 0.2805 0.3083 0.7270 0.0601  0.1362  0.0818  122 TYR B CB  
2317 C  CG  . TYR B 125 ? 0.2784 0.2759 0.7191 0.0659  0.1349  0.0779  122 TYR B CG  
2318 C  CD1 . TYR B 125 ? 0.2817 0.2600 0.7179 0.0810  0.1318  0.0787  122 TYR B CD1 
2319 C  CD2 . TYR B 125 ? 0.2672 0.2723 0.7136 0.0650  0.1315  0.0809  122 TYR B CD2 
2320 C  CE1 . TYR B 125 ? 0.2893 0.2420 0.7206 0.0677  0.1298  0.0779  122 TYR B CE1 
2321 C  CE2 . TYR B 125 ? 0.2666 0.2351 0.7162 0.0620  0.1370  0.0807  122 TYR B CE2 
2322 C  CZ  . TYR B 125 ? 0.2938 0.2372 0.7229 0.0664  0.1284  0.0755  122 TYR B CZ  
2323 O  OH  . TYR B 125 ? 0.3083 0.2471 0.7354 0.0583  0.1228  0.0709  122 TYR B OH  
2324 N  N   . GLN B 126 ? 0.3004 0.3079 0.7393 0.0554  0.1711  0.0674  123 GLN B N   
2325 C  CA  . GLN B 126 ? 0.3103 0.3042 0.7508 0.0565  0.1600  0.0569  123 GLN B CA  
2326 C  C   . GLN B 126 ? 0.3149 0.2846 0.7541 0.0452  0.1596  0.0531  123 GLN B C   
2327 O  O   . GLN B 126 ? 0.3592 0.2523 0.7550 0.0086  0.1394  0.0563  123 GLN B O   
2328 C  CB  . GLN B 126 ? 0.3145 0.3381 0.7464 0.0519  0.1721  0.0617  123 GLN B CB  
2329 C  CG  . GLN B 126 ? 0.3215 0.3496 0.7410 0.0558  0.1800  0.0500  123 GLN B CG  
2330 C  CD  . GLN B 126 ? 0.3401 0.3622 0.7328 0.0555  0.1864  0.0465  123 GLN B CD  
2331 O  OE1 . GLN B 126 ? 0.3612 0.3928 0.7189 0.0392  0.1880  0.0549  123 GLN B OE1 
2332 N  NE2 . GLN B 126 ? 0.3670 0.3596 0.7444 0.0705  0.1932  0.0462  123 GLN B NE2 
2333 N  N   . GLN B 127 ? 0.3208 0.2898 0.7579 0.0502  0.1480  0.0442  124 GLN B N   
2334 C  CA  . GLN B 127 ? 0.3371 0.3117 0.7716 0.0550  0.1417  0.0240  124 GLN B CA  
2335 C  C   . GLN B 127 ? 0.3405 0.2913 0.7691 0.0458  0.1186  0.0130  124 GLN B C   
2336 O  O   . GLN B 127 ? 0.3691 0.2711 0.7849 0.0441  0.1206  0.0216  124 GLN B O   
2337 C  CB  . GLN B 127 ? 0.3369 0.3414 0.7828 0.0629  0.1437  0.0187  124 GLN B CB  
2338 C  CG  . GLN B 127 ? 0.3585 0.3981 0.7962 0.0584  0.1458  0.0242  124 GLN B CG  
2339 C  CD  . GLN B 127 ? 0.3976 0.4367 0.8106 0.0300  0.1465  0.0264  124 GLN B CD  
2340 O  OE1 . GLN B 127 ? 0.4285 0.4644 0.8424 0.0045  0.1478  0.0219  124 GLN B OE1 
2341 N  NE2 . GLN B 127 ? 0.3931 0.4415 0.8107 0.0224  0.1611  0.0363  124 GLN B NE2 
2342 N  N   . LEU B 128 ? 0.3296 0.2922 0.7588 0.0205  0.0972  0.0047  125 LEU B N   
2343 C  CA  . LEU B 128 ? 0.3154 0.2803 0.7481 -0.0003 0.0731  -0.0099 125 LEU B CA  
2344 C  C   . LEU B 128 ? 0.2961 0.2306 0.7414 -0.0112 0.0622  -0.0039 125 LEU B C   
2345 O  O   . LEU B 128 ? 0.3244 0.2491 0.7370 -0.0374 0.0598  0.0012  125 LEU B O   
2346 C  CB  . LEU B 128 ? 0.3162 0.3106 0.7476 -0.0116 0.0699  -0.0189 125 LEU B CB  
2347 C  CG  . LEU B 128 ? 0.3459 0.3531 0.7561 -0.0268 0.0584  -0.0276 125 LEU B CG  
2348 C  CD1 . LEU B 128 ? 0.3429 0.3654 0.7597 -0.0416 0.0579  -0.0333 125 LEU B CD1 
2349 C  CD2 . LEU B 128 ? 0.3700 0.3534 0.7556 -0.0332 0.0500  -0.0335 125 LEU B CD2 
2350 N  N   . GLY B 129 ? 0.2972 0.2256 0.7301 -0.0072 0.0566  0.0018  126 GLY B N   
2351 C  CA  . GLY B 129 ? 0.2454 0.2014 0.7268 -0.0126 0.0494  0.0062  126 GLY B CA  
2352 C  C   . GLY B 129 ? 0.2349 0.2033 0.7252 0.0033  0.0428  0.0080  126 GLY B C   
2353 O  O   . GLY B 129 ? 0.2557 0.2044 0.7197 0.0155  0.0331  -0.0008 126 GLY B O   
2354 N  N   . PHE B 130 ? 0.2350 0.1941 0.7251 -0.0126 0.0309  0.0170  127 PHE B N   
2355 C  CA  . PHE B 130 ? 0.2237 0.1954 0.7263 -0.0024 0.0325  0.0180  127 PHE B CA  
2356 C  C   . PHE B 130 ? 0.2046 0.2137 0.7376 -0.0114 0.0402  0.0183  127 PHE B C   
2357 O  O   . PHE B 130 ? 0.2730 0.2568 0.7341 -0.0053 0.0444  0.0334  127 PHE B O   
2358 C  CB  . PHE B 130 ? 0.2242 0.1966 0.7172 -0.0009 0.0360  0.0110  127 PHE B CB  
2359 C  CG  . PHE B 130 ? 0.2177 0.1655 0.7017 -0.0003 0.0316  0.0023  127 PHE B CG  
2360 C  CD1 . PHE B 130 ? 0.2141 0.1629 0.6984 0.0038  0.0280  0.0097  127 PHE B CD1 
2361 C  CD2 . PHE B 130 ? 0.2192 0.1721 0.6976 -0.0083 0.0254  0.0025  127 PHE B CD2 
2362 C  CE1 . PHE B 130 ? 0.1997 0.1729 0.6917 0.0014  0.0255  0.0049  127 PHE B CE1 
2363 C  CE2 . PHE B 130 ? 0.2067 0.1810 0.6882 -0.0088 0.0234  -0.0035 127 PHE B CE2 
2364 C  CZ  . PHE B 130 ? 0.1835 0.1803 0.6907 0.0011  0.0242  0.0024  127 PHE B CZ  
