data_2QSQ
# 
_entry.id   2QSQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.387 
_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   2QSQ         pdb_00002qsq 10.2210/pdb2qsq/pdb 
RCSB  RCSB044007   ?            ?                   
WWPDB D_1000044007 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2008-01-01 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-10-25 
4 'Structure model' 1 3 2024-02-21 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Refinement description'    
4 4 'Structure model' 'Data collection'           
5 4 'Structure model' 'Database references'       
6 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software       
2 4 'Structure model' chem_comp_atom 
3 4 'Structure model' chem_comp_bond 
4 4 'Structure model' database_2     
5 4 'Structure model' struct_site    
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
3 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
4 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
5 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
_pdbx_database_status.entry_id                        2QSQ 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2007-07-31 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2QST 
_pdbx_database_related.details        
;Structure of the V39C mutant of the N-terminal domain 
of carcinoembryonic antigen (CEA)
;
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Le Trong, I.'   1 
'Korotkova, N.'  2 
'Moseley, S.L.'  3 
'Stenkamp, R.E.' 4 
# 
_citation.id                        primary 
_citation.title                     
'Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation.' 
_citation.journal_abbrev            Mol.Microbiol. 
_citation.journal_volume            67 
_citation.page_first                420 
_citation.page_last                 434 
_citation.year                      2008 
_citation.journal_id_ASTM           MOMIEE 
_citation.country                   UK 
_citation.journal_id_ISSN           0950-382X 
_citation.journal_id_CSD            2007 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18086185 
_citation.pdbx_database_id_DOI      10.1111/j.1365-2958.2007.06054.x 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Korotkova, N.'  1  ? 
primary 'Yang, Y.'       2  ? 
primary 'Le Trong, I.'   3  ? 
primary 'Cota, E.'       4  ? 
primary 'Demeler, B.'    5  ? 
primary 'Marchant, J.'   6  ? 
primary 'Thomas, W.E.'   7  ? 
primary 'Stenkamp, R.E.' 8  ? 
primary 'Moseley, S.L.'  9  ? 
primary 'Matthews, S.'   10 ? 
# 
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 'Carcinoembryonic antigen-related cell adhesion molecule 5' 12430.989 2   ? ? 
'N-terminal domain of CEA (UNP residues 34-110)' ? 
2 non-polymer syn 'CHLORIDE ION'                                              35.453    2   ? ? ? ? 
3 non-polymer syn GLYCEROL                                                    92.094    4   ? ? ? ? 
