data_9OFX
# 
_entry.id   9OFX 
# 
_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   9OFX         pdb_00009ofx 10.2210/pdb9ofx/pdb 
WWPDB D_1000288894 ?            ?                   
# 
_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       2025-05-14 
_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                        9OFX 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              titus.boggon@yale.edu 
_pdbx_contact_author.name_first         Titus 
_pdbx_contact_author.name_last          Boggon 
_pdbx_contact_author.name_mi            J 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2862-1637 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stiegler, A.L.' 1 0000-0003-0453-6104 
'Calicdan, X.'   2 0009-0009-5440-5955 
'Ha, B.H.'       3 0000-0001-6594-0835 
'Fisher, O.S.'   4 0000-0003-3215-0831 
'Boggon, T.J.'   5 0000-0003-2862-1637 
# 
_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 c-Src SH3 domain in H32 space group mediated by nickel' 
_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 'Calicdan, X.'   1 0009-0009-5440-5955 
primary 'Fisher, O.S.'   2 0000-0003-3215-0831 
primary 'Ha, B.H.'       3 0000-0001-6594-0835 
primary 'Boggon, T.J.'   4 0000-0003-2862-1637 
primary 'Stiegler, A.L.' 5 0000-0003-0453-6104 
# 
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 'Proto-oncogene tyrosine-protein kinase Src' 6620.198 4   2.7.10.2 ? 'c-Src SH3 domain' ? 
2 non-polymer syn 'NICKEL (II) ION'                            58.693   2   ?        ? ?                  ? 
3 non-polymer syn GLYCEROL                                     92.094   9   ?        ? ?                  ? 
4 water       nat water                                        18.015   163 ?        ? ?                  ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Proto-oncogene c-Src,pp60c-src,p60-Src' 
# 
_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       GVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPS 
_entity_poly.pdbx_seq_one_letter_code_can   GVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPS 
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NICKEL (II) ION' NI  
3 GLYCEROL          GOL 
4 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  VAL n 
1 3  THR n 
1 4  THR n 
1 5  PHE n 
1 6  VAL n 
1 7  ALA n 
1 8  LEU n 
1 9  TYR n 
1 10 ASP n 
1 11 TYR n 
1 12 GLU n 
1 13 SER n 
1 14 ARG n 
1 15 THR n 
1 16 GLU n 
1 17 THR n 
1 18 ASP n 
1 19 LEU n 
1 20 SER n 
1 21 PHE n 
1 22 LYS n 
1 23 LYS n 
1 24 GLY n 
1 25 GLU n 
1 26 ARG n 
1 27 LEU n 
1 28 GLN n 
1 29 ILE n 
1 30 VAL n 
1 31 ASN n 
1 32 ASN n 
1 33 THR n 
1 34 GLU n 
1 35 GLY n 
1 36 ASP n 
1 37 TRP n 
1 38 TRP n 
1 39 LEU n 
1 40 ALA n 
1 41 HIS n 
1 42 SER n 
1 43 LEU n 
1 44 SER n 
1 45 THR n 
1 46 GLY n 
1 47 GLN n 
1 48 THR n 
1 49 GLY n 
1 50 TYR n 
1 51 ILE n 
1 52 PRO n 
1 53 SER n 
1 54 ASN n 
1 55 TYR n 
1 56 VAL n 
1 57 ALA n 
1 58 PRO n 
1 59 SER 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                   59 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SRC, SRC1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_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                   'contains Thrombin and TEV cleavage sequences' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET28a(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ?                               'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE         ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL          'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE         ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ?                               'C6 H15 N2 O2 1' 147.195 
NI  non-polymer         . 'NICKEL (II) ION' ?                               'Ni 2'           58.693  
PHE 'L-peptide linking' y PHENYLALANINE     ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE          ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE            ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  85  85  GLY GLY A . n 
A 1 2  VAL 2  86  86  VAL VAL A . n 
A 1 3  THR 3  87  87  THR THR A . n 
A 1 4  THR 4  88  88  THR THR A . n 
A 1 5  PHE 5  89  89  PHE PHE A . n 
A 1 6  VAL 6  90  90  VAL VAL A . n 
A 1 7  ALA 7  91  91  ALA ALA A . n 
A 1 8  LEU 8  92  92  LEU LEU A . n 
A 1 9  TYR 9  93  93  TYR TYR A . n 
A 1 10 ASP 10 94  94  ASP ASP A . n 
A 1 11 TYR 11 95  95  TYR TYR A . n 
A 1 12 GLU 12 96  96  GLU GLU A . n 
A 1 13 SER 13 97  97  SER SER A . n 
A 1 14 ARG 14 98  98  ARG ARG A . n 
A 1 15 THR 15 99  99  THR THR A . n 
A 1 16 GLU 16 100 100 GLU GLU A . n 
A 1 17 THR 17 101 101 THR THR A . n 
A 1 18 ASP 18 102 102 ASP ASP A . n 
A 1 19 LEU 19 103 103 LEU LEU A . n 
A 1 20 SER 20 104 104 SER SER A . n 
A 1 21 PHE 21 105 105 PHE PHE A . n 
A 1 22 LYS 22 106 106 LYS LYS A . n 
A 1 23 LYS 23 107 107 LYS LYS A . n 
A 1 24 GLY 24 108 108 GLY GLY A . n 
A 1 25 GLU 25 109 109 GLU GLU A . n 
A 1 26 ARG 26 110 110 ARG ARG A . n 
A 1 27 LEU 27 111 111 LEU LEU A . n 
A 1 28 GLN 28 112 112 GLN GLN A . n 
A 1 29 ILE 29 113 113 ILE ILE A . n 
A 1 30 VAL 30 114 114 VAL VAL A . n 
A 1 31 ASN 31 115 115 ASN ASN A . n 
A 1 32 ASN 32 116 116 ASN ASN A . n 
A 1 33 THR 33 117 117 THR THR A . n 
A 1 34 GLU 34 118 118 GLU GLU A . n 
A 1 35 GLY 35 119 119 GLY GLY A . n 
A 1 36 ASP 36 120 120 ASP ASP A . n 
A 1 37 TRP 37 121 121 TRP TRP A . n 
A 1 38 TRP 38 122 122 TRP TRP A . n 
A 1 39 LEU 39 123 123 LEU LEU A . n 
A 1 40 ALA 40 124 124 ALA ALA A . n 
A 1 41 HIS 41 125 125 HIS HIS A . n 
A 1 42 SER 42 126 126 SER SER A . n 
A 1 43 LEU 43 127 127 LEU LEU A . n 
A 1 44 SER 44 128 128 SER SER A . n 
A 1 45 THR 45 129 129 THR THR A . n 
A 1 46 GLY 46 130 130 GLY GLY A . n 
A 1 47 GLN 47 131 131 GLN GLN A . n 
A 1 48 THR 48 132 132 THR THR A . n 
A 1 49 GLY 49 133 133 GLY GLY A . n 
A 1 50 TYR 50 134 134 TYR TYR A . n 
A 1 51 ILE 51 135 135 ILE ILE A . n 
A 1 52 PRO 52 136 136 PRO PRO A . n 
A 1 53 SER 53 137 137 SER SER A . n 
A 1 54 ASN 54 138 138 ASN ASN A . n 
A 1 55 TYR 55 139 139 TYR TYR A . n 
A 1 56 VAL 56 140 140 VAL VAL A . n 
A 1 57 ALA 57 141 141 ALA ALA A . n 
A 1 58 PRO 58 142 142 PRO PRO A . n 
A 1 59 SER 59 143 143 SER SER A . n 
B 1 1  GLY 1  85  85  GLY GLY B . n 
B 1 2  VAL 2  86  86  VAL VAL B . n 
B 1 3  THR 3  87  87  THR THR B . n 
B 1 4  THR 4  88  88  THR THR B . n 
B 1 5  PHE 5  89  89  PHE PHE B . n 
B 1 6  VAL 6  90  90  VAL VAL B . n 
B 1 7  ALA 7  91  91  ALA ALA B . n 
B 1 8  LEU 8  92  92  LEU LEU B . n 
B 1 9  TYR 9  93  93  TYR TYR B . n 
B 1 10 ASP 10 94  94  ASP ASP B . n 
B 1 11 TYR 11 95  95  TYR TYR B . n 
B 1 12 GLU 12 96  96  GLU GLU B . n 
B 1 13 SER 13 97  97  SER SER B . n 
B 1 14 ARG 14 98  98  ARG ARG B . n 
B 1 15 THR 15 99  99  THR THR B . n 
B 1 16 GLU 16 100 100 GLU GLU B . n 
B 1 17 THR 17 101 101 THR THR B . n 
B 1 18 ASP 18 102 102 ASP ASP B . n 
B 1 19 LEU 19 103 103 LEU LEU B . n 
B 1 20 SER 20 104 104 SER SER B . n 
B 1 21 PHE 21 105 105 PHE PHE B . n 
B 1 22 LYS 22 106 106 LYS LYS B . n 
B 1 23 LYS 23 107 107 LYS LYS B . n 
B 1 24 GLY 24 108 108 GLY GLY B . n 
B 1 25 GLU 25 109 109 GLU GLU B . n 
B 1 26 ARG 26 110 110 ARG ARG B . n 
B 1 27 LEU 27 111 111 LEU LEU B . n 
B 1 28 GLN 28 112 112 GLN GLN B . n 
B 1 29 ILE 29 113 113 ILE ILE B . n 
B 1 30 VAL 30 114 114 VAL VAL B . n 
B 1 31 ASN 31 115 115 ASN ASN B . n 
B 1 32 ASN 32 116 116 ASN ASN B . n 
B 1 33 THR 33 117 117 THR THR B . n 
B 1 34 GLU 34 118 118 GLU GLU B . n 
B 1 35 GLY 35 119 119 GLY GLY B . n 
B 1 36 ASP 36 120 120 ASP ASP B . n 
B 1 37 TRP 37 121 121 TRP TRP B . n 
B 1 38 TRP 38 122 122 TRP TRP B . n 
B 1 39 LEU 39 123 123 LEU LEU B . n 
B 1 40 ALA 40 124 124 ALA ALA B . n 
B 1 41 HIS 41 125 125 HIS HIS B . n 
B 1 42 SER 42 126 126 SER SER B . n 
B 1 43 LEU 43 127 127 LEU LEU B . n 
B 1 44 SER 44 128 128 SER SER B . n 
B 1 45 THR 45 129 129 THR THR B . n 
B 1 46 GLY 46 130 130 GLY GLY B . n 
B 1 47 GLN 47 131 131 GLN GLN B . n 
B 1 48 THR 48 132 132 THR THR B . n 
B 1 49 GLY 49 133 133 GLY GLY B . n 
B 1 50 TYR 50 134 134 TYR TYR B . n 
B 1 51 ILE 51 135 135 ILE ILE B . n 
B 1 52 PRO 52 136 136 PRO PRO B . n 
B 1 53 SER 53 137 137 SER SER B . n 
B 1 54 ASN 54 138 138 ASN ASN B . n 
B 1 55 TYR 55 139 139 TYR TYR B . n 
B 1 56 VAL 56 140 140 VAL VAL B . n 
B 1 57 ALA 57 141 141 ALA ALA B . n 
B 1 58 PRO 58 142 142 PRO PRO B . n 
B 1 59 SER 59 143 143 SER SER B . n 
C 1 1  GLY 1  85  85  GLY GLY C . n 
C 1 2  VAL 2  86  86  VAL VAL C . n 
C 1 3  THR 3  87  87  THR THR C . n 
C 1 4  THR 4  88  88  THR THR C . n 
C 1 5  PHE 5  89  89  PHE PHE C . n 
C 1 6  VAL 6  90  90  VAL VAL C . n 
C 1 7  ALA 7  91  91  ALA ALA C . n 
C 1 8  LEU 8  92  92  LEU LEU C . n 
C 1 9  TYR 9  93  93  TYR TYR C . n 
C 1 10 ASP 10 94  94  ASP ASP C . n 
C 1 11 TYR 11 95  95  TYR TYR C . n 
C 1 12 GLU 12 96  96  GLU GLU C . n 
C 1 13 SER 13 97  97  SER SER C . n 
C 1 14 ARG 14 98  98  ARG ARG C . n 
C 1 15 THR 15 99  99  THR THR C . n 
C 1 16 GLU 16 100 100 GLU GLU C . n 
C 1 17 THR 17 101 101 THR THR C . n 
C 1 18 ASP 18 102 102 ASP ASP C . n 
C 1 19 LEU 19 103 103 LEU LEU C . n 
C 1 20 SER 20 104 104 SER SER C . n 
C 1 21 PHE 21 105 105 PHE PHE C . n 
C 1 22 LYS 22 106 106 LYS LYS C . n 
C 1 23 LYS 23 107 107 LYS LYS C . n 
C 1 24 GLY 24 108 108 GLY GLY C . n 
C 1 25 GLU 25 109 109 GLU GLU C . n 
C 1 26 ARG 26 110 110 ARG ARG C . n 
C 1 27 LEU 27 111 111 LEU LEU C . n 
C 1 28 GLN 28 112 112 GLN GLN C . n 
C 1 29 ILE 29 113 113 ILE ILE C . n 
C 1 30 VAL 30 114 114 VAL VAL C . n 
C 1 31 ASN 31 115 115 ASN ASN C . n 
C 1 32 ASN 32 116 116 ASN ASN C . n 
C 1 33 THR 33 117 117 THR THR C . n 
C 1 34 GLU 34 118 118 GLU GLU C . n 
C 1 35 GLY 35 119 119 GLY GLY C . n 
C 1 36 ASP 36 120 120 ASP ASP C . n 
C 1 37 TRP 37 121 121 TRP TRP C . n 
C 1 38 TRP 38 122 122 TRP TRP C . n 
C 1 39 LEU 39 123 123 LEU LEU C . n 
C 1 40 ALA 40 124 124 ALA ALA C . n 
C 1 41 HIS 41 125 125 HIS HIS C . n 
C 1 42 SER 42 126 126 SER SER C . n 
C 1 43 LEU 43 127 127 LEU LEU C . n 
C 1 44 SER 44 128 128 SER SER C . n 
C 1 45 THR 45 129 129 THR THR C . n 
C 1 46 GLY 46 130 130 GLY GLY C . n 
C 1 47 GLN 47 131 131 GLN GLN C . n 
C 1 48 THR 48 132 132 THR THR C . n 
C 1 49 GLY 49 133 133 GLY GLY C . n 
C 1 50 TYR 50 134 134 TYR TYR C . n 
C 1 51 ILE 51 135 135 ILE ILE C . n 
C 1 52 PRO 52 136 136 PRO PRO C . n 
C 1 53 SER 53 137 137 SER SER C . n 
C 1 54 ASN 54 138 138 ASN ASN C . n 
C 1 55 TYR 55 139 139 TYR TYR C . n 
C 1 56 VAL 56 140 140 VAL VAL C . n 
C 1 57 ALA 57 141 141 ALA ALA C . n 
C 1 58 PRO 58 142 142 PRO PRO C . n 
C 1 59 SER 59 143 143 SER SER C . n 
D 1 1  GLY 1  85  85  GLY GLY D . n 
D 1 2  VAL 2  86  86  VAL VAL D . n 
D 1 3  THR 3  87  87  THR THR D . n 
D 1 4  THR 4  88  88  THR THR D . n 
D 1 5  PHE 5  89  89  PHE PHE D . n 
D 1 6  VAL 6  90  90  VAL VAL D . n 
D 1 7  ALA 7  91  91  ALA ALA D . n 
D 1 8  LEU 8  92  92  LEU LEU D . n 
D 1 9  TYR 9  93  93  TYR TYR D . n 
D 1 10 ASP 10 94  94  ASP ASP D . n 
D 1 11 TYR 11 95  95  TYR TYR D . n 
D 1 12 GLU 12 96  96  GLU GLU D . n 
D 1 13 SER 13 97  97  SER SER D . n 
D 1 14 ARG 14 98  98  ARG ARG D . n 
D 1 15 THR 15 99  99  THR THR D . n 
D 1 16 GLU 16 100 100 GLU GLU D . n 
D 1 17 THR 17 101 101 THR THR D . n 
D 1 18 ASP 18 102 102 ASP ASP D . n 
D 1 19 LEU 19 103 103 LEU LEU D . n 
D 1 20 SER 20 104 104 SER SER D . n 
D 1 21 PHE 21 105 105 PHE PHE D . n 
D 1 22 LYS 22 106 106 LYS LYS D . n 
D 1 23 LYS 23 107 107 LYS LYS D . n 
D 1 24 GLY 24 108 108 GLY GLY D . n 
D 1 25 GLU 25 109 109 GLU GLU D . n 
D 1 26 ARG 26 110 110 ARG ARG D . n 
D 1 27 LEU 27 111 111 LEU LEU D . n 
D 1 28 GLN 28 112 112 GLN GLN D . n 
D 1 29 ILE 29 113 113 ILE ILE D . n 
D 1 30 VAL 30 114 114 VAL VAL D . n 
D 1 31 ASN 31 115 ?   ?   ?   D . n 
D 1 32 ASN 32 116 ?   ?   ?   D . n 
D 1 33 THR 33 117 ?   ?   ?   D . n 
D 1 34 GLU 34 118 ?   ?   ?   D . n 
D 1 35 GLY 35 119 ?   ?   ?   D . n 
D 1 36 ASP 36 120 120 ASP ASP D . n 
D 1 37 TRP 37 121 121 TRP TRP D . n 
D 1 38 TRP 38 122 122 TRP TRP D . n 
D 1 39 LEU 39 123 123 LEU LEU D . n 
D 1 40 ALA 40 124 124 ALA ALA D . n 
D 1 41 HIS 41 125 125 HIS HIS D . n 
D 1 42 SER 42 126 126 SER SER D . n 
D 1 43 LEU 43 127 127 LEU LEU D . n 
D 1 44 SER 44 128 128 SER SER D . n 
D 1 45 THR 45 129 129 THR THR D . n 
D 1 46 GLY 46 130 130 GLY GLY D . n 
D 1 47 GLN 47 131 131 GLN GLN D . n 
D 1 48 THR 48 132 132 THR THR D . n 
D 1 49 GLY 49 133 133 GLY GLY D . n 
D 1 50 TYR 50 134 134 TYR TYR D . n 
D 1 51 ILE 51 135 135 ILE ILE D . n 
D 1 52 PRO 52 136 136 PRO PRO D . n 
D 1 53 SER 53 137 137 SER SER D . n 
D 1 54 ASN 54 138 138 ASN ASN D . n 
D 1 55 TYR 55 139 139 TYR TYR D . n 
D 1 56 VAL 56 140 140 VAL VAL D . n 
D 1 57 ALA 57 141 141 ALA ALA D . n 
D 1 58 PRO 58 142 142 PRO PRO D . n 
D 1 59 SER 59 143 143 SER SER D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 NI  1  201 2   NI  NI  A . 
F 3 GOL 1  202 2   GOL GOL A . 
G 3 GOL 1  203 3   GOL GOL A . 
H 2 NI  1  201 1   NI  NI  B . 
I 3 GOL 1  202 8   GOL GOL B . 
J 3 GOL 1  201 4   GOL GOL C . 
K 3 GOL 1  202 5   GOL GOL C . 
L 3 GOL 1  203 7   GOL GOL C . 
M 3 GOL 1  204 9   GOL GOL C . 
N 3 GOL 1  201 1   GOL GOL D . 
O 3 GOL 1  202 6   GOL GOL D . 
P 4 HOH 1  301 11  HOH HOH A . 
P 4 HOH 2  302 6   HOH HOH A . 
P 4 HOH 3  303 15  HOH HOH A . 
P 4 HOH 4  304 18  HOH HOH A . 
P 4 HOH 5  305 52  HOH HOH A . 
P 4 HOH 6  306 93  HOH HOH A . 
P 4 HOH 7  307 19  HOH HOH A . 
P 4 HOH 8  308 29  HOH HOH A . 
P 4 HOH 9  309 90  HOH HOH A . 
P 4 HOH 10 310 76  HOH HOH A . 
P 4 HOH 11 311 94  HOH HOH A . 
P 4 HOH 12 312 23  HOH HOH A . 
P 4 HOH 13 313 72  HOH HOH A . 
P 4 HOH 14 314 21  HOH HOH A . 
P 4 HOH 15 315 13  HOH HOH A . 
P 4 HOH 16 316 4   HOH HOH A . 
P 4 HOH 17 317 27  HOH HOH A . 
P 4 HOH 18 318 63  HOH HOH A . 
P 4 HOH 19 319 159 HOH HOH A . 
P 4 HOH 20 320 59  HOH HOH A . 
P 4 HOH 21 321 5   HOH HOH A . 
P 4 HOH 22 322 42  HOH HOH A . 
P 4 HOH 23 323 58  HOH HOH A . 
P 4 HOH 24 324 114 HOH HOH A . 
P 4 HOH 25 325 57  HOH HOH A . 
P 4 HOH 26 326 71  HOH HOH A . 
P 4 HOH 27 327 104 HOH HOH A . 
P 4 HOH 28 328 61  HOH HOH A . 
P 4 HOH 29 329 35  HOH HOH A . 
P 4 HOH 30 330 39  HOH HOH A . 
P 4 HOH 31 331 111 HOH HOH A . 
P 4 HOH 32 332 66  HOH HOH A . 
P 4 HOH 33 333 112 HOH HOH A . 
P 4 HOH 34 334 116 HOH HOH A . 
P 4 HOH 35 335 108 HOH HOH A . 
Q 4 HOH 1  301 137 HOH HOH B . 
Q 4 HOH 2  302 121 HOH HOH B . 
Q 4 HOH 3  303 67  HOH HOH B . 
Q 4 HOH 4  304 106 HOH HOH B . 
Q 4 HOH 5  305 49  HOH HOH B . 
Q 4 HOH 6  306 14  HOH HOH B . 
Q 4 HOH 7  307 24  HOH HOH B . 
Q 4 HOH 8  308 143 HOH HOH B . 
Q 4 HOH 9  309 79  HOH HOH B . 
Q 4 HOH 10 310 30  HOH HOH B . 
Q 4 HOH 11 311 74  HOH HOH B . 
Q 4 HOH 12 312 2   HOH HOH B . 
Q 4 HOH 13 313 3   HOH HOH B . 
Q 4 HOH 14 314 20  HOH HOH B . 
Q 4 HOH 15 315 133 HOH HOH B . 
Q 4 HOH 16 316 1   HOH HOH B . 
Q 4 HOH 17 317 150 HOH HOH B . 
Q 4 HOH 18 318 36  HOH HOH B . 
Q 4 HOH 19 319 126 HOH HOH B . 
Q 4 HOH 20 320 16  HOH HOH B . 
Q 4 HOH 21 321 103 HOH HOH B . 
Q 4 HOH 22 322 40  HOH HOH B . 
Q 4 HOH 23 323 96  HOH HOH B . 
Q 4 HOH 24 324 32  HOH HOH B . 
Q 4 HOH 25 325 82  HOH HOH B . 
Q 4 HOH 26 326 81  HOH HOH B . 
Q 4 HOH 27 327 102 HOH HOH B . 
Q 4 HOH 28 328 98  HOH HOH B . 
Q 4 HOH 29 329 125 HOH HOH B . 
Q 4 HOH 30 330 69  HOH HOH B . 
Q 4 HOH 31 331 134 HOH HOH B . 
Q 4 HOH 32 332 91  HOH HOH B . 
Q 4 HOH 33 333 124 HOH HOH B . 
Q 4 HOH 34 334 135 HOH HOH B . 
Q 4 HOH 35 335 130 HOH HOH B . 
Q 4 HOH 36 336 140 HOH HOH B . 
Q 4 HOH 37 337 145 HOH HOH B . 
Q 4 HOH 38 338 9   HOH HOH B . 
Q 4 HOH 39 339 77  HOH HOH B . 
Q 4 HOH 40 340 68  HOH HOH B . 
Q 4 HOH 41 341 157 HOH HOH B . 
R 4 HOH 1  301 141 HOH HOH C . 
R 4 HOH 2  302 132 HOH HOH C . 
R 4 HOH 3  303 105 HOH HOH C . 
R 4 HOH 4  304 43  HOH HOH C . 
R 4 HOH 5  305 117 HOH HOH C . 
R 4 HOH 6  306 12  HOH HOH C . 
R 4 HOH 7  307 64  HOH HOH C . 
R 4 HOH 8  308 87  HOH HOH C . 
R 4 HOH 9  309 110 HOH HOH C . 
R 4 HOH 10 310 54  HOH HOH C . 
R 4 HOH 11 311 144 HOH HOH C . 
R 4 HOH 12 312 70  HOH HOH C . 
R 4 HOH 13 313 48  HOH HOH C . 
R 4 HOH 14 314 161 HOH HOH C . 
R 4 HOH 15 315 8   HOH HOH C . 
R 4 HOH 16 316 22  HOH HOH C . 
R 4 HOH 17 317 53  HOH HOH C . 
R 4 HOH 18 318 7   HOH HOH C . 
R 4 HOH 19 319 109 HOH HOH C . 
R 4 HOH 20 320 99  HOH HOH C . 
R 4 HOH 21 321 97  HOH HOH C . 
R 4 HOH 22 322 50  HOH HOH C . 
R 4 HOH 23 323 10  HOH HOH C . 
R 4 HOH 24 324 113 HOH HOH C . 
R 4 HOH 25 325 73  HOH HOH C . 
R 4 HOH 26 326 100 HOH HOH C . 
R 4 HOH 27 327 26  HOH HOH C . 
R 4 HOH 28 328 85  HOH HOH C . 
R 4 HOH 29 329 65  HOH HOH C . 
R 4 HOH 30 330 25  HOH HOH C . 
R 4 HOH 31 331 38  HOH HOH C . 
R 4 HOH 32 332 92  HOH HOH C . 
R 4 HOH 33 333 80  HOH HOH C . 
R 4 HOH 34 334 51  HOH HOH C . 
R 4 HOH 35 335 46  HOH HOH C . 
R 4 HOH 36 336 86  HOH HOH C . 
R 4 HOH 37 337 45  HOH HOH C . 
R 4 HOH 38 338 156 HOH HOH C . 
R 4 HOH 39 339 147 HOH HOH C . 
R 4 HOH 40 340 152 HOH HOH C . 
R 4 HOH 41 341 62  HOH HOH C . 
R 4 HOH 42 342 107 HOH HOH C . 
R 4 HOH 43 343 33  HOH HOH C . 
R 4 HOH 44 344 123 HOH HOH C . 
R 4 HOH 45 345 154 HOH HOH C . 
R 4 HOH 46 346 148 HOH HOH C . 
R 4 HOH 47 347 151 HOH HOH C . 
R 4 HOH 48 348 136 HOH HOH C . 
R 4 HOH 49 349 160 HOH HOH C . 
R 4 HOH 50 350 115 HOH HOH C . 
R 4 HOH 51 351 158 HOH HOH C . 
R 4 HOH 52 352 163 HOH HOH C . 
S 4 HOH 1  301 28  HOH HOH D . 
S 4 HOH 2  302 138 HOH HOH D . 
S 4 HOH 3  303 149 HOH HOH D . 
S 4 HOH 4  304 78  HOH HOH D . 
S 4 HOH 5  305 83  HOH HOH D . 
S 4 HOH 6  306 155 HOH HOH D . 
S 4 HOH 7  307 31  HOH HOH D . 
S 4 HOH 8  308 44  HOH HOH D . 
S 4 HOH 9  309 153 HOH HOH D . 
S 4 HOH 10 310 84  HOH HOH D . 
S 4 HOH 11 311 47  HOH HOH D . 
S 4 HOH 12 312 119 HOH HOH D . 
S 4 HOH 13 313 129 HOH HOH D . 
S 4 HOH 14 314 146 HOH HOH D . 
S 4 HOH 15 315 120 HOH HOH D . 
S 4 HOH 16 316 17  HOH HOH D . 
S 4 HOH 17 317 56  HOH HOH D . 
S 4 HOH 18 318 131 HOH HOH D . 
S 4 HOH 19 319 128 HOH HOH D . 
S 4 HOH 20 320 118 HOH HOH D . 
S 4 HOH 21 321 139 HOH HOH D . 
S 4 HOH 22 322 88  HOH HOH D . 
S 4 HOH 23 323 101 HOH HOH D . 
S 4 HOH 24 324 89  HOH HOH D . 
S 4 HOH 25 325 37  HOH HOH D . 
S 4 HOH 26 326 60  HOH HOH D . 
S 4 HOH 27 327 162 HOH HOH D . 
S 4 HOH 28 328 95  HOH HOH D . 
S 4 HOH 29 329 41  HOH HOH D . 
S 4 HOH 30 330 34  HOH HOH D . 
S 4 HOH 31 331 142 HOH HOH D . 
S 4 HOH 32 332 75  HOH HOH D . 
S 4 HOH 33 333 55  HOH HOH D . 
S 4 HOH 34 334 127 HOH HOH D . 
S 4 HOH 35 335 122 HOH HOH D . 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21.1_5286: ???)' ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.15               ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3                ? 4 
# 
_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                     9OFX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.770 
_cell.length_a_esd                 ? 
_cell.length_b                     63.770 
_cell.length_b_esd                 ? 
_cell.length_c                     271.710 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        72 
_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                         9OFX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_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                   9OFX 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.6 
_exptl_crystal.description                  'rectangular prism' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'ambient temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.7 M Ammonium Sulfate, 5 mM NiCl2, 10% glycerol, 0.1 M HEPES pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             'cold Nitrogen gas stream' 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-23 
_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                    'horizontal bounce Si(111) double crystal 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   0.979315 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979315 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9OFX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.45 
_reflns.d_resolution_low                               31.95 
_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                                     73036 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                52.6 
_reflns.pdbx_netI_over_av_sigmaI                       22.9 
_reflns.pdbx_netI_over_sigmaI                          22.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.06 
_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                                0.087 
_reflns.pdbx_Rpim_I_all                                0.012 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.086 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.45 
_reflns_shell.d_res_low                                     1.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           90146 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1925 
_reflns_shell.percent_possible_obs                          100.0 
_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                               46.8 
_reflns_shell.pdbx_chi_squared                              1.29 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               3.505 
_reflns_shell.pdbx_Rpim_I_all                               0.509 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.784 
_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                                  3.467 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.07 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9OFX 
_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                            1.45 
_refine.ls_d_res_low                             31.89 
_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                     73036 
_refine.ls_number_reflns_R_free                  3450 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 4.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1642 
_refine.ls_R_factor_R_free                       0.1961 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1625 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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       ML 
_refine.pdbx_R_Free_selection_details            'Random selection' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.20 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        31.89 
_refine_hist.number_atoms_solvent             163 
_refine_hist.number_atoms_total               2059 
_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        1840 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 1985 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.879  ? 2704 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 12.480 ? 691  ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.080  ? 294  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 341  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.45 1.47  . . 137 2734 100.00 . . . . 0.2788 . . . . . . . . . . . . . . . 0.3745 
'X-RAY DIFFRACTION' 1.47 1.49  . . 138 2794 100.00 . . . . 0.2552 . . . . . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 1.49 1.51  . . 137 2807 100.00 . . . . 0.2317 . . . . . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 1.51 1.54  . . 138 2757 100.00 . . . . 0.2124 . . . . . . . . . . . . . . . 0.2796 
'X-RAY DIFFRACTION' 1.54 1.56  . . 140 2799 100.00 . . . . 0.1981 . . . . . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.56 1.59  . . 139 2796 100.00 . . . . 0.1890 . . . . . . . . . . . . . . . 0.2398 
'X-RAY DIFFRACTION' 1.59 1.62  . . 136 2737 100.00 . . . . 0.1836 . . . . . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 1.62 1.65  . . 142 2803 100.00 . . . . 0.1778 . . . . . . . . . . . . . . . 0.2204 
'X-RAY DIFFRACTION' 1.65 1.68  . . 137 2765 100.00 . . . . 0.1744 . . . . . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 1.68 1.72  . . 138 2798 100.00 . . . . 0.1677 . . . . . . . . . . . . . . . 0.2368 
'X-RAY DIFFRACTION' 1.72 1.76  . . 139 2764 100.00 . . . . 0.1653 . . . . . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 1.76 1.80  . . 130 2790 100.00 . . . . 0.1628 . . . . . . . . . . . . . . . 0.3204 
'X-RAY DIFFRACTION' 1.80 1.85  . . 135 2797 100.00 . . . . 0.1506 . . . . . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 1.85 1.91  . . 140 2771 100.00 . . . . 0.1533 . . . . . . . . . . . . . . . 0.1903 
'X-RAY DIFFRACTION' 1.91 1.97  . . 142 2776 100.00 . . . . 0.1406 . . . . . . . . . . . . . . . 0.1955 
'X-RAY DIFFRACTION' 1.97 2.04  . . 137 2811 100.00 . . . . 0.1413 . . . . . . . . . . . . . . . 0.1725 
'X-RAY DIFFRACTION' 2.04 2.12  . . 135 2803 100.00 . . . . 0.1493 . . . . . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 2.12 2.22  . . 141 2774 100.00 . . . . 0.1619 . . . . . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 2.22 2.33  . . 135 2800 100.00 . . . . 0.1523 . . . . . . . . . . . . . . . 0.1853 
'X-RAY DIFFRACTION' 2.33 2.48  . . 139 2759 100.00 . . . . 0.1743 . . . . . . . . . . . . . . . 0.2562 
'X-RAY DIFFRACTION' 2.48 2.67  . . 133 2806 100.00 . . . . 0.1789 . . . . . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 2.67 2.94  . . 134 2776 100.00 . . . . 0.1829 . . . . . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 2.94 3.36  . . 142 2797 100.00 . . . . 0.1581 . . . . . . . . . . . . . . . 0.1794 
'X-RAY DIFFRACTION' 3.36 4.24  . . 141 2789 100.00 . . . . 0.1457 . . . . . . . . . . . . . . . 0.1531 
'X-RAY DIFFRACTION' 4.24 31.89 . . 145 2783 100.00 . . . . 0.1588 . . . . . . . . . . . . . . . 0.1837 
# 
_struct.entry_id                     9OFX 
_struct.title                        'Crystal structure of c-Src SH3 domain in H32 space group mediated by nickel' 
_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        9OFX 
_struct_keywords.text            'SH3 domain, nickel, Src, ATCUN, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
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 4 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SRC_HUMAN 
_struct_ref.pdbx_db_accession          P12931 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   GVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPS 
_struct_ref.pdbx_align_begin           85 
# 
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 9OFX A 1 ? 59 ? P12931 85 ? 143 ? 85 143 
2 1 9OFX B 1 ? 59 ? P12931 85 ? 143 ? 85 143 
3 1 9OFX C 1 ? 59 ? P12931 85 ? 143 ? 85 143 
4 1 9OFX D 1 ? 59 ? P12931 85 ? 143 ? 85 143 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6030  ? 
1 MORE         -42   ? 
1 'SSA (A^2)'  11550 ? 
# 
_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 
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_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 GLY 1  N   ? ? ? 1_555 E NI  .  NI  ? ? A GLY 85  A NI  201 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
metalc2  metalc ? ? A GLY 1  O   ? ? ? 1_555 E NI  .  NI  ? ? A GLY 85  A NI  201 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
metalc3  metalc ? ? A HIS 41 NE2 ? ? ? 1_555 H NI  .  NI  ? ? A HIS 125 B NI  201 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc4  metalc ? ? E NI  .  NI  ? ? ? 1_555 P HOH .  O   ? ? A NI  201 A HOH 302 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc5  metalc ? ? E NI  .  NI  ? ? ? 1_555 P HOH .  O   ? ? A NI  201 A HOH 316 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc6  metalc ? ? E NI  .  NI  ? ? ? 1_555 P HOH .  O   ? ? A NI  201 A HOH 321 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc7  metalc ? ? E NI  .  NI  ? ? ? 1_555 B HIS 41 NE2 ? ? A NI  201 B HIS 125 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc8  metalc ? ? B GLY 1  N   ? ? ? 1_555 H NI  .  NI  ? ? B GLY 85  B NI  201 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc9  metalc ? ? B GLY 1  O   ? ? ? 1_555 H NI  .  NI  ? ? B GLY 85  B NI  201 1_555 ? ? ? ? ? ? ? 1.967 ? ? 
metalc10 metalc ? ? H NI  .  NI  ? ? ? 1_555 Q HOH .  O   ? ? B NI  201 B HOH 312 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc11 metalc ? ? H NI  .  NI  ? ? ? 1_555 Q HOH .  O   ? ? B NI  201 B HOH 313 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc12 metalc ? ? H NI  .  NI  ? ? ? 1_555 Q HOH .  O   ? ? B NI  201 B HOH 316 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
# 
_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  N   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? A GLY 1  ? A GLY 85  ? 1_555 82.6  ? 
2  N   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 302 ? 1_555 83.9  ? 
3  O   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 302 ? 1_555 93.3  ? 
4  N   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 316 ? 1_555 93.6  ? 
5  O   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 316 ? 1_555 88.6  ? 
6  O   ? P HOH .  ? A HOH 302 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 316 ? 1_555 176.7 ? 
7  N   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 321 ? 1_555 90.5  ? 
8  O   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 321 ? 1_555 173.2 ? 
9  O   ? P HOH .  ? A HOH 302 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 321 ? 1_555 86.5  ? 
10 O   ? P HOH .  ? A HOH 316 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 O   ? P HOH .  ? A HOH 321 ? 1_555 91.4  ? 
11 N   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 NE2 ? B HIS 41 ? B HIS 125 ? 1_555 165.8 ? 
12 O   ? A GLY 1  ? A GLY 85  ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 NE2 ? B HIS 41 ? B HIS 125 ? 1_555 87.1  ? 
13 O   ? P HOH .  ? A HOH 302 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 NE2 ? B HIS 41 ? B HIS 125 ? 1_555 86.8  ? 
14 O   ? P HOH .  ? A HOH 316 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 NE2 ? B HIS 41 ? B HIS 125 ? 1_555 96.0  ? 
15 O   ? P HOH .  ? A HOH 321 ? 1_555 NI ? E NI . ? A NI 201 ? 1_555 NE2 ? B HIS 41 ? B HIS 125 ? 1_555 99.7  ? 
16 NE2 ? A HIS 41 ? A HIS 125 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 N   ? B GLY 1  ? B GLY 85  ? 1_555 171.9 ? 
17 NE2 ? A HIS 41 ? A HIS 125 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? B GLY 1  ? B GLY 85  ? 1_555 90.0  ? 
18 N   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? B GLY 1  ? B GLY 85  ? 1_555 84.5  ? 
19 NE2 ? A HIS 41 ? A HIS 125 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 312 ? 1_555 97.0  ? 
20 N   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 312 ? 1_555 88.9  ? 
21 O   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 312 ? 1_555 172.7 ? 
22 NE2 ? A HIS 41 ? A HIS 125 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 313 ? 1_555 88.1  ? 
23 N   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 313 ? 1_555 86.1  ? 
24 O   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 313 ? 1_555 91.3  ? 
25 O   ? Q HOH .  ? B HOH 312 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 313 ? 1_555 91.1  ? 
26 NE2 ? A HIS 41 ? A HIS 125 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 316 ? 1_555 95.7  ? 
27 N   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 316 ? 1_555 90.0  ? 
28 O   ? B GLY 1  ? B GLY 85  ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 316 ? 1_555 87.5  ? 
29 O   ? Q HOH .  ? B HOH 312 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 316 ? 1_555 89.6  ? 
30 O   ? Q HOH .  ? B HOH 313 ? 1_555 NI ? H NI . ? B NI 201 ? 1_555 O   ? Q HOH .  ? B HOH 316 ? 1_555 176.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 48 ? PRO A 52 ? THR A 132 PRO A 136 
AA1 2 TRP A 37 ? SER A 42 ? TRP A 121 SER A 126 
AA1 3 ARG A 26 ? ASN A 31 ? ARG A 110 ASN A 115 
AA1 4 PHE A 5  ? ALA A 7  ? PHE A 89  ALA A 91  
AA1 5 VAL A 56 ? PRO A 58 ? VAL A 140 PRO A 142 
AA2 1 THR B 48 ? PRO B 52 ? THR B 132 PRO B 136 
AA2 2 TRP B 37 ? SER B 42 ? TRP B 121 SER B 126 
AA2 3 ARG B 26 ? ASN B 31 ? ARG B 110 ASN B 115 
AA2 4 PHE B 5  ? ALA B 7  ? PHE B 89  ALA B 91  
AA2 5 VAL B 56 ? PRO B 58 ? VAL B 140 PRO B 142 
AA3 1 THR C 48 ? PRO C 52 ? THR C 132 PRO C 136 
AA3 2 TRP C 37 ? SER C 42 ? TRP C 121 SER C 126 
AA3 3 ARG C 26 ? VAL C 30 ? ARG C 110 VAL C 114 
AA3 4 THR C 4  ? ALA C 7  ? THR C 88  ALA C 91  
AA3 5 VAL C 56 ? PRO C 58 ? VAL C 140 PRO C 142 
AA4 1 THR D 48 ? PRO D 52 ? THR D 132 PRO D 136 
AA4 2 TRP D 37 ? SER D 42 ? TRP D 121 SER D 126 
AA4 3 ARG D 26 ? VAL D 30 ? ARG D 110 VAL D 114 
AA4 4 THR D 4  ? ALA D 7  ? THR D 88  ALA D 91  
AA4 5 VAL D 56 ? PRO D 58 ? VAL D 140 PRO D 142 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 51 ? O ILE A 135 N TRP A 38 ? N TRP A 122 
AA1 2 3 O HIS A 41 ? O HIS A 125 N GLN A 28 ? N GLN A 112 
AA1 3 4 O LEU A 27 ? O LEU A 111 N PHE A 5  ? N PHE A 89  
AA1 4 5 N VAL A 6  ? N VAL A 90  O ALA A 57 ? O ALA A 141 
AA2 1 2 O GLY B 49 ? O GLY B 133 N ALA B 40 ? N ALA B 124 
AA2 2 3 O HIS B 41 ? O HIS B 125 N GLN B 28 ? N GLN B 112 
AA2 3 4 O LEU B 27 ? O LEU B 111 N PHE B 5  ? N PHE B 89  
AA2 4 5 N VAL B 6  ? N VAL B 90  O ALA B 57 ? O ALA B 141 
AA3 1 2 O ILE C 51 ? O ILE C 135 N TRP C 38 ? N TRP C 122 
AA3 2 3 O HIS C 41 ? O HIS C 125 N GLN C 28 ? N GLN C 112 
AA3 3 4 O LEU C 27 ? O LEU C 111 N PHE C 5  ? N PHE C 89  
AA3 4 5 N VAL C 6  ? N VAL C 90  O ALA C 57 ? O ALA C 141 
AA4 1 2 O ILE D 51 ? O ILE D 135 N TRP D 38 ? N TRP D 122 
AA4 2 3 O HIS D 41 ? O HIS D 125 N GLN D 28 ? N GLN D 112 
AA4 3 4 O LEU D 27 ? O LEU D 111 N PHE D 5  ? N PHE D 89  
AA4 4 5 N VAL D 6  ? N VAL D 90  O ALA D 57 ? O ALA D 141 
# 
_pdbx_entry_details.entry_id                   9OFX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 GLU A 118 ? ? -106.18 58.88   
2 1 ASN B 116 ? ? -140.21 31.59   
3 1 ASN C 115 ? ? 69.83   -155.05 
4 1 GLU D 100 ? ? -76.91  43.31   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    C 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     327 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   R 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 D ASN 115 ? D ASN 31 
2 1 Y 1 D ASN 116 ? D ASN 32 
3 1 Y 1 D THR 117 ? D THR 33 
4 1 Y 1 D GLU 118 ? D GLU 34 
5 1 Y 1 D GLY 119 ? D GLY 35 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
GOL C1   C  N N 123 
GOL O1   O  N N 124 
GOL C2   C  N N 125 
GOL O2   O  N N 126 
GOL C3   C  N N 127 
GOL O3   O  N N 128 
GOL H11  H  N N 129 
GOL H12  H  N N 130 
GOL HO1  H  N N 131 
GOL H2   H  N N 132 
GOL HO2  H  N N 133 
GOL H31  H  N N 134 
GOL H32  H  N N 135 
GOL HO3  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
NI  NI   NI N N 230 
PHE N    N  N N 231 
PHE CA   C  N S 232 
PHE C    C  N N 233 
PHE O    O  N N 234 
PHE CB   C  N N 235 
PHE CG   C  Y N 236 
PHE CD1  C  Y N 237 
PHE CD2  C  Y N 238 
PHE CE1  C  Y N 239 
PHE CE2  C  Y N 240 
PHE CZ   C  Y N 241 
PHE OXT  O  N N 242 
PHE H    H  N N 243 
PHE H2   H  N N 244 
PHE HA   H  N N 245 
PHE HB2  H  N N 246 
PHE HB3  H  N N 247 
PHE HD1  H  N N 248 
PHE HD2  H  N N 249 
PHE HE1  H  N N 250 
PHE HE2  H  N N 251 
PHE HZ   H  N N 252 
PHE HXT  H  N N 253 
PRO N    N  N N 254 
PRO CA   C  N S 255 
PRO C    C  N N 256 
PRO O    O  N N 257 
PRO CB   C  N N 258 
PRO CG   C  N N 259 
PRO CD   C  N N 260 
PRO OXT  O  N N 261 
PRO H    H  N N 262 
PRO HA   H  N N 263 
PRO HB2  H  N N 264 
PRO HB3  H  N N 265 
PRO HG2  H  N N 266 
PRO HG3  H  N N 267 
PRO HD2  H  N N 268 
PRO HD3  H  N N 269 
PRO HXT  H  N N 270 
SER N    N  N N 271 
SER CA   C  N S 272 
SER C    C  N N 273 
SER O    O  N N 274 
SER CB   C  N N 275 
SER OG   O  N N 276 
SER OXT  O  N N 277 
SER H    H  N N 278 
SER H2   H  N N 279 
SER HA   H  N N 280 
SER HB2  H  N N 281 
SER HB3  H  N N 282 
SER HG   H  N N 283 
SER HXT  H  N N 284 
THR N    N  N N 285 
THR CA   C  N S 286 
THR C    C  N N 287 
THR O    O  N N 288 
THR CB   C  N R 289 
THR OG1  O  N N 290 
THR CG2  C  N N 291 
THR OXT  O  N N 292 
THR H    H  N N 293 
THR H2   H  N N 294 
THR HA   H  N N 295 
THR HB   H  N N 296 
THR HG1  H  N N 297 
THR HG21 H  N N 298 
THR HG22 H  N N 299 
THR HG23 H  N N 300 
THR HXT  H  N N 301 
TRP N    N  N N 302 
TRP CA   C  N S 303 
TRP C    C  N N 304 
TRP O    O  N N 305 
TRP CB   C  N N 306 
TRP CG   C  Y N 307 
TRP CD1  C  Y N 308 
TRP CD2  C  Y N 309 
TRP NE1  N  Y N 310 
TRP CE2  C  Y N 311 
TRP CE3  C  Y N 312 
TRP CZ2  C  Y N 313 
TRP CZ3  C  Y N 314 
TRP CH2  C  Y N 315 
TRP OXT  O  N N 316 
TRP H    H  N N 317 
TRP H2   H  N N 318 
TRP HA   H  N N 319 
TRP HB2  H  N N 320 
TRP HB3  H  N N 321 
TRP HD1  H  N N 322 
TRP HE1  H  N N 323 
TRP HE3  H  N N 324 
TRP HZ2  H  N N 325 
TRP HZ3  H  N N 326 
TRP HH2  H  N N 327 
TRP HXT  H  N N 328 
TYR N    N  N N 329 
TYR CA   C  N S 330 
TYR C    C  N N 331 
TYR O    O  N N 332 
TYR CB   C  N N 333 
TYR CG   C  Y N 334 
TYR CD1  C  Y N 335 
TYR CD2  C  Y N 336 
TYR CE1  C  Y N 337 
TYR CE2  C  Y N 338 
TYR CZ   C  Y N 339 
TYR OH   O  N N 340 
TYR OXT  O  N N 341 
TYR H    H  N N 342 
TYR H2   H  N N 343 
TYR HA   H  N N 344 
TYR HB2  H  N N 345 
TYR HB3  H  N N 346 
TYR HD1  H  N N 347 
TYR HD2  H  N N 348 
TYR HE1  H  N N 349 
TYR HE2  H  N N 350 
TYR HH   H  N N 351 
TYR HXT  H  N N 352 
VAL N    N  N N 353 
VAL CA   C  N S 354 
VAL C    C  N N 355 
VAL O    O  N N 356 
VAL CB   C  N N 357 
VAL CG1  C  N N 358 
VAL CG2  C  N N 359 
VAL OXT  O  N N 360 
VAL H    H  N N 361 
VAL H2   H  N N 362 
VAL HA   H  N N 363 
VAL HB   H  N N 364 
VAL HG11 H  N N 365 
VAL HG12 H  N N 366 
VAL HG13 H  N N 367 
VAL HG21 H  N N 368 
VAL HG22 H  N N 369 
VAL HG23 H  N N 370 
VAL HXT  H  N N 371 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
GOL C1  O1   sing N N 116 
GOL C1  C2   sing N N 117 
GOL C1  H11  sing N N 118 
GOL C1  H12  sing N N 119 
GOL O1  HO1  sing N N 120 
GOL C2  O2   sing N N 121 
GOL C2  C3   sing N N 122 
GOL C2  H2   sing N N 123 
GOL O2  HO2  sing N N 124 
GOL C3  O3   sing N N 125 
GOL C3  H31  sing N N 126 
GOL C3  H32  sing N N 127 
GOL O3  HO3  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
PHE N   CA   sing N N 218 
PHE N   H    sing N N 219 
PHE N   H2   sing N N 220 
PHE CA  C    sing N N 221 
PHE CA  CB   sing N N 222 
PHE CA  HA   sing N N 223 
PHE C   O    doub N N 224 
PHE C   OXT  sing N N 225 
PHE CB  CG   sing N N 226 
PHE CB  HB2  sing N N 227 
PHE CB  HB3  sing N N 228 
PHE CG  CD1  doub Y N 229 
PHE CG  CD2  sing Y N 230 
PHE CD1 CE1  sing Y N 231 
PHE CD1 HD1  sing N N 232 
PHE CD2 CE2  doub Y N 233 
PHE CD2 HD2  sing N N 234 
PHE CE1 CZ   doub Y N 235 
PHE CE1 HE1  sing N N 236 
PHE CE2 CZ   sing Y N 237 
PHE CE2 HE2  sing N N 238 
PHE CZ  HZ   sing N N 239 
PHE OXT HXT  sing N N 240 
PRO N   CA   sing N N 241 
PRO N   CD   sing N N 242 
PRO N   H    sing N N 243 
PRO CA  C    sing N N 244 
PRO CA  CB   sing N N 245 
PRO CA  HA   sing N N 246 
PRO C   O    doub N N 247 
PRO C   OXT  sing N N 248 
PRO CB  CG   sing N N 249 
PRO CB  HB2  sing N N 250 
PRO CB  HB3  sing N N 251 
PRO CG  CD   sing N N 252 
PRO CG  HG2  sing N N 253 
PRO CG  HG3  sing N N 254 
PRO CD  HD2  sing N N 255 
PRO CD  HD3  sing N N 256 
PRO OXT HXT  sing N N 257 
SER N   CA   sing N N 258 
SER N   H    sing N N 259 
SER N   H2   sing N N 260 
SER CA  C    sing N N 261 
SER CA  CB   sing N N 262 
SER CA  HA   sing N N 263 
SER C   O    doub N N 264 
SER C   OXT  sing N N 265 
SER CB  OG   sing N N 266 
SER CB  HB2  sing N N 267 
SER CB  HB3  sing N N 268 
SER OG  HG   sing N N 269 
SER OXT HXT  sing N N 270 
THR N   CA   sing N N 271 
THR N   H    sing N N 272 
THR N   H2   sing N N 273 
THR CA  C    sing N N 274 
THR CA  CB   sing N N 275 
THR CA  HA   sing N N 276 
THR C   O    doub N N 277 
THR C   OXT  sing N N 278 
THR CB  OG1  sing N N 279 
THR CB  CG2  sing N N 280 
THR CB  HB   sing N N 281 
THR OG1 HG1  sing N N 282 
THR CG2 HG21 sing N N 283 
THR CG2 HG22 sing N N 284 
THR CG2 HG23 sing N N 285 
THR OXT HXT  sing N N 286 
TRP N   CA   sing N N 287 
TRP N   H    sing N N 288 
TRP N   H2   sing N N 289 
TRP CA  C    sing N N 290 
TRP CA  CB   sing N N 291 
TRP CA  HA   sing N N 292 
TRP C   O    doub N N 293 
TRP C   OXT  sing N N 294 
TRP CB  CG   sing N N 295 
TRP CB  HB2  sing N N 296 
TRP CB  HB3  sing N N 297 
TRP CG  CD1  doub Y N 298 
TRP CG  CD2  sing Y N 299 
TRP CD1 NE1  sing Y N 300 
TRP CD1 HD1  sing N N 301 
TRP CD2 CE2  doub Y N 302 
TRP CD2 CE3  sing Y N 303 
TRP NE1 CE2  sing Y N 304 
TRP NE1 HE1  sing N N 305 
TRP CE2 CZ2  sing Y N 306 
TRP CE3 CZ3  doub Y N 307 
TRP CE3 HE3  sing N N 308 
TRP CZ2 CH2  doub Y N 309 
TRP CZ2 HZ2  sing N N 310 
TRP CZ3 CH2  sing Y N 311 
TRP CZ3 HZ3  sing N N 312 
TRP CH2 HH2  sing N N 313 
TRP OXT HXT  sing N N 314 
TYR N   CA   sing N N 315 
TYR N   H    sing N N 316 
TYR N   H2   sing N N 317 
TYR CA  C    sing N N 318 
TYR CA  CB   sing N N 319 
TYR CA  HA   sing N N 320 
TYR C   O    doub N N 321 
TYR C   OXT  sing N N 322 
TYR CB  CG   sing N N 323 
TYR CB  HB2  sing N N 324 
TYR CB  HB3  sing N N 325 
TYR CG  CD1  doub Y N 326 
TYR CG  CD2  sing Y N 327 
TYR CD1 CE1  sing Y N 328 
TYR CD1 HD1  sing N N 329 
TYR CD2 CE2  doub Y N 330 
TYR CD2 HD2  sing N N 331 
TYR CE1 CZ   doub Y N 332 
TYR CE1 HE1  sing N N 333 
TYR CE2 CZ   sing Y N 334 
TYR CE2 HE2  sing N N 335 
TYR CZ  OH   sing N N 336 
TYR OH  HH   sing N N 337 
TYR OXT HXT  sing N N 338 
VAL N   CA   sing N N 339 
VAL N   H    sing N N 340 
VAL N   H2   sing N N 341 
VAL CA  C    sing N N 342 
VAL CA  CB   sing N N 343 
VAL CA  HA   sing N N 344 
VAL C   O    doub N N 345 
VAL C   OXT  sing N N 346 
VAL CB  CG1  sing N N 347 
VAL CB  CG2  sing N N 348 
VAL CB  HB   sing N N 349 
VAL CG1 HG11 sing N N 350 
VAL CG1 HG12 sing N N 351 
VAL CG1 HG13 sing N N 352 
VAL CG2 HG21 sing N N 353 
VAL CG2 HG22 sing N N 354 
VAL CG2 HG23 sing N N 355 
VAL OXT HXT  sing N N 356 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01GM102262 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4JZ4 
_pdbx_initial_refinement_model.details          'residues 86-140, hydrogens removed' 
# 
_pdbx_related_exp_data_set.ordinal              1 
_pdbx_related_exp_data_set.data_reference       10.15785/SBGRID/1158 
_pdbx_related_exp_data_set.metadata_reference   ? 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
# 
_atom_sites.entry_id                    9OFX 
_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]   0.015681 
_atom_sites.fract_transf_matrix[1][2]   0.009054 
_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]   0.018107 
_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]   0.003680 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NI 
O  
# 
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   . GLY A 1 1  ? 23.602  13.661 116.183 1.00 28.08  ? 85  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1  ? 22.580  12.690 115.841 1.00 28.12  ? 85  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1  ? 21.258  13.414 115.697 1.00 27.12  ? 85  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1  ? 21.245  14.639 115.636 1.00 26.00  ? 85  GLY A O   1 
ATOM   5    N  N   . VAL A 1 2  ? 20.149  12.677 115.640 1.00 27.97  ? 86  VAL A N   1 
ATOM   6    C  CA  . VAL A 1 2  ? 18.844  13.327 115.603 1.00 26.94  ? 86  VAL A CA  1 
ATOM   7    C  C   . VAL A 1 2  ? 18.577  13.964 116.955 1.00 27.31  ? 86  VAL A C   1 
ATOM   8    O  O   . VAL A 1 2  ? 18.864  13.373 118.004 1.00 30.97  ? 86  VAL A O   1 
ATOM   9    C  CB  . VAL A 1 2  ? 17.747  12.308 115.252 1.00 31.54  ? 86  VAL A CB  1 
ATOM   10   C  CG1 . VAL A 1 2  ? 17.814  11.136 116.201 1.00 38.08  ? 86  VAL A CG1 1 
ATOM   11   C  CG2 . VAL A 1 2  ? 16.347  12.961 115.286 1.00 31.07  ? 86  VAL A CG2 1 
ATOM   12   N  N   A THR A 1 3  ? 18.038  15.183 116.951 0.47 25.28  ? 87  THR A N   1 
ATOM   13   N  N   B THR A 1 3  ? 18.054  15.191 116.935 0.53 25.93  ? 87  THR A N   1 
ATOM   14   C  CA  A THR A 1 3  ? 17.673  15.839 118.199 0.47 26.32  ? 87  THR A CA  1 
ATOM   15   C  CA  B THR A 1 3  ? 17.636  15.837 118.167 0.53 27.67  ? 87  THR A CA  1 
ATOM   16   C  C   A THR A 1 3  ? 16.247  15.446 118.567 0.47 25.45  ? 87  THR A C   1 
ATOM   17   C  C   B THR A 1 3  ? 16.250  15.334 118.533 0.53 26.04  ? 87  THR A C   1 
ATOM   18   O  O   A THR A 1 3  ? 15.334  15.543 117.739 0.47 24.80  ? 87  THR A O   1 
ATOM   19   O  O   B THR A 1 3  ? 15.361  15.257 117.678 0.53 24.86  ? 87  THR A O   1 
ATOM   20   C  CB  A THR A 1 3  ? 17.806  17.358 118.093 0.47 30.02  ? 87  THR A CB  1 
ATOM   21   C  CB  B THR A 1 3  ? 17.587  17.350 118.003 0.53 32.32  ? 87  THR A CB  1 
ATOM   22   O  OG1 A THR A 1 3  ? 16.917  17.851 117.086 0.47 29.93  ? 87  THR A OG1 1 
ATOM   23   O  OG1 B THR A 1 3  ? 18.689  17.793 117.205 0.53 34.45  ? 87  THR A OG1 1 
ATOM   24   C  CG2 A THR A 1 3  ? 19.237  17.742 117.741 0.47 31.40  ? 87  THR A CG2 1 
ATOM   25   C  CG2 B THR A 1 3  ? 17.674  17.988 119.367 0.53 33.44  ? 87  THR A CG2 1 
ATOM   26   N  N   . THR A 1 4  ? 16.065  14.982 119.801 1.00 27.96  ? 88  THR A N   1 
ATOM   27   C  CA  . THR A 1 4  ? 14.810  14.399 120.241 1.00 29.54  ? 88  THR A CA  1 
ATOM   28   C  C   . THR A 1 4  ? 14.437  14.945 121.609 1.00 27.70  ? 88  THR A C   1 
ATOM   29   O  O   . THR A 1 4  ? 15.240  15.583 122.294 1.00 28.59  ? 88  THR A O   1 
ATOM   30   C  CB  . THR A 1 4  ? 14.918  12.877 120.350 1.00 30.10  ? 88  THR A CB  1 
ATOM   31   O  OG1 . THR A 1 4  ? 15.994  12.540 121.240 1.00 31.19  ? 88  THR A OG1 1 
ATOM   32   C  CG2 . THR A 1 4  ? 15.163  12.229 118.987 1.00 33.84  ? 88  THR A CG2 1 
ATOM   33   N  N   . PHE A 1 5  ? 13.200  14.664 121.996 1.00 26.83  ? 89  PHE A N   1 
ATOM   34   C  CA  . PHE A 1 5  ? 12.724  14.789 123.359 1.00 28.32  ? 89  PHE A CA  1 
ATOM   35   C  C   . PHE A 1 5  ? 12.475  13.396 123.922 1.00 28.51  ? 89  PHE A C   1 
ATOM   36   O  O   . PHE A 1 5  ? 12.420  12.406 123.190 1.00 27.76  ? 89  PHE A O   1 
ATOM   37   C  CB  . PHE A 1 5  ? 11.429  15.606 123.404 1.00 26.97  ? 89  PHE A CB  1 
ATOM   38   C  CG  . PHE A 1 5  ? 11.649  17.088 123.337 1.00 26.58  ? 89  PHE A CG  1 
ATOM   39   C  CD1 . PHE A 1 5  ? 12.136  17.667 122.185 1.00 28.58  ? 89  PHE A CD1 1 
ATOM   40   C  CD2 . PHE A 1 5  ? 11.365  17.896 124.426 1.00 30.51  ? 89  PHE A CD2 1 
ATOM   41   C  CE1 . PHE A 1 5  ? 12.342  19.028 122.114 1.00 30.11  ? 89  PHE A CE1 1 
ATOM   42   C  CE2 . PHE A 1 5  ? 11.575  19.269 124.368 1.00 30.99  ? 89  PHE A CE2 1 
ATOM   43   C  CZ  . PHE A 1 5  ? 12.058  19.831 123.212 1.00 28.92  ? 89  PHE A CZ  1 
ATOM   44   N  N   . VAL A 1 6  ? 12.345  13.320 125.244 1.00 26.23  ? 90  VAL A N   1 
ATOM   45   C  CA  . VAL A 1 6  ? 12.048  12.070 125.931 1.00 27.65  ? 90  VAL A CA  1 
ATOM   46   C  C   . VAL A 1 6  ? 10.781  12.260 126.754 1.00 25.77  ? 90  VAL A C   1 
ATOM   47   O  O   . VAL A 1 6  ? 10.578  13.315 127.362 1.00 30.04  ? 90  VAL A O   1 
ATOM   48   C  CB  . VAL A 1 6  ? 13.229  11.613 126.816 1.00 31.83  ? 90  VAL A CB  1 
ATOM   49   C  CG1 . VAL A 1 6  ? 13.585  12.686 127.842 1.00 34.83  ? 90  VAL A CG1 1 
ATOM   50   C  CG2 . VAL A 1 6  ? 12.912  10.294 127.503 1.00 29.61  ? 90  VAL A CG2 1 
ATOM   51   N  N   . ALA A 1 7  ? 9.926   11.238 126.768 1.00 24.35  ? 91  ALA A N   1 
ATOM   52   C  CA  . ALA A 1 7  ? 8.696   11.301 127.547 1.00 22.80  ? 91  ALA A CA  1 
ATOM   53   C  C   . ALA A 1 7  ? 8.994   11.196 129.039 1.00 26.13  ? 91  ALA A C   1 
ATOM   54   O  O   . ALA A 1 7  ? 9.711   10.290 129.482 1.00 27.13  ? 91  ALA A O   1 
ATOM   55   C  CB  . ALA A 1 7  ? 7.762   10.173 127.132 1.00 24.64  ? 91  ALA A CB  1 
ATOM   56   N  N   . LEU A 1 8  ? 8.444   12.141 129.806 1.00 28.17  ? 92  LEU A N   1 
ATOM   57   C  CA  . LEU A 1 8  ? 8.540   12.113 131.259 1.00 28.70  ? 92  LEU A CA  1 
ATOM   58   C  C   . LEU A 1 8  ? 7.499   11.207 131.899 1.00 30.05  ? 92  LEU A C   1 
ATOM   59   O  O   . LEU A 1 8  ? 7.720   10.737 133.022 1.00 31.85  ? 92  LEU A O   1 
ATOM   60   C  CB  . LEU A 1 8  ? 8.381   13.529 131.814 1.00 32.56  ? 92  LEU A CB  1 
ATOM   61   C  CG  . LEU A 1 8  ? 9.394   14.567 131.338 1.00 32.29  ? 92  LEU A CG  1 
ATOM   62   C  CD1 . LEU A 1 8  ? 8.955   15.969 131.734 1.00 35.07  ? 92  LEU A CD1 1 
ATOM   63   C  CD2 . LEU A 1 8  ? 10.766  14.243 131.914 1.00 39.02  ? 92  LEU A CD2 1 
ATOM   64   N  N   . TYR A 1 9  ? 6.399   10.933 131.198 1.00 29.96  ? 93  TYR A N   1 
ATOM   65   C  CA  . TYR A 1 9  ? 5.275   10.168 131.712 1.00 30.52  ? 93  TYR A CA  1 
ATOM   66   C  C   . TYR A 1 9  ? 4.640   9.411  130.557 1.00 26.53  ? 93  TYR A C   1 
ATOM   67   O  O   . TYR A 1 9  ? 4.776   9.800  129.388 1.00 27.07  ? 93  TYR A O   1 
ATOM   68   C  CB  . TYR A 1 9  ? 4.203   11.101 132.274 1.00 34.64  ? 93  TYR A CB  1 
ATOM   69   C  CG  . TYR A 1 9  ? 4.718   12.067 133.309 1.00 36.50  ? 93  TYR A CG  1 
ATOM   70   C  CD1 . TYR A 1 9  ? 4.882   11.667 134.622 1.00 39.86  ? 93  TYR A CD1 1 
ATOM   71   C  CD2 . TYR A 1 9  ? 5.046   13.375 132.973 1.00 39.10  ? 93  TYR A CD2 1 