2365 N  N   . VAL B 131 ? 0.2080 0.2074 0.7517 -0.0118 0.0358  0.0163  128 VAL B N   
2366 C  CA  . VAL B 131 ? 0.2126 0.2098 0.7639 -0.0170 0.0337  0.0174  128 VAL B CA  
2367 C  C   . VAL B 131 ? 0.1890 0.1881 0.7749 -0.0231 0.0417  0.0288  128 VAL B C   
2368 O  O   . VAL B 131 ? 0.1894 0.2074 0.7802 -0.0278 0.0321  0.0110  128 VAL B O   
2369 C  CB  . VAL B 131 ? 0.2062 0.2026 0.7667 -0.0199 0.0319  0.0209  128 VAL B CB  
2370 C  CG1 . VAL B 131 ? 0.2122 0.2008 0.7723 -0.0155 0.0285  0.0190  128 VAL B CG1 
2371 C  CG2 . VAL B 131 ? 0.2129 0.2251 0.7683 -0.0298 0.0255  0.0165  128 VAL B CG2 
2372 N  N   . PHE B 132 ? 0.2096 0.2059 0.7831 -0.0108 0.0426  0.0359  129 PHE B N   
2373 C  CA  . PHE B 132 ? 0.1886 0.1756 0.7881 -0.0156 0.0318  0.0492  129 PHE B CA  
2374 C  C   . PHE B 132 ? 0.1633 0.1813 0.8069 -0.0269 0.0222  0.0443  129 PHE B C   
2375 O  O   . PHE B 132 ? 0.1613 0.2477 0.8311 -0.0480 0.0119  0.0361  129 PHE B O   
2376 C  CB  . PHE B 132 ? 0.2238 0.1903 0.7844 -0.0071 0.0409  0.0504  129 PHE B CB  
2377 C  CG  . PHE B 132 ? 0.3215 0.1789 0.7693 -0.0030 0.0450  0.0455  129 PHE B CG  
2378 C  CD1 . PHE B 132 ? 0.3228 0.1261 0.7666 -0.0123 0.0518  0.0473  129 PHE B CD1 
2379 C  CD2 . PHE B 132 ? 0.3338 0.1859 0.7708 -0.0046 0.0612  0.0490  129 PHE B CD2 
2380 C  CE1 . PHE B 132 ? 0.3656 0.1496 0.7608 -0.0028 0.0533  0.0539  129 PHE B CE1 
2381 C  CE2 . PHE B 132 ? 0.3629 0.1781 0.7663 0.0003  0.0537  0.0521  129 PHE B CE2 
2382 C  CZ  . PHE B 132 ? 0.3616 0.1451 0.7626 0.0107  0.0598  0.0550  129 PHE B CZ  
2383 N  N   . ASN B 133 ? 0.1628 0.1680 0.8086 -0.0445 0.0087  0.0472  130 ASN B N   
2384 C  CA  . ASN B 133 ? 0.1834 0.2005 0.8087 -0.0379 -0.0212 0.0431  130 ASN B CA  
2385 C  C   . ASN B 133 ? 0.2030 0.1977 0.7951 -0.0456 -0.0230 0.0411  130 ASN B C   
2386 O  O   . ASN B 133 ? 0.2265 0.2094 0.8109 -0.0523 -0.0192 0.0326  130 ASN B O   
2387 C  CB  . ASN B 133 ? 0.2036 0.2428 0.8082 -0.0330 -0.0248 0.0482  130 ASN B CB  
2388 C  CG  . ASN B 133 ? 0.1992 0.2611 0.8086 -0.0448 -0.0310 0.0609  130 ASN B CG  
2389 O  OD1 . ASN B 133 ? 0.2105 0.2280 0.8214 -0.0210 -0.0193 0.0560  130 ASN B OD1 
2390 N  ND2 . ASN B 133 ? 0.2347 0.2858 0.8076 -0.0444 -0.0306 0.0715  130 ASN B ND2 
2391 N  N   . GLY B 134 ? 0.1911 0.1969 0.7695 -0.0417 -0.0192 0.0377  131 GLY B N   
2392 C  CA  . GLY B 134 ? 0.1931 0.1934 0.7445 -0.0437 -0.0155 0.0445  131 GLY B CA  
2393 C  C   . GLY B 134 ? 0.2203 0.1904 0.7218 -0.0380 -0.0138 0.0400  131 GLY B C   
2394 O  O   . GLY B 134 ? 0.2335 0.1868 0.7152 -0.0514 -0.0082 0.0404  131 GLY B O   
2395 N  N   . GLU B 135 ? 0.2053 0.1838 0.6830 -0.0361 -0.0241 0.0297  132 GLU B N   
2396 C  CA  . GLU B 135 ? 0.2192 0.1759 0.6559 -0.0341 -0.0228 0.0270  132 GLU B CA  
2397 C  C   . GLU B 135 ? 0.2167 0.1560 0.6276 -0.0309 -0.0135 0.0191  132 GLU B C   
2398 O  O   . GLU B 135 ? 0.1918 0.1294 0.6087 -0.0183 -0.0011 0.0247  132 GLU B O   
2399 C  CB  . GLU B 135 ? 0.2309 0.1918 0.6594 -0.0275 -0.0331 0.0373  132 GLU B CB  
2400 C  CG  . GLU B 135 ? 0.2667 0.2411 0.6630 -0.0219 -0.0422 0.0307  132 GLU B CG  
2401 C  CD  . GLU B 135 ? 0.2878 0.2536 0.6673 -0.0178 -0.0371 0.0322  132 GLU B CD  
2402 O  OE1 . GLU B 135 ? 0.3221 0.2910 0.6747 -0.0358 -0.0318 0.0166  132 GLU B OE1 
2403 O  OE2 . GLU B 135 ? 0.3262 0.2966 0.6628 0.0104  -0.0344 0.0338  132 GLU B OE2 
2404 N  N   . LEU B 136 ? 0.2097 0.1601 0.6119 -0.0405 -0.0176 0.0081  133 LEU B N   
2405 C  CA  . LEU B 136 ? 0.2158 0.1500 0.6015 -0.0458 -0.0195 0.0017  133 LEU B CA  
2406 C  C   . LEU B 136 ? 0.2013 0.2018 0.6055 -0.0498 -0.0092 -0.0125 133 LEU B C   
2407 O  O   . LEU B 136 ? 0.2082 0.2539 0.6028 -0.0532 -0.0129 -0.0318 133 LEU B O   
2408 C  CB  . LEU B 136 ? 0.2184 0.1393 0.5925 -0.0603 -0.0258 0.0040  133 LEU B CB  
2409 C  CG  . LEU B 136 ? 0.2373 0.1402 0.5784 -0.0562 -0.0342 0.0127  133 LEU B CG  
2410 C  CD1 . LEU B 136 ? 0.2472 0.1438 0.5832 -0.0488 -0.0355 0.0126  133 LEU B CD1 
2411 C  CD2 . LEU B 136 ? 0.2530 0.1288 0.5784 -0.0558 -0.0434 0.0155  133 LEU B CD2 
2412 N  N   . ASP B 137 ? 0.1874 0.1920 0.6225 -0.0328 -0.0069 -0.0235 134 ASP B N   