4 water       nat water                                                       18.015    193 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carcinoembryonic antigen, CEA, Meconium antigen 100, CD66e antigen' 
# 
_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       
;AKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNII
QNDAGFYTLHVIKSDLVNEEATGQFRVYPEL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNII
QNDAGFYTLHVIKSDLVNEEATGQFRVYPEL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION' CL  
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   ALA n 
1 2   LYS n 
1 3   LEU n 
1 4   THR n 
1 5   ILE n 
1 6   GLU n 
1 7   SER n 
1 8   THR n 
1 9   PRO n 
1 10  PHE n 
1 11  ASN n 
1 12  VAL n 
1 13  ALA n 
1 14  GLU n 
1 15  GLY n 
1 16  LYS n 
1 17  GLU n 
1 18  VAL n 
1 19  LEU n 
1 20  LEU n 
1 21  LEU n 
1 22  VAL n 
1 23  HIS n 
1 24  ASN n 
1 25  LEU n 
1 26  PRO n 
1 27  GLN n 
1 28  HIS n 
1 29  LEU n 
1 30  PHE n 
1 31  GLY n 
1 32  TYR n 
1 33  SER n 
1 34  TRP n 
1 35  TYR n 
1 36  LYS n 
1 37  GLY n 
1 38  GLU n 
1 39  ARG n 
1 40  VAL n 
1 41  ASP n 
1 42  GLY n 
1 43  ASN n 
1 44  ARG n 
1 45  GLN n 
1 46  ILE n 
1 47  ILE n 
1 48  GLY n 
1 49  TYR n 
1 50  VAL n 
1 51  ILE n 
1 52  GLY n 
1 53  THR n 
1 54  GLN n 
1 55  GLN n 
1 56  ALA n 
1 57  THR n 
1 58  PRO n 
1 59  GLY n 
1 60  PRO n 
1 61  ALA n 
1 62  TYR n 
1 63  SER n 
1 64  GLY n 
1 65  ARG n 
1 66  GLU n 
1 67  ILE n 
1 68  ILE n 
1 69  TYR n 
1 70  PRO n 
1 71  ASN n 
1 72  ALA n 
1 73  SER n 
1 74  LEU n 
1 75  LEU n 
1 76  ILE n 
1 77  GLN n 
1 78  ASN n 
1 79  ILE n 
1 80  ILE n 
1 81  GLN n 
1 82  ASN n 
1 83  ASP n 
1 84  ALA n 
1 85  GLY n 
1 86  PHE n 
1 87  TYR n 
1 88  THR n 
1 89  LEU n 
1 90  HIS n 
1 91  VAL n 
1 92  ILE n 
1 93  LYS n 
1 94  SER n 
1 95  ASP n 
1 96  LEU n 
1 97  VAL n 
1 98  ASN n 
1 99  GLU n 
1 100 GLU n 
1 101 ALA n 
1 102 THR n 
1 103 GLY n 
1 104 GLN n 
1 105 PHE n 
1 106 ARG n 
1 107 VAL n 
1 108 TYR n 
1 109 PRO n 
1 110 GLU n 
1 111 LEU 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 'CEACAM5, CEA' 
_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                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET-21d 
_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 
CL  non-polymer         . 'CHLORIDE ION'  ?                               'Cl -1'          35.453  
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 
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   ALA 1   0   0   ALA ALA A . n 
A 1 2   LYS 2   1   1   LYS LYS A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   THR 4   3   3   THR THR A . n 
A 1 5   ILE 5   4   4   ILE ILE A . n 
A 1 6   GLU 6   5   5   GLU GLU A . n 
A 1 7   SER 7   6   6   SER SER A . n 
A 1 8   THR 8   7   7   THR THR A . n 
A 1 9   PRO 9   8   8   PRO PRO A . n 
A 1 10  PHE 10  9   9   PHE PHE A . n 
A 1 11  ASN 11  10  10  ASN ASN A . n 
A 1 12  VAL 12  11  11  VAL VAL A . n 
A 1 13  ALA 13  12  12  ALA ALA A . n 
A 1 14  GLU 14  13  13  GLU GLU A . n 
A 1 15  GLY 15  14  14  GLY GLY A . n 
A 1 16  LYS 16  15  15  LYS LYS A . n 