ATOM   72   C  CE1 . TYR A 1 9  ? 5.337   12.543 135.581 1.00 42.17  ? 93  TYR A CE1 1 
ATOM   73   C  CE2 . TYR A 1 9  ? 5.522   14.260 133.927 1.00 41.74  ? 93  TYR A CE2 1 
ATOM   74   C  CZ  . TYR A 1 9  ? 5.662   13.835 135.232 1.00 45.53  ? 93  TYR A CZ  1 
ATOM   75   O  OH  . TYR A 1 9  ? 6.125   14.682 136.220 1.00 48.48  ? 93  TYR A OH  1 
ATOM   76   N  N   . ASP A 1 10 ? 3.919   8.342  130.901 1.00 25.72  ? 94  ASP A N   1 
ATOM   77   C  CA  . ASP A 1 10 ? 3.021   7.696  129.948 1.00 25.85  ? 94  ASP A CA  1 
ATOM   78   C  C   . ASP A 1 10 ? 1.930   8.675  129.536 1.00 25.48  ? 94  ASP A C   1 
ATOM   79   O  O   . ASP A 1 10 ? 1.454   9.483  130.337 1.00 27.93  ? 94  ASP A O   1 
ATOM   80   C  CB  . ASP A 1 10 ? 2.305   6.503  130.602 1.00 29.67  ? 94  ASP A CB  1 
ATOM   81   C  CG  . ASP A 1 10 ? 3.237   5.362  130.979 1.00 33.75  ? 94  ASP A CG  1 
ATOM   82   O  OD1 . ASP A 1 10 ? 4.424   5.359  130.588 1.00 32.04  ? 94  ASP A OD1 1 
ATOM   83   O  OD2 . ASP A 1 10 ? 2.759   4.437  131.678 1.00 38.41  ? 94  ASP A OD2 1 
ATOM   84   N  N   . TYR A 1 11 ? 1.497   8.568  128.284 1.00 24.63  ? 95  TYR A N   1 
ATOM   85   C  CA  . TYR A 1 11 ? 0.340   9.318  127.815 1.00 22.48  ? 95  TYR A CA  1 
ATOM   86   C  C   . TYR A 1 11 ? -0.527  8.398  126.974 1.00 22.46  ? 95  TYR A C   1 
ATOM   87   O  O   . TYR A 1 11 ? -0.034  7.776  126.033 1.00 24.99  ? 95  TYR A O   1 
ATOM   88   C  CB  . TYR A 1 11 ? 0.771   10.547 127.006 1.00 22.31  ? 95  TYR A CB  1 
ATOM   89   C  CG  . TYR A 1 11 ? -0.397  11.296 126.418 1.00 22.65  ? 95  TYR A CG  1 
ATOM   90   C  CD1 . TYR A 1 11 ? -1.235  12.050 127.226 1.00 24.75  ? 95  TYR A CD1 1 
ATOM   91   C  CD2 . TYR A 1 11 ? -0.682  11.242 125.050 1.00 22.42  ? 95  TYR A CD2 1 
ATOM   92   C  CE1 . TYR A 1 11 ? -2.319  12.727 126.701 1.00 24.13  ? 95  TYR A CE1 1 
ATOM   93   C  CE2 . TYR A 1 11 ? -1.765  11.924 124.518 1.00 21.57  ? 95  TYR A CE2 1 
ATOM   94   C  CZ  . TYR A 1 11 ? -2.587  12.662 125.352 1.00 21.56  ? 95  TYR A CZ  1 
ATOM   95   O  OH  . TYR A 1 11 ? -3.683  13.340 124.845 1.00 23.97  ? 95  TYR A OH  1 
ATOM   96   N  N   . GLU A 1 12 ? -1.807  8.298  127.318 1.00 23.42  ? 96  GLU A N   1 
ATOM   97   C  CA  . GLU A 1 12 ? -2.761  7.499  126.560 1.00 24.58  ? 96  GLU A CA  1 
ATOM   98   C  C   . GLU A 1 12 ? -3.548  8.392  125.612 1.00 23.07  ? 96  GLU A C   1 
ATOM   99   O  O   . GLU A 1 12 ? -4.018  9.466  125.998 1.00 25.64  ? 96  GLU A O   1 
ATOM   100  C  CB  . GLU A 1 12 ? -3.736  6.771  127.489 1.00 27.54  ? 96  GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 12 ? -3.151  5.521  128.112 1.00 38.03  ? 96  GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 12 ? -2.428  5.807  129.399 1.00 49.55  ? 96  GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 12 ? -2.889  6.699  130.143 1.00 54.83  ? 96  GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 12 ? -1.400  5.144  129.668 1.00 52.47  ? 96  GLU A OE2 1 
ATOM   105  N  N   . SER A 1 13 ? -3.731  7.915  124.381 1.00 25.07  ? 97  SER A N   1 
ATOM   106  C  CA  . SER A 1 13 ? -4.456  8.682  123.380 1.00 25.07  ? 97  SER A CA  1 
ATOM   107  C  C   . SER A 1 13 ? -5.908  8.896  123.798 1.00 23.69  ? 97  SER A C   1 
ATOM   108  O  O   . SER A 1 13 ? -6.585  7.975  124.272 1.00 26.11  ? 97  SER A O   1 
ATOM   109  C  CB  . SER A 1 13 ? -4.415  7.927  122.049 1.00 27.13  ? 97  SER A CB  1 
ATOM   110  O  OG  . SER A 1 13 ? -5.364  8.471  121.140 1.00 26.70  ? 97  SER A OG  1 
ATOM   111  N  N   . ARG A 1 14 ? -6.392  10.122 123.594 1.00 23.55  ? 98  ARG A N   1 
ATOM   112  C  CA  . ARG A 1 14 ? -7.764  10.503 123.882 1.00 26.11  ? 98  ARG A CA  1 
ATOM   113  C  C   . ARG A 1 14 ? -8.506  11.007 122.663 1.00 23.86  ? 98  ARG A C   1 
ATOM   114  O  O   . ARG A 1 14 ? -9.706  11.282 122.766 1.00 25.83  ? 98  ARG A O   1 
ATOM   115  C  CB  . ARG A 1 14 ? -7.787  11.633 124.921 1.00 25.95  ? 98  ARG A CB  1 
ATOM   116  C  CG  . ARG A 1 14 ? -7.089  11.294 126.228 1.00 27.02  ? 98  ARG A CG  1 
ATOM   117  C  CD  . ARG A 1 14 ? -7.920  10.336 127.068 1.00 28.35  ? 98  ARG A CD  1 
ATOM   118  N  NE  . ARG A 1 14 ? -7.728  8.944  126.682 1.00 29.41  ? 98  ARG A NE  1 
ATOM   119  C  CZ  . ARG A 1 14 ? -8.192  7.914  127.378 1.00 30.19  ? 98  ARG A CZ  1 
ATOM   120  N  NH1 . ARG A 1 14 ? -8.882  8.092  128.493 1.00 33.42  ? 98  ARG A NH1 1 
ATOM   121  N  NH2 . ARG A 1 14 ? -7.950  6.678  126.951 1.00 30.70  ? 98  ARG A NH2 1 
ATOM   122  N  N   . THR A 1 15 ? -7.824  11.187 121.531 1.00 23.13  ? 99  THR A N   1 
ATOM   123  C  CA  . THR A 1 15 ? -8.420  11.813 120.357 1.00 24.16  ? 99  THR A CA  1 
ATOM   124  C  C   . THR A 1 15 ? -7.982  11.043 119.118 1.00 22.17  ? 99  THR A C   1 
ATOM   125  O  O   . THR A 1 15 ? -7.174  10.111 119.188 1.00 24.01  ? 99  THR A O   1 
ATOM   126  C  CB  . THR A 1 15 ? -8.040  13.300 120.225 1.00 23.17  ? 99  THR A CB  1 
ATOM   127  O  OG1 . THR A 1 15 ? -6.729  13.415 119.669 1.00 25.35  ? 99  THR A OG1 1 
ATOM   128  C  CG2 . THR A 1 15 ? -8.038  14.002 121.579 1.00 23.62  ? 99  THR A CG2 1 
ATOM   129  N  N   . GLU A 1 16 ? -8.526  11.448 117.968 1.00 24.07  ? 100 GLU A N   1 
ATOM   130  C  CA  . GLU A 1 16 ? -8.143  10.840 116.704 1.00 23.89  ? 100 GLU A CA  1 
ATOM   131  C  C   . GLU A 1 16 ? -6.721  11.210 116.292 1.00 22.84  ? 100 GLU A C   1 
ATOM   132  O  O   . GLU A 1 16 ? -6.110  10.480 115.503 1.00 27.10  ? 100 GLU A O   1 
ATOM   133  C  CB  . GLU A 1 16 ? -9.157  11.218 115.622 1.00 25.28  ? 100 GLU A CB  1 
ATOM   134  C  CG  . GLU A 1 16 ? -10.557 10.745 115.988 1.00 31.84  ? 100 GLU A CG  1 
ATOM   135  C  CD  . GLU A 1 16 ? -11.605 11.039 114.938 1.00 43.22  ? 100 GLU A CD  1 
ATOM   136  O  OE1 . GLU A 1 16 ? -11.248 11.431 113.808 1.00 49.13  ? 100 GLU A OE1 1 
ATOM   137  O  OE2 . GLU A 1 16 ? -12.799 10.872 115.256 1.00 43.94  ? 100 GLU A OE2 1 
ATOM   138  N  N   . THR A 1 17 ? -6.164  12.306 116.823 1.00 20.19  ? 101 THR A N   1 
ATOM   139  C  CA  . THR A 1 17 ? -4.909  12.823 116.309 1.00 19.03  ? 101 THR A CA  1 
ATOM   140  C  C   . THR A 1 17 ? -3.777  12.882 117.323 1.00 20.48  ? 101 THR A C   1 
ATOM   141  O  O   . THR A 1 17 ? -2.656  13.206 116.932 1.00 20.78  ? 101 THR A O   1 
ATOM   142  C  CB  . THR A 1 17 ? -5.099  14.230 115.733 1.00 21.28  ? 101 THR A CB  1 
ATOM   143  O  OG1 . THR A 1 17 ? -5.668  15.060 116.746 1.00 20.86  ? 101 THR A OG1 1 
ATOM   144  C  CG2 . THR A 1 17 ? -6.014  14.198 114.528 1.00 23.08  ? 101 THR A CG2 1 
ATOM   145  N  N   . ASP A 1 18 ? -4.022  12.607 118.601 1.00 19.73  ? 102 ASP A N   1 
ATOM   146  C  CA  . ASP A 1 18 ? -2.922  12.624 119.550 1.00 21.07  ? 102 ASP A CA  1 
ATOM   147  C  C   . ASP A 1 18 ? -2.108  11.335 119.448 1.00 20.26  ? 102 ASP A C   1 
ATOM   148  O  O   . ASP A 1 18 ? -2.506  10.364 118.799 1.00 21.88  ? 102 ASP A O   1 
ATOM   149  C  CB  . ASP A 1 18 ? -3.386  12.954 120.975 1.00 20.53  ? 102 ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 18 ? -4.361  11.936 121.555 1.00 22.34  ? 102 ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 18 ? -4.796  10.999 120.845 1.00 25.21  ? 102 ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 18 ? -4.707  12.096 122.738 1.00 23.91  ? 102 ASP A OD2 1 
ATOM   153  N  N   . LEU A 1 19 ? -0.925  11.359 120.051 1.00 19.65  ? 103 LEU A N   1 
ATOM   154  C  CA  . LEU A 1 19 ? 0.036   10.268 119.980 1.00 19.51  ? 103 LEU A CA  1 
ATOM   155  C  C   . LEU A 1 19 ? 0.205   9.712  121.383 1.00 19.66  ? 103 LEU A C   1 
ATOM   156  O  O   . LEU A 1 19 ? 0.592   10.448 122.298 1.00 21.26  ? 103 LEU A O   1 
ATOM   157  C  CB  . LEU A 1 19 ? 1.387   10.792 119.476 1.00 19.81  ? 103 LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 19 ? 2.568   9.819  119.516 1.00 19.93  ? 103 LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 19 ? 2.343   8.677  118.511 1.00 22.36  ? 103 LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 19 ? 3.867   10.551 119.209 1.00 20.79  ? 103 LEU A CD2 1 
ATOM   161  N  N   . SER A 1 20 ? -0.103  8.431  121.562 1.00 20.04  ? 104 SER A N   1 
ATOM   162  C  CA  . SER A 1 20 ? 0.227   7.797  122.830 1.00 20.77  ? 104 SER A CA  1 
ATOM   163  C  C   . SER A 1 20 ? 1.718   7.466  122.895 1.00 22.40  ? 104 SER A C   1 
ATOM   164  O  O   . SER A 1 20 ? 2.377   7.235  121.875 1.00 22.74  ? 104 SER A O   1 
ATOM   165  C  CB  . SER A 1 20 ? -0.576  6.515  123.021 1.00 24.68  ? 104 SER A CB  1 
ATOM   166  O  OG  . SER A 1 20 ? -0.267  5.593  122.002 1.00 27.72  ? 104 SER A OG  1 
ATOM   167  N  N   . PHE A 1 21 ? 2.245   7.427  124.115 1.00 20.59  ? 105 PHE A N   1 
ATOM   168  C  CA  . PHE A 1 21 ? 3.645   7.080  124.315 1.00 21.97  ? 105 PHE A CA  1 
ATOM   169  C  C   . PHE A 1 21 ? 3.838   6.649  125.759 1.00 22.36  ? 105 PHE A C   1 
ATOM   170  O  O   . PHE A 1 21 ? 2.974   6.873  126.607 1.00 24.16  ? 105 PHE A O   1 
ATOM   171  C  CB  . PHE A 1 21 ? 4.576   8.246  123.953 1.00 21.37  ? 105 PHE A CB  1 
ATOM   172  C  CG  . PHE A 1 21 ? 4.198   9.559  124.586 1.00 21.56  ? 105 PHE A CG  1 
ATOM   173  C  CD1 . PHE A 1 21 ? 4.641   9.877  125.863 1.00 22.88  ? 105 PHE A CD1 1 
ATOM   174  C  CD2 . PHE A 1 21 ? 3.418   10.479 123.899 1.00 20.51  ? 105 PHE A CD2 1 
ATOM   175  C  CE1 . PHE A 1 21 ? 4.327   11.085 126.446 1.00 24.51  ? 105 PHE A CE1 1 
ATOM   176  C  CE2 . PHE A 1 21 ? 3.075   11.696 124.479 1.00 21.07  ? 105 PHE A CE2 1 
ATOM   177  C  CZ  . PHE A 1 21 ? 3.529   12.002 125.761 1.00 23.47  ? 105 PHE A CZ  1 
ATOM   178  N  N   . LYS A 1 22 ? 4.972   6.004  126.018 1.00 23.35  ? 106 LYS A N   1 
ATOM   179  C  CA  . LYS A 1 22 ? 5.324   5.560  127.356 1.00 24.22  ? 106 LYS A CA  1 
ATOM   180  C  C   . LYS A 1 22 ? 6.467   6.409  127.889 1.00 24.30  ? 106 LYS A C   1 
ATOM   181  O  O   . LYS A 1 22 ? 7.272   6.943  127.123 1.00 26.43  ? 106 LYS A O   1 
ATOM   182  C  CB  . LYS A 1 22 ? 5.769   4.096  127.338 1.00 25.75  ? 106 LYS A CB  1 
ATOM   183  C  CG  . LYS A 1 22 ? 4.698   3.133  126.877 1.00 30.07  ? 106 LYS A CG  1 
ATOM   184  C  CD  . LYS A 1 22 ? 3.558   3.092  127.891 1.00 35.03  ? 106 LYS A CD  1 
ATOM   185  C  CE  . LYS A 1 22 ? 2.478   2.103  127.485 1.00 43.36  ? 106 LYS A CE  1 
ATOM   186  N  NZ  . LYS A 1 22 ? 1.340   2.140  128.456 1.00 48.95  ? 106 LYS A NZ  1 
ATOM   187  N  N   . LYS A 1 23 ? 6.553   6.502  129.216 1.00 26.71  ? 107 LYS A N   1 
ATOM   188  C  CA  . LYS A 1 23 ? 7.681   7.177  129.842 1.00 26.83  ? 107 LYS A CA  1 
ATOM   189  C  C   . LYS A 1 23 ? 8.997   6.622  129.305 1.00 28.49  ? 107 LYS A C   1 
ATOM   190  O  O   . LYS A 1 23 ? 9.162   5.410  129.149 1.00 29.43  ? 107 LYS A O   1 
ATOM   191  C  CB  . LYS A 1 23 ? 7.619   6.998  131.364 1.00 31.17  ? 107 LYS A CB  1 
ATOM   192  C  CG  . LYS A 1 23 ? 8.764   7.684  132.101 1.00 34.20  ? 107 LYS A CG  1 
ATOM   193  C  CD  . LYS A 1 23 ? 8.580   7.677  133.613 1.00 41.27  ? 107 LYS A CD  1 
ATOM   194  C  CE  . LYS A 1 23 ? 9.811   8.262  134.314 1.00 46.80  ? 107 LYS A CE  1 
ATOM   195  N  NZ  . LYS A 1 23 ? 10.148  9.653  133.850 1.00 48.12  ? 107 LYS A NZ  1 
ATOM   196  N  N   . GLY A 1 24 ? 9.922   7.529  128.987 1.00 25.53  ? 108 GLY A N   1 
ATOM   197  C  CA  . GLY A 1 24 ? 11.212  7.173  128.442 1.00 26.33  ? 108 GLY A CA  1 
ATOM   198  C  C   . GLY A 1 24 ? 11.261  7.024  126.938 1.00 24.34  ? 108 GLY A C   1 
ATOM   199  O  O   . GLY A 1 24 ? 12.359  6.914  126.379 1.00 26.82  ? 108 GLY A O   1 
ATOM   200  N  N   . GLU A 1 25 ? 10.116  7.055  126.259 1.00 25.09  ? 109 GLU A N   1 
ATOM   201  C  CA  . GLU A 1 25 ? 10.096  6.896  124.812 1.00 24.07  ? 109 GLU A CA  1 
ATOM   202  C  C   . GLU A 1 25 ? 10.725  8.120  124.155 1.00 23.77  ? 109 GLU A C   1 
ATOM   203  O  O   . GLU A 1 25 ? 10.547  9.252  124.622 1.00 24.34  ? 109 GLU A O   1 
ATOM   204  C  CB  . GLU A 1 25 ? 8.652   6.714  124.349 1.00 25.28  ? 109 GLU A CB  1 
ATOM   205  C  CG  . GLU A 1 25 ? 8.449   6.295  122.895 1.00 25.42  ? 109 GLU A CG  1 
ATOM   206  C  CD  . GLU A 1 25 ? 7.031   5.807  122.630 1.00 24.18  ? 109 GLU A CD  1 
ATOM   207  O  OE1 . GLU A 1 25 ? 6.427   5.143  123.511 1.00 24.76  ? 109 GLU A OE1 1 
ATOM   208  O  OE2 . GLU A 1 25 ? 6.511   6.091  121.536 1.00 24.21  ? 109 GLU A OE2 1 
ATOM   209  N  N   . ARG A 1 26 ? 11.478  7.889  123.076 1.00 24.49  ? 110 ARG A N   1 
ATOM   210  C  CA  . ARG A 1 26 ? 12.155  8.960  122.351 1.00 22.03  ? 110 ARG A CA  1 
ATOM   211  C  C   . ARG A 1 26 ? 11.254  9.460  121.228 1.00 22.89  ? 110 ARG A C   1 
ATOM   212  O  O   . ARG A 1 26 ? 10.750  8.666  120.423 1.00 23.71  ? 110 ARG A O   1 
ATOM   213  C  CB  . ARG A 1 26 ? 13.496  8.485  121.788 1.00 28.20  ? 110 ARG A CB  1 
ATOM   214  C  CG  . ARG A 1 26 ? 14.639  8.561  122.800 1.00 36.03  ? 110 ARG A CG  1 
ATOM   215  C  CD  . ARG A 1 26 ? 15.903  7.816  122.344 1.00 41.98  ? 110 ARG A CD  1 
ATOM   216  N  NE  . ARG A 1 26 ? 16.170  7.950  120.916 1.00 48.26  ? 110 ARG A NE  1 
ATOM   217  C  CZ  . ARG A 1 26 ? 17.088  8.752  120.392 1.00 51.74  ? 110 ARG A CZ  1 
ATOM   218  N  NH1 . ARG A 1 26 ? 17.816  9.556  121.151 1.00 52.98  ? 110 ARG A NH1 1 
ATOM   219  N  NH2 . ARG A 1 26 ? 17.289  8.737  119.076 1.00 51.50  ? 110 ARG A NH2 1 
ATOM   220  N  N   . LEU A 1 27 ? 11.052  10.776 121.185 1.00 23.44  ? 111 LEU A N   1 
ATOM   221  C  CA  . LEU A 1 27 ? 10.126  11.410 120.255 1.00 21.22  ? 111 LEU A CA  1 
ATOM   222  C  C   . LEU A 1 27 ? 10.857  12.496 119.484 1.00 21.18  ? 111 LEU A C   1 
ATOM   223  O  O   . LEU A 1 27 ? 11.501  13.361 120.084 1.00 27.10  ? 111 LEU A O   1 
ATOM   224  C  CB  . LEU A 1 27 ? 8.984   12.076 121.028 1.00 22.57  ? 111 LEU A CB  1 
ATOM   225  C  CG  . LEU A 1 27 ? 8.153   11.202 121.968 1.00 22.42  ? 111 LEU A CG  1 
ATOM   226  C  CD1 . LEU A 1 27 ? 7.129   12.072 122.700 1.00 24.16  ? 111 LEU A CD1 1 
ATOM   227  C  CD2 . LEU A 1 27 ? 7.477   10.064 121.218 1.00 23.83  ? 111 LEU A CD2 1 
ATOM   228  N  N   . GLN A 1 28 ? 10.718  12.481 118.165 1.00 19.85  ? 112 GLN A N   1 
ATOM   229  C  CA  . GLN A 1 28 ? 11.216  13.567 117.337 1.00 19.39  ? 112 GLN A CA  1 
ATOM   230  C  C   . GLN A 1 28 ? 10.099  14.594 117.175 1.00 19.26  ? 112 GLN A C   1 
ATOM   231  O  O   . GLN A 1 28 ? 8.980   14.240 116.808 1.00 20.79  ? 112 GLN A O   1 
ATOM   232  C  CB  . GLN A 1 28 ? 11.637  13.020 115.977 1.00 20.56  ? 112 GLN A CB  1 
ATOM   233  C  CG  . GLN A 1 28 ? 12.179  14.085 115.046 1.00 24.73  ? 112 GLN A CG  1 
ATOM   234  C  CD  . GLN A 1 28 ? 12.418  13.559 113.661 1.00 25.98  ? 112 GLN A CD  1 
ATOM   235  O  OE1 . GLN A 1 28 ? 12.318  12.352 113.417 1.00 29.97  ? 112 GLN A OE1 1 
ATOM   236  N  NE2 . GLN A 1 28 ? 12.736  14.454 112.735 1.00 24.53  ? 112 GLN A NE2 1 
ATOM   237  N  N   . ILE A 1 29 ? 10.377  15.854 117.489 1.00 19.75  ? 113 ILE A N   1 
ATOM   238  C  CA  . ILE A 1 29 ? 9.342   16.882 117.405 1.00 20.32  ? 113 ILE A CA  1 
ATOM   239  C  C   . ILE A 1 29 ? 9.345   17.467 115.998 1.00 19.12  ? 113 ILE A C   1 
ATOM   240  O  O   . ILE A 1 29 ? 10.370  17.967 115.529 1.00 21.77  ? 113 ILE A O   1 
ATOM   241  C  CB  . ILE A 1 29 ? 9.542   17.977 118.464 1.00 20.71  ? 113 ILE A CB  1 
ATOM   242  C  CG1 . ILE A 1 29 ? 9.578   17.369 119.870 1.00 23.61  ? 113 ILE A CG1 1 
ATOM   243  C  CG2 . ILE A 1 29 ? 8.441   19.035 118.360 1.00 21.63  ? 113 ILE A CG2 1 
ATOM   244  C  CD1 . ILE A 1 29 ? 8.375   16.516 120.205 1.00 24.70  ? 113 ILE A CD1 1 
ATOM   245  N  N   . VAL A 1 30 ? 8.194   17.404 115.330 1.00 19.75  ? 114 VAL A N   1 
ATOM   246  C  CA  . VAL A 1 30 ? 8.049   17.927 113.973 1.00 19.87  ? 114 VAL A CA  1 
ATOM   247  C  C   . VAL A 1 30 ? 7.592   19.381 113.983 1.00 21.30  ? 114 VAL A C   1 
ATOM   248  O  O   . VAL A 1 30 ? 8.059   20.188 113.174 1.00 22.37  ? 114 VAL A O   1 
ATOM   249  C  CB  . VAL A 1 30 ? 7.062   17.016 113.204 1.00 21.40  ? 114 VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 30 ? 6.739   17.580 111.829 1.00 23.98  ? 114 VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 30 ? 7.619   15.575 113.080 1.00 23.05  ? 114 VAL A CG2 1 
ATOM   252  N  N   . ASN A 1 31 ? 6.691   19.743 114.900 1.00 20.79  ? 115 ASN A N   1 
ATOM   253  C  CA  . ASN A 1 31 ? 6.176   21.107 114.979 1.00 21.12  ? 115 ASN A CA  1 
ATOM   254  C  C   . ASN A 1 31 ? 5.933   21.436 116.442 1.00 20.07  ? 115 ASN A C   1 
ATOM   255  O  O   . ASN A 1 31 ? 5.226   20.696 117.127 1.00 22.12  ? 115 ASN A O   1 
ATOM   256  C  CB  . ASN A 1 31 ? 4.844   21.205 114.232 1.00 21.54  ? 115 ASN A CB  1 
ATOM   257  C  CG  . ASN A 1 31 ? 4.264   22.581 114.262 1.00 27.35  ? 115 ASN A CG  1 
ATOM   258  O  OD1 . ASN A 1 31 ? 3.773   23.040 115.291 1.00 33.18  ? 115 ASN A OD1 1 
ATOM   259  N  ND2 . ASN A 1 31 ? 4.285   23.243 113.127 1.00 30.26  ? 115 ASN A ND2 1 
ATOM   260  N  N   . ASN A 1 32 ? 6.512   22.536 116.923 1.00 22.93  ? 116 ASN A N   1 
ATOM   261  C  CA  . ASN A 1 32 ? 6.261   22.949 118.300 1.00 23.30  ? 116 ASN A CA  1 
ATOM   262  C  C   . ASN A 1 32 ? 5.965   24.433 118.402 1.00 26.30  ? 116 ASN A C   1 
ATOM   263  O  O   . ASN A 1 32 ? 6.284   25.065 119.408 1.00 28.28  ? 116 ASN A O   1 
ATOM   264  C  CB  . ASN A 1 32 ? 7.382   22.548 119.262 1.00 25.13  ? 116 ASN A CB  1 
ATOM   265  C  CG  . ASN A 1 32 ? 8.738   22.990 118.809 1.00 30.69  ? 116 ASN A CG  1 
ATOM   266  O  OD1 . ASN A 1 32 ? 8.873   23.775 117.875 1.00 36.07  ? 116 ASN A OD1 1 
ATOM   267  N  ND2 . ASN A 1 32 ? 9.771   22.511 119.503 1.00 37.16  ? 116 ASN A ND2 1 
ATOM   268  N  N   . THR A 1 33 ? 5.335   25.000 117.388 1.00 28.01  ? 117 THR A N   1 
ATOM   269  C  CA  . THR A 1 33 ? 5.063   26.427 117.392 1.00 30.60  ? 117 THR A CA  1 
ATOM   270  C  C   . THR A 1 33 ? 3.637   26.763 117.819 1.00 29.14  ? 117 THR A C   1 
ATOM   271  O  O   . THR A 1 33 ? 3.323   27.945 118.003 1.00 34.30  ? 117 THR A O   1 
ATOM   272  C  CB  . THR A 1 33 ? 5.380   27.005 116.012 1.00 32.37  ? 117 THR A CB  1 
ATOM   273  O  OG1 . THR A 1 33 ? 4.701   26.235 115.011 1.00 35.75  ? 117 THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 33 ? 6.887   26.934 115.763 1.00 35.64  ? 117 THR A CG2 1 
ATOM   275  N  N   . GLU A 1 34 ? 2.782   25.762 118.024 1.00 31.14  ? 118 GLU A N   1 
ATOM   276  C  CA  . GLU A 1 34 ? 1.365   25.996 118.299 1.00 36.27  ? 118 GLU A CA  1 
ATOM   277  C  C   . GLU A 1 34 ? 1.033   25.740 119.768 1.00 39.89  ? 118 GLU A C   1 
ATOM   278  O  O   . GLU A 1 34 ? 0.194   24.897 120.110 1.00 49.70  ? 118 GLU A O   1 
ATOM   279  C  CB  . GLU A 1 34 ? 0.495   25.138 117.379 1.00 35.44  ? 118 GLU A CB  1 
ATOM   280  C  CG  . GLU A 1 34 ? 0.817   25.239 115.886 1.00 38.89  ? 118 GLU A CG  1 
ATOM   281  C  CD  . GLU A 1 34 ? 0.200   26.466 115.214 1.00 45.53  ? 118 GLU A CD  1 
ATOM   282  O  OE1 . GLU A 1 34 ? -0.230  27.398 115.935 1.00 43.20  ? 118 GLU A OE1 1 
ATOM   283  O  OE2 . GLU A 1 34 ? 0.137   26.494 113.963 1.00 48.70  ? 118 GLU A OE2 1 
ATOM   284  N  N   . GLY A 1 35 ? 1.701   26.475 120.647 1.00 34.08  ? 119 GLY A N   1 
ATOM   285  C  CA  . GLY A 1 35 ? 1.346   26.412 122.060 1.00 33.32  ? 119 GLY A CA  1 
ATOM   286  C  C   . GLY A 1 35 ? 1.752   25.094 122.700 1.00 29.76  ? 119 GLY A C   1 
ATOM   287  O  O   . GLY A 1 35 ? 2.858   24.580 122.480 1.00 32.30  ? 119 GLY A O   1 
ATOM   288  N  N   . ASP A 1 36 ? 0.833   24.531 123.491 1.00 28.85  ? 120 ASP A N   1 
ATOM   289  C  CA  . ASP A 1 36 ? 1.093   23.412 124.393 1.00 31.09  ? 120 ASP A CA  1 
ATOM   290  C  C   . ASP A 1 36 ? 0.942   22.039 123.746 1.00 26.25  ? 120 ASP A C   1 
ATOM   291  O  O   . ASP A 1 36 ? 1.173   21.028 124.414 1.00 29.42  ? 120 ASP A O   1 
ATOM   292  C  CB  . ASP A 1 36 ? 0.135   23.477 125.588 1.00 40.64  ? 120 ASP A CB  1 
ATOM   293  C  CG  . ASP A 1 36 ? 0.369   24.685 126.467 1.00 49.18  ? 120 ASP A CG  1 
ATOM   294  O  OD1 . ASP A 1 36 ? 1.487   25.240 126.438 1.00 50.33  ? 120 ASP A OD1 1 
ATOM   295  O  OD2 . ASP A 1 36 ? -0.570  25.070 127.194 1.00 55.03  ? 120 ASP A OD2 1 
ATOM   296  N  N   . TRP A 1 37 ? 0.529   21.969 122.489 1.00 21.69  ? 121 TRP A N   1 
ATOM   297  C  CA  . TRP A 1 37 ? 0.398   20.709 121.774 1.00 19.15  ? 121 TRP A CA  1 
ATOM   298  C  C   . TRP A 1 37 ? 1.385   20.714 120.620 1.00 20.27  ? 121 TRP A C   1 
ATOM   299  O  O   . TRP A 1 37 ? 1.318   21.584 119.745 1.00 23.77  ? 121 TRP A O   1 
ATOM   300  C  CB  . TRP A 1 37 ? -1.034  20.497 121.285 1.00 21.24  ? 121 TRP A CB  1 
ATOM   301  C  CG  . TRP A 1 37 ? -1.968  20.248 122.416 1.00 20.44  ? 121 TRP A CG  1 
ATOM   302  C  CD1 . TRP A 1 37 ? -2.700  21.180 123.112 1.00 21.92  ? 121 TRP A CD1 1 
ATOM   303  C  CD2 . TRP A 1 37 ? -2.249  18.985 123.020 1.00 20.11  ? 121 TRP A CD2 1 
ATOM   304  N  NE1 . TRP A 1 37 ? -3.422  20.570 124.103 1.00 24.41  ? 121 TRP A NE1 1 
ATOM   305  C  CE2 . TRP A 1 37 ? -3.180  19.219 124.059 1.00 23.34  ? 121 TRP A CE2 1 
ATOM   306  C  CE3 . TRP A 1 37 ? -1.848  17.669 122.750 1.00 21.73  ? 121 TRP A CE3 1 
ATOM   307  C  CZ2 . TRP A 1 37 ? -3.691  18.193 124.849 1.00 24.45  ? 121 TRP A CZ2 1 
ATOM   308  C  CZ3 . TRP A 1 37 ? -2.358  16.645 123.548 1.00 22.62  ? 121 TRP A CZ3 1 
ATOM   309  C  CH2 . TRP A 1 37 ? -3.274  16.916 124.580 1.00 22.49  ? 121 TRP A CH2 1 
ATOM   310  N  N   . TRP A 1 38 ? 2.293   19.748 120.625 1.00 19.15  ? 122 TRP A N   1 
ATOM   311  C  CA  . TRP A 1 38 ? 3.351   19.650 119.637 1.00 17.53  ? 122 TRP A CA  1 
ATOM   312  C  C   . TRP A 1 38 ? 3.111   18.426 118.772 1.00 16.94  ? 122 TRP A C   1 
ATOM   313  O  O   . TRP A 1 38 ? 2.585   17.415 119.240 1.00 20.24  ? 122 TRP A O   1 
ATOM   314  C  CB  . TRP A 1 38 ? 4.700   19.473 120.331 1.00 19.83  ? 122 TRP A CB  1 
ATOM   315  C  CG  . TRP A 1 38 ? 5.155   20.654 121.140 1.00 20.82  ? 122 TRP A CG  1 
ATOM   316  C  CD1 . TRP A 1 38 ? 4.536   21.872 121.271 1.00 22.42  ? 122 TRP A CD1 1 
ATOM   317  C  CD2 . TRP A 1 38 ? 6.354   20.727 121.900 1.00 22.06  ? 122 TRP A CD2 1 
ATOM   318  N  NE1 . TRP A 1 38 ? 5.285   22.688 122.079 1.00 23.60  ? 122 TRP A NE1 1 
ATOM   319  C  CE2 . TRP A 1 38 ? 6.407   22.008 122.478 1.00 22.82  ? 122 TRP A CE2 1 
ATOM   320  C  CE3 . TRP A 1 38 ? 7.395   19.826 122.148 1.00 23.13  ? 122 TRP A CE3 1 
ATOM   321  C  CZ2 . TRP A 1 38 ? 7.459   22.408 123.295 1.00 25.83  ? 122 TRP A CZ2 1 
ATOM   322  C  CZ3 . TRP A 1 38 ? 8.430   20.220 122.961 1.00 25.01  ? 122 TRP A CZ3 1 
ATOM   323  C  CH2 . TRP A 1 38 ? 8.456   21.500 123.530 1.00 26.31  ? 122 TRP A CH2 1 
ATOM   324  N  N   . LEU A 1 39 ? 3.483   18.511 117.501 1.00 18.08  ? 123 LEU A N   1 
ATOM   325  C  CA  . LEU A 1 39 ? 3.402   17.350 116.630 1.00 16.22  ? 123 LEU A CA  1 
ATOM   326  C  C   . LEU A 1 39 ? 4.698   16.558 116.773 1.00 16.70  ? 123 LEU A C   1 
ATOM   327  O  O   . LEU A 1 39 ? 5.791   17.109 116.565 1.00 18.04  ? 123 LEU A O   1 
ATOM   328  C  CB  . LEU A 1 39 ? 3.175   17.773 115.181 1.00 17.92  ? 123 LEU A CB  1 
ATOM   329  C  CG  . LEU A 1 39 ? 2.951   16.560 114.279 1.00 17.54  ? 123 LEU A CG  1 
ATOM   330  C  CD1 . LEU A 1 39 ? 1.634   15.889 114.561 1.00 20.27  ? 123 LEU A CD1 1 
ATOM   331  C  CD2 . LEU A 1 39 ? 3.011   16.963 112.821 1.00 20.96  ? 123 LEU A CD2 1 
ATOM   332  N  N   . ALA A 1 40 ? 4.574   15.277 117.120 1.00 16.62  ? 124 ALA A N   1 
ATOM   333  C  CA  . ALA A 1 40 ? 5.722   14.429 117.393 1.00 17.17  ? 124 ALA A CA  1 
ATOM   334  C  C   . ALA A 1 40 ? 5.660   13.159 116.556 1.00 17.50  ? 124 ALA A C   1 
ATOM   335  O  O   . ALA A 1 40 ? 4.583   12.710 116.167 1.00 17.75  ? 124 ALA A O   1 
ATOM   336  C  CB  . ALA A 1 40 ? 5.765   14.053 118.884 1.00 21.43  ? 124 ALA A CB  1 
ATOM   337  N  N   . HIS A 1 41 ? 6.834   12.585 116.286 1.00 17.05  ? 125 HIS A N   1 
ATOM   338  C  CA  . HIS A 1 41 ? 6.967   11.312 115.589 1.00 16.80  ? 125 HIS A CA  1 
ATOM   339  C  C   . HIS A 1 41 ? 7.727   10.386 116.531 1.00 18.31  ? 125 HIS A C   1 
ATOM   340  O  O   . HIS A 1 41 ? 8.847   10.705 116.950 1.00 19.24  ? 125 HIS A O   1 
ATOM   341  C  CB  . HIS A 1 41 ? 7.755   11.499 114.282 1.00 19.48  ? 125 HIS A CB  1 
ATOM   342  C  CG  . HIS A 1 41 ? 7.936   10.241 113.478 1.00 18.85  ? 125 HIS A CG  1 
ATOM   343  N  ND1 . HIS A 1 41 ? 6.900   9.637  112.806 1.00 21.60  ? 125 HIS A ND1 1 
ATOM   344  C  CD2 . HIS A 1 41 ? 9.043   9.500  113.211 1.00 20.08  ? 125 HIS A CD2 1 
ATOM   345  C  CE1 . HIS A 1 41 ? 7.354   8.564  112.175 1.00 22.74  ? 125 HIS A CE1 1 
ATOM   346  N  NE2 . HIS A 1 41 ? 8.659   8.456  112.395 1.00 22.08  ? 125 HIS A NE2 1 
ATOM   347  N  N   . SER A 1 42 ? 7.123   9.254  116.883 1.00 17.60  ? 126 SER A N   1 
ATOM   348  C  CA  . SER A 1 42 ? 7.757   8.366  117.846 1.00 18.33  ? 126 SER A CA  1 
ATOM   349  C  C   . SER A 1 42 ? 8.860   7.558  117.180 1.00 18.82  ? 126 SER A C   1 
ATOM   350  O  O   . SER A 1 42 ? 8.647   6.930  116.134 1.00 20.40  ? 126 SER A O   1 
ATOM   351  C  CB  . SER A 1 42 ? 6.743   7.414  118.461 1.00 20.67  ? 126 SER A CB  1 
ATOM   352  O  OG  . SER A 1 42 ? 7.432   6.424  119.203 1.00 20.74  ? 126 SER A OG  1 
ATOM   353  N  N   . LEU A 1 43 ? 10.033  7.546  117.808 1.00 18.79  ? 127 LEU A N   1 
ATOM   354  C  CA  . LEU A 1 43 ? 11.110  6.703  117.321 1.00 21.71  ? 127 LEU A CA  1 
ATOM   355  C  C   . LEU A 1 43 ? 10.982  5.265  117.798 1.00 22.97  ? 127 LEU A C   1 
ATOM   356  O  O   . LEU A 1 43 ? 11.764  4.417  117.365 1.00 27.77  ? 127 LEU A O   1 
ATOM   357  C  CB  . LEU A 1 43 ? 12.460  7.313  117.695 1.00 23.28  ? 127 LEU A CB  1 
ATOM   358  C  CG  . LEU A 1 43 ? 12.614  8.735  117.129 1.00 23.76  ? 127 LEU A CG  1 
ATOM   359  C  CD1 . LEU A 1 43 ? 13.985  9.286  117.459 1.00 27.24  ? 127 LEU A CD1 1 
ATOM   360  C  CD2 . LEU A 1 43 ? 12.392  8.774  115.633 1.00 26.31  ? 127 LEU A CD2 1 
ATOM   361  N  N   . SER A 1 44 ? 10.011  4.971  118.658 1.00 22.50  ? 128 SER A N   1 
ATOM   362  C  CA  . SER A 1 44 ? 9.683   3.592  119.014 1.00 22.82  ? 128 SER A CA  1 
ATOM   363  C  C   . SER A 1 44 ? 8.625   3.006  118.094 1.00 23.52  ? 128 SER A C   1 
ATOM   364  O  O   . SER A 1 44 ? 8.809   1.918  117.546 1.00 27.03  ? 128 SER A O   1 
ATOM   365  C  CB  . SER A 1 44 ? 9.142   3.523  120.446 1.00 26.74  ? 128 SER A CB  1 
ATOM   366  O  OG  . SER A 1 44 ? 10.204  3.365  121.362 1.00 27.86  ? 128 SER A OG  1 
ATOM   367  N  N   . THR A 1 45 ? 7.499   3.703  117.936 1.00 22.94  ? 129 THR A N   1 
ATOM   368  C  CA  . THR A 1 45 ? 6.351   3.113  117.261 1.00 23.76  ? 129 THR A CA  1 
ATOM   369  C  C   . THR A 1 45 ? 6.217   3.515  115.810 1.00 21.56  ? 129 THR A C   1 
ATOM   370  O  O   . THR A 1 45 ? 5.460   2.863  115.082 1.00 24.41  ? 129 THR A O   1 
ATOM   371  C  CB  . THR A 1 45 ? 5.050   3.492  117.972 1.00 22.43  ? 129 THR A CB  1 
ATOM   372  O  OG1 . THR A 1 45 ? 4.827   4.903  117.839 1.00 22.53  ? 129 THR A OG1 1 
ATOM   373  C  CG2 . THR A 1 45 ? 5.155   3.129  119.443 1.00 24.95  ? 129 THR A CG2 1 
ATOM   374  N  N   . GLY A 1 46 ? 6.898   4.578  115.378 1.00 21.45  ? 130 GLY A N   1 
ATOM   375  C  CA  . GLY A 1 46 ? 6.687   5.096  114.046 1.00 21.26  ? 130 GLY A CA  1 
ATOM   376  C  C   . GLY A 1 46 ? 5.406   5.869  113.861 1.00 20.15  ? 130 GLY A C   1 
ATOM   377  O  O   . GLY A 1 46 ? 5.112   6.282  112.731 1.00 24.53  ? 130 GLY A O   1 
ATOM   378  N  N   . GLN A 1 47 ? 4.630   6.076  114.918 1.00 20.97  ? 131 GLN A N   1 
ATOM   379  C  CA  . GLN A 1 47 ? 3.391   6.831  114.821 1.00 19.48  ? 131 GLN A CA  1 
ATOM   380  C  C   . GLN A 1 47 ? 3.663   8.326  114.980 1.00 18.87  ? 131 GLN A C   1 
ATOM   381  O  O   . GLN A 1 47 ? 4.680   8.747  115.533 1.00 19.79  ? 131 GLN A O   1 
ATOM   382  C  CB  . GLN A 1 47 ? 2.406   6.351  115.884 1.00 22.65  ? 131 GLN A CB  1 
ATOM   383  C  CG  . GLN A 1 47 ? 2.037   4.872  115.736 1.00 24.57  ? 131 GLN A CG  1 
ATOM   384  C  CD  . GLN A 1 47 ? 1.391   4.282  116.975 1.00 33.76  ? 131 GLN A CD  1 
ATOM   385  O  OE1 . GLN A 1 47 ? 1.253   4.943  118.002 1.00 36.57  ? 131 GLN A OE1 1 
ATOM   386  N  NE2 . GLN A 1 47 ? 1.001   3.019  116.884 1.00 38.95  ? 131 GLN A NE2 1 
ATOM   387  N  N   . THR A 1 48 ? 2.738   9.134  114.474 1.00 20.38  ? 132 THR A N   1 
ATOM   388  C  CA  . THR A 1 48 ? 2.869   10.583 114.504 1.00 19.31  ? 132 THR A CA  1 
ATOM   389  C  C   . THR A 1 48 ? 1.577   11.145 115.067 1.00 18.58  ? 132 THR A C   1 
ATOM   390  O  O   . THR A 1 48 ? 0.489   10.668 114.734 1.00 21.72  ? 132 THR A O   1 
ATOM   391  C  CB  . THR A 1 48 ? 3.077   11.118 113.068 1.00 19.00  ? 132 THR A CB  1 
ATOM   392  O  OG1 . THR A 1 48 ? 4.232   10.476 112.503 1.00 21.40  ? 132 THR A OG1 1 
ATOM   393  C  CG2 . THR A 1 48 ? 3.266   12.612 113.049 1.00 20.46  ? 132 THR A CG2 1 
ATOM   394  N  N   . GLY A 1 49 ? 1.694   12.136 115.934 1.00 18.35  ? 133 GLY A N   1 
ATOM   395  C  CA  . GLY A 1 49 ? 0.498   12.777 116.440 1.00 17.04  ? 133 GLY A CA  1 
ATOM   396  C  C   . GLY A 1 49 ? 0.849   13.851 117.435 1.00 17.04  ? 133 GLY A C   1 
ATOM   397  O  O   . GLY A 1 49 ? 2.015   14.069 117.767 1.00 17.60  ? 133 GLY A O   1 
ATOM   398  N  N   . TYR A 1 50 ? -0.193  14.495 117.950 1.00 16.47  ? 134 TYR A N   1 
ATOM   399  C  CA  . TYR A 1 50 ? -0.003  15.606 118.861 1.00 16.90  ? 134 TYR A CA  1 
ATOM   400  C  C   . TYR A 1 50 ? 0.269   15.102 120.266 1.00 17.57  ? 134 TYR A C   1 
ATOM   401  O  O   . TYR A 1 50 ? -0.331  14.117 120.725 1.00 18.15  ? 134 TYR A O   1 
ATOM   402  C  CB  . TYR A 1 50 ? -1.237  16.501 118.870 1.00 17.99  ? 134 TYR A CB  1 
ATOM   403  C  CG  . TYR A 1 50 ? -1.541  17.073 117.512 1.00 17.27  ? 134 TYR A CG  1 
ATOM   404  C  CD1 . TYR A 1 50 ? -0.627  17.905 116.867 1.00 18.47  ? 134 TYR A CD1 1 
ATOM   405  C  CD2 . TYR A 1 50 ? -2.736  16.791 116.875 1.00 18.65  ? 134 TYR A CD2 1 
ATOM   406  C  CE1 . TYR A 1 50 ? -0.879  18.409 115.624 1.00 18.61  ? 134 TYR A CE1 1 
ATOM   407  C  CE2 . TYR A 1 50 ? -3.018  17.330 115.624 1.00 20.57  ? 134 TYR A CE2 1 
ATOM   408  C  CZ  . TYR A 1 50 ? -2.084  18.132 115.005 1.00 19.65  ? 134 TYR A CZ  1 
ATOM   409  O  OH  . TYR A 1 50 ? -2.328  18.674 113.757 1.00 20.81  ? 134 TYR A OH  1 
ATOM   410  N  N   . ILE A 1 51 ? 1.187   15.778 120.946 1.00 18.08  ? 135 ILE A N   1 
ATOM   411  C  CA  . ILE A 1 51 ? 1.520   15.412 122.319 1.00 18.33  ? 135 ILE A CA  1 
ATOM   412  C  C   . ILE A 1 51 ? 1.407   16.631 123.221 1.00 20.01  ? 135 ILE A C   1 
ATOM   413  O  O   . ILE A 1 51 ? 1.645   17.774 122.786 1.00 20.94  ? 135 ILE A O   1 
ATOM   414  C  CB  . ILE A 1 51 ? 2.926   14.790 122.416 1.00 20.31  ? 135 ILE A CB  1 
ATOM   415  C  CG1 . ILE A 1 51 ? 3.990   15.808 121.990 1.00 20.74  ? 135 ILE A CG1 1 
ATOM   416  C  CG2 . ILE A 1 51 ? 3.021   13.532 121.549 1.00 20.25  ? 135 ILE A CG2 1 
ATOM   417  C  CD1 . ILE A 1 51 ? 5.388   15.423 122.437 1.00 25.08  ? 135 ILE A CD1 1 
ATOM   418  N  N   . PRO A 1 52 ? 1.050   16.433 124.486 1.00 20.80  ? 136 PRO A N   1 
ATOM   419  C  CA  . PRO A 1 52 ? 1.058   17.550 125.441 1.00 21.35  ? 136 PRO A CA  1 
ATOM   420  C  C   . PRO A 1 52 ? 2.498   17.893 125.791 1.00 22.82  ? 136 PRO A C   1 
ATOM   421  O  O   . PRO A 1 52 ? 3.254   17.038 126.261 1.00 27.83  ? 136 PRO A O   1 
ATOM   422  C  CB  . PRO A 1 52 ? 0.298   16.982 126.649 1.00 25.60  ? 136 PRO A CB  1 
ATOM   423  C  CG  . PRO A 1 52 ? 0.421   15.491 126.521 1.00 24.91  ? 136 PRO A CG  1 
ATOM   424  C  CD  . PRO A 1 52 ? 0.533   15.181 125.074 1.00 22.69  ? 136 PRO A CD  1 
ATOM   425  N  N   . SER A 1 53 ? 2.885   19.145 125.534 1.00 24.68  ? 137 SER A N   1 
ATOM   426  C  CA  . SER A 1 53 ? 4.299   19.501 125.602 1.00 28.69  ? 137 SER A CA  1 
ATOM   427  C  C   . SER A 1 53 ? 4.870   19.375 127.009 1.00 31.94  ? 137 SER A C   1 
ATOM   428  O  O   . SER A 1 53 ? 6.070   19.121 127.160 1.00 31.31  ? 137 SER A O   1 
ATOM   429  C  CB  . SER A 1 53 ? 4.539   20.889 125.016 1.00 30.46  ? 137 SER A CB  1 
ATOM   430  O  OG  . SER A 1 53 ? 3.978   21.897 125.828 1.00 30.20  ? 137 SER A OG  1 
ATOM   431  N  N   . ASN A 1 54 ? 4.036   19.518 128.045 1.00 30.39  ? 138 ASN A N   1 
ATOM   432  C  CA  . ASN A 1 54 ? 4.522   19.368 129.413 1.00 33.83  ? 138 ASN A CA  1 
ATOM   433  C  C   . ASN A 1 54 ? 4.856   17.925 129.785 1.00 31.01  ? 138 ASN A C   1 
ATOM   434  O  O   . ASN A 1 54 ? 5.412   17.701 130.864 1.00 36.38  ? 138 ASN A O   1 
ATOM   435  C  CB  . ASN A 1 54 ? 3.549   19.992 130.424 1.00 34.61  ? 138 ASN A CB  1 
ATOM   436  C  CG  . ASN A 1 54 ? 2.185   19.325 130.424 1.00 39.68  ? 138 ASN A CG  1 
ATOM   437  O  OD1 . ASN A 1 54 ? 1.665   18.941 129.379 1.00 37.29  ? 138 ASN A OD1 1 
ATOM   438  N  ND2 . ASN A 1 54 ? 1.588   19.204 131.606 1.00 45.93  ? 138 ASN A ND2 1 
ATOM   439  N  N   . TYR A 1 55 ? 4.559   16.947 128.925 1.00 28.80  ? 139 TYR A N   1 
ATOM   440  C  CA  . TYR A 1 55 ? 4.899   15.558 129.207 1.00 27.11  ? 139 TYR A CA  1 
ATOM   441  C  C   . TYR A 1 55 ? 6.286   15.165 128.727 1.00 31.06  ? 139 TYR A C   1 
ATOM   442  O  O   . TYR A 1 55 ? 6.663   14.004 128.900 1.00 29.57  ? 139 TYR A O   1 
ATOM   443  C  CB  . TYR A 1 55 ? 3.908   14.607 128.541 1.00 27.38  ? 139 TYR A CB  1 
ATOM   444  C  CG  . TYR A 1 55 ? 2.626   14.363 129.294 1.00 26.25  ? 139 TYR A CG  1 
ATOM   445  C  CD1 . TYR A 1 55 ? 1.798   15.422 129.663 1.00 29.10  ? 139 TYR A CD1 1 
ATOM   446  C  CD2 . TYR A 1 55 ? 2.211   13.064 129.592 1.00 27.88  ? 139 TYR A CD2 1 
ATOM   447  C  CE1 . TYR A 1 55 ? 0.607   15.198 130.314 1.00 30.85  ? 139 TYR A CE1 1 
ATOM   448  C  CE2 . TYR A 1 55 ? 1.021   12.833 130.260 1.00 28.38  ? 139 TYR A CE2 1 
ATOM   449  C  CZ  . TYR A 1 55 ? 0.222   13.906 130.614 1.00 29.64  ? 139 TYR A CZ  1 
ATOM   450  O  OH  . TYR A 1 55 ? -0.967  13.702 131.271 1.00 35.33  ? 139 TYR A OH  1 
ATOM   451  N  N   . VAL A 1 56 ? 7.040   16.077 128.108 1.00 29.11  ? 140 VAL A N   1 
ATOM   452  C  CA  . VAL A 1 56 ? 8.314   15.729 127.496 1.00 30.68  ? 140 VAL A CA  1 
ATOM   453  C  C   . VAL A 1 56 ? 9.379   16.716 127.939 1.00 32.21  ? 140 VAL A C   1 
ATOM   454  O  O   . VAL A 1 56 ? 9.092   17.828 128.395 1.00 36.14  ? 140 VAL A O   1 
ATOM   455  C  CB  . VAL A 1 56 ? 8.256   15.643 125.946 1.00 28.38  ? 140 VAL A CB  1 
ATOM   456  C  CG1 . VAL A 1 56 ? 7.299   14.546 125.505 1.00 28.46  ? 140 VAL A CG1 1 
ATOM   457  C  CG2 . VAL A 1 56 ? 7.876   16.987 125.340 1.00 28.41  ? 140 VAL A CG2 1 
ATOM   458  N  N   . ALA A 1 57 ? 10.623  16.281 127.812 1.00 30.47  ? 141 ALA A N   1 
ATOM   459  C  CA  . ALA A 1 57 ? 11.774  17.100 128.133 1.00 32.40  ? 141 ALA A CA  1 
ATOM   460  C  C   . ALA A 1 57 ? 12.844  16.829 127.092 1.00 33.28  ? 141 ALA A C   1 
ATOM   461  O  O   . ALA A 1 57 ? 12.849  15.762 126.465 1.00 31.29  ? 141 ALA A O   1 
ATOM   462  C  CB  . ALA A 1 57 ? 12.323  16.768 129.532 1.00 36.31  ? 141 ALA A CB  1 
ATOM   463  N  N   . PRO A 1 58 ? 13.747  17.779 126.872 1.00 31.28  ? 142 PRO A N   1 
ATOM   464  C  CA  . PRO A 1 58 ? 14.815  17.560 125.893 1.00 32.40  ? 142 PRO A CA  1 
ATOM   465  C  C   . PRO A 1 58 ? 15.613  16.325 126.268 1.00 35.02  ? 142 PRO A C   1 
ATOM   466  O  O   . PRO A 1 58 ? 15.859  16.062 127.446 1.00 35.87  ? 142 PRO A O   1 
ATOM   467  C  CB  . PRO A 1 58 ? 15.672  18.824 126.019 1.00 32.57  ? 142 PRO A CB  1 
ATOM   468  C  CG  . PRO A 1 58 ? 14.776  19.845 126.612 1.00 33.24  ? 142 PRO A CG  1 
ATOM   469  C  CD  . PRO A 1 58 ? 13.783  19.129 127.460 1.00 33.39  ? 142 PRO A CD  1 
ATOM   470  N  N   . SER A 1 59 ? 15.992  15.546 125.258 1.00 35.75  ? 143 SER A N   1 
ATOM   471  C  CA  . SER A 1 59 ? 16.795  14.360 125.519 1.00 38.92  ? 143 SER A CA  1 
ATOM   472  C  C   . SER A 1 59 ? 18.183  14.756 126.020 1.00 43.89  ? 143 SER A C   1 
ATOM   473  O  O   . SER A 1 59 ? 18.691  15.824 125.683 1.00 44.59  ? 143 SER A O   1 
ATOM   474  C  CB  . SER A 1 59 ? 16.896  13.478 124.276 1.00 41.28  ? 143 SER A CB  1 
ATOM   475  O  OG  . SER A 1 59 ? 15.655  12.846 124.015 1.00 43.18  ? 143 SER A OG  1 
ATOM   476  O  OXT . SER A 1 59 ? 18.825  14.028 126.782 1.00 46.02  ? 143 SER A OXT 1 
ATOM   477  N  N   . GLY B 1 1  ? 11.176  5.585  111.361 1.00 25.92  ? 85  GLY B N   1 
ATOM   478  C  CA  . GLY B 1 1  ? 12.439  5.972  111.964 1.00 26.78  ? 85  GLY B CA  1 
ATOM   479  C  C   . GLY B 1 1  ? 12.470  7.483  112.052 1.00 23.53  ? 85  GLY B C   1 
ATOM   480  O  O   . GLY B 1 1  ? 11.421  8.119  112.093 1.00 23.71  ? 85  GLY B O   1 
ATOM   481  N  N   A VAL B 1 2  ? 13.662  8.076  112.067 0.40 25.25  ? 86  VAL B N   1 
ATOM   482  N  N   B VAL B 1 2  ? 13.679  8.046  112.107 0.60 25.38  ? 86  VAL B N   1 
ATOM   483  C  CA  A VAL B 1 2  ? 13.743  9.527  112.138 0.40 25.38  ? 86  VAL B CA  1 
ATOM   484  C  CA  B VAL B 1 2  ? 13.816  9.490  112.046 0.60 25.18  ? 86  VAL B CA  1 
ATOM   485  C  C   A VAL B 1 2  ? 13.267  10.132 110.824 0.40 24.35  ? 86  VAL B C   1 
ATOM   486  C  C   B VAL B 1 2  ? 13.229  9.976  110.734 0.60 22.90  ? 86  VAL B C   1 
ATOM   487  O  O   A VAL B 1 2  ? 13.567  9.624  109.734 0.40 26.31  ? 86  VAL B O   1 
ATOM   488  O  O   B VAL B 1 2  ? 13.437  9.369  109.674 0.60 24.77  ? 86  VAL B O   1 
ATOM   489  C  CB  A VAL B 1 2  ? 15.161  9.989  112.517 0.40 25.99  ? 86  VAL B CB  1 
ATOM   490  C  CB  B VAL B 1 2  ? 15.297  9.889  112.151 0.60 26.85  ? 86  VAL B CB  1 
ATOM   491  C  CG1 A VAL B 1 2  ? 15.602  9.326  113.819 0.40 30.65  ? 86  VAL B CG1 1 
ATOM   492  C  CG1 B VAL B 1 2  ? 15.435  11.409 112.157 0.60 29.35  ? 86  VAL B CG1 1 
ATOM   493  C  CG2 A VAL B 1 2  ? 16.147  9.695  111.401 0.40 26.48  ? 86  VAL B CG2 1 
ATOM   494  C  CG2 B VAL B 1 2  ? 15.946  9.266  113.387 0.60 30.22  ? 86  VAL B CG2 1 
ATOM   495  N  N   A THR B 1 3  ? 12.479  11.202 110.926 0.40 23.03  ? 87  THR B N   1 
ATOM   496  N  N   B THR B 1 3  ? 12.459  11.062 110.796 0.60 24.26  ? 87  THR B N   1 
ATOM   497  C  CA  A THR B 1 3  ? 11.926  11.856 109.750 0.40 23.81  ? 87  THR B CA  1 
ATOM   498  C  CA  B THR B 1 3  ? 11.902  11.660 109.593 0.60 22.95  ? 87  THR B CA  1 
ATOM   499  C  C   A THR B 1 3  ? 12.956  12.828 109.197 0.40 23.47  ? 87  THR B C   1 
ATOM   500  C  C   B THR B 1 3  ? 12.816  12.798 109.148 0.60 23.88  ? 87  THR B C   1 
ATOM   501  O  O   A THR B 1 3  ? 13.485  13.666 109.937 0.40 21.59  ? 87  THR B O   1 
ATOM   502  O  O   B THR B 1 3  ? 13.158  13.687 109.937 0.60 27.07  ? 87  THR B O   1 
ATOM   503  C  CB  A THR B 1 3  ? 10.669  12.621 110.144 0.40 25.66  ? 87  THR B CB  1 
ATOM   504  C  CB  B THR B 1 3  ? 10.427  12.053 109.759 0.60 26.93  ? 87  THR B CB  1 
ATOM   505  O  OG1 A THR B 1 3  ? 9.689   11.710 110.665 0.40 26.24  ? 87  THR B OG1 1 
ATOM   506  O  OG1 B THR B 1 3  ? 9.834   12.273 108.470 0.60 28.79  ? 87  THR B OG1 1 
ATOM   507  C  CG2 A THR B 1 3  ? 10.105  13.335 108.939 0.40 24.84  ? 87  THR B CG2 1 
ATOM   508  C  CG2 B THR B 1 3  ? 10.230  13.288 110.638 0.60 21.95  ? 87  THR B CG2 1 
ATOM   509  N  N   . THR B 1 4  ? 13.268  12.713 107.905 1.00 25.94  ? 88  THR B N   1 
ATOM   510  C  CA  . THR B 1 4  ? 14.371  13.502 107.389 1.00 27.47  ? 88  THR B CA  1 
ATOM   511  C  C   . THR B 1 4  ? 14.033  14.125 106.047 1.00 27.65  ? 88  THR B C   1 
ATOM   512  O  O   . THR B 1 4  ? 13.084  13.735 105.361 1.00 28.48  ? 88  THR B O   1 
ATOM   513  C  CB  . THR B 1 4  ? 15.656  12.667 107.237 1.00 30.48  ? 88  THR B CB  1 
ATOM   514  O  OG1 . THR B 1 4  ? 15.471  11.682 106.216 1.00 31.75  ? 88  THR B OG1 1 
ATOM   515  C  CG2 . THR B 1 4  ? 15.993  11.964 108.522 1.00 33.87  ? 88  THR B CG2 1 
ATOM   516  N  N   . PHE B 1 5  ? 14.849  15.107 105.692 1.00 25.60  ? 89  PHE B N   1 
ATOM   517  C  CA  . PHE B 1 5  ? 14.861  15.712 104.374 1.00 25.89  ? 89  PHE B CA  1 
ATOM   518  C  C   . PHE B 1 5  ? 16.195  15.425 103.711 1.00 25.26  ? 89  PHE B C   1 
ATOM   519  O  O   . PHE B 1 5  ? 17.185  15.107 104.369 1.00 24.94  ? 89  PHE B O   1 
ATOM   520  C  CB  . PHE B 1 5  ? 14.674  17.226 104.473 1.00 24.65  ? 89  PHE B CB  1 
ATOM   521  C  CG  . PHE B 1 5  ? 13.294  17.636 104.870 1.00 29.41  ? 89  PHE B CG  1 
ATOM   522  C  CD1 . PHE B 1 5  ? 12.833  17.402 106.151 1.00 30.36  ? 89  PHE B CD1 1 
ATOM   523  C  CD2 . PHE B 1 5  ? 12.462  18.259 103.963 1.00 30.85  ? 89  PHE B CD2 1 
ATOM   524  C  CE1 . PHE B 1 5  ? 11.556  17.805 106.537 1.00 32.03  ? 89  PHE B CE1 1 
ATOM   525  C  CE2 . PHE B 1 5  ? 11.184  18.651 104.328 1.00 34.64  ? 89  PHE B CE2 1 
ATOM   526  C  CZ  . PHE B 1 5  ? 10.733  18.420 105.613 1.00 34.41  ? 89  PHE B CZ  1 
ATOM   527  N  N   . VAL B 1 6  ? 16.209  15.529 102.391 1.00 24.73  ? 90  VAL B N   1 
ATOM   528  C  CA  . VAL B 1 6  ? 17.438  15.394 101.625 1.00 24.56  ? 90  VAL B CA  1 
ATOM   529  C  C   . VAL B 1 6  ? 17.668  16.688 100.863 1.00 24.66  ? 90  VAL B C   1 
ATOM   530  O  O   . VAL B 1 6  ? 16.720  17.288 100.342 1.00 26.26  ? 90  VAL B O   1 
ATOM   531  C  CB  . VAL B 1 6  ? 17.400  14.172 100.678 1.00 28.81  ? 90  VAL B CB  1 
ATOM   532  C  CG1 . VAL B 1 6  ? 16.262  14.292 99.673  1.00 30.56  ? 90  VAL B CG1 1 
ATOM   533  C  CG2 . VAL B 1 6  ? 18.728  14.015 99.973  1.00 28.90  ? 90  VAL B CG2 1 
ATOM   534  N  N   . ALA B 1 7  ? 18.923  17.130 100.819 1.00 22.63  ? 91  ALA B N   1 
ATOM   535  C  CA  . ALA B 1 7  ? 19.250  18.352 100.100 1.00 23.05  ? 91  ALA B CA  1 
ATOM   536  C  C   . ALA B 1 7  ? 19.203  18.101 98.602  1.00 25.50  ? 91  ALA B C   1 
ATOM   537  O  O   . ALA B 1 7  ? 19.738  17.101 98.109  1.00 26.33  ? 91  ALA B O   1 
ATOM   538  C  CB  . ALA B 1 7  ? 20.635  18.854 100.491 1.00 23.37  ? 91  ALA B CB  1 
ATOM   539  N  N   . LEU B 1 8  ? 18.550  19.018 97.888  1.00 29.23  ? 92  LEU B N   1 
ATOM   540  C  CA  . LEU B 1 8  ? 18.462  18.981 96.435  1.00 31.20  ? 92  LEU B CA  1 
ATOM   541  C  C   . LEU B 1 8  ? 19.668  19.616 95.759  1.00 32.51  ? 92  LEU B C   1 
ATOM   542  O  O   . LEU B 1 8  ? 19.968  19.276 94.609  1.00 36.64  ? 92  LEU B O   1 
ATOM   543  C  CB  . LEU B 1 8  ? 17.192  19.717 96.000  1.00 31.75  ? 92  LEU B CB  1 
ATOM   544  C  CG  . LEU B 1 8  ? 15.915  19.171 96.644  1.00 34.28  ? 92  LEU B CG  1 
ATOM   545  C  CD1 . LEU B 1 8  ? 14.715  20.030 96.253  1.00 36.19  ? 92  LEU B CD1 1 
ATOM   546  C  CD2 . LEU B 1 8  ? 15.688  17.717 96.253  1.00 35.96  ? 92  LEU B CD2 1 
ATOM   547  N  N   . TYR B 1 9  ? 20.361  20.528 96.440  1.00 31.18  ? 93  TYR B N   1 
ATOM   548  C  CA  . TYR B 1 9  ? 21.485  21.249 95.863  1.00 30.95  ? 93  TYR B CA  1 
ATOM   549  C  C   . TYR B 1 9  ? 22.525  21.480 96.947  1.00 31.37  ? 93  TYR B C   1 
ATOM   550  O  O   . TYR B 1 9  ? 22.224  21.412 98.138  1.00 29.22  ? 93  TYR B O   1 
ATOM   551  C  CB  . TYR B 1 9  ? 21.069  22.623 95.317  1.00 33.48  ? 93  TYR B CB  1 
ATOM   552  C  CG  . TYR B 1 9  ? 19.702  22.670 94.675  1.00 37.43  ? 93  TYR B CG  1 
ATOM   553  C  CD1 . TYR B 1 9  ? 19.499  22.201 93.382  1.00 40.99  ? 93  TYR B CD1 1 
ATOM   554  C  CD2 . TYR B 1 9  ? 18.617  23.207 95.356  1.00 37.03  ? 93  TYR B CD2 1 
ATOM   555  C  CE1 . TYR B 1 9  ? 18.246  22.253 92.793  1.00 41.66  ? 93  TYR B CE1 1 
ATOM   556  C  CE2 . TYR B 1 9  ? 17.364  23.258 94.779  1.00 39.65  ? 93  TYR B CE2 1 
ATOM   557  C  CZ  . TYR B 1 9  ? 17.183  22.784 93.501  1.00 42.84  ? 93  TYR B CZ  1 
ATOM   558  O  OH  . TYR B 1 9  ? 15.929  22.843 92.936  1.00 46.17  ? 93  TYR B OH  1 
ATOM   559  N  N   . ASP B 1 10 ? 23.756  21.765 96.524  1.00 30.88  ? 94  ASP B N   1 
ATOM   560  C  CA  . ASP B 1 10 ? 24.777  22.225 97.458  1.00 30.59  ? 94  ASP B CA  1 
ATOM   561  C  C   . ASP B 1 10 ? 24.420  23.618 97.969  1.00 31.32  ? 94  ASP B C   1 
ATOM   562  O  O   . ASP B 1 10 ? 23.833  24.437 97.254  1.00 33.24  ? 94  ASP B O   1 
ATOM   563  C  CB  . ASP B 1 10 ? 26.135  22.336 96.765  1.00 35.57  ? 94  ASP B CB  1 
ATOM   564  C  CG  . ASP B 1 10 ? 26.710  20.995 96.338  1.00 41.08  ? 94  ASP B CG  1 
ATOM   565  O  OD1 . ASP B 1 10 ? 26.292  19.945 96.857  1.00 40.46  ? 94  ASP B OD1 1 
ATOM   566  O  OD2 . ASP B 1 10 ? 27.616  21.005 95.478  1.00 43.19  ? 94  ASP B OD2 1 
ATOM   567  N  N   . TYR B 1 11 ? 24.788  23.894 99.220  1.00 29.27  ? 95  TYR B N   1 
ATOM   568  C  CA  . TYR B 1 11 ? 24.630  25.229 99.784  1.00 29.16  ? 95  TYR B CA  1 
ATOM   569  C  C   . TYR B 1 11 ? 25.811  25.534 100.692 1.00 28.27  ? 95  TYR B C   1 
ATOM   570  O  O   . TYR B 1 11 ? 26.169  24.724 101.547 1.00 27.47  ? 95  TYR B O   1 
ATOM   571  C  CB  . TYR B 1 11 ? 23.315  25.371 100.569 1.00 29.33  ? 95  TYR B CB  1 
ATOM   572  C  CG  . TYR B 1 11 ? 23.151  26.743 101.187 1.00 27.08  ? 95  TYR B CG  1 
ATOM   573  C  CD1 . TYR B 1 11 ? 22.729  27.823 100.423 1.00 29.57  ? 95  TYR B CD1 1 
ATOM   574  C  CD2 . TYR B 1 11 ? 23.434  26.958 102.529 1.00 25.80  ? 95  TYR B CD2 1 
ATOM   575  C  CE1 . TYR B 1 11 ? 22.596  29.076 100.978 1.00 29.92  ? 95  TYR B CE1 1 
ATOM   576  C  CE2 . TYR B 1 11 ? 23.296  28.211 103.098 1.00 25.47  ? 95  TYR B CE2 1 
ATOM   577  C  CZ  . TYR B 1 11 ? 22.879  29.265 102.319 1.00 27.05  ? 95  TYR B CZ  1 
ATOM   578  O  OH  . TYR B 1 11 ? 22.759  30.516 102.873 1.00 26.47  ? 95  TYR B OH  1 
ATOM   579  N  N   . GLU B 1 12 ? 26.404  26.707 100.519 1.00 30.89  ? 96  GLU B N   1 
ATOM   580  C  CA  . GLU B 1 12 ? 27.550  27.119 101.313 1.00 30.23  ? 96  GLU B CA  1 
ATOM   581  C  C   . GLU B 1 12 ? 27.144  28.228 102.273 1.00 28.95  ? 96  GLU B C   1 
ATOM   582  O  O   . GLU B 1 12 ? 26.604  29.256 101.851 1.00 30.72  ? 96  GLU B O   1 
ATOM   583  C  CB  . GLU B 1 12 ? 28.683  27.587 100.407 1.00 35.08  ? 96  GLU B CB  1 
ATOM   584  C  CG  . GLU B 1 12 ? 30.019  27.565 101.083 1.00 37.54  ? 96  GLU B CG  1 
ATOM   585  C  CD  . GLU B 1 12 ? 30.382  26.194 101.633 1.00 36.30  ? 96  GLU B CD  1 
ATOM   586  O  OE1 . GLU B 1 12 ? 30.377  25.207 100.866 1.00 41.44  ? 96  GLU B OE1 1 
ATOM   587  O  OE2 . GLU B 1 12 ? 30.667  26.105 102.844 1.00 32.57  ? 96  GLU B OE2 1 
ATOM   588  N  N   . SER B 1 13 ? 27.406  28.008 103.562 1.00 27.90  ? 97  SER B N   1 
ATOM   589  C  CA  . SER B 1 13 ? 27.091  28.993 104.587 1.00 26.46  ? 97  SER B CA  1 
ATOM   590  C  C   . SER B 1 13 ? 27.756  30.332 104.294 1.00 27.46  ? 97  SER B C   1 
ATOM   591  O  O   . SER B 1 13 ? 28.941  30.402 103.952 1.00 28.94  ? 97  SER B O   1 
ATOM   592  C  CB  . SER B 1 13 ? 27.556  28.482 105.954 1.00 27.05  ? 97  SER B CB  1 
ATOM   593  O  OG  . SER B 1 13 ? 27.566  29.534 106.907 1.00 28.27  ? 97  SER B OG  1 
ATOM   594  N  N   A ARG B 1 14 ? 26.980  31.403 104.443 0.71 27.01  ? 98  ARG B N   1 
ATOM   595  N  N   B ARG B 1 14 ? 26.979  31.404 104.424 0.29 28.19  ? 98  ARG B N   1 
ATOM   596  C  CA  A ARG B 1 14 ? 27.471  32.750 104.236 0.71 29.21  ? 98  ARG B CA  1 
ATOM   597  C  CA  B ARG B 1 14 ? 27.494  32.746 104.241 0.29 30.36  ? 98  ARG B CA  1 
ATOM   598  C  C   A ARG B 1 14 ? 27.336  33.635 105.463 0.71 28.22  ? 98  ARG B C   1 
ATOM   599  C  C   B ARG B 1 14 ? 27.363  33.625 105.474 0.29 29.55  ? 98  ARG B C   1 
ATOM   600  O  O   A ARG B 1 14 ? 27.811  34.778 105.435 0.71 30.22  ? 98  ARG B O   1 
ATOM   601  O  O   B ARG B 1 14 ? 27.865  34.754 105.458 0.29 30.57  ? 98  ARG B O   1 
ATOM   602  C  CB  A ARG B 1 14 ? 26.741  33.403 103.057 0.71 32.51  ? 98  ARG B CB  1 
ATOM   603  C  CB  B ARG B 1 14 ? 26.801  33.436 103.054 0.29 33.52  ? 98  ARG B CB  1 
ATOM   604  C  CG  A ARG B 1 14 ? 27.294  33.011 101.718 0.71 36.62  ? 98  ARG B CG  1 
ATOM   605  C  CG  B ARG B 1 14 ? 26.915  32.685 101.735 0.29 37.28  ? 98  ARG B CG  1 
ATOM   606  C  CD  A ARG B 1 14 ? 28.774  33.349 101.659 0.71 36.74  ? 98  ARG B CD  1 
ATOM   607  C  CD  B ARG B 1 14 ? 26.338  33.498 100.589 0.29 40.13  ? 98  ARG B CD  1 
ATOM   608  N  NE  A ARG B 1 14 ? 29.386  32.834 100.444 0.71 38.88  ? 98  ARG B NE  1 
ATOM   609  N  NE  B ARG B 1 14 ? 26.480  32.826 99.303  0.29 43.54  ? 98  ARG B NE  1 
ATOM   610  C  CZ  A ARG B 1 14 ? 30.182  31.776 100.417 0.71 36.36  ? 98  ARG B CZ  1 
ATOM   611  C  CZ  B ARG B 1 14 ? 27.542  32.931 98.515  0.29 45.00  ? 98  ARG B CZ  1 
ATOM   612  N  NH1 A ARG B 1 14 ? 30.525  31.144 101.528 0.71 29.94  ? 98  ARG B NH1 1 
ATOM   613  N  NH1 B ARG B 1 14 ? 28.586  33.669 98.856  0.29 44.67  ? 98  ARG B NH1 1 
ATOM   614  N  NH2 A ARG B 1 14 ? 30.650  31.346 99.248  0.71 40.89  ? 98  ARG B NH2 1 
ATOM   615  N  NH2 B ARG B 1 14 ? 27.556  32.280 97.356  0.29 46.50  ? 98  ARG B NH2 1 
ATOM   616  N  N   . THR B 1 15 ? 26.708  33.154 106.534 1.00 29.60  ? 99  THR B N   1 
ATOM   617  C  CA  . THR B 1 15 ? 26.456  33.963 107.720 1.00 27.87  ? 99  THR B CA  1 
ATOM   618  C  C   . THR B 1 15 ? 26.803  33.162 108.975 1.00 28.67  ? 99  THR B C   1 
ATOM   619  O  O   . THR B 1 15 ? 27.173  31.983 108.911 1.00 27.91  ? 99  THR B O   1 
ATOM   620  C  CB  . THR B 1 15 ? 24.995  34.435 107.785 1.00 28.87  ? 99  THR B CB  1 
ATOM   621  O  OG1 . THR B 1 15 ? 24.191  33.385 108.323 1.00 27.38  ? 99  THR B OG1 1 