2413 C  CA  . ASP B 137 ? 0.2021 0.2004 0.6405 -0.0331 0.0028  -0.0193 134 ASP B CA  
2414 C  C   . ASP B 137 ? 0.2072 0.2002 0.6476 -0.0313 0.0116  -0.0243 134 ASP B C   
2415 O  O   . ASP B 137 ? 0.2203 0.1936 0.6519 -0.0283 0.0184  -0.0231 134 ASP B O   
2416 C  CB  . ASP B 137 ? 0.1845 0.1860 0.6492 -0.0385 0.0042  -0.0118 134 ASP B CB  
2417 C  CG  . ASP B 137 ? 0.1939 0.1991 0.6471 -0.0384 -0.0014 -0.0035 134 ASP B CG  
2418 O  OD1 . ASP B 137 ? 0.2126 0.2242 0.6504 -0.0278 -0.0058 0.0080  134 ASP B OD1 
2419 O  OD2 . ASP B 137 ? 0.1963 0.1957 0.6612 -0.0328 -0.0201 -0.0123 134 ASP B OD2 
2420 N  N   . THR B 138 ? 0.2380 0.2156 0.6577 -0.0308 0.0337  -0.0243 135 THR B N   
2421 C  CA  . THR B 138 ? 0.2427 0.2313 0.6610 -0.0114 0.0366  -0.0128 135 THR B CA  
2422 C  C   . THR B 138 ? 0.2325 0.2187 0.6604 0.0081  0.0382  -0.0151 135 THR B C   
2423 O  O   . THR B 138 ? 0.2271 0.2498 0.6757 0.0242  0.0511  0.0006  135 THR B O   
2424 C  CB  . THR B 138 ? 0.2636 0.2580 0.6564 -0.0007 0.0524  -0.0144 135 THR B CB  
2425 O  OG1 . THR B 138 ? 0.2535 0.2739 0.6599 -0.0165 0.0592  -0.0069 135 THR B OG1 
2426 C  CG2 . THR B 138 ? 0.2701 0.2787 0.6547 0.0121  0.0537  -0.0114 135 THR B CG2 
2427 N  N   . ASN B 139 ? 0.2146 0.1916 0.6538 0.0215  0.0323  -0.0129 136 ASN B N   
2428 C  CA  . ASN B 139 ? 0.1857 0.1786 0.6562 0.0370  0.0196  -0.0138 136 ASN B CA  
2429 C  C   . ASN B 139 ? 0.1977 0.1650 0.6485 0.0421  0.0106  -0.0060 136 ASN B C   
2430 O  O   . ASN B 139 ? 0.2111 0.2063 0.6687 0.0578  0.0005  -0.0046 136 ASN B O   
2431 C  CB  . ASN B 139 ? 0.1731 0.1641 0.6530 0.0280  0.0181  -0.0007 136 ASN B CB  
2432 C  CG  . ASN B 139 ? 0.1559 0.1623 0.6481 0.0174  0.0181  -0.0057 136 ASN B CG  
2433 O  OD1 . ASN B 139 ? 0.1484 0.1173 0.6373 0.0139  0.0248  0.0058  136 ASN B OD1 
2434 N  ND2 . ASN B 139 ? 0.1599 0.1724 0.6465 -0.0016 0.0222  -0.0065 136 ASN B ND2 
2435 N  N   . GLY B 140 ? 0.2115 0.1331 0.6420 0.0266  0.0132  -0.0034 137 GLY B N   
2436 C  CA  . GLY B 140 ? 0.2152 0.1236 0.6364 0.0184  0.0133  -0.0061 137 GLY B CA  
2437 C  C   . GLY B 140 ? 0.2231 0.1189 0.6241 0.0052  0.0124  -0.0016 137 GLY B C   
2438 O  O   . GLY B 140 ? 0.2511 0.1338 0.6452 -0.0009 0.0281  -0.0039 137 GLY B O   
2439 N  N   . GLU B 141 ? 0.2004 0.1212 0.6099 -0.0102 0.0048  0.0097  138 GLU B N   
2440 C  CA  . GLU B 141 ? 0.1918 0.1526 0.5902 -0.0127 0.0030  0.0100  138 GLU B CA  
2441 C  C   . GLU B 141 ? 0.1946 0.1795 0.5790 -0.0188 -0.0007 0.0134  138 GLU B C   
2442 O  O   . GLU B 141 ? 0.2020 0.2149 0.5765 -0.0270 -0.0039 0.0070  138 GLU B O   
2443 C  CB  . GLU B 141 ? 0.1926 0.1628 0.5866 -0.0229 -0.0004 0.0162  138 GLU B CB  
2444 C  CG  . GLU B 141 ? 0.2048 0.1676 0.5827 -0.0203 0.0019  0.0233  138 GLU B CG  
2445 C  CD  . GLU B 141 ? 0.2199 0.1652 0.5752 -0.0186 0.0078  0.0284  138 GLU B CD  
2446 O  OE1 . GLU B 141 ? 0.2410 0.1633 0.5931 0.0119  0.0129  0.0462  138 GLU B OE1 
2447 O  OE2 . GLU B 141 ? 0.2396 0.1839 0.5691 -0.0126 0.0211  0.0270  138 GLU B OE2 
2448 N  N   . ARG B 142 ? 0.1984 0.1748 0.5783 -0.0275 0.0019  0.0134  139 ARG B N   
2449 C  CA  . ARG B 142 ? 0.1923 0.1869 0.5807 -0.0320 0.0065  0.0112  139 ARG B CA  
2450 C  C   . ARG B 142 ? 0.1803 0.1810 0.5869 -0.0337 0.0012  0.0002  139 ARG B C   
2451 O  O   . ARG B 142 ? 0.1977 0.1979 0.5876 -0.0375 0.0138  -0.0136 139 ARG B O   
2452 C  CB  . ARG B 142 ? 0.2093 0.2127 0.5846 -0.0354 0.0138  0.0218  139 ARG B CB  
2453 C  CG  . ARG B 142 ? 0.2463 0.2202 0.5884 -0.0408 0.0181  0.0367  139 ARG B CG  
2454 C  CD  . ARG B 142 ? 0.2913 0.2278 0.5983 -0.0487 0.0228  0.0480  139 ARG B CD  
2455 N  NE  . ARG B 142 ? 0.3303 0.2364 0.6192 -0.0372 0.0323  0.0484  139 ARG B NE  
2456 C  CZ  . ARG B 142 ? 0.3575 0.2651 0.6252 -0.0241 0.0353  0.0526  139 ARG B CZ  
2457 N  NH1 . ARG B 142 ? 0.3734 0.3101 0.6374 -0.0089 0.0253  0.0493  139 ARG B NH1 
2458 N  NH2 . ARG B 142 ? 0.3728 0.2787 0.6370 -0.0130 0.0340  0.0557  139 ARG B NH2 
2459 N  N   . VAL B 143 ? 0.1490 0.1820 0.6016 -0.0357 -0.0114 -0.0028 140 VAL B N   
2460 C  CA  . VAL B 143 ? 0.1391 0.1675 0.6164 -0.0318 -0.0100 -0.0069 140 VAL B CA  
2461 C  C   . VAL B 143 ? 0.1651 0.1641 0.6373 -0.0143 -0.0052 -0.0060 140 VAL B C   