A 1 17  GLU 17  16  16  GLU GLU A . n 
A 1 18  VAL 18  17  17  VAL VAL A . n 
A 1 19  LEU 19  18  18  LEU LEU A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  LEU 21  20  20  LEU LEU A . n 
A 1 22  VAL 22  21  21  VAL VAL A . n 
A 1 23  HIS 23  22  22  HIS HIS A . n 
A 1 24  ASN 24  23  23  ASN ASN A . n 
A 1 25  LEU 25  24  24  LEU LEU A . n 
A 1 26  PRO 26  25  25  PRO PRO A . n 
A 1 27  GLN 27  26  26  GLN GLN A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  LEU 29  28  28  LEU LEU A . n 
A 1 30  PHE 30  29  29  PHE PHE A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  TYR 32  31  31  TYR TYR A . n 
A 1 33  SER 33  32  32  SER SER A . n 
A 1 34  TRP 34  33  33  TRP TRP A . n 
A 1 35  TYR 35  34  34  TYR TYR A . n 
A 1 36  LYS 36  35  35  LYS LYS A . n 
A 1 37  GLY 37  36  36  GLY GLY A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ARG 39  38  38  ARG ARG A . n 
A 1 40  VAL 40  39  39  VAL VAL A . n 
A 1 41  ASP 41  40  40  ASP ASP A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  ASN 43  42  42  ASN ASN A . n 
A 1 44  ARG 44  43  43  ARG ARG A . n 
A 1 45  GLN 45  44  44  GLN GLN A . n 
A 1 46  ILE 46  45  45  ILE ILE A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  GLY 48  47  47  GLY GLY A . n 
A 1 49  TYR 49  48  48  TYR TYR A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  ILE 51  50  50  ILE ILE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  THR 53  52  52  THR THR A . n 
A 1 54  GLN 54  53  53  GLN GLN A . n 
A 1 55  GLN 55  54  54  GLN GLN A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  THR 57  56  56  THR THR A . n 
A 1 58  PRO 58  57  57  PRO PRO A . n 
A 1 59  GLY 59  58  58  GLY GLY A . n 
A 1 60  PRO 60  59  59  PRO PRO A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  TYR 62  61  61  TYR TYR A . n 
A 1 63  SER 63  62  62  SER SER A . n 
A 1 64  GLY 64  63  63  GLY GLY A . n 
A 1 65  ARG 65  64  64  ARG ARG A . n 
A 1 66  GLU 66  65  65  GLU GLU A . n 
A 1 67  ILE 67  66  66  ILE ILE A . n 
A 1 68  ILE 68  67  67  ILE ILE A . n 
A 1 69  TYR 69  68  68  TYR TYR A . n 
A 1 70  PRO 70  69  69  PRO PRO A . n 
A 1 71  ASN 71  70  70  ASN ASN A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  SER 73  72  72  SER SER A . n 
A 1 74  LEU 74  73  73  LEU LEU A . n 
A 1 75  LEU 75  74  74  LEU LEU A . n 
A 1 76  ILE 76  75  75  ILE ILE A . n 
A 1 77  GLN 77  76  76  GLN GLN A . n 
A 1 78  ASN 78  77  77  ASN ASN A . n 
A 1 79  ILE 79  78  78  ILE ILE A . n 
A 1 80  ILE 80  79  79  ILE ILE A . n 
A 1 81  GLN 81  80  80  GLN GLN A . n 
A 1 82  ASN 82  81  81  ASN ASN A . n 
A 1 83  ASP 83  82  82  ASP ASP A . n 
A 1 84  ALA 84  83  83  ALA ALA A . n 
A 1 85  GLY 85  84  84  GLY GLY A . n 
A 1 86  PHE 86  85  85  PHE PHE A . n 
A 1 87  TYR 87  86  86  TYR TYR A . n 
A 1 88  THR 88  87  87  THR THR A . n 
A 1 89  LEU 89  88  88  LEU LEU A . n 
A 1 90  HIS 90  89  89  HIS HIS A . n 
A 1 91  VAL 91  90  90  VAL VAL A . n 
A 1 92  ILE 92  91  91  ILE ILE A . n 