ATOM   622  C  CG2 . THR B 1 15 ? 24.450  34.779 106.408 1.00 28.19  ? 99  THR B CG2 1 
ATOM   623  N  N   . GLU B 1 16 ? 26.662  33.816 110.133 1.00 30.76  ? 100 GLU B N   1 
ATOM   624  C  CA  . GLU B 1 16 ? 26.875  33.160 111.417 1.00 35.39  ? 100 GLU B CA  1 
ATOM   625  C  C   . GLU B 1 16 ? 25.798  32.147 111.763 1.00 31.60  ? 100 GLU B C   1 
ATOM   626  O  O   . GLU B 1 16 ? 25.990  31.377 112.707 1.00 36.68  ? 100 GLU B O   1 
ATOM   627  C  CB  . GLU B 1 16 ? 26.966  34.189 112.554 1.00 37.78  ? 100 GLU B CB  1 
ATOM   628  C  CG  . GLU B 1 16 ? 28.379  34.499 112.969 1.00 45.40  ? 100 GLU B CG  1 
ATOM   629  C  CD  . GLU B 1 16 ? 29.285  34.576 111.771 1.00 48.82  ? 100 GLU B CD  1 
ATOM   630  O  OE1 . GLU B 1 16 ? 29.192  35.581 111.030 1.00 49.85  ? 100 GLU B OE1 1 
ATOM   631  O  OE2 . GLU B 1 16 ? 30.051  33.609 111.548 1.00 48.62  ? 100 GLU B OE2 1 
ATOM   632  N  N   . THR B 1 17 ? 24.667  32.137 111.052 1.00 26.91  ? 101 THR B N   1 
ATOM   633  C  CA  . THR B 1 17 ? 23.548  31.291 111.441 1.00 25.02  ? 101 THR B CA  1 
ATOM   634  C  C   . THR B 1 17 ? 23.064  30.334 110.365 1.00 25.21  ? 101 THR B C   1 
ATOM   635  O  O   . THR B 1 17 ? 22.262  29.457 110.686 1.00 26.07  ? 101 THR B O   1 
ATOM   636  C  CB  . THR B 1 17 ? 22.351  32.126 111.923 1.00 25.64  ? 101 THR B CB  1 
ATOM   637  O  OG1 . THR B 1 17 ? 21.913  32.975 110.868 1.00 26.60  ? 101 THR B OG1 1 
ATOM   638  C  CG2 . THR B 1 17 ? 22.713  32.968 113.134 1.00 27.47  ? 101 THR B CG2 1 
ATOM   639  N  N   . ASP B 1 18 ? 23.496  30.471 109.114 1.00 24.62  ? 102 ASP B N   1 
ATOM   640  C  CA  . ASP B 1 18 ? 23.068  29.478 108.138 1.00 24.71  ? 102 ASP B CA  1 
ATOM   641  C  C   . ASP B 1 18 ? 23.958  28.230 108.184 1.00 25.43  ? 102 ASP B C   1 
ATOM   642  O  O   . ASP B 1 18 ? 25.006  28.187 108.841 1.00 27.77  ? 102 ASP B O   1 
ATOM   643  C  CB  . ASP B 1 18 ? 22.934  30.078 106.731 1.00 23.30  ? 102 ASP B CB  1 
ATOM   644  C  CG  . ASP B 1 18 ? 24.227  30.630 106.198 1.00 24.56  ? 102 ASP B CG  1 
ATOM   645  O  OD1 . ASP B 1 18 ? 25.201  30.694 106.971 1.00 25.12  ? 102 ASP B OD1 1 
ATOM   646  O  OD2 . ASP B 1 18 ? 24.264  31.013 105.003 1.00 26.43  ? 102 ASP B OD2 1 
ATOM   647  N  N   . LEU B 1 19 ? 23.514  27.187 107.485 1.00 23.76  ? 103 LEU B N   1 
ATOM   648  C  CA  . LEU B 1 19 ? 24.120  25.865 107.585 1.00 24.49  ? 103 LEU B CA  1 
ATOM   649  C  C   . LEU B 1 19 ? 24.598  25.432 106.212 1.00 23.34  ? 103 LEU B C   1 
ATOM   650  O  O   . LEU B 1 19 ? 23.814  25.438 105.260 1.00 26.37  ? 103 LEU B O   1 
ATOM   651  C  CB  . LEU B 1 19 ? 23.067  24.862 108.068 1.00 25.97  ? 103 LEU B CB  1 
ATOM   652  C  CG  . LEU B 1 19 ? 23.512  23.396 108.058 1.00 27.25  ? 103 LEU B CG  1 
ATOM   653  C  CD1 . LEU B 1 19 ? 24.593  23.161 109.103 1.00 28.44  ? 103 LEU B CD1 1 
ATOM   654  C  CD2 . LEU B 1 19 ? 22.315  22.468 108.255 1.00 28.00  ? 103 LEU B CD2 1 
ATOM   655  N  N   . SER B 1 20 ? 25.868  25.045 106.114 1.00 25.17  ? 104 SER B N   1 
ATOM   656  C  CA  . SER B 1 20 ? 26.371  24.429 104.893 1.00 24.76  ? 104 SER B CA  1 
ATOM   657  C  C   . SER B 1 20 ? 25.884  22.997 104.784 1.00 25.28  ? 104 SER B C   1 
ATOM   658  O  O   . SER B 1 20 ? 25.801  22.277 105.781 1.00 27.00  ? 104 SER B O   1 
ATOM   659  C  CB  . SER B 1 20 ? 27.897  24.394 104.894 1.00 25.52  ? 104 SER B CB  1 
ATOM   660  O  OG  . SER B 1 20 ? 28.425  25.701 104.900 1.00 27.57  ? 104 SER B OG  1 
ATOM   661  N  N   . PHE B 1 21 ? 25.605  22.575 103.556 1.00 25.09  ? 105 PHE B N   1 
ATOM   662  C  CA  . PHE B 1 21 ? 25.264  21.186 103.297 1.00 23.89  ? 105 PHE B CA  1 
ATOM   663  C  C   . PHE B 1 21 ? 25.537  20.893 101.831 1.00 26.85  ? 105 PHE B C   1 
ATOM   664  O  O   . PHE B 1 21 ? 25.679  21.806 101.013 1.00 27.68  ? 105 PHE B O   1 
ATOM   665  C  CB  . PHE B 1 21 ? 23.806  20.885 103.666 1.00 22.30  ? 105 PHE B CB  1 
ATOM   666  C  CG  . PHE B 1 21 ? 22.812  21.807 103.026 1.00 22.67  ? 105 PHE B CG  1 
ATOM   667  C  CD1 . PHE B 1 21 ? 22.271  21.500 101.787 1.00 24.77  ? 105 PHE B CD1 1 
ATOM   668  C  CD2 . PHE B 1 21 ? 22.396  22.965 103.665 1.00 23.07  ? 105 PHE B CD2 1 
ATOM   669  C  CE1 . PHE B 1 21 ? 21.338  22.325 101.188 1.00 23.39  ? 105 PHE B CE1 1 
ATOM   670  C  CE2 . PHE B 1 21 ? 21.465  23.807 103.069 1.00 24.80  ? 105 PHE B CE2 1 
ATOM   671  C  CZ  . PHE B 1 21 ? 20.922  23.483 101.831 1.00 24.21  ? 105 PHE B CZ  1 
ATOM   672  N  N   . LYS B 1 22 ? 25.635  19.608 101.505 1.00 25.85  ? 106 LYS B N   1 
ATOM   673  C  CA  . LYS B 1 22 ? 25.856  19.229 100.117 1.00 30.65  ? 106 LYS B CA  1 
ATOM   674  C  C   . LYS B 1 22 ? 24.635  18.525 99.539  1.00 28.59  ? 106 LYS B C   1 
ATOM   675  O  O   . LYS B 1 22 ? 23.783  18.006 100.262 1.00 26.97  ? 106 LYS B O   1 
ATOM   676  C  CB  . LYS B 1 22 ? 27.126  18.392 99.942  1.00 38.73  ? 106 LYS B CB  1 
ATOM   677  C  CG  . LYS B 1 22 ? 27.205  17.186 100.817 1.00 42.40  ? 106 LYS B CG  1 
ATOM   678  C  CD  . LYS B 1 22 ? 28.561  16.524 100.627 1.00 43.35  ? 106 LYS B CD  1 
ATOM   679  C  CE  . LYS B 1 22 ? 28.856  16.246 99.149  1.00 48.34  ? 106 LYS B CE  1 
ATOM   680  N  NZ  . LYS B 1 22 ? 27.962  15.213 98.537  1.00 48.81  ? 106 LYS B NZ  1 
ATOM   681  N  N   . LYS B 1 23 ? 24.536  18.560 98.211  1.00 32.31  ? 107 LYS B N   1 
ATOM   682  C  CA  . LYS B 1 23 ? 23.486  17.824 97.524  1.00 32.86  ? 107 LYS B CA  1 
ATOM   683  C  C   . LYS B 1 23 ? 23.470  16.381 98.007  1.00 31.13  ? 107 LYS B C   1 
ATOM   684  O  O   . LYS B 1 23 ? 24.516  15.731 98.104  1.00 32.51  ? 107 LYS B O   1 
ATOM   685  C  CB  . LYS B 1 23 ? 23.739  17.867 96.014  1.00 38.33  ? 107 LYS B CB  1 
ATOM   686  C  CG  . LYS B 1 23 ? 22.760  17.054 95.182  1.00 43.09  ? 107 LYS B CG  1 
ATOM   687  C  CD  . LYS B 1 23 ? 23.134  17.125 93.704  1.00 49.35  ? 107 LYS B CD  1 
ATOM   688  C  CE  . LYS B 1 23 ? 22.847  15.810 92.980  1.00 54.38  ? 107 LYS B CE  1 
ATOM   689  N  NZ  . LYS B 1 23 ? 23.618  15.667 91.699  1.00 56.97  ? 107 LYS B NZ  1 
ATOM   690  N  N   . GLY B 1 24 ? 22.279  15.891 98.342  1.00 29.56  ? 108 GLY B N   1 
ATOM   691  C  CA  . GLY B 1 24 ? 22.128  14.528 98.799  1.00 28.47  ? 108 GLY B CA  1 
ATOM   692  C  C   . GLY B 1 24 ? 22.247  14.346 100.293 1.00 27.52  ? 108 GLY B C   1 
ATOM   693  O  O   . GLY B 1 24 ? 22.003  13.238 100.784 1.00 29.07  ? 108 GLY B O   1 
ATOM   694  N  N   . GLU B 1 25 ? 22.603  15.395 101.033 1.00 26.36  ? 109 GLU B N   1 
ATOM   695  C  CA  . GLU B 1 25 ? 22.785  15.275 102.474 1.00 23.77  ? 109 GLU B CA  1 
ATOM   696  C  C   . GLU B 1 25 ? 21.449  15.108 103.184 1.00 21.64  ? 109 GLU B C   1 
ATOM   697  O  O   . GLU B 1 25 ? 20.473  15.785 102.868 1.00 22.78  ? 109 GLU B O   1 
ATOM   698  C  CB  . GLU B 1 25 ? 23.491  16.518 103.008 1.00 25.12  ? 109 GLU B CB  1 
ATOM   699  C  CG  . GLU B 1 25 ? 23.910  16.427 104.453 1.00 25.63  ? 109 GLU B CG  1 
ATOM   700  C  CD  . GLU B 1 25 ? 24.881  17.533 104.853 1.00 25.15  ? 109 GLU B CD  1 
ATOM   701  O  OE1 . GLU B 1 25 ? 25.668  18.001 103.992 1.00 26.65  ? 109 GLU B OE1 1 
ATOM   702  O  OE2 . GLU B 1 25 ? 24.884  17.916 106.033 1.00 31.71  ? 109 GLU B OE2 1 
ATOM   703  N  N   . ARG B 1 26 ? 21.424  14.200 104.159 1.00 23.99  ? 110 ARG B N   1 
ATOM   704  C  CA  . ARG B 1 26 ? 20.259  13.935 104.989 1.00 25.41  ? 110 ARG B CA  1 
ATOM   705  C  C   . ARG B 1 26 ? 20.222  14.950 106.136 1.00 24.11  ? 110 ARG B C   1 
ATOM   706  O  O   . ARG B 1 26 ? 21.209  15.108 106.867 1.00 25.99  ? 110 ARG B O   1 
ATOM   707  C  CB  . ARG B 1 26 ? 20.431  12.515 105.534 1.00 29.91  ? 110 ARG B CB  1 
ATOM   708  C  CG  . ARG B 1 26 ? 19.220  11.805 106.069 1.00 33.95  ? 110 ARG B CG  1 
ATOM   709  C  CD  . ARG B 1 26 ? 19.486  10.290 106.055 1.00 33.66  ? 110 ARG B CD  1 
ATOM   710  N  NE  . ARG B 1 26 ? 18.524  9.559  106.862 1.00 38.15  ? 110 ARG B NE  1 
ATOM   711  C  CZ  . ARG B 1 26 ? 18.690  9.291  108.148 1.00 40.18  ? 110 ARG B CZ  1 
ATOM   712  N  NH1 . ARG B 1 26 ? 19.787  9.658  108.793 1.00 39.21  ? 110 ARG B NH1 1 
ATOM   713  N  NH2 . ARG B 1 26 ? 17.734  8.636  108.802 1.00 44.20  ? 110 ARG B NH2 1 
ATOM   714  N  N   . LEU B 1 27 ? 19.092  15.653 106.284 1.00 23.09  ? 111 LEU B N   1 
ATOM   715  C  CA  . LEU B 1 27 ? 18.953  16.715 107.271 1.00 22.49  ? 111 LEU B CA  1 
ATOM   716  C  C   . LEU B 1 27 ? 17.708  16.496 108.115 1.00 21.51  ? 111 LEU B C   1 
ATOM   717  O  O   . LEU B 1 27 ? 16.684  16.019 107.620 1.00 22.63  ? 111 LEU B O   1 
ATOM   718  C  CB  . LEU B 1 27 ? 18.835  18.102 106.593 1.00 23.57  ? 111 LEU B CB  1 
ATOM   719  C  CG  . LEU B 1 27 ? 19.971  18.520 105.670 1.00 24.28  ? 111 LEU B CG  1 
ATOM   720  C  CD1 . LEU B 1 27 ? 19.591  19.831 105.000 1.00 26.16  ? 111 LEU B CD1 1 
ATOM   721  C  CD2 . LEU B 1 27 ? 21.238  18.667 106.482 1.00 24.99  ? 111 LEU B CD2 1 
ATOM   722  N  N   . GLN B 1 28 ? 17.801  16.858 109.390 1.00 21.31  ? 112 GLN B N   1 
ATOM   723  C  CA  . GLN B 1 28 ? 16.627  16.969 110.242 1.00 20.69  ? 112 GLN B CA  1 
ATOM   724  C  C   . GLN B 1 28 ? 16.161  18.412 110.222 1.00 21.09  ? 112 GLN B C   1 
ATOM   725  O  O   . GLN B 1 28 ? 16.965  19.325 110.426 1.00 22.39  ? 112 GLN B O   1 
ATOM   726  C  CB  . GLN B 1 28 ? 16.964  16.567 111.676 1.00 22.13  ? 112 GLN B CB  1 
ATOM   727  C  CG  . GLN B 1 28 ? 15.812  16.818 112.643 1.00 22.72  ? 112 GLN B CG  1 
ATOM   728  C  CD  . GLN B 1 28 ? 16.152  16.423 114.050 1.00 24.70  ? 112 GLN B CD  1 
ATOM   729  O  OE1 . GLN B 1 28 ? 17.305  16.094 114.361 1.00 28.08  ? 112 GLN B OE1 1 
ATOM   730  N  NE2 . GLN B 1 28 ? 15.153  16.432 114.917 1.00 25.18  ? 112 GLN B NE2 1 
ATOM   731  N  N   . ILE B 1 29 ? 14.875  18.626 109.970 1.00 20.26  ? 113 ILE B N   1 
ATOM   732  C  CA  . ILE B 1 29 ? 14.307  19.965 110.034 1.00 19.43  ? 113 ILE B CA  1 
ATOM   733  C  C   . ILE B 1 29 ? 13.723  20.159 111.419 1.00 18.84  ? 113 ILE B C   1 
ATOM   734  O  O   . ILE B 1 29 ? 12.821  19.425 111.833 1.00 21.06  ? 113 ILE B O   1 
ATOM   735  C  CB  . ILE B 1 29 ? 13.273  20.212 108.930 1.00 21.52  ? 113 ILE B CB  1 
ATOM   736  C  CG1 . ILE B 1 29 ? 13.945  20.119 107.559 1.00 23.66  ? 113 ILE B CG1 1 
ATOM   737  C  CG2 . ILE B 1 29 ? 12.646  21.589 109.105 1.00 21.54  ? 113 ILE B CG2 1 
ATOM   738  C  CD1 . ILE B 1 29 ? 15.122  21.027 107.362 1.00 25.66  ? 113 ILE B CD1 1 
ATOM   739  N  N   . VAL B 1 30 ? 14.244  21.153 112.135 1.00 20.84  ? 114 VAL B N   1 
ATOM   740  C  CA  . VAL B 1 30 ? 13.810  21.433 113.497 1.00 23.31  ? 114 VAL B CA  1 
ATOM   741  C  C   . VAL B 1 30 ? 12.684  22.468 113.506 1.00 23.21  ? 114 VAL B C   1 
ATOM   742  O  O   . VAL B 1 30 ? 11.779  22.395 114.343 1.00 25.48  ? 114 VAL B O   1 
ATOM   743  C  CB  . VAL B 1 30 ? 15.034  21.894 114.325 1.00 25.63  ? 114 VAL B CB  1 
ATOM   744  C  CG1 . VAL B 1 30 ? 14.619  22.355 115.703 1.00 28.33  ? 114 VAL B CG1 1 
ATOM   745  C  CG2 . VAL B 1 30 ? 16.054  20.772 114.442 1.00 28.75  ? 114 VAL B CG2 1 
ATOM   746  N  N   . ASN B 1 31 ? 12.698  23.409 112.566 1.00 24.15  ? 115 ASN B N   1 
ATOM   747  C  CA  . ASN B 1 31 ? 11.649  24.418 112.478 1.00 22.58  ? 115 ASN B CA  1 
ATOM   748  C  C   . ASN B 1 31 ? 11.451  24.730 111.009 1.00 23.49  ? 115 ASN B C   1 
ATOM   749  O  O   . ASN B 1 31 ? 12.425  24.977 110.290 1.00 25.29  ? 115 ASN B O   1 
ATOM   750  C  CB  . ASN B 1 31 ? 12.045  25.718 113.204 1.00 24.48  ? 115 ASN B CB  1 
ATOM   751  C  CG  . ASN B 1 31 ? 10.996  26.805 113.069 1.00 29.48  ? 115 ASN B CG  1 
ATOM   752  O  OD1 . ASN B 1 31 ? 11.102  27.689 112.213 1.00 32.14  ? 115 ASN B OD1 1 
ATOM   753  N  ND2 . ASN B 1 31 ? 9.965   26.735 113.901 1.00 32.29  ? 115 ASN B ND2 1 
ATOM   754  N  N   . ASN B 1 32 ? 10.197  24.757 110.580 1.00 23.38  ? 116 ASN B N   1 
ATOM   755  C  CA  . ASN B 1 32 ? 9.896   25.133 109.211 1.00 25.01  ? 116 ASN B CA  1 
ATOM   756  C  C   . ASN B 1 32 ? 8.655   26.002 109.136 1.00 30.61  ? 116 ASN B C   1 
ATOM   757  O  O   . ASN B 1 32 ? 7.930   25.978 108.136 1.00 31.71  ? 116 ASN B O   1 
ATOM   758  C  CB  . ASN B 1 32 ? 9.836   23.924 108.270 1.00 30.50  ? 116 ASN B CB  1 
ATOM   759  C  CG  . ASN B 1 32 ? 8.998   22.774 108.802 1.00 31.65  ? 116 ASN B CG  1 
ATOM   760  O  OD1 . ASN B 1 32 ? 8.122   22.947 109.648 1.00 31.64  ? 116 ASN B OD1 1 
ATOM   761  N  ND2 . ASN B 1 32 ? 9.280   21.577 108.301 1.00 35.59  ? 116 ASN B ND2 1 
ATOM   762  N  N   . THR B 1 33 ? 8.414   26.801 110.171 1.00 28.91  ? 117 THR B N   1 
ATOM   763  C  CA  . THR B 1 33 ? 7.209   27.610 110.242 1.00 32.15  ? 117 THR B CA  1 
ATOM   764  C  C   . THR B 1 33 ? 7.426   29.064 109.848 1.00 31.81  ? 117 THR B C   1 
ATOM   765  O  O   . THR B 1 33 ? 6.459   29.833 109.841 1.00 36.50  ? 117 THR B O   1 
ATOM   766  C  CB  . THR B 1 33 ? 6.583   27.540 111.644 1.00 31.40  ? 117 THR B CB  1 
ATOM   767  O  OG1 . THR B 1 33 ? 7.532   28.006 112.616 1.00 31.32  ? 117 THR B OG1 1 
ATOM   768  C  CG2 . THR B 1 33 ? 6.148   26.108 111.975 1.00 32.51  ? 117 THR B CG2 1 
ATOM   769  N  N   . GLU B 1 34 ? 8.655   29.467 109.512 1.00 33.01  ? 118 GLU B N   1 
ATOM   770  C  CA  . GLU B 1 34 ? 8.945   30.882 109.318 1.00 35.17  ? 118 GLU B CA  1 
ATOM   771  C  C   . GLU B 1 34 ? 9.086   31.298 107.857 1.00 37.99  ? 118 GLU B C   1 
ATOM   772  O  O   . GLU B 1 34 ? 9.504   32.427 107.596 1.00 36.90  ? 118 GLU B O   1 
ATOM   773  C  CB  . GLU B 1 34 ? 10.187  31.293 110.120 1.00 35.32  ? 118 GLU B CB  1 
ATOM   774  C  CG  . GLU B 1 34 ? 10.069  31.087 111.632 1.00 41.87  ? 118 GLU B CG  1 
ATOM   775  C  CD  . GLU B 1 34 ? 9.282   32.197 112.331 1.00 50.84  ? 118 GLU B CD  1 
ATOM   776  O  OE1 . GLU B 1 34 ? 8.503   32.907 111.653 1.00 50.40  ? 118 GLU B OE1 1 
ATOM   777  O  OE2 . GLU B 1 34 ? 9.452   32.362 113.566 1.00 52.10  ? 118 GLU B OE2 1 
ATOM   778  N  N   . GLY B 1 35 ? 8.755   30.430 106.902 1.00 37.45  ? 119 GLY B N   1 
ATOM   779  C  CA  . GLY B 1 35 ? 8.800   30.834 105.506 1.00 35.20  ? 119 GLY B CA  1 
ATOM   780  C  C   . GLY B 1 35 ? 10.000  30.362 104.702 1.00 34.26  ? 119 GLY B C   1 
ATOM   781  O  O   . GLY B 1 35 ? 10.214  29.156 104.564 1.00 35.94  ? 119 GLY B O   1 
ATOM   782  N  N   . ASP B 1 36 ? 10.790  31.307 104.162 1.00 31.58  ? 120 ASP B N   1 
ATOM   783  C  CA  . ASP B 1 36 ? 11.821  30.971 103.184 1.00 27.77  ? 120 ASP B CA  1 
ATOM   784  C  C   . ASP B 1 36 ? 13.040  30.304 103.805 1.00 24.35  ? 120 ASP B C   1 
ATOM   785  O  O   . ASP B 1 36 ? 13.860  29.745 103.070 1.00 29.98  ? 120 ASP B O   1 
ATOM   786  C  CB  . ASP B 1 36 ? 12.294  32.218 102.424 1.00 30.77  ? 120 ASP B CB  1 
ATOM   787  C  CG  . ASP B 1 36 ? 11.330  32.659 101.340 1.00 37.16  ? 120 ASP B CG  1 
ATOM   788  O  OD1 . ASP B 1 36 ? 10.334  31.954 101.071 1.00 40.59  ? 120 ASP B OD1 1 
ATOM   789  O  OD2 . ASP B 1 36 ? 11.584  33.721 100.740 1.00 38.92  ? 120 ASP B OD2 1 
ATOM   790  N  N   . TRP B 1 37 ? 13.202  30.372 105.126 1.00 22.39  ? 121 TRP B N   1 
ATOM   791  C  CA  . TRP B 1 37 ? 14.372  29.814 105.794 1.00 20.70  ? 121 TRP B CA  1 
ATOM   792  C  C   . TRP B 1 37 ? 13.911  28.918 106.929 1.00 20.48  ? 121 TRP B C   1 
ATOM   793  O  O   . TRP B 1 37 ? 13.087  29.332 107.756 1.00 21.74  ? 121 TRP B O   1 
ATOM   794  C  CB  . TRP B 1 37 ? 15.265  30.934 106.337 1.00 19.72  ? 121 TRP B CB  1 
ATOM   795  C  CG  . TRP B 1 37 ? 15.918  31.697 105.246 1.00 19.25  ? 121 TRP B CG  1 
ATOM   796  C  CD1 . TRP B 1 37 ? 15.396  32.758 104.546 1.00 20.89  ? 121 TRP B CD1 1 
ATOM   797  C  CD2 . TRP B 1 37 ? 17.202  31.432 104.681 1.00 20.19  ? 121 TRP B CD2 1 
ATOM   798  N  NE1 . TRP B 1 37 ? 16.296  33.175 103.594 1.00 22.01  ? 121 TRP B NE1 1 
ATOM   799  C  CE2 . TRP B 1 37 ? 17.412  32.375 103.653 1.00 21.25  ? 121 TRP B CE2 1 
ATOM   800  C  CE3 . TRP B 1 37 ? 18.205  30.497 104.960 1.00 21.73  ? 121 TRP B CE3 1 
ATOM   801  C  CZ2 . TRP B 1 37 ? 18.583  32.409 102.901 1.00 22.31  ? 121 TRP B CZ2 1 
ATOM   802  C  CZ3 . TRP B 1 37 ? 19.363  30.525 104.212 1.00 20.94  ? 121 TRP B CZ3 1 
ATOM   803  C  CH2 . TRP B 1 37 ? 19.546  31.479 103.194 1.00 22.35  ? 121 TRP B CH2 1 
ATOM   804  N  N   . TRP B 1 38 ? 14.444  27.698 106.964 1.00 18.98  ? 122 TRP B N   1 
ATOM   805  C  CA  . TRP B 1 38 ? 14.075  26.691 107.946 1.00 18.49  ? 122 TRP B CA  1 
ATOM   806  C  C   . TRP B 1 38 ? 15.304  26.392 108.793 1.00 18.56  ? 122 TRP B C   1 
ATOM   807  O  O   . TRP B 1 38 ? 16.431  26.537 108.328 1.00 21.20  ? 122 TRP B O   1 
ATOM   808  C  CB  . TRP B 1 38 ? 13.669  25.405 107.231 1.00 20.57  ? 122 TRP B CB  1 
ATOM   809  C  CG  . TRP B 1 38 ? 12.381  25.471 106.473 1.00 21.66  ? 122 TRP B CG  1 
ATOM   810  C  CD1 . TRP B 1 38 ? 11.509  26.519 106.390 1.00 23.67  ? 122 TRP B CD1 1 
ATOM   811  C  CD2 . TRP B 1 38 ? 11.820  24.414 105.705 1.00 21.90  ? 122 TRP B CD2 1 
ATOM   812  N  NE1 . TRP B 1 38 ? 10.415  26.165 105.614 1.00 23.48  ? 122 TRP B NE1 1 
ATOM   813  C  CE2 . TRP B 1 38 ? 10.590  24.875 105.179 1.00 23.09  ? 122 TRP B CE2 1 
ATOM   814  C  CE3 . TRP B 1 38 ? 12.237  23.112 105.411 1.00 22.35  ? 122 TRP B CE3 1 
ATOM   815  C  CZ2 . TRP B 1 38 ? 9.780   24.077 104.369 1.00 24.46  ? 122 TRP B CZ2 1 
ATOM   816  C  CZ3 . TRP B 1 38 ? 11.412  22.313 104.623 1.00 26.50  ? 122 TRP B CZ3 1 
ATOM   817  C  CH2 . TRP B 1 38 ? 10.207  22.806 104.104 1.00 26.50  ? 122 TRP B CH2 1 
ATOM   818  N  N   . LEU B 1 39 ? 15.104  25.972 110.035 1.00 19.73  ? 123 LEU B N   1 
ATOM   819  C  CA  . LEU B 1 39 ? 16.236  25.577 110.857 1.00 19.72  ? 123 LEU B CA  1 
ATOM   820  C  C   . LEU B 1 39 ? 16.469  24.087 110.693 1.00 17.57  ? 123 LEU B C   1 
ATOM   821  O  O   . LEU B 1 39 ? 15.553  23.285 110.912 1.00 20.18  ? 123 LEU B O   1 
ATOM   822  C  CB  . LEU B 1 39 ? 16.006  25.895 112.330 1.00 20.82  ? 123 LEU B CB  1 
ATOM   823  C  CG  . LEU B 1 39 ? 17.234  25.586 113.179 1.00 22.33  ? 123 LEU B CG  1 
ATOM   824  C  CD1 . LEU B 1 39 ? 18.401  26.476 112.772 1.00 26.83  ? 123 LEU B CD1 1 
ATOM   825  C  CD2 . LEU B 1 39 ? 16.944  25.744 114.654 1.00 24.86  ? 123 LEU B CD2 1 
ATOM   826  N  N   . ALA B 1 40 ? 17.705  23.722 110.344 1.00 19.81  ? 124 ALA B N   1 
ATOM   827  C  CA  . ALA B 1 40 ? 18.082  22.342 110.098 1.00 19.74  ? 124 ALA B CA  1 
ATOM   828  C  C   . ALA B 1 40 ? 19.195  21.896 111.036 1.00 20.93  ? 124 ALA B C   1 
ATOM   829  O  O   . ALA B 1 40 ? 20.022  22.695 111.476 1.00 22.53  ? 124 ALA B O   1 
ATOM   830  C  CB  . ALA B 1 40 ? 18.541  22.152 108.659 1.00 22.24  ? 124 ALA B CB  1 
ATOM   831  N  N   . HIS B 1 41 ? 19.221  20.598 111.311 1.00 20.88  ? 125 HIS B N   1 
ATOM   832  C  CA  . HIS B 1 41 ? 20.325  19.956 112.019 1.00 21.96  ? 125 HIS B CA  1 
ATOM   833  C  C   . HIS B 1 41 ? 20.804  18.844 111.104 1.00 22.93  ? 125 HIS B C   1 
ATOM   834  O  O   . HIS B 1 41 ? 20.023  17.969 110.737 1.00 24.41  ? 125 HIS B O   1 
ATOM   835  C  CB  . HIS B 1 41 ? 19.841  19.395 113.365 1.00 23.25  ? 125 HIS B CB  1 
ATOM   836  C  CG  . HIS B 1 41 ? 20.888  18.653 114.142 1.00 23.70  ? 125 HIS B CG  1 
ATOM   837  N  ND1 . HIS B 1 41 ? 21.997  19.272 114.681 1.00 24.36  ? 125 HIS B ND1 1 
ATOM   838  C  CD2 . HIS B 1 41 ? 20.989  17.340 114.473 1.00 25.51  ? 125 HIS B CD2 1 
ATOM   839  C  CE1 . HIS B 1 41 ? 22.737  18.365 115.307 1.00 28.52  ? 125 HIS B CE1 1 
ATOM   840  N  NE2 . HIS B 1 41 ? 22.150  17.182 115.195 1.00 26.31  ? 125 HIS B NE2 1 
ATOM   841  N  N   . SER B 1 42 ? 22.064  18.902 110.684 1.00 27.42  ? 126 SER B N   1 
ATOM   842  C  CA  . SER B 1 42 ? 22.551  17.880 109.758 1.00 28.06  ? 126 SER B CA  1 
ATOM   843  C  C   . SER B 1 42 ? 22.786  16.555 110.471 1.00 29.80  ? 126 SER B C   1 
ATOM   844  O  O   . SER B 1 42 ? 23.457  16.500 111.506 1.00 32.11  ? 126 SER B O   1 
ATOM   845  C  CB  . SER B 1 42 ? 23.829  18.304 109.051 1.00 27.60  ? 126 SER B CB  1 
ATOM   846  O  OG  . SER B 1 42 ? 24.322  17.188 108.301 1.00 31.61  ? 126 SER B OG  1 
ATOM   847  N  N   . LEU B 1 43 ? 22.228  15.486 109.905 1.00 33.76  ? 127 LEU B N   1 
ATOM   848  C  CA  . LEU B 1 43 ? 22.485  14.142 110.394 1.00 28.71  ? 127 LEU B CA  1 
ATOM   849  C  C   . LEU B 1 43 ? 23.779  13.580 109.842 1.00 38.79  ? 127 LEU B C   1 
ATOM   850  O  O   . LEU B 1 43 ? 24.239  12.537 110.318 1.00 45.05  ? 127 LEU B O   1 
ATOM   851  C  CB  . LEU B 1 43 ? 21.306  13.229 110.038 1.00 33.55  ? 127 LEU B CB  1 
ATOM   852  C  CG  . LEU B 1 43 ? 19.988  13.740 110.621 1.00 30.76  ? 127 LEU B CG  1 
ATOM   853  C  CD1 . LEU B 1 43 ? 18.825  12.845 110.247 1.00 34.74  ? 127 LEU B CD1 1 
ATOM   854  C  CD2 . LEU B 1 43 ? 20.106  13.875 112.144 1.00 34.59  ? 127 LEU B CD2 1 
ATOM   855  N  N   . SER B 1 44 ? 24.378  14.268 108.871 1.00 36.25  ? 128 SER B N   1 
ATOM   856  C  CA  . SER B 1 44 ? 25.616  13.871 108.214 1.00 32.82  ? 128 SER B CA  1 
ATOM   857  C  C   . SER B 1 44 ? 26.833  14.504 108.879 1.00 35.13  ? 128 SER B C   1 
ATOM   858  O  O   . SER B 1 44 ? 27.868  13.855 109.017 1.00 38.45  ? 128 SER B O   1 
ATOM   859  C  CB  . SER B 1 44 ? 25.537  14.273 106.733 1.00 36.22  ? 128 SER B CB  1 
ATOM   860  O  OG  . SER B 1 44 ? 26.752  14.109 106.027 1.00 42.18  ? 128 SER B OG  1 
ATOM   861  N  N   . THR B 1 45 ? 26.707  15.748 109.328 1.00 36.15  ? 129 THR B N   1 
ATOM   862  C  CA  . THR B 1 45 ? 27.827  16.509 109.858 1.00 32.58  ? 129 THR B CA  1 
ATOM   863  C  C   . THR B 1 45 ? 27.658  16.965 111.297 1.00 31.33  ? 129 THR B C   1 
ATOM   864  O  O   . THR B 1 45 ? 28.636  17.428 111.885 1.00 34.95  ? 129 THR B O   1 
ATOM   865  C  CB  . THR B 1 45 ? 28.073  17.762 109.004 1.00 31.93  ? 129 THR B CB  1 
ATOM   866  O  OG1 . THR B 1 45 ? 27.018  18.697 109.243 1.00 33.05  ? 129 THR B OG1 1 
ATOM   867  C  CG2 . THR B 1 45 ? 28.103  17.420 107.521 1.00 35.12  ? 129 THR B CG2 1 
ATOM   868  N  N   . GLY B 1 46 ? 26.452  16.911 111.865 1.00 30.76  ? 130 GLY B N   1 
ATOM   869  C  CA  . GLY B 1 46 ? 26.222  17.386 113.222 1.00 34.44  ? 130 GLY B CA  1 
ATOM   870  C  C   . GLY B 1 46 ? 26.058  18.883 113.386 1.00 35.77  ? 130 GLY B C   1 
ATOM   871  O  O   . GLY B 1 46 ? 25.891  19.351 114.521 1.00 35.30  ? 130 GLY B O   1 
ATOM   872  N  N   . GLN B 1 47 ? 26.083  19.646 112.304 1.00 34.38  ? 131 GLN B N   1 
ATOM   873  C  CA  . GLN B 1 47 ? 26.008  21.095 112.388 1.00 31.09  ? 131 GLN B CA  1 
ATOM   874  C  C   . GLN B 1 47 ? 24.547  21.552 112.307 1.00 31.37  ? 131 GLN B C   1 
ATOM   875  O  O   . GLN B 1 47 ? 23.679  20.839 111.793 1.00 30.69  ? 131 GLN B O   1 
ATOM   876  C  CB  . GLN B 1 47 ? 26.832  21.706 111.256 1.00 33.82  ? 131 GLN B CB  1 
ATOM   877  C  CG  . GLN B 1 47 ? 28.253  21.166 111.177 1.00 36.93  ? 131 GLN B CG  1 
ATOM   878  C  CD  . GLN B 1 47 ? 28.849  21.259 109.780 1.00 40.24  ? 131 GLN B CD  1 
ATOM   879  O  OE1 . GLN B 1 47 ? 28.348  21.986 108.917 1.00 43.76  ? 131 GLN B OE1 1 
ATOM   880  N  NE2 . GLN B 1 47 ? 29.926  20.504 109.545 1.00 43.04  ? 131 GLN B NE2 1 
ATOM   881  N  N   . THR B 1 48 ? 24.277  22.757 112.833 1.00 32.08  ? 132 THR B N   1 
ATOM   882  C  CA  . THR B 1 48 ? 22.919  23.301 112.905 1.00 30.13  ? 132 THR B CA  1 
ATOM   883  C  C   . THR B 1 48 ? 22.889  24.705 112.312 1.00 29.42  ? 132 THR B C   1 
ATOM   884  O  O   . THR B 1 48 ? 23.822  25.490 112.508 1.00 32.97  ? 132 THR B O   1 
ATOM   885  C  CB  . THR B 1 48 ? 22.432  23.357 114.376 1.00 30.45  ? 132 THR B CB  1 
ATOM   886  O  OG1 . THR B 1 48 ? 22.530  22.053 114.969 1.00 32.94  ? 132 THR B OG1 1 
ATOM   887  C  CG2 . THR B 1 48 ? 20.988  23.858 114.478 1.00 32.06  ? 132 THR B CG2 1 
ATOM   888  N  N   . GLY B 1 49 ? 21.823  25.023 111.587 1.00 26.42  ? 133 GLY B N   1 
ATOM   889  C  CA  . GLY B 1 49 ? 21.670  26.372 111.080 1.00 24.73  ? 133 GLY B CA  1 
ATOM   890  C  C   . GLY B 1 49 ? 20.516  26.478 110.107 1.00 23.31  ? 133 GLY B C   1 
ATOM   891  O  O   . GLY B 1 49 ? 19.874  25.496 109.761 1.00 21.76  ? 133 GLY B O   1 
ATOM   892  N  N   . TYR B 1 50 ? 20.260  27.710 109.688 1.00 21.93  ? 134 TYR B N   1 
ATOM   893  C  CA  . TYR B 1 50 ? 19.179  27.983 108.756 1.00 20.62  ? 134 TYR B CA  1 
ATOM   894  C  C   . TYR B 1 50 ? 19.544  27.580 107.334 1.00 22.02  ? 134 TYR B C   1 
ATOM   895  O  O   . TYR B 1 50 ? 20.697  27.722 106.901 1.00 20.60  ? 134 TYR B O   1 
ATOM   896  C  CB  . TYR B 1 50 ? 18.846  29.462 108.771 1.00 21.48  ? 134 TYR B CB  1 
ATOM   897  C  CG  . TYR B 1 50 ? 18.414  29.973 110.115 1.00 22.31  ? 134 TYR B CG  1 
ATOM   898  C  CD1 . TYR B 1 50 ? 17.271  29.477 110.738 1.00 23.34  ? 134 TYR B CD1 1 
ATOM   899  C  CD2 . TYR B 1 50 ? 19.139  30.959 110.759 1.00 21.11  ? 134 TYR B CD2 1 
ATOM   900  C  CE1 . TYR B 1 50 ? 16.884  29.944 111.975 1.00 21.96  ? 134 TYR B CE1 1 
ATOM   901  C  CE2 . TYR B 1 50 ? 18.745  31.440 111.986 1.00 21.81  ? 134 TYR B CE2 1 
ATOM   902  C  CZ  . TYR B 1 50 ? 17.622  30.940 112.588 1.00 22.73  ? 134 TYR B CZ  1 
ATOM   903  O  OH  . TYR B 1 50 ? 17.233  31.436 113.817 1.00 24.91  ? 134 TYR B OH  1 
ATOM   904  N  N   . ILE B 1 51 ? 18.544  27.096 106.600 1.00 19.90  ? 135 ILE B N   1 
ATOM   905  C  CA  . ILE B 1 51 ? 18.734  26.658 105.216 1.00 20.50  ? 135 ILE B CA  1 
ATOM   906  C  C   . ILE B 1 51 ? 17.607  27.223 104.360 1.00 20.96  ? 135 ILE B C   1 
ATOM   907  O  O   . ILE B 1 51 ? 16.513  27.487 104.872 1.00 19.64  ? 135 ILE B O   1 
ATOM   908  C  CB  . ILE B 1 51 ? 18.759  25.129 105.087 1.00 20.89  ? 135 ILE B CB  1 
ATOM   909  C  CG1 . ILE B 1 51 ? 17.386  24.528 105.427 1.00 22.65  ? 135 ILE B CG1 1 
ATOM   910  C  CG2 . ILE B 1 51 ? 19.840  24.539 105.976 1.00 22.34  ? 135 ILE B CG2 1 
ATOM   911  C  CD1 . ILE B 1 51 ? 17.267  23.083 105.048 1.00 26.57  ? 135 ILE B CD1 1 
ATOM   912  N  N   . PRO B 1 52 ? 17.823  27.435 103.064 1.00 21.27  ? 136 PRO B N   1 
ATOM   913  C  CA  . PRO B 1 52 ? 16.715  27.874 102.203 1.00 22.29  ? 136 PRO B CA  1 
ATOM   914  C  C   . PRO B 1 52 ? 15.697  26.755 102.104 1.00 23.89  ? 136 PRO B C   1 
ATOM   915  O  O   . PRO B 1 52 ? 16.059  25.617 101.821 1.00 25.39  ? 136 PRO B O   1 
ATOM   916  C  CB  . PRO B 1 52 ? 17.387  28.103 100.844 1.00 25.33  ? 136 PRO B CB  1 
ATOM   917  C  CG  . PRO B 1 52 ? 18.857  28.110 101.104 1.00 26.86  ? 136 PRO B CG  1 
ATOM   918  C  CD  . PRO B 1 52 ? 19.087  27.296 102.325 1.00 22.14  ? 136 PRO B CD  1 
ATOM   919  N  N   . SER B 1 53 ? 14.419  27.092 102.301 1.00 24.46  ? 137 SER B N   1 
ATOM   920  C  CA  . SER B 1 53 ? 13.381  26.070 102.366 1.00 27.74  ? 137 SER B CA  1 
ATOM   921  C  C   . SER B 1 53 ? 13.260  25.289 101.065 1.00 28.34  ? 137 SER B C   1 
ATOM   922  O  O   . SER B 1 53 ? 12.924  24.098 101.091 1.00 33.14  ? 137 SER B O   1 
ATOM   923  C  CB  . SER B 1 53 ? 12.041  26.700 102.740 1.00 29.96  ? 137 SER B CB  1 
ATOM   924  O  OG  . SER B 1 53 ? 11.584  27.562 101.716 1.00 31.32  ? 137 SER B OG  1 
ATOM   925  N  N   . ASN B 1 54 ? 13.525  25.923 99.926  1.00 28.02  ? 138 ASN B N   1 
ATOM   926  C  CA  . ASN B 1 54 ? 13.349  25.232 98.657  1.00 29.40  ? 138 ASN B CA  1 
ATOM   927  C  C   . ASN B 1 54 ? 14.545  24.372 98.272  1.00 30.46  ? 138 ASN B C   1 
ATOM   928  O  O   . ASN B 1 54 ? 14.542  23.799 97.176  1.00 32.96  ? 138 ASN B O   1 
ATOM   929  C  CB  . ASN B 1 54 ? 12.975  26.216 97.537  1.00 32.54  ? 138 ASN B CB  1 
ATOM   930  C  CG  . ASN B 1 54 ? 14.090  27.191 97.205  1.00 36.10  ? 138 ASN B CG  1 
ATOM   931  O  OD1 . ASN B 1 54 ? 14.904  27.547 98.056  1.00 37.44  ? 138 ASN B OD1 1 
ATOM   932  N  ND2 . ASN B 1 54 ? 14.120  27.639 95.959  1.00 42.14  ? 138 ASN B ND2 1 
ATOM   933  N  N   . TYR B 1 55 ? 15.545  24.240 99.145  1.00 28.49  ? 139 TYR B N   1 
ATOM   934  C  CA  . TYR B 1 55 ? 16.720  23.425 98.865  1.00 28.58  ? 139 TYR B CA  1 
ATOM   935  C  C   . TYR B 1 55 ? 16.604  22.000 99.374  1.00 26.30  ? 139 TYR B C   1 
ATOM   936  O  O   . TYR B 1 55 ? 17.569  21.237 99.246  1.00 26.96  ? 139 TYR B O   1 
ATOM   937  C  CB  . TYR B 1 55 ? 17.961  24.047 99.500  1.00 28.35  ? 139 TYR B CB  1 
ATOM   938  C  CG  . TYR B 1 55 ? 18.676  25.037 98.629  1.00 30.06  ? 139 TYR B CG  1 
ATOM   939  C  CD1 . TYR B 1 55 ? 17.993  26.098 98.040  1.00 30.80  ? 139 TYR B CD1 1 
ATOM   940  C  CD2 . TYR B 1 55 ? 20.048  24.944 98.431  1.00 27.91  ? 139 TYR B CD2 1 
ATOM   941  C  CE1 . TYR B 1 55 ? 18.651  27.006 97.257  1.00 32.49  ? 139 TYR B CE1 1 
ATOM   942  C  CE2 . TYR B 1 55 ? 20.716  25.855 97.653  1.00 32.94  ? 139 TYR B CE2 1 
ATOM   943  C  CZ  . TYR B 1 55 ? 20.013  26.884 97.071  1.00 33.24  ? 139 TYR B CZ  1 
ATOM   944  O  OH  . TYR B 1 55 ? 20.667  27.800 96.289  1.00 39.15  ? 139 TYR B OH  1 
ATOM   945  N  N   . VAL B 1 56 ? 15.470  21.621 99.960  1.00 27.12  ? 140 VAL B N   1 
ATOM   946  C  CA  . VAL B 1 56 ? 15.320  20.309 100.568 1.00 26.50  ? 140 VAL B CA  1 
ATOM   947  C  C   . VAL B 1 56 ? 13.969  19.714 100.195 1.00 29.04  ? 140 VAL B C   1 
ATOM   948  O  O   . VAL B 1 56 ? 13.007  20.423 99.884  1.00 29.39  ? 140 VAL B O   1 
ATOM   949  C  CB  . VAL B 1 56 ? 15.498  20.354 102.103 1.00 26.84  ? 140 VAL B CB  1 
ATOM   950  C  CG1 . VAL B 1 56 ? 16.927  20.729 102.465 1.00 27.61  ? 140 VAL B CG1 1 
ATOM   951  C  CG2 . VAL B 1 56 ? 14.512  21.350 102.735 1.00 27.29  ? 140 VAL B CG2 1 
ATOM   952  N  N   . ALA B 1 57 ? 13.910  18.391 100.226 1.00 29.07  ? 141 ALA B N   1 
ATOM   953  C  CA  . ALA B 1 57 ? 12.674  17.654 100.022 1.00 29.57  ? 141 ALA B CA  1 
ATOM   954  C  C   . ALA B 1 57 ? 12.645  16.514 101.025 1.00 30.86  ? 141 ALA B C   1 
ATOM   955  O  O   . ALA B 1 57 ? 13.698  16.078 101.500 1.00 30.59  ? 141 ALA B O   1 
ATOM   956  C  CB  . ALA B 1 57 ? 12.588  17.090 98.598  1.00 31.61  ? 141 ALA B CB  1 
ATOM   957  N  N   . PRO B 1 58 ? 11.456  16.016 101.372 1.00 32.94  ? 142 PRO B N   1 
ATOM   958  C  CA  . PRO B 1 58 ? 11.383  14.853 102.261 1.00 34.93  ? 142 PRO B CA  1 
ATOM   959  C  C   . PRO B 1 58 ? 12.161  13.690 101.678 1.00 37.32  ? 142 PRO B C   1 
ATOM   960  O  O   . PRO B 1 58 ? 12.162  13.467 100.465 1.00 38.23  ? 142 PRO B O   1 
ATOM   961  C  CB  . PRO B 1 58 ? 9.885   14.527 102.307 1.00 35.85  ? 142 PRO B CB  1 
ATOM   962  C  CG  . PRO B 1 58 ? 9.205   15.716 101.831 1.00 36.62  ? 142 PRO B CG  1 
ATOM   963  C  CD  . PRO B 1 58 ? 10.125  16.491 100.965 1.00 36.43  ? 142 PRO B CD  1 
ATOM   964  N  N   . SER B 1 59 ? 12.835  12.953 102.552 1.00 39.32  ? 143 SER B N   1 
ATOM   965  C  CA  . SER B 1 59 ? 13.542  11.757 102.135 1.00 44.06  ? 143 SER B CA  1 
ATOM   966  C  C   . SER B 1 59 ? 12.522  10.665 101.869 1.00 49.60  ? 143 SER B C   1 
ATOM   967  O  O   . SER B 1 59 ? 12.689  9.860  100.955 1.00 53.37  ? 143 SER B O   1 
ATOM   968  C  CB  . SER B 1 59 ? 14.521  11.302 103.215 1.00 44.78  ? 143 SER B CB  1 
ATOM   969  O  OG  . SER B 1 59 ? 15.483  12.306 103.472 1.00 47.61  ? 143 SER B OG  1 
ATOM   970  O  OXT . SER B 1 59 ? 11.508  10.579 102.565 1.00 50.53  ? 143 SER B OXT 1 
ATOM   971  N  N   . GLY C 1 1  ? -2.753  28.318 116.058 1.00 36.58  ? 85  GLY C N   1 
ATOM   972  C  CA  . GLY C 1 1  ? -3.252  27.160 116.773 1.00 34.10  ? 85  GLY C CA  1 
ATOM   973  C  C   . GLY C 1 1  ? -3.127  25.910 115.924 1.00 29.99  ? 85  GLY C C   1 
ATOM   974  O  O   . GLY C 1 1  ? -2.955  25.999 114.709 1.00 35.75  ? 85  GLY C O   1 
ATOM   975  N  N   . VAL C 1 2  ? -3.222  24.742 116.556 1.00 28.34  ? 86  VAL C N   1 
ATOM   976  C  CA  . VAL C 1 2  ? -3.077  23.478 115.838 1.00 27.35  ? 86  VAL C CA  1 
ATOM   977  C  C   . VAL C 1 2  ? -4.229  23.330 114.850 1.00 25.70  ? 86  VAL C C   1 
ATOM   978  O  O   . VAL C 1 2  ? -5.397  23.264 115.248 1.00 27.99  ? 86  VAL C O   1 
ATOM   979  C  CB  . VAL C 1 2  ? -3.062  22.313 116.828 1.00 29.95  ? 86  VAL C CB  1 
ATOM   980  C  CG1 . VAL C 1 2  ? -3.032  21.019 116.087 1.00 28.44  ? 86  VAL C CG1 1 
ATOM   981  C  CG2 . VAL C 1 2  ? -1.869  22.429 117.759 1.00 31.21  ? 86  VAL C CG2 1 
ATOM   982  N  N   . THR C 1 3  ? -3.907  23.270 113.552 1.00 23.07  ? 87  THR C N   1 
ATOM   983  C  CA  . THR C 1 3  ? -4.923  23.195 112.500 1.00 21.77  ? 87  THR C CA  1 
ATOM   984  C  C   . THR C 1 3  ? -4.768  21.866 111.773 1.00 20.54  ? 87  THR C C   1 
ATOM   985  O  O   . THR C 1 3  ? -3.756  21.639 111.111 1.00 22.26  ? 87  THR C O   1 
ATOM   986  C  CB  . THR C 1 3  ? -4.745  24.343 111.514 1.00 23.45  ? 87  THR C CB  1 
ATOM   987  O  OG1 . THR C 1 3  ? -5.041  25.580 112.162 1.00 26.44  ? 87  THR C OG1 1 
ATOM   988  C  CG2 . THR C 1 3  ? -5.666  24.158 110.333 1.00 25.77  ? 87  THR C CG2 1 
ATOM   989  N  N   . THR C 1 4  ? -5.767  20.997 111.873 1.00 20.83  ? 88  THR C N   1 
ATOM   990  C  CA  . THR C 1 4  ? -5.698  19.684 111.247 1.00 19.68  ? 88  THR C CA  1 
ATOM   991  C  C   . THR C 1 4  ? -6.758  19.575 110.164 1.00 22.29  ? 88  THR C C   1 
ATOM   992  O  O   . THR C 1 4  ? -7.942  19.812 110.415 1.00 21.42  ? 88  THR C O   1 
ATOM   993  C  CB  . THR C 1 4  ? -5.889  18.552 112.255 1.00 21.81  ? 88  THR C CB  1 
ATOM   994  O  OG1 . THR C 1 4  ? -4.979  18.726 113.347 1.00 23.54  ? 88  THR C OG1 1 
ATOM   995  C  CG2 . THR C 1 4  ? -5.612  17.209 111.590 1.00 23.37  ? 88  THR C CG2 1 
ATOM   996  N  N   . PHE C 1 5  ? -6.332  19.195 108.973 1.00 19.33  ? 89  PHE C N   1 
ATOM   997  C  CA  . PHE C 1 5  ? -7.219  18.919 107.856 1.00 18.53  ? 89  PHE C CA  1 
ATOM   998  C  C   . PHE C 1 5  ? -7.168  17.433 107.532 1.00 18.21  ? 89  PHE C C   1 
ATOM   999  O  O   . PHE C 1 5  ? -6.304  16.689 108.018 1.00 20.37  ? 89  PHE C O   1 
ATOM   1000 C  CB  . PHE C 1 5  ? -6.835  19.781 106.639 1.00 19.14  ? 89  PHE C CB  1 
ATOM   1001 C  CG  . PHE C 1 5  ? -7.469  21.146 106.664 1.00 20.61  ? 89  PHE C CG  1 
ATOM   1002 C  CD1 . PHE C 1 5  ? -7.267  22.000 107.746 1.00 22.04  ? 89  PHE C CD1 1 
ATOM   1003 C  CD2 . PHE C 1 5  ? -8.267  21.580 105.620 1.00 22.05  ? 89  PHE C CD2 1 
ATOM   1004 C  CE1 . PHE C 1 5  ? -7.864  23.253 107.781 1.00 23.06  ? 89  PHE C CE1 1 
ATOM   1005 C  CE2 . PHE C 1 5  ? -8.860  22.825 105.654 1.00 23.74  ? 89  PHE C CE2 1 
ATOM   1006 C  CZ  . PHE C 1 5  ? -8.654  23.661 106.735 1.00 24.48  ? 89  PHE C CZ  1 
ATOM   1007 N  N   . VAL C 1 6  ? -8.095  17.001 106.686 1.00 18.48  ? 90  VAL C N   1 
ATOM   1008 C  CA  . VAL C 1 6  ? -8.157  15.613 106.250 1.00 19.85  ? 90  VAL C CA  1 
ATOM   1009 C  C   . VAL C 1 6  ? -8.255  15.574 104.733 1.00 20.36  ? 90  VAL C C   1 
ATOM   1010 O  O   . VAL C 1 6  ? -8.963  16.383 104.124 1.00 21.52  ? 90  VAL C O   1 
ATOM   1011 C  CB  . VAL C 1 6  ? -9.317  14.843 106.922 1.00 20.48  ? 90  VAL C CB  1 
ATOM   1012 C  CG1 . VAL C 1 6  ? -10.684 15.460 106.572 1.00 21.79  ? 90  VAL C CG1 1 
ATOM   1013 C  CG2 . VAL C 1 6  ? -9.259  13.345 106.558 1.00 22.98  ? 90  VAL C CG2 1 
ATOM   1014 N  N   . ALA C 1 7  ? -7.529  14.635 104.128 1.00 20.69  ? 91  ALA C N   1 
ATOM   1015 C  CA  . ALA C 1 7  ? -7.579  14.442 102.686 1.00 22.38  ? 91  ALA C CA  1 
ATOM   1016 C  C   . ALA C 1 7  ? -8.919  13.843 102.267 1.00 24.26  ? 91  ALA C C   1 
ATOM   1017 O  O   . ALA C 1 7  ? -9.376  12.845 102.834 1.00 24.60  ? 91  ALA C O   1 
ATOM   1018 C  CB  . ALA C 1 7  ? -6.454  13.514 102.250 1.00 22.08  ? 91  ALA C CB  1 
ATOM   1019 N  N   . LEU C 1 8  ? -9.534  14.449 101.258 1.00 24.19  ? 92  LEU C N   1 
ATOM   1020 C  CA  . LEU C 1 8  ? -10.779 13.971 100.679 1.00 24.70  ? 92  LEU C CA  1 
ATOM   1021 C  C   . LEU C 1 8  ? -10.559 12.972 99.554  1.00 25.69  ? 92  LEU C C   1 
ATOM   1022 O  O   . LEU C 1 8  ? -11.495 12.241 99.200  1.00 26.66  ? 92  LEU C O   1 
ATOM   1023 C  CB  . LEU C 1 8  ? -11.554 15.165 100.120 1.00 25.63  ? 92  LEU C CB  1 
ATOM   1024 C  CG  . LEU C 1 8  ? -11.787 16.294 101.119 1.00 27.85  ? 92  LEU C CG  1 
ATOM   1025 C  CD1 . LEU C 1 8  ? -12.197 17.570 100.391 1.00 29.85  ? 92  LEU C CD1 1 
ATOM   1026 C  CD2 . LEU C 1 8  ? -12.852 15.888 102.132 1.00 29.20  ? 92  LEU C CD2 1 
ATOM   1027 N  N   . TYR C 1 9  ? -9.356  12.939 98.976  1.00 26.49  ? 93  TYR C N   1 
ATOM   1028 C  CA  . TYR C 1 9  ? -9.043  12.064 97.858  1.00 28.02  ? 93  TYR C CA  1 
ATOM   1029 C  C   . TYR C 1 9  ? -7.589  11.647 97.974  1.00 24.67  ? 93  TYR C C   1 
ATOM   1030 O  O   . TYR C 1 9  ? -6.779  12.332 98.607  1.00 27.15  ? 93  TYR C O   1 
ATOM   1031 C  CB  . TYR C 1 9  ? -9.191  12.795 96.518  1.00 30.83  ? 93  TYR C CB  1 
ATOM   1032 C  CG  . TYR C 1 9  ? -10.392 13.689 96.444  1.00 32.48  ? 93  TYR C CG  1 
ATOM   1033 C  CD1 . TYR C 1 9  ? -11.643 13.163 96.176  1.00 36.43  ? 93  TYR C CD1 1 
ATOM   1034 C  CD2 . TYR C 1 9  ? -10.281 15.061 96.656  1.00 32.90  ? 93  TYR C CD2 1 
ATOM   1035 C  CE1 . TYR C 1 9  ? -12.744 13.967 96.113  1.00 39.08  ? 93  TYR C CE1 1 
ATOM   1036 C  CE2 . TYR C 1 9  ? -11.387 15.881 96.591  1.00 36.19  ? 93  TYR C CE2 1 
ATOM   1037 C  CZ  . TYR C 1 9  ? -12.613 15.324 96.324  1.00 39.89  ? 93  TYR C CZ  1 
ATOM   1038 O  OH  . TYR C 1 9  ? -13.721 16.126 96.261  1.00 44.30  ? 93  TYR C OH  1 
ATOM   1039 N  N   . ASP C 1 10 ? -7.256  10.532 97.323  1.00 27.18  ? 94  ASP C N   1 
ATOM   1040 C  CA  . ASP C 1 10 ? -5.854  10.177 97.157  1.00 27.12  ? 94  ASP C CA  1 
ATOM   1041 C  C   . ASP C 1 10 ? -5.174  11.217 96.273  1.00 28.17  ? 94  ASP C C   1 
ATOM   1042 O  O   . ASP C 1 10 ? -5.778  11.775 95.352  1.00 29.38  ? 94  ASP C O   1 
ATOM   1043 C  CB  . ASP C 1 10 ? -5.708  8.831  96.450  1.00 28.63  ? 94  ASP C CB  1 
ATOM   1044 C  CG  . ASP C 1 10 ? -6.231  7.647  97.259  1.00 32.52  ? 94  ASP C CG  1 
ATOM   1045 O  OD1 . ASP C 1 10 ? -6.488  7.754  98.474  1.00 32.30  ? 94  ASP C OD1 1 
ATOM   1046 O  OD2 . ASP C 1 10 ? -6.380  6.574  96.652  1.00 36.68  ? 94  ASP C OD2 1 
ATOM   1047 N  N   . TYR C 1 11 ? -3.898  11.471 96.542  1.00 24.81  ? 95  TYR C N   1 
ATOM   1048 C  CA  . TYR C 1 11 ? -3.108  12.325 95.665  1.00 25.44  ? 95  TYR C CA  1 
ATOM   1049 C  C   . TYR C 1 11 ? -1.718  11.735 95.512  1.00 25.67  ? 95  TYR C C   1 
ATOM   1050 O  O   . TYR C 1 11 ? -1.028  11.498 96.506  1.00 26.78  ? 95  TYR C O   1 
ATOM   1051 C  CB  . TYR C 1 11 ? -3.014  13.764 96.197  1.00 25.21  ? 95  TYR C CB  1 
ATOM   1052 C  CG  . TYR C 1 11 ? -2.282  14.699 95.254  1.00 24.87  ? 95  TYR C CG  1 
ATOM   1053 C  CD1 . TYR C 1 11 ? -2.806  15.003 94.000  1.00 26.55  ? 95  TYR C CD1 1 
ATOM   1054 C  CD2 . TYR C 1 11 ? -1.056  15.266 95.608  1.00 25.21  ? 95  TYR C CD2 1 
ATOM   1055 C  CE1 . TYR C 1 11 ? -2.133  15.853 93.136  1.00 26.13  ? 95  TYR C CE1 1 
ATOM   1056 C  CE2 . TYR C 1 11 ? -0.388  16.118 94.757  1.00 24.71  ? 95  TYR C CE2 1 
ATOM   1057 C  CZ  . TYR C 1 11 ? -0.932  16.404 93.518  1.00 27.21  ? 95  TYR C CZ  1 
ATOM   1058 O  OH  . TYR C 1 11 ? -0.267  17.238 92.654  1.00 28.18  ? 95  TYR C OH  1 
ATOM   1059 N  N   . GLU C 1 12 ? -1.310  11.502 94.270  1.00 26.15  ? 96  GLU C N   1 
ATOM   1060 C  CA  . GLU C 1 12 ? 0.053   11.095 93.959  1.00 25.82  ? 96  GLU C CA  1 
ATOM   1061 C  C   . GLU C 1 12 ? 0.782   12.319 93.417  1.00 23.91  ? 96  GLU C C   1 
ATOM   1062 O  O   . GLU C 1 12 ? 0.457   12.823 92.333  1.00 27.42  ? 96  GLU C O   1 
ATOM   1063 C  CB  . GLU C 1 12 ? 0.074   9.933  92.968  1.00 31.73  ? 96  GLU C CB  1 
ATOM   1064 C  CG  . GLU C 1 12 ? 1.452   9.291  92.845  1.00 40.01  ? 96  GLU C CG  1 
ATOM   1065 C  CD  . GLU C 1 12 ? 2.023   8.841  94.193  1.00 50.26  ? 96  GLU C CD  1 
ATOM   1066 O  OE1 . GLU C 1 12 ? 1.241   8.472  95.104  1.00 51.97  ? 96  GLU C OE1 1 
ATOM   1067 O  OE2 . GLU C 1 12 ? 3.264   8.865  94.344  1.00 53.74  ? 96  GLU C OE2 1 
ATOM   1068 N  N   . SER C 1 13 ? 1.745   12.816 94.182  1.00 23.57  ? 97  SER C N   1 
ATOM   1069 C  CA  . SER C 1 13 ? 2.323   14.110 93.861  1.00 24.34  ? 97  SER C CA  1 
ATOM   1070 C  C   . SER C 1 13 ? 3.283   14.014 92.678  1.00 22.87  ? 97  SER C C   1 
ATOM   1071 O  O   . SER C 1 13 ? 3.690   12.935 92.242  1.00 25.93  ? 97  SER C O   1 
ATOM   1072 C  CB  . SER C 1 13 ? 3.011   14.709 95.079  1.00 28.17  ? 97  SER C CB  1 
ATOM   1073 O  OG  . SER C 1 13 ? 4.232   14.056 95.324  1.00 30.74  ? 97  SER C OG  1 
ATOM   1074 N  N   . ARG C 1 14 ? 3.651   15.183 92.167  1.00 23.19  ? 98  ARG C N   1 
ATOM   1075 C  CA  . ARG C 1 14 ? 4.442   15.293 90.953  1.00 22.74  ? 98  ARG C CA  1 
ATOM   1076 C  C   . ARG C 1 14 ? 5.868   15.734 91.217  1.00 23.16  ? 98  ARG C C   1 
ATOM   1077 O  O   . ARG C 1 14 ? 6.685   15.743 90.287  1.00 25.75  ? 98  ARG C O   1 
ATOM   1078 C  CB  . ARG C 1 14 ? 3.774   16.273 89.980  1.00 24.57  ? 98  ARG C CB  1 
ATOM   1079 C  CG  . ARG C 1 14 ? 2.322   15.931 89.689  1.00 22.25  ? 98  ARG C CG  1 
ATOM   1080 C  CD  . ARG C 1 14 ? 2.211   14.573 89.008  1.00 23.02  ? 98  ARG C CD  1 
ATOM   1081 N  NE  . ARG C 1 14 ? 2.781   14.617 87.666  1.00 23.86  ? 98  ARG C NE  1 
ATOM   1082 C  CZ  . ARG C 1 14 ? 2.946   13.557 86.889  1.00 23.37  ? 98  ARG C CZ  1 
ATOM   1083 N  NH1 . ARG C 1 14 ? 2.635   12.332 87.305  1.00 24.79  ? 98  ARG C NH1 1 
ATOM   1084 N  NH2 . ARG C 1 14 ? 3.430   13.727 85.660  1.00 24.74  ? 98  ARG C NH2 1 
ATOM   1085 N  N   . THR C 1 15 ? 6.189   16.087 92.457  1.00 24.09  ? 99  THR C N   1 
ATOM   1086 C  CA  . THR C 1 15 ? 7.531   16.501 92.818  1.00 26.38  ? 99  THR C CA  1 
ATOM   1087 C  C   . THR C 1 15 ? 7.746   16.131 94.275  1.00 26.63  ? 99  THR C C   1 
ATOM   1088 O  O   . THR C 1 15 ? 6.793   16.000 95.047  1.00 25.64  ? 99  THR C O   1 
ATOM   1089 C  CB  . THR C 1 15 ? 7.743   18.005 92.568  1.00 27.72  ? 99  THR C CB  1 
ATOM   1090 O  OG1 . THR C 1 15 ? 9.106   18.350 92.829  1.00 30.82  ? 99  THR C OG1 1 
ATOM   1091 C  CG2 . THR C 1 15 ? 6.820   18.861 93.449  1.00 28.76  ? 99  THR C CG2 1 
ATOM   1092 N  N   . GLU C 1 16 ? 9.015   15.960 94.645  1.00 28.95  ? 100 GLU C N   1 
ATOM   1093 C  CA  . GLU C 1 16 ? 9.320   15.459 95.977  1.00 30.05  ? 100 GLU C CA  1 
ATOM   1094 C  C   . GLU C 1 16 ? 8.902   16.418 97.083  1.00 27.28  ? 100 GLU C C   1 
ATOM   1095 O  O   . GLU C 1 16 ? 8.652   15.968 98.204  1.00 30.38  ? 100 GLU C O   1 
ATOM   1096 C  CB  . GLU C 1 16 ? 10.805  15.126 96.073  1.00 34.63  ? 100 GLU C CB  1 
ATOM   1097 C  CG  . GLU C 1 16 ? 11.207  13.921 95.211  1.00 43.38  ? 100 GLU C CG  1 
ATOM   1098 C  CD  . GLU C 1 16 ? 10.758  12.594 95.813  1.00 53.62  ? 100 GLU C CD  1 
ATOM   1099 O  OE1 . GLU C 1 16 ? 11.224  12.255 96.924  1.00 57.31  ? 100 GLU C OE1 1 
ATOM   1100 O  OE2 . GLU C 1 16 ? 9.939   11.891 95.177  1.00 57.91  ? 100 GLU C OE2 1 
ATOM   1101 N  N   . THR C 1 17 ? 8.799   17.719 96.790  1.00 24.87  ? 101 THR C N   1 
ATOM   1102 C  CA  . THR C 1 17 ? 8.440   18.708 97.801  1.00 23.56  ? 101 THR C CA  1 
ATOM   1103 C  C   . THR C 1 17 ? 6.941   18.779 98.072  1.00 21.78  ? 101 THR C C   1 
ATOM   1104 O  O   . THR C 1 17 ? 6.533   19.465 99.018  1.00 23.93  ? 101 THR C O   1 
ATOM   1105 C  CB  . THR C 1 17 ? 8.988   20.080 97.405  1.00 23.49  ? 101 THR C CB  1 
ATOM   1106 O  OG1 . THR C 1 17 ? 8.668   20.349 96.034  1.00 26.48  ? 101 THR C OG1 1 
ATOM   1107 C  CG2 . THR C 1 17 ? 10.494  20.112 97.601  1.00 24.60  ? 101 THR C CG2 1 
ATOM   1108 N  N   . ASP C 1 18 ? 6.123   18.100 97.266  1.00 22.34  ? 102 ASP C N   1 
ATOM   1109 C  CA  . ASP C 1 18 ? 4.690   17.959 97.495  1.00 22.29  ? 102 ASP C CA  1 
ATOM   1110 C  C   . ASP C 1 18 ? 4.423   16.572 98.079  1.00 22.30  ? 102 ASP C C   1 
ATOM   1111 O  O   . ASP C 1 18 ? 4.987   15.577 97.621  1.00 24.91  ? 102 ASP C O   1 
ATOM   1112 C  CB  . ASP C 1 18 ? 3.919   18.096 96.173  1.00 21.36  ? 102 ASP C CB  1 
ATOM   1113 C  CG  . ASP C 1 18 ? 3.928   19.520 95.611  1.00 22.27  ? 102 ASP C CG  1 
ATOM   1114 O  OD1 . ASP C 1 18 ? 4.317   20.476 96.315  1.00 24.01  ? 102 ASP C OD1 1 
ATOM   1115 O  OD2 . ASP C 1 18 ? 3.518   19.686 94.440  1.00 22.88  ? 102 ASP C OD2 1 
ATOM   1116 N  N   . LEU C 1 19 ? 3.574   16.504 99.100  1.00 20.97  ? 103 LEU C N   1 
ATOM   1117 C  CA  . LEU C 1 19 ? 3.248   15.214 99.700  1.00 20.63  ? 103 LEU C CA  1 
ATOM   1118 C  C   . LEU C 1 19 ? 2.310   14.414 98.801  1.00 22.96  ? 103 LEU C C   1 
ATOM   1119 O  O   . LEU C 1 19 ? 1.396   14.964 98.182  1.00 24.81  ? 103 LEU C O   1 
ATOM   1120 C  CB  . LEU C 1 19 ? 2.558   15.411 101.052 1.00 21.99  ? 103 LEU C CB  1 
ATOM   1121 C  CG  . LEU C 1 19 ? 3.350   16.024 102.198 1.00 23.71  ? 103 LEU C CG  1 
ATOM   1122 C  CD1 . LEU C 1 19 ? 2.488   16.089 103.441 1.00 25.13  ? 103 LEU C CD1 1 
ATOM   1123 C  CD2 . LEU C 1 19 ? 4.639   15.233 102.484 1.00 27.78  ? 103 LEU C CD2 1 
ATOM   1124 N  N   . SER C 1 20 ? 2.539   13.108 98.731  1.00 21.87  ? 104 SER C N   1 
ATOM   1125 C  CA  . SER C 1 20 ? 1.508   12.184 98.297  1.00 21.76  ? 104 SER C CA  1 
ATOM   1126 C  C   . SER C 1 20 ? 0.752   11.744 99.541  1.00 23.04  ? 104 SER C C   1 
ATOM   1127 O  O   . SER C 1 20 ? 1.323   11.651 100.628 1.00 27.05  ? 104 SER C O   1 
ATOM   1128 C  CB  . SER C 1 20 ? 2.127   10.960 97.622  1.00 24.17  ? 104 SER C CB  1 
ATOM   1129 O  OG  . SER C 1 20 ? 2.834   11.331 96.446  1.00 27.03  ? 104 SER C OG  1 
ATOM   1130 N  N   . PHE C 1 21 ? -0.550  11.519 99.391  1.00 21.80  ? 105 PHE C N   1 
ATOM   1131 C  CA  . PHE C 1 21 ? -1.353  11.125 100.540 1.00 22.06  ? 105 PHE C CA  1 
ATOM   1132 C  C   . PHE C 1 21 ? -2.546  10.305 100.083 1.00 24.66  ? 105 PHE C C   1 
ATOM   1133 O  O   . PHE C 1 21 ? -2.870  10.242 98.897  1.00 25.38  ? 105 PHE C O   1 
ATOM   1134 C  CB  . PHE C 1 21 ? -1.800  12.343 101.365 1.00 21.87  ? 105 PHE C CB  1 
ATOM   1135 C  CG  . PHE C 1 21 ? -2.405  13.464 100.539 1.00 21.74  ? 105 PHE C CG  1 
ATOM   1136 C  CD1 . PHE C 1 21 ? -3.753  13.447 100.187 1.00 22.39  ? 105 PHE C CD1 1 
ATOM   1137 C  CD2 . PHE C 1 21 ? -1.624  14.526 100.116 1.00 22.94  ? 105 PHE C CD2 1 
ATOM   1138 C  CE1 . PHE C 1 21 ? -4.311  14.486 99.445  1.00 22.21  ? 105 PHE C CE1 1 
ATOM   1139 C  CE2 . PHE C 1 21 ? -2.170  15.563 99.366  1.00 22.82  ? 105 PHE C CE2 1 
ATOM   1140 C  CZ  . PHE C 1 21 ? -3.516  15.541 99.022  1.00 23.17  ? 105 PHE C CZ  1 
ATOM   1141 N  N   . LYS C 1 22 ? -3.192  9.658  101.046 1.00 24.49  ? 106 LYS C N   1 
ATOM   1142 C  CA  . LYS C 1 22 ? -4.374  8.852  100.784 1.00 24.98  ? 106 LYS C CA  1 
ATOM   1143 C  C   . LYS C 1 22 ? -5.600  9.535  101.369 1.00 24.88  ? 106 LYS C C   1 
ATOM   1144 O  O   . LYS C 1 22 ? -5.512  10.271 102.356 1.00 23.88  ? 106 LYS C O   1 
ATOM   1145 C  CB  . LYS C 1 22 ? -4.252  7.463  101.419 1.00 26.88  ? 106 LYS C CB  1 
ATOM   1146 C  CG  . LYS C 1 22 ? -3.110  6.628  100.886 1.00 32.48  ? 106 LYS C CG  1 
ATOM   1147 C  CD  . LYS C 1 22 ? -3.259  6.418  99.394  1.00 40.27  ? 106 LYS C CD  1 
ATOM   1148 C  CE  . LYS C 1 22 ? -2.339  5.316  98.880  1.00 44.85  ? 106 LYS C CE  1 
ATOM   1149 N  NZ  . LYS C 1 22 ? -0.894  5.617  99.108  1.00 49.16  ? 106 LYS C NZ  1 
ATOM   1150 N  N   . LYS C 1 23 ? -6.747  9.275  100.757 1.00 25.20  ? 107 LYS C N   1 
ATOM   1151 C  CA  . LYS C 1 23 ? -8.024  9.682  101.327 1.00 26.86  ? 107 LYS C CA  1 
ATOM   1152 C  C   . LYS C 1 23 ? -8.084  9.301  102.802 1.00 24.49  ? 107 LYS C C   1 
ATOM   1153 O  O   . LYS C 1 23 ? -7.743  8.175  103.185 1.00 26.83  ? 107 LYS C O   1 
ATOM   1154 C  CB  . LYS C 1 23 ? -9.151  8.987  100.559 1.00 27.41  ? 107 LYS C CB  1 
ATOM   1155 C  CG  . LYS C 1 23 ? -10.544 9.292  101.050 1.00 30.77  ? 107 LYS C CG  1 
ATOM   1156 C  CD  . LYS C 1 23 ? -11.550 8.480  100.243 1.00 34.30  ? 107 LYS C CD  1 
ATOM   1157 C  CE  . LYS C 1 23 ? -12.812 9.252  99.956  1.00 42.37  ? 107 LYS C CE  1 
ATOM   1158 N  NZ  . LYS C 1 23 ? -13.662 9.342  101.164 1.00 46.74  ? 107 LYS C NZ  1 
ATOM   1159 N  N   . GLY C 1 24 ? -8.487  10.261 103.639 1.00 24.23  ? 108 GLY C N   1 
ATOM   1160 C  CA  . GLY C 1 24 ? -8.583  10.041 105.068 1.00 24.75  ? 108 GLY C CA  1 
ATOM   1161 C  C   . GLY C 1 24 ? -7.331  10.368 105.859 1.00 23.09  ? 108 GLY C C   1 
ATOM   1162 O  O   . GLY C 1 24 ? -7.383  10.365 107.093 1.00 25.44  ? 108 GLY C O   1 
ATOM   1163 N  N   . GLU C 1 25 ? -6.213  10.636 105.193 1.00 22.59  ? 109 GLU C N   1 
ATOM   1164 C  CA  . GLU C 1 25 ? -4.993  11.008 105.889 1.00 21.71  ? 109 GLU C CA  1 
ATOM   1165 C  C   . GLU C 1 25 ? -5.175  12.379 106.535 1.00 21.71  ? 109 GLU C C   1 
ATOM   1166 O  O   . GLU C 1 25 ? -5.709  13.308 105.925 1.00 21.28  ? 109 GLU C O   1 
ATOM   1167 C  CB  . GLU C 1 25 ? -3.844  11.041 104.879 1.00 23.46  ? 109 GLU C CB  1 
ATOM   1168 C  CG  . GLU C 1 25 ? -2.462  11.236 105.456 1.00 22.17  ? 109 GLU C CG  1 
ATOM   1169 C  CD  . GLU C 1 25 ? -1.362  10.753 104.504 1.00 24.48  ? 109 GLU C CD  1 
ATOM   1170 O  OE1 . GLU C 1 25 ? -1.647  9.932  103.594 1.00 25.92  ? 109 GLU C OE1 1 
ATOM   1171 O  OE2 . GLU C 1 25 ? -0.198  11.188 104.672 1.00 25.97  ? 109 GLU C OE2 1 
ATOM   1172 N  N   . ARG C 1 26 ? -4.745  12.503 107.785 1.00 20.87  ? 110 ARG C N   1 
ATOM   1173 C  CA  . ARG C 1 26 ? -4.819  13.782 108.471 1.00 19.61  ? 110 ARG C CA  1 