2462 O  O   . VAL B 143 ? 0.1615 0.2010 0.6635 -0.0099 0.0025  0.0061  140 VAL B O   
2463 C  CB  . VAL B 143 ? 0.1552 0.1858 0.6131 -0.0350 -0.0161 -0.0057 140 VAL B CB  
2464 C  CG1 . VAL B 143 ? 0.1691 0.1828 0.6142 -0.0376 -0.0164 -0.0065 140 VAL B CG1 
2465 C  CG2 . VAL B 143 ? 0.1756 0.2067 0.6134 -0.0266 -0.0155 -0.0113 140 VAL B CG2 
2466 N  N   . MET B 144 ? 0.1499 0.1479 0.6522 -0.0160 0.0040  0.0041  141 MET B N   
2467 C  CA  . MET B 144 ? 0.1497 0.1519 0.6662 -0.0160 0.0117  -0.0005 141 MET B CA  
2468 C  C   . MET B 144 ? 0.1619 0.1673 0.6824 -0.0061 0.0153  0.0013  141 MET B C   
2469 O  O   . MET B 144 ? 0.1577 0.1600 0.6822 -0.0022 0.0090  -0.0004 141 MET B O   
2470 C  CB  . MET B 144 ? 0.1439 0.1663 0.6621 0.0063  0.0245  0.0091  141 MET B CB  
2471 C  CG  . MET B 144 ? 0.1713 0.1627 0.6658 -0.0096 0.0367  0.0287  141 MET B CG  
2472 S  SD  . MET B 144 ? 0.2173 0.1796 0.6647 0.0326  0.0567  0.0539  141 MET B SD  
2473 C  CE  . MET B 144 ? 0.2142 0.1923 0.6601 0.0297  0.0713  0.0410  141 MET B CE  
2474 N  N   . GLU B 145 ? 0.1563 0.1869 0.7053 -0.0096 0.0125  0.0088  142 GLU B N   
2475 C  CA  . GLU B 145 ? 0.1735 0.2188 0.7246 0.0066  0.0034  -0.0002 142 GLU B CA  
2476 C  C   . GLU B 145 ? 0.1683 0.2032 0.7403 -0.0019 0.0002  -0.0019 142 GLU B C   
2477 O  O   . GLU B 145 ? 0.1692 0.2150 0.7417 -0.0021 -0.0095 -0.0105 142 GLU B O   
2478 C  CB  . GLU B 145 ? 0.2192 0.2371 0.7395 -0.0079 -0.0060 -0.0016 142 GLU B CB  
2479 C  CG  . GLU B 145 ? 0.2511 0.2666 0.7520 -0.0185 -0.0090 0.0104  142 GLU B CG  
2480 C  CD  . GLU B 145 ? 0.2879 0.3094 0.7723 -0.0187 -0.0315 0.0099  142 GLU B CD  
2481 O  OE1 . GLU B 145 ? 0.3381 0.3142 0.7942 -0.0287 -0.0308 0.0213  142 GLU B OE1 
2482 O  OE2 . GLU B 145 ? 0.3320 0.3430 0.7886 -0.0075 -0.0474 0.0262  142 GLU B OE2 
2483 N  N   . TRP B 146 ? 0.1426 0.1983 0.7449 -0.0047 -0.0092 -0.0028 143 TRP B N   
2484 C  CA  . TRP B 146 ? 0.1465 0.2047 0.7646 -0.0067 0.0024  0.0029  143 TRP B CA  
2485 C  C   . TRP B 146 ? 0.1856 0.2286 0.7755 -0.0113 -0.0005 0.0125  143 TRP B C   
2486 O  O   . TRP B 146 ? 0.2053 0.2288 0.7705 -0.0002 -0.0024 0.0269  143 TRP B O   
2487 C  CB  . TRP B 146 ? 0.1521 0.2162 0.7591 0.0068  0.0032  -0.0042 143 TRP B CB  
2488 C  CG  . TRP B 146 ? 0.1690 0.2238 0.7565 0.0175  0.0188  0.0074  143 TRP B CG  
2489 C  CD1 . TRP B 146 ? 0.1946 0.2258 0.7559 0.0343  0.0292  0.0169  143 TRP B CD1 
2490 C  CD2 . TRP B 146 ? 0.1705 0.2181 0.7593 0.0359  0.0212  0.0118  143 TRP B CD2 
2491 N  NE1 . TRP B 146 ? 0.2064 0.2357 0.7572 0.0557  0.0388  0.0141  143 TRP B NE1 
2492 C  CE2 . TRP B 146 ? 0.1924 0.2217 0.7587 0.0356  0.0295  0.0081  143 TRP B CE2 
2493 C  CE3 . TRP B 146 ? 0.1672 0.2214 0.7560 0.0138  0.0128  0.0064  143 TRP B CE3 
2494 C  CZ2 . TRP B 146 ? 0.2172 0.2361 0.7577 0.0305  0.0256  0.0236  143 TRP B CZ2 
2495 C  CZ3 . TRP B 146 ? 0.1675 0.2322 0.7499 0.0095  0.0139  0.0156  143 TRP B CZ3 
2496 C  CH2 . TRP B 146 ? 0.1871 0.2373 0.7546 0.0173  0.0168  0.0137  143 TRP B CH2 
2497 N  N   . THR B 147 ? 0.1994 0.2873 0.8144 -0.0090 -0.0109 0.0181  144 THR B N   
2498 C  CA  . THR B 147 ? 0.2303 0.3167 0.8305 0.0017  -0.0080 0.0228  144 THR B CA  
2499 C  C   . THR B 147 ? 0.2565 0.3162 0.8529 0.0078  -0.0047 0.0088  144 THR B C   
2500 O  O   . THR B 147 ? 0.2959 0.3328 0.8629 0.0520  0.0150  0.0006  144 THR B O   
2501 C  CB  . THR B 147 ? 0.2782 0.3529 0.8337 -0.0078 -0.0247 0.0201  144 THR B CB  
2502 O  OG1 . THR B 147 ? 0.3046 0.3638 0.8384 0.0081  -0.0291 0.0255  144 THR B OG1 
2503 C  CG2 . THR B 147 ? 0.2990 0.3572 0.8367 -0.0132 -0.0226 0.0271  144 THR B CG2 
2504 N  N   A HIS B 148 ? 0.2466 0.3230 0.8621 0.0067  -0.0033 0.0092  145 HIS B N   
2505 N  N   B HIS B 148 ? 0.2338 0.2837 0.8596 0.0203  -0.0132 -0.0028 145 HIS B N   
2506 C  CA  A HIS B 148 ? 0.2866 0.3254 0.8750 0.0126  0.0019  0.0031  145 HIS B CA  
2507 C  CA  B HIS B 148 ? 0.2691 0.2720 0.8677 0.0214  -0.0149 -0.0091 145 HIS B CA  
2508 C  C   A HIS B 148 ? 0.3054 0.3365 0.8718 0.0018  -0.0062 0.0107  145 HIS B C   
2509 C  C   B HIS B 148 ? 0.2833 0.2663 0.8657 0.0224  -0.0203 -0.0038 145 HIS B C   
2510 O  O   A HIS B 148 ? 0.3356 0.3253 0.8685 -0.0062 -0.0079 0.0219  145 HIS B O   