A 1 93  LYS 93  92  92  LYS LYS A . n 
A 1 94  SER 94  93  93  SER SER A . n 
A 1 95  ASP 95  94  94  ASP ASP A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  VAL 97  96  96  VAL VAL A . n 
A 1 98  ASN 98  97  97  ASN ASN A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 GLU 100 99  99  GLU GLU A . n 
A 1 101 ALA 101 100 100 ALA ALA A . n 
A 1 102 THR 102 101 101 THR THR A . n 
A 1 103 GLY 103 102 102 GLY GLY A . n 
A 1 104 GLN 104 103 103 GLN GLN A . n 
A 1 105 PHE 105 104 104 PHE PHE A . n 
A 1 106 ARG 106 105 105 ARG ARG A . n 
A 1 107 VAL 107 106 106 VAL VAL A . n 
A 1 108 TYR 108 107 107 TYR TYR A . n 
A 1 109 PRO 109 108 108 PRO PRO A . n 
A 1 110 GLU 110 109 109 GLU GLU A . n 
A 1 111 LEU 111 110 110 LEU LEU A . n 
B 1 1   ALA 1   0   0   ALA ALA B . n 
B 1 2   LYS 2   1   1   LYS LYS B . n 
B 1 3   LEU 3   2   2   LEU LEU B . n 
B 1 4   THR 4   3   3   THR THR B . n 
B 1 5   ILE 5   4   4   ILE ILE B . n 
B 1 6   GLU 6   5   5   GLU GLU B . n 
B 1 7   SER 7   6   6   SER SER B . n 
B 1 8   THR 8   7   7   THR THR B . n 
B 1 9   PRO 9   8   8   PRO PRO B . n 
B 1 10  PHE 10  9   9   PHE PHE B . n 
B 1 11  ASN 11  10  10  ASN ASN B . n 
B 1 12  VAL 12  11  11  VAL VAL B . n 
B 1 13  ALA 13  12  12  ALA ALA B . n 
B 1 14  GLU 14  13  13  GLU GLU B . n 
B 1 15  GLY 15  14  14  GLY GLY B . n 
B 1 16  LYS 16  15  15  LYS LYS B . n 
B 1 17  GLU 17  16  16  GLU GLU B . n 
B 1 18  VAL 18  17  17  VAL VAL B . n 
B 1 19  LEU 19  18  18  LEU LEU B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  LEU 21  20  20  LEU LEU B . n 
B 1 22  VAL 22  21  21  VAL VAL B . n 
B 1 23  HIS 23  22  22  HIS HIS B . n 
B 1 24  ASN 24  23  23  ASN ASN B . n 
B 1 25  LEU 25  24  24  LEU LEU B . n 
B 1 26  PRO 26  25  25  PRO PRO B . n 
B 1 27  GLN 27  26  26  GLN GLN B . n 
B 1 28  HIS 28  27  27  HIS HIS B . n 
B 1 29  LEU 29  28  28  LEU LEU B . n 
B 1 30  PHE 30  29  29  PHE PHE B . n 
B 1 31  GLY 31  30  30  GLY GLY B . n 
B 1 32  TYR 32  31  31  TYR TYR B . n 
B 1 33  SER 33  32  32  SER SER B . n 
B 1 34  TRP 34  33  33  TRP TRP B . n 
B 1 35  TYR 35  34  34  TYR TYR B . n 
B 1 36  LYS 36  35  35  LYS LYS B . n 
B 1 37  GLY 37  36  36  GLY GLY B . n 
B 1 38  GLU 38  37  37  GLU GLU B . n 
B 1 39  ARG 39  38  38  ARG ARG B . n 
B 1 40  VAL 40  39  39  VAL VAL B . n 
B 1 41  ASP 41  40  40  ASP ASP B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  ASN 43  42  42  ASN ASN B . n 
B 1 44  ARG 44  43  43  ARG ARG B . n 
B 1 45  GLN 45  44  44  GLN GLN B . n 
B 1 46  ILE 46  45  45  ILE ILE B . n 
B 1 47  ILE 47  46  46  ILE ILE B . n 
B 1 48  GLY 48  47  47  GLY GLY B . n 
B 1 49  TYR 49  48  48  TYR TYR B . n 
B 1 50  VAL 50  49  49  VAL VAL B . n 
B 1 51  ILE 51  50  50  ILE ILE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  THR 53  52  52  THR THR B . n 
B 1 54  GLN 54  53  53  GLN GLN B . n 
B 1 55  GLN 55  54  54  GLN GLN B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  THR 57  56  56  THR THR B . n 
B 1 58  PRO 58  57  57  PRO PRO B . n 