ATOM   1174 C  C   . ARG C 1 26 ? -3.515  14.549 108.313 1.00 20.40  ? 110 ARG C C   1 
ATOM   1175 O  O   . ARG C 1 26 ? -2.425  13.965 108.298 1.00 21.33  ? 110 ARG C O   1 
ATOM   1176 C  CB  . ARG C 1 26 ? -5.210  13.596 109.936 1.00 21.72  ? 110 ARG C CB  1 
ATOM   1177 C  CG  . ARG C 1 26 ? -6.622  13.054 110.029 1.00 28.77  ? 110 ARG C CG  1 
ATOM   1178 C  CD  . ARG C 1 26 ? -7.245  13.262 111.375 1.00 39.94  ? 110 ARG C CD  1 
ATOM   1179 N  NE  . ARG C 1 26 ? -8.679  12.998 111.325 1.00 49.83  ? 110 ARG C NE  1 
ATOM   1180 C  CZ  . ARG C 1 26 ? -9.238  11.823 111.581 1.00 54.86  ? 110 ARG C CZ  1 
ATOM   1181 N  NH1 . ARG C 1 26 ? -8.512  10.771 111.936 1.00 57.55  ? 110 ARG C NH1 1 
ATOM   1182 N  NH2 . ARG C 1 26 ? -10.560 11.700 111.484 1.00 53.74  ? 110 ARG C NH2 1 
ATOM   1183 N  N   . LEU C 1 27 ? -3.641  15.869 108.202 1.00 19.18  ? 111 LEU C N   1 
ATOM   1184 C  CA  . LEU C 1 27 ? -2.534  16.743 107.835 1.00 19.28  ? 111 LEU C CA  1 
ATOM   1185 C  C   . LEU C 1 27 ? -2.581  17.966 108.734 1.00 20.81  ? 111 LEU C C   1 
ATOM   1186 O  O   . LEU C 1 27 ? -3.601  18.650 108.783 1.00 21.31  ? 111 LEU C O   1 
ATOM   1187 C  CB  . LEU C 1 27 ? -2.714  17.185 106.381 1.00 23.21  ? 111 LEU C CB  1 
ATOM   1188 C  CG  . LEU C 1 27 ? -2.616  16.034 105.376 1.00 23.96  ? 111 LEU C CG  1 
ATOM   1189 C  CD1 . LEU C 1 27 ? -3.395  16.339 104.121 1.00 27.55  ? 111 LEU C CD1 1 
ATOM   1190 C  CD2 . LEU C 1 27 ? -1.149  15.803 105.046 1.00 26.87  ? 111 LEU C CD2 1 
ATOM   1191 N  N   . GLN C 1 28 ? -1.491  18.252 109.440 1.00 18.33  ? 112 GLN C N   1 
ATOM   1192 C  CA  . GLN C 1 28 ? -1.395  19.519 110.148 1.00 18.79  ? 112 GLN C CA  1 
ATOM   1193 C  C   . GLN C 1 28 ? -0.997  20.604 109.158 1.00 19.71  ? 112 GLN C C   1 
ATOM   1194 O  O   . GLN C 1 28 ? 0.006   20.476 108.462 1.00 20.58  ? 112 GLN C O   1 
ATOM   1195 C  CB  . GLN C 1 28 ? -0.365  19.460 111.275 1.00 18.27  ? 112 GLN C CB  1 
ATOM   1196 C  CG  . GLN C 1 28 ? -0.283  20.815 112.006 1.00 19.40  ? 112 GLN C CG  1 
ATOM   1197 C  CD  . GLN C 1 28 ? 0.721   20.869 113.133 1.00 18.59  ? 112 GLN C CD  1 
ATOM   1198 O  OE1 . GLN C 1 28 ? 1.539   19.974 113.302 1.00 21.16  ? 112 GLN C OE1 1 
ATOM   1199 N  NE2 . GLN C 1 28 ? 0.689   21.956 113.890 1.00 22.10  ? 112 GLN C NE2 1 
ATOM   1200 N  N   . ILE C 1 29 ? -1.781  21.672 109.083 1.00 19.29  ? 113 ILE C N   1 
ATOM   1201 C  CA  . ILE C 1 29 ? -1.498  22.758 108.157 1.00 21.27  ? 113 ILE C CA  1 
ATOM   1202 C  C   . ILE C 1 29 ? -0.642  23.778 108.884 1.00 22.02  ? 113 ILE C C   1 
ATOM   1203 O  O   . ILE C 1 29 ? -1.025  24.275 109.949 1.00 24.49  ? 113 ILE C O   1 
ATOM   1204 C  CB  . ILE C 1 29 ? -2.797  23.400 107.651 1.00 22.99  ? 113 ILE C CB  1 
ATOM   1205 C  CG1 . ILE C 1 29 ? -3.694  22.341 107.014 1.00 24.17  ? 113 ILE C CG1 1 
ATOM   1206 C  CG2 . ILE C 1 29 ? -2.472  24.488 106.645 1.00 24.38  ? 113 ILE C CG2 1 
ATOM   1207 C  CD1 . ILE C 1 29 ? -2.982  21.511 105.974 1.00 24.52  ? 113 ILE C CD1 1 
ATOM   1208 N  N   . VAL C 1 30 ? 0.512   24.101 108.312 1.00 25.10  ? 114 VAL C N   1 
ATOM   1209 C  CA  . VAL C 1 30 ? 1.373   25.112 108.892 1.00 31.55  ? 114 VAL C CA  1 
ATOM   1210 C  C   . VAL C 1 30 ? 1.464   26.298 107.939 1.00 37.68  ? 114 VAL C C   1 
ATOM   1211 O  O   . VAL C 1 30 ? 1.198   26.188 106.736 1.00 41.58  ? 114 VAL C O   1 
ATOM   1212 C  CB  . VAL C 1 30 ? 2.750   24.541 109.253 1.00 37.99  ? 114 VAL C CB  1 
ATOM   1213 C  CG1 . VAL C 1 30 ? 2.608   23.614 110.441 1.00 43.52  ? 114 VAL C CG1 1 
ATOM   1214 C  CG2 . VAL C 1 30 ? 3.304   23.779 108.097 1.00 34.34  ? 114 VAL C CG2 1 
ATOM   1215 N  N   . ASN C 1 31 ? 1.802   27.457 108.503 1.00 49.12  ? 115 ASN C N   1 
ATOM   1216 C  CA  . ASN C 1 31 ? 2.126   28.663 107.742 1.00 61.00  ? 115 ASN C CA  1 
ATOM   1217 C  C   . ASN C 1 31 ? 0.937   29.299 107.031 1.00 70.22  ? 115 ASN C C   1 
ATOM   1218 O  O   . ASN C 1 31 ? -0.217  29.124 107.439 1.00 72.25  ? 115 ASN C O   1 
ATOM   1219 C  CB  . ASN C 1 31 ? 3.273   28.410 106.755 1.00 62.49  ? 115 ASN C CB  1 
ATOM   1220 C  CG  . ASN C 1 31 ? 4.595   28.202 107.456 1.00 66.05  ? 115 ASN C CG  1 
ATOM   1221 O  OD1 . ASN C 1 31 ? 4.637   28.106 108.682 1.00 66.64  ? 115 ASN C OD1 1 
ATOM   1222 N  ND2 . ASN C 1 31 ? 5.682   28.131 106.688 1.00 66.47  ? 115 ASN C ND2 1 
ATOM   1223 N  N   . ASN C 1 32 ? 1.232   30.036 105.961 1.00 74.74  ? 116 ASN C N   1 
ATOM   1224 C  CA  . ASN C 1 32 ? 0.272   30.906 105.292 1.00 76.38  ? 116 ASN C CA  1 
ATOM   1225 C  C   . ASN C 1 32 ? -0.565  30.100 104.302 1.00 76.13  ? 116 ASN C C   1 
ATOM   1226 O  O   . ASN C 1 32 ? -0.021  29.436 103.412 1.00 74.63  ? 116 ASN C O   1 
ATOM   1227 C  CB  . ASN C 1 32 ? 1.025   32.034 104.585 1.00 78.90  ? 116 ASN C CB  1 
ATOM   1228 C  CG  . ASN C 1 32 ? 0.181   32.751 103.556 1.00 80.83  ? 116 ASN C CG  1 
ATOM   1229 O  OD1 . ASN C 1 32 ? -0.549  33.690 103.877 1.00 82.95  ? 116 ASN C OD1 1 
ATOM   1230 N  ND2 . ASN C 1 32 ? 0.289   32.324 102.302 1.00 80.70  ? 116 ASN C ND2 1 
ATOM   1231 N  N   . THR C 1 33 ? -1.887  30.169 104.455 1.00 76.78  ? 117 THR C N   1 
ATOM   1232 C  CA  . THR C 1 33 ? -2.830  29.407 103.643 1.00 76.40  ? 117 THR C CA  1 
ATOM   1233 C  C   . THR C 1 33 ? -3.556  30.300 102.639 1.00 75.84  ? 117 THR C C   1 
ATOM   1234 O  O   . THR C 1 33 ? -4.735  30.103 102.337 1.00 74.97  ? 117 THR C O   1 
ATOM   1235 C  CB  . THR C 1 33 ? -3.809  28.628 104.522 1.00 74.28  ? 117 THR C CB  1 
ATOM   1236 O  OG1 . THR C 1 33 ? -4.690  29.536 105.193 1.00 76.32  ? 117 THR C OG1 1 
ATOM   1237 C  CG2 . THR C 1 33 ? -3.052  27.829 105.562 1.00 72.18  ? 117 THR C CG2 1 
ATOM   1238 N  N   . GLU C 1 34 ? -2.845  31.292 102.106 1.00 76.43  ? 118 GLU C N   1 
ATOM   1239 C  CA  . GLU C 1 34 ? -3.424  32.229 101.154 1.00 76.28  ? 118 GLU C CA  1 
ATOM   1240 C  C   . GLU C 1 34 ? -3.331  31.749 99.712  1.00 71.27  ? 118 GLU C C   1 
ATOM   1241 O  O   . GLU C 1 34 ? -4.057  32.262 98.854  1.00 71.68  ? 118 GLU C O   1 
ATOM   1242 C  CB  . GLU C 1 34 ? -2.749  33.597 101.294 1.00 81.59  ? 118 GLU C CB  1 
ATOM   1243 C  CG  . GLU C 1 34 ? -3.486  34.732 100.616 1.00 86.63  ? 118 GLU C CG  1 
ATOM   1244 C  CD  . GLU C 1 34 ? -3.006  36.083 101.098 1.00 92.42  ? 118 GLU C CD  1 
ATOM   1245 O  OE1 . GLU C 1 34 ? -2.206  36.110 102.060 1.00 95.27  ? 118 GLU C OE1 1 
ATOM   1246 O  OE2 . GLU C 1 34 ? -3.430  37.112 100.528 1.00 93.42  ? 118 GLU C OE2 1 
ATOM   1247 N  N   . GLY C 1 35 ? -2.473  30.769 99.426  1.00 63.62  ? 119 GLY C N   1 
ATOM   1248 C  CA  . GLY C 1 35 ? -2.360  30.208 98.100  1.00 57.46  ? 119 GLY C CA  1 
ATOM   1249 C  C   . GLY C 1 35 ? -3.168  28.926 97.935  1.00 50.00  ? 119 GLY C C   1 
ATOM   1250 O  O   . GLY C 1 35 ? -3.872  28.467 98.831  1.00 50.95  ? 119 GLY C O   1 
ATOM   1251 N  N   . ASP C 1 36 ? -3.054  28.352 96.735  1.00 43.32  ? 120 ASP C N   1 
ATOM   1252 C  CA  . ASP C 1 36 ? -3.705  27.082 96.437  1.00 40.16  ? 120 ASP C CA  1 
ATOM   1253 C  C   . ASP C 1 36 ? -2.986  25.907 97.082  1.00 34.20  ? 120 ASP C C   1 
ATOM   1254 O  O   . ASP C 1 36 ? -3.578  24.830 97.217  1.00 34.29  ? 120 ASP C O   1 
ATOM   1255 C  CB  . ASP C 1 36 ? -3.745  26.847 94.921  1.00 44.37  ? 120 ASP C CB  1 
ATOM   1256 C  CG  . ASP C 1 36 ? -4.749  27.728 94.204  1.00 50.38  ? 120 ASP C CG  1 
ATOM   1257 O  OD1 . ASP C 1 36 ? -5.648  28.305 94.859  1.00 50.69  ? 120 ASP C OD1 1 
ATOM   1258 O  OD2 . ASP C 1 36 ? -4.647  27.819 92.961  1.00 53.66  ? 120 ASP C OD2 1 
ATOM   1259 N  N   . TRP C 1 37 ? -1.728  26.082 97.472  1.00 28.26  ? 121 TRP C N   1 
ATOM   1260 C  CA  . TRP C 1 37 ? -0.905  25.008 98.011  1.00 24.50  ? 121 TRP C CA  1 
ATOM   1261 C  C   . TRP C 1 37 ? -0.458  25.375 99.416  1.00 23.61  ? 121 TRP C C   1 
ATOM   1262 O  O   . TRP C 1 37 ? 0.027   26.487 99.642  1.00 26.61  ? 121 TRP C O   1 
ATOM   1263 C  CB  . TRP C 1 37 ? 0.305   24.740 97.116  1.00 25.12  ? 121 TRP C CB  1 
ATOM   1264 C  CG  . TRP C 1 37 ? -0.096  24.077 95.831  1.00 25.82  ? 121 TRP C CG  1 
ATOM   1265 C  CD1 . TRP C 1 37 ? -0.598  24.688 94.704  1.00 27.81  ? 121 TRP C CD1 1 
ATOM   1266 C  CD2 . TRP C 1 37 ? -0.068  22.678 95.550  1.00 24.61  ? 121 TRP C CD2 1 
ATOM   1267 N  NE1 . TRP C 1 37 ? -0.859  23.748 93.744  1.00 27.97  ? 121 TRP C NE1 1 
ATOM   1268 C  CE2 . TRP C 1 37 ? -0.545  22.506 94.233  1.00 23.81  ? 121 TRP C CE2 1 
ATOM   1269 C  CE3 . TRP C 1 37 ? 0.338   21.557 96.272  1.00 25.96  ? 121 TRP C CE3 1 
ATOM   1270 C  CZ2 . TRP C 1 37 ? -0.634  21.250 93.630  1.00 25.88  ? 121 TRP C CZ2 1 
ATOM   1271 C  CZ3 . TRP C 1 37 ? 0.237   20.307 95.674  1.00 28.20  ? 121 TRP C CZ3 1 
ATOM   1272 C  CH2 . TRP C 1 37 ? -0.235  20.167 94.365  1.00 27.67  ? 121 TRP C CH2 1 
ATOM   1273 N  N   . TRP C 1 38 ? -0.616  24.437 100.350 1.00 23.16  ? 122 TRP C N   1 
ATOM   1274 C  CA  . TRP C 1 38 ? -0.354  24.683 101.761 1.00 23.41  ? 122 TRP C CA  1 
ATOM   1275 C  C   . TRP C 1 38 ? 0.739   23.747 102.246 1.00 22.79  ? 122 TRP C C   1 
ATOM   1276 O  O   . TRP C 1 38 ? 0.750   22.567 101.888 1.00 23.20  ? 122 TRP C O   1 
ATOM   1277 C  CB  . TRP C 1 38 ? -1.609  24.388 102.603 1.00 23.89  ? 122 TRP C CB  1 
ATOM   1278 C  CG  . TRP C 1 38 ? -2.789  25.257 102.328 1.00 24.78  ? 122 TRP C CG  1 
ATOM   1279 C  CD1 . TRP C 1 38 ? -2.822  26.406 101.598 1.00 25.50  ? 122 TRP C CD1 1 
ATOM   1280 C  CD2 . TRP C 1 38 ? -4.125  25.029 102.785 1.00 23.81  ? 122 TRP C CD2 1 
ATOM   1281 N  NE1 . TRP C 1 38 ? -4.103  26.920 101.581 1.00 28.02  ? 122 TRP C NE1 1 
ATOM   1282 C  CE2 . TRP C 1 38 ? -4.920  26.091 102.307 1.00 28.28  ? 122 TRP C CE2 1 
ATOM   1283 C  CE3 . TRP C 1 38 ? -4.727  24.032 103.559 1.00 23.92  ? 122 TRP C CE3 1 
ATOM   1284 C  CZ2 . TRP C 1 38 ? -6.287  26.180 102.572 1.00 28.77  ? 122 TRP C CZ2 1 
ATOM   1285 C  CZ3 . TRP C 1 38 ? -6.081  24.123 103.824 1.00 26.60  ? 122 TRP C CZ3 1 
ATOM   1286 C  CH2 . TRP C 1 38 ? -6.848  25.187 103.328 1.00 28.10  ? 122 TRP C CH2 1 
ATOM   1287 N  N   . LEU C 1 39 ? 1.636   24.266 103.088 1.00 22.87  ? 123 LEU C N   1 
ATOM   1288 C  CA  . LEU C 1 39 ? 2.636   23.419 103.735 1.00 20.08  ? 123 LEU C CA  1 
ATOM   1289 C  C   . LEU C 1 39 ? 1.957   22.599 104.829 1.00 20.30  ? 123 LEU C C   1 
ATOM   1290 O  O   . LEU C 1 39 ? 1.187   23.138 105.623 1.00 22.34  ? 123 LEU C O   1 
ATOM   1291 C  CB  . LEU C 1 39 ? 3.745   24.287 104.344 1.00 21.58  ? 123 LEU C CB  1 
ATOM   1292 C  CG  . LEU C 1 39 ? 4.983   23.524 104.839 1.00 23.62  ? 123 LEU C CG  1 
ATOM   1293 C  CD1 . LEU C 1 39 ? 5.655   22.716 103.721 1.00 26.16  ? 123 LEU C CD1 1 
ATOM   1294 C  CD2 . LEU C 1 39 ? 6.024   24.458 105.485 1.00 24.64  ? 123 LEU C CD2 1 
ATOM   1295 N  N   . ALA C 1 40 ? 2.242   21.297 104.871 1.00 19.08  ? 124 ALA C N   1 
ATOM   1296 C  CA  . ALA C 1 40 ? 1.550   20.406 105.788 1.00 18.01  ? 124 ALA C CA  1 
ATOM   1297 C  C   . ALA C 1 40 ? 2.492   19.337 106.321 1.00 18.22  ? 124 ALA C C   1 
ATOM   1298 O  O   . ALA C 1 40 ? 3.504   18.997 105.692 1.00 20.81  ? 124 ALA C O   1 
ATOM   1299 C  CB  . ALA C 1 40 ? 0.383   19.728 105.072 1.00 20.15  ? 124 ALA C CB  1 
ATOM   1300 N  N   . HIS C 1 41 ? 2.160   18.812 107.503 1.00 18.62  ? 125 HIS C N   1 
ATOM   1301 C  CA  . HIS C 1 41 ? 2.810   17.619 108.035 1.00 19.88  ? 125 HIS C CA  1 
ATOM   1302 C  C   . HIS C 1 41 ? 1.790   16.486 108.041 1.00 18.52  ? 125 HIS C C   1 
ATOM   1303 O  O   . HIS C 1 41 ? 0.676   16.655 108.551 1.00 19.72  ? 125 HIS C O   1 
ATOM   1304 C  CB  . HIS C 1 41 ? 3.259   17.813 109.485 1.00 20.44  ? 125 HIS C CB  1 
ATOM   1305 C  CG  . HIS C 1 41 ? 4.016   19.085 109.768 1.00 21.52  ? 125 HIS C CG  1 
ATOM   1306 N  ND1 . HIS C 1 41 ? 5.247   19.374 109.218 1.00 25.18  ? 125 HIS C ND1 1 
ATOM   1307 C  CD2 . HIS C 1 41 ? 3.744   20.101 110.625 1.00 22.92  ? 125 HIS C CD2 1 
ATOM   1308 C  CE1 . HIS C 1 41 ? 5.679   20.534 109.684 1.00 27.74  ? 125 HIS C CE1 1 
ATOM   1309 N  NE2 . HIS C 1 41 ? 4.784   21.001 110.538 1.00 25.04  ? 125 HIS C NE2 1 
ATOM   1310 N  N   . SER C 1 42 ? 2.186   15.314 107.545 1.00 18.61  ? 126 SER C N   1 
ATOM   1311 C  CA  . SER C 1 42 ? 1.295   14.161 107.557 1.00 18.68  ? 126 SER C CA  1 
ATOM   1312 C  C   . SER C 1 42 ? 1.263   13.503 108.932 1.00 19.05  ? 126 SER C C   1 
ATOM   1313 O  O   . SER C 1 42 ? 2.306   13.137 109.476 1.00 21.00  ? 126 SER C O   1 
ATOM   1314 C  CB  . SER C 1 42 ? 1.749   13.139 106.527 1.00 20.45  ? 126 SER C CB  1 
ATOM   1315 O  OG  . SER C 1 42 ? 1.064   11.916 106.744 1.00 21.63  ? 126 SER C OG  1 
ATOM   1316 N  N   . LEU C 1 43 ? 0.062   13.319 109.476 1.00 20.42  ? 127 LEU C N   1 
ATOM   1317 C  CA  . LEU C 1 43 ? -0.068  12.566 110.715 1.00 21.22  ? 127 LEU C CA  1 
ATOM   1318 C  C   . LEU C 1 43 ? -0.006  11.064 110.492 1.00 23.83  ? 127 LEU C C   1 
ATOM   1319 O  O   . LEU C 1 43 ? 0.038   10.310 111.469 1.00 24.55  ? 127 LEU C O   1 
ATOM   1320 C  CB  . LEU C 1 43 ? -1.362  12.938 111.452 1.00 22.15  ? 127 LEU C CB  1 
ATOM   1321 C  CG  . LEU C 1 43 ? -1.249  14.147 112.392 1.00 24.47  ? 127 LEU C CG  1 
ATOM   1322 C  CD1 . LEU C 1 43 ? -0.939  15.432 111.658 1.00 26.65  ? 127 LEU C CD1 1 
ATOM   1323 C  CD2 . LEU C 1 43 ? -2.526  14.291 113.193 1.00 24.34  ? 127 LEU C CD2 1 
ATOM   1324 N  N   . SER C 1 44 ? -0.017  10.610 109.238 1.00 21.75  ? 128 SER C N   1 
ATOM   1325 C  CA  . SER C 1 44 ? 0.174   9.193  108.951 1.00 23.17  ? 128 SER C CA  1 
ATOM   1326 C  C   . SER C 1 44 ? 1.646   8.824  108.874 1.00 24.33  ? 128 SER C C   1 
ATOM   1327 O  O   . SER C 1 44 ? 2.051   7.768  109.376 1.00 27.21  ? 128 SER C O   1 
ATOM   1328 C  CB  . SER C 1 44 ? -0.506  8.834  107.630 1.00 26.35  ? 128 SER C CB  1 
ATOM   1329 O  OG  . SER C 1 44 ? -1.912  8.860  107.752 1.00 30.73  ? 128 SER C OG  1 
ATOM   1330 N  N   . THR C 1 45 ? 2.462   9.666  108.243 1.00 23.18  ? 129 THR C N   1 
ATOM   1331 C  CA  . THR C 1 45 ? 3.860   9.332  107.995 1.00 25.48  ? 129 THR C CA  1 
ATOM   1332 C  C   . THR C 1 45 ? 4.859   10.230 108.705 1.00 23.52  ? 129 THR C C   1 
ATOM   1333 O  O   . THR C 1 45 ? 6.027   9.840  108.826 1.00 26.11  ? 129 THR C O   1 
ATOM   1334 C  CB  . THR C 1 45 ? 4.177   9.444  106.497 1.00 27.17  ? 129 THR C CB  1 
ATOM   1335 O  OG1 . THR C 1 45 ? 4.100   10.831 106.129 1.00 28.66  ? 129 THR C OG1 1 
ATOM   1336 C  CG2 . THR C 1 45 ? 3.190   8.630  105.657 1.00 29.46  ? 129 THR C CG2 1 
ATOM   1337 N  N   . GLY C 1 46 ? 4.460   11.428 109.133 1.00 24.16  ? 130 GLY C N   1 
ATOM   1338 C  CA  . GLY C 1 46 ? 5.402   12.379 109.684 1.00 24.02  ? 130 GLY C CA  1 
ATOM   1339 C  C   . GLY C 1 46 ? 6.156   13.221 108.669 1.00 24.87  ? 130 GLY C C   1 
ATOM   1340 O  O   . GLY C 1 46 ? 6.943   14.083 109.071 1.00 26.14  ? 130 GLY C O   1 
ATOM   1341 N  N   . GLN C 1 47 ? 5.939   13.019 107.370 1.00 25.77  ? 131 GLN C N   1 
ATOM   1342 C  CA  . GLN C 1 47 ? 6.641   13.820 106.376 1.00 26.03  ? 131 GLN C CA  1 
ATOM   1343 C  C   . GLN C 1 47 ? 6.002   15.205 106.245 1.00 23.62  ? 131 GLN C C   1 
ATOM   1344 O  O   . GLN C 1 47 ? 4.834   15.405 106.581 1.00 24.76  ? 131 GLN C O   1 
ATOM   1345 C  CB  . GLN C 1 47 ? 6.586   13.131 105.018 1.00 29.98  ? 131 GLN C CB  1 
ATOM   1346 C  CG  . GLN C 1 47 ? 7.249   11.778 104.956 1.00 34.42  ? 131 GLN C CG  1 
ATOM   1347 C  CD  . GLN C 1 47 ? 7.339   11.293 103.531 1.00 43.83  ? 131 GLN C CD  1 
ATOM   1348 O  OE1 . GLN C 1 47 ? 6.422   11.523 102.731 1.00 49.71  ? 131 GLN C OE1 1 
ATOM   1349 N  NE2 . GLN C 1 47 ? 8.458   10.664 103.186 1.00 45.99  ? 131 GLN C NE2 1 
ATOM   1350 N  N   . THR C 1 48 ? 6.779   16.154 105.717 1.00 25.10  ? 132 THR C N   1 
ATOM   1351 C  CA  . THR C 1 48 ? 6.358   17.537 105.512 1.00 24.83  ? 132 THR C CA  1 
ATOM   1352 C  C   . THR C 1 48 ? 6.471   17.908 104.042 1.00 24.13  ? 132 THR C C   1 
ATOM   1353 O  O   . THR C 1 48 ? 7.519   17.692 103.426 1.00 26.11  ? 132 THR C O   1 
ATOM   1354 C  CB  . THR C 1 48 ? 7.257   18.494 106.289 1.00 25.70  ? 132 THR C CB  1 
ATOM   1355 O  OG1 . THR C 1 48 ? 7.184   18.183 107.680 1.00 28.67  ? 132 THR C OG1 1 
ATOM   1356 C  CG2 . THR C 1 48 ? 6.824   19.942 106.062 1.00 23.91  ? 132 THR C CG2 1 
ATOM   1357 N  N   . GLY C 1 49 ? 5.418   18.510 103.497 1.00 20.72  ? 133 GLY C N   1 
ATOM   1358 C  CA  . GLY C 1 49 ? 5.481   19.006 102.132 1.00 22.43  ? 133 GLY C CA  1 
ATOM   1359 C  C   . GLY C 1 49 ? 4.207   19.747 101.807 1.00 20.21  ? 133 GLY C C   1 
ATOM   1360 O  O   . GLY C 1 49 ? 3.295   19.849 102.631 1.00 21.58  ? 133 GLY C O   1 
ATOM   1361 N  N   . TYR C 1 50 ? 4.134   20.246 100.576 1.00 21.71  ? 134 TYR C N   1 
ATOM   1362 C  CA  . TYR C 1 50 ? 2.975   21.020 100.176 1.00 22.33  ? 134 TYR C CA  1 
ATOM   1363 C  C   . TYR C 1 50 ? 1.839   20.113 99.733  1.00 21.67  ? 134 TYR C C   1 
ATOM   1364 O  O   . TYR C 1 50 ? 2.056   19.026 99.190  1.00 22.92  ? 134 TYR C O   1 
ATOM   1365 C  CB  . TYR C 1 50 ? 3.342   22.001 99.061  1.00 24.37  ? 134 TYR C CB  1 
ATOM   1366 C  CG  . TYR C 1 50 ? 4.310   23.023 99.556  1.00 29.07  ? 134 TYR C CG  1 
ATOM   1367 C  CD1 . TYR C 1 50 ? 3.865   24.160 100.224 1.00 31.35  ? 134 TYR C CD1 1 
ATOM   1368 C  CD2 . TYR C 1 50 ? 5.674   22.835 99.408  1.00 32.13  ? 134 TYR C CD2 1 
ATOM   1369 C  CE1 . TYR C 1 50 ? 4.757   25.097 100.712 1.00 35.52  ? 134 TYR C CE1 1 
ATOM   1370 C  CE2 . TYR C 1 50 ? 6.571   23.759 99.895  1.00 35.60  ? 134 TYR C CE2 1 
ATOM   1371 C  CZ  . TYR C 1 50 ? 6.110   24.886 100.548 1.00 38.72  ? 134 TYR C CZ  1 
ATOM   1372 O  OH  . TYR C 1 50 ? 7.021   25.804 101.029 1.00 43.13  ? 134 TYR C OH  1 
ATOM   1373 N  N   A ILE C 1 51 ? 0.614   20.562 99.993  0.75 20.65  ? 135 ILE C N   1 
ATOM   1374 N  N   B ILE C 1 51 ? 0.614   20.569 99.973  0.25 21.31  ? 135 ILE C N   1 
ATOM   1375 C  CA  A ILE C 1 51 ? -0.578  19.828 99.573  0.75 21.42  ? 135 ILE C CA  1 
ATOM   1376 C  CA  B ILE C 1 51 ? -0.575  19.821 99.575  0.25 21.68  ? 135 ILE C CA  1 
ATOM   1377 C  C   A ILE C 1 51 ? -1.528  20.771 98.847  0.75 21.26  ? 135 ILE C C   1 
ATOM   1378 C  C   B ILE C 1 51 ? -1.550  20.759 98.874  0.25 22.09  ? 135 ILE C C   1 
ATOM   1379 O  O   A ILE C 1 51 ? -1.525  21.987 99.105  0.75 21.59  ? 135 ILE C O   1 
ATOM   1380 O  O   B ILE C 1 51 ? -1.587  21.960 99.180  0.25 22.67  ? 135 ILE C O   1 
ATOM   1381 C  CB  A ILE C 1 51 ? -1.268  19.114 100.752 0.75 21.67  ? 135 ILE C CB  1 
ATOM   1382 C  CB  B ILE C 1 51 ? -1.233  19.123 100.776 0.25 21.78  ? 135 ILE C CB  1 
ATOM   1383 C  CG1 A ILE C 1 51 ? -1.720  20.104 101.833 0.75 23.64  ? 135 ILE C CG1 1 
ATOM   1384 C  CG1 B ILE C 1 51 ? -1.579  20.143 101.860 0.25 22.42  ? 135 ILE C CG1 1 
ATOM   1385 C  CG2 A ILE C 1 51 ? -0.328  18.062 101.348 0.75 21.74  ? 135 ILE C CG2 1 
ATOM   1386 C  CG2 B ILE C 1 51 ? -0.323  18.027 101.325 0.25 21.62  ? 135 ILE C CG2 1 
ATOM   1387 C  CD1 A ILE C 1 51 ? -3.149  20.672 101.644 0.75 23.17  ? 135 ILE C CD1 1 
ATOM   1388 C  CD1 B ILE C 1 51 ? -2.649  19.673 102.804 0.25 20.52  ? 135 ILE C CD1 1 
ATOM   1389 N  N   . PRO C 1 52 ? -2.349  20.264 97.927  1.00 22.75  ? 136 PRO C N   1 
ATOM   1390 C  CA  . PRO C 1 52 ? -3.302  21.140 97.233  1.00 23.79  ? 136 PRO C CA  1 
ATOM   1391 C  C   . PRO C 1 52 ? -4.535  21.347 98.101  1.00 22.87  ? 136 PRO C C   1 
ATOM   1392 O  O   . PRO C 1 52 ? -5.150  20.389 98.575  1.00 24.58  ? 136 PRO C O   1 
ATOM   1393 C  CB  . PRO C 1 52 ? -3.628  20.363 95.951  1.00 24.88  ? 136 PRO C CB  1 
ATOM   1394 C  CG  . PRO C 1 52 ? -3.360  18.925 96.281  1.00 24.93  ? 136 PRO C CG  1 
ATOM   1395 C  CD  . PRO C 1 52 ? -2.347  18.886 97.399  1.00 22.53  ? 136 PRO C CD  1 
ATOM   1396 N  N   . SER C 1 53 ? -4.889  22.618 98.319  1.00 24.76  ? 137 SER C N   1 
ATOM   1397 C  CA  . SER C 1 53 ? -5.925  22.938 99.292  1.00 26.13  ? 137 SER C CA  1 
ATOM   1398 C  C   . SER C 1 53 ? -7.287  22.377 98.896  1.00 27.12  ? 137 SER C C   1 
ATOM   1399 O  O   . SER C 1 53 ? -8.111  22.088 99.771  1.00 27.00  ? 137 SER C O   1 
ATOM   1400 C  CB  . SER C 1 53 ? -5.987  24.449 99.515  1.00 29.74  ? 137 SER C CB  1 
ATOM   1401 O  OG  . SER C 1 53 ? -6.391  25.113 98.339  1.00 31.55  ? 137 SER C OG  1 
ATOM   1402 N  N   . ASN C 1 54 ? -7.539  22.194 97.597  1.00 26.97  ? 138 ASN C N   1 
ATOM   1403 C  CA  . ASN C 1 54 ? -8.821  21.652 97.164  1.00 27.53  ? 138 ASN C CA  1 
ATOM   1404 C  C   . ASN C 1 54 ? -8.965  20.155 97.433  1.00 27.63  ? 138 ASN C C   1 
ATOM   1405 O  O   . ASN C 1 54 ? -10.042 19.600 97.186  1.00 30.70  ? 138 ASN C O   1 
ATOM   1406 C  CB  . ASN C 1 54 ? -9.106  22.008 95.695  1.00 30.97  ? 138 ASN C CB  1 
ATOM   1407 C  CG  . ASN C 1 54 ? -8.105  21.394 94.730  1.00 37.49  ? 138 ASN C CG  1 
ATOM   1408 O  OD1 . ASN C 1 54 ? -6.930  21.240 95.050  1.00 38.69  ? 138 ASN C OD1 1 
ATOM   1409 N  ND2 . ASN C 1 54 ? -8.571  21.046 93.534  1.00 43.50  ? 138 ASN C ND2 1 
ATOM   1410 N  N   . TYR C 1 55 ? -7.924  19.494 97.935  1.00 26.22  ? 139 TYR C N   1 
ATOM   1411 C  CA  . TYR C 1 55 ? -7.995  18.081 98.268  1.00 23.89  ? 139 TYR C CA  1 
ATOM   1412 C  C   . TYR C 1 55 ? -8.282  17.824 99.737  1.00 24.34  ? 139 TYR C C   1 
ATOM   1413 O  O   . TYR C 1 55 ? -8.316  16.662 100.141 1.00 24.62  ? 139 TYR C O   1 
ATOM   1414 C  CB  . TYR C 1 55 ? -6.679  17.384 97.903  1.00 23.89  ? 139 TYR C CB  1 
ATOM   1415 C  CG  . TYR C 1 55 ? -6.609  16.906 96.474  1.00 24.76  ? 139 TYR C CG  1 
ATOM   1416 C  CD1 . TYR C 1 55 ? -6.629  17.806 95.414  1.00 27.59  ? 139 TYR C CD1 1 
ATOM   1417 C  CD2 . TYR C 1 55 ? -6.510  15.555 96.186  1.00 24.85  ? 139 TYR C CD2 1 
ATOM   1418 C  CE1 . TYR C 1 55 ? -6.553  17.364 94.094  1.00 29.94  ? 139 TYR C CE1 1 
ATOM   1419 C  CE2 . TYR C 1 55 ? -6.429  15.102 94.879  1.00 27.03  ? 139 TYR C CE2 1 
ATOM   1420 C  CZ  . TYR C 1 55 ? -6.446  16.006 93.836  1.00 29.91  ? 139 TYR C CZ  1 
ATOM   1421 O  OH  . TYR C 1 55 ? -6.369  15.537 92.538  1.00 31.54  ? 139 TYR C OH  1 
ATOM   1422 N  N   . VAL C 1 56 ? -8.449  18.869 100.552 1.00 23.95  ? 140 VAL C N   1 
ATOM   1423 C  CA  . VAL C 1 56 ? -8.551  18.709 101.998 1.00 21.49  ? 140 VAL C CA  1 
ATOM   1424 C  C   . VAL C 1 56 ? -9.713  19.535 102.530 1.00 21.76  ? 140 VAL C C   1 
ATOM   1425 O  O   . VAL C 1 56 ? -10.157 20.501 101.906 1.00 24.96  ? 140 VAL C O   1 
ATOM   1426 C  CB  . VAL C 1 56 ? -7.237  19.075 102.736 1.00 22.20  ? 140 VAL C CB  1 
ATOM   1427 C  CG1 . VAL C 1 56 ? -6.110  18.085 102.380 1.00 22.46  ? 140 VAL C CG1 1 
ATOM   1428 C  CG2 . VAL C 1 56 ? -6.830  20.511 102.425 1.00 23.83  ? 140 VAL C CG2 1 
ATOM   1429 N  N   . ALA C 1 57 ? -10.204 19.141 103.701 1.00 21.62  ? 141 ALA C N   1 
ATOM   1430 C  CA  . ALA C 1 57 ? -11.216 19.899 104.419 1.00 22.13  ? 141 ALA C CA  1 
ATOM   1431 C  C   . ALA C 1 57 ? -10.895 19.796 105.903 1.00 19.59  ? 141 ALA C C   1 
ATOM   1432 O  O   . ALA C 1 57 ? -10.132 18.917 106.310 1.00 20.29  ? 141 ALA C O   1 
ATOM   1433 C  CB  . ALA C 1 57 ? -12.609 19.322 104.141 1.00 23.48  ? 141 ALA C CB  1 
ATOM   1434 N  N   . PRO C 1 58 ? -11.438 20.694 106.729 1.00 21.72  ? 142 PRO C N   1 
ATOM   1435 C  CA  . PRO C 1 58 ? -11.142 20.627 108.167 1.00 21.75  ? 142 PRO C CA  1 
ATOM   1436 C  C   . PRO C 1 58 ? -11.503 19.258 108.735 1.00 23.58  ? 142 PRO C C   1 
ATOM   1437 O  O   . PRO C 1 58 ? -12.537 18.681 108.403 1.00 25.23  ? 142 PRO C O   1 
ATOM   1438 C  CB  . PRO C 1 58 ? -12.026 21.730 108.759 1.00 23.17  ? 142 PRO C CB  1 
ATOM   1439 C  CG  . PRO C 1 58 ? -12.232 22.664 107.653 1.00 24.76  ? 142 PRO C CG  1 
ATOM   1440 C  CD  . PRO C 1 58 ? -12.277 21.857 106.403 1.00 21.92  ? 142 PRO C CD  1 
ATOM   1441 N  N   . SER C 1 59 ? -10.633 18.728 109.589 1.00 24.37  ? 143 SER C N   1 
ATOM   1442 C  CA  . SER C 1 59 ? -10.792 17.342 110.030 1.00 30.27  ? 143 SER C CA  1 
ATOM   1443 C  C   . SER C 1 59 ? -11.781 17.279 111.170 1.00 39.59  ? 143 SER C C   1 
ATOM   1444 O  O   . SER C 1 59 ? -12.467 16.263 111.356 1.00 40.70  ? 143 SER C O   1 
ATOM   1445 C  CB  . SER C 1 59 ? -9.443  16.756 110.465 1.00 34.67  ? 143 SER C CB  1 
ATOM   1446 O  OG  . SER C 1 59 ? -9.201  17.042 111.831 1.00 41.37  ? 143 SER C OG  1 
ATOM   1447 O  OXT . SER C 1 59 ? -11.902 18.245 111.928 1.00 44.18  ? 143 SER C OXT 1 
ATOM   1448 N  N   . GLY D 1 1  ? 9.508   35.941 110.249 1.00 40.02  ? 85  GLY D N   1 
ATOM   1449 C  CA  . GLY D 1 1  ? 10.735  35.326 109.770 1.00 36.13  ? 85  GLY D CA  1 
ATOM   1450 C  C   . GLY D 1 1  ? 11.534  34.764 110.927 1.00 32.24  ? 85  GLY D C   1 
ATOM   1451 O  O   . GLY D 1 1  ? 11.103  34.863 112.081 1.00 33.39  ? 85  GLY D O   1 
ATOM   1452 N  N   . VAL D 1 2  ? 12.693  34.172 110.645 1.00 27.18  ? 86  VAL D N   1 
ATOM   1453 C  CA  . VAL D 1 2  ? 13.477  33.575 111.724 1.00 24.72  ? 86  VAL D CA  1 
ATOM   1454 C  C   . VAL D 1 2  ? 14.020  34.655 112.647 1.00 25.56  ? 86  VAL D C   1 
ATOM   1455 O  O   . VAL D 1 2  ? 14.554  35.684 112.202 1.00 28.90  ? 86  VAL D O   1 
ATOM   1456 C  CB  . VAL D 1 2  ? 14.570  32.628 111.198 1.00 27.65  ? 86  VAL D CB  1 
ATOM   1457 C  CG1 . VAL D 1 2  ? 13.938  31.435 110.488 1.00 30.18  ? 86  VAL D CG1 1 
ATOM   1458 C  CG2 . VAL D 1 2  ? 15.539  33.347 110.294 1.00 30.54  ? 86  VAL D CG2 1 
ATOM   1459 N  N   . THR D 1 3  ? 13.870  34.432 113.945 1.00 24.71  ? 87  THR D N   1 
ATOM   1460 C  CA  . THR D 1 3  ? 14.277  35.385 114.970 1.00 25.14  ? 87  THR D CA  1 
ATOM   1461 C  C   . THR D 1 3  ? 15.408  34.729 115.747 1.00 25.38  ? 87  THR D C   1 
ATOM   1462 O  O   . THR D 1 3  ? 15.194  33.709 116.402 1.00 26.00  ? 87  THR D O   1 
ATOM   1463 C  CB  . THR D 1 3  ? 13.094  35.678 115.888 1.00 30.33  ? 87  THR D CB  1 
ATOM   1464 O  OG1 . THR D 1 3  ? 12.093  36.398 115.161 1.00 30.40  ? 87  THR D OG1 1 
ATOM   1465 C  CG2 . THR D 1 3  ? 13.537  36.487 117.097 1.00 31.58  ? 87  THR D CG2 1 
ATOM   1466 N  N   . THR D 1 4  ? 16.612  35.282 115.650 1.00 23.13  ? 88  THR D N   1 
ATOM   1467 C  CA  . THR D 1 4  ? 17.762  34.725 116.345 1.00 23.58  ? 88  THR D CA  1 
ATOM   1468 C  C   . THR D 1 4  ? 18.197  35.675 117.446 1.00 23.26  ? 88  THR D C   1 
ATOM   1469 O  O   . THR D 1 4  ? 18.416  36.864 117.200 1.00 24.33  ? 88  THR D O   1 
ATOM   1470 C  CB  . THR D 1 4  ? 18.945  34.481 115.403 1.00 25.17  ? 88  THR D CB  1 
ATOM   1471 O  OG1 . THR D 1 4  ? 18.504  33.772 114.242 1.00 25.71  ? 88  THR D OG1 1 
ATOM   1472 C  CG2 . THR D 1 4  ? 20.034  33.672 116.118 1.00 27.98  ? 88  THR D CG2 1 
ATOM   1473 N  N   . PHE D 1 5  ? 18.327  35.144 118.651 1.00 23.67  ? 89  PHE D N   1 
ATOM   1474 C  CA  . PHE D 1 5  ? 18.899  35.870 119.772 1.00 24.56  ? 89  PHE D CA  1 
ATOM   1475 C  C   . PHE D 1 5  ? 20.227  35.225 120.152 1.00 23.88  ? 89  PHE D C   1 
ATOM   1476 O  O   . PHE D 1 5  ? 20.585  34.158 119.658 1.00 24.90  ? 89  PHE D O   1 
ATOM   1477 C  CB  . PHE D 1 5  ? 17.921  35.884 120.955 1.00 24.53  ? 89  PHE D CB  1 
ATOM   1478 C  CG  . PHE D 1 5  ? 16.895  36.984 120.884 1.00 23.54  ? 89  PHE D CG  1 
ATOM   1479 C  CD1 . PHE D 1 5  ? 16.032  37.086 119.806 1.00 27.36  ? 89  PHE D CD1 1 
ATOM   1480 C  CD2 . PHE D 1 5  ? 16.782  37.895 121.910 1.00 23.34  ? 89  PHE D CD2 1 
ATOM   1481 C  CE1 . PHE D 1 5  ? 15.092  38.102 119.752 1.00 27.48  ? 89  PHE D CE1 1 
ATOM   1482 C  CE2 . PHE D 1 5  ? 15.844  38.905 121.859 1.00 23.29  ? 89  PHE D CE2 1 
ATOM   1483 C  CZ  . PHE D 1 5  ? 14.998  39.012 120.780 1.00 26.01  ? 89  PHE D CZ  1 
ATOM   1484 N  N   . VAL D 1 6  ? 20.980  35.905 121.005 1.00 21.86  ? 90  VAL D N   1 
ATOM   1485 C  CA  . VAL D 1 6  ? 22.267  35.411 121.470 1.00 23.81  ? 90  VAL D CA  1 
ATOM   1486 C  C   . VAL D 1 6  ? 22.289  35.440 122.991 1.00 22.16  ? 90  VAL D C   1 
ATOM   1487 O  O   . VAL D 1 6  ? 21.770  36.371 123.613 1.00 23.53  ? 90  VAL D O   1 
ATOM   1488 C  CB  . VAL D 1 6  ? 23.463  36.181 120.855 1.00 25.66  ? 90  VAL D CB  1 
ATOM   1489 C  CG1 . VAL D 1 6  ? 23.423  37.679 121.203 1.00 24.33  ? 90  VAL D CG1 1 
ATOM   1490 C  CG2 . VAL D 1 6  ? 24.792  35.546 121.281 1.00 25.97  ? 90  VAL D CG2 1 
ATOM   1491 N  N   . ALA D 1 7  ? 22.897  34.422 123.592 1.00 24.49  ? 91  ALA D N   1 
ATOM   1492 C  CA  . ALA D 1 7  ? 22.978  34.364 125.044 1.00 25.73  ? 91  ALA D CA  1 
ATOM   1493 C  C   . ALA D 1 7  ? 23.966  35.392 125.583 1.00 25.21  ? 91  ALA D C   1 
ATOM   1494 O  O   . ALA D 1 7  ? 25.113  35.472 125.128 1.00 26.88  ? 91  ALA D O   1 
ATOM   1495 C  CB  . ALA D 1 7  ? 23.424  32.974 125.481 1.00 24.74  ? 91  ALA D CB  1 
ATOM   1496 N  N   . LEU D 1 8  ? 23.523  36.167 126.575 1.00 27.01  ? 92  LEU D N   1 
ATOM   1497 C  CA  . LEU D 1 8  ? 24.394  37.120 127.252 1.00 27.73  ? 92  LEU D CA  1 
ATOM   1498 C  C   . LEU D 1 8  ? 25.196  36.485 128.378 1.00 28.91  ? 92  LEU D C   1 
ATOM   1499 O  O   . LEU D 1 8  ? 26.229  37.039 128.772 1.00 31.92  ? 92  LEU D O   1 
ATOM   1500 C  CB  . LEU D 1 8  ? 23.550  38.258 127.825 1.00 28.22  ? 92  LEU D CB  1 
ATOM   1501 C  CG  . LEU D 1 8  ? 22.775  39.047 126.770 1.00 26.71  ? 92  LEU D CG  1 
ATOM   1502 C  CD1 . LEU D 1 8  ? 21.723  39.944 127.401 1.00 28.91  ? 92  LEU D CD1 1 
ATOM   1503 C  CD2 . LEU D 1 8  ? 23.728  39.865 125.918 1.00 28.49  ? 92  LEU D CD2 1 
ATOM   1504 N  N   . TYR D 1 9  ? 24.744  35.344 128.891 1.00 28.72  ? 93  TYR D N   1 
ATOM   1505 C  CA  . TYR D 1 9  ? 25.357  34.690 130.034 1.00 30.77  ? 93  TYR D CA  1 
ATOM   1506 C  C   . TYR D 1 9  ? 25.225  33.190 129.846 1.00 33.24  ? 93  TYR D C   1 
ATOM   1507 O  O   . TYR D 1 9  ? 24.403  32.719 129.058 1.00 32.83  ? 93  TYR D O   1 
ATOM   1508 C  CB  . TYR D 1 9  ? 24.626  35.048 131.330 1.00 32.43  ? 93  TYR D CB  1 
ATOM   1509 C  CG  . TYR D 1 9  ? 24.182  36.486 131.407 1.00 32.69  ? 93  TYR D CG  1 
ATOM   1510 C  CD1 . TYR D 1 9  ? 25.092  37.493 131.688 1.00 34.50  ? 93  TYR D CD1 1 
ATOM   1511 C  CD2 . TYR D 1 9  ? 22.850  36.834 131.219 1.00 32.46  ? 93  TYR D CD2 1 
ATOM   1512 C  CE1 . TYR D 1 9  ? 24.696  38.814 131.764 1.00 36.31  ? 93  TYR D CE1 1 
ATOM   1513 C  CE2 . TYR D 1 9  ? 22.442  38.148 131.293 1.00 34.21  ? 93  TYR D CE2 1 
ATOM   1514 C  CZ  . TYR D 1 9  ? 23.371  39.137 131.567 1.00 36.28  ? 93  TYR D CZ  1 
ATOM   1515 O  OH  . TYR D 1 9  ? 22.978  40.452 131.639 1.00 40.46  ? 93  TYR D OH  1 
ATOM   1516 N  N   . ASP D 1 10 ? 26.028  32.438 130.597 1.00 36.09  ? 94  ASP D N   1 
ATOM   1517 C  CA  . ASP D 1 10 ? 25.805  31.003 130.672 1.00 34.41  ? 94  ASP D CA  1 
ATOM   1518 C  C   . ASP D 1 10 ? 24.547  30.723 131.487 1.00 36.56  ? 94  ASP D C   1 
ATOM   1519 O  O   . ASP D 1 10 ? 24.201  31.465 132.409 1.00 36.88  ? 94  ASP D O   1 
ATOM   1520 C  CB  . ASP D 1 10 ? 26.960  30.300 131.385 1.00 36.75  ? 94  ASP D CB  1 
ATOM   1521 C  CG  . ASP D 1 10 ? 28.299  30.484 130.700 1.00 37.92  ? 94  ASP D CG  1 
ATOM   1522 O  OD1 . ASP D 1 10 ? 28.364  30.726 129.485 1.00 39.37  ? 94  ASP D OD1 1 
ATOM   1523 O  OD2 . ASP D 1 10 ? 29.315  30.352 131.401 1.00 41.77  ? 94  ASP D OD2 1 
ATOM   1524 N  N   . TYR D 1 11 ? 23.870  29.626 131.156 1.00 36.52  ? 95  TYR D N   1 
ATOM   1525 C  CA  . TYR D 1 11 ? 22.777  29.127 131.982 1.00 38.32  ? 95  TYR D CA  1 
ATOM   1526 C  C   . TYR D 1 11 ? 22.848  27.609 132.021 1.00 40.62  ? 95  TYR D C   1 
ATOM   1527 O  O   . TYR D 1 11 ? 22.827  26.956 130.972 1.00 41.64  ? 95  TYR D O   1 
ATOM   1528 C  CB  . TYR D 1 11 ? 21.405  29.597 131.484 1.00 38.54  ? 95  TYR D CB  1 
ATOM   1529 C  CG  . TYR D 1 11 ? 20.279  29.127 132.379 1.00 39.62  ? 95  TYR D CG  1 
ATOM   1530 C  CD1 . TYR D 1 11 ? 19.995  29.783 133.572 1.00 39.71  ? 95  TYR D CD1 1 
ATOM   1531 C  CD2 . TYR D 1 11 ? 19.519  28.009 132.047 1.00 40.83  ? 95  TYR D CD2 1 
ATOM   1532 C  CE1 . TYR D 1 11 ? 18.973  29.348 134.404 1.00 41.99  ? 95  TYR D CE1 1 
ATOM   1533 C  CE2 . TYR D 1 11 ? 18.492  27.569 132.868 1.00 40.59  ? 95  TYR D CE2 1 
ATOM   1534 C  CZ  . TYR D 1 11 ? 18.225  28.242 134.045 1.00 41.28  ? 95  TYR D CZ  1 
ATOM   1535 O  OH  . TYR D 1 11 ? 17.209  27.802 134.867 1.00 43.23  ? 95  TYR D OH  1 
ATOM   1536 N  N   . GLU D 1 12 ? 22.950  27.058 133.230 1.00 43.81  ? 96  GLU D N   1 
ATOM   1537 C  CA  . GLU D 1 12 ? 22.932  25.620 133.466 1.00 45.28  ? 96  GLU D CA  1 
ATOM   1538 C  C   . GLU D 1 12 ? 21.587  25.255 134.078 1.00 44.24  ? 96  GLU D C   1 
ATOM   1539 O  O   . GLU D 1 12 ? 21.321  25.581 135.240 1.00 44.09  ? 96  GLU D O   1 
ATOM   1540 C  CB  . GLU D 1 12 ? 24.065  25.220 134.408 1.00 52.78  ? 96  GLU D CB  1 
ATOM   1541 C  CG  . GLU D 1 12 ? 25.365  24.922 133.697 1.00 60.30  ? 96  GLU D CG  1 
ATOM   1542 C  CD  . GLU D 1 12 ? 25.275  23.671 132.843 1.00 65.90  ? 96  GLU D CD  1 
ATOM   1543 O  OE1 . GLU D 1 12 ? 24.767  22.643 133.343 1.00 68.54  ? 96  GLU D OE1 1 
ATOM   1544 O  OE2 . GLU D 1 12 ? 25.706  23.719 131.671 1.00 66.71  ? 96  GLU D OE2 1 
ATOM   1545 N  N   . SER D 1 13 ? 20.748  24.584 133.295 1.00 45.64  ? 97  SER D N   1 
ATOM   1546 C  CA  . SER D 1 13 ? 19.487  24.050 133.793 1.00 45.28  ? 97  SER D CA  1 
ATOM   1547 C  C   . SER D 1 13 ? 19.771  22.864 134.708 1.00 45.75  ? 97  SER D C   1 
ATOM   1548 O  O   . SER D 1 13 ? 20.309  21.847 134.258 1.00 47.25  ? 97  SER D O   1 
ATOM   1549 C  CB  . SER D 1 13 ? 18.627  23.611 132.610 1.00 48.08  ? 97  SER D CB  1 
ATOM   1550 O  OG  . SER D 1 13 ? 17.445  22.957 133.038 1.00 48.17  ? 97  SER D OG  1 
ATOM   1551 N  N   . ARG D 1 14 ? 19.395  22.995 135.985 1.00 45.95  ? 98  ARG D N   1 
ATOM   1552 C  CA  . ARG D 1 14 ? 19.757  21.999 136.995 1.00 49.11  ? 98  ARG D CA  1 
ATOM   1553 C  C   . ARG D 1 14 ? 19.356  20.597 136.565 1.00 54.63  ? 98  ARG D C   1 
ATOM   1554 O  O   . ARG D 1 14 ? 20.161  19.659 136.610 1.00 52.56  ? 98  ARG D O   1 
ATOM   1555 C  CB  . ARG D 1 14 ? 19.093  22.342 138.327 1.00 48.37  ? 98  ARG D CB  1 
ATOM   1556 C  CG  . ARG D 1 14 ? 19.486  21.408 139.451 1.00 47.32  ? 98  ARG D CG  1 
ATOM   1557 C  CD  . ARG D 1 14 ? 18.817  21.785 140.755 1.00 45.97  ? 98  ARG D CD  1 
ATOM   1558 N  NE  . ARG D 1 14 ? 17.376  21.572 140.735 1.00 44.53  ? 98  ARG D NE  1 
ATOM   1559 C  CZ  . ARG D 1 14 ? 16.781  20.430 141.053 1.00 46.72  ? 98  ARG D CZ  1 
ATOM   1560 N  NH1 . ARG D 1 14 ? 17.478  19.358 141.402 1.00 48.32  ? 98  ARG D NH1 1 
ATOM   1561 N  NH2 . ARG D 1 14 ? 15.454  20.362 141.024 1.00 48.54  ? 98  ARG D NH2 1 
ATOM   1562 N  N   . THR D 1 15 ? 18.100  20.430 136.182 1.00 58.52  ? 99  THR D N   1 
ATOM   1563 C  CA  . THR D 1 15 ? 17.661  19.231 135.496 1.00 66.19  ? 99  THR D CA  1 
ATOM   1564 C  C   . THR D 1 15 ? 17.557  19.554 134.015 1.00 72.60  ? 99  THR D C   1 
ATOM   1565 O  O   . THR D 1 15 ? 17.413  20.712 133.619 1.00 74.56  ? 99  THR D O   1 
ATOM   1566 C  CB  . THR D 1 15 ? 16.312  18.763 136.044 1.00 67.51  ? 99  THR D CB  1 
ATOM   1567 O  OG1 . THR D 1 15 ? 15.368  19.838 135.973 1.00 69.99  ? 99  THR D OG1 1 
ATOM   1568 C  CG2 . THR D 1 15 ? 16.456  18.317 137.492 1.00 67.01  ? 99  THR D CG2 1 
ATOM   1569 N  N   . GLU D 1 16 ? 17.644  18.519 133.190 1.00 77.77  ? 100 GLU D N   1 
ATOM   1570 C  CA  . GLU D 1 16 ? 17.659  18.753 131.753 1.00 79.59  ? 100 GLU D CA  1 
ATOM   1571 C  C   . GLU D 1 16 ? 16.260  19.064 131.244 1.00 73.21  ? 100 GLU D C   1 
ATOM   1572 O  O   . GLU D 1 16 ? 15.849  18.557 130.198 1.00 75.81  ? 100 GLU D O   1 
ATOM   1573 C  CB  . GLU D 1 16 ? 18.260  17.548 131.029 1.00 86.63  ? 100 GLU D CB  1 
ATOM   1574 C  CG  . GLU D 1 16 ? 19.660  17.201 131.505 1.00 91.84  ? 100 GLU D CG  1 
ATOM   1575 C  CD  . GLU D 1 16 ? 20.173  15.894 130.934 1.00 95.84  ? 100 GLU D CD  1 
ATOM   1576 O  OE1 . GLU D 1 16 ? 19.584  15.386 129.954 1.00 96.84  ? 100 GLU D OE1 1 
ATOM   1577 O  OE2 . GLU D 1 16 ? 21.169  15.372 131.478 1.00 97.31  ? 100 GLU D OE2 1 
ATOM   1578 N  N   . THR D 1 17 ? 15.524  19.900 131.976 1.00 63.10  ? 101 THR D N   1 
ATOM   1579 C  CA  . THR D 1 17 ? 14.164  20.242 131.579 1.00 58.42  ? 101 THR D CA  1 
ATOM   1580 C  C   . THR D 1 17 ? 14.087  21.510 130.745 1.00 53.39  ? 101 THR D C   1 
ATOM   1581 O  O   . THR D 1 17 ? 13.179  21.632 129.920 1.00 50.45  ? 101 THR D O   1 
ATOM   1582 C  CB  . THR D 1 17 ? 13.240  20.364 132.797 1.00 62.81  ? 101 THR D CB  1 
ATOM   1583 O  OG1 . THR D 1 17 ? 11.932  20.739 132.348 1.00 67.48  ? 101 THR D OG1 1 
ATOM   1584 C  CG2 . THR D 1 17 ? 13.746  21.415 133.764 1.00 61.85  ? 101 THR D CG2 1 
ATOM   1585 N  N   . ASP D 1 18 ? 14.997  22.459 130.959 1.00 47.73  ? 102 ASP D N   1 
ATOM   1586 C  CA  . ASP D 1 18 ? 15.148  23.642 130.130 1.00 45.94  ? 102 ASP D CA  1 
ATOM   1587 C  C   . ASP D 1 18 ? 16.451  23.534 129.356 1.00 44.56  ? 102 ASP D C   1 
ATOM   1588 O  O   . ASP D 1 18 ? 17.260  22.629 129.576 1.00 45.69  ? 102 ASP D O   1 
ATOM   1589 C  CB  . ASP D 1 18 ? 15.163  24.914 130.988 1.00 42.15  ? 102 ASP D CB  1 
ATOM   1590 C  CG  . ASP D 1 18 ? 13.849  25.150 131.694 1.00 46.62  ? 102 ASP D CG  1 
ATOM   1591 O  OD1 . ASP D 1 18 ? 12.796  25.008 131.038 1.00 46.65  ? 102 ASP D OD1 1 
ATOM   1592 O  OD2 . ASP D 1 18 ? 13.860  25.448 132.905 1.00 50.14  ? 102 ASP D OD2 1 
ATOM   1593 N  N   . LEU D 1 19 ? 16.655  24.471 128.439 1.00 43.71  ? 103 LEU D N   1 
ATOM   1594 C  CA  . LEU D 1 19 ? 17.862  24.457 127.633 1.00 42.40  ? 103 LEU D CA  1 
ATOM   1595 C  C   . LEU D 1 19 ? 19.021  25.003 128.459 1.00 44.01  ? 103 LEU D C   1 
ATOM   1596 O  O   . LEU D 1 19 ? 18.884  26.030 129.130 1.00 47.73  ? 103 LEU D O   1 
ATOM   1597 C  CB  . LEU D 1 19 ? 17.648  25.293 126.370 1.00 43.82  ? 103 LEU D CB  1 
ATOM   1598 C  CG  . LEU D 1 19 ? 18.586  25.009 125.200 1.00 45.12  ? 103 LEU D CG  1 
ATOM   1599 C  CD1 . LEU D 1 19 ? 18.565  23.533 124.850 1.00 44.47  ? 103 LEU D CD1 1 
ATOM   1600 C  CD2 . LEU D 1 19 ? 18.206  25.850 123.996 1.00 48.06  ? 103 LEU D CD2 1 
ATOM   1601 N  N   . SER D 1 20 ? 20.145  24.288 128.452 1.00 42.08  ? 104 SER D N   1 
ATOM   1602 C  CA  . SER D 1 20 ? 21.392  24.814 128.992 1.00 42.40  ? 104 SER D CA  1 
ATOM   1603 C  C   . SER D 1 20 ? 22.200  25.428 127.856 1.00 40.57  ? 104 SER D C   1 
ATOM   1604 O  O   . SER D 1 20 ? 22.228  24.897 126.743 1.00 42.44  ? 104 SER D O   1 
ATOM   1605 C  CB  . SER D 1 20 ? 22.204  23.706 129.667 1.00 42.35  ? 104 SER D CB  1 
ATOM   1606 O  OG  . SER D 1 20 ? 21.562  23.227 130.838 1.00 43.61  ? 104 SER D OG  1 
ATOM   1607 N  N   . PHE D 1 21 ? 22.844  26.561 128.126 1.00 37.87  ? 105 PHE D N   1 
ATOM   1608 C  CA  . PHE D 1 21 ? 23.549  27.250 127.052 1.00 36.94  ? 105 PHE D CA  1 
ATOM   1609 C  C   . PHE D 1 21 ? 24.708  28.068 127.607 1.00 38.99  ? 105 PHE D C   1 
ATOM   1610 O  O   . PHE D 1 21 ? 24.790  28.343 128.808 1.00 39.95  ? 105 PHE D O   1 
ATOM   1611 C  CB  . PHE D 1 21 ? 22.597  28.108 126.200 1.00 36.49  ? 105 PHE D CB  1 
ATOM   1612 C  CG  . PHE D 1 21 ? 21.769  29.082 126.999 1.00 33.41  ? 105 PHE D CG  1 
ATOM   1613 C  CD1 . PHE D 1 21 ? 22.275  30.327 127.339 1.00 34.21  ? 105 PHE D CD1 1 
ATOM   1614 C  CD2 . PHE D 1 21 ? 20.488  28.748 127.414 1.00 36.64  ? 105 PHE D CD2 1 
ATOM   1615 C  CE1 . PHE D 1 21 ? 21.514  31.230 128.067 1.00 33.75  ? 105 PHE D CE1 1 
ATOM   1616 C  CE2 . PHE D 1 21 ? 19.729  29.640 128.152 1.00 33.92  ? 105 PHE D CE2 1 
ATOM   1617 C  CZ  . PHE D 1 21 ? 20.240  30.887 128.471 1.00 34.86  ? 105 PHE D CZ  1 
ATOM   1618 N  N   . LYS D 1 22 ? 25.609  28.449 126.711 1.00 36.64  ? 106 LYS D N   1 
ATOM   1619 C  CA  . LYS D 1 22 ? 26.768  29.256 127.058 1.00 37.55  ? 106 LYS D CA  1 
ATOM   1620 C  C   . LYS D 1 22 ? 26.653  30.648 126.450 1.00 34.96  ? 106 LYS D C   1 
ATOM   1621 O  O   . LYS D 1 22 ? 25.931  30.870 125.473 1.00 35.01  ? 106 LYS D O   1 
ATOM   1622 C  CB  . LYS D 1 22 ? 28.060  28.583 126.585 1.00 41.54  ? 106 LYS D CB  1 
ATOM   1623 C  CG  . LYS D 1 22 ? 28.347  27.262 127.286 1.00 47.30  ? 106 LYS D CG  1 
ATOM   1624 C  CD  . LYS D 1 22 ? 28.542  27.469 128.785 1.00 51.76  ? 106 LYS D CD  1 
ATOM   1625 C  CE  . LYS D 1 22 ? 28.777  26.156 129.518 1.00 56.19  ? 106 LYS D CE  1 
ATOM   1626 N  NZ  . LYS D 1 22 ? 28.827  26.344 131.001 1.00 57.93  ? 106 LYS D NZ  1 
ATOM   1627 N  N   . LYS D 1 23 ? 27.362  31.592 127.063 1.00 34.46  ? 107 LYS D N   1 
ATOM   1628 C  CA  . LYS D 1 23 ? 27.414  32.957 126.558 1.00 34.61  ? 107 LYS D CA  1 
ATOM   1629 C  C   . LYS D 1 23 ? 27.954  32.967 125.133 1.00 33.24  ? 107 LYS D C   1 
ATOM   1630 O  O   . LYS D 1 23 ? 28.916  32.266 124.810 1.00 37.40  ? 107 LYS D O   1 
ATOM   1631 C  CB  . LYS D 1 23 ? 28.322  33.788 127.471 1.00 37.08  ? 107 LYS D CB  1 
ATOM   1632 C  CG  . LYS D 1 23 ? 28.650  35.175 126.941 1.00 42.96  ? 107 LYS D CG  1 
ATOM   1633 C  CD  . LYS D 1 23 ? 29.303  36.053 128.005 1.00 46.19  ? 107 LYS D CD  1 
ATOM   1634 C  CE  . LYS D 1 23 ? 30.412  35.321 128.756 1.00 51.42  ? 107 LYS D CE  1 
ATOM   1635 N  NZ  . LYS D 1 23 ? 31.067  36.198 129.782 1.00 53.96  ? 107 LYS D NZ  1 
ATOM   1636 N  N   . GLY D 1 24 ? 27.318  33.760 124.270 1.00 33.19  ? 108 GLY D N   1 
ATOM   1637 C  CA  . GLY D 1 24 ? 27.651  33.773 122.864 1.00 33.31  ? 108 GLY D CA  1 
ATOM   1638 C  C   . GLY D 1 24 ? 26.897  32.768 122.011 1.00 31.69  ? 108 GLY D C   1 
ATOM   1639 O  O   . GLY D 1 24 ? 26.966  32.857 120.780 1.00 32.98  ? 108 GLY D O   1 
ATOM   1640 N  N   . GLU D 1 25 ? 26.189  31.814 122.615 1.00 28.41  ? 109 GLU D N   1 
ATOM   1641 C  CA  . GLU D 1 25 ? 25.436  30.832 121.843 1.00 29.05  ? 109 GLU D CA  1 
ATOM   1642 C  C   . GLU D 1 25 ? 24.231  31.493 121.181 1.00 28.95  ? 109 GLU D C   1 
ATOM   1643 O  O   . GLU D 1 25 ? 23.525  32.301 121.796 1.00 27.92  ? 109 GLU D O   1 
ATOM   1644 C  CB  . GLU D 1 25 ? 24.972  29.716 122.771 1.00 33.43  ? 109 GLU D CB  1 
ATOM   1645 C  CG  . GLU D 1 25 ? 24.423  28.496 122.078 1.00 35.23  ? 109 GLU D CG  1 
ATOM   1646 C  CD  . GLU D 1 25 ? 24.415  27.270 122.985 1.00 35.58  ? 109 GLU D CD  1 
ATOM   1647 O  OE1 . GLU D 1 25 ? 25.168  27.248 123.985 1.00 40.17  ? 109 GLU D OE1 1 
ATOM   1648 O  OE2 . GLU D 1 25 ? 23.649  26.327 122.696 1.00 37.62  ? 109 GLU D OE2 1 
ATOM   1649 N  N   . ARG D 1 26 ? 23.997  31.163 119.912 1.00 26.27  ? 110 ARG D N   1 
ATOM   1650 C  CA  . ARG D 1 26 ? 22.840  31.707 119.212 1.00 25.61  ? 110 ARG D CA  1 
ATOM   1651 C  C   . ARG D 1 26 ? 21.642  30.776 119.333 1.00 26.53  ? 110 ARG D C   1 
ATOM   1652 O  O   . ARG D 1 26 ? 21.781  29.551 119.356 1.00 27.42  ? 110 ARG D O   1 
ATOM   1653 C  CB  . ARG D 1 26 ? 23.167  32.017 117.751 1.00 26.40  ? 110 ARG D CB  1 
ATOM   1654 C  CG  . ARG D 1 26 ? 24.058  33.259 117.648 1.00 30.57  ? 110 ARG D CG  1 
ATOM   1655 C  CD  . ARG D 1 26 ? 24.499  33.562 116.233 1.00 36.46  ? 110 ARG D CD  1 
ATOM   1656 N  NE  . ARG D 1 26 ? 25.133  34.872 116.141 1.00 44.15  ? 110 ARG D NE  1 
ATOM   1657 C  CZ  . ARG D 1 26 ? 26.403  35.113 116.438 1.00 48.03  ? 110 ARG D CZ  1 
ATOM   1658 N  NH1 . ARG D 1 26 ? 27.215  34.150 116.846 1.00 49.53  ? 110 ARG D NH1 1 
ATOM   1659 N  NH2 . ARG D 1 26 ? 26.869  36.353 116.329 1.00 49.27  ? 110 ARG D NH2 1 
ATOM   1660 N  N   . LEU D 1 27 ? 20.454  31.376 119.406 1.00 23.88  ? 111 LEU D N   1 
ATOM   1661 C  CA  . LEU D 1 27 ? 19.222  30.644 119.675 1.00 26.24  ? 111 LEU D CA  1 
ATOM   1662 C  C   . LEU D 1 27 ? 18.117  31.173 118.780 1.00 24.55  ? 111 LEU D C   1 
ATOM   1663 O  O   . LEU D 1 27 ? 17.889  32.385 118.744 1.00 26.91  ? 111 LEU D O   1 
ATOM   1664 C  CB  . LEU D 1 27 ? 18.803  30.873 121.128 1.00 27.82  ? 111 LEU D CB  1 
ATOM   1665 C  CG  . LEU D 1 27 ? 19.796  30.402 122.186 1.00 31.14  ? 111 LEU D CG  1 
ATOM   1666 C  CD1 . LEU D 1 27 ? 19.543  31.087 123.509 1.00 35.59  ? 111 LEU D CD1 1 
ATOM   1667 C  CD2 . LEU D 1 27 ? 19.709  28.894 122.348 1.00 34.27  ? 111 LEU D CD2 1 
ATOM   1668 N  N   . GLN D 1 28 ? 17.414  30.276 118.084 1.00 23.31  ? 112 GLN D N   1 
ATOM   1669 C  CA  . GLN D 1 28 ? 16.203  30.690 117.392 1.00 22.82  ? 112 GLN D CA  1 
ATOM   1670 C  C   . GLN D 1 28 ? 15.060  30.740 118.392 1.00 25.16  ? 112 GLN D C   1 
ATOM   1671 O  O   . GLN D 1 28 ? 14.813  29.764 119.105 1.00 26.88  ? 112 GLN D O   1 
ATOM   1672 C  CB  . GLN D 1 28 ? 15.849  29.752 116.238 1.00 23.32  ? 112 GLN D CB  1 
ATOM   1673 C  CG  . GLN D 1 28 ? 14.581  30.220 115.520 1.00 24.73  ? 112 GLN D CG  1 
ATOM   1674 C  CD  . GLN D 1 28 ? 14.046  29.268 114.448 1.00 23.94  ? 112 GLN D CD  1 
ATOM   1675 O  OE1 . GLN D 1 28 ? 14.489  28.135 114.319 1.00 24.81  ? 112 GLN D OE1 1 
ATOM   1676 N  NE2 . GLN D 1 28 ? 13.073  29.742 113.683 1.00 26.12  ? 112 GLN D NE2 1 
ATOM   1677 N  N   . ILE D 1 29 ? 14.372  31.876 118.455 1.00 22.66  ? 113 ILE D N   1 
ATOM   1678 C  CA  . ILE D 1 29 ? 13.234  32.024 119.349 1.00 25.25  ? 113 ILE D CA  1 
ATOM   1679 C  C   . ILE D 1 29 ? 11.981  31.699 118.557 1.00 25.07  ? 113 ILE D C   1 
ATOM   1680 O  O   . ILE D 1 29 ? 11.715  32.322 117.522 1.00 29.29  ? 113 ILE D O   1 
ATOM   1681 C  CB  . ILE D 1 29 ? 13.174  33.440 119.934 1.00 27.95  ? 113 ILE D CB  1 
ATOM   1682 C  CG1 . ILE D 1 29 ? 14.516  33.795 120.593 1.00 28.21  ? 113 ILE D CG1 1 
ATOM   1683 C  CG2 . ILE D 1 29 ? 12.019  33.548 120.925 1.00 29.78  ? 113 ILE D CG2 1 
ATOM   1684 C  CD1 . ILE D 1 29 ? 14.938  32.847 121.725 1.00 26.68  ? 113 ILE D CD1 1 
ATOM   1685 N  N   . VAL D 1 30 ? 11.223  30.713 119.025 1.00 28.52  ? 114 VAL D N   1 
ATOM   1686 C  CA  . VAL D 1 30 ? 10.006  30.295 118.332 1.00 34.30  ? 114 VAL D CA  1 
ATOM   1687 C  C   . VAL D 1 30 ? 8.741   30.585 119.136 1.00 39.93  ? 114 VAL D C   1 
ATOM   1688 O  O   . VAL D 1 30 ? 8.766   30.673 120.362 1.00 41.82  ? 114 VAL D O   1 
ATOM   1689 C  CB  . VAL D 1 30 ? 10.083  28.820 117.875 1.00 37.30  ? 114 VAL D CB  1 
ATOM   1690 C  CG1 . VAL D 1 30 ? 11.152  28.648 116.803 1.00 38.36  ? 114 VAL D CG1 1 
ATOM   1691 C  CG2 . VAL D 1 30 ? 10.363  27.907 119.037 1.00 36.32  ? 114 VAL D CG2 1 
ATOM   1692 N  N   . ASP D 1 36 ? 8.164   35.118 130.405 1.00 47.09  ? 120 ASP D N   1 
ATOM   1693 C  CA  . ASP D 1 36 ? 9.509   35.196 130.962 1.00 47.73  ? 120 ASP D CA  1 
ATOM   1694 C  C   . ASP D 1 36 ? 10.400  34.103 130.392 1.00 43.14  ? 120 ASP D C   1 
ATOM   1695 O  O   . ASP D 1 36 ? 11.628  34.211 130.418 1.00 43.77  ? 120 ASP D O   1 
ATOM   1696 C  CB  . ASP D 1 36 ? 9.466   35.073 132.484 1.00 52.94  ? 120 ASP D CB  1 
ATOM   1697 C  CG  . ASP D 1 36 ? 8.869   36.294 133.154 1.00 58.02  ? 120 ASP D CG  1 
ATOM   1698 O  OD1 . ASP D 1 36 ? 8.574   37.279 132.444 1.00 57.79  ? 120 ASP D OD1 1 
ATOM   1699 O  OD2 . ASP D 1 36 ? 8.699   36.264 134.394 1.00 61.09  ? 120 ASP D OD2 1 
ATOM   1700 N  N   . TRP D 1 37 ? 9.779   33.045 129.885 1.00 38.83  ? 121 TRP D N   1 
ATOM   1701 C  CA  . TRP D 1 37 ? 10.492  31.911 129.319 1.00 36.07  ? 121 TRP D CA  1 
ATOM   1702 C  C   . TRP D 1 37 ? 10.072  31.743 127.867 1.00 33.42  ? 121 TRP D C   1 
ATOM   1703 O  O   . TRP D 1 37 ? 8.877   31.747 127.552 1.00 35.05  ? 121 TRP D O   1 
ATOM   1704 C  CB  . TRP D 1 37 ? 10.233  30.631 130.121 1.00 37.26  ? 121 TRP D CB  1 
ATOM   1705 C  CG  . TRP D 1 37 ? 10.866  30.667 131.476 1.00 37.44  ? 121 TRP D CG  1 
ATOM   1706 C  CD1 . TRP D 1 37 ? 10.361  31.251 132.600 1.00 38.87  ? 121 TRP D CD1 1 
ATOM   1707 C  CD2 . TRP D 1 37 ? 12.133  30.103 131.850 1.00 37.70  ? 121 TRP D CD2 1 
ATOM   1708 N  NE1 . TRP D 1 37 ? 11.233  31.083 133.651 1.00 38.65  ? 121 TRP D NE1 1 
ATOM   1709 C  CE2 . TRP D 1 37 ? 12.324  30.378 133.217 1.00 37.75  ? 121 TRP D CE2 1 
ATOM   1710 C  CE3 . TRP D 1 37 ? 13.116  29.383 131.164 1.00 36.95  ? 121 TRP D CE3 1 
ATOM   1711 C  CZ2 . TRP D 1 37 ? 13.463  29.966 133.909 1.00 37.67  ? 121 TRP D CZ2 1 
ATOM   1712 C  CZ3 . TRP D 1 37 ? 14.248  28.976 131.851 1.00 36.91  ? 121 TRP D CZ3 1 
ATOM   1713 C  CH2 . TRP D 1 37 ? 14.409  29.267 133.209 1.00 37.39  ? 121 TRP D CH2 1 
ATOM   1714 N  N   . TRP D 1 38 ? 11.056  31.624 126.989 1.00 29.53  ? 122 TRP D N   1 
ATOM   1715 C  CA  . TRP D 1 38 ? 10.823  31.521 125.559 1.00 28.55  ? 122 TRP D CA  1 
ATOM   1716 C  C   . TRP D 1 38 ? 11.280  30.156 125.079 1.00 27.55  ? 122 TRP D C   1 
ATOM   1717 O  O   . TRP D 1 38 ? 12.327  29.666 125.497 1.00 28.29  ? 122 TRP D O   1 
ATOM   1718 C  CB  . TRP D 1 38 ? 11.652  32.562 124.828 1.00 27.25  ? 122 TRP D CB  1 
ATOM   1719 C  CG  . TRP D 1 38 ? 11.212  33.963 125.034 1.00 28.00  ? 122 TRP D CG  1 
ATOM   1720 C  CD1 . TRP D 1 38 ? 10.078  34.389 125.676 1.00 28.63  ? 122 TRP D CD1 1 
ATOM   1721 C  CD2 . TRP D 1 38 ? 11.883  35.143 124.575 1.00 28.12  ? 122 TRP D CD2 1 
ATOM   1722 N  NE1 . TRP D 1 38 ? 10.011  35.766 125.648 1.00 28.72  ? 122 TRP D NE1 1 
ATOM   1723 C  CE2 . TRP D 1 38 ? 11.102  36.248 124.971 1.00 28.72  ? 122 TRP D CE2 1 
ATOM   1724 C  CE3 . TRP D 1 38 ? 13.072  35.371 123.871 1.00 27.00  ? 122 TRP D CE3 1 
ATOM   1725 C  CZ2 . TRP D 1 38 ? 11.471  37.565 124.686 1.00 28.23  ? 122 TRP D CZ2 1 