2511 O  O   B HIS B 148 ? 0.2808 0.2224 0.8614 0.0359  -0.0219 0.0032  145 HIS B O   
2512 C  CB  A HIS B 148 ? 0.2939 0.3262 0.8841 0.0166  0.0071  0.0034  145 HIS B CB  
2513 C  CB  B HIS B 148 ? 0.2809 0.2516 0.8736 0.0275  -0.0164 -0.0146 145 HIS B CB  
2514 C  CG  A HIS B 148 ? 0.3210 0.3369 0.9009 0.0253  0.0128  -0.0029 145 HIS B CG  
2515 C  CG  B HIS B 148 ? 0.3122 0.2514 0.8856 0.0312  -0.0177 -0.0226 145 HIS B CG  
2516 N  ND1 A HIS B 148 ? 0.3411 0.3513 0.9076 0.0264  0.0207  -0.0029 145 HIS B ND1 
2517 N  ND1 B HIS B 148 ? 0.3358 0.2505 0.8893 0.0353  -0.0135 -0.0249 145 HIS B ND1 
2518 C  CD2 A HIS B 148 ? 0.3399 0.3499 0.9058 0.0260  0.0168  0.0002  145 HIS B CD2 
2519 C  CD2 B HIS B 148 ? 0.3411 0.2591 0.8880 0.0268  -0.0223 -0.0298 145 HIS B CD2 
2520 C  CE1 A HIS B 148 ? 0.3341 0.3462 0.9114 0.0239  0.0204  -0.0054 145 HIS B CE1 
2521 C  CE1 B HIS B 148 ? 0.3504 0.2573 0.8912 0.0428  -0.0157 -0.0308 145 HIS B CE1 
2522 N  NE2 A HIS B 148 ? 0.3542 0.3611 0.9100 0.0313  0.0188  -0.0057 145 HIS B NE2 
2523 N  NE2 B HIS B 148 ? 0.3563 0.2706 0.8938 0.0411  -0.0224 -0.0303 145 HIS B NE2 
2524 C  C   . ACT C .   ? 0.3004 0.3136 0.3518 -0.0105 0.0181  -0.0062 201 ACT A C   
2525 O  O   . ACT C .   ? 0.3364 0.3307 0.3780 -0.0154 0.0228  -0.0095 201 ACT A O   
2526 O  OXT . ACT C .   ? 0.2433 0.2756 0.3402 -0.0094 0.0175  0.0051  201 ACT A OXT 
2527 C  CH3 . ACT C .   ? 0.3170 0.3116 0.3635 -0.0174 0.0080  -0.0142 201 ACT A CH3 
2528 CL CL  . CL  D .   ? 0.3551 0.5878 0.9333 -0.0982 -0.0562 -0.1024 202 CL  A CL  
2529 CL CL  . CL  E .   ? 0.2825 0.2537 0.6942 0.0309  -0.0606 0.0261  203 CL  A CL  
2530 CL CL  . CL  F .   ? 0.3298 0.2873 0.5545 0.0040  -0.0405 -0.0281 204 CL  A CL  
2531 CL CL  . CL  G .   ? 0.5487 0.4419 0.6468 -0.0234 0.0060  0.0177  205 CL  A CL  
2532 NA NA  . NA  H .   ? 0.2855 0.2325 0.6069 -0.0255 -0.0419 -0.0064 206 NA  A NA  
2533 K  K   . K   I .   ? 0.3570 0.2691 0.4908 0.0690  0.0137  0.0161  207 K   A K   
2534 CL CL  . CL  J .   ? 0.4311 0.3313 0.8615 0.0804  0.1359  0.0621  201 CL  B CL  
2535 CL CL  . CL  K .   ? 0.3085 0.3121 0.7117 0.0076  0.0896  -0.0450 202 CL  B CL  
2536 CL CL  . CL  L .   ? 0.4038 0.5005 0.6015 0.0094  -0.0434 -0.0149 203 CL  B CL  
2537 CL CL  . CL  M .   ? 0.2844 0.2638 0.3823 0.0064  0.0018  -0.0150 204 CL  B CL  
2538 CL CL  . CL  N .   ? 0.5292 0.5484 0.6086 0.0296  -0.0688 0.0545  205 CL  B CL  
2539 CL CL  . CL  O .   ? 0.2682 0.2638 0.5517 0.0171  0.0837  0.0036  206 CL  B CL  
2540 CL CL  . CL  P .   ? 0.2715 0.4217 0.5414 -0.0091 -0.0377 -0.0155 207 CL  B CL  
2541 NA NA  . NA  Q .   ? 0.1594 0.2313 0.5200 0.0237  -0.0256 0.0183  208 NA  B NA  
2542 NA NA  . NA  R .   ? 0.2215 0.2827 0.6181 -0.0223 0.0229  0.0528  209 NA  B NA  
2543 O  O   . HOH S .   ? 0.2998 0.4103 0.4377 -0.0229 -0.0201 0.0004  301 HOH A O   
2544 O  O   . HOH S .   ? 0.3271 0.2537 0.4201 0.0047  0.0213  0.0544  302 HOH A O   
2545 O  O   . HOH S .   ? 0.2579 0.5097 0.5787 0.0469  0.0004  0.0000  303 HOH A O   
2546 O  O   . HOH S .   ? 0.3292 0.3499 0.6765 -0.0177 0.0324  -0.0335 304 HOH A O   
2547 O  O   . HOH S .   ? 0.2514 0.3145 0.4755 0.0001  -0.0385 0.0316  305 HOH A O   
2548 O  O   . HOH S .   ? 0.2799 0.7444 0.6606 -0.0658 -0.0143 -0.0094 306 HOH A O   
2549 O  O   . HOH S .   ? 0.3598 0.1541 0.4504 -0.0019 -0.0034 0.0334  307 HOH A O   
2550 O  O   . HOH S .   ? 0.6054 0.1600 0.6575 -0.0476 0.0067  -0.0013 308 HOH A O   
2551 O  O   . HOH S .   ? 0.6069 0.4440 0.5288 0.0799  0.1003  0.0655  309 HOH A O   
2552 O  O   . HOH S .   ? 0.1953 0.2440 0.3594 0.0086  0.0001  -0.0105 310 HOH A O   
2553 O  O   . HOH S .   ? 0.3316 0.2313 0.4679 -0.0083 -0.0669 0.0439  311 HOH A O   
2554 O  O   . HOH S .   ? 0.2846 0.1776 0.5172 0.0518  0.0055  0.0130  312 HOH A O   
2555 O  O   . HOH S .   ? 0.5663 0.3794 0.7757 -0.1117 0.2166  -0.1048 313 HOH A O   
2556 O  O   . HOH S .   ? 0.3006 0.3232 0.3919 0.0834  -0.0200 -0.0261 314 HOH A O   
2557 O  O   . HOH S .   ? 0.4560 0.3099 0.7205 0.0853  -0.0539 0.0434  315 HOH A O   
2558 O  O   . HOH S .   ? 0.5895 0.1538 0.5036 -0.0504 -0.0502 -0.0006 316 HOH A O   