B 1 59  GLY 59  58  58  GLY GLY B . n 
B 1 60  PRO 60  59  59  PRO PRO B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  TYR 62  61  61  TYR TYR B . n 
B 1 63  SER 63  62  62  SER SER B . n 
B 1 64  GLY 64  63  63  GLY GLY B . n 
B 1 65  ARG 65  64  64  ARG ARG B . n 
B 1 66  GLU 66  65  65  GLU GLU B . n 
B 1 67  ILE 67  66  66  ILE ILE B . n 
B 1 68  ILE 68  67  67  ILE ILE B . n 
B 1 69  TYR 69  68  68  TYR TYR B . n 
B 1 70  PRO 70  69  69  PRO PRO B . n 
B 1 71  ASN 71  70  70  ASN ASN B . n 
B 1 72  ALA 72  71  71  ALA ALA B . n 
B 1 73  SER 73  72  72  SER SER B . n 
B 1 74  LEU 74  73  73  LEU LEU B . n 
B 1 75  LEU 75  74  74  LEU LEU B . n 
B 1 76  ILE 76  75  75  ILE ILE B . n 
B 1 77  GLN 77  76  76  GLN GLN B . n 
B 1 78  ASN 78  77  77  ASN ASN B . n 
B 1 79  ILE 79  78  78  ILE ILE B . n 
B 1 80  ILE 80  79  79  ILE ILE B . n 
B 1 81  GLN 81  80  80  GLN GLN B . n 
B 1 82  ASN 82  81  81  ASN ASN B . n 
B 1 83  ASP 83  82  82  ASP ASP B . n 
B 1 84  ALA 84  83  83  ALA ALA B . n 
B 1 85  GLY 85  84  84  GLY GLY B . n 
B 1 86  PHE 86  85  85  PHE PHE B . n 
B 1 87  TYR 87  86  86  TYR TYR B . n 
B 1 88  THR 88  87  87  THR THR B . n 
B 1 89  LEU 89  88  88  LEU LEU B . n 
B 1 90  HIS 90  89  89  HIS HIS B . n 
B 1 91  VAL 91  90  90  VAL VAL B . n 
B 1 92  ILE 92  91  91  ILE ILE B . n 
B 1 93  LYS 93  92  92  LYS LYS B . n 
B 1 94  SER 94  93  93  SER SER B . n 
B 1 95  ASP 95  94  94  ASP ASP B . n 
B 1 96  LEU 96  95  95  LEU LEU B . n 
B 1 97  VAL 97  96  96  VAL VAL B . n 
B 1 98  ASN 98  97  97  ASN ASN B . n 
B 1 99  GLU 99  98  98  GLU GLU B . n 
B 1 100 GLU 100 99  99  GLU GLU B . n 
B 1 101 ALA 101 100 100 ALA ALA B . n 
B 1 102 THR 102 101 101 THR THR B . n 
B 1 103 GLY 103 102 102 GLY GLY B . n 
B 1 104 GLN 104 103 103 GLN GLN B . n 
B 1 105 PHE 105 104 104 PHE PHE B . n 
B 1 106 ARG 106 105 105 ARG ARG B . n 
B 1 107 VAL 107 106 106 VAL VAL B . n 
B 1 108 TYR 108 107 107 TYR TYR B . n 
B 1 109 PRO 109 108 108 PRO PRO B . n 
B 1 110 GLU 110 109 ?   ?   ?   B . n 
B 1 111 LEU 111 110 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CL  1   502 502 CL  CL  A . 
D 3 GOL 1   202 202 GOL GOL A . 
E 3 GOL 1   203 203 GOL GOL A . 
F 3 GOL 1   204 204 GOL GOL A . 
G 3 GOL 1   201 201 GOL GOL B . 
H 2 CL  1   501 501 CL  CL  B . 
I 4 HOH 1   304 304 HOH HOH A . 
I 4 HOH 2   305 305 HOH HOH A . 
I 4 HOH 3   306 306 HOH HOH A . 
I 4 HOH 4   307 307 HOH HOH A . 
I 4 HOH 5   311 311 HOH HOH A . 
I 4 HOH 6   313 313 HOH HOH A . 
I 4 HOH 7   314 314 HOH HOH A . 
I 4 HOH 8   315 315 HOH HOH A . 
I 4 HOH 9   316 316 HOH HOH A . 
I 4 HOH 10  317 317 HOH HOH A . 
I 4 HOH 11  324 324 HOH HOH A . 
I 4 HOH 12  325 325 HOH HOH A . 
I 4 HOH 13  326 326 HOH HOH A . 
I 4 HOH 14  327 327 HOH HOH A . 
I 4 HOH 15  331 331 HOH HOH A . 
I 4 HOH 16  332 332 HOH HOH A . 
I 4 HOH 17  333 333 HOH HOH A . 
I 4 HOH 18  334 334 HOH HOH A . 
I 4 HOH 19  335 335 HOH HOH A . 
I 4 HOH 20  336 336 HOH HOH A . 
I 4 HOH 21  337 337 HOH HOH A . 