ATOM   1726 C  CZ3 . TRP D 1 38 ? 13.434  36.683 123.580 1.00 26.49  ? 122 TRP D CZ3 1 
ATOM   1727 C  CH2 . TRP D 1 38 ? 12.633  37.763 123.987 1.00 29.36  ? 122 TRP D CH2 1 
ATOM   1728 N  N   . LEU D 1 39 ? 10.507  29.555 124.179 1.00 28.68  ? 123 LEU D N   1 
ATOM   1729 C  CA  . LEU D 1 39 ? 10.922  28.302 123.563 1.00 28.48  ? 123 LEU D CA  1 
ATOM   1730 C  C   . LEU D 1 39 ? 11.965  28.604 122.497 1.00 28.59  ? 123 LEU D C   1 
ATOM   1731 O  O   . LEU D 1 39 ? 11.769  29.506 121.676 1.00 31.37  ? 123 LEU D O   1 
ATOM   1732 C  CB  . LEU D 1 39 ? 9.719   27.593 122.948 1.00 28.50  ? 123 LEU D CB  1 
ATOM   1733 C  CG  . LEU D 1 39 ? 9.963   26.193 122.377 1.00 29.19  ? 123 LEU D CG  1 
ATOM   1734 C  CD1 . LEU D 1 39 ? 10.460  25.240 123.466 1.00 30.99  ? 123 LEU D CD1 1 
ATOM   1735 C  CD2 . LEU D 1 39 ? 8.699   25.651 121.735 1.00 29.53  ? 123 LEU D CD2 1 
ATOM   1736 N  N   . ALA D 1 40 ? 13.079  27.868 122.520 1.00 26.99  ? 124 ALA D N   1 
ATOM   1737 C  CA  . ALA D 1 40 ? 14.211  28.189 121.665 1.00 26.73  ? 124 ALA D CA  1 
ATOM   1738 C  C   . ALA D 1 40 ? 14.887  26.931 121.133 1.00 28.34  ? 124 ALA D C   1 
ATOM   1739 O  O   . ALA D 1 40 ? 14.835  25.858 121.742 1.00 28.93  ? 124 ALA D O   1 
ATOM   1740 C  CB  . ALA D 1 40 ? 15.260  29.027 122.405 1.00 28.36  ? 124 ALA D CB  1 
ATOM   1741 N  N   . HIS D 1 41 ? 15.550  27.085 119.986 1.00 28.96  ? 125 HIS D N   1 
ATOM   1742 C  CA  . HIS D 1 41 ? 16.415  26.053 119.428 1.00 26.98  ? 125 HIS D CA  1 
ATOM   1743 C  C   . HIS D 1 41 ? 17.844  26.570 119.468 1.00 26.98  ? 125 HIS D C   1 
ATOM   1744 O  O   . HIS D 1 41 ? 18.107  27.688 119.026 1.00 26.35  ? 125 HIS D O   1 
ATOM   1745 C  CB  . HIS D 1 41 ? 16.065  25.750 117.968 1.00 28.11  ? 125 HIS D CB  1 
ATOM   1746 C  CG  . HIS D 1 41 ? 14.623  25.416 117.726 1.00 30.75  ? 125 HIS D CG  1 
ATOM   1747 N  ND1 . HIS D 1 41 ? 14.013  24.298 118.254 1.00 34.88  ? 125 HIS D ND1 1 
ATOM   1748 C  CD2 . HIS D 1 41 ? 13.684  26.031 116.964 1.00 32.85  ? 125 HIS D CD2 1 
ATOM   1749 C  CE1 . HIS D 1 41 ? 12.755  24.254 117.849 1.00 34.07  ? 125 HIS D CE1 1 
ATOM   1750 N  NE2 . HIS D 1 41 ? 12.532  25.288 117.060 1.00 34.71  ? 125 HIS D NE2 1 
ATOM   1751 N  N   . SER D 1 42 ? 18.765  25.767 119.984 1.00 28.18  ? 126 SER D N   1 
ATOM   1752 C  CA  . SER D 1 42 ? 20.168  26.167 119.996 1.00 28.82  ? 126 SER D CA  1 
ATOM   1753 C  C   . SER D 1 42 ? 20.790  25.975 118.623 1.00 28.84  ? 126 SER D C   1 
ATOM   1754 O  O   . SER D 1 42 ? 20.743  24.877 118.062 1.00 29.17  ? 126 SER D O   1 
ATOM   1755 C  CB  . SER D 1 42 ? 20.970  25.338 120.992 1.00 29.71  ? 126 SER D CB  1 
ATOM   1756 O  OG  . SER D 1 42 ? 22.352  25.549 120.744 1.00 31.14  ? 126 SER D OG  1 
ATOM   1757 N  N   . LEU D 1 43 ? 21.406  27.030 118.098 1.00 28.99  ? 127 LEU D N   1 
ATOM   1758 C  CA  . LEU D 1 43 ? 22.135  26.909 116.843 1.00 30.89  ? 127 LEU D CA  1 
ATOM   1759 C  C   . LEU D 1 43 ? 23.514  26.291 117.011 1.00 32.41  ? 127 LEU D C   1 
ATOM   1760 O  O   . LEU D 1 43 ? 24.178  26.022 116.006 1.00 35.04  ? 127 LEU D O   1 
ATOM   1761 C  CB  . LEU D 1 43 ? 22.241  28.267 116.151 1.00 31.70  ? 127 LEU D CB  1 
ATOM   1762 C  CG  . LEU D 1 43 ? 21.054  28.658 115.279 1.00 35.84  ? 127 LEU D CG  1 
ATOM   1763 C  CD1 . LEU D 1 43 ? 19.739  28.679 116.040 1.00 35.36  ? 127 LEU D CD1 1 
ATOM   1764 C  CD2 . LEU D 1 43 ? 21.334  30.007 114.689 1.00 34.00  ? 127 LEU D CD2 1 
ATOM   1765 N  N   . SER D 1 44 ? 23.957  26.061 118.244 1.00 31.51  ? 128 SER D N   1 
ATOM   1766 C  CA  . SER D 1 44 ? 25.213  25.358 118.476 1.00 33.54  ? 128 SER D CA  1 
ATOM   1767 C  C   . SER D 1 44 ? 25.018  23.852 118.579 1.00 37.74  ? 128 SER D C   1 
ATOM   1768 O  O   . SER D 1 44 ? 25.850  23.085 118.082 1.00 39.68  ? 128 SER D O   1 
ATOM   1769 C  CB  . SER D 1 44 ? 25.870  25.857 119.763 1.00 37.09  ? 128 SER D CB  1 
ATOM   1770 O  OG  . SER D 1 44 ? 26.285  27.204 119.648 1.00 40.78  ? 128 SER D OG  1 
ATOM   1771 N  N   . THR D 1 45 ? 23.937  23.405 119.223 1.00 36.61  ? 129 THR D N   1 
ATOM   1772 C  CA  . THR D 1 45 ? 23.736  21.980 119.464 1.00 36.24  ? 129 THR D CA  1 
ATOM   1773 C  C   . THR D 1 45 ? 22.547  21.381 118.731 1.00 37.13  ? 129 THR D C   1 
ATOM   1774 O  O   . THR D 1 45 ? 22.450  20.151 118.661 1.00 37.69  ? 129 THR D O   1 
ATOM   1775 C  CB  . THR D 1 45 ? 23.522  21.702 120.960 1.00 37.64  ? 129 THR D CB  1 
ATOM   1776 O  OG1 . THR D 1 45 ? 22.250  22.237 121.356 1.00 39.97  ? 129 THR D OG1 1 
ATOM   1777 C  CG2 . THR D 1 45 ? 24.631  22.331 121.800 1.00 37.06  ? 129 THR D CG2 1 
ATOM   1778 N  N   . GLY D 1 46 ? 21.633  22.202 118.213 1.00 35.60  ? 130 GLY D N   1 
ATOM   1779 C  CA  . GLY D 1 46 ? 20.392  21.704 117.658 1.00 35.65  ? 130 GLY D CA  1 
ATOM   1780 C  C   . GLY D 1 46 ? 19.337  21.318 118.673 1.00 35.95  ? 130 GLY D C   1 
ATOM   1781 O  O   . GLY D 1 46 ? 18.244  20.906 118.271 1.00 36.20  ? 130 GLY D O   1 
ATOM   1782 N  N   . GLN D 1 47 ? 19.625  21.428 119.967 1.00 38.65  ? 131 GLN D N   1 
ATOM   1783 C  CA  . GLN D 1 47 ? 18.658  21.094 121.001 1.00 40.42  ? 131 GLN D CA  1 
ATOM   1784 C  C   . GLN D 1 47 ? 17.578  22.164 121.111 1.00 38.60  ? 131 GLN D C   1 
ATOM   1785 O  O   . GLN D 1 47 ? 17.789  23.336 120.797 1.00 36.19  ? 131 GLN D O   1 
ATOM   1786 C  CB  . GLN D 1 47 ? 19.339  21.012 122.363 1.00 45.45  ? 131 GLN D CB  1 
ATOM   1787 C  CG  . GLN D 1 47 ? 20.001  19.708 122.675 1.00 49.62  ? 131 GLN D CG  1 
ATOM   1788 C  CD  . GLN D 1 47 ? 20.441  19.649 124.121 1.00 54.61  ? 131 GLN D CD  1 
ATOM   1789 O  OE1 . GLN D 1 47 ? 20.999  20.613 124.649 1.00 54.85  ? 131 GLN D OE1 1 
ATOM   1790 N  NE2 . GLN D 1 47 ? 20.170  18.529 124.780 1.00 55.26  ? 131 GLN D NE2 1 
ATOM   1791 N  N   . THR D 1 48 ? 16.421  21.748 121.618 1.00 38.40  ? 132 THR D N   1 
ATOM   1792 C  CA  . THR D 1 48 ? 15.272  22.619 121.816 1.00 37.67  ? 132 THR D CA  1 
ATOM   1793 C  C   . THR D 1 48 ? 14.878  22.611 123.287 1.00 37.43  ? 132 THR D C   1 
ATOM   1794 O  O   . THR D 1 48 ? 14.883  21.560 123.932 1.00 38.61  ? 132 THR D O   1 
ATOM   1795 C  CB  . THR D 1 48 ? 14.089  22.121 120.981 1.00 37.66  ? 132 THR D CB  1 
ATOM   1796 O  OG1 . THR D 1 48 ? 14.461  22.081 119.597 1.00 41.68  ? 132 THR D OG1 1 
ATOM   1797 C  CG2 . THR D 1 48 ? 12.875  23.030 121.146 1.00 39.88  ? 132 THR D CG2 1 
ATOM   1798 N  N   . GLY D 1 49 ? 14.526  23.780 123.807 1.00 35.06  ? 133 GLY D N   1 
ATOM   1799 C  CA  . GLY D 1 49 ? 14.044  23.890 125.176 1.00 34.08  ? 133 GLY D CA  1 
ATOM   1800 C  C   . GLY D 1 49 ? 13.732  25.335 125.501 1.00 32.39  ? 133 GLY D C   1 
ATOM   1801 O  O   . GLY D 1 49 ? 13.982  26.245 124.706 1.00 33.92  ? 133 GLY D O   1 
ATOM   1802 N  N   . TYR D 1 50 ? 13.171  25.536 126.691 1.00 33.50  ? 134 TYR D N   1 
ATOM   1803 C  CA  . TYR D 1 50 ? 12.854  26.886 127.138 1.00 32.49  ? 134 TYR D CA  1 
ATOM   1804 C  C   . TYR D 1 50 ? 14.078  27.592 127.698 1.00 31.52  ? 134 TYR D C   1 
ATOM   1805 O  O   . TYR D 1 50 ? 14.945  26.972 128.318 1.00 34.69  ? 134 TYR D O   1 
ATOM   1806 C  CB  . TYR D 1 50 ? 11.734  26.867 128.173 1.00 34.76  ? 134 TYR D CB  1 
ATOM   1807 C  CG  . TYR D 1 50 ? 10.395  26.604 127.538 1.00 36.28  ? 134 TYR D CG  1 
ATOM   1808 C  CD1 . TYR D 1 50 ? 9.613   27.649 127.067 1.00 37.57  ? 134 TYR D CD1 1 
ATOM   1809 C  CD2 . TYR D 1 50 ? 9.915   25.308 127.396 1.00 39.12  ? 134 TYR D CD2 1 
ATOM   1810 C  CE1 . TYR D 1 50 ? 8.391   27.411 126.475 1.00 39.83  ? 134 TYR D CE1 1 
ATOM   1811 C  CE2 . TYR D 1 50 ? 8.693   25.064 126.812 1.00 39.38  ? 134 TYR D CE2 1 
ATOM   1812 C  CZ  . TYR D 1 50 ? 7.937   26.117 126.354 1.00 40.55  ? 134 TYR D CZ  1 
ATOM   1813 O  OH  . TYR D 1 50 ? 6.720   25.876 125.768 1.00 43.77  ? 134 TYR D OH  1 
ATOM   1814 N  N   A ILE D 1 51 ? 14.141  28.898 127.477 0.72 29.98  ? 135 ILE D N   1 
ATOM   1815 N  N   B ILE D 1 51 ? 14.146  28.900 127.469 0.28 31.05  ? 135 ILE D N   1 
ATOM   1816 C  CA  A ILE D 1 51 ? 15.245  29.702 127.985 0.72 30.29  ? 135 ILE D CA  1 
ATOM   1817 C  CA  B ILE D 1 51 ? 15.257  29.720 127.946 0.28 31.22  ? 135 ILE D CA  1 
ATOM   1818 C  C   A ILE D 1 51 ? 14.673  30.925 128.686 0.72 29.91  ? 135 ILE D C   1 
ATOM   1819 C  C   B ILE D 1 51 ? 14.698  30.953 128.647 0.28 30.75  ? 135 ILE D C   1 
ATOM   1820 O  O   A ILE D 1 51 ? 13.559  31.368 128.365 0.72 30.72  ? 135 ILE D O   1 
ATOM   1821 O  O   B ILE D 1 51 ? 13.611  31.430 128.286 0.28 31.08  ? 135 ILE D O   1 
ATOM   1822 C  CB  A ILE D 1 51 ? 16.204  30.130 126.862 0.72 30.24  ? 135 ILE D CB  1 
ATOM   1823 C  CB  B ILE D 1 51 ? 16.214  30.098 126.800 0.28 30.35  ? 135 ILE D CB  1 
ATOM   1824 C  CG1 A ILE D 1 51 ? 15.506  31.097 125.908 0.72 29.25  ? 135 ILE D CG1 1 
ATOM   1825 C  CG1 B ILE D 1 51 ? 15.488  30.898 125.712 0.28 29.12  ? 135 ILE D CG1 1 
ATOM   1826 C  CG2 A ILE D 1 51 ? 16.756  28.911 126.127 0.72 31.50  ? 135 ILE D CG2 1 
ATOM   1827 C  CG2 B ILE D 1 51 ? 16.867  28.855 126.210 0.28 30.61  ? 135 ILE D CG2 1 
ATOM   1828 C  CD1 A ILE D 1 51 ? 16.374  31.537 124.796 0.72 32.14  ? 135 ILE D CD1 1 
ATOM   1829 C  CD1 B ILE D 1 51 ? 15.668  32.397 125.828 0.28 28.22  ? 135 ILE D CD1 1 
ATOM   1830 N  N   . PRO D 1 52 ? 15.394  31.505 129.643 1.00 30.66  ? 136 PRO D N   1 
ATOM   1831 C  CA  . PRO D 1 52 ? 14.913  32.737 130.280 1.00 30.15  ? 136 PRO D CA  1 
ATOM   1832 C  C   . PRO D 1 52 ? 15.185  33.926 129.371 1.00 30.52  ? 136 PRO D C   1 
ATOM   1833 O  O   . PRO D 1 52 ? 16.314  34.132 128.921 1.00 29.99  ? 136 PRO D O   1 
ATOM   1834 C  CB  . PRO D 1 52 ? 15.725  32.809 131.577 1.00 31.98  ? 136 PRO D CB  1 
ATOM   1835 C  CG  . PRO D 1 52 ? 16.931  31.968 131.328 1.00 33.62  ? 136 PRO D CG  1 
ATOM   1836 C  CD  . PRO D 1 52 ? 16.626  30.981 130.261 1.00 33.63  ? 136 PRO D CD  1 
ATOM   1837 N  N   . SER D 1 53 ? 14.132  34.693 129.078 1.00 30.07  ? 137 SER D N   1 
ATOM   1838 C  CA  . SER D 1 53 ? 14.245  35.755 128.083 1.00 30.37  ? 137 SER D CA  1 
ATOM   1839 C  C   . SER D 1 53 ? 15.224  36.844 128.502 1.00 28.98  ? 137 SER D C   1 
ATOM   1840 O  O   . SER D 1 53 ? 15.788  37.533 127.641 1.00 30.26  ? 137 SER D O   1 
ATOM   1841 C  CB  . SER D 1 53 ? 12.871  36.354 127.808 1.00 31.77  ? 137 SER D CB  1 
ATOM   1842 O  OG  . SER D 1 53 ? 12.354  36.980 128.962 1.00 35.81  ? 137 SER D OG  1 
ATOM   1843 N  N   . ASN D 1 54 ? 15.445  37.032 129.805 1.00 29.35  ? 138 ASN D N   1 
ATOM   1844 C  CA  . ASN D 1 54 ? 16.382  38.074 130.205 1.00 31.57  ? 138 ASN D CA  1 
ATOM   1845 C  C   . ASN D 1 54 ? 17.841  37.657 130.053 1.00 30.75  ? 138 ASN D C   1 
ATOM   1846 O  O   . ASN D 1 54 ? 18.732  38.456 130.364 1.00 31.99  ? 138 ASN D O   1 
ATOM   1847 C  CB  . ASN D 1 54 ? 16.086  38.611 131.614 1.00 33.92  ? 138 ASN D CB  1 
ATOM   1848 C  CG  . ASN D 1 54 ? 16.208  37.553 132.692 1.00 36.65  ? 138 ASN D CG  1 
ATOM   1849 O  OD1 . ASN D 1 54 ? 16.165  36.356 132.414 1.00 37.09  ? 138 ASN D OD1 1 
ATOM   1850 N  ND2 . ASN D 1 54 ? 16.347  37.996 133.941 1.00 42.13  ? 138 ASN D ND2 1 
ATOM   1851 N  N   . TYR D 1 55 ? 18.106  36.446 129.567 1.00 29.23  ? 139 TYR D N   1 
ATOM   1852 C  CA  . TYR D 1 55 ? 19.466  35.994 129.305 1.00 26.56  ? 139 TYR D CA  1 
ATOM   1853 C  C   . TYR D 1 55 ? 19.899  36.232 127.868 1.00 26.06  ? 139 TYR D C   1 
ATOM   1854 O  O   . TYR D 1 55 ? 21.033  35.902 127.521 1.00 27.59  ? 139 TYR D O   1 
ATOM   1855 C  CB  . TYR D 1 55 ? 19.612  34.506 129.623 1.00 27.56  ? 139 TYR D CB  1 
ATOM   1856 C  CG  . TYR D 1 55 ? 19.900  34.216 131.070 1.00 27.42  ? 139 TYR D CG  1 
ATOM   1857 C  CD1 . TYR D 1 55 ? 19.027  34.624 132.064 1.00 29.24  ? 139 TYR D CD1 1 
ATOM   1858 C  CD2 . TYR D 1 55 ? 21.053  33.540 131.440 1.00 28.81  ? 139 TYR D CD2 1 
ATOM   1859 C  CE1 . TYR D 1 55 ? 19.287  34.349 133.394 1.00 29.63  ? 139 TYR D CE1 1 
ATOM   1860 C  CE2 . TYR D 1 55 ? 21.325  33.271 132.759 1.00 31.57  ? 139 TYR D CE2 1 
ATOM   1861 C  CZ  . TYR D 1 55 ? 20.442  33.680 133.729 1.00 32.15  ? 139 TYR D CZ  1 
ATOM   1862 O  OH  . TYR D 1 55 ? 20.719  33.412 135.045 1.00 35.14  ? 139 TYR D OH  1 
ATOM   1863 N  N   . VAL D 1 56 ? 19.027  36.780 127.020 1.00 25.41  ? 140 VAL D N   1 
ATOM   1864 C  CA  . VAL D 1 56 ? 19.300  36.874 125.593 1.00 24.58  ? 140 VAL D CA  1 
ATOM   1865 C  C   . VAL D 1 56 ? 19.035  38.282 125.058 1.00 24.75  ? 140 VAL D C   1 
ATOM   1866 O  O   . VAL D 1 56 ? 18.285  39.073 125.638 1.00 27.26  ? 140 VAL D O   1 
ATOM   1867 C  CB  . VAL D 1 56 ? 18.527  35.806 124.775 1.00 23.99  ? 140 VAL D CB  1 
ATOM   1868 C  CG1 . VAL D 1 56 ? 18.993  34.392 125.132 1.00 25.93  ? 140 VAL D CG1 1 
ATOM   1869 C  CG2 . VAL D 1 56 ? 17.009  35.940 124.964 1.00 26.46  ? 140 VAL D CG2 1 
ATOM   1870 N  N   . ALA D 1 57 ? 19.663  38.578 123.928 1.00 23.71  ? 141 ALA D N   1 
ATOM   1871 C  CA  . ALA D 1 57 ? 19.531  39.843 123.224 1.00 22.40  ? 141 ALA D CA  1 
ATOM   1872 C  C   . ALA D 1 57 ? 19.549  39.519 121.739 1.00 23.25  ? 141 ALA D C   1 
ATOM   1873 O  O   . ALA D 1 57 ? 20.037  38.457 121.343 1.00 22.94  ? 141 ALA D O   1 
ATOM   1874 C  CB  . ALA D 1 57 ? 20.697  40.794 123.551 1.00 22.86  ? 141 ALA D CB  1 
ATOM   1875 N  N   . PRO D 1 58 ? 18.993  40.392 120.903 1.00 22.00  ? 142 PRO D N   1 
ATOM   1876 C  CA  . PRO D 1 58 ? 18.971  40.105 119.462 1.00 23.00  ? 142 PRO D CA  1 
ATOM   1877 C  C   . PRO D 1 58 ? 20.384  39.880 118.956 1.00 24.94  ? 142 PRO D C   1 
ATOM   1878 O  O   . PRO D 1 58 ? 21.320  40.581 119.349 1.00 25.88  ? 142 PRO D O   1 
ATOM   1879 C  CB  . PRO D 1 58 ? 18.357  41.373 118.858 1.00 24.09  ? 142 PRO D CB  1 
ATOM   1880 C  CG  . PRO D 1 58 ? 17.562  41.982 119.959 1.00 25.85  ? 142 PRO D CG  1 
ATOM   1881 C  CD  . PRO D 1 58 ? 18.296  41.641 121.234 1.00 22.63  ? 142 PRO D CD  1 
ATOM   1882 N  N   . SER D 1 59 ? 20.547  38.871 118.109 1.00 26.18  ? 143 SER D N   1 
ATOM   1883 C  CA  . SER D 1 59 ? 21.896  38.509 117.687 1.00 31.25  ? 143 SER D CA  1 
ATOM   1884 C  C   . SER D 1 59 ? 22.370  39.427 116.568 1.00 35.21  ? 143 SER D C   1 
ATOM   1885 O  O   . SER D 1 59 ? 23.571  39.545 116.314 1.00 35.75  ? 143 SER D O   1 
ATOM   1886 C  CB  . SER D 1 59 ? 21.965  37.046 117.255 1.00 33.41  ? 143 SER D CB  1 
ATOM   1887 O  OG  . SER D 1 59 ? 21.459  36.898 115.946 1.00 37.45  ? 143 SER D OG  1 
ATOM   1888 O  OXT . SER D 1 59 ? 21.566  40.074 115.887 1.00 33.91  ? 143 SER D OXT 1 
HETATM 1889 NI NI  . NI  E 2 .  ? 23.001  15.517 115.877 1.00 27.23  ? 201 NI  A NI  1 
HETATM 1890 C  C1  . GOL F 3 .  ? -1.632  6.275  118.417 1.00 65.45  ? 202 GOL A C1  1 
HETATM 1891 O  O1  . GOL F 3 .  ? -0.547  6.819  119.129 1.00 34.26  ? 202 GOL A O1  1 
HETATM 1892 C  C2  . GOL F 3 .  ? -2.680  5.878  119.426 1.00 32.51  ? 202 GOL A C2  1 
HETATM 1893 O  O2  . GOL F 3 .  ? -3.936  5.850  118.794 1.00 131.54 ? 202 GOL A O2  1 
HETATM 1894 C  C3  . GOL F 3 .  ? -2.333  4.554  120.086 1.00 56.64  ? 202 GOL A C3  1 
HETATM 1895 O  O3  . GOL F 3 .  ? -2.899  4.545  121.385 1.00 47.50  ? 202 GOL A O3  1 
HETATM 1896 C  C1  . GOL G 3 .  ? 2.162   16.390 133.955 1.00 53.65  ? 203 GOL A C1  1 
HETATM 1897 O  O1  . GOL G 3 .  ? 2.460   17.443 134.838 1.00 68.76  ? 203 GOL A O1  1 
HETATM 1898 C  C2  . GOL G 3 .  ? 1.782   15.161 134.753 1.00 53.50  ? 203 GOL A C2  1 
HETATM 1899 O  O2  . GOL G 3 .  ? 0.726   15.498 135.623 1.00 85.47  ? 203 GOL A O2  1 
HETATM 1900 C  C3  . GOL G 3 .  ? 1.387   14.036 133.811 1.00 48.46  ? 203 GOL A C3  1 
HETATM 1901 O  O3  . GOL G 3 .  ? 0.897   12.954 134.576 1.00 69.54  ? 203 GOL A O3  1 
HETATM 1902 NI NI  . NI  H 2 .  ? 9.846   6.988  111.761 1.00 22.00  ? 201 NI  B NI  1 
HETATM 1903 C  C1  . GOL I 3 .  ? 8.552   2.292  112.640 1.00 52.47  ? 202 GOL B C1  1 
HETATM 1904 O  O1  . GOL I 3 .  ? 8.945   3.082  111.544 1.00 47.11  ? 202 GOL B O1  1 
HETATM 1905 C  C2  . GOL I 3 .  ? 9.345   2.691  113.870 1.00 57.61  ? 202 GOL B C2  1 
HETATM 1906 O  O2  . GOL I 3 .  ? 9.333   1.622  114.791 1.00 54.27  ? 202 GOL B O2  1 
HETATM 1907 C  C3  . GOL I 3 .  ? 10.765  3.089  113.506 1.00 56.37  ? 202 GOL B C3  1 
HETATM 1908 O  O3  . GOL I 3 .  ? 11.211  4.026  114.468 1.00 33.12  ? 202 GOL B O3  1 
HETATM 1909 C  C1  . GOL J 3 .  ? 1.876   28.117 94.781  1.00 68.24  ? 201 GOL C C1  1 
HETATM 1910 O  O1  . GOL J 3 .  ? 2.609   27.025 95.296  1.00 49.58  ? 201 GOL C O1  1 
HETATM 1911 C  C2  . GOL J 3 .  ? 0.533   28.231 95.477  1.00 49.16  ? 201 GOL C C2  1 
HETATM 1912 O  O2  . GOL J 3 .  ? 0.715   28.108 96.867  1.00 61.72  ? 201 GOL C O2  1 
HETATM 1913 C  C3  . GOL J 3 .  ? -0.072  29.583 95.179  1.00 38.37  ? 201 GOL C C3  1 
HETATM 1914 O  O3  . GOL J 3 .  ? -1.401  29.379 94.752  1.00 45.74  ? 201 GOL C O3  1 
HETATM 1915 C  C1  . GOL K 3 .  ? -9.829  14.678 92.654  1.00 58.07  ? 202 GOL C C1  1 
HETATM 1916 O  O1  . GOL K 3 .  ? -9.599  13.660 91.707  1.00 75.96  ? 202 GOL C O1  1 
HETATM 1917 C  C2  . GOL K 3 .  ? -10.309 15.922 91.940  1.00 74.12  ? 202 GOL C C2  1 
HETATM 1918 O  O2  . GOL K 3 .  ? -11.591 15.662 91.415  1.00 85.72  ? 202 GOL C O2  1 
HETATM 1919 C  C3  . GOL K 3 .  ? -10.337 17.097 92.903  1.00 50.41  ? 202 GOL C C3  1 
HETATM 1920 O  O3  . GOL K 3 .  ? -10.152 18.277 92.150  1.00 84.62  ? 202 GOL C O3  1 
HETATM 1921 C  C1  . GOL L 3 .  ? -13.005 12.853 106.808 1.00 37.91  ? 203 GOL C C1  1 
HETATM 1922 O  O1  . GOL L 3 .  ? -13.474 11.857 105.936 1.00 52.65  ? 203 GOL C O1  1 
HETATM 1923 C  C2  . GOL L 3 .  ? -13.199 12.474 108.267 1.00 50.15  ? 203 GOL C C2  1 
HETATM 1924 O  O2  . GOL L 3 .  ? -12.903 11.103 108.431 1.00 70.41  ? 203 GOL C O2  1 
HETATM 1925 C  C3  . GOL L 3 .  ? -12.326 13.341 109.172 1.00 51.84  ? 203 GOL C C3  1 
HETATM 1926 O  O3  . GOL L 3 .  ? -13.148 13.968 110.138 1.00 51.28  ? 203 GOL C O3  1 
HETATM 1927 C  C1  . GOL M 3 .  ? -9.409  6.085  107.279 1.00 51.71  ? 204 GOL C C1  1 
HETATM 1928 O  O1  . GOL M 3 .  ? -10.067 7.038  108.089 1.00 51.05  ? 204 GOL C O1  1 
HETATM 1929 C  C2  . GOL M 3 .  ? -7.923  6.386  107.201 1.00 56.24  ? 204 GOL C C2  1 
HETATM 1930 O  O2  . GOL M 3 .  ? -7.269  5.852  108.333 1.00 76.15  ? 204 GOL C O2  1 
HETATM 1931 C  C3  . GOL M 3 .  ? -7.328  5.845  105.909 1.00 55.67  ? 204 GOL C C3  1 
HETATM 1932 O  O3  . GOL M 3 .  ? -6.356  6.768  105.455 1.00 53.45  ? 204 GOL C O3  1 
HETATM 1933 C  C1  . GOL N 3 .  ? 23.751  36.117 136.370 1.00 55.83  ? 201 GOL D C1  1 
HETATM 1934 O  O1  . GOL N 3 .  ? 22.737  37.083 136.194 1.00 57.98  ? 201 GOL D O1  1 
HETATM 1935 C  C2  . GOL N 3 .  ? 24.995  36.496 135.588 1.00 64.56  ? 201 GOL D C2  1 
HETATM 1936 O  O2  . GOL N 3 .  ? 25.395  37.794 135.963 1.00 78.73  ? 201 GOL D O2  1 
HETATM 1937 C  C3  . GOL N 3 .  ? 26.118  35.500 135.839 1.00 66.36  ? 201 GOL D C3  1 
HETATM 1938 O  O3  . GOL N 3 .  ? 27.289  35.986 135.216 1.00 68.78  ? 201 GOL D O3  1 
HETATM 1939 C  C1  . GOL O 3 .  ? 23.862  28.849 135.621 1.00 35.92  ? 202 GOL D C1  1 
HETATM 1940 O  O1  . GOL O 3 .  ? 25.200  29.093 135.993 1.00 74.53  ? 202 GOL D O1  1 
HETATM 1941 C  C2  . GOL O 3 .  ? 22.973  29.064 136.827 1.00 70.60  ? 202 GOL D C2  1 
HETATM 1942 O  O2  . GOL O 3 .  ? 23.731  28.822 137.994 1.00 71.11  ? 202 GOL D O2  1 
HETATM 1943 C  C3  . GOL O 3 .  ? 22.370  30.462 136.823 1.00 52.56  ? 202 GOL D C3  1 
HETATM 1944 O  O3  . GOL O 3 .  ? 23.051  31.252 135.869 1.00 69.78  ? 202 GOL D O3  1 
HETATM 1945 O  O   . HOH P 4 .  ? 4.034   8.217  111.262 1.00 26.02  ? 301 HOH A O   1 
HETATM 1946 O  O   . HOH P 4 .  ? 23.557  15.169 114.017 1.00 28.67  ? 302 HOH A O   1 
HETATM 1947 O  O   . HOH P 4 .  ? 4.195   6.108  120.239 1.00 26.46  ? 303 HOH A O   1 
HETATM 1948 O  O   . HOH P 4 .  ? 12.999  16.729 118.240 1.00 27.89  ? 304 HOH A O   1 
HETATM 1949 O  O   . HOH P 4 .  ? 11.672  9.857  131.242 1.00 37.05  ? 305 HOH A O   1 
HETATM 1950 O  O   . HOH P 4 .  ? -2.180  11.046 114.613 1.00 35.68  ? 306 HOH A O   1 
HETATM 1951 O  O   . HOH P 4 .  ? -4.742  8.936  118.272 1.00 29.93  ? 307 HOH A O   1 
HETATM 1952 O  O   . HOH P 4 .  ? 2.860   23.023 118.038 1.00 28.77  ? 308 HOH A O   1 
HETATM 1953 O  O   . HOH P 4 .  ? 4.934   26.528 121.254 1.00 35.03  ? 309 HOH A O   1 
HETATM 1954 O  O   . HOH P 4 .  ? -11.980 12.524 121.915 1.00 39.66  ? 310 HOH A O   1 
HETATM 1955 O  O   . HOH P 4 .  ? 1.755   4.266  120.740 1.00 46.52  ? 311 HOH A O   1 
HETATM 1956 O  O   . HOH P 4 .  ? -6.307  5.291  124.675 1.00 26.31  ? 312 HOH A O   1 
HETATM 1957 O  O   . HOH P 4 .  ? -2.244  24.210 121.130 1.00 40.03  ? 313 HOH A O   1 
HETATM 1958 O  O   . HOH P 4 .  ? 4.195   3.714  122.843 1.00 28.77  ? 314 HOH A O   1 
HETATM 1959 O  O   . HOH P 4 .  ? 12.092  5.179  122.149 1.00 28.80  ? 315 HOH A O   1 
HETATM 1960 O  O   . HOH P 4 .  ? 22.539  15.812 117.771 1.00 30.61  ? 316 HOH A O   1 
HETATM 1961 O  O   . HOH P 4 .  ? -4.681  10.359 128.531 1.00 31.90  ? 317 HOH A O   1 
HETATM 1962 O  O   . HOH P 4 .  ? -1.851  25.180 123.668 1.00 35.29  ? 318 HOH A O   1 
HETATM 1963 O  O   . HOH P 4 .  ? 3.777   0.824  115.908 1.00 47.61  ? 319 HOH A O   1 
HETATM 1964 O  O   . HOH P 4 .  ? 13.196  4.864  124.710 1.00 31.22  ? 320 HOH A O   1 
HETATM 1965 O  O   . HOH P 4 .  ? 24.835  16.179 116.172 1.00 33.68  ? 321 HOH A O   1 
HETATM 1966 O  O   . HOH P 4 .  ? -5.399  14.577 126.719 1.00 31.45  ? 322 HOH A O   1 
HETATM 1967 O  O   . HOH P 4 .  ? 0.496   4.925  126.337 1.00 32.29  ? 323 HOH A O   1 
HETATM 1968 O  O   . HOH P 4 .  ? 15.876  6.067  118.683 1.00 42.58  ? 324 HOH A O   1 
HETATM 1969 O  O   . HOH P 4 .  ? -2.447  9.601  129.924 1.00 39.90  ? 325 HOH A O   1 
HETATM 1970 O  O   . HOH P 4 .  ? -11.424 11.547 125.147 1.00 37.80  ? 326 HOH A O   1 
HETATM 1971 O  O   . HOH P 4 .  ? 7.723   24.118 114.741 1.00 36.02  ? 327 HOH A O   1 
HETATM 1972 O  O   . HOH P 4 .  ? -3.574  4.935  124.262 1.00 31.81  ? 328 HOH A O   1 
HETATM 1973 O  O   . HOH P 4 .  ? 18.428  15.472 121.573 1.00 36.31  ? 329 HOH A O   1 
HETATM 1974 O  O   . HOH P 4 .  ? 13.699  4.735  119.920 1.00 34.84  ? 330 HOH A O   1 
HETATM 1975 O  O   . HOH P 4 .  ? 10.256  21.033 127.273 1.00 49.11  ? 331 HOH A O   1 
HETATM 1976 O  O   . HOH P 4 .  ? 1.799   3.653  124.219 1.00 38.49  ? 332 HOH A O   1 
HETATM 1977 O  O   . HOH P 4 .  ? -1.061  20.418 127.473 1.00 54.94  ? 333 HOH A O   1 
HETATM 1978 O  O   . HOH P 4 .  ? -1.771  3.763  125.735 1.00 38.52  ? 334 HOH A O   1 
HETATM 1979 O  O   . HOH P 4 .  ? -3.296  21.026 128.368 1.00 50.39  ? 335 HOH A O   1 
HETATM 1980 O  O   . HOH Q 4 .  ? 29.068  18.668 113.681 1.00 45.04  ? 301 HOH B O   1 
HETATM 1981 O  O   . HOH Q 4 .  ? 7.245   30.279 113.321 1.00 55.17  ? 302 HOH B O   1 
HETATM 1982 O  O   . HOH Q 4 .  ? 24.497  21.517 116.380 1.00 38.25  ? 303 HOH B O   1 
HETATM 1983 O  O   . HOH Q 4 .  ? 31.632  23.924 103.839 1.00 43.24  ? 304 HOH B O   1 
HETATM 1984 O  O   . HOH Q 4 .  ? 12.077  32.156 107.397 1.00 37.91  ? 305 HOH B O   1 
HETATM 1985 O  O   . HOH Q 4 .  ? 26.011  20.006 107.115 1.00 31.52  ? 306 HOH B O   1 
HETATM 1986 O  O   . HOH Q 4 .  ? 28.166  11.292 108.586 1.00 32.47  ? 307 HOH B O   1 
HETATM 1987 O  O   . HOH Q 4 .  ? 26.092  30.191 99.451  1.00 45.15  ? 308 HOH B O   1 
HETATM 1988 O  O   . HOH Q 4 .  ? 13.432  13.188 98.182  1.00 42.93  ? 309 HOH B O   1 
HETATM 1989 O  O   . HOH Q 4 .  ? 29.890  30.448 107.779 1.00 31.08  ? 310 HOH B O   1 
HETATM 1990 O  O   . HOH Q 4 .  ? 28.081  19.084 104.376 1.00 39.63  ? 311 HOH B O   1 
HETATM 1991 O  O   . HOH Q 4 .  ? 8.411   5.709  111.282 1.00 27.30  ? 312 HOH B O   1 
HETATM 1992 O  O   . HOH Q 4 .  ? 9.886   6.305  113.625 1.00 22.07  ? 313 HOH B O   1 
HETATM 1993 O  O   . HOH Q 4 .  ? 13.059  16.388 109.857 1.00 27.50  ? 314 HOH B O   1 
HETATM 1994 O  O   . HOH Q 4 .  ? 9.185   29.545 101.606 1.00 46.65  ? 315 HOH B O   1 
HETATM 1995 O  O   . HOH Q 4 .  ? 9.917   7.591  109.885 1.00 30.29  ? 316 HOH B O   1 
HETATM 1996 O  O   . HOH Q 4 .  ? 10.696  12.488 105.801 1.00 48.70  ? 317 HOH B O   1 
HETATM 1997 O  O   . HOH Q 4 .  ? 8.339   22.971 112.372 1.00 29.90  ? 318 HOH B O   1 
HETATM 1998 O  O   . HOH Q 4 .  ? 29.819  31.054 112.503 1.00 40.50  ? 319 HOH B O   1 
HETATM 1999 O  O   . HOH Q 4 .  ? 11.258  28.183 109.446 1.00 30.25  ? 320 HOH B O   1 
HETATM 2000 O  O   . HOH Q 4 .  ? 30.822  28.438 104.320 1.00 23.83  ? 321 HOH B O   1 
HETATM 2001 O  O   . HOH Q 4 .  ? 16.176  35.147 101.662 1.00 35.54  ? 322 HOH B O   1 
HETATM 2002 O  O   . HOH Q 4 .  ? 10.932  22.209 100.323 1.00 42.89  ? 323 HOH B O   1 
HETATM 2003 O  O   . HOH Q 4 .  ? 11.551  20.381 116.239 1.00 29.15  ? 324 HOH B O   1 
HETATM 2004 O  O   . HOH Q 4 .  ? 23.020  32.512 100.951 1.00 41.88  ? 325 HOH B O   1 
HETATM 2005 O  O   . HOH Q 4 .  ? 19.235  15.113 96.192  1.00 41.70  ? 326 HOH B O   1 
HETATM 2006 O  O   . HOH Q 4 .  ? 10.043  19.370 111.328 1.00 25.12  ? 327 HOH B O   1 
HETATM 2007 O  O   . HOH Q 4 .  ? 12.529  17.315 113.689 1.00 20.17  ? 328 HOH B O   1 
HETATM 2008 O  O   . HOH Q 4 .  ? 29.355  38.234 112.051 1.00 42.61  ? 329 HOH B O   1 
HETATM 2009 O  O   . HOH Q 4 .  ? 15.236  31.026 100.872 1.00 38.33  ? 330 HOH B O   1 
HETATM 2010 O  O   . HOH Q 4 .  ? 9.916   26.070 99.862  1.00 44.58  ? 331 HOH B O   1 
HETATM 2011 O  O   . HOH Q 4 .  ? 12.428  10.310 106.497 1.00 38.35  ? 332 HOH B O   1 
HETATM 2012 O  O   . HOH Q 4 .  ? 17.824  10.674 102.858 1.00 46.56  ? 333 HOH B O   1 
HETATM 2013 O  O   . HOH Q 4 .  ? 15.300  8.738  106.105 1.00 54.85  ? 334 HOH B O   1 
HETATM 2014 O  O   . HOH Q 4 .  ? 13.276  29.334 100.021 1.00 42.01  ? 335 HOH B O   1 
HETATM 2015 O  O   . HOH Q 4 .  ? 28.500  22.804 100.816 1.00 36.47  ? 336 HOH B O   1 
HETATM 2016 O  O   . HOH Q 4 .  ? 25.595  28.317 98.051  1.00 44.99  ? 337 HOH B O   1 
HETATM 2017 O  O   . HOH Q 4 .  ? 10.491  16.727 110.503 1.00 28.82  ? 338 HOH B O   1 
HETATM 2018 O  O   . HOH Q 4 .  ? 29.150  21.105 102.807 1.00 43.55  ? 339 HOH B O   1 
HETATM 2019 O  O   . HOH Q 4 .  ? 9.957   23.959 98.293  1.00 44.05  ? 340 HOH B O   1 
HETATM 2020 O  O   . HOH Q 4 .  ? 20.783  32.506 99.452  1.00 56.53  ? 341 HOH B O   1 
HETATM 2021 O  O   . HOH R 4 .  ? -8.889  15.356 113.304 1.00 48.38  ? 301 HOH C O   1 
HETATM 2022 O  O   . HOH R 4 .  ? -14.041 9.013  108.543 1.00 47.26  ? 302 HOH C O   1 
HETATM 2023 O  O   . HOH R 4 .  ? 4.069   25.813 96.802  1.00 43.51  ? 303 HOH C O   1 
HETATM 2024 O  O   . HOH R 4 .  ? 3.722   11.191 103.690 1.00 39.96  ? 304 HOH C O   1 
HETATM 2025 O  O   . HOH R 4 .  ? 1.569   12.111 103.095 1.00 45.50  ? 305 HOH C O   1 
HETATM 2026 O  O   . HOH R 4 .  ? 6.548   21.715 95.700  1.00 25.85  ? 306 HOH C O   1 
HETATM 2027 O  O   . HOH R 4 .  ? -7.413  11.103 93.521  1.00 38.40  ? 307 HOH C O   1 
HETATM 2028 O  O   . HOH R 4 .  ? -11.903 11.801 103.885 1.00 34.33  ? 308 HOH C O   1 
HETATM 2029 O  O   . HOH R 4 .  ? 8.581   9.902  108.347 1.00 47.07  ? 309 HOH C O   1 
HETATM 2030 O  O   . HOH R 4 .  ? -11.209 20.739 112.209 1.00 41.41  ? 310 HOH C O   1 
HETATM 2031 O  O   . HOH R 4 .  ? 5.394   11.291 97.000  1.00 43.91  ? 311 HOH C O   1 
HETATM 2032 O  O   . HOH R 4 .  ? -5.898  13.005 92.037  1.00 45.94  ? 312 HOH C O   1 
HETATM 2033 O  O   . HOH R 4 .  ? -6.626  18.983 115.400 1.00 38.65  ? 313 HOH C O   1 
HETATM 2034 O  O   . HOH R 4 .  ? 0.114   8.276  102.475 1.00 41.78  ? 314 HOH C O   1 
HETATM 2035 O  O   . HOH R 4 .  ? 8.640   16.095 108.483 1.00 25.06  ? 315 HOH C O   1 
HETATM 2036 O  O   . HOH R 4 .  ? 0.657   17.438 97.429  1.00 28.71  ? 316 HOH C O   1 
HETATM 2037 O  O   . HOH R 4 .  ? -1.472  13.385 90.513  1.00 34.59  ? 317 HOH C O   1 
HETATM 2038 O  O   . HOH R 4 .  ? -3.642  10.298 109.281 1.00 29.71  ? 318 HOH C O   1 
HETATM 2039 O  O   . HOH R 4 .  ? -7.410  5.514  99.741  1.00 42.63  ? 319 HOH C O   1 
HETATM 2040 O  O   . HOH R 4 .  ? 2.498   17.570 93.014  1.00 23.65  ? 320 HOH C O   1 
HETATM 2041 O  O   . HOH R 4 .  ? -9.511  10.404 108.859 1.00 41.77  ? 321 HOH C O   1 
HETATM 2042 O  O   . HOH R 4 .  ? -11.741 21.274 99.774  1.00 40.81  ? 322 HOH C O   1 
HETATM 2043 O  O   . HOH R 4 .  ? 6.571   14.124 88.035  1.00 28.95  ? 323 HOH C O   1 
HETATM 2044 O  O   . HOH R 4 .  ? 1.363   26.923 103.866 1.00 38.79  ? 324 HOH C O   1 
HETATM 2045 O  O   . HOH R 4 .  ? -9.427  22.080 111.064 1.00 34.57  ? 325 HOH C O   1 
HETATM 2046 O  O   . HOH R 4 .  ? -1.235  24.004 112.724 1.00 21.70  ? 326 HOH C O   1 
HETATM 2047 O  O   . HOH R 4 .  ? -1.721  18.409 90.570  0.50 32.12  ? 327 HOH C O   1 
HETATM 2048 O  O   . HOH R 4 .  ? -7.544  5.614  102.073 1.00 40.09  ? 328 HOH C O   1 
HETATM 2049 O  O   . HOH R 4 .  ? -14.206 12.725 99.787  1.00 41.46  ? 329 HOH C O   1 
HETATM 2050 O  O   . HOH R 4 .  ? 0.841   7.835  112.691 1.00 26.44  ? 330 HOH C O   1 
HETATM 2051 O  O   . HOH R 4 .  ? 1.437   11.458 89.836  1.00 31.90  ? 331 HOH C O   1 
HETATM 2052 O  O   . HOH R 4 .  ? -0.860  8.554  97.158  1.00 35.99  ? 332 HOH C O   1 
HETATM 2053 O  O   . HOH R 4 .  ? -3.688  25.414 119.383 1.00 41.04  ? 333 HOH C O   1 
HETATM 2054 O  O   . HOH R 4 .  ? 6.658   6.967  108.941 1.00 36.40  ? 334 HOH C O   1 
HETATM 2055 O  O   . HOH R 4 .  ? -3.327  11.842 92.144  1.00 34.93  ? 335 HOH C O   1 
HETATM 2056 O  O   . HOH R 4 .  ? -6.079  24.026 95.538  1.00 44.38  ? 336 HOH C O   1 
HETATM 2057 O  O   . HOH R 4 .  ? 4.938   12.029 100.109 1.00 32.88  ? 337 HOH C O   1 
HETATM 2058 O  O   . HOH R 4 .  ? 9.560   15.722 89.535  1.00 47.10  ? 338 HOH C O   1 
HETATM 2059 O  O   . HOH R 4 .  ? -5.557  8.571  108.684 1.00 50.03  ? 339 HOH C O   1 
HETATM 2060 O  O   . HOH R 4 .  ? -9.542  8.970  96.105  1.00 47.01  ? 340 HOH C O   1 
HETATM 2061 O  O   . HOH R 4 .  ? 8.745   19.852 101.074 1.00 40.61  ? 341 HOH C O   1 
HETATM 2062 O  O   . HOH R 4 .  ? -7.627  19.556 90.897  1.00 51.26  ? 342 HOH C O   1 
HETATM 2063 O  O   . HOH R 4 .  ? 9.704   15.126 105.960 1.00 31.66  ? 343 HOH C O   1 
HETATM 2064 O  O   . HOH R 4 .  ? 3.637   10.580 90.209  1.00 50.44  ? 344 HOH C O   1 
HETATM 2065 O  O   . HOH R 4 .  ? 6.944   13.222 98.533  1.00 58.23  ? 345 HOH C O   1 
HETATM 2066 O  O   . HOH R 4 .  ? -17.017 9.317  100.271 1.00 46.98  ? 346 HOH C O   1 
HETATM 2067 O  O   . HOH R 4 .  ? 11.307  16.462 90.847  1.00 44.22  ? 347 HOH C O   1 
HETATM 2068 O  O   . HOH R 4 .  ? -6.481  26.657 106.524 1.00 45.10  ? 348 HOH C O   1 
HETATM 2069 O  O   . HOH R 4 .  ? -2.807  6.932  96.035  1.00 54.42  ? 349 HOH C O   1 
HETATM 2070 O  O   . HOH R 4 .  ? -0.208  27.283 91.912  1.00 39.24  ? 350 HOH C O   1 
HETATM 2071 O  O   . HOH R 4 .  ? 7.649   24.139 96.723  1.00 51.76  ? 351 HOH C O   1 
HETATM 2072 O  O   . HOH R 4 .  ? -3.694  16.272 89.441  1.00 56.75  ? 352 HOH C O   1 
HETATM 2073 O  O   . HOH S 4 .  ? 15.458  20.101 118.885 1.00 36.21  ? 301 HOH D O   1 
HETATM 2074 O  O   . HOH S 4 .  ? 25.293  25.765 130.481 1.00 43.26  ? 302 HOH D O   1 
HETATM 2075 O  O   . HOH S 4 .  ? 13.088  26.577 134.888 1.00 46.06  ? 303 HOH D O   1 
HETATM 2076 O  O   . HOH S 4 .  ? 21.070  43.002 119.626 1.00 33.55  ? 304 HOH D O   1 
HETATM 2077 O  O   . HOH S 4 .  ? 4.930   24.664 124.591 1.00 44.00  ? 305 HOH D O   1 
HETATM 2078 O  O   . HOH S 4 .  ? 25.139  29.581 139.927 1.00 48.37  ? 306 HOH D O   1 
HETATM 2079 O  O   . HOH S 4 .  ? 25.679  29.303 118.394 1.00 32.33  ? 307 HOH D O   1 
HETATM 2080 O  O   . HOH S 4 .  ? 12.569  22.796 127.742 1.00 37.86  ? 308 HOH D O   1 
HETATM 2081 O  O   . HOH S 4 .  ? 23.299  35.999 114.405 1.00 52.99  ? 309 HOH D O   1 
HETATM 2082 O  O   . HOH S 4 .  ? 10.636  20.282 130.177 1.00 47.74  ? 310 HOH D O   1 
HETATM 2083 O  O   . HOH S 4 .  ? 25.478  39.278 118.052 1.00 35.57  ? 311 HOH D O   1 
HETATM 2084 O  O   . HOH S 4 .  ? 22.309  24.577 124.107 1.00 45.83  ? 312 HOH D O   1 
HETATM 2085 O  O   . HOH S 4 .  ? 30.847  30.896 128.649 1.00 51.26  ? 313 HOH D O   1 
HETATM 2086 O  O   . HOH S 4 .  ? 16.414  25.023 134.297 1.00 44.69  ? 314 HOH D O   1 
HETATM 2087 O  O   . HOH S 4 .  ? 25.685  32.626 134.274 1.00 45.62  ? 315 HOH D O   1 
HETATM 2088 O  O   . HOH S 4 .  ? 18.037  40.532 127.881 1.00 30.44  ? 316 HOH D O   1 
HETATM 2089 O  O   . HOH S 4 .  ? 16.900  39.050 116.805 1.00 31.37  ? 317 HOH D O   1 
HETATM 2090 O  O   . HOH S 4 .  ? 20.590  21.682 127.095 1.00 47.93  ? 318 HOH D O   1 
HETATM 2091 O  O   . HOH S 4 .  ? 13.107  34.340 107.959 1.00 39.41  ? 319 HOH D O   1 
HETATM 2092 O  O   . HOH S 4 .  ? 19.934  37.755 113.841 1.00 41.19  ? 320 HOH D O   1 
HETATM 2093 O  O   . HOH S 4 .  ? 18.008  17.387 123.528 1.00 45.69  ? 321 HOH D O   1 
HETATM 2094 O  O   . HOH S 4 .  ? 20.135  18.711 141.681 1.00 49.45  ? 322 HOH D O   1 
HETATM 2095 O  O   . HOH S 4 .  ? 11.977  32.360 114.774 1.00 24.76  ? 323 HOH D O   1 
HETATM 2096 O  O   . HOH S 4 .  ? 24.881  41.787 130.055 1.00 43.00  ? 324 HOH D O   1 
HETATM 2097 O  O   . HOH S 4 .  ? 15.217  39.650 125.860 1.00 34.89  ? 325 HOH D O   1 
HETATM 2098 O  O   . HOH S 4 .  ? 27.313  39.530 127.862 1.00 41.82  ? 326 HOH D O   1 
HETATM 2099 O  O   . HOH S 4 .  ? 14.719  17.695 141.781 1.00 44.13  ? 327 HOH D O   1 
HETATM 2100 O  O   . HOH S 4 .  ? 27.195  37.238 124.162 1.00 36.26  ? 328 HOH D O   1 
HETATM 2101 O  O   . HOH S 4 .  ? 15.943  18.901 122.311 1.00 34.67  ? 329 HOH D O   1 
HETATM 2102 O  O   . HOH S 4 .  ? 17.275  37.483 113.730 1.00 30.23  ? 330 HOH D O   1 
HETATM 2103 O  O   . HOH S 4 .  ? 28.152  33.924 132.241 1.00 43.10  ? 331 HOH D O   1 
HETATM 2104 O  O   . HOH S 4 .  ? 26.914  37.693 119.270 1.00 38.51  ? 332 HOH D O   1 
HETATM 2105 O  O   . HOH S 4 .  ? 23.531  43.946 128.911 1.00 37.55  ? 333 HOH D O   1 
HETATM 2106 O  O   . HOH S 4 .  ? 19.623  42.781 127.978 1.00 36.40  ? 334 HOH D O   1 
HETATM 2107 O  O   . HOH S 4 .  ? 5.707   29.097 129.601 1.00 56.19  ? 335 HOH D 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   . GLY A 1  ? 0.2862 0.3079 0.4728 0.0559  -0.0609 0.0635  85  GLY A N   
2    C  CA  . GLY A 1  ? 0.2797 0.3174 0.4714 0.0491  -0.0361 0.0666  85  GLY A CA  
3    C  C   . GLY A 1  ? 0.2469 0.3175 0.4660 -0.0228 -0.0152 0.0574  85  GLY A C   
4    O  O   . GLY A 1  ? 0.2467 0.2795 0.4615 0.0011  -0.0189 0.0583  85  GLY A O   
5    N  N   . VAL A 2  ? 0.3021 0.2905 0.4703 0.0201  -0.0217 0.0361  86  VAL A N   
6    C  CA  . VAL A 2  ? 0.2370 0.3194 0.4673 -0.0546 -0.0441 -0.0151 86  VAL A CA  
7    C  C   . VAL A 2  ? 0.2456 0.3430 0.4490 -0.0261 -0.0527 0.0190  86  VAL A C   
8    O  O   . VAL A 2  ? 0.3254 0.3952 0.4562 -0.0276 -0.0272 0.0533  86  VAL A O   
9    C  CB  . VAL A 2  ? 0.3201 0.4010 0.4774 -0.0024 -0.0616 -0.0403 86  VAL A CB  
10   C  CG1 . VAL A 2  ? 0.4754 0.4856 0.4857 0.0285  -0.0664 -0.0602 86  VAL A CG1 
11   C  CG2 . VAL A 2  ? 0.2484 0.4570 0.4753 -0.0042 -0.0658 -0.0509 86  VAL A CG2 
12   N  N   A THR A 3  ? 0.2127 0.3086 0.4394 -0.0330 -0.0454 0.0180  87  THR A N   
13   N  N   B THR A 3  ? 0.2548 0.2912 0.4392 -0.0365 -0.0361 0.0130  87  THR A N   
14   C  CA  A THR A 3  ? 0.2434 0.3300 0.4266 -0.0327 -0.0584 0.0107  87  THR A CA  
15   C  CA  B THR A 3  ? 0.3026 0.3227 0.4259 -0.0568 -0.0370 0.0011  87  THR A CA  
16   C  C   A THR A 3  ? 0.2587 0.2964 0.4120 -0.0284 -0.0579 0.0273  87  THR A C   
17   C  C   B THR A 3  ? 0.2786 0.3008 0.4101 -0.0393 -0.0413 0.0203  87  THR A C   
18   O  O   A THR A 3  ? 0.2670 0.2677 0.4076 -0.0054 -0.0815 0.0250  87  THR A O   
19   O  O   B THR A 3  ? 0.2522 0.2904 0.4020 -0.0253 -0.0609 0.0054  87  THR A O   
20   C  CB  A THR A 3  ? 0.3069 0.4037 0.4299 -0.0819 -0.0477 0.0146  87  THR A CB  
21   C  CB  B THR A 3  ? 0.4019 0.3962 0.4301 -0.1494 -0.0070 0.0132  87  THR A CB  
22   O  OG1 A THR A 3  ? 0.3257 0.3832 0.4282 -0.0694 -0.0507 0.0232  87  THR A OG1 
23   O  OG1 B THR A 3  ? 0.4198 0.4582 0.4308 -0.1715 0.0103  0.0428  87  THR A OG1 
24   C  CG2 A THR A 3  ? 0.3364 0.4268 0.4297 -0.1183 -0.0519 0.0057  87  THR A CG2 
25   C  CG2 B THR A 3  ? 0.4829 0.3579 0.4297 -0.1412 0.0034  -0.0012 87  THR A CG2 
26   N  N   . THR A 4  ? 0.3224 0.3369 0.4031 -0.0311 -0.0312 0.0306  88  THR A N   
27   C  CA  . THR A 4  ? 0.3314 0.3995 0.3913 -0.0698 -0.0408 0.0104  88  THR A CA  
28   C  C   . THR A 4  ? 0.2958 0.3774 0.3792 -0.1188 -0.0655 0.0309  88  THR A C   
29   O  O   . THR A 4  ? 0.3422 0.3519 0.3921 -0.0599 -0.0578 0.0242  88  THR A O   
30   C  CB  . THR A 4  ? 0.4025 0.3464 0.3948 -0.0250 -0.0167 0.0037  88  THR A CB  
31   O  OG1 . THR A 4  ? 0.4029 0.3715 0.4106 0.0289  -0.0359 0.0181  88  THR A OG1 
32   C  CG2 . THR A 4  ? 0.4736 0.4189 0.3931 -0.0338 0.0001  -0.0028 88  THR A CG2 
33   N  N   . PHE A 5  ? 0.2704 0.3785 0.3705 -0.0791 -0.0728 0.0160  89  PHE A N   
34   C  CA  . PHE A 5  ? 0.3004 0.4094 0.3663 -0.0417 -0.0611 0.0188  89  PHE A CA  
35   C  C   . PHE A 5  ? 0.3388 0.4025 0.3418 0.0170  -0.0454 0.0301  89  PHE A C   
36   O  O   . PHE A 5  ? 0.3291 0.4094 0.3164 -0.0229 -0.0032 0.0152  89  PHE A O   
37   C  CB  . PHE A 5  ? 0.3130 0.3223 0.3893 -0.0890 -0.0723 0.0317  89  PHE A CB  
38   C  CG  . PHE A 5  ? 0.3023 0.2962 0.4114 -0.0329 -0.0588 0.0103  89  PHE A CG  
39   C  CD1 . PHE A 5  ? 0.3200 0.3398 0.4261 -0.0199 -0.0360 0.0398  89  PHE A CD1 
40   C  CD2 . PHE A 5  ? 0.3397 0.3968 0.4228 0.0452  -0.0714 0.0071  89  PHE A CD2 
41   C  CE1 . PHE A 5  ? 0.3703 0.3404 0.4334 -0.0372 -0.0357 0.0182  89  PHE A CE1 
42   C  CE2 . PHE A 5  ? 0.3280 0.4204 0.4291 0.0263  -0.0594 0.0259  89  PHE A CE2 
43   C  CZ  . PHE A 5  ? 0.3217 0.3445 0.4326 -0.0820 -0.0433 0.0073  89  PHE A CZ  
44   N  N   . VAL A 6  ? 0.3227 0.3375 0.3364 -0.0251 -0.0397 0.0438  90  VAL A N   
45   C  CA  . VAL A 6  ? 0.3100 0.4053 0.3354 0.0338  -0.0415 0.0565  90  VAL A CA  
46   C  C   . VAL A 6  ? 0.3088 0.3365 0.3339 0.0324  -0.0408 0.0316  90  VAL A C   
47   O  O   . VAL A 6  ? 0.4079 0.3893 0.3441 0.0524  -0.0542 -0.0196 90  VAL A O   
48   C  CB  . VAL A 6  ? 0.4019 0.4662 0.3414 0.0731  -0.0343 0.0574  90  VAL A CB  
49   C  CG1 . VAL A 6  ? 0.4478 0.5300 0.3454 0.0694  -0.0675 0.0238  90  VAL A CG1 
50   C  CG2 . VAL A 6  ? 0.3776 0.4004 0.3471 0.0775  -0.0251 0.0594  90  VAL A CG2 
51   N  N   . ALA A 7  ? 0.2804 0.3262 0.3187 0.0586  -0.0388 0.0289  91  ALA A N   
52   C  CA  . ALA A 7  ? 0.2696 0.2969 0.2999 0.0299  -0.0393 0.0006  91  ALA A CA  
53   C  C   . ALA A 7  ? 0.3452 0.3575 0.2903 0.0540  -0.0308 0.0079  91  ALA A C   
54   O  O   . ALA A 7  ? 0.3743 0.3675 0.2891 0.0481  -0.0022 0.0157  91  ALA A O   
55   C  CB  . ALA A 7  ? 0.3348 0.2916 0.3099 0.0238  -0.0194 0.0006  91  ALA A CB  
56   N  N   . LEU A 8  ? 0.4250 0.3682 0.2770 0.1217  -0.0162 -0.0250 92  LEU A N   
57   C  CA  . LEU A 8  ? 0.4484 0.3553 0.2867 0.1473  -0.0226 0.0017  92  LEU A CA  
58   C  C   . LEU A 8  ? 0.4061 0.4464 0.2892 0.1279  -0.0224 -0.0064 92  LEU A C   
59   O  O   . LEU A 8  ? 0.3768 0.5460 0.2875 0.1710  -0.0032 -0.0096 92  LEU A O   
60   C  CB  . LEU A 8  ? 0.5175 0.4102 0.3093 0.1127  -0.0502 -0.0337 92  LEU A CB  
61   C  CG  . LEU A 8  ? 0.5145 0.3832 0.3293 0.0597  -0.0489 -0.0398 92  LEU A CG  
62   C  CD1 . LEU A 8  ? 0.5839 0.4100 0.3385 0.0978  -0.0532 -0.0717 92  LEU A CD1 
63   C  CD2 . LEU A 8  ? 0.5892 0.5510 0.3425 0.0893  -0.0576 -0.0149 92  LEU A CD2 
64   N  N   . TYR A 9  ? 0.3545 0.4895 0.2945 0.1187  -0.0106 0.0112  93  TYR A N   
65   C  CA  . TYR A 9  ? 0.3697 0.4987 0.2911 0.1368  -0.0264 -0.0297 93  TYR A CA  
66   C  C   . TYR A 9  ? 0.3186 0.4087 0.2806 0.0462  -0.0238 -0.0344 93  TYR A C   
67   O  O   . TYR A 9  ? 0.3716 0.3773 0.2796 0.0591  0.0132  0.0319  93  TYR A O   
68   C  CB  . TYR A 9  ? 0.4272 0.5861 0.3030 0.1809  -0.0508 -0.0763 93  TYR A CB  
69   C  CG  . TYR A 9  ? 0.4062 0.6580 0.3225 0.1505  -0.0635 -0.1409 93  TYR A CG  
70   C  CD1 . TYR A 9  ? 0.4336 0.7480 0.3330 0.2677  -0.0868 -0.1446 93  TYR A CD1 
71   C  CD2 . TYR A 9  ? 0.4712 0.6822 0.3323 0.1989  -0.0558 -0.1641 93  TYR A CD2 
72   C  CE1 . TYR A 9  ? 0.5177 0.7412 0.3435 0.2926  -0.1086 -0.1913 93  TYR A CE1 
73   C  CE2 . TYR A 9  ? 0.4983 0.7434 0.3443 0.1515  -0.1026 -0.2033 93  TYR A CE2 
74   C  CZ  . TYR A 9  ? 0.5700 0.8072 0.3526 0.2139  -0.1041 -0.2065 93  TYR A CZ  
75   O  OH  . TYR A 9  ? 0.6210 0.8515 0.3697 0.1928  -0.0907 -0.2189 93  TYR A OH  
76   N  N   . ASP A 10 ? 0.3105 0.3907 0.2762 0.0523  -0.0428 -0.0470 94  ASP A N   
77   C  CA  . ASP A 10 ? 0.3324 0.3519 0.2977 0.0664  0.0104  0.0276  94  ASP A CA  
78   C  C   . ASP A 10 ? 0.3239 0.3443 0.2999 0.1024  0.0200  0.0272  94  ASP A C   
79   O  O   . ASP A 10 ? 0.3526 0.3998 0.3088 0.1236  0.0042  0.0205  94  ASP A O   
80   C  CB  . ASP A 10 ? 0.3979 0.4045 0.3249 0.0732  0.0577  0.0686  94  ASP A CB  
81   C  CG  . ASP A 10 ? 0.4926 0.4407 0.3489 0.1487  0.0832  0.1096  94  ASP A CG  
82   O  OD1 . ASP A 10 ? 0.4117 0.4478 0.3579 0.1233  0.0880  0.0850  94  ASP A OD1 
83   O  OD2 . ASP A 10 ? 0.5726 0.5135 0.3733 0.1653  0.0928  0.1112  94  ASP A OD2 
84   N  N   . TYR A 11 ? 0.2890 0.3461 0.3008 0.0583  0.0093  0.0357  95  TYR A N   
85   C  CA  . TYR A 11 ? 0.3015 0.2546 0.2981 0.0229  0.0208  0.0168  95  TYR A CA  
86   C  C   . TYR A 11 ? 0.2838 0.2644 0.3052 -0.0024 0.0400  0.0188  95  TYR A C   
87   O  O   . TYR A 11 ? 0.3192 0.3384 0.2918 0.0768  0.0363  -0.0073 95  TYR A O   
88   C  CB  . TYR A 11 ? 0.3039 0.2423 0.3014 -0.0008 0.0394  0.0284  95  TYR A CB  
89   C  CG  . TYR A 11 ? 0.2952 0.2627 0.3027 0.0861  0.0409  0.0136  95  TYR A CG  
90   C  CD1 . TYR A 11 ? 0.2790 0.3537 0.3077 0.0904  0.0578  0.0239  95  TYR A CD1 
91   C  CD2 . TYR A 11 ? 0.3191 0.2296 0.3033 0.0106  0.0440  0.0533  95  TYR A CD2 
92   C  CE1 . TYR A 11 ? 0.2617 0.3357 0.3194 0.0671  0.0468  0.0133  95  TYR A CE1 
93   C  CE2 . TYR A 11 ? 0.2916 0.2124 0.3157 0.0481  0.0512  0.0407  95  TYR A CE2 
94   C  CZ  . TYR A 11 ? 0.2394 0.2515 0.3283 -0.0021 0.0155  0.0299  95  TYR A CZ  
95   O  OH  . TYR A 11 ? 0.2836 0.2758 0.3512 0.0324  0.0068  0.0247  95  TYR A OH  
96   N  N   . GLU A 12 ? 0.3112 0.2532 0.3256 -0.0173 0.0468  0.0032  96  GLU A N   
97   C  CA  . GLU A 12 ? 0.2875 0.2948 0.3516 0.0108  0.0259  0.0215  96  GLU A CA  
98   C  C   . GLU A 12 ? 0.2890 0.2389 0.3486 0.0294  -0.0042 0.0112  96  GLU A C   
99   O  O   . GLU A 12 ? 0.3617 0.2554 0.3572 0.0405  0.0275  0.0199  96  GLU A O   
100  C  CB  . GLU A 12 ? 0.3632 0.3019 0.3813 -0.0211 0.0479  0.0703  96  GLU A CB  
101  C  CG  . GLU A 12 ? 0.5915 0.4382 0.4153 0.0395  0.0488  0.0898  96  GLU A CG  
102  C  CD  . GLU A 12 ? 0.7554 0.6758 0.4516 0.1809  0.0456  0.0562  96  GLU A CD  
103  O  OE1 . GLU A 12 ? 0.8143 0.8062 0.4627 0.1976  0.0423  0.0566  96  GLU A OE1 
104  O  OE2 . GLU A 12 ? 0.7735 0.7502 0.4700 0.2582  0.0335  0.0512  96  GLU A OE2 
105  N  N   . SER A 13 ? 0.2265 0.3762 0.3499 0.0028  -0.0170 0.0045  97  SER A N   
106  C  CA  . SER A 13 ? 0.2791 0.3151 0.3582 0.0583  -0.0309 -0.0007 97  SER A CA  
107  C  C   . SER A 13 ? 0.2815 0.2495 0.3692 0.0501  -0.0143 0.0271  97  SER A C   
108  O  O   . SER A 13 ? 0.3402 0.2829 0.3690 0.0227  0.0021  0.0322  97  SER A O   
109  C  CB  . SER A 13 ? 0.3483 0.3241 0.3585 0.0673  -0.0335 0.0053  97  SER A CB  
110  O  OG  . SER A 13 ? 0.3664 0.2871 0.3610 0.0491  -0.0144 0.0322  97  SER A OG  
111  N  N   . ARG A 14 ? 0.2536 0.2574 0.3838 0.0523  0.0343  0.0291  98  ARG A N   
112  C  CA  . ARG A 14 ? 0.2541 0.3465 0.3914 0.0442  0.0266  0.0256  98  ARG A CA  
113  C  C   . ARG A 14 ? 0.2230 0.2846 0.3990 -0.0910 0.0403  0.0709  98  ARG A C   
114  O  O   . ARG A 14 ? 0.2544 0.3323 0.3946 -0.0134 0.0650  0.0728  98  ARG A O   
115  C  CB  . ARG A 14 ? 0.2906 0.2984 0.3969 0.0159  0.0557  0.0280  98  ARG A CB  
116  C  CG  . ARG A 14 ? 0.2949 0.3326 0.3990 0.0231  0.0500  0.0546  98  ARG A CG  
117  C  CD  . ARG A 14 ? 0.3894 0.2843 0.4035 0.0724  0.0334  0.0177  98  ARG A CD  
118  N  NE  . ARG A 14 ? 0.4312 0.2812 0.4049 0.0563  0.0324  0.0054  98  ARG A NE  
119  C  CZ  . ARG A 14 ? 0.4184 0.3279 0.4006 0.0428  0.0445  0.0137  98  ARG A CZ  
120  N  NH1 . ARG A 14 ? 0.3758 0.4907 0.4034 0.0153  0.0438  0.0290  98  ARG A NH1 
121  N  NH2 . ARG A 14 ? 0.4013 0.3686 0.3965 0.0139  0.0443  -0.0319 98  ARG A NH2 
122  N  N   . THR A 15 ? 0.2384 0.2403 0.4003 -0.0191 0.0529  0.0968  99  THR A N   
123  C  CA  . THR A 15 ? 0.2685 0.2423 0.4071 0.0432  0.0390  0.0706  99  THR A CA  
124  C  C   . THR A 15 ? 0.1833 0.2477 0.4112 -0.0241 0.0287  0.0685  99  THR A C   
125  O  O   . THR A 15 ? 0.2552 0.2398 0.4171 -0.0149 0.0341  0.0222  99  THR A O   
126  C  CB  . THR A 15 ? 0.2795 0.1944 0.4063 0.0122  0.0703  0.0305  99  THR A CB  
127  O  OG1 . THR A 15 ? 0.3037 0.2534 0.4059 -0.0274 0.0828  0.0158  99  THR A OG1 
128  C  CG2 . THR A 15 ? 0.2493 0.2472 0.4011 0.0266  0.0831  0.0205  99  THR A CG2 
129  N  N   . GLU A 16 ? 0.2194 0.2862 0.4088 -0.0554 0.0205  0.0625  100 GLU A N   
130  C  CA  . GLU A 16 ? 0.2198 0.2714 0.4166 -0.0915 -0.0070 -0.0022 100 GLU A CA  
131  C  C   . GLU A 16 ? 0.2770 0.1993 0.3915 -0.0430 0.0175  0.0084  100 GLU A C   
132  O  O   . GLU A 16 ? 0.3572 0.2755 0.3970 -0.0251 0.0148  -0.0317 100 GLU A O   
133  C  CB  . GLU A 16 ? 0.2003 0.3228 0.4373 -0.0919 0.0094  0.0215  100 GLU A CB  
134  C  CG  . GLU A 16 ? 0.3583 0.3851 0.4663 -0.1086 -0.0030 0.0112  100 GLU A CG  
135  C  CD  . GLU A 16 ? 0.5043 0.6466 0.4911 -0.0362 -0.0082 0.0085  100 GLU A CD  
136  O  OE1 . GLU A 16 ? 0.6280 0.7388 0.5001 0.0074  -0.0128 -0.0034 100 GLU A OE1 
137  O  OE2 . GLU A 16 ? 0.4553 0.7091 0.5051 -0.0107 -0.0196 0.0018  100 GLU A OE2 
138  N  N   . THR A 17 ? 0.2002 0.2053 0.3615 -0.0455 -0.0085 0.0168  101 THR A N   
139  C  CA  . THR A 17 ? 0.1864 0.1875 0.3492 0.0089  -0.0075 0.0059  101 THR A CA  
140  C  C   . THR A 17 ? 0.2255 0.2072 0.3456 0.0100  0.0035  -0.0103 101 THR A C   
141  O  O   . THR A 17 ? 0.2154 0.2331 0.3410 0.0125  0.0048  0.0103  101 THR A O   
142  C  CB  . THR A 17 ? 0.2288 0.2342 0.3454 0.0296  -0.0030 -0.0044 101 THR A CB  
143  O  OG1 . THR A 17 ? 0.2136 0.2323 0.3468 -0.0085 0.0537  0.0137  101 THR A OG1 
144  C  CG2 . THR A 17 ? 0.2433 0.2835 0.3502 -0.0124 -0.0220 -0.0049 101 THR A CG2 
145  N  N   . ASP A 18 ? 0.2307 0.1778 0.3411 0.0012  0.0152  -0.0146 102 ASP A N   
146  C  CA  . ASP A 18 ? 0.2382 0.2175 0.3448 0.0264  0.0322  0.0201  102 ASP A CA  
147  C  C   . ASP A 18 ? 0.2300 0.1947 0.3452 0.0300  0.0205  -0.0093 102 ASP A C   
148  O  O   . ASP A 18 ? 0.2475 0.2177 0.3662 0.0015  0.0089  -0.0462 102 ASP A O   
149  C  CB  . ASP A 18 ? 0.2165 0.2149 0.3485 -0.0056 0.0414  0.0330  102 ASP A CB  
150  C  CG  . ASP A 18 ? 0.2750 0.2340 0.3399 -0.0518 0.0131  0.0002  102 ASP A CG  
151  O  OD1 . ASP A 18 ? 0.3193 0.3006 0.3379 -0.0580 0.0108  -0.0227 102 ASP A OD1 
152  O  OD2 . ASP A 18 ? 0.2880 0.2820 0.3384 -0.0014 0.0235  0.0333  102 ASP A OD2 
153  N  N   . LEU A 19 ? 0.2033 0.2106 0.3327 -0.0004 0.0245  0.0196  103 LEU A N   
154  C  CA  . LEU A 19 ? 0.2020 0.2121 0.3271 0.0343  0.0257  0.0281  103 LEU A CA  
155  C  C   . LEU A 19 ? 0.2523 0.1670 0.3278 0.0455  0.0051  0.0247  103 LEU A C   
156  O  O   . LEU A 19 ? 0.2790 0.2146 0.3142 0.0340  0.0396  -0.0003 103 LEU A O   
157  C  CB  . LEU A 19 ? 0.1874 0.2381 0.3272 0.0373  0.0095  -0.0027 103 LEU A CB  
158  C  CG  . LEU A 19 ? 0.1930 0.2344 0.3300 0.0281  0.0169  -0.0086 103 LEU A CG  
159  C  CD1 . LEU A 19 ? 0.2668 0.2426 0.3403 0.0528  0.0229  -0.0314 103 LEU A CD1 
160  C  CD2 . LEU A 19 ? 0.1969 0.2564 0.3367 0.0144  0.0258  0.0066  103 LEU A CD2 
161  N  N   . SER A 20 ? 0.2333 0.1968 0.3313 0.0331  0.0162  0.0524  104 SER A N   
162  C  CA  . SER A 20 ? 0.2447 0.2093 0.3350 0.0123  0.0298  0.0661  104 SER A CA  
163  C  C   . SER A 20 ? 0.2713 0.2606 0.3192 0.0425  0.0278  0.0375  104 SER A C   
164  O  O   . SER A 20 ? 0.2715 0.2855 0.3069 0.0255  0.0347  0.0329  104 SER A O   
165  C  CB  . SER A 20 ? 0.3698 0.2087 0.3591 0.0256  0.0257  -0.0092 104 SER A CB  
166  O  OG  . SER A 20 ? 0.3685 0.3038 0.3811 -0.0228 0.0158  -0.0279 104 SER A OG  
167  N  N   . PHE A 21 ? 0.2340 0.2340 0.3142 0.0233  0.0021  0.0273  105 PHE A N   
168  C  CA  . PHE A 21 ? 0.2436 0.2846 0.3067 0.0528  0.0137  0.0363  105 PHE A CA  
169  C  C   . PHE A 21 ? 0.2596 0.2913 0.2986 0.0749  0.0406  0.0529  105 PHE A C   
170  O  O   . PHE A 21 ? 0.2642 0.3566 0.2971 0.0804  0.0542  0.0495  105 PHE A O   
171  C  CB  . PHE A 21 ? 0.3008 0.2000 0.3112 0.0254  0.0142  0.0095  105 PHE A CB  
172  C  CG  . PHE A 21 ? 0.2684 0.2491 0.3015 0.0307  0.0183  0.0370  105 PHE A CG  
173  C  CD1 . PHE A 21 ? 0.2604 0.3104 0.2984 -0.0019 0.0177  0.0277  105 PHE A CD1 
174  C  CD2 . PHE A 21 ? 0.2413 0.2390 0.2989 0.0488  0.0234  0.0451  105 PHE A CD2 
175  C  CE1 . PHE A 21 ? 0.3191 0.3151 0.2970 0.0228  0.0040  0.0145  105 PHE A CE1 
176  C  CE2 . PHE A 21 ? 0.2768 0.2353 0.2884 0.0117  0.0112  -0.0053 105 PHE A CE2 