2559 O  O   . HOH S .   ? 0.4328 0.2872 0.5293 -0.0412 0.0378  0.0168  317 HOH A O   
2560 O  O   . HOH S .   ? 0.1190 0.1377 0.2234 -0.0051 0.0046  -0.0087 318 HOH A O   
2561 O  O   . HOH S .   ? 0.2619 0.2248 0.3803 -0.0286 -0.0060 0.0136  319 HOH A O   
2562 O  O   . HOH S .   ? 0.4067 0.4361 0.5467 0.0061  -0.0694 -0.0197 320 HOH A O   
2563 O  O   . HOH S .   ? 0.3772 0.3344 0.4752 0.0535  -0.0085 -0.0498 321 HOH A O   
2564 O  O   . HOH S .   ? 0.3968 0.2806 0.6314 -0.0007 0.0493  0.0150  322 HOH A O   
2565 O  O   . HOH S .   ? 0.2604 0.1378 0.5888 0.0349  0.0156  -0.0730 323 HOH A O   
2566 O  O   . HOH S .   ? 0.2706 0.5313 0.6516 0.1731  -0.0723 -0.0480 324 HOH A O   
2567 O  O   . HOH S .   ? 0.4089 0.4454 0.6036 0.0986  -0.0015 0.0257  325 HOH A O   
2568 O  O   . HOH S .   ? 0.6210 0.4483 0.5320 -0.0013 -0.1579 -0.0900 326 HOH A O   
2569 O  O   . HOH S .   ? 0.3336 0.3416 0.6520 -0.0242 -0.1056 0.2044  327 HOH A O   
2570 O  O   . HOH S .   ? 0.2937 0.4527 0.7514 -0.0330 0.0162  0.0188  328 HOH A O   
2571 O  O   . HOH S .   ? 0.3591 0.3521 0.6824 -0.1001 0.0876  0.0543  329 HOH A O   
2572 O  O   . HOH S .   ? 0.2635 0.3449 0.6430 -0.0503 -0.0735 0.0444  330 HOH A O   
2573 O  O   . HOH S .   ? 0.3049 0.1905 0.4023 -0.0095 0.0004  0.0403  331 HOH A O   
2574 O  O   . HOH S .   ? 0.3505 0.2902 0.7600 -0.0344 0.0229  -0.0348 332 HOH A O   
2575 O  O   . HOH S .   ? 0.5643 0.3704 0.6735 -0.0699 -0.0043 -0.0002 333 HOH A O   
2576 O  O   . HOH S .   ? 0.2787 0.2544 0.4489 -0.0453 0.0042  -0.0289 334 HOH A O   
2577 O  O   . HOH S .   ? 0.4182 0.0981 0.7488 -0.0131 -0.0666 0.0707  335 HOH A O   
2578 O  O   . HOH S .   ? 0.3242 0.1935 0.4539 0.0767  0.0286  -0.0389 336 HOH A O   
2579 O  O   . HOH S .   ? 0.1905 0.2101 0.3638 -0.0199 0.0131  -0.0351 337 HOH A O   
2580 O  O   . HOH S .   ? 0.1622 0.1944 0.3333 -0.0005 0.0110  0.0232  338 HOH A O   
2581 O  O   . HOH S .   ? 0.1755 0.1643 0.3393 -0.0235 -0.0149 -0.0091 339 HOH A O   
2582 O  O   . HOH S .   ? 0.3929 0.4155 0.5062 -0.0932 -0.0091 0.0055  340 HOH A O   
2583 O  O   . HOH S .   ? 0.4426 0.3825 0.5964 0.0191  0.0113  -0.0759 341 HOH A O   
2584 O  O   . HOH S .   ? 0.3006 0.2596 0.7033 -0.0282 -0.0376 -0.0768 342 HOH A O   
2585 O  O   . HOH S .   ? 0.4355 0.6166 0.5570 0.0727  0.0651  0.0417  343 HOH A O   
2586 O  O   . HOH S .   ? 0.2130 0.3216 0.5752 0.0726  -0.0298 0.0346  344 HOH A O   
2587 O  O   . HOH S .   ? 0.4926 0.3899 0.6807 0.0010  -0.1345 -0.0413 345 HOH A O   
2588 O  O   . HOH S .   ? 0.2948 0.2051 0.4836 -0.0523 -0.0745 -0.0076 346 HOH A O   
2589 O  O   . HOH S .   ? 0.2271 0.3662 0.5515 0.0902  -0.0698 -0.1056 347 HOH A O   
2590 O  O   . HOH S .   ? 0.1470 0.1738 0.2153 -0.0118 0.0013  0.0081  348 HOH A O   
2591 O  O   . HOH S .   ? 0.3327 0.2273 0.5070 -0.0214 0.0031  0.0209  349 HOH A O   
2592 O  O   . HOH S .   ? 0.3246 0.2403 0.5485 0.0969  -0.0670 -0.0044 350 HOH A O   
2593 O  O   . HOH S .   ? 0.5531 0.2426 0.6313 -0.0282 0.0230  0.0188  351 HOH A O   
2594 O  O   . HOH S .   ? 0.5719 0.6200 0.8701 0.1125  0.0733  -0.1502 352 HOH A O   
2595 O  O   . HOH S .   ? 0.2991 0.3431 0.6158 0.0484  0.0541  0.0054  353 HOH A O   
2596 O  O   . HOH S .   ? 0.4330 0.3313 0.5986 -0.0559 -0.0216 0.0278  354 HOH A O   
2597 O  O   . HOH S .   ? 0.5870 0.4119 0.4916 -0.0355 -0.0047 0.0208  355 HOH A O   
2598 O  O   . HOH S .   ? 0.5597 0.5401 0.6300 -0.0590 0.0151  -0.0979 356 HOH A O   
2599 O  O   . HOH S .   ? 0.5154 0.1505 0.6829 0.1057  0.1196  0.0371  357 HOH A O   
2600 O  O   . HOH S .   ? 0.4678 0.3448 0.8128 -0.0525 0.0513  0.0880  358 HOH A O   
2601 O  O   . HOH S .   ? 0.4775 0.5212 0.5252 0.0010  0.0919  0.0068  359 HOH A O   
2602 O  O   . HOH S .   ? 0.3615 0.4675 0.5325 0.0232  0.0774  -0.0001 360 HOH A O   
2603 O  O   . HOH S .   ? 0.1818 0.2541 0.4067 -0.0301 -0.0195 0.0370  361 HOH A O   
2604 O  O   . HOH S .   ? 0.3141 0.3033 0.5034 -0.0274 0.0423  0.0104  362 HOH A O   
2605 O  O   . HOH S .   ? 0.5294 0.3621 0.6844 -0.0997 -0.0995 0.0882  363 HOH A O   
2606 O  O   . HOH S .   ? 0.5926 0.4817 0.7711 0.0494  0.0439  -0.0171 364 HOH A O   
2607 O  O   . HOH S .   ? 0.1996 0.1804 0.3326 -0.0051 0.0068  -0.0137 365 HOH A O   