I 4 HOH 22  338 338 HOH HOH A . 
I 4 HOH 23  350 350 HOH HOH A . 
I 4 HOH 24  351 351 HOH HOH A . 
I 4 HOH 25  352 352 HOH HOH A . 
I 4 HOH 26  353 353 HOH HOH A . 
I 4 HOH 27  356 356 HOH HOH A . 
I 4 HOH 28  357 357 HOH HOH A . 
I 4 HOH 29  358 358 HOH HOH A . 
I 4 HOH 30  361 361 HOH HOH A . 
I 4 HOH 31  362 362 HOH HOH A . 
I 4 HOH 32  363 363 HOH HOH A . 
I 4 HOH 33  364 364 HOH HOH A . 
I 4 HOH 34  365 365 HOH HOH A . 
I 4 HOH 35  366 366 HOH HOH A . 
I 4 HOH 36  373 373 HOH HOH A . 
I 4 HOH 37  374 374 HOH HOH A . 
I 4 HOH 38  375 375 HOH HOH A . 
I 4 HOH 39  377 377 HOH HOH A . 
I 4 HOH 40  378 378 HOH HOH A . 
I 4 HOH 41  382 382 HOH HOH A . 
I 4 HOH 42  383 383 HOH HOH A . 
I 4 HOH 43  384 384 HOH HOH A . 
I 4 HOH 44  385 385 HOH HOH A . 
I 4 HOH 45  387 387 HOH HOH A . 
I 4 HOH 46  388 388 HOH HOH A . 
I 4 HOH 47  389 389 HOH HOH A . 
I 4 HOH 48  390 390 HOH HOH A . 
I 4 HOH 49  391 391 HOH HOH A . 
I 4 HOH 50  392 392 HOH HOH A . 
I 4 HOH 51  394 394 HOH HOH A . 
I 4 HOH 52  396 396 HOH HOH A . 
I 4 HOH 53  397 397 HOH HOH A . 
I 4 HOH 54  400 400 HOH HOH A . 
I 4 HOH 55  402 402 HOH HOH A . 
I 4 HOH 56  403 403 HOH HOH A . 
I 4 HOH 57  404 404 HOH HOH A . 
I 4 HOH 58  405 405 HOH HOH A . 
I 4 HOH 59  406 406 HOH HOH A . 
I 4 HOH 60  407 407 HOH HOH A . 
I 4 HOH 61  414 414 HOH HOH A . 
I 4 HOH 62  415 415 HOH HOH A . 
I 4 HOH 63  416 416 HOH HOH A . 
I 4 HOH 64  417 417 HOH HOH A . 
I 4 HOH 65  418 418 HOH HOH A . 
I 4 HOH 66  419 419 HOH HOH A . 
I 4 HOH 67  423 423 HOH HOH A . 
I 4 HOH 68  424 424 HOH HOH A . 
I 4 HOH 69  428 428 HOH HOH A . 
I 4 HOH 70  429 429 HOH HOH A . 
I 4 HOH 71  430 430 HOH HOH A . 
I 4 HOH 72  431 431 HOH HOH A . 
I 4 HOH 73  432 432 HOH HOH A . 
I 4 HOH 74  433 433 HOH HOH A . 
I 4 HOH 75  434 434 HOH HOH A . 
I 4 HOH 76  435 435 HOH HOH A . 
I 4 HOH 77  439 439 HOH HOH A . 
I 4 HOH 78  440 440 HOH HOH A . 
I 4 HOH 79  441 441 HOH HOH A . 
I 4 HOH 80  442 442 HOH HOH A . 
I 4 HOH 81  443 443 HOH HOH A . 
I 4 HOH 82  444 444 HOH HOH A . 
I 4 HOH 83  445 445 HOH HOH A . 
I 4 HOH 84  453 453 HOH HOH A . 
I 4 HOH 85  454 454 HOH HOH A . 
I 4 HOH 86  455 455 HOH HOH A . 
I 4 HOH 87  456 456 HOH HOH A . 
I 4 HOH 88  457 457 HOH HOH A . 
I 4 HOH 89  458 458 HOH HOH A . 