177  C  CZ  . PHE A 21 ? 0.2857 0.3155 0.2905 0.0150  -0.0398 -0.0082 105 PHE A CZ  
178  N  N   . LYS A 22 ? 0.2700 0.3275 0.2898 0.0888  0.0026  0.0627  106 LYS A N   
179  C  CA  . LYS A 22 ? 0.3010 0.3082 0.3112 0.0794  -0.0011 0.0444  106 LYS A CA  
180  C  C   . LYS A 22 ? 0.3529 0.2640 0.3062 0.0418  0.0164  0.0455  106 LYS A C   
181  O  O   . LYS A 22 ? 0.3736 0.3235 0.3072 0.0783  0.0286  0.0592  106 LYS A O   
182  C  CB  . LYS A 22 ? 0.3534 0.2789 0.3461 0.0825  0.0219  0.0456  106 LYS A CB  
183  C  CG  . LYS A 22 ? 0.3998 0.3647 0.3779 0.1154  0.0726  0.0241  106 LYS A CG  
184  C  CD  . LYS A 22 ? 0.4591 0.4701 0.4018 0.0978  0.0854  0.0111  106 LYS A CD  
185  C  CE  . LYS A 22 ? 0.5908 0.6364 0.4202 0.1489  0.1034  -0.0090 106 LYS A CE  
186  N  NZ  . LYS A 22 ? 0.7022 0.7249 0.4326 0.2007  0.1103  -0.0189 106 LYS A NZ  
187  N  N   . LYS A 23 ? 0.3740 0.3406 0.3003 0.1205  0.0480  0.0440  107 LYS A N   
188  C  CA  . LYS A 23 ? 0.3138 0.3986 0.3069 0.1023  0.0366  0.0497  107 LYS A CA  
189  C  C   . LYS A 23 ? 0.3552 0.4151 0.3123 0.1290  0.0231  0.0638  107 LYS A C   
190  O  O   . LYS A 23 ? 0.4012 0.4043 0.3127 0.1036  0.0004  0.0781  107 LYS A O   
191  C  CB  . LYS A 23 ? 0.3943 0.4727 0.3175 0.1252  0.0410  0.0664  107 LYS A CB  
192  C  CG  . LYS A 23 ? 0.4261 0.5409 0.3325 0.1598  0.0241  0.0536  107 LYS A CG  
193  C  CD  . LYS A 23 ? 0.5833 0.6276 0.3573 0.1639  -0.0207 0.0419  107 LYS A CD  
194  C  CE  . LYS A 23 ? 0.6882 0.7139 0.3762 0.2229  -0.0504 0.0440  107 LYS A CE  
195  N  NZ  . LYS A 23 ? 0.7084 0.7337 0.3864 0.2437  -0.0640 0.0449  107 LYS A NZ  
196  N  N   . GLY A 24 ? 0.2851 0.3728 0.3120 0.0664  0.0215  0.0729  108 GLY A N   
197  C  CA  . GLY A 24 ? 0.2860 0.3958 0.3185 0.1054  -0.0032 0.0638  108 GLY A CA  
198  C  C   . GLY A 24 ? 0.2827 0.3226 0.3196 0.0657  -0.0055 0.0405  108 GLY A C   
199  O  O   . GLY A 24 ? 0.2853 0.4011 0.3325 0.0824  -0.0079 0.0475  108 GLY A O   
200  N  N   . GLU A 25 ? 0.3283 0.3175 0.3074 0.0979  -0.0214 0.0330  109 GLU A N   
201  C  CA  . GLU A 25 ? 0.2727 0.3412 0.3006 0.0310  -0.0005 0.0390  109 GLU A CA  
202  C  C   . GLU A 25 ? 0.2706 0.3279 0.3045 0.0892  0.0149  0.0295  109 GLU A C   
203  O  O   . GLU A 25 ? 0.3116 0.3157 0.2976 0.0560  0.0044  0.0265  109 GLU A O   
204  C  CB  . GLU A 25 ? 0.2953 0.3668 0.2986 0.0536  0.0020  -0.0120 109 GLU A CB  
205  C  CG  . GLU A 25 ? 0.2649 0.3976 0.3034 0.0725  0.0176  -0.0096 109 GLU A CG  
206  C  CD  . GLU A 25 ? 0.2606 0.3517 0.3064 0.0832  0.0213  0.0217  109 GLU A CD  
207  O  OE1 . GLU A 25 ? 0.2998 0.3368 0.3042 0.0318  0.0414  0.0149  109 GLU A OE1 
208  O  OE2 . GLU A 25 ? 0.3105 0.2942 0.3150 0.0601  -0.0024 0.0091  109 GLU A OE2 
209  N  N   . ARG A 26 ? 0.2722 0.3471 0.3112 0.0860  0.0157  0.0022  110 ARG A N   
210  C  CA  . ARG A 26 ? 0.2278 0.2924 0.3168 0.0577  0.0011  -0.0029 110 ARG A CA  
211  C  C   . ARG A 26 ? 0.2630 0.3069 0.2997 0.0771  -0.0085 -0.0057 110 ARG A C   
212  O  O   . ARG A 26 ? 0.2882 0.3140 0.2988 0.0380  0.0082  -0.0090 110 ARG A O   
213  C  CB  . ARG A 26 ? 0.2873 0.4409 0.3431 0.1465  -0.0278 -0.0520 110 ARG A CB  
214  C  CG  . ARG A 26 ? 0.3708 0.6214 0.3768 0.2115  -0.0343 -0.0343 110 ARG A CG  
215  C  CD  . ARG A 26 ? 0.4749 0.7146 0.4056 0.2247  -0.0199 -0.0048 110 ARG A CD  
216  N  NE  . ARG A 26 ? 0.6156 0.7822 0.4357 0.1117  -0.0088 0.0191  110 ARG A NE  
217  C  CZ  . ARG A 26 ? 0.7030 0.8111 0.4519 0.1496  -0.0143 0.0269  110 ARG A CZ  
218  N  NH1 . ARG A 26 ? 0.7358 0.8154 0.4619 0.1830  -0.0084 0.0230  110 ARG A NH1 
219  N  NH2 . ARG A 26 ? 0.6918 0.8098 0.4552 0.1666  -0.0087 0.0363  110 ARG A NH2 
220  N  N   . LEU A 27 ? 0.2404 0.3548 0.2954 0.0495  -0.0225 0.0237  111 LEU A N   
221  C  CA  . LEU A 27 ? 0.2207 0.2842 0.3012 -0.0009 -0.0083 0.0429  111 LEU A CA  
222  C  C   . LEU A 27 ? 0.2861 0.2126 0.3062 -0.0459 -0.0278 0.0192  111 LEU A C   
223  O  O   . LEU A 27 ? 0.3819 0.3316 0.3162 -0.0989 -0.0614 0.0339  111 LEU A O   
224  C  CB  . LEU A 27 ? 0.2503 0.3094 0.2978 -0.0119 0.0182  -0.0048 111 LEU A CB  
225  C  CG  . LEU A 27 ? 0.2738 0.2932 0.2847 0.0015  0.0358  0.0139  111 LEU A CG  
226  C  CD1 . LEU A 27 ? 0.3023 0.3143 0.3014 0.0308  0.0427  0.0018  111 LEU A CD1 
227  C  CD2 . LEU A 27 ? 0.3260 0.3114 0.2680 -0.0091 -0.0097 0.0022  111 LEU A CD2 
228  N  N   . GLN A 28 ? 0.2234 0.2276 0.3033 0.0327  -0.0297 0.0315  112 GLN A N   
229  C  CA  . GLN A 28 ? 0.2372 0.1922 0.3072 0.0025  -0.0157 0.0068  112 GLN A CA  
230  C  C   . GLN A 28 ? 0.2707 0.1427 0.3183 0.0584  -0.0227 -0.0006 112 GLN A C   
231  O  O   . GLN A 28 ? 0.2365 0.2158 0.3375 -0.0028 -0.0321 -0.0026 112 GLN A O   
232  C  CB  . GLN A 28 ? 0.2528 0.2133 0.3150 0.0083  0.0117  0.0008  112 GLN A CB  
233  C  CG  . GLN A 28 ? 0.3926 0.2288 0.3183 0.0231  0.0473  0.0077  112 GLN A CG  
234  C  CD  . GLN A 28 ? 0.4534 0.2108 0.3230 0.0019  0.0853  0.0013  112 GLN A CD  
235  O  OE1 . GLN A 28 ? 0.5907 0.2138 0.3343 -0.0033 0.1070  -0.0132 112 GLN A OE1 
236  N  NE2 . GLN A 28 ? 0.3711 0.2367 0.3243 -0.0334 0.0787  0.0302  112 GLN A NE2 
237  N  N   . ILE A 29 ? 0.2378 0.1924 0.3201 0.0559  0.0024  0.0067  113 ILE A N   
238  C  CA  . ILE A 29 ? 0.2468 0.2011 0.3241 0.0447  -0.0036 0.0049  113 ILE A CA  
239  C  C   . ILE A 29 ? 0.1705 0.2295 0.3266 -0.0079 0.0215  0.0254  113 ILE A C   
240  O  O   . ILE A 29 ? 0.1833 0.2901 0.3537 0.0045  0.0109  0.0467  113 ILE A O   
241  C  CB  . ILE A 29 ? 0.2488 0.2147 0.3235 0.0395  0.0031  -0.0493 113 ILE A CB  
242  C  CG1 . ILE A 29 ? 0.2624 0.3118 0.3227 -0.0203 0.0135  -0.0410 113 ILE A CG1 
243  C  CG2 . ILE A 29 ? 0.2604 0.2339 0.3276 0.0425  -0.0174 -0.0380 113 ILE A CG2 
244  C  CD1 . ILE A 29 ? 0.3342 0.2778 0.3266 -0.0094 0.0344  -0.0304 113 ILE A CD1 
245  N  N   . VAL A 30 ? 0.2141 0.2280 0.3084 -0.0006 -0.0156 0.0031  114 VAL A N   
246  C  CA  . VAL A 30 ? 0.2348 0.2157 0.3046 -0.0332 0.0074  -0.0049 114 VAL A CA  
247  C  C   . VAL A 30 ? 0.2337 0.2524 0.3231 -0.0149 0.0176  0.0036  114 VAL A C   
248  O  O   . VAL A 30 ? 0.2624 0.2462 0.3412 0.0102  0.0216  0.0089  114 VAL A O   
249  C  CB  . VAL A 30 ? 0.2971 0.2179 0.2980 0.0263  -0.0029 0.0025  114 VAL A CB  
250  C  CG1 . VAL A 30 ? 0.3156 0.3142 0.2813 -0.0184 0.0292  0.0490  114 VAL A CG1 
251  C  CG2 . VAL A 30 ? 0.3421 0.2324 0.3012 0.0318  -0.0024 -0.0215 114 VAL A CG2 
252  N  N   . ASN A 31 ? 0.2364 0.2175 0.3362 -0.0066 0.0065  -0.0179 115 ASN A N   
253  C  CA  . ASN A 31 ? 0.2311 0.2203 0.3509 0.0051  -0.0041 -0.0125 115 ASN A CA  
254  C  C   . ASN A 31 ? 0.2030 0.1988 0.3608 -0.0437 -0.0033 -0.0372 115 ASN A C   
255  O  O   . ASN A 31 ? 0.2921 0.1861 0.3622 -0.0585 0.0146  -0.0304 115 ASN A O   
256  C  CB  . ASN A 31 ? 0.2553 0.1944 0.3687 0.0622  -0.0157 -0.0132 115 ASN A CB  
257  C  CG  . ASN A 31 ? 0.3638 0.2936 0.3816 0.0909  -0.0335 0.0031  115 ASN A CG  
258  O  OD1 . ASN A 31 ? 0.5255 0.3501 0.3850 0.1704  -0.0637 -0.0008 115 ASN A OD1 
259  N  ND2 . ASN A 31 ? 0.4132 0.3412 0.3954 0.0609  0.0041  0.0627  115 ASN A ND2 
260  N  N   . ASN A 32 ? 0.2783 0.2192 0.3736 -0.0281 -0.0182 -0.0457 116 ASN A N   
261  C  CA  . ASN A 32 ? 0.2679 0.2147 0.4028 -0.0146 -0.0036 -0.0507 116 ASN A CA  
262  C  C   . ASN A 32 ? 0.3064 0.2579 0.4351 0.0298  0.0078  -0.0281 116 ASN A C   
263  O  O   . ASN A 32 ? 0.3631 0.2818 0.4296 -0.0111 -0.0303 -0.0766 116 ASN A O   
264  C  CB  . ASN A 32 ? 0.2623 0.2813 0.4114 0.0005  -0.0290 -0.0627 116 ASN A CB  
265  C  CG  . ASN A 32 ? 0.3314 0.4119 0.4227 -0.0282 -0.0703 -0.0624 116 ASN A CG  
266  O  OD1 . ASN A 32 ? 0.3843 0.5618 0.4244 -0.1124 -0.0583 -0.0253 116 ASN A OD1 
267  N  ND2 . ASN A 32 ? 0.3695 0.6059 0.4367 0.0470  -0.0938 -0.0638 116 ASN A ND2 
268  N  N   . THR A 33 ? 0.3363 0.2539 0.4739 -0.0075 -0.0015 -0.0252 117 THR A N   
269  C  CA  . THR A 33 ? 0.3860 0.2683 0.5084 0.0091  -0.0117 -0.0302 117 THR A CA  
270  C  C   . THR A 33 ? 0.3304 0.2443 0.5323 -0.0308 -0.0200 -0.0570 117 THR A C   
271  O  O   . THR A 33 ? 0.4381 0.3189 0.5461 0.0174  -0.0085 -0.0634 117 THR A O   
272  C  CB  . THR A 33 ? 0.4380 0.2666 0.5252 -0.0831 -0.0124 -0.0077 117 THR A CB  
273  O  OG1 . THR A 33 ? 0.5241 0.3046 0.5295 0.0138  -0.0453 -0.0155 117 THR A OG1 
274  C  CG2 . THR A 33 ? 0.4547 0.3716 0.5278 0.0084  0.0152  0.0506  117 THR A CG2 
275  N  N   . GLU A 34 ? 0.3351 0.3044 0.5435 0.0013  -0.0124 -0.0778 118 GLU A N   
276  C  CA  . GLU A 34 ? 0.4187 0.4065 0.5529 0.0477  -0.0097 -0.0813 118 GLU A CA  
277  C  C   . GLU A 34 ? 0.4642 0.5045 0.5469 -0.0155 0.0051  -0.0749 118 GLU A C   
278  O  O   . GLU A 34 ? 0.6059 0.7280 0.5543 0.0947  0.0127  -0.0738 118 GLU A O   
279  C  CB  . GLU A 34 ? 0.3956 0.3853 0.5658 0.0141  -0.0218 -0.0913 118 GLU A CB  
280  C  CG  . GLU A 34 ? 0.4967 0.4075 0.5736 0.0667  0.0075  -0.0773 118 GLU A CG  
281  C  CD  . GLU A 34 ? 0.6172 0.5293 0.5835 0.1519  0.0324  -0.0901 118 GLU A CD  
282  O  OE1 . GLU A 34 ? 0.5750 0.4771 0.5892 0.1039  0.0357  -0.1211 118 GLU A OE1 
283  O  OE2 . GLU A 34 ? 0.6708 0.5927 0.5868 0.1195  0.0531  -0.0687 118 GLU A OE2 
284  N  N   . GLY A 35 ? 0.4287 0.3332 0.5328 -0.0548 0.0196  -0.0916 119 GLY A N   
285  C  CA  . GLY A 35 ? 0.4444 0.2967 0.5250 0.0183  0.0168  -0.0765 119 GLY A CA  
286  C  C   . GLY A 35 ? 0.3580 0.2577 0.5152 0.1277  0.0167  -0.0574 119 GLY A C   
287  O  O   . GLY A 35 ? 0.3879 0.3010 0.5383 0.0722  0.0062  -0.0561 119 GLY A O   
288  N  N   . ASP A 36 ? 0.4231 0.1947 0.4783 -0.0032 -0.0024 -0.0456 120 ASP A N   
289  C  CA  . ASP A 36 ? 0.5145 0.2238 0.4430 0.0278  -0.0012 -0.0510 120 ASP A CA  
290  C  C   . ASP A 36 ? 0.4235 0.1823 0.3916 0.0342  -0.0327 -0.0206 120 ASP A C   
291  O  O   . ASP A 36 ? 0.4902 0.2393 0.3884 0.1056  -0.0854 -0.0734 120 ASP A O   
292  C  CB  . ASP A 36 ? 0.7462 0.3407 0.4572 0.0717  0.0027  -0.0713 120 ASP A CB  
293  C  CG  . ASP A 36 ? 0.8899 0.4980 0.4809 0.0416  -0.0307 -0.0690 120 ASP A CG  
294  O  OD1 . ASP A 36 ? 0.8813 0.5415 0.4894 -0.0625 -0.0853 -0.0750 120 ASP A OD1 
295  O  OD2 . ASP A 36 ? 1.0022 0.6002 0.4885 0.1178  -0.0191 -0.0689 120 ASP A OD2 
296  N  N   . TRP A 37 ? 0.2748 0.2057 0.3438 -0.0388 0.0043  -0.0248 121 TRP A N   
297  C  CA  . TRP A 37 ? 0.1888 0.2210 0.3178 -0.0165 0.0220  -0.0260 121 TRP A CA  
298  C  C   . TRP A 37 ? 0.2157 0.2397 0.3147 0.0204  0.0254  0.0067  121 TRP A C   
299  O  O   . TRP A 37 ? 0.3087 0.2786 0.3157 0.0612  0.0168  0.0318  121 TRP A O   
300  C  CB  . TRP A 37 ? 0.2282 0.2688 0.3102 0.0022  0.0248  -0.0389 121 TRP A CB  
301  C  CG  . TRP A 37 ? 0.2134 0.2520 0.3111 0.0167  0.0460  -0.0418 121 TRP A CG  
302  C  CD1 . TRP A 37 ? 0.2376 0.2711 0.3242 -0.0141 0.0347  -0.0019 121 TRP A CD1 
303  C  CD2 . TRP A 37 ? 0.2570 0.1936 0.3135 -0.0081 0.0284  -0.0395 121 TRP A CD2 
304  N  NE1 . TRP A 37 ? 0.3493 0.2575 0.3208 -0.0005 0.0288  -0.0010 121 TRP A NE1 
305  C  CE2 . TRP A 37 ? 0.3114 0.2566 0.3188 0.0270  0.0325  -0.0090 121 TRP A CE2 
306  C  CE3 . TRP A 37 ? 0.2630 0.2516 0.3112 -0.0071 0.0177  -0.0133 121 TRP A CE3 
307  C  CZ2 . TRP A 37 ? 0.3186 0.2863 0.3242 0.0547  0.0400  -0.0104 121 TRP A CZ2 
308  C  CZ3 . TRP A 37 ? 0.2447 0.2910 0.3238 0.0607  0.0310  -0.0025 121 TRP A CZ3 
309  C  CH2 . TRP A 37 ? 0.2244 0.3079 0.3222 0.0643  0.0324  -0.0070 121 TRP A CH2 
310  N  N   . TRP A 38 ? 0.2282 0.1967 0.3026 0.0289  0.0277  -0.0245 122 TRP A N   
311  C  CA  . TRP A 38 ? 0.1604 0.2142 0.2916 0.0073  0.0061  -0.0347 122 TRP A CA  
312  C  C   . TRP A 38 ? 0.1782 0.1937 0.2717 -0.0169 -0.0031 -0.0133 122 TRP A C   
313  O  O   . TRP A 38 ? 0.2605 0.2346 0.2740 -0.0500 0.0234  -0.0076 122 TRP A O   
314  C  CB  . TRP A 38 ? 0.2344 0.2199 0.2990 -0.0147 -0.0128 -0.0761 122 TRP A CB  
315  C  CG  . TRP A 38 ? 0.2492 0.2305 0.3113 0.0544  -0.0273 -0.0729 122 TRP A CG  
316  C  CD1 . TRP A 38 ? 0.2661 0.2674 0.3182 0.0043  -0.0216 -0.0655 122 TRP A CD1 
317  C  CD2 . TRP A 38 ? 0.2274 0.2917 0.3189 -0.0361 -0.0332 -0.0533 122 TRP A CD2 
318  N  NE1 . TRP A 38 ? 0.2923 0.2771 0.3272 -0.0007 -0.0428 -0.0704 122 TRP A NE1 
319  C  CE2 . TRP A 38 ? 0.2403 0.2992 0.3276 -0.0536 -0.0393 -0.0514 122 TRP A CE2 
320  C  CE3 . TRP A 38 ? 0.2187 0.3382 0.3220 -0.0070 -0.0277 -0.0159 122 TRP A CE3 
321  C  CZ2 . TRP A 38 ? 0.2807 0.3680 0.3326 -0.0327 -0.0601 -0.0446 122 TRP A CZ2 
322  C  CZ3 . TRP A 38 ? 0.3045 0.3230 0.3226 -0.0130 -0.0578 -0.0257 122 TRP A CZ3 
323  C  CH2 . TRP A 38 ? 0.3102 0.3572 0.3324 -0.0032 -0.0554 -0.0364 122 TRP A CH2 
324  N  N   . LEU A 39 ? 0.2293 0.1939 0.2637 0.0004  0.0044  -0.0138 123 LEU A N   
325  C  CA  . LEU A 39 ? 0.1887 0.1695 0.2580 0.0302  0.0077  -0.0137 123 LEU A CA  
326  C  C   . LEU A 39 ? 0.2088 0.1581 0.2675 0.0125  0.0141  -0.0027 123 LEU A C   
327  O  O   . LEU A 39 ? 0.2047 0.2042 0.2764 -0.0125 0.0199  0.0043  123 LEU A O   
328  C  CB  . LEU A 39 ? 0.2486 0.1810 0.2513 0.0006  -0.0071 -0.0075 123 LEU A CB  
329  C  CG  . LEU A 39 ? 0.2107 0.2027 0.2530 -0.0146 -0.0080 -0.0056 123 LEU A CG  
330  C  CD1 . LEU A 39 ? 0.2564 0.2528 0.2611 -0.0724 -0.0089 0.0041  123 LEU A CD1 
331  C  CD2 . LEU A 39 ? 0.2817 0.2757 0.2389 0.0052  -0.0218 -0.0261 123 LEU A CD2 
332  N  N   . ALA A 40 ? 0.1937 0.1723 0.2655 0.0263  0.0125  -0.0056 124 ALA A N   
333  C  CA  . ALA A 40 ? 0.2335 0.1536 0.2653 0.0388  -0.0072 -0.0166 124 ALA A CA  
334  C  C   . ALA A 40 ? 0.1721 0.2117 0.2810 0.0294  0.0090  -0.0019 124 ALA A C   
335  O  O   . ALA A 40 ? 0.1746 0.2086 0.2913 0.0111  0.0000  0.0050  124 ALA A O   
336  C  CB  . ALA A 40 ? 0.2900 0.2761 0.2482 0.0484  -0.0081 -0.0224 124 ALA A CB  
337  N  N   . HIS A 41 ? 0.1734 0.1926 0.2817 0.0263  0.0114  0.0232  125 HIS A N   
338  C  CA  . HIS A 41 ? 0.1906 0.1653 0.2825 0.0587  0.0135  -0.0144 125 HIS A CA  
339  C  C   . HIS A 41 ? 0.2357 0.1782 0.2818 0.0228  0.0081  0.0029  125 HIS A C   
340  O  O   . HIS A 41 ? 0.2366 0.2243 0.2701 0.0129  0.0019  0.0092  125 HIS A O   
341  C  CB  . HIS A 41 ? 0.2653 0.1817 0.2933 0.0196  0.0265  -0.0212 125 HIS A CB  
342  C  CG  . HIS A 41 ? 0.2799 0.1321 0.3041 0.0032  0.0282  -0.0312 125 HIS A CG  
343  N  ND1 . HIS A 41 ? 0.2337 0.2791 0.3079 -0.0048 -0.0014 -0.0363 125 HIS A ND1 
344  C  CD2 . HIS A 41 ? 0.2511 0.2006 0.3112 0.0868  0.0366  -0.0168 125 HIS A CD2 
345  C  CE1 . HIS A 41 ? 0.2879 0.2598 0.3165 0.0688  0.0481  -0.0700 125 HIS A CE1 
346  N  NE2 . HIS A 41 ? 0.2521 0.2615 0.3255 0.0467  0.0311  -0.0447 125 HIS A NE2 
347  N  N   . SER A 42 ? 0.2328 0.1487 0.2872 0.0049  0.0130  0.0241  126 SER A N   
348  C  CA  . SER A 42 ? 0.1992 0.2005 0.2966 0.0403  0.0250  0.0341  126 SER A CA  
349  C  C   . SER A 42 ? 0.1814 0.2244 0.3091 0.0667  -0.0080 0.0020  126 SER A C   
350  O  O   . SER A 42 ? 0.2520 0.2245 0.2986 0.0356  -0.0035 -0.0044 126 SER A O   
351  C  CB  . SER A 42 ? 0.2775 0.2151 0.2928 0.0701  0.0367  0.0352  126 SER A CB  
352  O  OG  . SER A 42 ? 0.2731 0.2216 0.2932 0.0404  0.0276  0.0100  126 SER A OG  
353  N  N   . LEU A 43 ? 0.1668 0.2122 0.3351 0.0611  0.0286  0.0191  127 LEU A N   
354  C  CA  . LEU A 43 ? 0.2001 0.2664 0.3582 0.0351  0.0156  -0.0252 127 LEU A CA  
355  C  C   . LEU A 43 ? 0.2232 0.2773 0.3721 0.0052  0.0067  -0.0127 127 LEU A C   
356  O  O   . LEU A 43 ? 0.3392 0.3214 0.3946 0.0798  0.0522  0.0190  127 LEU A O   
357  C  CB  . LEU A 43 ? 0.2336 0.2871 0.3640 0.1067  0.0174  -0.0007 127 LEU A CB  
358  C  CG  . LEU A 43 ? 0.2694 0.2690 0.3643 0.0203  0.0129  0.0057  127 LEU A CG  
359  C  CD1 . LEU A 43 ? 0.3178 0.3397 0.3775 -0.0453 -0.0028 0.0544  127 LEU A CD1 
360  C  CD2 . LEU A 43 ? 0.2995 0.3337 0.3666 0.0918  -0.0011 0.0052  127 LEU A CD2 
361  N  N   . SER A 44 ? 0.2733 0.2119 0.3697 0.0313  0.0138  -0.0077 128 SER A N   
362  C  CA  . SER A 44 ? 0.3117 0.1807 0.3745 0.0375  0.0183  0.0262  128 SER A CA  
363  C  C   . SER A 44 ? 0.3123 0.1967 0.3848 0.0514  0.0154  -0.0113 128 SER A C   
364  O  O   . SER A 44 ? 0.3743 0.2393 0.4133 0.0668  -0.0413 -0.0549 128 SER A O   
365  C  CB  . SER A 44 ? 0.2930 0.3524 0.3705 0.0214  0.0067  0.0295  128 SER A CB  
366  O  OG  . SER A 44 ? 0.2679 0.4123 0.3783 0.0260  -0.0367 0.0142  128 SER A OG  
367  N  N   . THR A 45 ? 0.2906 0.2000 0.3810 0.0383  -0.0017 0.0304  129 THR A N   
368  C  CA  . THR A 45 ? 0.2873 0.2376 0.3777 0.0192  0.0179  0.0055  129 THR A CA  
369  C  C   . THR A 45 ? 0.2845 0.1610 0.3736 0.0432  0.0036  -0.0183 129 THR A C   
370  O  O   . THR A 45 ? 0.2955 0.2383 0.3935 -0.0120 0.0122  -0.0302 129 THR A O   
371  C  CB  . THR A 45 ? 0.2647 0.2137 0.3739 0.0023  0.0325  0.0260  129 THR A CB  
372  O  OG1 . THR A 45 ? 0.2884 0.2032 0.3643 0.0092  0.0176  0.0283  129 THR A OG1 
373  C  CG2 . THR A 45 ? 0.3597 0.2096 0.3788 0.0183  0.0317  0.0396  129 THR A CG2 
374  N  N   . GLY A 46 ? 0.2780 0.1771 0.3598 0.0655  -0.0019 0.0278  130 GLY A N   
375  C  CA  . GLY A 46 ? 0.2664 0.1881 0.3533 0.0647  0.0079  0.0040  130 GLY A CA  
376  C  C   . GLY A 46 ? 0.2378 0.1756 0.3522 0.0325  0.0249  -0.0338 130 GLY A C   
377  O  O   . GLY A 46 ? 0.3375 0.2426 0.3521 0.0381  0.0214  -0.0283 130 GLY A O   
378  N  N   . GLN A 47 ? 0.2208 0.2193 0.3566 0.0105  0.0211  -0.0387 131 GLN A N   
379  C  CA  . GLN A 47 ? 0.1853 0.1967 0.3583 -0.0161 0.0157  -0.0132 131 GLN A CA  
380  C  C   . GLN A 47 ? 0.2022 0.1852 0.3295 0.0227  0.0220  -0.0102 131 GLN A C   
381  O  O   . GLN A 47 ? 0.1989 0.2175 0.3356 0.0292  0.0010  -0.0170 131 GLN A O   
382  C  CB  . GLN A 47 ? 0.2792 0.1972 0.3842 -0.0078 0.0436  0.0015  131 GLN A CB  
383  C  CG  . GLN A 47 ? 0.3060 0.2076 0.4198 -0.0486 0.0425  -0.0211 131 GLN A CG  
384  C  CD  . GLN A 47 ? 0.4977 0.3343 0.4507 -0.0035 0.0494  -0.0396 131 GLN A CD  
385  O  OE1 . GLN A 47 ? 0.5228 0.3981 0.4685 -0.0345 0.0548  -0.0056 131 GLN A OE1 
386  N  NE2 . GLN A 47 ? 0.5702 0.4467 0.4631 0.0072  0.0463  -0.0326 131 GLN A NE2 
387  N  N   . THR A 48 ? 0.2555 0.2163 0.3024 0.0798  0.0154  -0.0182 132 THR A N   
388  C  CA  . THR A 48 ? 0.2513 0.1940 0.2884 0.0805  0.0197  -0.0144 132 THR A CA  
389  C  C   . THR A 48 ? 0.2425 0.1707 0.2926 0.0426  -0.0008 -0.0530 132 THR A C   
390  O  O   . THR A 48 ? 0.2739 0.2429 0.3086 0.0106  -0.0181 -0.0665 132 THR A O   
391  C  CB  . THR A 48 ? 0.2565 0.1866 0.2789 0.0461  0.0191  -0.0293 132 THR A CB  
392  O  OG1 . THR A 48 ? 0.2305 0.3074 0.2752 0.0750  0.0016  -0.0148 132 THR A OG1 
393  C  CG2 . THR A 48 ? 0.2283 0.2744 0.2748 0.0681  0.0372  0.0117  132 THR A CG2 
394  N  N   . GLY A 49 ? 0.2466 0.1726 0.2780 0.0439  0.0255  -0.0303 133 GLY A N   
395  C  CA  . GLY A 49 ? 0.2102 0.1645 0.2728 0.0435  0.0142  -0.0572 133 GLY A CA  
396  C  C   . GLY A 49 ? 0.1864 0.1910 0.2702 0.0501  0.0233  -0.0312 133 GLY A C   
397  O  O   . GLY A 49 ? 0.1737 0.2096 0.2854 0.0091  0.0075  -0.0029 133 GLY A O   
398  N  N   . TYR A 50 ? 0.2188 0.1356 0.2714 0.0190  0.0213  0.0055  134 TYR A N   
399  C  CA  . TYR A 50 ? 0.2284 0.1409 0.2728 0.0328  0.0044  -0.0052 134 TYR A CA  
400  C  C   . TYR A 50 ? 0.2019 0.1946 0.2710 -0.0061 0.0241  0.0112  134 TYR A C   
401  O  O   . TYR A 50 ? 0.2171 0.1987 0.2740 0.0011  0.0261  -0.0046 134 TYR A O   
402  C  CB  . TYR A 50 ? 0.2075 0.2008 0.2754 0.0264  0.0097  0.0052  134 TYR A CB  
403  C  CG  . TYR A 50 ? 0.2276 0.1487 0.2798 0.0093  -0.0018 0.0103  134 TYR A CG  
404  C  CD1 . TYR A 50 ? 0.2132 0.2055 0.2832 -0.0099 0.0149  0.0358  134 TYR A CD1 
405  C  CD2 . TYR A 50 ? 0.2185 0.2118 0.2784 0.0115  -0.0199 -0.0132 134 TYR A CD2 
406  C  CE1 . TYR A 50 ? 0.2049 0.2126 0.2896 0.0063  0.0026  0.0353  134 TYR A CE1 
407  C  CE2 . TYR A 50 ? 0.2593 0.2466 0.2757 0.0620  0.0100  0.0255  134 TYR A CE2 
408  C  CZ  . TYR A 50 ? 0.2032 0.2587 0.2846 0.0326  -0.0067 0.0208  134 TYR A CZ  
409  O  OH  . TYR A 50 ? 0.2704 0.2304 0.2898 0.0301  -0.0137 0.0159  134 TYR A OH  
410  N  N   . ILE A 51 ? 0.2136 0.2030 0.2704 0.0221  0.0085  0.0031  135 ILE A N   
411  C  CA  . ILE A 51 ? 0.2159 0.1965 0.2839 0.0242  -0.0059 0.0103  135 ILE A CA  
412  C  C   . ILE A 51 ? 0.2690 0.2039 0.2874 0.0433  0.0010  0.0250  135 ILE A C   
413  O  O   . ILE A 51 ? 0.2847 0.2242 0.2868 0.0445  0.0218  0.0162  135 ILE A O   
414  C  CB  . ILE A 51 ? 0.2203 0.2414 0.3099 -0.0146 0.0073  -0.0063 135 ILE A CB  
415  C  CG1 . ILE A 51 ? 0.2113 0.2562 0.3204 0.0150  0.0107  -0.0055 135 ILE A CG1 
416  C  CG2 . ILE A 51 ? 0.2788 0.1783 0.3122 0.0194  0.0160  -0.0367 135 ILE A CG2 
417  C  CD1 . ILE A 51 ? 0.2380 0.3804 0.3344 0.0090  0.0021  -0.0460 135 ILE A CD1 
418  N  N   . PRO A 52 ? 0.2678 0.2424 0.2800 0.0120  0.0072  -0.0028 136 PRO A N   
419  C  CA  . PRO A 52 ? 0.2943 0.2297 0.2871 -0.0141 0.0140  -0.0276 136 PRO A CA  
420  C  C   . PRO A 52 ? 0.2962 0.2626 0.3082 0.0577  -0.0240 -0.0396 136 PRO A C   
421  O  O   . PRO A 52 ? 0.3964 0.3437 0.3172 0.1353  -0.0551 -0.0645 136 PRO A O   
422  C  CB  . PRO A 52 ? 0.3831 0.3080 0.2816 0.0743  0.0743  0.0016  136 PRO A CB  
423  C  CG  . PRO A 52 ? 0.3424 0.3286 0.2753 0.0177  0.0307  -0.0268 136 PRO A CG  
424  C  CD  . PRO A 52 ? 0.2943 0.2955 0.2723 -0.0243 0.0164  0.0011  136 PRO A CD  
425  N  N   . SER A 53 ? 0.3342 0.2791 0.3245 0.0172  -0.0327 -0.0557 137 SER A N   
426  C  CA  . SER A 53 ? 0.3533 0.3970 0.3399 0.0388  -0.0628 -0.0537 137 SER A CA  
427  C  C   . SER A 53 ? 0.4134 0.4465 0.3536 0.0849  -0.0781 -0.0810 137 SER A C   
428  O  O   . SER A 53 ? 0.3814 0.4447 0.3635 0.0581  -0.0853 -0.0981 137 SER A O   
429  C  CB  . SER A 53 ? 0.4013 0.4066 0.3496 0.0459  -0.0432 -0.0558 137 SER A CB  
430  O  OG  . SER A 53 ? 0.4254 0.3668 0.3554 0.0296  -0.0368 -0.0620 137 SER A OG  
431  N  N   . ASN A 54 ? 0.4387 0.3678 0.3481 0.0605  -0.0929 -0.1098 138 ASN A N   
432  C  CA  . ASN A 54 ? 0.5092 0.4220 0.3541 0.1064  -0.0676 -0.0989 138 ASN A CA  
433  C  C   . ASN A 54 ? 0.4999 0.3349 0.3433 0.0879  -0.0984 -0.1055 138 ASN A C   
434  O  O   . ASN A 54 ? 0.5644 0.4730 0.3450 0.1574  -0.1066 -0.0800 138 ASN A O   
435  C  CB  . ASN A 54 ? 0.5244 0.4260 0.3647 0.0973  -0.0195 -0.0996 138 ASN A CB  
436  C  CG  . ASN A 54 ? 0.5847 0.5468 0.3761 0.1659  0.0149  -0.0834 138 ASN A CG  
437  O  OD1 . ASN A 54 ? 0.5875 0.4469 0.3826 0.1146  0.0277  -0.1045 138 ASN A OD1 
438  N  ND2 . ASN A 54 ? 0.6926 0.6648 0.3879 0.2085  0.0103  -0.0467 138 ASN A ND2 
439  N  N   . TYR A 55 ? 0.4358 0.3196 0.3389 0.0981  -0.0651 -0.0955 139 TYR A N   
440  C  CA  . TYR A 55 ? 0.3489 0.3387 0.3423 0.0499  -0.0431 -0.0687 139 TYR A CA  
441  C  C   . TYR A 55 ? 0.3836 0.4432 0.3534 0.1105  -0.0624 -0.0785 139 TYR A C   
442  O  O   . TYR A 55 ? 0.3045 0.4571 0.3619 0.0973  -0.0640 -0.0577 139 TYR A O   
443  C  CB  . TYR A 55 ? 0.3119 0.3899 0.3384 0.0395  -0.0222 -0.0318 139 TYR A CB  
444  C  CG  . TYR A 55 ? 0.3108 0.3508 0.3359 0.0811  0.0086  -0.0250 139 TYR A CG  
445  C  CD1 . TYR A 55 ? 0.3860 0.3788 0.3410 0.1475  0.0423  -0.0280 139 TYR A CD1 
446  C  CD2 . TYR A 55 ? 0.3071 0.4154 0.3368 0.0813  -0.0097 -0.0159 139 TYR A CD2 
447  C  CE1 . TYR A 55 ? 0.4380 0.3878 0.3465 0.1488  0.0561  -0.0197 139 TYR A CE1 
448  C  CE2 . TYR A 55 ? 0.3617 0.3737 0.3431 0.1245  0.0314  -0.0178 139 TYR A CE2 
449  C  CZ  . TYR A 55 ? 0.3763 0.3978 0.3521 0.0982  0.0758  -0.0038 139 TYR A CZ  
450  O  OH  . TYR A 55 ? 0.4808 0.4963 0.3653 0.1424  0.0959  0.0076  139 TYR A OH  
451  N  N   . VAL A 56 ? 0.3426 0.4096 0.3537 0.0374  -0.0732 -0.0904 140 VAL A N   
452  C  CA  . VAL A 56 ? 0.3691 0.4311 0.3656 0.0392  -0.1094 -0.0825 140 VAL A CA  
453  C  C   . VAL A 56 ? 0.3886 0.4466 0.3886 0.0719  -0.1107 -0.0726 140 VAL A C   
454  O  O   . VAL A 56 ? 0.4382 0.5334 0.4014 0.1258  -0.1343 -0.0752 140 VAL A O   
455  C  CB  . VAL A 56 ? 0.3773 0.3396 0.3615 0.0640  -0.0999 -0.0679 140 VAL A CB  
456  C  CG1 . VAL A 56 ? 0.3842 0.3368 0.3605 0.0821  -0.1091 -0.0425 140 VAL A CG1 
457  C  CG2 . VAL A 56 ? 0.3988 0.3130 0.3678 0.0684  -0.0781 -0.0343 140 VAL A CG2 
458  N  N   . ALA A 57 ? 0.3650 0.3999 0.3928 0.0446  -0.1119 -0.0647 141 ALA A N   
459  C  CA  . ALA A 57 ? 0.3821 0.4449 0.4041 -0.0052 -0.1253 -0.0335 141 ALA A CA  
460  C  C   . ALA A 57 ? 0.3882 0.4512 0.4252 0.0645  -0.1188 -0.0068 141 ALA A C   
461  O  O   . ALA A 57 ? 0.3671 0.4078 0.4138 0.0290  -0.1137 -0.0131 141 ALA A O   
462  C  CB  . ALA A 57 ? 0.4742 0.5070 0.3983 0.0206  -0.1568 -0.0333 141 ALA A CB  
463  N  N   . PRO A 58 ? 0.3594 0.3767 0.4524 -0.0177 -0.1173 -0.0011 142 PRO A N   
464  C  CA  . PRO A 58 ? 0.3278 0.4354 0.4680 0.0168  -0.1153 -0.0218 142 PRO A CA  
465  C  C   . PRO A 58 ? 0.4080 0.4463 0.4764 0.1064  -0.1555 -0.0400 142 PRO A C   
466  O  O   . PRO A 58 ? 0.4285 0.4641 0.4703 0.0548  -0.1782 -0.0484 142 PRO A O   
467  C  CB  . PRO A 58 ? 0.3604 0.4066 0.4704 0.0039  -0.0918 -0.0240 142 PRO A CB  
468  C  CG  . PRO A 58 ? 0.3981 0.4005 0.4643 0.0062  -0.0751 0.0191  142 PRO A CG  
469  C  CD  . PRO A 58 ? 0.4086 0.4018 0.4583 0.0038  -0.1034 -0.0016 142 PRO A CD  
470  N  N   . SER A 59 ? 0.3786 0.4945 0.4853 0.0428  -0.1423 -0.0326 143 SER A N   
471  C  CA  . SER A 59 ? 0.4303 0.5480 0.5005 0.0862  -0.1403 -0.0056 143 SER A CA  
472  C  C   . SER A 59 ? 0.4758 0.6726 0.5194 0.0534  -0.1419 0.0163  143 SER A C   
473  O  O   . SER A 59 ? 0.4851 0.6804 0.5288 0.0609  -0.1434 0.0126  143 SER A O   
474  C  CB  . SER A 59 ? 0.4872 0.5809 0.5003 0.0880  -0.1505 -0.0194 143 SER A CB  
475  O  OG  . SER A 59 ? 0.5908 0.5465 0.5034 0.0799  -0.1273 -0.0297 143 SER A OG  
476  O  OXT . SER A 59 ? 0.5069 0.7107 0.5310 0.0687  -0.1225 0.0270  143 SER A OXT 
477  N  N   . GLY B 1  ? 0.3695 0.2269 0.3886 0.0248  0.0300  -0.0338 85  GLY B N   
478  C  CA  . GLY B 1  ? 0.3916 0.2264 0.3996 0.1084  0.0364  -0.0031 85  GLY B CA  
479  C  C   . GLY B 1  ? 0.2730 0.2291 0.3920 -0.0210 0.0712  -0.0094 85  GLY B C   
480  O  O   . GLY B 1  ? 0.2724 0.2517 0.3769 0.0523  0.0657  -0.0151 85  GLY B O   
481  N  N   A VAL B 2  ? 0.2737 0.2898 0.3957 -0.0236 0.0506  -0.0144 86  VAL B N   
482  N  N   B VAL B 2  ? 0.2902 0.2759 0.3982 -0.0455 0.0411  -0.0203 86  VAL B N   
483  C  CA  A VAL B 2  ? 0.2445 0.3264 0.3935 -0.0204 0.0491  -0.0165 86  VAL B CA  
484  C  CA  B VAL B 2  ? 0.2716 0.2913 0.3939 -0.0742 0.0395  -0.0370 86  VAL B CA  
485  C  C   A VAL B 2  ? 0.2503 0.2806 0.3941 0.0325  0.0524  -0.0180 86  VAL B C   
486  C  C   B VAL B 2  ? 0.2343 0.2437 0.3922 -0.0623 0.0741  -0.0430 86  VAL B C   
487  O  O   A VAL B 2  ? 0.3210 0.2814 0.3971 0.0799  0.0447  -0.0261 86  VAL B O   
488  O  O   B VAL B 2  ? 0.2924 0.2587 0.3899 -0.0428 0.0716  -0.0840 86  VAL B O   
489  C  CB  A VAL B 2  ? 0.2254 0.3722 0.3899 -0.0571 0.0449  -0.0060 86  VAL B CB  
490  C  CB  B VAL B 2  ? 0.3021 0.3283 0.3897 -0.1282 0.0021  -0.0260 86  VAL B CB  
491  C  CG1 A VAL B 2  ? 0.3323 0.4381 0.3940 0.0489  0.0327  -0.0021 86  VAL B CG1 
492  C  CG1 B VAL B 2  ? 0.3533 0.3770 0.3847 -0.0820 -0.0303 -0.0348 86  VAL B CG1 
493  C  CG2 A VAL B 2  ? 0.1939 0.4274 0.3849 -0.0052 0.0574  0.0004  86  VAL B CG2 
494  C  CG2 B VAL B 2  ? 0.3741 0.3811 0.3929 0.0025  0.0158  -0.0043 86  VAL B CG2 
495  N  N   A THR B 3  ? 0.2625 0.2169 0.3956 0.0071  0.0390  -0.0170 87  THR B N   
496  N  N   B THR B 3  ? 0.2730 0.2512 0.3974 -0.0322 0.0591  -0.0185 87  THR B N   
497  C  CA  A THR B 3  ? 0.2698 0.2396 0.3954 -0.0094 0.0449  -0.0028 87  THR B CA  
498  C  CA  B THR B 3  ? 0.2254 0.2493 0.3974 -0.0489 0.0616  -0.0043 87  THR B CA  
499  C  C   A THR B 3  ? 0.2602 0.2420 0.3895 -0.0159 0.0666  -0.0299 87  THR B C   
500  C  C   B THR B 3  ? 0.2491 0.2678 0.3904 -0.0372 0.0765  -0.0360 87  THR B C   
501  O  O   A THR B 3  ? 0.2699 0.1677 0.3826 -0.0464 0.0711  -0.0298 87  THR B O   
502  O  O   B THR B 3  ? 0.3437 0.3005 0.3843 -0.0127 0.0806  -0.0404 87  THR B O   
503  C  CB  A THR B 3  ? 0.3163 0.2575 0.4010 0.0308  0.0381  0.0204  87  THR B CB  
504  C  CB  B THR B 3  ? 0.3090 0.3103 0.4039 0.0564  0.0648  -0.0130 87  THR B CB  
505  O  OG1 A THR B 3  ? 0.2778 0.3159 0.4032 0.0362  0.0487  0.0676  87  THR B OG1 
506  O  OG1 B THR B 3  ? 0.3432 0.3468 0.4037 0.0538  0.0314  -0.0264 87  THR B OG1 
507  C  CG2 A THR B 3  ? 0.3271 0.2123 0.4043 0.0989  0.0195  0.0210  87  THR B CG2 
508  C  CG2 B THR B 3  ? 0.2472 0.1775 0.4092 0.0374  0.0680  -0.0468 87  THR B CG2 
509  N  N   . THR B 4  ? 0.2730 0.3217 0.3910 -0.0111 0.0777  -0.0407 88  THR B N   
510  C  CA  . THR B 4  ? 0.3197 0.3254 0.3987 -0.0189 0.0659  -0.0354 88  THR B CA  
511  C  C   . THR B 4  ? 0.2971 0.3557 0.3978 -0.0751 0.0442  -0.0738 88  THR B C   
512  O  O   . THR B 4  ? 0.3433 0.3346 0.4042 -0.0960 0.0605  -0.0952 88  THR B O   
513  C  CB  . THR B 4  ? 0.3686 0.3785 0.4111 0.0366  0.0560  -0.0524 88  THR B CB  
514  O  OG1 . THR B 4  ? 0.4588 0.3268 0.4209 0.0689  0.0856  -0.0492 88  THR B OG1 
515  C  CG2 . THR B 4  ? 0.3579 0.5123 0.4168 0.1119  0.0466  -0.0152 88  THR B CG2 
516  N  N   . PHE B 5  ? 0.2510 0.3251 0.3966 -0.0743 0.0649  -0.0291 89  PHE B N   
517  C  CA  . PHE B 5  ? 0.2439 0.3311 0.4088 -0.0414 0.0541  -0.0478 89  PHE B CA  
518  C  C   . PHE B 5  ? 0.2580 0.3165 0.3854 -0.0650 0.0452  -0.0478 89  PHE B C   
519  O  O   . PHE B 5  ? 0.2276 0.3376 0.3825 -0.0321 0.0325  -0.0596 89  PHE B O   
520  C  CB  . PHE B 5  ? 0.2281 0.2628 0.4457 -0.0354 0.0602  -0.0954 89  PHE B CB  
521  C  CG  . PHE B 5  ? 0.3060 0.3224 0.4890 -0.0532 0.0844  -0.1320 89  PHE B CG  
522  C  CD1 . PHE B 5  ? 0.2846 0.3558 0.5133 -0.1103 0.1466  -0.0828 89  PHE B CD1 
523  C  CD2 . PHE B 5  ? 0.3159 0.3499 0.5065 -0.0591 0.0623  -0.1664 89  PHE B CD2 
524  C  CE1 . PHE B 5  ? 0.3404 0.3454 0.5311 -0.1202 0.1280  -0.0948 89  PHE B CE1 
525  C  CE2 . PHE B 5  ? 0.3897 0.4089 0.5177 0.0009  0.1059  -0.1769 89  PHE B CE2 
526  C  CZ  . PHE B 5  ? 0.3407 0.4361 0.5305 -0.0776 0.1045  -0.1232 89  PHE B CZ  
527  N  N   . VAL B 6  ? 0.2369 0.3360 0.3668 -0.0272 0.0477  -0.0676 90  VAL B N   
528  C  CA  . VAL B 6  ? 0.2525 0.3100 0.3705 0.0127  0.0309  -0.0528 90  VAL B CA  
529  C  C   . VAL B 6  ? 0.2746 0.3016 0.3607 0.0000  -0.0077 -0.0599 90  VAL B C   
530  O  O   . VAL B 6  ? 0.3044 0.3215 0.3718 0.0134  -0.0208 -0.0484 90  VAL B O   
531  C  CB  . VAL B 6  ? 0.3624 0.3448 0.3873 -0.0126 0.0501  -0.0722 90  VAL B CB  
532  C  CG1 . VAL B 6  ? 0.4215 0.3478 0.3918 -0.0071 0.0360  -0.0846 90  VAL B CG1 
533  C  CG2 . VAL B 6  ? 0.3926 0.3051 0.4004 -0.0221 0.0824  -0.0843 90  VAL B CG2 
534  N  N   . ALA B 7  ? 0.2838 0.2309 0.3452 -0.0128 -0.0071 -0.0504 91  ALA B N   
535  C  CA  . ALA B 7  ? 0.3075 0.2289 0.3395 0.0017  -0.0265 -0.0658 91  ALA B CA  
536  C  C   . ALA B 7  ? 0.3516 0.2740 0.3431 0.0407  -0.0276 -0.0594 91  ALA B C   
537  O  O   . ALA B 7  ? 0.3739 0.2870 0.3394 0.0138  0.0009  -0.0469 91  ALA B O   
538  C  CB  . ALA B 7  ? 0.2828 0.2665 0.3386 0.0126  -0.0206 -0.0427 91  ALA B CB  
539  N  N   . LEU B 8  ? 0.4377 0.3209 0.3520 0.0721  -0.0420 -0.0346 92  LEU B N   
540  C  CA  . LEU B 8  ? 0.4960 0.3208 0.3685 0.0338  -0.0524 -0.0449 92  LEU B CA  
541  C  C   . LEU B 8  ? 0.5184 0.3424 0.3744 -0.0094 -0.0322 -0.0547 92  LEU B C   
542  O  O   . LEU B 8  ? 0.5785 0.4384 0.3751 0.0021  -0.0367 -0.0637 92  LEU B O   
543  C  CB  . LEU B 8  ? 0.4887 0.3355 0.3821 0.0489  -0.0459 -0.0345 92  LEU B CB  
544  C  CG  . LEU B 8  ? 0.5108 0.3937 0.3979 0.1003  -0.0574 -0.0558 92  LEU B CG  
545  C  CD1 . LEU B 8  ? 0.5316 0.4388 0.4047 0.0814  -0.0765 -0.0359 92  LEU B CD1 
546  C  CD2 . LEU B 8  ? 0.5446 0.4198 0.4019 -0.0161 -0.0716 -0.0686 92  LEU B CD2 
547  N  N   . TYR B 9  ? 0.4964 0.3011 0.3872 -0.0450 -0.0222 -0.0511 93  TYR B N   
548  C  CA  . TYR B 9  ? 0.4811 0.2908 0.4040 -0.0666 0.0218  -0.0115 93  TYR B CA  
549  C  C   . TYR B 9  ? 0.4485 0.3245 0.4190 -0.0098 0.0511  -0.0140 93  TYR B C   
550  O  O   . TYR B 9  ? 0.3989 0.3060 0.4054 -0.0457 0.0324  -0.0264 93  TYR B O   
551  C  CB  . TYR B 9  ? 0.5284 0.3330 0.4108 -0.0898 0.0147  0.0103  93  TYR B CB  
552  C  CG  . TYR B 9  ? 0.6317 0.3734 0.4169 -0.0122 -0.0243 -0.0029 93  TYR B CG  
553  C  CD1 . TYR B 9  ? 0.6946 0.4372 0.4255 0.0397  -0.0411 -0.0149 93  TYR B CD1 
554  C  CD2 . TYR B 9  ? 0.6272 0.3600 0.4198 0.0167  -0.0471 -0.0135 93  TYR B CD2 
555  C  CE1 . TYR B 9  ? 0.6943 0.4552 0.4335 0.0388  -0.0459 -0.0129 93  TYR B CE1 
556  C  CE2 . TYR B 9  ? 0.6764 0.4026 0.4274 0.0576  -0.0548 -0.0246 93  TYR B CE2 
557  C  CZ  . TYR B 9  ? 0.7074 0.4833 0.4372 0.0659  -0.0687 -0.0312 93  TYR B CZ  
558  O  OH  . TYR B 9  ? 0.7556 0.5526 0.4459 0.0776  -0.1014 -0.0431 93  TYR B OH  
559  N  N   . ASP B 10 ? 0.4152 0.3149 0.4433 -0.0062 0.1032  0.0141  94  ASP B N   
560  C  CA  . ASP B 10 ? 0.3939 0.3021 0.4664 -0.0351 0.1155  0.0045  94  ASP B CA  
561  C  C   . ASP B 10 ? 0.3828 0.3347 0.4727 0.0483  0.0797  -0.0089 94  ASP B C   
562  O  O   . ASP B 10 ? 0.4250 0.3664 0.4714 -0.0156 0.0490  -0.0056 94  ASP B O   
563  C  CB  . ASP B 10 ? 0.4721 0.3986 0.4809 -0.0126 0.1619  0.0088  94  ASP B CB  
564  C  CG  . ASP B 10 ? 0.5512 0.5160 0.4937 -0.0115 0.1922  0.0039  94  ASP B CG  
565  O  OD1 . ASP B 10 ? 0.5892 0.4511 0.4970 -0.0114 0.1944  -0.0189 94  ASP B OD1 
566  O  OD2 . ASP B 10 ? 0.5520 0.5863 0.5029 -0.0147 0.2109  0.0231  94  ASP B OD2 
567  N  N   . TYR B 11 ? 0.3432 0.2849 0.4840 0.0476  0.0810  0.0072  95  TYR B N   
568  C  CA  . TYR B 11 ? 0.2898 0.3186 0.4994 0.0201  0.0769  0.0100  95  TYR B CA  
569  C  C   . TYR B 11 ? 0.2926 0.2622 0.5192 0.0121  0.0792  0.0130  95  TYR B C   
570  O  O   . TYR B 11 ? 0.2779 0.2465 0.5193 -0.0194 0.0694  0.0265  95  TYR B O   
571  C  CB  . TYR B 11 ? 0.3031 0.3135 0.4978 0.0086  0.0686  0.0071  95  TYR B CB  
572  C  CG  . TYR B 11 ? 0.2967 0.2315 0.5007 -0.0040 0.0513  0.0011  95  TYR B CG  
573  C  CD1 . TYR B 11 ? 0.3788 0.2428 0.5020 -0.0271 0.0373  0.0076  95  TYR B CD1 
574  C  CD2 . TYR B 11 ? 0.2402 0.2393 0.5006 -0.0223 0.0582  -0.0171 95  TYR B CD2 
575  C  CE1 . TYR B 11 ? 0.3612 0.2744 0.5014 0.0365  0.0242  0.0052  95  TYR B CE1 
576  C  CE2 . TYR B 11 ? 0.2143 0.2508 0.5027 -0.0306 0.0460  0.0047  95  TYR B CE2 
577  C  CZ  . TYR B 11 ? 0.2923 0.2310 0.5046 -0.0109 0.0212  0.0013  95  TYR B CZ  
578  O  OH  . TYR B 11 ? 0.2545 0.2429 0.5085 0.0088  -0.0181 -0.0209 95  TYR B OH  
579  N  N   . GLU B 12 ? 0.3078 0.3241 0.5419 0.0494  0.0801  -0.0209 96  GLU B N   
580  C  CA  . GLU B 12 ? 0.2441 0.3414 0.5632 -0.0075 0.0642  -0.0146 96  GLU B CA  
581  C  C   . GLU B 12 ? 0.2222 0.2957 0.5820 0.0343  0.0280  -0.0255 96  GLU B C   
582  O  O   . GLU B 12 ? 0.2729 0.3135 0.5810 -0.0198 0.0317  -0.0321 96  GLU B O   
583  C  CB  . GLU B 12 ? 0.3424 0.4255 0.5650 0.0086  0.0668  0.0089  96  GLU B CB  
584  C  CG  . GLU B 12 ? 0.3871 0.4770 0.5622 0.0165  0.0527  -0.0222 96  GLU B CG  
585  C  CD  . GLU B 12 ? 0.3725 0.4473 0.5593 -0.0471 0.0507  -0.0342 96  GLU B CD  
586  O  OE1 . GLU B 12 ? 0.4625 0.5497 0.5622 0.0091  0.0511  -0.0605 96  GLU B OE1 
587  O  OE2 . GLU B 12 ? 0.2865 0.4055 0.5454 -0.0448 0.0250  -0.0489 96  GLU B OE2 
588  N  N   . SER B 13 ? 0.1862 0.2721 0.6017 -0.0092 0.0203  -0.0216 97  SER B N   
589  C  CA  . SER B 13 ? 0.2041 0.1837 0.6174 -0.0248 0.0111  -0.0015 97  SER B CA  
590  C  C   . SER B 13 ? 0.1958 0.2207 0.6268 0.0448  0.0471  0.0401  97  SER B C   
591  O  O   . SER B 13 ? 0.2226 0.2451 0.6319 0.0294  0.0632  0.0232  97  SER B O   
592  C  CB  . SER B 13 ? 0.2187 0.1891 0.6198 0.0414  -0.0090 0.0127  97  SER B CB  
593  O  OG  . SER B 13 ? 0.2369 0.2181 0.6192 0.0402  -0.0126 0.0019  97  SER B OG  
594  N  N   A ARG B 14 ? 0.1924 0.1976 0.6361 0.0291  0.0464  0.0696  98  ARG B N   
595  N  N   B ARG B 14 ? 0.2099 0.2168 0.6444 0.0339  0.0460  0.0570  98  ARG B N   
596  C  CA  A ARG B 14 ? 0.2545 0.2133 0.6421 0.0626  0.0433  0.0624  98  ARG B CA  
597  C  CA  B ARG B 14 ? 0.2594 0.2408 0.6533 0.0496  0.0446  0.0583  98  ARG B CA  
598  C  C   A ARG B 14 ? 0.1886 0.2308 0.6528 -0.0036 0.0246  0.0437  98  ARG B C   
599  C  C   B ARG B 14 ? 0.2282 0.2427 0.6519 0.0218  0.0248  0.0442  98  ARG B C   
600  O  O   A ARG B 14 ? 0.2659 0.2189 0.6633 0.0117  -0.0031 0.0249  98  ARG B O   
601  O  O   B ARG B 14 ? 0.2661 0.2392 0.6563 0.0327  0.0114  0.0346  98  ARG B O   
602  C  CB  A ARG B 14 ? 0.2778 0.3049 0.6525 0.1138  0.0711  0.0907  98  ARG B CB  
603  C  CB  B ARG B 14 ? 0.2988 0.3119 0.6629 0.0972  0.0657  0.0792  98  ARG B CB  
604  C  CG  A ARG B 14 ? 0.3928 0.3383 0.6602 0.1305  0.0918  0.1055  98  ARG B CG  
605  C  CG  B ARG B 14 ? 0.3804 0.3643 0.6716 0.1417  0.0814  0.0928  98  ARG B CG  
606  C  CD  A ARG B 14 ? 0.4063 0.3284 0.6614 0.1676  0.1158  0.1076  98  ARG B CD  
607  C  CD  B ARG B 14 ? 0.4140 0.4309 0.6800 0.1853  0.0967  0.0925  98  ARG B CD  
608  N  NE  A ARG B 14 ? 0.4240 0.3910 0.6622 0.1635  0.1256  0.1086  98  ARG B NE  
609  N  NE  B ARG B 14 ? 0.4704 0.4965 0.6874 0.1522  0.1084  0.0862  98  ARG B NE  
610  C  CZ  A ARG B 14 ? 0.3813 0.3394 0.6610 0.1500  0.1434  0.1050  98  ARG B CZ  
611  C  CZ  B ARG B 14 ? 0.4931 0.5239 0.6928 0.1177  0.1203  0.0809  98  ARG B CZ  
612  N  NH1 A ARG B 14 ? 0.2516 0.2296 0.6565 0.0505  0.1129  0.1076  98  ARG B NH1 
613  N  NH1 B ARG B 14 ? 0.4980 0.5045 0.6948 0.0604  0.1207  0.0786  98  ARG B NH1 
614  N  NH2 A ARG B 14 ? 0.4820 0.4124 0.6594 0.1763  0.1675  0.0894  98  ARG B NH2 
615  N  NH2 B ARG B 14 ? 0.5266 0.5461 0.6941 0.1618  0.1202  0.0800  98  ARG B NH2 
616  N  N   . THR B 15 ? 0.2108 0.2675 0.6464 0.0181  0.0032  0.0374  99  THR B N   
617  C  CA  . THR B 15 ? 0.2224 0.2089 0.6277 -0.0440 0.0113  0.0408  99  THR B CA  
618  C  C   . THR B 15 ? 0.2480 0.2226 0.6189 -0.0283 -0.0373 0.0088  99  THR B C   
619  O  O   . THR B 15 ? 0.2036 0.2353 0.6214 -0.0010 -0.0549 -0.0370 99  THR B O   
620  C  CB  . THR B 15 ? 0.1912 0.2858 0.6201 0.0429  0.0229  0.0311  99  THR B CB  
621  O  OG1 . THR B 15 ? 0.2030 0.2216 0.6159 -0.0114 0.0139  0.0014  99  THR B OG1 
622  C  CG2 . THR B 15 ? 0.1955 0.2616 0.6140 0.0091  0.0483  0.0434  99  THR B CG2 
623  N  N   . GLU B 16 ? 0.2300 0.3427 0.5961 -0.1128 -0.0639 0.0108  100 GLU B N   
624  C  CA  . GLU B 16 ? 0.3037 0.4339 0.6070 -0.0645 -0.1081 -0.0015 100 GLU B CA  
625  C  C   . GLU B 16 ? 0.2788 0.3378 0.5841 -0.0703 -0.1394 -0.0056 100 GLU B C   
626  O  O   . GLU B 16 ? 0.3535 0.4461 0.5940 -0.0700 -0.1764 -0.0083 100 GLU B O   
627  C  CB  . GLU B 16 ? 0.3513 0.4575 0.6267 -0.1208 -0.1071 -0.0207 100 GLU B CB  
628  C  CG  . GLU B 16 ? 0.4823 0.6010 0.6416 -0.0486 -0.0800 -0.0175 100 GLU B CG  
629  C  CD  . GLU B 16 ? 0.4803 0.7220 0.6526 -0.1327 -0.0896 -0.0203 100 GLU B CD  
630  O  OE1 . GLU B 16 ? 0.4907 0.7499 0.6534 -0.1784 -0.1202 -0.0593 100 GLU B OE1 
631  O  OE2 . GLU B 16 ? 0.4470 0.7425 0.6580 -0.1223 -0.0842 -0.0089 100 GLU B OE2 
632  N  N   . THR B 17 ? 0.2235 0.2537 0.5454 -0.0633 -0.1019 -0.0380 101 THR B N   
633  C  CA  . THR B 17 ? 0.2120 0.2231 0.5155 -0.0719 -0.0812 0.0048  101 THR B CA  
634  C  C   . THR B 17 ? 0.1985 0.2497 0.5097 -0.0678 -0.0879 -0.0075 101 THR B C   
635  O  O   . THR B 17 ? 0.2451 0.2443 0.5012 -0.0773 -0.0934 0.0224  101 THR B O   
636  C  CB  . THR B 17 ? 0.2645 0.2089 0.5007 -0.0191 -0.0715 0.0024  101 THR B CB  
637  O  OG1 . THR B 17 ? 0.2794 0.2370 0.4944 -0.0354 -0.0844 0.0570  101 THR B OG1 
638  C  CG2 . THR B 17 ? 0.3000 0.2476 0.4961 -0.0630 -0.0688 -0.0375 101 THR B CG2 
639  N  N   . ASP B 18 ? 0.2269 0.1990 0.5096 0.0415  -0.0678 -0.0147 102 ASP B N   
640  C  CA  . ASP B 18 ? 0.2386 0.1853 0.5151 0.0410  -0.0601 -0.0221 102 ASP B CA  
641  C  C   . ASP B 18 ? 0.2262 0.2180 0.5220 -0.0098 -0.0639 -0.0134 102 ASP B C   
642  O  O   . ASP B 18 ? 0.2587 0.2635 0.5330 -0.0001 -0.0728 -0.0341 102 ASP B O   
643  C  CB  . ASP B 18 ? 0.1354 0.2448 0.5051 -0.0122 -0.0412 0.0187  102 ASP B CB  
644  C  CG  . ASP B 18 ? 0.1852 0.2269 0.5212 0.0361  -0.0422 0.0097  102 ASP B CG  
645  O  OD1 . ASP B 18 ? 0.1776 0.2445 0.5322 0.0113  -0.0527 0.0076  102 ASP B OD1 
646  O  OD2 . ASP B 18 ? 0.2073 0.2717 0.5251 0.0026  0.0044  0.0291  102 ASP B OD2 
647  N  N   . LEU B 19 ? 0.1802 0.2061 0.5165 0.0188  -0.0451 -0.0045 103 LEU B N   
648  C  CA  . LEU B 19 ? 0.1600 0.2544 0.5162 -0.0037 -0.0303 0.0380  103 LEU B CA  
649  C  C   . LEU B 19 ? 0.1574 0.2202 0.5092 0.0430  -0.0413 0.0129  103 LEU B C   
650  O  O   . LEU B 19 ? 0.1909 0.3097 0.5013 0.0549  -0.0661 -0.0272 103 LEU B O   
651  C  CB  . LEU B 19 ? 0.2206 0.2391 0.5269 -0.0445 -0.0191 0.0632  103 LEU B CB  
652  C  CG  . LEU B 19 ? 0.2192 0.2796 0.5367 -0.0646 -0.0442 0.0548  103 LEU B CG  
653  C  CD1 . LEU B 19 ? 0.2929 0.2528 0.5349 -0.0565 -0.0355 0.0596  103 LEU B CD1 
654  C  CD2 . LEU B 19 ? 0.2686 0.2507 0.5444 -0.0679 -0.0489 0.0422  103 LEU B CD2 
655  N  N   . SER B 20 ? 0.2120 0.2320 0.5123 0.0449  -0.0014 0.0356  104 SER B N   
656  C  CA  . SER B 20 ? 0.2097 0.2202 0.5107 -0.0216 0.0043  0.0275  104 SER B CA  
657  C  C   . SER B 20 ? 0.2265 0.2424 0.4917 -0.0193 -0.0161 0.0247  104 SER B C   
658  O  O   . SER B 20 ? 0.2964 0.2414 0.4881 0.0119  -0.0192 0.0521  104 SER B O   
659  C  CB  . SER B 20 ? 0.2033 0.2377 0.5285 0.0038  0.0016  0.0122  104 SER B CB  
660  O  OG  . SER B 20 ? 0.2758 0.2326 0.5393 -0.0025 0.0003  0.0078  104 SER B OG  
661  N  N   . PHE B 21 ? 0.2255 0.2516 0.4761 0.0240  -0.0092 -0.0099 105 PHE B N   
662  C  CA  . PHE B 21 ? 0.2105 0.2340 0.4631 0.0162  0.0286  -0.0278 105 PHE B CA  
663  C  C   . PHE B 21 ? 0.2773 0.2794 0.4636 0.0104  0.0574  -0.0309 105 PHE B C   
664  O  O   . PHE B 21 ? 0.3152 0.2793 0.4572 -0.0135 0.0624  -0.0131 105 PHE B O   
665  C  CB  . PHE B 21 ? 0.1987 0.1986 0.4500 0.0263  0.0255  -0.0330 105 PHE B CB  
666  C  CG  . PHE B 21 ? 0.1903 0.2335 0.4376 -0.0182 -0.0105 -0.0416 105 PHE B CG  
667  C  CD1 . PHE B 21 ? 0.2346 0.2743 0.4321 -0.0278 -0.0049 -0.0540 105 PHE B CD1 
668  C  CD2 . PHE B 21 ? 0.1890 0.2525 0.4349 0.0119  -0.0009 -0.0154 105 PHE B CD2 
669  C  CE1 . PHE B 21 ? 0.2445 0.2139 0.4302 -0.0109 0.0055  -0.0173 105 PHE B CE1 
670  C  CE2 . PHE B 21 ? 0.2309 0.2831 0.4283 0.0186  0.0115  -0.0309 105 PHE B CE2 
671  C  CZ  . PHE B 21 ? 0.2622 0.2311 0.4265 0.0022  0.0151  -0.0230 105 PHE B CZ  
672  N  N   . LYS B 22 ? 0.2609 0.2527 0.4684 0.0027  0.0731  -0.0302 106 LYS B N   
673  C  CA  . LYS B 22 ? 0.3495 0.3386 0.4764 0.0589  0.0753  -0.0520 106 LYS B CA  
674  C  C   . LYS B 22 ? 0.3849 0.2507 0.4505 0.0061  0.0773  -0.0435 106 LYS B C   
675  O  O   . LYS B 22 ? 0.3329 0.2592 0.4326 0.0277  0.0332  -0.0268 106 LYS B O   
676  C  CB  . LYS B 22 ? 0.5332 0.4279 0.5104 0.1627  0.0779  -0.0583 106 LYS B CB  
677  C  CG  . LYS B 22 ? 0.5872 0.4910 0.5329 0.2103  0.0932  -0.0460 106 LYS B CG  
678  C  CD  . LYS B 22 ? 0.6320 0.4638 0.5512 0.2319  0.0981  -0.0578 106 LYS B CD  
679  C  CE  . LYS B 22 ? 0.7550 0.5185 0.5631 0.1331  0.0887  -0.0799 106 LYS B CE  
680  N  NZ  . LYS B 22 ? 0.8218 0.4646 0.5683 0.0901  0.0907  -0.1088 106 LYS B NZ  
681  N  N   . LYS B 23 ? 0.4337 0.3492 0.4446 0.0337  0.1053  -0.0395 107 LYS B N   
682  C  CA  . LYS B 23 ? 0.5202 0.2830 0.4454 -0.0030 0.1075  -0.0432 107 LYS B CA  
683  C  C   . LYS B 23 ? 0.4931 0.2408 0.4488 -0.0164 0.0744  -0.0707 107 LYS B C   
684  O  O   . LYS B 23 ? 0.4630 0.3107 0.4615 0.0074  0.0895  -0.0715 107 LYS B O   
685  C  CB  . LYS B 23 ? 0.6544 0.3485 0.4534 0.0267  0.1256  -0.0272 107 LYS B CB  
686  C  CG  . LYS B 23 ? 0.7288 0.4419 0.4666 0.0244  0.1183  -0.0401 107 LYS B CG  
687  C  CD  . LYS B 23 ? 0.8151 0.5806 0.4793 0.0729  0.1058  -0.0692 107 LYS B CD  
688  C  CE  . LYS B 23 ? 0.8689 0.7066 0.4906 0.1033  0.0857  -0.0836 107 LYS B CE  
689  N  NZ  . LYS B 23 ? 0.9026 0.7617 0.5003 0.0867  0.0693  -0.0738 107 LYS B NZ  
690  N  N   . GLY B 24 ? 0.4376 0.2528 0.4327 0.0135  0.0602  -0.0537 108 GLY B N   
691  C  CA  . GLY B 24 ? 0.4139 0.2347 0.4331 0.0365  0.0534  -0.0424 108 GLY B CA  
692  C  C   . GLY B 24 ? 0.3711 0.2394 0.4353 0.0541  0.0321  -0.0247 108 GLY B C   
693  O  O   . GLY B 24 ? 0.4195 0.2353 0.4497 0.0085  0.0214  -0.0274 108 GLY B O   
694  N  N   . GLU B 25 ? 0.3132 0.2640 0.4245 0.0443  0.0003  -0.0527 109 GLU B N   
695  C  CA  . GLU B 25 ? 0.2314 0.2516 0.4203 0.0039  0.0151  -0.0333 109 GLU B CA  
696  C  C   . GLU B 25 ? 0.1983 0.2117 0.4122 -0.0109 0.0180  0.0008  109 GLU B C   
697  O  O   . GLU B 25 ? 0.2294 0.2363 0.4000 0.0302  -0.0336 -0.0149 109 GLU B O   
698  C  CB  . GLU B 25 ? 0.2684 0.2601 0.4259 -0.0220 0.0230  -0.0464 109 GLU B CB  
699  C  CG  . GLU B 25 ? 0.2844 0.2566 0.4328 0.0025  0.0259  -0.0462 109 GLU B CG  
700  C  CD  . GLU B 25 ? 0.2289 0.2875 0.4392 -0.0375 0.0527  -0.0391 109 GLU B CD  
701  O  OE1 . GLU B 25 ? 0.3156 0.2600 0.4370 0.0367  0.0615  -0.0014 109 GLU B OE1 
702  O  OE2 . GLU B 25 ? 0.3055 0.4459 0.4535 -0.0213 0.0411  -0.0566 109 GLU B OE2 
703  N  N   . ARG B 26 ? 0.2525 0.2398 0.4194 -0.0159 0.0570  0.0221  110 ARG B N   
704  C  CA  . ARG B 26 ? 0.3398 0.1964 0.4293 -0.0189 0.0454  0.0021  110 ARG B CA  
705  C  C   . ARG B 26 ? 0.2663 0.2425 0.4073 0.0248  0.0164  -0.0372 110 ARG B C   
706  O  O   . ARG B 26 ? 0.2774 0.3059 0.4041 0.0066  -0.0243 -0.0383 110 ARG B O   
707  C  CB  . ARG B 26 ? 0.4222 0.2529 0.4614 -0.0810 0.0704  0.0491  110 ARG B CB  
708  C  CG  . ARG B 26 ? 0.4737 0.3290 0.4873 -0.0118 0.0893  0.0543  110 ARG B CG  
709  C  CD  . ARG B 26 ? 0.5787 0.1923 0.5078 -0.0408 0.1082  0.0601  110 ARG B CD  
710  N  NE  . ARG B 26 ? 0.6769 0.2467 0.5259 0.1323  0.0997  0.0636  110 ARG B NE  
711  C  CZ  . ARG B 26 ? 0.6985 0.2876 0.5405 0.1683  0.1053  0.0388  110 ARG B CZ  
712  N  NH1 . ARG B 26 ? 0.6508 0.2884 0.5507 0.1993  0.1057  0.0238  110 ARG B NH1 
713  N  NH2 . ARG B 26 ? 0.6995 0.4374 0.5425 0.1037  0.1218  0.0357  110 ARG B NH2 
714  N  N   . LEU B 27 ? 0.2652 0.2226 0.3895 -0.0007 0.0227  -0.0227 111 LEU B N   
715  C  CA  . LEU B 27 ? 0.2394 0.2449 0.3703 -0.0495 0.0173  0.0176  111 LEU B CA  
716  C  C   . LEU B 27 ? 0.2136 0.2419 0.3618 -0.0037 0.0049  0.0065  111 LEU B C   
717  O  O   . LEU B 27 ? 0.2366 0.2676 0.3558 -0.0231 -0.0042 -0.0430 111 LEU B O   
718  C  CB  . LEU B 27 ? 0.2456 0.2785 0.3713 -0.0234 0.0193  0.0379  111 LEU B CB  
719  C  CG  . LEU B 27 ? 0.2091 0.3349 0.3787 0.0261  0.0095  0.0640  111 LEU B CG  
720  C  CD1 . LEU B 27 ? 0.2746 0.3373 0.3821 0.0487  0.0140  0.0802  111 LEU B CD1 
721  C  CD2 . LEU B 27 ? 0.2434 0.3211 0.3850 0.0383  0.0474  0.0755  111 LEU B CD2 
722  N  N   . GLN B 28 ? 0.2205 0.2275 0.3616 0.0392  0.0179  0.0033  112 GLN B N   
723  C  CA  . GLN B 28 ? 0.2510 0.1747 0.3605 0.0349  0.0061  0.0047  112 GLN B CA  
724  C  C   . GLN B 28 ? 0.2056 0.2161 0.3798 -0.0052 -0.0395 -0.0080 112 GLN B C   
725  O  O   . GLN B 28 ? 0.2244 0.2185 0.4078 0.0160  -0.0700 -0.0110 112 GLN B O   
726  C  CB  . GLN B 28 ? 0.2097 0.2751 0.3560 0.0368  0.0079  0.0119  112 GLN B CB  
727  C  CG  . GLN B 28 ? 0.2435 0.2565 0.3633 0.0154  0.0063  0.0213  112 GLN B CG  
728  C  CD  . GLN B 28 ? 0.2344 0.3319 0.3723 0.0508  -0.0057 0.0206  112 GLN B CD  
729  O  OE1 . GLN B 28 ? 0.2375 0.4526 0.3768 0.0584  -0.0123 0.0264  112 GLN B OE1 
730  N  NE2 . GLN B 28 ? 0.2436 0.3420 0.3713 0.0446  -0.0095 -0.0029 112 GLN B NE2 
731  N  N   . ILE B 29 ? 0.1914 0.2008 0.3776 0.0080  -0.0151 0.0026  113 ILE B N   
732  C  CA  . ILE B 29 ? 0.1686 0.1853 0.3843 0.0026  -0.0109 -0.0125 113 ILE B CA  
733  C  C   . ILE B 29 ? 0.1844 0.1439 0.3876 0.0006  0.0085  -0.0013 113 ILE B C   
734  O  O   . ILE B 29 ? 0.2214 0.1937 0.3851 -0.0376 0.0165  0.0118  113 ILE B O   
735  C  CB  . ILE B 29 ? 0.2061 0.2224 0.3890 0.0156  0.0094  -0.0192 113 ILE B CB  
736  C  CG1 . ILE B 29 ? 0.2697 0.2323 0.3971 -0.0059 0.0273  0.0000  113 ILE B CG1 
737  C  CG2 . ILE B 29 ? 0.2033 0.2290 0.3860 0.0237  0.0109  0.0038  113 ILE B CG2 
738  C  CD1 . ILE B 29 ? 0.2971 0.2755 0.4024 -0.0198 0.0286  0.0065  113 ILE B CD1 
739  N  N   . VAL B 30 ? 0.2193 0.1775 0.3951 0.0087  0.0275  -0.0298 114 VAL B N   
740  C  CA  . VAL B 30 ? 0.2153 0.2702 0.4003 0.0368  0.0008  -0.0530 114 VAL B CA  
741  C  C   . VAL B 30 ? 0.2099 0.2654 0.4064 -0.0064 -0.0059 -0.0055 114 VAL B C   
742  O  O   . VAL B 30 ? 0.2885 0.2786 0.4012 0.0207  -0.0118 0.0254  114 VAL B O   
743  C  CB  . VAL B 30 ? 0.2029 0.3649 0.4059 0.0545  -0.0066 -0.0860 114 VAL B CB  
744  C  CG1 . VAL B 30 ? 0.3001 0.3657 0.4108 0.0823  0.0092  -0.0818 114 VAL B CG1 
745  C  CG2 . VAL B 30 ? 0.2831 0.3930 0.4162 0.1424  -0.0202 -0.0676 114 VAL B CG2 
746  N  N   . ASN B 31 ? 0.2520 0.2510 0.4145 0.0177  0.0001  -0.0231 115 ASN B N   
747  C  CA  . ASN B 31 ? 0.2266 0.2058 0.4254 0.0108  -0.0241 -0.0125 115 ASN B CA  