2608 O  O   . HOH S .   ? 0.4201 0.5121 0.6055 -0.0413 0.0348  -0.0109 366 HOH A O   
2609 O  O   . HOH S .   ? 0.4130 0.2841 0.5823 0.0308  0.0497  0.0037  367 HOH A O   
2610 O  O   . HOH S .   ? 0.5295 0.3962 0.6802 0.1570  -0.0806 -0.0455 368 HOH A O   
2611 O  O   . HOH S .   ? 0.2703 0.2861 0.4568 0.0322  -0.0072 0.0698  369 HOH A O   
2612 O  O   . HOH S .   ? 0.6102 0.2028 0.5956 0.0083  -0.0709 0.0790  370 HOH A O   
2613 O  O   . HOH S .   ? 0.3674 0.4539 0.5825 -0.1203 -0.0424 0.0204  371 HOH A O   
2614 O  O   . HOH S .   ? 0.2554 0.1817 0.4815 -0.0141 -0.0137 0.0556  372 HOH A O   
2615 O  O   . HOH S .   ? 0.5473 0.4948 0.7103 -0.1483 0.1770  0.2083  373 HOH A O   
2616 O  O   . HOH S .   ? 0.4908 0.3494 0.5526 -0.1117 -0.0219 0.0039  374 HOH A O   
2617 O  O   . HOH S .   ? 0.4211 0.4963 0.6263 -0.1674 -0.0588 0.0604  375 HOH A O   
2618 O  O   . HOH T .   ? 0.1947 0.2565 0.5540 0.0287  0.0052  0.0601  301 HOH B O   
2619 O  O   . HOH T .   ? 0.3756 0.2335 0.4561 0.0285  -0.0243 0.0310  302 HOH B O   
2620 O  O   . HOH T .   ? 0.2065 0.2263 0.3654 -0.0059 -0.0060 -0.0225 303 HOH B O   
2621 O  O   . HOH T .   ? 0.2220 0.3904 0.5741 0.0097  0.0495  -0.0437 304 HOH B O   
2622 O  O   . HOH T .   ? 0.3174 0.2305 0.5194 -0.0390 -0.0644 -0.0230 305 HOH B O   
2623 O  O   . HOH T .   ? 0.2103 0.1928 0.4014 -0.0023 0.0125  0.0031  306 HOH B O   
2624 O  O   . HOH T .   ? 0.4929 0.3029 0.7421 0.0165  -0.0297 0.0384  307 HOH B O   
2625 O  O   . HOH T .   ? 0.2047 0.1892 0.3555 -0.0219 -0.0140 -0.0164 308 HOH B O   
2626 O  O   . HOH T .   ? 0.5949 0.4542 0.7042 -0.0843 -0.0696 -0.2269 309 HOH B O   
2627 O  O   . HOH T .   ? 0.2221 0.2420 0.5882 0.0398  0.0734  -0.0209 310 HOH B O   
2628 O  O   . HOH T .   ? 0.3422 0.2474 0.4356 0.0518  0.0270  0.0076  311 HOH B O   
2629 O  O   . HOH T .   ? 0.2079 0.1783 0.4655 -0.0331 -0.0040 0.0427  312 HOH B O   
2630 O  O   . HOH T .   ? 0.2145 0.2203 0.4608 0.0146  -0.0200 0.0109  313 HOH B O   
2631 O  O   . HOH T .   ? 0.4423 0.3664 0.5892 -0.1117 0.1407  -0.0050 314 HOH B O   
2632 O  O   . HOH T .   ? 0.2467 0.2857 0.5249 0.0606  -0.0007 0.0209  315 HOH B O   
2633 O  O   . HOH T .   ? 0.3270 0.5207 0.6780 -0.0264 0.0631  -0.0662 316 HOH B O   
2634 O  O   . HOH T .   ? 0.3186 0.4940 0.7602 -0.0116 0.1009  -0.0347 317 HOH B O   
2635 O  O   . HOH T .   ? 0.2328 0.3097 0.4607 -0.0135 -0.1056 -0.0709 318 HOH B O   
2636 O  O   . HOH T .   ? 0.4809 0.3537 0.7053 0.0792  0.1018  0.0847  319 HOH B O   
2637 O  O   . HOH T .   ? 0.6284 0.4463 0.5677 0.0176  0.1118  -0.0625 320 HOH B O   
2638 O  O   . HOH T .   ? 0.4921 0.3191 0.5360 0.0553  0.0569  0.0028  321 HOH B O   
2639 O  O   . HOH T .   ? 0.2796 0.3827 0.7123 0.0221  -0.0474 0.1088  322 HOH B O   
2640 O  O   . HOH T .   ? 0.3791 0.4798 0.7074 -0.0654 0.0601  -0.0093 323 HOH B O   
2641 O  O   . HOH T .   ? 0.2678 0.1864 0.4327 -0.0401 -0.0249 -0.0051 324 HOH B O   
2642 O  O   . HOH T .   ? 0.1972 0.2446 0.3590 0.0160  0.0018  -0.0024 325 HOH B O   
2643 O  O   . HOH T .   ? 0.1942 0.3577 0.4677 -0.0063 0.0102  0.0026  326 HOH B O   
2644 O  O   . HOH T .   ? 0.2700 0.3101 0.6043 0.0587  -0.0393 0.0692  327 HOH B O   
2645 O  O   . HOH T .   ? 0.2545 0.4166 0.4517 -0.0642 -0.0259 0.0314  328 HOH B O   
2646 O  O   . HOH T .   ? 0.3300 0.5161 0.6464 -0.0974 0.0553  -0.0557 329 HOH B O   
2647 O  O   . HOH T .   ? 0.4292 0.2321 0.5018 -0.1015 0.0064  -0.0107 330 HOH B O   
2648 O  O   . HOH T .   ? 0.4766 0.2595 0.4762 0.0218  0.0213  0.0748  331 HOH B O   
2649 O  O   . HOH T .   ? 0.5454 0.3318 0.5306 -0.0423 0.0591  0.0382  332 HOH B O   
2650 O  O   . HOH T .   ? 0.4023 0.3603 0.4990 0.0250  0.0871  0.0029  333 HOH B O   
2651 O  O   . HOH T .   ? 0.3884 0.2011 0.7012 0.0388  0.0043  -0.0041 334 HOH B O   
2652 O  O   . HOH T .   ? 0.2438 0.2281 0.4931 -0.0034 -0.0296 0.0065  335 HOH B O   
2653 O  O   . HOH T .   ? 0.3257 0.5852 0.5159 0.0741  -0.0042 -0.0784 336 HOH B O   
2654 O  O   . HOH T .   ? 0.6110 0.4866 0.5220 0.0381  -0.0273 -0.0379 337 HOH B O   
2655 O  O   . HOH T .   ? 0.4506 0.4120 0.7422 -0.0655 0.0059  0.0443  338 HOH B O   