748  C  C   . ASN B 31 ? 0.1777 0.2806 0.4342 0.0356  -0.0136 0.0247  115 ASN B C   
749  O  O   . ASN B 31 ? 0.2290 0.2970 0.4348 -0.0081 0.0029  -0.0017 115 ASN B O   
750  C  CB  . ASN B 31 ? 0.2420 0.2546 0.4337 0.1147  -0.0067 -0.0565 115 ASN B CB  
751  C  CG  . ASN B 31 ? 0.2839 0.3984 0.4378 0.0231  0.0023  -0.0711 115 ASN B CG  
752  O  OD1 . ASN B 31 ? 0.2974 0.4793 0.4443 0.0087  0.0145  -0.0674 115 ASN B OD1 
753  N  ND2 . ASN B 31 ? 0.3179 0.4695 0.4396 0.0995  0.0235  -0.0366 115 ASN B ND2 
754  N  N   . ASN B 32 ? 0.2127 0.2309 0.4448 -0.0134 -0.0038 0.0086  116 ASN B N   
755  C  CA  . ASN B 32 ? 0.2113 0.2619 0.4770 -0.0203 -0.0311 0.0082  116 ASN B CA  
756  C  C   . ASN B 32 ? 0.2608 0.4016 0.5007 -0.0097 -0.0039 0.0058  116 ASN B C   
757  O  O   . ASN B 32 ? 0.2041 0.5028 0.4981 -0.0174 -0.0261 0.0238  116 ASN B O   
758  C  CB  . ASN B 32 ? 0.2848 0.3785 0.4957 0.0230  -0.0532 -0.0342 116 ASN B CB  
759  C  CG  . ASN B 32 ? 0.2743 0.4088 0.5195 -0.0010 -0.0252 -0.0571 116 ASN B CG  
760  O  OD1 . ASN B 32 ? 0.2809 0.3927 0.5287 -0.1032 -0.0186 -0.0188 116 ASN B OD1 
761  N  ND2 . ASN B 32 ? 0.3071 0.5151 0.5300 0.0240  -0.0140 -0.1050 116 ASN B ND2 
762  N  N   . THR B 33 ? 0.2586 0.3157 0.5243 -0.0101 0.0170  -0.0248 117 THR B N   
763  C  CA  . THR B 33 ? 0.3342 0.3398 0.5475 0.0209  -0.0212 -0.0332 117 THR B CA  
764  C  C   . THR B 33 ? 0.3630 0.2786 0.5672 -0.0479 -0.0348 -0.0327 117 THR B C   
765  O  O   . THR B 33 ? 0.4663 0.3410 0.5796 0.1497  -0.0412 -0.0505 117 THR B O   
766  C  CB  . THR B 33 ? 0.2699 0.3738 0.5493 0.0160  -0.0355 -0.0553 117 THR B CB  
767  O  OG1 . THR B 33 ? 0.2406 0.4030 0.5463 0.0339  -0.0713 -0.0663 117 THR B OG1 
768  C  CG2 . THR B 33 ? 0.3323 0.3515 0.5516 -0.0077 0.0087  -0.0447 117 THR B CG2 
769  N  N   . GLU B 34 ? 0.3619 0.3223 0.5701 -0.0874 -0.0484 -0.0157 118 GLU B N   
770  C  CA  . GLU B 34 ? 0.3458 0.4212 0.5692 -0.0231 -0.0692 0.0190  118 GLU B CA  
771  C  C   . GLU B 34 ? 0.4072 0.4698 0.5666 -0.0155 -0.0296 0.0622  118 GLU B C   
772  O  O   . GLU B 34 ? 0.4605 0.3642 0.5773 -0.0592 0.0143  0.1108  118 GLU B O   
773  C  CB  . GLU B 34 ? 0.3724 0.3967 0.5730 -0.0811 -0.1046 -0.0262 118 GLU B CB  
774  C  CG  . GLU B 34 ? 0.4699 0.5449 0.5759 0.1446  -0.1241 -0.0219 118 GLU B CG  
775  C  CD  . GLU B 34 ? 0.5926 0.7562 0.5827 0.1649  -0.1329 -0.0082 118 GLU B CD  
776  O  OE1 . GLU B 34 ? 0.5666 0.7641 0.5842 0.1142  -0.1603 -0.0317 118 GLU B OE1 
777  O  OE2 . GLU B 34 ? 0.5916 0.8027 0.5851 0.1484  -0.1259 0.0312  118 GLU B OE2 
778  N  N   . GLY B 35 ? 0.3857 0.4847 0.5524 -0.0309 -0.0508 0.0606  119 GLY B N   
779  C  CA  . GLY B 35 ? 0.3614 0.4395 0.5367 -0.0441 -0.0534 0.0456  119 GLY B CA  
780  C  C   . GLY B 35 ? 0.3547 0.4208 0.5263 0.0646  -0.0620 0.0364  119 GLY B C   
781  O  O   . GLY B 35 ? 0.4521 0.3723 0.5410 0.0319  -0.0731 0.0253  119 GLY B O   
782  N  N   . ASP B 36 ? 0.2717 0.4335 0.4947 0.0586  -0.0484 0.0619  120 ASP B N   
783  C  CA  . ASP B 36 ? 0.2746 0.3121 0.4684 0.0279  -0.0574 0.0419  120 ASP B CA  
784  C  C   . ASP B 36 ? 0.2337 0.2685 0.4229 0.0080  -0.0718 -0.0150 120 ASP B C   
785  O  O   . ASP B 36 ? 0.3038 0.4202 0.4152 0.0845  -0.0503 -0.0354 120 ASP B O   
786  C  CB  . ASP B 36 ? 0.3633 0.3242 0.4815 -0.0108 -0.1074 0.0507  120 ASP B CB  
787  C  CG  . ASP B 36 ? 0.4972 0.4121 0.5028 0.0328  -0.1252 0.0769  120 ASP B CG  
788  O  OD1 . ASP B 36 ? 0.5226 0.5056 0.5142 0.0708  -0.1390 0.0845  120 ASP B OD1 
789  O  OD2 . ASP B 36 ? 0.5874 0.3861 0.5051 0.0224  -0.1516 0.0680  120 ASP B OD2 
790  N  N   . TRP B 37 ? 0.2077 0.2523 0.3909 0.0297  -0.0743 -0.0057 121 TRP B N   
791  C  CA  . TRP B 37 ? 0.2242 0.1922 0.3700 -0.0102 -0.0405 0.0152  121 TRP B CA  
792  C  C   . TRP B 37 ? 0.2147 0.2015 0.3620 -0.0076 -0.0312 0.0062  121 TRP B C   
793  O  O   . TRP B 37 ? 0.2217 0.2299 0.3745 0.0277  -0.0005 -0.0170 121 TRP B O   
794  C  CB  . TRP B 37 ? 0.2087 0.1853 0.3552 -0.0239 -0.0200 0.0005  121 TRP B CB  
795  C  CG  . TRP B 37 ? 0.2182 0.1589 0.3544 -0.0269 -0.0202 0.0129  121 TRP B CG  
796  C  CD1 . TRP B 37 ? 0.2311 0.2078 0.3547 -0.0088 -0.0198 0.0023  121 TRP B CD1 
797  C  CD2 . TRP B 37 ? 0.1937 0.2194 0.3541 -0.0278 -0.0332 -0.0062 121 TRP B CD2 
798  N  NE1 . TRP B 37 ? 0.2342 0.2424 0.3598 -0.0008 -0.0041 -0.0094 121 TRP B NE1 
799  C  CE2 . TRP B 37 ? 0.2261 0.2232 0.3581 0.0342  -0.0177 -0.0180 121 TRP B CE2 
800  C  CE3 . TRP B 37 ? 0.2100 0.2617 0.3538 -0.0161 -0.0183 -0.0185 121 TRP B CE3 
801  C  CZ2 . TRP B 37 ? 0.2632 0.2236 0.3609 0.0247  -0.0118 -0.0378 121 TRP B CZ2 
802  C  CZ3 . TRP B 37 ? 0.1992 0.2462 0.3503 -0.0215 0.0070  -0.0113 121 TRP B CZ3 
803  C  CH2 . TRP B 37 ? 0.2554 0.2383 0.3556 -0.0143 0.0161  -0.0056 121 TRP B CH2 
804  N  N   . TRP B 38 ? 0.2065 0.1693 0.3454 0.0184  -0.0266 0.0064  122 TRP B N   
805  C  CA  . TRP B 38 ? 0.1865 0.1683 0.3476 0.0017  -0.0266 -0.0008 122 TRP B CA  
806  C  C   . TRP B 38 ? 0.1859 0.1776 0.3417 0.0117  -0.0254 0.0009  122 TRP B C   
807  O  O   . TRP B 38 ? 0.1740 0.2844 0.3472 -0.0329 -0.0182 -0.0160 122 TRP B O   
808  C  CB  . TRP B 38 ? 0.1941 0.2346 0.3529 -0.0266 -0.0450 0.0172  122 TRP B CB  
809  C  CG  . TRP B 38 ? 0.2082 0.2556 0.3593 -0.0052 -0.0274 0.0343  122 TRP B CG  
810  C  CD1 . TRP B 38 ? 0.2221 0.3126 0.3647 -0.0712 -0.0165 0.0606  122 TRP B CD1 
811  C  CD2 . TRP B 38 ? 0.2176 0.2472 0.3672 -0.0083 -0.0425 0.0048  122 TRP B CD2 
812  N  NE1 . TRP B 38 ? 0.2013 0.3237 0.3670 -0.0714 -0.0325 0.0182  122 TRP B NE1 
813  C  CE2 . TRP B 38 ? 0.2246 0.2842 0.3686 -0.0736 -0.0490 -0.0231 122 TRP B CE2 
814  C  CE3 . TRP B 38 ? 0.2394 0.2351 0.3747 -0.0318 0.0149  0.0011  122 TRP B CE3 
815  C  CZ2 . TRP B 38 ? 0.2724 0.2880 0.3689 -0.0358 -0.0245 -0.0279 122 TRP B CZ2 
816  C  CZ3 . TRP B 38 ? 0.2775 0.3582 0.3711 -0.0264 0.0036  -0.0318 122 TRP B CZ3 
817  C  CH2 . TRP B 38 ? 0.2956 0.3366 0.3746 -0.0481 0.0079  -0.0157 122 TRP B CH2 
818  N  N   . LEU B 39 ? 0.1953 0.2091 0.3451 0.0228  -0.0522 0.0017  123 LEU B N   
819  C  CA  . LEU B 39 ? 0.2130 0.1894 0.3470 0.0326  -0.0547 0.0062  123 LEU B CA  
820  C  C   . LEU B 39 ? 0.1685 0.1491 0.3499 0.0090  -0.0354 0.0105  123 LEU B C   
821  O  O   . LEU B 39 ? 0.1931 0.2267 0.3468 -0.0209 -0.0135 0.0221  123 LEU B O   
822  C  CB  . LEU B 39 ? 0.1882 0.2515 0.3515 0.0117  -0.0505 -0.0038 123 LEU B CB  
823  C  CG  . LEU B 39 ? 0.2308 0.2555 0.3621 -0.0028 -0.0662 0.0210  123 LEU B CG  
824  C  CD1 . LEU B 39 ? 0.2607 0.3873 0.3714 -0.0227 -0.1229 0.0145  123 LEU B CD1 
825  C  CD2 . LEU B 39 ? 0.3188 0.2617 0.3640 0.0290  -0.0823 -0.0230 123 LEU B CD2 
826  N  N   . ALA B 40 ? 0.1936 0.1936 0.3656 0.0352  -0.0329 -0.0053 124 ALA B N   
827  C  CA  . ALA B 40 ? 0.1917 0.1761 0.3822 0.0135  -0.0415 0.0048  124 ALA B CA  
828  C  C   . ALA B 40 ? 0.2132 0.1808 0.4011 0.0135  -0.0463 0.0114  124 ALA B C   
829  O  O   . ALA B 40 ? 0.2166 0.2174 0.4219 -0.0058 -0.0348 0.0210  124 ALA B O   
830  C  CB  . ALA B 40 ? 0.2415 0.2263 0.3773 0.0050  -0.0117 -0.0136 124 ALA B CB  
831  N  N   . HIS B 41 ? 0.1822 0.1950 0.4162 0.0216  -0.0345 0.0124  125 HIS B N   
832  C  CA  . HIS B 41 ? 0.1931 0.2121 0.4290 0.0841  -0.0327 0.0334  125 HIS B CA  
833  C  C   . HIS B 41 ? 0.1700 0.2547 0.4467 0.0622  0.0062  0.0670  125 HIS B C   
834  O  O   . HIS B 41 ? 0.2231 0.2646 0.4396 0.0528  0.0225  0.0311  125 HIS B O   
835  C  CB  . HIS B 41 ? 0.2179 0.2343 0.4312 0.0515  -0.0595 0.0105  125 HIS B CB  
836  C  CG  . HIS B 41 ? 0.1867 0.2713 0.4425 0.0015  -0.0684 -0.0001 125 HIS B CG  
837  N  ND1 . HIS B 41 ? 0.2227 0.2465 0.4563 -0.0430 -0.0946 0.0051  125 HIS B ND1 
838  C  CD2 . HIS B 41 ? 0.2798 0.2367 0.4526 0.0943  -0.0615 0.0552  125 HIS B CD2 
839  C  CE1 . HIS B 41 ? 0.2764 0.3481 0.4593 0.1001  -0.1084 0.0431  125 HIS B CE1 
840  N  NE2 . HIS B 41 ? 0.2708 0.2689 0.4598 0.0476  -0.0774 0.0372  125 HIS B NE2 
841  N  N   . SER B 42 ? 0.1946 0.3696 0.4777 0.1024  0.0637  0.0826  126 SER B N   
842  C  CA  . SER B 42 ? 0.2141 0.3363 0.5157 0.1101  0.0760  0.0784  126 SER B CA  
843  C  C   . SER B 42 ? 0.2966 0.2851 0.5505 0.0824  0.0312  0.0795  126 SER B C   
844  O  O   . SER B 42 ? 0.2332 0.4238 0.5632 0.0869  0.0161  0.0950  126 SER B O   
845  C  CB  . SER B 42 ? 0.2533 0.2716 0.5237 0.0474  0.0671  0.0350  126 SER B CB  
846  O  OG  . SER B 42 ? 0.3095 0.3691 0.5224 0.0737  0.0577  0.0112  126 SER B OG  
847  N  N   . LEU B 43 ? 0.3896 0.3222 0.5711 0.1361  0.0434  0.0790  127 LEU B N   
848  C  CA  . LEU B 43 ? 0.2680 0.2282 0.5947 0.0312  0.0671  0.0579  127 LEU B CA  
849  C  C   . LEU B 43 ? 0.4071 0.4357 0.6312 0.1854  0.0709  0.0420  127 LEU B C   
850  O  O   . LEU B 43 ? 0.5328 0.5346 0.6444 0.3090  0.0872  0.0553  127 LEU B O   
851  C  CB  . LEU B 43 ? 0.3311 0.3580 0.5855 0.0970  0.0883  0.0270  127 LEU B CB  
852  C  CG  . LEU B 43 ? 0.3247 0.2641 0.5801 0.0319  0.0805  -0.0185 127 LEU B CG  
853  C  CD1 . LEU B 43 ? 0.3653 0.3722 0.5826 0.0255  0.0820  -0.0214 127 LEU B CD1 
854  C  CD2 . LEU B 43 ? 0.3855 0.3490 0.5796 0.1100  0.0566  -0.0125 127 LEU B CD2 
855  N  N   . SER B 44 ? 0.3388 0.3851 0.6535 0.1247  0.0711  0.0101  128 SER B N   
856  C  CA  . SER B 44 ? 0.2313 0.3454 0.6704 0.0384  0.0287  -0.0607 128 SER B CA  
857  C  C   . SER B 44 ? 0.2352 0.4245 0.6749 0.0466  0.0131  -0.0624 128 SER B C   
858  O  O   . SER B 44 ? 0.3671 0.4126 0.6814 0.1203  0.0237  -0.0664 128 SER B O   
859  C  CB  . SER B 44 ? 0.2630 0.4354 0.6777 0.1351  0.0254  -0.0465 128 SER B CB  
860  O  OG  . SER B 44 ? 0.3933 0.5214 0.6879 0.1753  0.0078  -0.0503 128 SER B OG  
861  N  N   . THR B 45 ? 0.3412 0.3614 0.6710 -0.0079 -0.0086 -0.0861 129 THR B N   
862  C  CA  . THR B 45 ? 0.2165 0.3534 0.6680 -0.0473 -0.0240 -0.0458 129 THR B CA  
863  C  C   . THR B 45 ? 0.1999 0.3258 0.6648 0.0216  -0.0288 0.0053  129 THR B C   
864  O  O   . THR B 45 ? 0.2593 0.4044 0.6644 -0.0022 -0.0476 -0.0248 129 THR B O   
865  C  CB  . THR B 45 ? 0.2375 0.3046 0.6711 0.0085  -0.0217 -0.0778 129 THR B CB  
866  O  OG1 . THR B 45 ? 0.2134 0.3641 0.6782 -0.0021 -0.0226 -0.0799 129 THR B OG1 
867  C  CG2 . THR B 45 ? 0.3492 0.3175 0.6676 0.1260  -0.0063 -0.0540 129 THR B CG2 
868  N  N   . GLY B 46 ? 0.2217 0.2882 0.6587 -0.0145 -0.0469 0.0475  130 GLY B N   
869  C  CA  . GLY B 46 ? 0.3310 0.3444 0.6331 0.1459  -0.0643 0.0876  130 GLY B CA  
870  C  C   . GLY B 46 ? 0.3305 0.3758 0.6528 0.0181  -0.0777 0.1100  130 GLY B C   
871  O  O   . GLY B 46 ? 0.2768 0.4160 0.6485 -0.0495 -0.0902 0.1230  130 GLY B O   
872  N  N   . GLN B 47 ? 0.2551 0.3982 0.6529 0.0520  -0.0680 0.1374  131 GLN B N   
873  C  CA  . GLN B 47 ? 0.2431 0.2858 0.6523 0.0170  -0.0571 0.1045  131 GLN B CA  
874  C  C   . GLN B 47 ? 0.2208 0.3323 0.6387 0.0041  -0.1028 0.1006  131 GLN B C   
875  O  O   . GLN B 47 ? 0.2487 0.2787 0.6387 -0.0053 -0.0848 0.0822  131 GLN B O   
876  C  CB  . GLN B 47 ? 0.2290 0.3932 0.6628 0.0216  -0.0255 0.1003  131 GLN B CB  
877  C  CG  . GLN B 47 ? 0.2785 0.4549 0.6697 0.1494  -0.0339 0.0898  131 GLN B CG  
878  C  CD  . GLN B 47 ? 0.3643 0.4863 0.6784 0.0422  -0.0660 0.0248  131 GLN B CD  
879  O  OE1 . GLN B 47 ? 0.4824 0.4961 0.6841 -0.0220 -0.0787 -0.0216 131 GLN B OE1 
880  N  NE2 . GLN B 47 ? 0.3837 0.5651 0.6864 0.0580  -0.0604 0.0097  131 GLN B NE2 
881  N  N   . THR B 48 ? 0.2363 0.3601 0.6225 0.0108  -0.1243 0.1134  132 THR B N   
882  C  CA  . THR B 48 ? 0.2900 0.2692 0.5855 0.0435  -0.1602 0.0765  132 THR B CA  
883  C  C   . THR B 48 ? 0.3045 0.2469 0.5665 -0.0450 -0.1716 0.0798  132 THR B C   
884  O  O   . THR B 48 ? 0.3153 0.3626 0.5747 -0.1408 -0.1683 0.1374  132 THR B O   
885  C  CB  . THR B 48 ? 0.3496 0.2162 0.5912 -0.0021 -0.2065 0.0489  132 THR B CB  
886  O  OG1 . THR B 48 ? 0.4272 0.2318 0.5925 0.0084  -0.1884 0.0483  132 THR B OG1 
887  C  CG2 . THR B 48 ? 0.4177 0.2089 0.5914 0.0362  -0.1988 0.0278  132 THR B CG2 
888  N  N   . GLY B 49 ? 0.2505 0.2217 0.5315 0.0006  -0.1423 0.0690  133 GLY B N   
889  C  CA  . GLY B 49 ? 0.2091 0.2428 0.4876 0.0104  -0.1386 0.0611  133 GLY B CA  
890  C  C   . GLY B 49 ? 0.2329 0.1975 0.4552 0.0033  -0.0989 0.0212  133 GLY B C   
891  O  O   . GLY B 49 ? 0.1811 0.1983 0.4475 -0.0146 -0.0853 0.0157  133 GLY B O   
892  N  N   . TYR B 50 ? 0.1930 0.2138 0.4266 -0.0275 -0.0690 0.0196  134 TYR B N   
893  C  CA  . TYR B 50 ? 0.1752 0.2094 0.3989 -0.0253 -0.0517 -0.0011 134 TYR B CA  
894  C  C   . TYR B 50 ? 0.2153 0.2264 0.3951 -0.0444 -0.0105 0.0060  134 TYR B C   
895  O  O   . TYR B 50 ? 0.1809 0.1936 0.4083 -0.0108 -0.0339 -0.0028 134 TYR B O   
896  C  CB  . TYR B 50 ? 0.2106 0.2189 0.3868 -0.0060 -0.0593 -0.0042 134 TYR B CB  
897  C  CG  . TYR B 50 ? 0.2616 0.2127 0.3733 -0.0034 -0.0309 0.0061  134 TYR B CG  
898  C  CD1 . TYR B 50 ? 0.3021 0.2125 0.3724 0.0044  0.0049  -0.0067 134 TYR B CD1 
899  C  CD2 . TYR B 50 ? 0.2564 0.1756 0.3700 0.0411  -0.0642 -0.0018 134 TYR B CD2 
900  C  CE1 . TYR B 50 ? 0.2927 0.1759 0.3659 -0.0284 0.0008  -0.0080 134 TYR B CE1 
901  C  CE2 . TYR B 50 ? 0.2787 0.1837 0.3662 0.0206  -0.0352 -0.0021 134 TYR B CE2 
902  C  CZ  . TYR B 50 ? 0.3031 0.1970 0.3636 -0.0003 -0.0053 0.0145  134 TYR B CZ  
903  O  OH  . TYR B 50 ? 0.3151 0.2645 0.3667 0.0279  0.0012  0.0175  134 TYR B OH  
904  N  N   . ILE B 51 ? 0.2007 0.1807 0.3747 -0.0010 -0.0385 -0.0255 135 ILE B N   
905  C  CA  . ILE B 51 ? 0.2233 0.1875 0.3682 -0.0260 -0.0087 -0.0387 135 ILE B CA  
906  C  C   . ILE B 51 ? 0.1990 0.2330 0.3643 0.0288  -0.0179 -0.0234 135 ILE B C   
907  O  O   . ILE B 51 ? 0.2139 0.1811 0.3514 0.0239  -0.0285 -0.0179 135 ILE B O   
908  C  CB  . ILE B 51 ? 0.2045 0.2072 0.3821 -0.0425 0.0250  -0.0150 135 ILE B CB  
909  C  CG1 . ILE B 51 ? 0.2740 0.1944 0.3921 -0.0366 0.0584  -0.0167 135 ILE B CG1 
910  C  CG2 . ILE B 51 ? 0.2068 0.2612 0.3807 0.0482  -0.0271 -0.0402 135 ILE B CG2 
911  C  CD1 . ILE B 51 ? 0.3517 0.2546 0.4034 -0.0859 0.0556  -0.0340 135 ILE B CD1 
912  N  N   . PRO B 52 ? 0.2006 0.2393 0.3681 -0.0148 0.0114  0.0096  136 PRO B N   
913  C  CA  . PRO B 52 ? 0.2134 0.2571 0.3765 0.0023  0.0120  0.0250  136 PRO B CA  
914  C  C   . PRO B 52 ? 0.2805 0.2349 0.3925 -0.0372 -0.0456 0.0176  136 PRO B C   
915  O  O   . PRO B 52 ? 0.3486 0.2190 0.3971 0.0164  -0.0859 -0.0175 136 PRO B O   
916  C  CB  . PRO B 52 ? 0.2650 0.3255 0.3720 0.0315  0.0581  0.0896  136 PRO B CB  
917  C  CG  . PRO B 52 ? 0.2845 0.3588 0.3772 -0.0102 0.0320  0.0435  136 PRO B CG  
918  C  CD  . PRO B 52 ? 0.2076 0.2542 0.3793 -0.0233 0.0419  0.0272  136 PRO B CD  
919  N  N   . SER B 53 ? 0.2674 0.2534 0.4087 -0.0491 -0.0698 -0.0302 137 SER B N   
920  C  CA  . SER B 53 ? 0.3408 0.2872 0.4259 -0.0473 -0.0814 -0.0148 137 SER B CA  
921  C  C   . SER B 53 ? 0.3583 0.2858 0.4328 -0.0537 -0.1206 -0.0164 137 SER B C   
922  O  O   . SER B 53 ? 0.4313 0.3783 0.4495 -0.0887 -0.1546 -0.0422 137 SER B O   
923  C  CB  . SER B 53 ? 0.3201 0.3789 0.4395 -0.1034 -0.0278 0.0217  137 SER B CB  
924  O  OG  . SER B 53 ? 0.2801 0.4556 0.4544 -0.0239 -0.0066 0.0193  137 SER B OG  
925  N  N   . ASN B 54 ? 0.3488 0.2942 0.4218 0.0408  -0.0786 -0.0125 138 ASN B N   
926  C  CA  . ASN B 54 ? 0.4209 0.2767 0.4196 0.0362  -0.0784 -0.0232 138 ASN B CA  
927  C  C   . ASN B 54 ? 0.4211 0.3201 0.4160 0.0640  -0.1053 -0.0460 138 ASN B C   
928  O  O   . ASN B 54 ? 0.4544 0.3824 0.4155 0.0830  -0.0907 -0.0802 138 ASN B O   
929  C  CB  . ASN B 54 ? 0.5213 0.2926 0.4223 0.0291  -0.0664 0.0021  138 ASN B CB  
930  C  CG  . ASN B 54 ? 0.5796 0.3663 0.4259 0.0675  -0.0605 0.0526  138 ASN B CG  
931  O  OD1 . ASN B 54 ? 0.6338 0.3615 0.4273 0.0952  -0.0393 0.0742  138 ASN B OD1 
932  N  ND2 . ASN B 54 ? 0.6575 0.5104 0.4331 0.0728  -0.0391 0.0744  138 ASN B ND2 
933  N  N   . TYR B 55 ? 0.3804 0.2903 0.4118 0.0794  -0.1219 -0.0294 139 TYR B N   
934  C  CA  . TYR B 55 ? 0.3350 0.3379 0.4131 0.0668  -0.1100 -0.0182 139 TYR B CA  
935  C  C   . TYR B 55 ? 0.2530 0.3276 0.4186 0.0362  -0.1189 -0.0445 139 TYR B C   
936  O  O   . TYR B 55 ? 0.2604 0.3477 0.4161 0.0376  -0.1019 -0.0335 139 TYR B O   
937  C  CB  . TYR B 55 ? 0.3499 0.3186 0.4085 0.0198  -0.0863 -0.0134 139 TYR B CB  
938  C  CG  . TYR B 55 ? 0.4092 0.3311 0.4019 0.0753  -0.0563 0.0058  139 TYR B CG  
939  C  CD1 . TYR B 55 ? 0.4463 0.3268 0.3973 0.0331  -0.0482 0.0278  139 TYR B CD1 
940  C  CD2 . TYR B 55 ? 0.3390 0.3243 0.3973 -0.0718 -0.0357 -0.0047 139 TYR B CD2 
941  C  CE1 . TYR B 55 ? 0.5156 0.3240 0.3948 0.0085  -0.0296 0.0298  139 TYR B CE1 
942  C  CE2 . TYR B 55 ? 0.4885 0.3641 0.3988 0.0269  -0.0268 0.0056  139 TYR B CE2 
943  C  CZ  . TYR B 55 ? 0.5073 0.3594 0.3961 0.0138  -0.0265 0.0350  139 TYR B CZ  
944  O  OH  . TYR B 55 ? 0.6041 0.4835 0.4001 0.0202  -0.0034 0.0644  139 TYR B OH  
945  N  N   . VAL B 56 ? 0.3105 0.2877 0.4323 0.0032  -0.1112 -0.0639 140 VAL B N   
946  C  CA  . VAL B 56 ? 0.2738 0.2841 0.4489 -0.0157 -0.1078 -0.0661 140 VAL B CA  
947  C  C   . VAL B 56 ? 0.3271 0.3075 0.4689 0.0656  -0.1166 -0.0901 140 VAL B C   
948  O  O   . VAL B 56 ? 0.3007 0.3347 0.4812 0.0757  -0.1336 -0.0886 140 VAL B O   
949  C  CB  . VAL B 56 ? 0.2757 0.2967 0.4474 0.0491  -0.1060 -0.0916 140 VAL B CB  
950  C  CG1 . VAL B 56 ? 0.2723 0.3271 0.4495 0.0640  -0.0772 -0.0998 140 VAL B CG1 
951  C  CG2 . VAL B 56 ? 0.2957 0.2879 0.4532 0.0420  -0.0963 -0.0894 140 VAL B CG2 
952  N  N   . ALA B 57 ? 0.3316 0.2997 0.4732 0.0325  -0.1072 -0.1066 141 ALA B N   
953  C  CA  . ALA B 57 ? 0.2999 0.3455 0.4782 0.0076  -0.1142 -0.1476 141 ALA B CA  
954  C  C   . ALA B 57 ? 0.3068 0.3757 0.4902 -0.0459 -0.0756 -0.1514 141 ALA B C   
955  O  O   . ALA B 57 ? 0.2925 0.3843 0.4855 0.0016  -0.0613 -0.1451 141 ALA B O   
956  C  CB  . ALA B 57 ? 0.3317 0.3958 0.4736 0.0411  -0.1355 -0.1498 141 ALA B CB  
957  N  N   . PRO B 58 ? 0.3066 0.4417 0.5032 -0.0801 -0.0489 -0.1600 142 PRO B N   
958  C  CA  . PRO B 58 ? 0.3485 0.4653 0.5133 -0.1344 -0.0256 -0.1189 142 PRO B CA  
959  C  C   . PRO B 58 ? 0.4765 0.4186 0.5230 -0.1281 -0.0036 -0.1021 142 PRO B C   
960  O  O   . PRO B 58 ? 0.5302 0.4094 0.5131 -0.1086 -0.0276 -0.1176 142 PRO B O   
961  C  CB  . PRO B 58 ? 0.3234 0.5229 0.5159 -0.1236 -0.0397 -0.1366 142 PRO B CB  
962  C  CG  . PRO B 58 ? 0.3234 0.5540 0.5139 0.0066  -0.0405 -0.1608 142 PRO B CG  
963  C  CD  . PRO B 58 ? 0.3164 0.5594 0.5083 -0.0412 -0.0587 -0.1670 142 PRO B CD  
964  N  N   . SER B 59 ? 0.5171 0.4344 0.5425 -0.1452 0.0299  -0.0832 143 SER B N   
965  C  CA  . SER B 59 ? 0.6297 0.4809 0.5636 -0.1173 0.0280  -0.1100 143 SER B CA  
966  C  C   . SER B 59 ? 0.7414 0.5587 0.5846 -0.0702 0.0118  -0.0743 143 SER B C   
967  O  O   . SER B 59 ? 0.8172 0.6180 0.5926 0.0082  -0.0099 -0.0653 143 SER B O   
968  C  CB  . SER B 59 ? 0.6219 0.5141 0.5653 -0.0789 0.0451  -0.1432 143 SER B CB  
969  O  OG  . SER B 59 ? 0.6733 0.5678 0.5678 0.0345  0.0576  -0.1448 143 SER B OG  
970  O  OXT . SER B 59 ? 0.7755 0.5464 0.5979 -0.1092 0.0005  -0.0370 143 SER B OXT 
971  N  N   . GLY C 1  ? 0.5662 0.3622 0.4616 0.0266  0.0096  0.0234  85  GLY C N   
972  C  CA  . GLY C 1  ? 0.4900 0.3533 0.4522 0.0188  0.0201  -0.0058 85  GLY C CA  
973  C  C   . GLY C 1  ? 0.3691 0.3362 0.4342 0.0159  0.0388  -0.0321 85  GLY C C   
974  O  O   . GLY C 1  ? 0.4874 0.4281 0.4428 -0.0332 0.0321  0.0059  85  GLY C O   
975  N  N   . VAL C 2  ? 0.2619 0.4005 0.4143 -0.0879 0.0372  -0.0650 86  VAL C N   
976  C  CA  . VAL C 2  ? 0.3205 0.3199 0.3989 -0.0302 -0.0092 -0.0265 86  VAL C CA  
977  C  C   . VAL C 2  ? 0.2643 0.3439 0.3683 -0.0732 0.0133  -0.0306 86  VAL C C   
978  O  O   . VAL C 2  ? 0.2850 0.4162 0.3623 -0.0335 0.0364  -0.0374 86  VAL C O   
979  C  CB  . VAL C 2  ? 0.4007 0.3230 0.4141 -0.0137 -0.0459 -0.0107 86  VAL C CB  
980  C  CG1 . VAL C 2  ? 0.3985 0.2609 0.4212 0.0964  -0.0124 -0.0262 86  VAL C CG1 
981  C  CG2 . VAL C 2  ? 0.3904 0.3825 0.4129 -0.0420 -0.1043 0.0139  86  VAL C CG2 
982  N  N   . THR C 3  ? 0.2561 0.2706 0.3499 0.0010  0.0092  -0.0373 87  THR C N   
983  C  CA  . THR C 3  ? 0.2613 0.2238 0.3421 -0.0337 0.0279  -0.0310 87  THR C CA  
984  C  C   . THR C 3  ? 0.2091 0.2418 0.3294 -0.0151 0.0132  -0.0262 87  THR C C   
985  O  O   . THR C 3  ? 0.2353 0.2808 0.3296 0.0106  0.0586  -0.0092 87  THR C O   
986  C  CB  . THR C 3  ? 0.3239 0.2133 0.3538 0.0289  0.0406  -0.0181 87  THR C CB  
987  O  OG1 . THR C 3  ? 0.3462 0.2872 0.3711 0.0152  0.0422  0.0167  87  THR C OG1 
988  C  CG2 . THR C 3  ? 0.2826 0.3371 0.3595 0.0347  -0.0010 -0.0147 87  THR C CG2 
989  N  N   . THR C 4  ? 0.1979 0.2700 0.3237 -0.0185 -0.0242 -0.0211 88  THR C N   
990  C  CA  . THR C 4  ? 0.2095 0.2203 0.3178 -0.0251 -0.0129 0.0230  88  THR C CA  
991  C  C   . THR C 4  ? 0.1756 0.3514 0.3198 0.0165  -0.0122 -0.0067 88  THR C C   
992  O  O   . THR C 4  ? 0.2155 0.2780 0.3205 -0.0233 0.0092  -0.0324 88  THR C O   
993  C  CB  . THR C 4  ? 0.2367 0.2661 0.3258 -0.0057 0.0124  0.0460  88  THR C CB  
994  O  OG1 . THR C 4  ? 0.2471 0.3224 0.3251 -0.0035 -0.0137 0.0207  88  THR C OG1 
995  C  CG2 . THR C 4  ? 0.3165 0.2417 0.3298 0.0372  0.0173  0.0304  88  THR C CG2 
996  N  N   . PHE C 5  ? 0.2106 0.2087 0.3153 -0.0492 0.0034  -0.0036 89  PHE C N   
997  C  CA  . PHE C 5  ? 0.1763 0.2112 0.3165 -0.0195 -0.0047 0.0202  89  PHE C CA  
998  C  C   . PHE C 5  ? 0.1802 0.1890 0.3227 -0.0117 -0.0172 -0.0060 89  PHE C C   
999  O  O   . PHE C 5  ? 0.1887 0.2540 0.3312 0.0300  -0.0103 0.0102  89  PHE C O   
1000 C  CB  . PHE C 5  ? 0.1843 0.2239 0.3189 -0.0037 0.0256  0.0732  89  PHE C CB  
1001 C  CG  . PHE C 5  ? 0.2130 0.2515 0.3184 0.0510  0.0388  0.0522  89  PHE C CG  
1002 C  CD1 . PHE C 5  ? 0.2877 0.2178 0.3321 0.0290  0.0340  0.0239  89  PHE C CD1 
1003 C  CD2 . PHE C 5  ? 0.2404 0.2697 0.3277 0.0111  0.0149  0.0408  89  PHE C CD2 
1004 C  CE1 . PHE C 5  ? 0.2672 0.2737 0.3354 0.0367  0.0237  0.0519  89  PHE C CE1 
1005 C  CE2 . PHE C 5  ? 0.2698 0.3016 0.3307 0.0123  0.0080  0.0254  89  PHE C CE2 
1006 C  CZ  . PHE C 5  ? 0.2743 0.3234 0.3325 0.0544  0.0323  0.0517  89  PHE C CZ  
1007 N  N   . VAL C 6  ? 0.1777 0.1985 0.3260 -0.0021 -0.0064 -0.0046 90  VAL C N   
1008 C  CA  . VAL C 6  ? 0.2098 0.2050 0.3393 -0.0281 -0.0105 0.0026  90  VAL C CA  
1009 C  C   . VAL C 6  ? 0.1973 0.2445 0.3316 0.0206  -0.0211 0.0232  90  VAL C C   
1010 O  O   . VAL C 6  ? 0.2120 0.2733 0.3322 0.0113  -0.0020 -0.0194 90  VAL C O   
1011 C  CB  . VAL C 6  ? 0.1825 0.2348 0.3608 -0.0522 -0.0307 -0.0011 90  VAL C CB  
1012 C  CG1 . VAL C 6  ? 0.1952 0.2609 0.3718 -0.0079 -0.0043 -0.0029 90  VAL C CG1 
1013 C  CG2 . VAL C 6  ? 0.2499 0.2535 0.3697 -0.0394 -0.0126 -0.0080 90  VAL C CG2 
1014 N  N   . ALA C 7  ? 0.2102 0.2511 0.3248 0.0363  -0.0363 -0.0185 91  ALA C N   
1015 C  CA  . ALA C 7  ? 0.2704 0.2487 0.3312 0.0178  -0.0245 -0.0315 91  ALA C CA  
1016 C  C   . ALA C 7  ? 0.2475 0.3252 0.3492 0.0120  -0.0265 -0.0040 91  ALA C C   
1017 O  O   . ALA C 7  ? 0.2758 0.3002 0.3587 -0.0051 -0.0116 -0.0144 91  ALA C O   
1018 C  CB  . ALA C 7  ? 0.2413 0.2635 0.3340 -0.0066 -0.0111 -0.0122 91  ALA C CB  
1019 N  N   . LEU C 8  ? 0.2206 0.3405 0.3580 -0.0029 -0.0431 -0.0226 92  LEU C N   
1020 C  CA  . LEU C 8  ? 0.2339 0.3301 0.3746 -0.0137 -0.0328 -0.0386 92  LEU C CA  
1021 C  C   . LEU C 8  ? 0.2525 0.3329 0.3908 -0.0118 -0.0091 -0.0398 92  LEU C C   
1022 O  O   . LEU C 8  ? 0.2478 0.3739 0.3912 -0.0508 -0.0086 -0.0431 92  LEU C O   
1023 C  CB  . LEU C 8  ? 0.2504 0.3460 0.3774 0.0247  -0.0432 -0.0266 92  LEU C CB  
1024 C  CG  . LEU C 8  ? 0.2923 0.3748 0.3912 0.0123  -0.0244 0.0017  92  LEU C CG  
1025 C  CD1 . LEU C 8  ? 0.2264 0.5062 0.4016 0.0471  -0.0408 0.0287  92  LEU C CD1 
1026 C  CD2 . LEU C 8  ? 0.3278 0.3755 0.4061 -0.0395 0.0102  -0.0249 92  LEU C CD2 
1027 N  N   . TYR C 9  ? 0.2420 0.3701 0.3945 0.0112  -0.0084 -0.0498 93  TYR C N   
1028 C  CA  . TYR C 9  ? 0.2619 0.4109 0.3918 0.0282  -0.0227 -0.0467 93  TYR C CA  
1029 C  C   . TYR C 9  ? 0.2250 0.3260 0.3865 -0.0137 -0.0398 -0.0604 93  TYR C C   
1030 O  O   . TYR C 9  ? 0.2898 0.3579 0.3840 -0.0295 -0.0543 -0.0855 93  TYR C O   
1031 C  CB  . TYR C 9  ? 0.3414 0.4310 0.3989 0.0057  -0.0514 -0.0433 93  TYR C CB  
1032 C  CG  . TYR C 9  ? 0.3643 0.4622 0.4076 -0.0007 -0.0678 -0.0220 93  TYR C CG  
1033 C  CD1 . TYR C 9  ? 0.4037 0.5603 0.4200 0.0181  -0.0874 -0.0072 93  TYR C CD1 
1034 C  CD2 . TYR C 9  ? 0.3555 0.4840 0.4106 0.0208  -0.0800 -0.0085 93  TYR C CD2 
1035 C  CE1 . TYR C 9  ? 0.4214 0.6338 0.4296 0.1210  -0.0759 -0.0006 93  TYR C CE1 
1036 C  CE2 . TYR C 9  ? 0.4166 0.5386 0.4200 0.1088  -0.1098 0.0007  93  TYR C CE2 
1037 C  CZ  . TYR C 9  ? 0.4559 0.6273 0.4325 0.1476  -0.0926 0.0127  93  TYR C CZ  
1038 O  OH  . TYR C 9  ? 0.4755 0.7624 0.4454 0.2254  -0.0876 0.0007  93  TYR C OH  
1039 N  N   . ASP C 10 ? 0.2728 0.3734 0.3866 0.0061  -0.0028 -0.0533 94  ASP C N   
1040 C  CA  . ASP C 10 ? 0.2883 0.3603 0.3819 -0.0287 -0.0080 -0.0582 94  ASP C CA  
1041 C  C   . ASP C 10 ? 0.3195 0.3873 0.3635 -0.0380 -0.0048 -0.0466 94  ASP C C   
1042 O  O   . ASP C 10 ? 0.3270 0.4307 0.3587 -0.0111 -0.0104 -0.0518 94  ASP C O   
1043 C  CB  . ASP C 10 ? 0.3797 0.3186 0.3896 -0.0009 -0.0162 -0.0954 94  ASP C CB  
1044 C  CG  . ASP C 10 ? 0.4649 0.3688 0.4021 -0.0174 -0.0172 -0.1016 94  ASP C CG  
1045 O  OD1 . ASP C 10 ? 0.4389 0.3870 0.4013 -0.0654 -0.0199 -0.0692 94  ASP C OD1 
1046 O  OD2 . ASP C 10 ? 0.5652 0.4153 0.4131 -0.0333 -0.0112 -0.1153 94  ASP C OD2 
1047 N  N   . TYR C 11 ? 0.2546 0.3346 0.3533 -0.0285 -0.0143 -0.0650 95  TYR C N   
1048 C  CA  . TYR C 11 ? 0.2974 0.3277 0.3416 0.0030  -0.0067 -0.0449 95  TYR C CA  
1049 C  C   . TYR C 11 ? 0.3182 0.3244 0.3327 -0.0035 -0.0122 -0.0370 95  TYR C C   
1050 O  O   . TYR C 11 ? 0.2895 0.4033 0.3248 0.0055  -0.0071 -0.0167 95  TYR C O   
1051 C  CB  . TYR C 11 ? 0.2805 0.3335 0.3439 -0.0030 0.0002  -0.0259 95  TYR C CB  
1052 C  CG  . TYR C 11 ? 0.2844 0.3232 0.3373 -0.0122 -0.0299 -0.0174 95  TYR C CG  
1053 C  CD1 . TYR C 11 ? 0.3060 0.3615 0.3414 -0.0116 -0.0350 -0.0081 95  TYR C CD1 
1054 C  CD2 . TYR C 11 ? 0.3008 0.3229 0.3340 -0.0169 0.0024  -0.0163 95  TYR C CD2 
1055 C  CE1 . TYR C 11 ? 0.2797 0.3757 0.3373 -0.0240 -0.0230 0.0028  95  TYR C CE1 
1056 C  CE2 . TYR C 11 ? 0.2877 0.3220 0.3293 0.0167  -0.0126 -0.0072 95  TYR C CE2 
1057 C  CZ  . TYR C 11 ? 0.3425 0.3557 0.3357 0.0073  -0.0088 -0.0102 95  TYR C CZ  
1058 O  OH  . TYR C 11 ? 0.3626 0.3706 0.3375 0.0168  0.0243  0.0026  95  TYR C OH  
1059 N  N   . GLU C 12 ? 0.3315 0.3319 0.3302 -0.0053 0.0097  -0.0419 96  GLU C N   
1060 C  CA  . GLU C 12 ? 0.3301 0.3183 0.3325 -0.0270 -0.0041 -0.0661 96  GLU C CA  
1061 C  C   . GLU C 12 ? 0.3195 0.2735 0.3153 -0.0347 -0.0177 -0.0490 96  GLU C C   
1062 O  O   . GLU C 12 ? 0.3803 0.3424 0.3192 0.0126  -0.0465 0.0162  96  GLU C O   
1063 C  CB  . GLU C 12 ? 0.4754 0.3716 0.3585 0.0426  -0.0204 -0.0956 96  GLU C CB  
1064 C  CG  . GLU C 12 ? 0.6240 0.5089 0.3874 0.0952  -0.0342 -0.0777 96  GLU C CG  
1065 C  CD  . GLU C 12 ? 0.7566 0.7341 0.4191 0.1860  -0.0286 -0.0586 96  GLU C CD  
1066 O  OE1 . GLU C 12 ? 0.8150 0.7358 0.4240 0.1821  -0.0193 -0.0425 96  GLU C OE1 
1067 O  OE2 . GLU C 12 ? 0.7635 0.8408 0.4377 0.2115  -0.0253 -0.0610 96  GLU C OE2 
1068 N  N   . SER C 13 ? 0.3003 0.2910 0.3044 -0.0365 0.0258  -0.0201 97  SER C N   
1069 C  CA  . SER C 13 ? 0.3087 0.3106 0.3055 -0.0477 0.0322  -0.0348 97  SER C CA  
1070 C  C   . SER C 13 ? 0.2845 0.2846 0.2998 -0.0002 0.0139  -0.0190 97  SER C C   
1071 O  O   . SER C 13 ? 0.3606 0.3103 0.3143 -0.0144 0.0292  0.0013  97  SER C O   
1072 C  CB  . SER C 13 ? 0.3697 0.3826 0.3182 -0.0126 0.0076  -0.0507 97  SER C CB  
1073 O  OG  . SER C 13 ? 0.3750 0.4643 0.3286 0.0652  -0.0096 -0.0580 97  SER C OG  
1074 N  N   . ARG C 14 ? 0.2806 0.3160 0.2847 -0.0180 0.0150  -0.0388 98  ARG C N   
1075 C  CA  . ARG C 14 ? 0.2585 0.3315 0.2740 -0.0206 0.0269  -0.0277 98  ARG C CA  
1076 C  C   . ARG C 14 ? 0.2573 0.3423 0.2804 -0.0080 0.0012  -0.0715 98  ARG C C   
1077 O  O   . ARG C 14 ? 0.2970 0.3996 0.2819 0.0230  0.0105  -0.0528 98  ARG C O   
1078 C  CB  . ARG C 14 ? 0.2995 0.3623 0.2716 0.0314  -0.0143 -0.0303 98  ARG C CB  
1079 C  CG  . ARG C 14 ? 0.2677 0.3181 0.2597 0.0210  -0.0126 -0.0558 98  ARG C CG  
1080 C  CD  . ARG C 14 ? 0.3113 0.3080 0.2552 0.0534  0.0107  -0.0286 98  ARG C CD  
1081 N  NE  . ARG C 14 ? 0.3086 0.3395 0.2584 0.0076  -0.0004 -0.0355 98  ARG C NE  
1082 C  CZ  . ARG C 14 ? 0.3302 0.2945 0.2632 -0.0161 -0.0153 -0.0171 98  ARG C CZ  
1083 N  NH1 . ARG C 14 ? 0.3482 0.3245 0.2693 -0.0048 -0.0191 0.0416  98  ARG C NH1 
1084 N  NH2 . ARG C 14 ? 0.3030 0.3742 0.2627 -0.0053 -0.0344 -0.0093 98  ARG C NH2 
1085 N  N   . THR C 15 ? 0.2432 0.3804 0.2918 0.0274  -0.0263 -0.0735 99  THR C N   
1086 C  CA  . THR C 15 ? 0.2834 0.4090 0.3100 0.0168  -0.0265 -0.0751 99  THR C CA  
1087 C  C   . THR C 15 ? 0.3020 0.4009 0.3091 0.0395  -0.0330 -0.0747 99  THR C C   
1088 O  O   . THR C 15 ? 0.3261 0.3391 0.3091 0.0088  -0.0208 -0.0620 99  THR C O   
1089 C  CB  . THR C 15 ? 0.3348 0.3812 0.3373 -0.0086 -0.0159 -0.0683 99  THR C CB  
1090 O  OG1 . THR C 15 ? 0.3708 0.4232 0.3770 -0.0339 -0.0024 -0.0432 99  THR C OG1 
1091 C  CG2 . THR C 15 ? 0.3245 0.4356 0.3328 -0.0111 -0.0043 -0.0975 99  THR C CG2 
1092 N  N   . GLU C 16 ? 0.3551 0.4328 0.3121 0.0812  -0.0663 -0.0982 100 GLU C N   
1093 C  CA  . GLU C 16 ? 0.3873 0.4266 0.3279 0.1183  -0.0876 -0.1145 100 GLU C CA  
1094 C  C   . GLU C 16 ? 0.3275 0.3835 0.3257 0.0757  -0.0575 -0.0686 100 GLU C C   
1095 O  O   . GLU C 16 ? 0.4362 0.3926 0.3255 0.0837  -0.0927 -0.0660 100 GLU C O   
1096 C  CB  . GLU C 16 ? 0.4405 0.5224 0.3530 0.1699  -0.1138 -0.1451 100 GLU C CB  
1097 C  CG  . GLU C 16 ? 0.6091 0.6600 0.3791 0.2232  -0.1125 -0.1547 100 GLU C CG  
1098 C  CD  . GLU C 16 ? 0.7962 0.8370 0.4042 0.2324  -0.1168 -0.1311 100 GLU C CD  
1099 O  OE1 . GLU C 16 ? 0.8682 0.8961 0.4134 0.2340  -0.1166 -0.1064 100 GLU C OE1 
1100 O  OE2 . GLU C 16 ? 0.8595 0.9211 0.4199 0.2266  -0.0975 -0.1071 100 GLU C OE2 
1101 N  N   . THR C 17 ? 0.3155 0.3134 0.3161 0.0430  -0.0200 -0.0658 101 THR C N   
1102 C  CA  . THR C 17 ? 0.2609 0.3319 0.3024 -0.0086 0.0127  -0.0405 101 THR C CA  
1103 C  C   . THR C 17 ? 0.2268 0.3116 0.2890 -0.0073 0.0089  -0.0225 101 THR C C   
1104 O  O   . THR C 17 ? 0.3138 0.3080 0.2874 0.0239  0.0429  -0.0256 101 THR C O   
1105 C  CB  . THR C 17 ? 0.2322 0.3638 0.2966 -0.0088 0.0410  0.0067  101 THR C CB  
1106 O  OG1 . THR C 17 ? 0.3235 0.3871 0.2954 0.0308  0.0191  0.0154  101 THR C OG1 
1107 C  CG2 . THR C 17 ? 0.2609 0.3647 0.3089 0.0057  0.0059  -0.0393 101 THR C CG2 
1108 N  N   . ASP C 18 ? 0.2579 0.3192 0.2716 -0.0112 -0.0255 -0.0362 102 ASP C N   
1109 C  CA  . ASP C 18 ? 0.2337 0.3440 0.2694 0.0302  -0.0193 -0.0112 102 ASP C CA  
1110 C  C   . ASP C 18 ? 0.2664 0.3041 0.2769 0.0176  -0.0024 -0.0093 102 ASP C C   
1111 O  O   . ASP C 18 ? 0.3641 0.2957 0.2865 0.0123  -0.0005 -0.0234 102 ASP C O   
1112 C  CB  . ASP C 18 ? 0.2494 0.2965 0.2655 0.0156  -0.0237 0.0007  102 ASP C CB  
1113 C  CG  . ASP C 18 ? 0.2665 0.3182 0.2615 -0.0165 -0.0074 0.0062  102 ASP C CG  
1114 O  OD1 . ASP C 18 ? 0.3216 0.3237 0.2669 0.0018  -0.0050 0.0171  102 ASP C OD1 
1115 O  OD2 . ASP C 18 ? 0.3045 0.3048 0.2602 0.0231  0.0107  0.0270  102 ASP C OD2 
1116 N  N   . LEU C 19 ? 0.2573 0.2625 0.2769 0.0017  0.0030  -0.0102 103 LEU C N   
1117 C  CA  . LEU C 19 ? 0.2620 0.2427 0.2791 -0.0129 -0.0022 -0.0252 103 LEU C CA  
1118 C  C   . LEU C 19 ? 0.3014 0.2832 0.2878 -0.0062 -0.0183 -0.0259 103 LEU C C   
1119 O  O   . LEU C 19 ? 0.2834 0.3564 0.3027 0.0069  -0.0422 -0.0209 103 LEU C O   
1120 C  CB  . LEU C 19 ? 0.3111 0.2356 0.2888 0.0296  0.0038  -0.0561 103 LEU C CB  
1121 C  CG  . LEU C 19 ? 0.2864 0.3086 0.3059 0.0204  -0.0278 -0.0626 103 LEU C CG  
1122 C  CD1 . LEU C 19 ? 0.3258 0.3251 0.3040 0.0185  0.0252  -0.0157 103 LEU C CD1 
1123 C  CD2 . LEU C 19 ? 0.3535 0.3857 0.3163 0.1125  -0.0637 -0.0658 103 LEU C CD2 
1124 N  N   . SER C 20 ? 0.2821 0.2678 0.2812 -0.0206 -0.0049 -0.0112 104 SER C N   
1125 C  CA  . SER C 20 ? 0.2883 0.2551 0.2833 -0.0012 0.0133  -0.0437 104 SER C CA  
1126 C  C   . SER C 20 ? 0.2605 0.3136 0.3013 -0.0136 -0.0012 -0.0093 104 SER C C   
1127 O  O   . SER C 20 ? 0.3001 0.4127 0.3151 -0.0669 -0.0210 -0.0167 104 SER C O   
1128 C  CB  . SER C 20 ? 0.3748 0.2681 0.2753 0.0643  0.0372  -0.0483 104 SER C CB  
1129 O  OG  . SER C 20 ? 0.3760 0.3740 0.2769 0.0405  0.0523  -0.0208 104 SER C OG  
1130 N  N   . PHE C 21 ? 0.2538 0.2634 0.3110 -0.0265 0.0069  -0.0085 105 PHE C N   
1131 C  CA  . PHE C 21 ? 0.2522 0.2730 0.3131 -0.0374 0.0037  -0.0157 105 PHE C CA  
1132 C  C   . PHE C 21 ? 0.2741 0.3263 0.3365 -0.0192 0.0059  -0.0275 105 PHE C C   
1133 O  O   . PHE C 21 ? 0.3215 0.3125 0.3302 0.0270  -0.0249 -0.0287 105 PHE C O   
1134 C  CB  . PHE C 21 ? 0.2986 0.2320 0.3005 0.0285  -0.0070 -0.0282 105 PHE C CB  
1135 C  CG  . PHE C 21 ? 0.2619 0.2587 0.3055 -0.0406 -0.0199 -0.0382 105 PHE C CG  
1136 C  CD1 . PHE C 21 ? 0.2647 0.2800 0.3062 0.0214  -0.0405 -0.0291 105 PHE C CD1 
1137 C  CD2 . PHE C 21 ? 0.3181 0.2450 0.3087 -0.0200 -0.0127 -0.0244 105 PHE C CD2 
1138 C  CE1 . PHE C 21 ? 0.2774 0.2579 0.3087 0.0337  -0.0195 -0.0098 105 PHE C CE1 
1139 C  CE2 . PHE C 21 ? 0.2767 0.2784 0.3120 -0.0228 -0.0435 -0.0133 105 PHE C CE2 
1140 C  CZ  . PHE C 21 ? 0.2719 0.2957 0.3127 -0.0673 -0.0371 -0.0138 105 PHE C CZ  
1141 N  N   . LYS C 22 ? 0.2924 0.2764 0.3617 -0.0486 -0.0050 -0.0449 106 LYS C N   
1142 C  CA  . LYS C 22 ? 0.2855 0.2717 0.3920 -0.0666 -0.0036 -0.0287 106 LYS C CA  
1143 C  C   . LYS C 22 ? 0.2820 0.2670 0.3965 -0.0499 -0.0048 -0.0215 106 LYS C C   
1144 O  O   . LYS C 22 ? 0.2579 0.2505 0.3990 -0.0270 -0.0200 -0.0474 106 LYS C O   
1145 C  CB  . LYS C 22 ? 0.3265 0.2783 0.4164 -0.0036 0.0262  -0.0174 106 LYS C CB  
1146 C  CG  . LYS C 22 ? 0.4008 0.3931 0.4402 0.0598  0.0279  -0.0096 106 LYS C CG  
1147 C  CD  . LYS C 22 ? 0.5302 0.5345 0.4653 0.1243  -0.0101 -0.0091 106 LYS C CD  
1148 C  CE  . LYS C 22 ? 0.5623 0.6555 0.4864 0.1193  -0.0181 -0.0081 106 LYS C CE  
1149 N  NZ  . LYS C 22 ? 0.6334 0.7334 0.5010 0.1198  -0.0219 0.0048  106 LYS C NZ  
1150 N  N   . LYS C 23 ? 0.2698 0.2812 0.4066 -0.0890 -0.0153 -0.0139 107 LYS C N   
1151 C  CA  . LYS C 23 ? 0.2463 0.3530 0.4211 -0.0823 -0.0442 -0.0118 107 LYS C CA  
1152 C  C   . LYS C 23 ? 0.2645 0.2543 0.4118 -0.0458 -0.0455 -0.0270 107 LYS C C   
1153 O  O   . LYS C 23 ? 0.2894 0.3077 0.4225 -0.0183 -0.0318 0.0039  107 LYS C O   
1154 C  CB  . LYS C 23 ? 0.3093 0.2956 0.4366 -0.0626 -0.0479 -0.0145 107 LYS C CB  
1155 C  CG  . LYS C 23 ? 0.3512 0.3696 0.4483 -0.1013 -0.0709 0.0010  107 LYS C CG  
1156 C  CD  . LYS C 23 ? 0.3436 0.5064 0.4534 -0.1431 -0.1092 -0.0550 107 LYS C CD  
1157 C  CE  . LYS C 23 ? 0.5324 0.6092 0.4683 0.0641  -0.0545 -0.0213 107 LYS C CE  
1158 N  NZ  . LYS C 23 ? 0.6045 0.6952 0.4761 0.0944  -0.0335 0.0016  107 LYS C NZ  
1159 N  N   . GLY C 24 ? 0.2680 0.2586 0.3942 -0.0635 -0.0382 -0.0289 108 GLY C N   
1160 C  CA  . GLY C 24 ? 0.2892 0.2683 0.3827 -0.0320 -0.0501 -0.0177 108 GLY C CA  
1161 C  C   . GLY C 24 ? 0.2580 0.2406 0.3789 -0.0245 -0.0332 -0.0041 108 GLY C C   
1162 O  O   . GLY C 24 ? 0.3005 0.2814 0.3848 -0.0203 -0.0306 -0.0053 108 GLY C O   
1163 N  N   . GLU C 25 ? 0.2661 0.2212 0.3710 0.0135  -0.0408 -0.0327 109 GLU C N   
1164 C  CA  . GLU C 25 ? 0.2603 0.2066 0.3580 -0.0173 -0.0147 -0.0243 109 GLU C CA  
1165 C  C   . GLU C 25 ? 0.2411 0.2264 0.3573 -0.0220 -0.0164 -0.0088 109 GLU C C   
1166 O  O   . GLU C 25 ? 0.2166 0.2365 0.3556 -0.0104 -0.0145 -0.0065 109 GLU C O   
1167 C  CB  . GLU C 25 ? 0.2414 0.3018 0.3483 0.0007  -0.0148 -0.0021 109 GLU C CB  
1168 C  CG  . GLU C 25 ? 0.1704 0.3358 0.3361 0.0211  0.0055  -0.0243 109 GLU C CG  
1169 C  CD  . GLU C 25 ? 0.2841 0.3161 0.3298 0.0167  0.0034  -0.0347 109 GLU C CD  
1170 O  OE1 . GLU C 25 ? 0.3415 0.3134 0.3299 0.0308  -0.0251 -0.0652 109 GLU C OE1 
1171 O  OE2 . GLU C 25 ? 0.3420 0.3150 0.3296 0.0171  -0.0157 -0.0619 109 GLU C OE2 
1172 N  N   . ARG C 26 ? 0.2388 0.2046 0.3496 -0.0366 0.0007  -0.0192 110 ARG C N   
1173 C  CA  . ARG C 26 ? 0.1812 0.2145 0.3495 -0.0359 0.0138  -0.0074 110 ARG C CA  
1174 C  C   . ARG C 26 ? 0.1950 0.2427 0.3375 -0.0234 -0.0014 -0.0199 110 ARG C C   
1175 O  O   . ARG C 26 ? 0.1979 0.2693 0.3432 0.0311  -0.0175 -0.0375 110 ARG C O   
1176 C  CB  . ARG C 26 ? 0.2116 0.2385 0.3751 -0.0265 0.0313  -0.0034 110 ARG C CB  
1177 C  CG  . ARG C 26 ? 0.3142 0.3630 0.4159 -0.1390 0.0537  0.0270  110 ARG C CG  
1178 C  CD  . ARG C 26 ? 0.4927 0.5606 0.4642 -0.1744 0.0349  0.0381  110 ARG C CD  
1179 N  NE  . ARG C 26 ? 0.6681 0.7200 0.5052 -0.0915 0.0107  0.0599  110 ARG C NE  
1180 C  CZ  . ARG C 26 ? 0.7812 0.7740 0.5293 -0.0459 0.0044  0.0746  110 ARG C CZ  
1181 N  NH1 . ARG C 26 ? 0.8240 0.8282 0.5345 -0.0159 -0.0015 0.0681  110 ARG C NH1 
1182 N  NH2 . ARG C 26 ? 0.7687 0.7346 0.5386 -0.0804 0.0038  0.0853  110 ARG C NH2 
1183 N  N   . LEU C 27 ? 0.1832 0.2144 0.3313 -0.0304 -0.0032 -0.0019 111 LEU C N   
1184 C  CA  . LEU C 27 ? 0.1808 0.2238 0.3281 -0.0071 0.0248  -0.0083 111 LEU C CA  
1185 C  C   . LEU C 27 ? 0.2420 0.2250 0.3235 0.0007  0.0248  -0.0167 111 LEU C C   
1186 O  O   . LEU C 27 ? 0.2151 0.2553 0.3393 0.0065  0.0206  -0.0296 111 LEU C O   
1187 C  CB  . LEU C 27 ? 0.2736 0.2748 0.3333 -0.0241 0.0226  -0.0026 111 LEU C CB  
1188 C  CG  . LEU C 27 ? 0.2902 0.2767 0.3436 -0.0354 0.0259  0.0088  111 LEU C CG  
1189 C  CD1 . LEU C 27 ? 0.3083 0.3898 0.3485 -0.0110 -0.0031 -0.0190 111 LEU C CD1 
1190 C  CD2 . LEU C 27 ? 0.3011 0.3614 0.3583 0.0724  -0.0071 -0.0207 111 LEU C CD2 
1191 N  N   . GLN C 28 ? 0.1717 0.2294 0.2955 -0.0024 0.0213  -0.0057 112 GLN C N   
1192 C  CA  . GLN C 28 ? 0.2023 0.2150 0.2967 0.0061  0.0190  0.0046  112 GLN C CA  
1193 C  C   . GLN C 28 ? 0.1993 0.2374 0.3122 0.0162  0.0235  0.0110  112 GLN C C   
1194 O  O   . GLN C 28 ? 0.2121 0.2533 0.3167 0.0178  0.0506  0.0113  112 GLN C O   
1195 C  CB  . GLN C 28 ? 0.2257 0.1894 0.2792 -0.0334 -0.0028 -0.0128 112 GLN C CB  
1196 C  CG  . GLN C 28 ? 0.2710 0.1848 0.2814 -0.0492 0.0064  -0.0182 112 GLN C CG  
1197 C  CD  . GLN C 28 ? 0.2539 0.1582 0.2944 -0.0205 -0.0137 0.0021  112 GLN C CD  
1198 O  OE1 . GLN C 28 ? 0.2698 0.2275 0.3067 0.0353  -0.0242 -0.0095 112 GLN C OE1 
1199 N  NE2 . GLN C 28 ? 0.2965 0.2420 0.3011 -0.0103 -0.0076 -0.0189 112 GLN C NE2 
1200 N  N   . ILE C 29 ? 0.2089 0.2076 0.3165 0.0158  0.0022  0.0032  113 ILE C N   
1201 C  CA  . ILE C 29 ? 0.2263 0.2420 0.3399 -0.0006 0.0185  0.0270  113 ILE C CA  
1202 C  C   . ILE C 29 ? 0.2402 0.2312 0.3652 -0.0009 0.0368  -0.0032 113 ILE C C   
1203 O  O   . ILE C 29 ? 0.3338 0.2525 0.3441 0.0032  0.0393  -0.0140 113 ILE C O   
1204 C  CB  . ILE C 29 ? 0.2458 0.2965 0.3314 0.0502  0.0154  0.0464  113 ILE C CB  
1205 C  CG1 . ILE C 29 ? 0.2544 0.3340 0.3301 0.0105  0.0165  0.0048  113 ILE C CG1 
1206 C  CG2 . ILE C 29 ? 0.3195 0.2814 0.3254 0.0711  0.0293  0.0697  113 ILE C CG2 
1207 C  CD1 . ILE C 29 ? 0.2479 0.3509 0.3330 -0.0178 0.0297  0.0069  113 ILE C CD1 
1208 N  N   . VAL C 30 ? 0.2653 0.2823 0.4059 -0.0792 0.0260  -0.0174 114 VAL C N   
1209 C  CA  . VAL C 30 ? 0.3873 0.3406 0.4707 -0.1846 0.0181  -0.0265 114 VAL C CA  
1210 C  C   . VAL C 30 ? 0.5285 0.3595 0.5438 -0.2503 0.0032  0.0146  114 VAL C C   
1211 O  O   . VAL C 30 ? 0.5432 0.4789 0.5579 -0.0665 0.0203  0.0587  114 VAL C O   
1212 C  CB  . VAL C 30 ? 0.4920 0.4791 0.4725 -0.0612 -0.0273 -0.0567 114 VAL C CB  
1213 C  CG1 . VAL C 30 ? 0.5981 0.5742 0.4811 -0.0778 -0.0110 -0.0512 114 VAL C CG1 
1214 C  CG2 . VAL C 30 ? 0.2885 0.5561 0.4600 -0.1749 -0.0463 -0.1072 114 VAL C CG2 
1215 N  N   . ASN C 31 ? 0.8018 0.4592 0.6053 -0.1675 -0.0168 0.0043  115 ASN C N   
1216 C  CA  . ASN C 31 ? 1.1199 0.5288 0.6692 -0.0558 -0.0464 -0.0016 115 ASN C CA  
1217 C  C   . ASN C 31 ? 1.2986 0.6481 0.7213 0.0614  -0.0468 0.0343  115 ASN C C   
1218 O  O   . ASN C 31 ? 1.3117 0.7084 0.7252 0.1149  -0.0494 0.0353  115 ASN C O   
1219 C  CB  . ASN C 31 ? 1.2043 0.4925 0.6775 -0.1473 -0.0576 -0.0142 115 ASN C CB  
1220 C  CG  . ASN C 31 ? 1.3082 0.5174 0.6841 -0.1678 -0.0643 -0.0431 115 ASN C CG  
1221 O  OD1 . ASN C 31 ? 1.3068 0.5384 0.6869 -0.2129 -0.0651 -0.0281 115 ASN C OD1 
1222 N  ND2 . ASN C 31 ? 1.3768 0.4651 0.6835 -0.1378 -0.0678 -0.0789 115 ASN C ND2 
1223 N  N   . ASN C 32 ? 1.4084 0.6647 0.7666 0.0452  -0.0376 0.0747  116 ASN C N   
1224 C  CA  . ASN C 32 ? 1.4820 0.6117 0.8084 0.0079  -0.0198 0.1201  116 ASN C CA  
1225 C  C   . ASN C 32 ? 1.4662 0.5932 0.8332 -0.0230 -0.0032 0.1516  116 ASN C C   
1226 O  O   . ASN C 32 ? 1.4484 0.5531 0.8342 -0.0992 0.0082  0.1750  116 ASN C O   
1227 C  CB  . ASN C 32 ? 1.5496 0.6264 0.8217 0.0030  -0.0165 0.1243  116 ASN C CB  
1228 C  CG  . ASN C 32 ? 1.6068 0.6321 0.8321 -0.0076 -0.0124 0.1169  116 ASN C CG  
1229 O  OD1 . ASN C 32 ? 1.6307 0.6859 0.8350 -0.0074 -0.0125 0.1132  116 ASN C OD1 
1230 N  ND2 . ASN C 32 ? 1.6212 0.6100 0.8352 -0.0131 -0.0098 0.1109  116 ASN C ND2 
1231 N  N   . THR C 33 ? 1.4592 0.6045 0.8537 0.0362  0.0016  0.1580  117 THR C N   
1232 C  CA  . THR C 33 ? 1.4502 0.5849 0.8679 0.0953  0.0126  0.1773  117 THR C CA  
1233 C  C   . THR C 33 ? 1.4505 0.5624 0.8685 0.1508  0.0335  0.2171  117 THR C C   
1234 O  O   . THR C 33 ? 1.4457 0.5300 0.8728 0.2149  0.0318  0.2124  117 THR C O   
1235 C  CB  . THR C 33 ? 1.4319 0.5124 0.8781 0.0610  0.0118  0.1664  117 THR C CB  
1236 O  OG1 . THR C 33 ? 1.4247 0.5919 0.8832 0.0534  0.0129  0.1546  117 THR C OG1 
1237 C  CG2 . THR C 33 ? 1.4285 0.4343 0.8797 0.0386  0.0069  0.1644  117 THR C CG2 
1238 N  N   . GLU C 34 ? 1.4381 0.6048 0.8612 0.1783  0.0456  0.2537  118 GLU C N   
1239 C  CA  . GLU C 34 ? 1.4256 0.6213 0.8514 0.1973  0.0652  0.2848  118 GLU C CA  
1240 C  C   . GLU C 34 ? 1.2718 0.6244 0.8119 0.1948  0.0662  0.2995  118 GLU C C   
1241 O  O   . GLU C 34 ? 1.2808 0.6289 0.8139 0.2212  0.0722  0.3175  118 GLU C O   
1242 C  CB  . GLU C 34 ? 1.5508 0.6719 0.8774 0.2364  0.0797  0.3033  118 GLU C CB  
1243 C  CG  . GLU C 34 ? 1.6701 0.7220 0.8993 0.2605  0.0890  0.3125  118 GLU C CG  
1244 C  CD  . GLU C 34 ? 1.7727 0.8228 0.9161 0.3060  0.0932  0.3173  118 GLU C CD  
1245 O  OE1 . GLU C 34 ? 1.8130 0.8832 0.9236 0.3212  0.0981  0.3080  118 GLU C OE1 
1246 O  OE2 . GLU C 34 ? 1.8047 0.8248 0.9199 0.3209  0.0919  0.3306  118 GLU C OE2 
1247 N  N   . GLY C 35 ? 1.0727 0.5793 0.7652 0.2288  0.0621  0.2957  119 GLY C N   
1248 C  CA  . GLY C 35 ? 0.8920 0.5767 0.7146 0.2153  0.0631  0.2928  119 GLY C CA  
1249 C  C   . GLY C 35 ? 0.7260 0.5117 0.6621 0.2064  0.0715  0.2862  119 GLY C C   
1250 O  O   . GLY C 35 ? 0.7666 0.5035 0.6656 0.2139  0.0926  0.2808  119 GLY C O   
1251 N  N   . ASP C 36 ? 0.5294 0.5133 0.6034 0.1830  0.0678  0.2612  120 ASP C N   
1252 C  CA  . ASP C 36 ? 0.4556 0.5261 0.5441 0.1361  0.0599  0.2516  120 ASP C CA  
1253 C  C   . ASP C 36 ? 0.3553 0.4543 0.4898 0.0512  0.0305  0.1860  120 ASP C C   
1254 O  O   . ASP C 36 ? 0.3296 0.4754 0.4977 0.0369  -0.0202 0.1921  120 ASP C O   
1255 C  CB  . ASP C 36 ? 0.4760 0.6635 0.5464 0.1930  0.0291  0.2640  120 ASP C CB  
1256 C  CG  . ASP C 36 ? 0.5865 0.7792 0.5486 0.2006  0.0460  0.2879  120 ASP C CG  
1257 O  OD1 . ASP C 36 ? 0.5765 0.7993 0.5501 0.2235  0.0427  0.2736  120 ASP C OD1 
1258 O  OD2 . ASP C 36 ? 0.6447 0.8472 0.5470 0.2232  0.0545  0.3048  120 ASP C OD2 
1259 N  N   . TRP C 37 ? 0.3319 0.3159 0.4260 0.0415  0.0200  0.1214  121 TRP C N   
1260 C  CA  . TRP C 37 ? 0.2615 0.2958 0.3734 -0.0314 0.0190  0.0699  121 TRP C CA  
1261 C  C   . TRP C 37 ? 0.2704 0.2757 0.3509 -0.0371 0.0312  0.0516  121 TRP C C   
1262 O  O   . TRP C 37 ? 0.3773 0.2835 0.3503 -0.0411 0.0329  0.0246  121 TRP C O   
1263 C  CB  . TRP C 37 ? 0.2460 0.3610 0.3476 -0.0381 0.0123  0.0513  121 TRP C CB  
1264 C  CG  . TRP C 37 ? 0.3016 0.3507 0.3286 0.0612  -0.0078 0.0390  121 TRP C CG  
1265 C  CD1 . TRP C 37 ? 0.3255 0.4080 0.3230 0.0309  -0.0086 0.0183  121 TRP C CD1 
1266 C  CD2 . TRP C 37 ? 0.3091 0.3031 0.3227 0.0011  0.0241  0.0285  121 TRP C CD2 
1267 N  NE1 . TRP C 37 ? 0.3653 0.3767 0.3207 -0.0093 0.0022  0.0280  121 TRP C NE1 
1268 C  CE2 . TRP C 37 ? 0.3165 0.2666 0.3215 -0.0412 0.0296  0.0380  121 TRP C CE2 
1269 C  CE3 . TRP C 37 ? 0.3416 0.3178 0.3268 0.0278  0.0530  0.0387  121 TRP C CE3 
1270 C  CZ2 . TRP C 37 ? 0.3455 0.3151 0.3227 -0.0203 0.0538  0.0429  121 TRP C CZ2 
1271 C  CZ3 . TRP C 37 ? 0.3276 0.4169 0.3268 -0.0087 0.0588  0.0290  121 TRP C CZ3 
1272 C  CH2 . TRP C 37 ? 0.3224 0.4088 0.3200 0.0039  0.0597  0.0472  121 TRP C CH2 
1273 N  N   . TRP C 38 ? 0.2763 0.2741 0.3294 -0.0089 0.0471  0.0564  122 TRP C N   
1274 C  CA  . TRP C 38 ? 0.2829 0.2809 0.3257 0.0064  0.0402  0.0313  122 TRP C CA  
1275 C  C   . TRP C 38 ? 0.2769 0.2663 0.3226 0.0381  0.0347  0.0021  122 TRP C C   
1276 O  O   . TRP C 38 ? 0.3056 0.2492 0.3267 0.0180  0.0241  -0.0132 122 TRP C O   
1277 C  CB  . TRP C 38 ? 0.2475 0.3145 0.3459 0.0226  0.0689  0.0377  122 TRP C CB  
1278 C  CG  . TRP C 38 ? 0.3048 0.2700 0.3668 0.0104  0.0568  0.0349  122 TRP C CG  
1279 C  CD1 . TRP C 38 ? 0.3243 0.2654 0.3790 0.0194  0.0457  0.0180  122 TRP C CD1 
1280 C  CD2 . TRP C 38 ? 0.2661 0.2605 0.3780 0.0077  0.0320  0.0212  122 TRP C CD2 
1281 N  NE1 . TRP C 38 ? 0.3587 0.3196 0.3864 0.0697  0.0495  0.0406  122 TRP C NE1 
1282 C  CE2 . TRP C 38 ? 0.3258 0.3604 0.3883 0.0925  0.0369  0.0174  122 TRP C CE2 
1283 C  CE3 . TRP C 38 ? 0.2836 0.2444 0.3810 -0.0136 0.0107  0.0095  122 TRP C CE3 
1284 C  CZ2 . TRP C 38 ? 0.3297 0.3704 0.3932 0.0591  0.0238  0.0213  122 TRP C CZ2 
1285 C  CZ3 . TRP C 38 ? 0.2513 0.3650 0.3942 0.0563  0.0022  0.0051  122 TRP C CZ3 
1286 C  CH2 . TRP C 38 ? 0.2851 0.3879 0.3946 0.0650  -0.0001 0.0188  122 TRP C CH2 
1287 N  N   . LEU C 39 ? 0.2772 0.2723 0.3196 0.0086  0.0123  -0.0080 123 LEU C N   
1288 C  CA  . LEU C 39 ? 0.2043 0.2360 0.3228 -0.0310 0.0304  0.0181  123 LEU C CA  
1289 C  C   . LEU C 39 ? 0.2360 0.2330 0.3023 0.0113  0.0360  0.0147  123 LEU C C   
1290 O  O   . LEU C 39 ? 0.2476 0.2963 0.3048 -0.0320 0.0269  -0.0127 123 LEU C O   
1291 C  CB  . LEU C 39 ? 0.1989 0.2715 0.3494 -0.0183 0.0261  0.0041  123 LEU C CB  
1292 C  CG  . LEU C 39 ? 0.1876 0.3390 0.3710 -0.0111 0.0148  -0.0328 123 LEU C CG  
1293 C  CD1 . LEU C 39 ? 0.2208 0.3922 0.3810 0.0407  0.0241  -0.0453 123 LEU C CD1 
1294 C  CD2 . LEU C 39 ? 0.2176 0.3380 0.3807 -0.0664 0.0010  -0.0444 123 LEU C CD2 
1295 N  N   . ALA C 40 ? 0.2033 0.2367 0.2850 0.0031  0.0328  0.0358  124 ALA C N   
1296 C  CA  . ALA C 40 ? 0.1835 0.2206 0.2803 -0.0275 -0.0046 0.0534  124 ALA C CA  
1297 C  C   . ALA C 40 ? 0.1901 0.2311 0.2709 -0.0155 0.0094  0.0233  124 ALA C C   
1298 O  O   . ALA C 40 ? 0.1970 0.3287 0.2650 -0.0072 0.0238  -0.0069 124 ALA C O   
1299 C  CB  . ALA C 40 ? 0.1844 0.3109 0.2704 -0.0526 -0.0072 0.0341  124 ALA C CB  
1300 N  N   . HIS C 41 ? 0.2011 0.2360 0.2703 -0.0206 -0.0015 0.0140  125 HIS C N   
1301 C  CA  . HIS C 41 ? 0.2074 0.2623 0.2855 -0.0110 -0.0097 0.0009  125 HIS C CA  
1302 C  C   . HIS C 41 ? 0.1791 0.2419 0.2827 0.0341  0.0013  -0.0446 125 HIS C C   
1303 O  O   . HIS C 41 ? 0.1969 0.2598 0.2926 0.0210  0.0206  -0.0467 125 HIS C O   
1304 C  CB  . HIS C 41 ? 0.2166 0.2630 0.2971 -0.0480 -0.0167 -0.0058 125 HIS C CB  
1305 C  CG  . HIS C 41 ? 0.2002 0.2928 0.3246 -0.0783 -0.0143 0.0234  125 HIS C CG  
1306 N  ND1 . HIS C 41 ? 0.2758 0.3455 0.3353 -0.0625 -0.0100 0.0492  125 HIS C ND1 
1307 C  CD2 . HIS C 41 ? 0.2532 0.2807 0.3370 -0.1014 -0.0485 0.0023  125 HIS C CD2 
1308 C  CE1 . HIS C 41 ? 0.2935 0.4171 0.3433 -0.0216 -0.0082 0.0646  125 HIS C CE1 
1309 N  NE2 . HIS C 41 ? 0.2743 0.3267 0.3503 -0.0907 -0.0327 0.0433  125 HIS C NE2 
1310 N  N   . SER C 42 ? 0.2081 0.2254 0.2735 0.0555  -0.0011 -0.0328 126 SER C N   
1311 C  CA  . SER C 42 ? 0.2401 0.2024 0.2671 -0.0090 0.0030  -0.0098 126 SER C CA  
1312 C  C   . SER C 42 ? 0.1957 0.2577 0.2705 -0.0288 0.0022  0.0166  126 SER C C   
1313 O  O   . SER C 42 ? 0.1927 0.3334 0.2717 0.0148  -0.0071 -0.0195 126 SER C O   
1314 C  CB  . SER C 42 ? 0.2596 0.2314 0.2860 0.0068  0.0185  -0.0245 126 SER C CB  
1315 O  OG  . SER C 42 ? 0.2726 0.2632 0.2861 0.0417  -0.0022 -0.0216 126 SER C OG  
1316 N  N   . LEU C 43 ? 0.2423 0.2573 0.2763 -0.0119 0.0099  0.0009  127 LEU C N   
1317 C  CA  . LEU C 43 ? 0.2157 0.2855 0.3051 0.0009  0.0197  -0.0219 127 LEU C CA  
1318 C  C   . LEU C 43 ? 0.2662 0.3096 0.3298 0.0704  -0.0139 -0.0066 127 LEU C C   
1319 O  O   . LEU C 43 ? 0.2875 0.3180 0.3274 0.0409  -0.0403 0.0090  127 LEU C O   
1320 C  CB  . LEU C 43 ? 0.2389 0.2873 0.3154 0.0036  0.0658  -0.0299 127 LEU C CB  
1321 C  CG  . LEU C 43 ? 0.3366 0.2611 0.3321 -0.0103 0.0877  -0.0278 127 LEU C CG  
1322 C  CD1 . LEU C 43 ? 0.4054 0.2731 0.3342 0.0441  0.0715  -0.0020 127 LEU C CD1 
1323 C  CD2 . LEU C 43 ? 0.3216 0.2642 0.3390 -0.0148 0.1282  -0.0508 127 LEU C CD2 
1324 N  N   . SER C 44 ? 0.2395 0.2313 0.3555 0.0203  -0.0105 -0.0107 128 SER C N   
1325 C  CA  . SER C 44 ? 0.2481 0.2491 0.3832 0.0459  -0.0110 -0.0234 128 SER C CA  
1326 C  C   . SER C 44 ? 0.2565 0.2705 0.3976 -0.0026 -0.0274 -0.0032 128 SER C C   
1327 O  O   . SER C 44 ? 0.3243 0.2928 0.4166 0.0637  -0.0340 -0.0151 128 SER C O   
1328 C  CB  . SER C 44 ? 0.2879 0.3140 0.3991 0.0198  -0.0177 -0.0309 128 SER C CB  
1329 O  OG  . SER C 44 ? 0.4020 0.3484 0.4172 0.0186  0.0230  0.0059  128 SER C OG  
1330 N  N   . THR C 45 ? 0.2163 0.2649 0.3994 0.0045  -0.0116 0.0079  129 THR C N   
1331 C  CA  . THR C 45 ? 0.2278 0.3396 0.4006 0.0698  0.0177  0.0185  129 THR C CA  
1332 C  C   . THR C 45 ? 0.1855 0.3241 0.3839 0.0633  -0.0427 0.0113  129 THR C C   
1333 O  O   . THR C 45 ? 0.2750 0.3221 0.3951 0.0513  -0.0030 0.0146  129 THR C O   
1334 C  CB  . THR C 45 ? 0.2994 0.3270 0.4058 0.0290  0.0508  -0.0113 129 THR C CB  
1335 O  OG1 . THR C 45 ? 0.3256 0.3484 0.4149 0.0684  0.0731  0.0034  129 THR C OG1 
1336 C  CG2 . THR C 45 ? 0.3791 0.3314 0.4090 0.0286  0.0648  -0.0393 129 THR C CG2 
1337 N  N   . GLY C 46 ? 0.2666 0.2923 0.3589 0.0160  0.0044  0.0335  130 GLY C N   
1338 C  CA  . GLY C 46 ? 0.2082 0.3594 0.3451 -0.0287 0.0112  0.0418  130 GLY C CA  
1339 C  C   . GLY C 46 ? 0.1936 0.4133 0.3382 0.0180  0.0154  0.0419  130 GLY C C   
1340 O  O   . GLY C 46 ? 0.2377 0.4174 0.3382 -0.0420 0.0034  0.0355  130 GLY C O   
1341 N  N   . GLN C 47 ? 0.2322 0.4060 0.3409 0.0121  0.0029  0.0423  131 GLN C N   
1342 C  CA  . GLN C 47 ? 0.2018 0.4382 0.3491 0.0079  0.0140  0.0230  131 GLN C CA  
1343 C  C   . GLN C 47 ? 0.1797 0.3866 0.3312 0.0021  0.0236  0.0314  131 GLN C C   
1344 O  O   . GLN C 47 ? 0.1820 0.4252 0.3334 0.0340  0.0168  0.0220  131 GLN C O   
1345 C  CB  . GLN C 47 ? 0.2704 0.4925 0.3761 0.1533  0.0496  0.0272  131 GLN C CB  
1346 C  CG  . GLN C 47 ? 0.3692 0.5368 0.4018 0.1375  0.0486  0.0057  131 GLN C CG  
1347 C  CD  . GLN C 47 ? 0.5407 0.6940 0.4305 0.1987  0.0362  -0.0354 131 GLN C CD  
1348 O  OE1 . GLN C 47 ? 0.6910 0.7574 0.4402 0.2515  0.0556  -0.0439 131 GLN C OE1 
1349 N  NE2 . GLN C 47 ? 0.5861 0.7179 0.4435 0.1649  0.0317  -0.0498 131 GLN C NE2 
1350 N  N   . THR C 48 ? 0.2447 0.3966 0.3124 0.0172  0.0056  0.0157  132 THR C N   
1351 C  CA  . THR C 48 ? 0.2341 0.4058 0.3034 0.0208  0.0040  0.0058  132 THR C CA  
1352 C  C   . THR C 48 ? 0.2367 0.3912 0.2888 0.0330  0.0208  0.0091  132 THR C C   
1353 O  O   . THR C 48 ? 0.2632 0.4269 0.3021 0.0229  0.0317  0.0075  132 THR C O   
1354 C  CB  . THR C 48 ? 0.2304 0.4236 0.3225 -0.0250 0.0149  0.0240  132 THR C CB  
1355 O  OG1 . THR C 48 ? 0.2317 0.5399 0.3176 0.0082  0.0052  0.0156  132 THR C OG1 
1356 C  CG2 . THR C 48 ? 0.2126 0.3680 0.3278 -0.0343 -0.0043 0.0044  132 THR C CG2 
1357 N  N   . GLY C 49 ? 0.2286 0.2880 0.2706 0.0027  0.0183  0.0121  133 GLY C N   
1358 C  CA  . GLY C 49 ? 0.2739 0.3122 0.2662 0.0052  0.0206  0.0067  133 GLY C CA  
1359 C  C   . GLY C 49 ? 0.2406 0.2659 0.2613 -0.0440 0.0039  -0.0149 133 GLY C C   
1360 O  O   . GLY C 49 ? 0.2572 0.3105 0.2524 0.0072  0.0168  -0.0127 133 GLY C O   
1361 N  N   . TYR C 50 ? 0.2879 0.2615 0.2756 -0.0165 0.0201  0.0035  134 TYR C N   
1362 C  CA  . TYR C 50 ? 0.2963 0.2621 0.2899 -0.0265 0.0140  0.0161  134 TYR C CA  
1363 C  C   . TYR C 50 ? 0.2656 0.2799 0.2777 -0.0009 -0.0162 -0.0018 134 TYR C C   
1364 O  O   . TYR C 50 ? 0.3086 0.2823 0.2798 0.0411  -0.0093 -0.0114 134 TYR C O   
1365 C  CB  . TYR C 50 ? 0.3599 0.2483 0.3178 -0.0059 0.0587  0.0371  134 TYR C CB  
1366 C  CG  . TYR C 50 ? 0.4433 0.3067 0.3546 -0.0581 0.1083  0.0196  134 TYR C CG  
1367 C  CD1 . TYR C 50 ? 0.4953 0.3323 0.3635 -0.0834 0.1414  -0.0131 134 TYR C CD1 
1368 C  CD2 . TYR C 50 ? 0.4597 0.3819 0.3793 -0.1882 0.0968  -0.0088 134 TYR C CD2 
1369 C  CE1 . TYR C 50 ? 0.5764 0.3893 0.3839 -0.1890 0.1324  -0.0218 134 TYR C CE1 
1370 C  CE2 . TYR C 50 ? 0.5690 0.3842 0.3996 -0.2459 0.0841  -0.0352 134 TYR C CE2 
1371 C  CZ  . TYR C 50 ? 0.6340 0.4355 0.4017 -0.2511 0.1037  -0.0511 134 TYR C CZ  
1372 O  OH  . TYR C 50 ? 0.7596 0.4607 0.4183 -0.2247 0.0983  -0.0616 134 TYR C OH  
1373 N  N   A ILE C 51 ? 0.2139 0.2918 0.2790 -0.0005 -0.0119 0.0137  135 ILE C N   
1374 N  N   B ILE C 51 ? 0.2463 0.2841 0.2794 0.0044  -0.0250 0.0051  135 ILE C N   
1375 C  CA  A ILE C 51 ? 0.2420 0.2850 0.2868 0.0000  -0.0084 0.0155  135 ILE C CA  
1376 C  CA  B ILE C 51 ? 0.2516 0.2883 0.2838 0.0010  -0.0333 0.0122  135 ILE C CA  
1377 C  C   A ILE C 51 ? 0.2552 0.2602 0.2923 0.0177  -0.0053 0.0203  135 ILE C C   
1378 C  C   B ILE C 51 ? 0.2566 0.2928 0.2898 0.0207  -0.0180 0.0181  135 ILE C C   
1379 O  O   A ILE C 51 ? 0.2754 0.2441 0.3007 0.0135  0.0143  0.0308  135 ILE C O   
1380 O  O   B ILE C 51 ? 0.2647 0.3040 0.2925 0.0265  -0.0058 0.0271  135 ILE C O   
1381 C  CB  A ILE C 51 ? 0.2427 0.2998 0.2808 0.0356  0.0214  0.0195  135 ILE C CB  
1382 C  CB  B ILE C 51 ? 0.2500 0.2978 0.2796 0.0061  -0.0482 0.0139  135 ILE C CB  
1383 C  CG1 A ILE C 51 ? 0.2928 0.3216 0.2837 0.1200  0.0331  0.0257  135 ILE C CG1 
1384 C  CG1 B ILE C 51 ? 0.2583 0.3161 0.2773 0.0245  -0.0719 0.0109  135 ILE C CG1 
1385 C  CG2 A ILE C 51 ? 0.2756 0.2706 0.2797 0.0379  -0.0156 -0.0069 135 ILE C CG2 
1386 C  CG2 B ILE C 51 ? 0.2446 0.2975 0.2795 0.0021  -0.0562 0.0117  135 ILE C CG2 
1387 C  CD1 A ILE C 51 ? 0.3078 0.2811 0.2916 0.0455  0.0611  0.0359  135 ILE C CD1 
1388 C  CD1 B ILE C 51 ? 0.2405 0.2635 0.2756 -0.0732 -0.1033 -0.0005 135 ILE C CD1 
1389 N  N   . PRO C 52 ? 0.2517 0.3173 0.2954 0.0274  -0.0143 0.0093  136 PRO C N   
1390 C  CA  . PRO C 52 ? 0.2466 0.3558 0.3016 0.0680  -0.0476 0.0064  136 PRO C CA  
1391 C  C   . PRO C 52 ? 0.2451 0.2989 0.3251 0.0316  -0.0193 0.0355  136 PRO C C   
1392 O  O   . PRO C 52 ? 0.2884 0.3189 0.3268 0.0031  0.0014  0.0479  136 PRO C O   
1393 C  CB  . PRO C 52 ? 0.2959 0.3583 0.2912 0.0139  -0.0390 0.0130  136 PRO C CB  
1394 C  CG  . PRO C 52 ? 0.2996 0.3617 0.2861 0.0229  -0.0268 0.0143  136 PRO C CG  
1395 C  CD  . PRO C 52 ? 0.2783 0.2850 0.2927 -0.0165 -0.0186 0.0256  136 PRO C CD  
1396 N  N   . SER C 53 ? 0.2644 0.3244 0.3521 0.0277  0.0032  0.0412  137 SER C N   
1397 C  CA  . SER C 53 ? 0.2978 0.3113 0.3837 0.0130  0.0320  0.0283  137 SER C CA  
1398 C  C   . SER C 53 ? 0.3038 0.3334 0.3934 0.0296  0.0159  0.0515  137 SER C C   
1399 O  O   . SER C 53 ? 0.3059 0.3191 0.4008 0.0345  0.0330  0.0557  137 SER C O   
1400 C  CB  . SER C 53 ? 0.3758 0.3530 0.4013 0.0003  0.0663  0.0522  137 SER C CB  
1401 O  OG  . SER C 53 ? 0.4606 0.3215 0.4168 0.0306  0.0615  0.0739  137 SER C OG  
1402 N  N   . ASN C 54 ? 0.3113 0.3107 0.4026 -0.0090 -0.0088 0.0589  138 ASN C N   
1403 C  CA  . ASN C 54 ? 0.3271 0.3201 0.3990 0.0188  -0.0401 0.0993  138 ASN C CA  
1404 C  C   . ASN C 54 ? 0.2602 0.4016 0.3880 0.0170  -0.0297 0.0647  138 ASN C C   
1405 O  O   . ASN C 54 ? 0.3097 0.4508 0.4058 0.0529  -0.0487 0.0422  138 ASN C O   
1406 C  CB  . ASN C 54 ? 0.3829 0.3851 0.4086 0.0595  -0.0653 0.1220  138 ASN C CB  
1407 C  CG  . ASN C 54 ? 0.5062 0.4953 0.4230 0.1183  -0.0948 0.1011  138 ASN C CG  
1408 O  OD1 . ASN C 54 ? 0.5266 0.5176 0.4258 0.1504  -0.1013 0.0923  138 ASN C OD1 
1409 N  ND2 . ASN C 54 ? 0.5550 0.6582 0.4397 0.1173  -0.0951 0.0872  138 ASN C ND2 
1410 N  N   . TYR C 55 ? 0.2326 0.4092 0.3544 0.0789  -0.0262 0.0456  139 TYR C N   
1411 C  CA  . TYR C 55 ? 0.2394 0.3350 0.3332 0.0412  -0.0137 0.0263  139 TYR C CA  
1412 C  C   . TYR C 55 ? 0.2543 0.3427 0.3279 0.0119  -0.0144 0.0257  139 TYR C C   
1413 O  O   . TYR C 55 ? 0.2743 0.3311 0.3299 -0.0129 -0.0162 0.0178  139 TYR C O   
1414 C  CB  . TYR C 55 ? 0.2632 0.3229 0.3217 -0.0105 -0.0318 -0.0129 139 TYR C CB  
1415 C  CG  . TYR C 55 ? 0.2975 0.3280 0.3153 -0.0067 -0.0546 -0.0412 139 TYR C CG  
1416 C  CD1 . TYR C 55 ? 0.3050 0.4243 0.3190 0.0318  -0.0676 -0.0360 139 TYR C CD1 
1417 C  CD2 . TYR C 55 ? 0.2869 0.3378 0.3194 -0.0130 -0.0761 -0.0561 139 TYR C CD2 
1418 C  CE1 . TYR C 55 ? 0.3869 0.4315 0.3191 0.0618  -0.0634 -0.0660 139 TYR C CE1 
1419 C  CE2 . TYR C 55 ? 0.3234 0.3816 0.3220 0.0422  -0.0607 -0.0724 139 TYR C CE2 
1420 C  CZ  . TYR C 55 ? 0.3772 0.4339 0.3255 0.0917  -0.0551 -0.0674 139 TYR C CZ  
1421 O  OH  . TYR C 55 ? 0.4093 0.4498 0.3393 0.0467  -0.0413 -0.0446 139 TYR C OH  
1422 N  N   . VAL C 56 ? 0.2584 0.3267 0.3249 0.0227  0.0211  0.0390  140 VAL C N   
1423 C  CA  . VAL C 56 ? 0.2230 0.2655 0.3282 0.0041  0.0059  0.0348  140 VAL C CA  
1424 C  C   . VAL C 56 ? 0.2591 0.2268 0.3410 0.0032  0.0218  0.0498  140 VAL C C   
1425 O  O   . VAL C 56 ? 0.2924 0.3064 0.3494 0.0506  0.0078  0.0283  140 VAL C O   
1426 C  CB  . VAL C 56 ? 0.2366 0.2794 0.3276 -0.0092 0.0022  0.0055  140 VAL C CB  
1427 C  CG1 . VAL C 56 ? 0.2199 0.3053 0.3283 0.0154  -0.0049 -0.0004 140 VAL C CG1 
1428 C  CG2 . VAL C 56 ? 0.2821 0.3007 0.3228 -0.0063 0.0007  0.0346  140 VAL C CG2 
1429 N  N   . ALA C 57 ? 0.1847 0.2867 0.3501 0.0164  0.0002  0.0384  141 ALA C N   
1430 C  CA  . ALA C 57 ? 0.1546 0.3365 0.3498 0.0536  -0.0128 0.0203  141 ALA C CA  
1431 C  C   . ALA C 57 ? 0.1814 0.2069 0.3562 0.0344  -0.0187 0.0217  141 ALA C C   
1432 O  O   . ALA C 57 ? 0.1859 0.2185 0.3664 0.0280  0.0037  0.0251  141 ALA C O   
1433 C  CB  . ALA C 57 ? 0.1506 0.3891 0.3524 0.0221  -0.0205 0.0432  141 ALA C CB  
1434 N  N   . PRO C 58 ? 0.2117 0.2557 0.3578 0.0480  -0.0286 0.0284  142 PRO C N   
1435 C  CA  . PRO C 58 ? 0.2501 0.2032 0.3730 0.0652  -0.0267 0.0291  142 PRO C CA  
1436 C  C   . PRO C 58 ? 0.2449 0.2440 0.4069 0.0520  0.0075  0.0265  142 PRO C C   
1437 O  O   . PRO C 58 ? 0.2415 0.3148 0.4024 0.0258  0.0061  0.0416  142 PRO C O   
1438 C  CB  . PRO C 58 ? 0.2879 0.2209 0.3714 0.0610  -0.0239 0.0187  142 PRO C CB  
1439 C  CG  . PRO C 58 ? 0.3276 0.2460 0.3671 0.0713  -0.0204 0.0160  142 PRO C CG  
1440 C  CD  . PRO C 58 ? 0.2322 0.2413 0.3593 0.0503  -0.0245 0.0234  142 PRO C CD  
1441 N  N   . SER C 59 ? 0.2691 0.2196 0.4372 -0.0292 0.0208  0.0495  143 SER C N   
1442 C  CA  . SER C 59 ? 0.3188 0.3571 0.4741 -0.0698 0.0314  0.0856  143 SER C CA  
1443 C  C   . SER C 59 ? 0.5002 0.4963 0.5076 0.0281  0.0587  0.0784  143 SER C C   
1444 O  O   . SER C 59 ? 0.4653 0.5580 0.5230 0.0149  0.0583  0.1213  143 SER C O   
1445 C  CB  . SER C 59 ? 0.3502 0.4848 0.4824 0.1014  0.0366  0.0833  143 SER C CB  
1446 O  OG  . SER C 59 ? 0.4332 0.6404 0.4984 0.0428  0.0355  0.0874  143 SER C OG  
1447 O  OXT . SER C 59 ? 0.6544 0.5066 0.5177 0.0729  0.0797  0.0528  143 SER C OXT 
1448 N  N   . GLY D 1  ? 0.5576 0.4706 0.4924 0.2025  -0.1000 0.0159  85  GLY D N   
1449 C  CA  . GLY D 1  ? 0.4772 0.4212 0.4743 0.1083  -0.1082 0.0269  85  GLY D CA  
1450 C  C   . GLY D 1  ? 0.4412 0.3339 0.4500 0.0797  -0.0966 0.0155  85  GLY D C   
1451 O  O   . GLY D 1  ? 0.3965 0.4124 0.4597 0.0629  -0.0886 -0.0132 85  GLY D O   
1452 N  N   . VAL D 2  ? 0.3612 0.2521 0.4194 -0.0220 -0.0919 0.0402  86  VAL D N   
1453 C  CA  . VAL D 2  ? 0.2720 0.2785 0.3887 -0.0505 -0.0968 0.0342  86  VAL D CA  
1454 C  C   . VAL D 2  ? 0.3252 0.2687 0.3773 -0.0928 -0.0791 0.0501  86  VAL D C   
1455 O  O   . VAL D 2  ? 0.4429 0.2794 0.3758 -0.0864 -0.0714 0.0324  86  VAL D O   
1456 C  CB  . VAL D 2  ? 0.3503 0.3110 0.3894 0.0176  -0.0654 0.0200  86  VAL D CB  
1457 C  CG1 . VAL D 2  ? 0.3770 0.3835 0.3861 -0.0122 -0.0557 0.0176  86  VAL D CG1 
1458 C  CG2 . VAL D 2  ? 0.4032 0.3591 0.3979 -0.0140 -0.0442 0.0170  86  VAL D CG2 
1459 N  N   . THR D 3  ? 0.3353 0.2397 0.3640 -0.0005 -0.0935 0.0607  87  THR D N   
1460 C  CA  . THR D 3  ? 0.3037 0.2881 0.3634 -0.0058 -0.0995 0.0442  87  THR D CA  
1461 C  C   . THR D 3  ? 0.3199 0.2894 0.3551 0.0251  -0.0979 0.0529  87  THR D C   
1462 O  O   . THR D 3  ? 0.3324 0.2870 0.3685 -0.0175 -0.0961 0.0899  87  THR D O   
1463 C  CB  . THR D 3  ? 0.3654 0.4208 0.3662 0.0648  -0.1074 -0.0003 87  THR D CB  
1464 O  OG1 . THR D 3  ? 0.3510 0.4198 0.3842 0.0643  -0.0737 0.0165  87  THR D OG1 
1465 C  CG2 . THR D 3  ? 0.4021 0.4381 0.3596 0.0724  -0.0927 -0.0147 87  THR D CG2 
1466 N  N   . THR D 4  ? 0.2695 0.2692 0.3400 0.0077  -0.0826 -0.0004 88  THR D N   
1467 C  CA  . THR D 4  ? 0.3167 0.2457 0.3337 -0.0389 -0.0826 -0.0101 88  THR D CA  
1468 C  C   . THR D 4  ? 0.3495 0.2108 0.3235 -0.0085 -0.0605 0.0031  88  THR D C   
1469 O  O   . THR D 4  ? 0.3742 0.2308 0.3194 -0.0188 -0.0734 0.0167  88  THR D O   
1470 C  CB  . THR D 4  ? 0.3294 0.2922 0.3346 -0.0277 -0.0767 -0.0038 88  THR D CB  
1471 O  OG1 . THR D 4  ? 0.3729 0.2648 0.3392 -0.0280 -0.0706 -0.0406 88  THR D OG1 
1472 C  CG2 . THR D 4  ? 0.3492 0.3638 0.3503 0.0252  -0.0501 -0.0037 88  THR D CG2 
1473 N  N   . PHE D 5  ? 0.3670 0.2061 0.3261 -0.0544 -0.0446 0.0279  89  PHE D N   
1474 C  CA  . PHE D 5  ? 0.3539 0.2452 0.3340 -0.0285 -0.0704 0.0229  89  PHE D CA  
1475 C  C   . PHE D 5  ? 0.3258 0.2288 0.3526 -0.0303 -0.0904 0.0143  89  PHE D C   
1476 O  O   . PHE D 5  ? 0.3567 0.2223 0.3669 -0.0451 -0.1061 0.0114  89  PHE D O   
1477 C  CB  . PHE D 5  ? 0.3495 0.2556 0.3271 0.0277  -0.0698 0.0317  89  PHE D CB  
1478 C  CG  . PHE D 5  ? 0.3320 0.2394 0.3230 0.0089  -0.0580 0.0195  89  PHE D CG  
1479 C  CD1 . PHE D 5  ? 0.4204 0.2908 0.3284 0.0430  -0.0472 0.0326  89  PHE D CD1 
1480 C  CD2 . PHE D 5  ? 0.3279 0.2284 0.3306 -0.0182 -0.0338 0.0208  89  PHE D CD2 
1481 C  CE1 . PHE D 5  ? 0.3881 0.3324 0.3238 0.0411  -0.0449 0.0186  89  PHE D CE1 
1482 C  CE2 . PHE D 5  ? 0.3413 0.2133 0.3304 -0.0235 -0.0254 0.0331  89  PHE D CE2 
1483 C  CZ  . PHE D 5  ? 0.3680 0.2910 0.3293 0.0028  -0.0330 0.0269  89  PHE D CZ  
1484 N  N   . VAL D 6  ? 0.2837 0.1958 0.3510 -0.0069 -0.0977 0.0246  90  VAL D N   
1485 C  CA  . VAL D 6  ? 0.2998 0.2468 0.3582 -0.0361 -0.0937 0.0178  90  VAL D CA  
1486 C  C   . VAL D 6  ? 0.2852 0.1974 0.3595 -0.0563 -0.0893 0.0229  90  VAL D C   
1487 O  O   . VAL D 6  ? 0.3210 0.2134 0.3595 -0.0304 -0.0854 0.0067  90  VAL D O   
1488 C  CB  . VAL D 6  ? 0.3381 0.2708 0.3660 0.0260  -0.0579 0.0059  90  VAL D CB  
1489 C  CG1 . VAL D 6  ? 0.3483 0.2125 0.3635 0.0119  -0.0479 -0.0299 90  VAL D CG1 
1490 C  CG2 . VAL D 6  ? 0.2944 0.3270 0.3652 -0.0288 -0.0329 0.0233  90  VAL D CG2 
1491 N  N   . ALA D 7  ? 0.3174 0.2452 0.3679 -0.0538 -0.0868 0.0499  91  ALA D N   
1492 C  CA  . ALA D 7  ? 0.3492 0.2577 0.3709 -0.0137 -0.1014 0.0290  91  ALA D CA  
1493 C  C   . ALA D 7  ? 0.3140 0.2581 0.3859 -0.0379 -0.1000 0.0321  91  ALA D C   
1494 O  O   . ALA D 7  ? 0.3227 0.3093 0.3893 -0.0627 -0.0928 0.0428  91  ALA D O   
1495 C  CB  . ALA D 7  ? 0.3120 0.2545 0.3736 -0.0081 -0.1011 0.0413  91  ALA D CB  
1496 N  N   . LEU D 8  ? 0.3380 0.2927 0.3956 -0.0660 -0.1128 0.0106  92  LEU D N   
1497 C  CA  . LEU D 8  ? 0.3517 0.2993 0.4027 -0.0653 -0.1089 0.0244  92  LEU D CA  
1498 C  C   . LEU D 8  ? 0.3308 0.3474 0.4202 -0.0759 -0.1243 0.0185  92  LEU D C   
1499 O  O   . LEU D 8  ? 0.3535 0.4321 0.4272 -0.0608 -0.1279 0.0324  92  LEU D O   
1500 C  CB  . LEU D 8  ? 0.3515 0.3176 0.4031 -0.0348 -0.0933 0.0245  92  LEU D CB  
1501 C  CG  . LEU D 8  ? 0.3596 0.2554 0.4000 -0.0744 -0.0904 0.0324  92  LEU D CG  
1502 C  CD1 . LEU D 8  ? 0.3915 0.3023 0.4045 -0.0116 -0.0691 0.0456  92  LEU D CD1 
1503 C  CD2 . LEU D 8  ? 0.3654 0.3193 0.3978 -0.0869 -0.0681 0.0504  92  LEU D CD2 
1504 N  N   . TYR D 9  ? 0.3543 0.3109 0.4262 -0.0961 -0.1162 0.0409  93  TYR D N   
1505 C  CA  . TYR D 9  ? 0.4282 0.3024 0.4385 -0.0024 -0.1472 0.0446  93  TYR D CA  
1506 C  C   . TYR D 9  ? 0.4908 0.3208 0.4515 -0.0183 -0.1736 0.0457  93  TYR D C   
1507 O  O   . TYR D 9  ? 0.5060 0.3032 0.4382 -0.0127 -0.1968 0.0147  93  TYR D O   
1508 C  CB  . TYR D 9  ? 0.4212 0.3707 0.4404 -0.0523 -0.1262 0.0525  93  TYR D CB  
1509 C  CG  . TYR D 9  ? 0.4170 0.3860 0.4391 -0.0603 -0.1230 0.0513  93  TYR D CG  
1510 C  CD1 . TYR D 9  ? 0.4775 0.3859 0.4475 -0.0254 -0.1004 0.0555  93  TYR D CD1 
1511 C  CD2 . TYR D 9  ? 0.4628 0.3368 0.4336 -0.0904 -0.0860 0.0918  93  TYR D CD2 
1512 C  CE1 . TYR D 9  ? 0.5379 0.3894 0.4523 -0.0469 -0.0886 0.0502  93  TYR D CE1 
1513 C  CE2 . TYR D 9  ? 0.5049 0.3577 0.4374 -0.0529 -0.0796 0.0858  93  TYR D CE2 
1514 C  CZ  . TYR D 9  ? 0.5465 0.3818 0.4503 -0.0270 -0.0681 0.0573  93  TYR D CZ  
1515 O  OH  . TYR D 9  ? 0.6206 0.4577 0.4589 0.0560  -0.0405 0.0417  93  TYR D OH  
1516 N  N   . ASP D 10 ? 0.4749 0.4264 0.4699 0.0591  -0.1731 0.0913  94  ASP D N   
1517 C  CA  . ASP D 10 ? 0.4453 0.3698 0.4924 -0.0318 -0.1675 0.0956  94  ASP D CA  
1518 C  C   . ASP D 10 ? 0.4590 0.4282 0.5020 -0.0468 -0.1584 0.1020  94  ASP D C   
1519 O  O   . ASP D 10 ? 0.4536 0.4434 0.5044 -0.0744 -0.1246 0.1024  94  ASP D O   
1520 C  CB  . ASP D 10 ? 0.4149 0.4824 0.4990 0.0452  -0.1999 0.0619  94  ASP D CB  
1521 C  CG  . ASP D 10 ? 0.3837 0.5457 0.5113 0.0097  -0.2071 0.0211  94  ASP D CG  
1522 O  OD1 . ASP D 10 ? 0.4111 0.5660 0.5187 0.0218  -0.1776 0.0356  94  ASP D OD1 
1523 O  OD2 . ASP D 10 ? 0.4406 0.6275 0.5188 0.0229  -0.2148 -0.0117 94  ASP D OD2 
1524 N  N   . TYR D 11 ? 0.5003 0.3806 0.5068 -0.0710 -0.1854 0.1283  95  TYR D N   
1525 C  CA  . TYR D 11 ? 0.5425 0.4013 0.5122 -0.0387 -0.2187 0.1360  95  TYR D CA  
1526 C  C   . TYR D 11 ? 0.6392 0.3845 0.5195 -0.0554 -0.2168 0.1739  95  TYR D C   
1527 O  O   . TYR D 11 ? 0.6697 0.3892 0.5234 -0.0532 -0.2063 0.1909  95  TYR D O   
1528 C  CB  . TYR D 11 ? 0.5772 0.3764 0.5109 -0.0272 -0.2035 0.1429  95  TYR D CB  
1529 C  CG  . TYR D 11 ? 0.5560 0.4408 0.5085 -0.0602 -0.2001 0.1485  95  TYR D CG  
1530 C  CD1 . TYR D 11 ? 0.5613 0.4361 0.5115 -0.0448 -0.1972 0.1427  95  TYR D CD1 
1531 C  CD2 . TYR D 11 ? 0.5794 0.4627 0.5092 -0.0759 -0.1852 0.1466  95  TYR D CD2 
1532 C  CE1 . TYR D 11 ? 0.5749 0.5083 0.5122 -0.0456 -0.1974 0.1340  95  TYR D CE1 
1533 C  CE2 . TYR D 11 ? 0.5561 0.4762 0.5101 -0.0720 -0.1971 0.1443  95  TYR D CE2 
1534 C  CZ  . TYR D 11 ? 0.5389 0.5174 0.5122 -0.1161 -0.2100 0.1224  95  TYR D CZ  
1535 O  OH  . TYR D 11 ? 0.5156 0.6155 0.5115 -0.1496 -0.2463 0.0874  95  TYR D OH  
1536 N  N   . GLU D 12 ? 0.6725 0.4665 0.5255 -0.0231 -0.2294 0.1787  96  GLU D N   
1537 C  CA  . GLU D 12 ? 0.7023 0.4834 0.5348 0.0323  -0.2315 0.1836  96  GLU D CA  
1538 C  C   . GLU D 12 ? 0.7023 0.4520 0.5266 -0.0428 -0.2163 0.1894  96  GLU D C   
1539 O  O   . GLU D 12 ? 0.6727 0.4822 0.5202 -0.0877 -0.2139 0.1876  96  GLU D O   
1540 C  CB  . GLU D 12 ? 0.8129 0.6387 0.5537 0.1082  -0.2182 0.1605  96  GLU D CB  
1541 C  CG  . GLU D 12 ? 0.9518 0.7681 0.5713 0.1839  -0.1863 0.1583  96  GLU D CG  
1542 C  CD  . GLU D 12 ? 1.0518 0.8678 0.5842 0.2196  -0.1691 0.1645  96  GLU D CD  
1543 O  OE1 . GLU D 12 ? 1.1194 0.8898 0.5950 0.1812  -0.1424 0.1721  96  GLU D OE1 
1544 O  OE2 . GLU D 12 ? 1.0376 0.9141 0.5831 0.2770  -0.1861 0.1595  96  GLU D OE2 
1545 N  N   . SER D 13 ? 0.7183 0.4986 0.5174 -0.0667 -0.2348 0.1662  97  SER D N   
1546 C  CA  . SER D 13 ? 0.7427 0.4631 0.5145 -0.0940 -0.2465 0.1745  97  SER D CA  
1547 C  C   . SER D 13 ? 0.8062 0.4155 0.5165 -0.0674 -0.2454 0.1803  97  SER D C   
1548 O  O   . SER D 13 ? 0.8243 0.4535 0.5174 -0.0400 -0.2303 0.2055  97  SER D O   
1549 C  CB  . SER D 13 ? 0.7689 0.5393 0.5186 -0.0513 -0.2396 0.1779  97  SER D CB  
1550 O  OG  . SER D 13 ? 0.7726 0.5361 0.5217 -0.0359 -0.2320 0.1705  97  SER D OG  
1551 N  N   . ARG D 14 ? 0.8615 0.3725 0.5119 -0.0931 -0.2694 0.1363  98  ARG D N   
1552 C  CA  . ARG D 14 ? 0.9292 0.4205 0.5161 -0.1062 -0.2770 0.1262  98  ARG D CA  
1553 C  C   . ARG D 14 ? 0.9970 0.5410 0.5376 -0.0728 -0.2784 0.1245  98  ARG D C   
1554 O  O   . ARG D 14 ? 0.9462 0.5189 0.5318 -0.0600 -0.3051 0.1066  98  ARG D O   
1555 C  CB  . ARG D 14 ? 0.9266 0.4137 0.4974 -0.1239 -0.2843 0.1141  98  ARG D CB  
1556 C  CG  . ARG D 14 ? 0.9055 0.4085 0.4838 -0.1417 -0.2840 0.1166  98  ARG D CG  
1557 C  CD  . ARG D 14 ? 0.8817 0.3994 0.4657 -0.1791 -0.3035 0.0825  98  ARG D CD  
1558 N  NE  . ARG D 14 ? 0.8998 0.3395 0.4527 -0.1840 -0.2914 0.0660  98  ARG D NE  
1559 C  CZ  . ARG D 14 ? 0.9237 0.3965 0.4549 -0.2032 -0.2954 0.0741  98  ARG D CZ  
1560 N  NH1 . ARG D 14 ? 0.9786 0.4016 0.4556 -0.1553 -0.2784 0.0802  98  ARG D NH1 
1561 N  NH2 . ARG D 14 ? 0.9136 0.4703 0.4605 -0.2343 -0.2750 0.1082  98  ARG D NH2 
1562 N  N   . THR D 15 ? 1.0747 0.5848 0.5641 -0.0909 -0.2729 0.1149  99  THR D N   
1563 C  CA  . THR D 15 ? 1.1869 0.7335 0.5947 -0.0779 -0.2424 0.1066  99  THR D CA  
1564 C  C   . THR D 15 ? 1.2995 0.8438 0.6152 -0.0232 -0.2213 0.0992  99  THR D C   
1565 O  O   . THR D 15 ? 1.3348 0.8768 0.6212 -0.0344 -0.2079 0.1053  99  THR D O   
1566 C  CB  . THR D 15 ? 1.2020 0.7595 0.6034 -0.1267 -0.2193 0.1034  99  THR D CB  
1567 O  OG1 . THR D 15 ? 1.2207 0.8286 0.6100 -0.1612 -0.1999 0.0781  99  THR D OG1 
1568 C  CG2 . THR D 15 ? 1.2085 0.7314 0.6061 -0.1607 -0.2070 0.1171  99  THR D CG2 
1569 N  N   . GLU D 16 ? 1.3764 0.9472 0.6313 0.0446  -0.2062 0.1045  100 GLU D N   
1570 C  CA  . GLU D 16 ? 1.4356 0.9488 0.6395 0.0572  -0.1939 0.1197  100 GLU D CA  
1571 C  C   . GLU D 16 ? 1.3390 0.8072 0.6354 0.0015  -0.1975 0.1346  100 GLU D C   
1572 O  O   . GLU D 16 ? 1.3731 0.8672 0.6400 0.0243  -0.1917 0.1326  100 GLU D O   
1573 C  CB  . GLU D 16 ? 1.5642 1.0746 0.6526 0.1239  -0.1810 0.1221  100 GLU D CB  
1574 C  CG  . GLU D 16 ? 1.6661 1.1618 0.6616 0.1646  -0.1736 0.1237  100 GLU D CG  
1575 C  CD  . GLU D 16 ? 1.7404 1.2323 0.6688 0.1973  -0.1692 0.1253  100 GLU D CD  
1576 O  OE1 . GLU D 16 ? 1.7657 1.2446 0.6691 0.1946  -0.1693 0.1232  100 GLU D OE1 
1577 O  OE2 . GLU D 16 ? 1.7634 1.2615 0.6723 0.2045  -0.1708 0.1253  100 GLU D OE2 
1578 N  N   . THR D 17 ? 1.2098 0.5616 0.6263 -0.1127 -0.2057 0.1249  101 THR D N   
1579 C  CA  . THR D 17 ? 1.1029 0.4980 0.6188 -0.1122 -0.2169 0.1179  101 THR D CA  
1580 C  C   . THR D 17 ? 0.9829 0.4426 0.6032 -0.1402 -0.2467 0.0818  101 THR D C   
1581 O  O   . THR D 17 ? 0.9451 0.3779 0.5937 -0.1267 -0.2880 0.0470  101 THR D O   
1582 C  CB  . THR D 17 ? 1.1147 0.6459 0.6260 -0.0631 -0.2101 0.1179  101 THR D CB  
1583 O  OG1 . THR D 17 ? 1.1583 0.7716 0.6339 -0.0391 -0.1921 0.1054  101 THR D OG1 
1584 C  CG2 . THR D 17 ? 1.0962 0.6324 0.6216 -0.0626 -0.2216 0.1232  101 THR D CG2 
1585 N  N   . ASP D 18 ? 0.8476 0.3765 0.5893 -0.2441 -0.2321 0.0718  102 ASP D N   
1586 C  CA  . ASP D 18 ? 0.7743 0.3918 0.5793 -0.1854 -0.2453 0.1180  102 ASP D CA  
1587 C  C   . ASP D 18 ? 0.7467 0.3684 0.5779 -0.1234 -0.1994 0.1669  102 ASP D C   
1588 O  O   . ASP D 18 ? 0.6966 0.4638 0.5755 -0.1228 -0.2121 0.1903  102 ASP D O   
1589 C  CB  . ASP D 18 ? 0.7256 0.3221 0.5537 -0.1895 -0.2456 0.1136  102 ASP D CB  
1590 C  CG  . ASP D 18 ? 0.7693 0.4378 0.5643 -0.2051 -0.2711 0.0933  102 ASP D CG  
1591 O  OD1 . ASP D 18 ? 0.7420 0.4723 0.5581 -0.2369 -0.2800 0.0921  102 ASP D OD1 
1592 O  OD2 . ASP D 18 ? 0.7982 0.5406 0.5663 -0.2055 -0.2641 0.0713  102 ASP D OD2 
1593 N  N   . LEU D 19 ? 0.6973 0.3860 0.5776 -0.1363 -0.1758 0.1656  103 LEU D N   
1594 C  CA  . LEU D 19 ? 0.7004 0.3302 0.5804 -0.1099 -0.1470 0.1755  103 LEU D CA  
1595 C  C   . LEU D 19 ? 0.6766 0.4095 0.5859 -0.1053 -0.1437 0.1546  103 LEU D C   
1596 O  O   . LEU D 19 ? 0.6548 0.5677 0.5911 -0.1296 -0.1548 0.1075  103 LEU D O   
1597 C  CB  . LEU D 19 ? 0.7430 0.3426 0.5795 -0.0822 -0.1089 0.1950  103 LEU D CB  
1598 C  CG  . LEU D 19 ? 0.7687 0.3675 0.5781 0.0161  -0.1146 0.1720  103 LEU D CG  
1599 C  CD1 . LEU D 19 ? 0.7484 0.3660 0.5752 -0.0051 -0.1348 0.1474  103 LEU D CD1 
1600 C  CD2 . LEU D 19 ? 0.7690 0.4789 0.5781 0.0204  -0.1086 0.1795  103 LEU D CD2 
1601 N  N   . SER D 20 ? 0.6302 0.3890 0.5798 -0.0665 -0.1516 0.1621  104 SER D N   
1602 C  CA  . SER D 20 ? 0.6299 0.4049 0.5762 0.0192  -0.1736 0.1329  104 SER D CA  
1603 C  C   . SER D 20 ? 0.5973 0.3698 0.5744 -0.0129 -0.1788 0.1024  104 SER D C   
1604 O  O   . SER D 20 ? 0.6652 0.3654 0.5819 -0.0140 -0.1450 0.0666  104 SER D O   
1605 C  CB  . SER D 20 ? 0.6555 0.3779 0.5758 0.0397  -0.1747 0.1349  104 SER D CB  
1606 O  OG  . SER D 20 ? 0.6602 0.4226 0.5743 0.0483  -0.1785 0.1251  104 SER D OG  
1607 N  N   . PHE D 21 ? 0.5452 0.3250 0.5685 0.0409  -0.2025 0.1053  105 PHE D N   
1608 C  CA  . PHE D 21 ? 0.4892 0.3518 0.5624 0.0656  -0.2222 0.1107  105 PHE D CA  
1609 C  C   . PHE D 21 ? 0.5292 0.3934 0.5588 0.0346  -0.2138 0.1004  105 PHE D C   
1610 O  O   . PHE D 21 ? 0.5636 0.3985 0.5560 -0.0103 -0.2231 0.1041  105 PHE D O   
1611 C  CB  . PHE D 21 ? 0.4820 0.3426 0.5617 0.0059  -0.2323 0.0927  105 PHE D CB  
1612 C  CG  . PHE D 21 ? 0.4192 0.2885 0.5617 -0.0011 -0.2061 0.1021  105 PHE D CG  
1613 C  CD1 . PHE D 21 ? 0.4593 0.2799 0.5605 -0.0083 -0.1947 0.1145  105 PHE D CD1 
1614 C  CD2 . PHE D 21 ? 0.4701 0.3595 0.5625 0.0228  -0.1862 0.0994  105 PHE D CD2 
1615 C  CE1 . PHE D 21 ? 0.4155 0.3087 0.5580 -0.0396 -0.1904 0.1204  105 PHE D CE1 
1616 C  CE2 . PHE D 21 ? 0.4236 0.3039 0.5613 0.0031  -0.1830 0.0976  105 PHE D CE2 
1617 C  CZ  . PHE D 21 ? 0.4276 0.3401 0.5568 -0.0516 -0.1865 0.0985  105 PHE D CZ  
1618 N  N   . LYS D 22 ? 0.4286 0.4094 0.5543 -0.0039 -0.2103 0.0629  106 LYS D N   
1619 C  CA  . LYS D 22 ? 0.4209 0.4536 0.5521 0.0235  -0.2119 0.0303  106 LYS D CA  
1620 C  C   . LYS D 22 ? 0.4011 0.3852 0.5420 0.0285  -0.2158 -0.0036 106 LYS D C   
1621 O  O   . LYS D 22 ? 0.4478 0.3428 0.5395 0.0550  -0.2159 -0.0089 106 LYS D O   
1622 C  CB  . LYS D 22 ? 0.4813 0.5334 0.5635 0.0945  -0.2078 0.0553  106 LYS D CB  
1623 C  CG  . LYS D 22 ? 0.6091 0.6131 0.5751 0.1963  -0.1870 0.0667  106 LYS D CG  
1624 C  CD  . LYS D 22 ? 0.6697 0.7143 0.5826 0.2033  -0.1965 0.0682  106 LYS D CD  
1625 C  CE  . LYS D 22 ? 0.7636 0.7812 0.5903 0.2219  -0.1811 0.0726  106 LYS D CE  
1626 N  NZ  . LYS D 22 ? 0.8033 0.8037 0.5939 0.2410  -0.1814 0.0782  106 LYS D NZ  
1627 N  N   . LYS D 23 ? 0.4241 0.3475 0.5379 0.0177  -0.1987 -0.0180 107 LYS D N   
1628 C  CA  . LYS D 23 ? 0.4066 0.3727 0.5358 0.0318  -0.2067 -0.0499 107 LYS D CA  
1629 C  C   . LYS D 23 ? 0.3940 0.3407 0.5283 0.0482  -0.2053 -0.0453 107 LYS D C   
1630 O  O   . LYS D 23 ? 0.4660 0.4212 0.5337 0.1149  -0.1693 -0.0413 107 LYS D O   
1631 C  CB  . LYS D 23 ? 0.4174 0.4466 0.5449 0.0046  -0.2022 -0.0615 107 LYS D CB  
1632 C  CG  . LYS D 23 ? 0.5002 0.5785 0.5535 0.0158  -0.2112 -0.0880 107 LYS D CG  
1633 C  CD  . LYS D 23 ? 0.5178 0.6808 0.5563 -0.0154 -0.2269 -0.1014 107 LYS D CD  
1634 C  CE  . LYS D 23 ? 0.6094 0.7807 0.5636 0.0764  -0.2012 -0.0778 107 LYS D CE  
1635 N  NZ  . LYS D 23 ? 0.6368 0.8430 0.5704 0.0896  -0.1835 -0.0684 107 LYS D NZ  
1636 N  N   . GLY D 24 ? 0.3835 0.3613 0.5162 0.0089  -0.2187 -0.0480 108 GLY D N   
1637 C  CA  . GLY D 24 ? 0.4418 0.3109 0.5131 -0.0042 -0.1814 0.0064  108 GLY D CA  
1638 C  C   . GLY D 24 ? 0.4259 0.2750 0.5031 0.0362  -0.1768 -0.0062 108 GLY D C   
1639 O  O   . GLY D 24 ? 0.4779 0.2799 0.4953 0.0348  -0.1792 -0.0186 108 GLY D O   
1640 N  N   . GLU D 25 ? 0.3233 0.2554 0.5009 0.0241  -0.1764 -0.0132 109 GLU D N   
1641 C  CA  . GLU D 25 ? 0.3511 0.2523 0.5002 0.0084  -0.1580 0.0216  109 GLU D CA  
1642 C  C   . GLU D 25 ? 0.3553 0.2676 0.4772 0.0277  -0.1519 0.0082  109 GLU D C   
1643 O  O   . GLU D 25 ? 0.3676 0.2251 0.4680 -0.0114 -0.1402 0.0212  109 GLU D O   
1644 C  CB  . GLU D 25 ? 0.4463 0.3029 0.5208 0.0086  -0.1700 0.0078  109 GLU D CB  
1645 C  CG  . GLU D 25 ? 0.5015 0.3004 0.5365 -0.0475 -0.2031 0.0303  109 GLU D CG  
1646 C  CD  . GLU D 25 ? 0.5494 0.2540 0.5485 0.0237  -0.2296 0.0310  109 GLU D CD  
1647 O  OE1 . GLU D 25 ? 0.5864 0.3844 0.5555 -0.0257 -0.2366 0.0209  109 GLU D OE1 
1648 O  OE2 . GLU D 25 ? 0.5516 0.3222 0.5554 0.0002  -0.2267 0.0359  109 GLU D OE2 
1649 N  N   . ARG D 26 ? 0.3052 0.2299 0.4630 -0.0109 -0.1324 0.0041  110 ARG D N   
1650 C  CA  . ARG D 26 ? 0.2897 0.2365 0.4467 -0.0239 -0.1107 0.0517  110 ARG D CA  
1651 C  C   . ARG D 26 ? 0.3370 0.2489 0.4222 0.0249  -0.1154 0.0298  110 ARG D C   
1652 O  O   . ARG D 26 ? 0.4336 0.1870 0.4211 -0.0450 -0.1378 0.0128  110 ARG D O   
1653 C  CB  . ARG D 26 ? 0.2571 0.2823 0.4636 -0.0551 -0.1117 0.0590  110 ARG D CB  
1654 C  CG  . ARG D 26 ? 0.3333 0.3403 0.4878 -0.0776 -0.0915 0.0426  110 ARG D CG  
1655 C  CD  . ARG D 26 ? 0.4406 0.4362 0.5085 0.0249  -0.0731 0.0429  110 ARG D CD  
1656 N  NE  . ARG D 26 ? 0.5825 0.5648 0.5301 0.0051  -0.0488 0.0432  110 ARG D NE  
1657 C  CZ  . ARG D 26 ? 0.6819 0.5952 0.5477 0.0444  -0.0430 0.0542  110 ARG D CZ  
1658 N  NH1 . ARG D 26 ? 0.7168 0.6128 0.5524 0.0938  -0.0514 0.0458  110 ARG D NH1 
1659 N  NH2 . ARG D 26 ? 0.7493 0.5664 0.5562 0.0185  -0.0220 0.0857  110 ARG D NH2 
1660 N  N   . LEU D 27 ? 0.3049 0.1931 0.4094 -0.0465 -0.1103 0.0308  111 LEU D N   
1661 C  CA  . LEU D 27 ? 0.3223 0.2700 0.4048 -0.0431 -0.1110 0.0674  111 LEU D CA  
1662 C  C   . LEU D 27 ? 0.3104 0.2274 0.3951 -0.0212 -0.1248 0.0407  111 LEU D C   
1663 O  O   . LEU D 27 ? 0.3876 0.2255 0.4092 -0.0276 -0.1274 0.0477  111 LEU D O   
1664 C  CB  . LEU D 27 ? 0.3598 0.2933 0.4038 -0.0397 -0.1020 0.0793  111 LEU D CB  
1665 C  CG  . LEU D 27 ? 0.4134 0.3628 0.4070 -0.0100 -0.1325 0.0589  111 LEU D CG  
1666 C  CD1 . LEU D 27 ? 0.4749 0.4617 0.4155 0.0121  -0.1184 0.0502  111 LEU D CD1 
1667 C  CD2 . LEU D 27 ? 0.5024 0.3902 0.4096 0.0498  -0.1628 0.0295  111 LEU D CD2 
1668 N  N   . GLN D 28 ? 0.2538 0.2558 0.3761 -0.0146 -0.0847 0.0777  112 GLN D N   
1669 C  CA  . GLN D 28 ? 0.2535 0.2505 0.3630 -0.0450 -0.0730 0.0558  112 GLN D CA  
1670 C  C   . GLN D 28 ? 0.3387 0.2533 0.3640 0.0169  -0.0620 0.0576  112 GLN D C   
1671 O  O   . GLN D 28 ? 0.3919 0.2667 0.3629 -0.0264 -0.0762 0.0792  112 GLN D O   
1672 C  CB  . GLN D 28 ? 0.2904 0.2346 0.3610 -0.0384 -0.0793 0.0324  112 GLN D CB  
1673 C  CG  . GLN D 28 ? 0.2593 0.3244 0.3558 -0.0105 -0.0837 0.0048  112 GLN D CG  
1674 C  CD  . GLN D 28 ? 0.2418 0.3126 0.3554 -0.0346 -0.0578 0.0063  112 GLN D CD  
1675 O  OE1 . GLN D 28 ? 0.2641 0.3146 0.3640 0.0052  -0.0588 -0.0289 112 GLN D OE1 
1676 N  NE2 . GLN D 28 ? 0.2835 0.3610 0.3479 -0.0070 -0.0546 0.0352  112 GLN D NE2 
1677 N  N   . ILE D 29 ? 0.2540 0.2486 0.3585 -0.0052 -0.0411 0.0610  113 ILE D N   
1678 C  CA  . ILE D 29 ? 0.2892 0.3069 0.3633 -0.0366 -0.0353 0.0430  113 ILE D CA  
1679 C  C   . ILE D 29 ? 0.2870 0.2974 0.3682 0.0017  -0.0624 0.0821  113 ILE D C   
1680 O  O   . ILE D 29 ? 0.3530 0.3963 0.3636 0.0523  -0.0931 0.0769  113 ILE D O   
1681 C  CB  . ILE D 29 ? 0.3505 0.3508 0.3605 0.0056  -0.0205 0.0388  113 ILE D CB  
1682 C  CG1 . ILE D 29 ? 0.3499 0.3592 0.3628 -0.0085 -0.0185 0.0474  113 ILE D CG1 
1683 C  CG2 . ILE D 29 ? 0.3996 0.3740 0.3580 -0.0042 -0.0188 0.0380  113 ILE D CG2 
1684 C  CD1 . ILE D 29 ? 0.3828 0.2669 0.3642 -0.0107 -0.0004 0.0345  113 ILE D CD1 
1685 N  N   . VAL D 30 ? 0.3263 0.3792 0.3780 -0.0711 -0.0783 0.0488  114 VAL D N   
1686 C  CA  . VAL D 30 ? 0.4033 0.5138 0.3863 -0.0738 -0.0897 0.0355  114 VAL D CA  
1687 C  C   . VAL D 30 ? 0.5067 0.6220 0.3884 0.0165  -0.0898 0.0357  114 VAL D C   
1688 O  O   . VAL D 30 ? 0.5459 0.6567 0.3862 0.0242  -0.0993 0.0122  114 VAL D O   
1689 C  CB  . VAL D 30 ? 0.4417 0.5807 0.3947 -0.1238 -0.0687 0.0325  114 VAL D CB  
1690 C  CG1 . VAL D 30 ? 0.4552 0.6043 0.3979 -0.1068 -0.0659 0.0154  114 VAL D CG1 
1691 C  CG2 . VAL D 30 ? 0.4556 0.5309 0.3934 -0.1157 -0.0976 0.0170  114 VAL D CG2 
1692 N  N   . ASP D 36 ? 0.7743 0.5709 0.4440 -0.0491 -0.0378 -0.0042 120 ASP D N   
1693 C  CA  . ASP D 36 ? 0.7776 0.5913 0.4445 -0.0539 -0.0292 0.0188  120 ASP D CA  
1694 C  C   . ASP D 36 ? 0.6698 0.5491 0.4202 -0.1928 -0.0226 0.0359  120 ASP D C   
1695 O  O   . ASP D 36 ? 0.6927 0.5345 0.4359 -0.2135 -0.0088 0.0307  120 ASP D O   
1696 C  CB  . ASP D 36 ? 0.8862 0.6583 0.4671 0.0476  -0.0358 0.0145  120 ASP D CB  
1697 C  CG  . ASP D 36 ? 0.9548 0.7647 0.4849 0.1007  -0.0438 0.0130  120 ASP D CG  
1698 O  OD1 . ASP D 36 ? 0.9508 0.7523 0.4927 0.1101  -0.0546 0.0268  120 ASP D OD1 
1699 O  OD2 . ASP D 36 ? 0.9994 0.8258 0.4959 0.1066  -0.0454 -0.0147 120 ASP D OD2 
1700 N  N   . TRP D 37 ? 0.5751 0.5217 0.3787 -0.2221 -0.0461 0.0700  121 TRP D N   
1701 C  CA  . TRP D 37 ? 0.5353 0.4838 0.3514 -0.1731 -0.0871 0.0901  121 TRP D CA  
1702 C  C   . TRP D 37 ? 0.4887 0.4410 0.3401 -0.1187 -0.0737 0.0689  121 TRP D C   
1703 O  O   . TRP D 37 ? 0.4665 0.5250 0.3402 -0.1125 -0.0338 0.1021  121 TRP D O   
1704 C  CB  . TRP D 37 ? 0.5503 0.5123 0.3532 -0.1957 -0.1035 0.0976  121 TRP D CB  
1705 C  CG  . TRP D 37 ? 0.5642 0.5022 0.3561 -0.1829 -0.1107 0.1372  121 TRP D CG  
1706 C  CD1 . TRP D 37 ? 0.5702 0.5497 0.3569 -0.1576 -0.1224 0.1500  121 TRP D CD1 
1707 C  CD2 . TRP D 37 ? 0.5699 0.5011 0.3613 -0.1617 -0.1198 0.1445  121 TRP D CD2 
1708 N  NE1 . TRP D 37 ? 0.5506 0.5580 0.3598 -0.1612 -0.1355 0.1425  121 TRP D NE1 
1709 C  CE2 . TRP D 37 ? 0.5481 0.5249 0.3613 -0.1408 -0.1373 0.1441  121 TRP D CE2 
1710 C  CE3 . TRP D 37 ? 0.5644 0.4730 0.3664 -0.2324 -0.1329 0.1447  121 TRP D CE3 
1711 C  CZ2 . TRP D 37 ? 0.5552 0.5104 0.3655 -0.1233 -0.1402 0.1603  121 TRP D CZ2 
1712 C  CZ3 . TRP D 37 ? 0.5754 0.4607 0.3664 -0.1660 -0.1401 0.1619  121 TRP D CZ3 
1713 C  CH2 . TRP D 37 ? 0.5483 0.5064 0.3661 -0.1414 -0.1380 0.1670  121 TRP D CH2 
1714 N  N   . TRP D 38 ? 0.4338 0.3572 0.3310 -0.1450 -0.0816 0.0679  122 TRP D N   
1715 C  CA  . TRP D 38 ? 0.3830 0.3730 0.3286 -0.1239 -0.0918 0.0551  122 TRP D CA  
1716 C  C   . TRP D 38 ? 0.3646 0.3527 0.3294 -0.1478 -0.1025 0.0600  122 TRP D C   
1717 O  O   . TRP D 38 ? 0.4013 0.3520 0.3217 -0.0661 -0.1129 0.0442  122 TRP D O   
1718 C  CB  . TRP D 38 ? 0.3610 0.3374 0.3369 -0.0787 -0.0714 0.0704  122 TRP D CB  
1719 C  CG  . TRP D 38 ? 0.3711 0.3456 0.3472 -0.0384 -0.0573 0.0700  122 TRP D CG  
1720 C  CD1 . TRP D 38 ? 0.3389 0.3915 0.3574 -0.0512 -0.0423 0.0544  122 TRP D CD1 
1721 C  CD2 . TRP D 38 ? 0.3993 0.3220 0.3472 -0.0926 -0.0508 0.0708  122 TRP D CD2 
1722 N  NE1 . TRP D 38 ? 0.3555 0.3743 0.3615 -0.0705 -0.0310 0.0558  122 TRP D NE1 
1723 C  CE2 . TRP D 38 ? 0.3806 0.3594 0.3514 -0.0697 -0.0335 0.0621  122 TRP D CE2 
1724 C  CE3 . TRP D 38 ? 0.3717 0.3022 0.3521 -0.0688 -0.0477 0.0345  122 TRP D CE3 
1725 C  CZ2 . TRP D 38 ? 0.3946 0.3200 0.3582 -0.0515 0.0181  0.0830  122 TRP D CZ2 
1726 C  CZ3 . TRP D 38 ? 0.3289 0.3172 0.3604 -0.0562 -0.0117 0.0533  122 TRP D CZ3 
1727 C  CH2 . TRP D 38 ? 0.4074 0.3442 0.3641 0.0701  0.0009  0.0532  122 TRP D CH2 
1728 N  N   . LEU D 39 ? 0.4019 0.3566 0.3313 -0.0852 -0.1140 0.0573  123 LEU D N   
1729 C  CA  . LEU D 39 ? 0.3916 0.3415 0.3489 -0.1396 -0.1103 0.0726  123 LEU D CA  
1730 C  C   . LEU D 39 ? 0.3580 0.3721 0.3560 -0.1331 -0.1133 0.0855  123 LEU D C   
1731 O  O   . LEU D 39 ? 0.4600 0.3675 0.3643 -0.1123 -0.1312 0.0888  123 LEU D O   
1732 C  CB  . LEU D 39 ? 0.3718 0.3600 0.3510 -0.1336 -0.1405 0.0619  123 LEU D CB  
1733 C  CG  . LEU D 39 ? 0.4125 0.3484 0.3481 -0.0730 -0.1505 0.0246  123 LEU D CG  
1734 C  CD1 . LEU D 39 ? 0.4606 0.3789 0.3380 0.0018  -0.1531 0.0604  123 LEU D CD1 
1735 C  CD2 . LEU D 39 ? 0.4237 0.3410 0.3573 -0.1304 -0.1206 -0.0146 123 LEU D CD2 
1736 N  N   . ALA D 40 ? 0.3061 0.3497 0.3697 -0.1327 -0.0983 0.0736  124 ALA D N   
1737 C  CA  . ALA D 40 ? 0.3287 0.3083 0.3788 -0.1223 -0.0766 0.1077  124 ALA D CA  
1738 C  C   . ALA D 40 ? 0.4119 0.2733 0.3917 -0.1094 -0.0724 0.0925  124 ALA D C   
1739 O  O   . ALA D 40 ? 0.4197 0.2777 0.4017 -0.0931 -0.0848 0.1151  124 ALA D O   
1740 C  CB  . ALA D 40 ? 0.3478 0.3504 0.3793 -0.1117 -0.1011 0.0466  124 ALA D CB  
1741 N  N   . HIS D 41 ? 0.3723 0.3331 0.3949 -0.1077 -0.0894 0.0720  125 HIS D N   
1742 C  CA  . HIS D 41 ? 0.3524 0.2713 0.4016 -0.0467 -0.1190 0.0477  125 HIS D CA  
1743 C  C   . HIS D 41 ? 0.3618 0.2474 0.4161 -0.0670 -0.1259 0.0583  125 HIS D C   
1744 O  O   . HIS D 41 ? 0.3582 0.2346 0.4083 -0.0366 -0.1182 0.0830  125 HIS D O   
1745 C  CB  . HIS D 41 ? 0.3589 0.3132 0.3960 -0.0698 -0.1177 0.0459  125 HIS D CB  
1746 C  CG  . HIS D 41 ? 0.4185 0.3479 0.4018 -0.1299 -0.0872 0.0443  125 HIS D CG  
1747 N  ND1 . HIS D 41 ? 0.4371 0.4784 0.4096 -0.2080 -0.0461 0.0571  125 HIS D ND1 
1748 C  CD2 . HIS D 41 ? 0.3702 0.4710 0.4069 -0.1993 -0.0550 0.0097  125 HIS D CD2 
1749 C  CE1 . HIS D 41 ? 0.4538 0.4316 0.4090 -0.2458 -0.0281 0.0596  125 HIS D CE1 
1750 N  NE2 . HIS D 41 ? 0.4315 0.4806 0.4066 -0.2080 -0.0036 0.0336  125 HIS D NE2 
1751 N  N   . SER D 42 ? 0.3607 0.2676 0.4423 -0.0500 -0.1489 0.0392  126 SER D N   
1752 C  CA  . SER D 42 ? 0.3732 0.2514 0.4703 -0.0312 -0.1550 0.0257  126 SER D CA  
1753 C  C   . SER D 42 ? 0.3793 0.2228 0.4935 -0.0686 -0.1446 0.0128  126 SER D C   
1754 O  O   . SER D 42 ? 0.3868 0.2208 0.5007 -0.0263 -0.1386 0.0197  126 SER D O   
1755 C  CB  . SER D 42 ? 0.3462 0.3006 0.4822 -0.0122 -0.1510 0.0609  126 SER D CB  
1756 O  OG  . SER D 42 ? 0.4132 0.2762 0.4939 0.0481  -0.1310 0.0670  126 SER D OG  
1757 N  N   . LEU D 43 ? 0.3746 0.2147 0.5122 -0.0215 -0.1504 0.0050  127 LEU D N   
1758 C  CA  . LEU D 43 ? 0.3794 0.2567 0.5377 -0.0133 -0.1452 0.0189  127 LEU D CA  
1759 C  C   . LEU D 43 ? 0.3959 0.2615 0.5741 -0.0046 -0.1348 0.0114  127 LEU D C   
1760 O  O   . LEU D 43 ? 0.3730 0.3763 0.5819 -0.0513 -0.1177 0.0185  127 LEU D O   
1761 C  CB  . LEU D 43 ? 0.4117 0.2603 0.5325 -0.0148 -0.1150 0.0545  127 LEU D CB  
1762 C  CG  . LEU D 43 ? 0.4334 0.3943 0.5339 0.0274  -0.0953 0.0980  127 LEU D CG  
1763 C  CD1 . LEU D 43 ? 0.4638 0.3432 0.5364 -0.0036 -0.0897 0.1094  127 LEU D CD1 
1764 C  CD2 . LEU D 43 ? 0.4109 0.3517 0.5293 0.0145  -0.1167 0.1384  127 LEU D CD2 
1765 N  N   . SER D 44 ? 0.3293 0.2659 0.6022 -0.0056 -0.1710 0.0138  128 SER D N   
1766 C  CA  . SER D 44 ? 0.3681 0.2785 0.6278 0.0405  -0.1598 0.0329  128 SER D CA  
1767 C  C   . SER D 44 ? 0.4702 0.3146 0.6492 0.0051  -0.1218 0.0535  128 SER D C   
1768 O  O   . SER D 44 ? 0.4897 0.3612 0.6566 0.0047  -0.1108 0.0380  128 SER D O   
1769 C  CB  . SER D 44 ? 0.4637 0.3109 0.6348 0.0478  -0.1560 0.0203  128 SER D CB  
1770 O  OG  . SER D 44 ? 0.5115 0.3955 0.6423 0.0520  -0.1642 0.0029  128 SER D OG  
1771 N  N   . THR D 45 ? 0.4445 0.2865 0.6602 -0.0705 -0.1275 0.0809  129 THR D N   
1772 C  CA  . THR D 45 ? 0.5069 0.2077 0.6624 -0.0019 -0.1457 0.0670  129 THR D CA  
1773 C  C   . THR D 45 ? 0.5255 0.2227 0.6627 0.0319  -0.1364 0.0374  129 THR D C   
1774 O  O   . THR D 45 ? 0.5294 0.2273 0.6754 0.0236  -0.1260 0.0483  129 THR D O   
1775 C  CB  . THR D 45 ? 0.4995 0.2709 0.6598 -0.0338 -0.1929 0.0617  129 THR D CB  
1776 O  OG1 . THR D 45 ? 0.5786 0.2797 0.6604 0.0157  -0.1801 0.0810  129 THR D OG1 
1777 C  CG2 . THR D 45 ? 0.4739 0.2733 0.6610 -0.0650 -0.2113 0.0892  129 THR D CG2 
1778 N  N   . GLY D 46 ? 0.4733 0.2304 0.6488 -0.0035 -0.1398 0.0260  130 GLY D N   
1779 C  CA  . GLY D 46 ? 0.5048 0.2134 0.6363 -0.0244 -0.1331 0.0099  130 GLY D CA  
1780 C  C   . GLY D 46 ? 0.4792 0.2632 0.6234 0.0081  -0.1521 0.0310  130 GLY D C   
1781 O  O   . GLY D 46 ? 0.4052 0.3471 0.6232 -0.0523 -0.1665 0.0454  130 GLY D O   
1782 N  N   . GLN D 47 ? 0.5360 0.3227 0.6098 0.0077  -0.1672 0.0544  131 GLN D N   
1783 C  CA  . GLN D 47 ? 0.5808 0.3571 0.5980 -0.0400 -0.1707 0.0836  131 GLN D CA  
1784 C  C   . GLN D 47 ? 0.5704 0.3161 0.5803 -0.0187 -0.1643 0.0917  131 GLN D C   
1785 O  O   . GLN D 47 ? 0.5410 0.2496 0.5846 -0.0401 -0.1550 0.1143  131 GLN D O   
1786 C  CB  . GLN D 47 ? 0.6655 0.4575 0.6039 -0.0104 -0.1846 0.0972  131 GLN D CB  
1787 C  CG  . GLN D 47 ? 0.7743 0.4988 0.6123 0.0163  -0.1915 0.0956  131 GLN D CG  
1788 C  CD  . GLN D 47 ? 0.8686 0.5882 0.6181 0.0775  -0.2036 0.0926  131 GLN D CD  
1789 O  OE1 . GLN D 47 ? 0.8711 0.5919 0.6209 0.0978  -0.2259 0.0956  131 GLN D OE1 
1790 N  NE2 . GLN D 47 ? 0.9203 0.5574 0.6219 0.0878  -0.1891 0.0850  131 GLN D NE2 
1791 N  N   . THR D 48 ? 0.5435 0.3555 0.5601 -0.1164 -0.1809 0.0714  132 THR D N   
1792 C  CA  . THR D 48 ? 0.5273 0.3650 0.5388 -0.1444 -0.1565 0.1057  132 THR D CA  
1793 C  C   . THR D 48 ? 0.5568 0.3496 0.5158 -0.1506 -0.1580 0.1260  132 THR D C   
1794 O  O   . THR D 48 ? 0.5830 0.3579 0.5261 -0.1830 -0.1462 0.1352  132 THR D O   
1795 C  CB  . THR D 48 ? 0.5477 0.3390 0.5442 -0.1959 -0.1335 0.0882  132 THR D CB  
1796 O  OG1 . THR D 48 ? 0.5548 0.4784 0.5504 -0.1495 -0.1259 0.0884  132 THR D OG1 
1797 C  CG2 . THR D 48 ? 0.5744 0.3962 0.5448 -0.1791 -0.1160 0.1044  132 THR D CG2 
1798 N  N   . GLY D 49 ? 0.5355 0.3103 0.4863 -0.1631 -0.1663 0.1238  133 GLY D N   
1799 C  CA  . GLY D 49 ? 0.5265 0.3044 0.4641 -0.1305 -0.1588 0.1248  133 GLY D CA  
1800 C  C   . GLY D 49 ? 0.5124 0.2874 0.4310 -0.1204 -0.1672 0.1235  133 GLY D C   
1801 O  O   . GLY D 49 ? 0.5459 0.3174 0.4255 -0.1049 -0.1617 0.1646  133 GLY D O   
1802 N  N   . TYR D 50 ? 0.4632 0.4058 0.4039 -0.1745 -0.1549 0.0966  134 TYR D N   
1803 C  CA  . TYR D 50 ? 0.4327 0.4202 0.3815 -0.1954 -0.1281 0.1164  134 TYR D CA  
1804 C  C   . TYR D 50 ? 0.4548 0.3771 0.3656 -0.1773 -0.1018 0.1253  134 TYR D C   
1805 O  O   . TYR D 50 ? 0.5447 0.4063 0.3670 -0.0431 -0.1038 0.1258  134 TYR D O   
1806 C  CB  . TYR D 50 ? 0.4596 0.4922 0.3688 -0.1654 -0.1199 0.1127  134 TYR D CB  
1807 C  CG  . TYR D 50 ? 0.4925 0.5173 0.3687 -0.2179 -0.0956 0.0926  134 TYR D CG  
1808 C  CD1 . TYR D 50 ? 0.4870 0.5691 0.3712 -0.2043 -0.0881 0.0847  134 TYR D CD1 
1809 C  CD2 . TYR D 50 ? 0.5267 0.5877 0.3719 -0.2038 -0.0905 0.0561  134 TYR D CD2 
1810 C  CE1 . TYR D 50 ? 0.4495 0.6881 0.3758 -0.1872 -0.0862 0.0623  134 TYR D CE1 
1811 C  CE2 . TYR D 50 ? 0.5035 0.6175 0.3753 -0.1991 -0.0681 0.0443  134 TYR D CE2 
1812 C  CZ  . TYR D 50 ? 0.4686 0.6944 0.3779 -0.1877 -0.0818 0.0237  134 TYR D CZ  
1813 O  OH  . TYR D 50 ? 0.4735 0.7997 0.3897 -0.1902 -0.0621 0.0023  134 TYR D OH  
1814 N  N   A ILE D 51 ? 0.4417 0.3372 0.3602 -0.1688 -0.1161 0.0769  135 ILE D N   
1815 N  N   B ILE D 51 ? 0.4536 0.3675 0.3588 -0.1467 -0.1100 0.1070  135 ILE D N   
1816 C  CA  A ILE D 51 ? 0.4081 0.3887 0.3542 -0.1898 -0.1146 0.0761  135 ILE D CA  
1817 C  CA  B ILE D 51 ? 0.4419 0.3938 0.3504 -0.1323 -0.1131 0.1005  135 ILE D CA  
1818 C  C   A ILE D 51 ? 0.4170 0.3803 0.3390 -0.1171 -0.1010 0.0797  135 ILE D C   
1819 C  C   B ILE D 51 ? 0.4344 0.3891 0.3448 -0.1154 -0.1122 0.0907  135 ILE D C   
1820 O  O   A ILE D 51 ? 0.3918 0.4444 0.3310 -0.0902 -0.0760 0.0590  135 ILE D O   
1821 O  O   B ILE D 51 ? 0.4272 0.4099 0.3437 -0.1031 -0.1089 0.0750  135 ILE D O   
1822 C  CB  A ILE D 51 ? 0.4445 0.3500 0.3545 -0.1357 -0.1142 0.0951  135 ILE D CB  
1823 C  CB  B ILE D 51 ? 0.4489 0.3600 0.3443 -0.1250 -0.1143 0.1124  135 ILE D CB  
1824 C  CG1 A ILE D 51 ? 0.4448 0.3022 0.3642 -0.1473 -0.1070 0.0821  135 ILE D CG1 
1825 C  CG1 B ILE D 51 ? 0.4414 0.3231 0.3419 -0.1364 -0.1083 0.1231  135 ILE D CG1 
1826 C  CG2 A ILE D 51 ? 0.4703 0.3733 0.3533 -0.0739 -0.1187 0.0949  135 ILE D CG2 
1827 C  CG2 B ILE D 51 ? 0.4565 0.3629 0.3438 -0.1063 -0.1174 0.1072  135 ILE D CG2 
1828 C  CD1 A ILE D 51 ? 0.4754 0.3779 0.3679 -0.0809 -0.1092 0.0727  135 ILE D CD1 
1829 C  CD1 B ILE D 51 ? 0.4232 0.3118 0.3371 -0.1707 -0.1112 0.1335  135 ILE D CD1 
1830 N  N   . PRO D 52 ? 0.4154 0.4052 0.3445 -0.1221 -0.1151 0.0944  136 PRO D N   
1831 C  CA  . PRO D 52 ? 0.4112 0.3829 0.3513 -0.1031 -0.0855 0.0791  136 PRO D CA  
1832 C  C   . PRO D 52 ? 0.4070 0.3943 0.3582 -0.0612 -0.0735 0.0453  136 PRO D C   
1833 O  O   . PRO D 52 ? 0.3678 0.4014 0.3702 -0.0707 -0.0485 0.0493  136 PRO D O   
1834 C  CB  . PRO D 52 ? 0.4164 0.4487 0.3500 -0.1174 -0.1059 0.0685  136 PRO D CB  
1835 C  CG  . PRO D 52 ? 0.4854 0.4437 0.3484 -0.0792 -0.1089 0.0759  136 PRO D CG  
1836 C  CD  . PRO D 52 ? 0.4612 0.4713 0.3454 -0.0657 -0.1218 0.1016  136 PRO D CD  
1837 N  N   . SER D 53 ? 0.3805 0.4072 0.3550 -0.0791 -0.0859 0.0450  137 SER D N   
1838 C  CA  . SER D 53 ? 0.3763 0.4187 0.3589 -0.0598 -0.0621 0.0700  137 SER D CA  
1839 C  C   . SER D 53 ? 0.4049 0.3456 0.3505 -0.1080 -0.0354 0.0853  137 SER D C   
1840 O  O   . SER D 53 ? 0.3917 0.4106 0.3474 -0.1149 -0.0095 0.0846  137 SER D O   
1841 C  CB  . SER D 53 ? 0.3677 0.4725 0.3668 -0.0600 -0.0359 0.0815  137 SER D CB  
1842 O  OG  . SER D 53 ? 0.4518 0.5284 0.3806 -0.0098 -0.0206 0.0681  137 SER D OG  
1843 N  N   . ASN D 54 ? 0.3815 0.3855 0.3482 -0.1104 -0.0704 0.0601  138 ASN D N   
1844 C  CA  . ASN D 54 ? 0.4551 0.3958 0.3488 -0.0563 -0.0706 0.0586  138 ASN D CA  
1845 C  C   . ASN D 54 ? 0.4511 0.3622 0.3552 -0.0533 -0.0702 0.0379  138 ASN D C   
1846 O  O   . ASN D 54 ? 0.4047 0.4279 0.3830 -0.0715 -0.0514 0.0034  138 ASN D O   
1847 C  CB  . ASN D 54 ? 0.4855 0.4569 0.3463 -0.0541 -0.0600 0.0557  138 ASN D CB  
1848 C  CG  . ASN D 54 ? 0.5272 0.5149 0.3504 -0.0837 -0.0527 0.0290  138 ASN D CG  
1849 O  OD1 . ASN D 54 ? 0.5390 0.5215 0.3487 -0.0802 -0.0345 0.0327  138 ASN D OD1 
1850 N  ND2 . ASN D 54 ? 0.6077 0.6321 0.3608 -0.0481 -0.0447 0.0229  138 ASN D ND2 
1851 N  N   . TYR D 55 ? 0.4341 0.3452 0.3313 -0.0639 -0.0751 0.0630  139 TYR D N   
1852 C  CA  . TYR D 55 ? 0.3932 0.2981 0.3180 -0.0721 -0.0840 0.0766  139 TYR D CA  
1853 C  C   . TYR D 55 ? 0.3557 0.3144 0.3202 -0.0690 -0.0687 0.0650  139 TYR D C   
1854 O  O   . TYR D 55 ? 0.3798 0.3400 0.3284 -0.0336 -0.0735 0.0550  139 TYR D O   
1855 C  CB  . TYR D 55 ? 0.4228 0.3230 0.3012 -0.0791 -0.1072 0.0697  139 TYR D CB  
1856 C  CG  . TYR D 55 ? 0.4009 0.3464 0.2947 -0.1148 -0.1116 0.0905  139 TYR D CG  
1857 C  CD1 . TYR D 55 ? 0.4513 0.3646 0.2949 -0.0804 -0.1087 0.0679  139 TYR D CD1 
1858 C  CD2 . TYR D 55 ? 0.4517 0.3510 0.2918 -0.0635 -0.1243 0.0870  139 TYR D CD2 
1859 C  CE1 . TYR D 55 ? 0.4582 0.3751 0.2924 -0.0687 -0.1174 0.0693  139 TYR D CE1 
1860 C  CE2 . TYR D 55 ? 0.4707 0.4365 0.2923 -0.0196 -0.0990 0.1051  139 TYR D CE2 
1861 C  CZ  . TYR D 55 ? 0.4755 0.4486 0.2975 -0.0457 -0.1037 0.0871  139 TYR D CZ  
1862 O  OH  . TYR D 55 ? 0.5303 0.5017 0.3032 -0.0823 -0.0911 0.1087  139 TYR D OH  
1863 N  N   . VAL D 56 ? 0.3630 0.2882 0.3143 -0.0729 -0.0747 0.0799  140 VAL D N   
1864 C  CA  . VAL D 56 ? 0.3960 0.2280 0.3101 -0.0623 -0.0670 0.0366  140 VAL D CA  
1865 C  C   . VAL D 56 ? 0.3658 0.2611 0.3134 -0.0480 -0.0408 0.0211  140 VAL D C   
1866 O  O   . VAL D 56 ? 0.3806 0.3342 0.3211 -0.0071 -0.0510 0.0325  140 VAL D O   
1867 C  CB  . VAL D 56 ? 0.3244 0.2695 0.3177 -0.0798 -0.0671 0.0541  140 VAL D CB  
1868 C  CG1 . VAL D 56 ? 0.3658 0.2937 0.3256 -0.0510 -0.0653 0.0658  140 VAL D CG1 
1869 C  CG2 . VAL D 56 ? 0.3142 0.3716 0.3195 -0.0704 -0.0565 0.0780  140 VAL D CG2 
1870 N  N   . ALA D 57 ? 0.3574 0.2328 0.3107 -0.0632 -0.0439 0.0266  141 ALA D N   
1871 C  CA  . ALA D 57 ? 0.3698 0.1710 0.3104 -0.0416 -0.0186 0.0262  141 ALA D CA  
1872 C  C   . ALA D 57 ? 0.3435 0.2328 0.3070 0.0331  -0.0389 0.0064  141 ALA D C   
1873 O  O   . ALA D 57 ? 0.3491 0.2176 0.3049 0.0010  -0.0419 -0.0106 141 ALA D O   
1874 C  CB  . ALA D 57 ? 0.3641 0.1885 0.3159 -0.1112 -0.0086 0.0256  141 ALA D CB  
1875 N  N   . PRO D 58 ? 0.3370 0.1954 0.3034 -0.0117 -0.0408 -0.0058 142 PRO D N   
1876 C  CA  . PRO D 58 ? 0.3222 0.2364 0.3152 0.0344  -0.0275 -0.0004 142 PRO D CA  
1877 C  C   . PRO D 58 ? 0.3388 0.2674 0.3414 0.0470  -0.0403 0.0045  142 PRO D C   
1878 O  O   . PRO D 58 ? 0.3253 0.3202 0.3378 0.0245  -0.0523 0.0049  142 PRO D O   
1879 C  CB  . PRO D 58 ? 0.3895 0.2157 0.3101 0.0507  -0.0191 -0.0093 142 PRO D CB  
1880 C  CG  . PRO D 58 ? 0.3950 0.2879 0.2993 0.0470  -0.0184 0.0072  142 PRO D CG  
1881 C  CD  . PRO D 58 ? 0.3620 0.1980 0.2997 0.0444  -0.0256 0.0244  142 PRO D CD  
1882 N  N   . SER D 59 ? 0.2954 0.3235 0.3757 0.0287  -0.0520 0.0180  143 SER D N   
1883 C  CA  . SER D 59 ? 0.4359 0.3285 0.4230 -0.0261 -0.0247 0.0420  143 SER D CA  
1884 C  C   . SER D 59 ? 0.4835 0.3940 0.4603 -0.0378 -0.0399 0.0609  143 SER D C   
1885 O  O   . SER D 59 ? 0.4470 0.4328 0.4784 -0.0904 -0.0481 0.0557  143 SER D O   
1886 C  CB  . SER D 59 ? 0.5183 0.3198 0.4314 0.0176  -0.0048 0.0248  143 SER D CB  
1887 O  OG  . SER D 59 ? 0.6341 0.3424 0.4466 -0.0274 0.0003  0.0261  143 SER D OG  
1888 O  OXT . SER D 59 ? 0.4677 0.3488 0.4721 -0.1154 -0.0348 0.0856  143 SER D OXT 
1889 NI NI  . NI  E .  ? 0.2542 0.3143 0.4662 0.0375  -0.0506 0.0734  201 NI  A NI  
1902 NI NI  . NI  H .  ? 0.2716 0.2225 0.3419 0.0106  0.0572  -0.0297 201 NI  B NI  
# 