2656 O  O   . HOH T .   ? 0.3278 0.2743 0.5773 0.0463  -0.0206 -0.0591 339 HOH B O   
2657 O  O   . HOH T .   ? 0.3660 0.3669 0.6088 0.0376  0.0777  -0.0669 340 HOH B O   
2658 O  O   . HOH T .   ? 0.4776 0.3556 0.4947 -0.0236 0.0108  -0.0590 341 HOH B O   
2659 O  O   . HOH T .   ? 0.5144 0.4569 0.4871 0.0632  -0.1280 -0.1294 342 HOH B O   
2660 O  O   . HOH T .   ? 0.4351 0.2845 0.5899 0.0594  -0.0262 -0.0374 343 HOH B O   
2661 O  O   . HOH T .   ? 0.3630 0.3155 0.5761 0.0464  0.0264  0.0312  344 HOH B O   
2662 O  O   . HOH T .   ? 0.4486 0.3704 0.6078 -0.0661 0.0302  0.0137  345 HOH B O   
2663 O  O   . HOH T .   ? 0.2100 0.5521 0.6378 -0.0475 0.0356  0.0162  346 HOH B O   
2664 O  O   . HOH T .   ? 0.3735 0.4329 0.8018 0.0127  -0.0560 0.1721  347 HOH B O   
2665 O  O   . HOH T .   ? 0.4295 0.2749 0.5813 -0.0734 0.0128  0.0393  348 HOH B O   
2666 O  O   . HOH T .   ? 0.4412 0.3684 0.5037 0.0431  -0.0505 -0.0237 349 HOH B O   
2667 O  O   . HOH T .   ? 0.3084 0.3120 0.5133 0.0084  0.0171  -0.0325 350 HOH B O   
2668 O  O   . HOH T .   ? 0.3519 0.3943 0.6707 0.0876  0.0797  0.0896  351 HOH B O   
2669 O  O   . HOH T .   ? 0.4968 0.3113 0.7559 0.0771  -0.0003 0.0582  352 HOH B O   
2670 O  O   . HOH T .   ? 0.4052 0.3700 0.3973 0.0364  0.0166  0.0340  353 HOH B O   
2671 O  O   . HOH T .   ? 0.3302 0.1455 0.7231 -0.1151 0.0024  0.0000  354 HOH B O   
2672 O  O   . HOH T .   ? 0.3798 0.3784 0.5285 -0.0455 0.0690  0.0062  355 HOH B O   
2673 O  O   . HOH T .   ? 0.4176 0.3861 0.6100 -0.0370 -0.0352 -0.0042 356 HOH B O   
2674 O  O   . HOH T .   ? 0.5965 0.4307 0.5715 0.0319  0.0216  -0.1718 357 HOH B O   
2675 O  O   . HOH T .   ? 0.2727 0.3555 0.5690 -0.1270 -0.0373 0.0472  358 HOH B O   
2676 O  O   . HOH T .   ? 0.5096 0.3533 0.6364 0.2460  -0.0042 -0.0483 359 HOH B O   
2677 O  O   . HOH T .   ? 0.1790 0.2493 0.3090 -0.0161 0.0281  -0.0165 360 HOH B O   
2678 O  O   . HOH T .   ? 0.1992 0.3000 0.4370 -0.0493 -0.0267 -0.0469 361 HOH B O   
2679 O  O   . HOH T .   ? 0.2789 0.4075 0.6313 0.0671  -0.0811 0.0010  362 HOH B O   
2680 O  O   . HOH T .   ? 0.2899 0.3058 0.7269 -0.0615 -0.0886 0.0001  363 HOH B O   
2681 O  O   . HOH T .   ? 0.3647 0.1586 0.7219 0.0839  0.0413  0.0294  364 HOH B O   
2682 O  O   . HOH T .   ? 0.2837 0.2226 0.6488 -0.0127 -0.0425 0.0754  365 HOH B O   
2683 O  O   . HOH T .   ? 0.4995 0.7224 0.8679 0.3712  -0.0420 -0.0893 366 HOH B O   
2684 O  O   . HOH T .   ? 0.5384 0.5119 0.6375 -0.0862 0.0116  -0.0338 367 HOH B O   
2685 O  O   . HOH T .   ? 0.3086 0.2106 0.3817 0.0608  0.0104  -0.0239 368 HOH B O   
2686 O  O   . HOH T .   ? 0.2363 0.4326 0.9775 0.1350  -0.0336 -0.1261 369 HOH B O   
2687 O  O   . HOH T .   ? 0.4760 0.4691 0.6678 0.0719  0.0122  0.0507  370 HOH B O   
2688 O  O   . HOH T .   ? 0.3642 0.3476 0.5054 0.1042  -0.0701 -0.0176 371 HOH B O   
2689 O  O   . HOH T .   ? 0.3614 0.3924 0.6528 -0.0582 0.0050  0.0208  372 HOH B O   
2690 O  O   . HOH T .   ? 0.3303 0.4774 0.5605 -0.0071 -0.0728 0.0459  373 HOH B O   
2691 O  O   . HOH T .   ? 0.3113 0.4727 0.6440 -0.1039 0.0280  -0.0361 374 HOH B O   
2692 O  O   . HOH T .   ? 0.3894 0.4275 0.4948 0.0611  -0.0102 0.0621  375 HOH B O   
2693 O  O   . HOH T .   ? 0.3556 0.2998 0.4386 -0.0421 0.0434  0.0188  376 HOH B O   
2694 O  O   . HOH T .   ? 0.3367 0.2069 0.4227 -0.0149 0.0060  0.0304  377 HOH B O   
2695 O  O   . HOH T .   ? 0.4179 0.1610 0.5382 0.0092  0.0055  -0.0220 378 HOH B O   
2696 O  O   . HOH T .   ? 0.3594 0.4215 0.5632 0.0034  -0.0458 0.0289  379 HOH B O   
2697 O  O   . HOH T .   ? 0.5499 0.2975 0.5649 0.0069  0.0863  0.0975  380 HOH B O   
2698 O  O   . HOH T .   ? 0.2848 0.3372 0.4825 -0.0547 -0.0404 -0.0736 381 HOH B O   
2699 O  O   . HOH T .   ? 0.6467 0.5003 0.5103 0.2451  0.0038  0.2128  382 HOH B O   
2700 O  O   . HOH T .   ? 0.6671 0.2845 0.5945 -0.0893 0.0328  0.0055  383 HOH B O   
2701 O  O   . HOH T .   ? 0.2475 0.5184 0.5954 0.0317  -0.0027 0.0332  384 HOH B O   
2702 O  O   . HOH T .   ? 0.3153 0.5020 0.5517 -0.0076 -0.0534 -0.0259 385 HOH B O   
2703 O  O   . HOH T .   ? 0.1810 0.4416 0.5113 -0.0146 0.0137  0.0429  386 HOH B O   
2704 O  O   . HOH T .   ? 0.4148 0.4616 0.4189 0.0175  -0.0121 -0.0030 387 HOH B O   
# 