I 4 HOH 90  459 459 HOH HOH A . 
I 4 HOH 91  460 460 HOH HOH A . 
I 4 HOH 92  461 461 HOH HOH A . 
I 4 HOH 93  462 462 HOH HOH A . 
I 4 HOH 94  463 463 HOH HOH A . 
I 4 HOH 95  466 466 HOH HOH A . 
I 4 HOH 96  469 469 HOH HOH A . 
I 4 HOH 97  473 473 HOH HOH A . 
I 4 HOH 98  481 481 HOH HOH A . 
I 4 HOH 99  482 482 HOH HOH A . 
I 4 HOH 100 491 491 HOH HOH A . 
I 4 HOH 101 492 492 HOH HOH A . 
I 4 HOH 102 493 493 HOH HOH A . 
J 4 HOH 1   301 301 HOH HOH B . 
J 4 HOH 2   302 302 HOH HOH B . 
J 4 HOH 3   303 303 HOH HOH B . 
J 4 HOH 4   308 308 HOH HOH B . 
J 4 HOH 5   309 309 HOH HOH B . 
J 4 HOH 6   310 310 HOH HOH B . 
J 4 HOH 7   312 312 HOH HOH B . 
J 4 HOH 8   318 318 HOH HOH B . 
J 4 HOH 9   319 319 HOH HOH B . 
J 4 HOH 10  320 320 HOH HOH B . 
J 4 HOH 11  321 321 HOH HOH B . 
J 4 HOH 12  322 322 HOH HOH B . 
J 4 HOH 13  323 323 HOH HOH B . 
J 4 HOH 14  328 328 HOH HOH B . 
J 4 HOH 15  329 329 HOH HOH B . 
J 4 HOH 16  330 330 HOH HOH B . 
J 4 HOH 17  339 339 HOH HOH B . 
J 4 HOH 18  340 340 HOH HOH B . 
J 4 HOH 19  341 341 HOH HOH B . 
J 4 HOH 20  342 342 HOH HOH B . 
J 4 HOH 21  343 343 HOH HOH B . 
J 4 HOH 22  344 344 HOH HOH B . 
J 4 HOH 23  345 345 HOH HOH B . 
J 4 HOH 24  346 346 HOH HOH B . 
J 4 HOH 25  347 347 HOH HOH B . 
J 4 HOH 26  348 348 HOH HOH B . 
J 4 HOH 27  349 349 HOH HOH B . 
J 4 HOH 28  354 354 HOH HOH B . 
J 4 HOH 29  355 355 HOH HOH B . 
J 4 HOH 30  359 359 HOH HOH B . 
J 4 HOH 31  360 360 HOH HOH B . 
J 4 HOH 32  367 367 HOH HOH B . 
J 4 HOH 33  368 368 HOH HOH B . 
J 4 HOH 34  369 369 HOH HOH B . 
J 4 HOH 35  370 370 HOH HOH B . 
J 4 HOH 36  371 371 HOH HOH B . 
J 4 HOH 37  372 372 HOH HOH B . 
J 4 HOH 38  376 376 HOH HOH B . 
J 4 HOH 39  379 379 HOH HOH B . 
J 4 HOH 40  380 380 HOH HOH B . 
J 4 HOH 41  381 381 HOH HOH B . 
J 4 HOH 42  386 386 HOH HOH B . 
J 4 HOH 43  393 393 HOH HOH B . 
J 4 HOH 44  395 395 HOH HOH B . 
J 4 HOH 45  398 398 HOH HOH B . 
J 4 HOH 46  399 399 HOH HOH B . 
J 4 HOH 47  401 401 HOH HOH B . 
J 4 HOH 48  408 408 HOH HOH B . 
J 4 HOH 49  409 409 HOH HOH B . 
J 4 HOH 50  410 410 HOH HOH B . 
J 4 HOH 51  411 411 HOH HOH B . 
J 4 HOH 52  412 412 HOH HOH B . 
J 4 HOH 53  413 413 HOH HOH B . 
J 4 HOH 54  420 420 HOH HOH B . 
J 4 HOH 55  421 421 HOH HOH B . 
J 4 HOH 56  422 422 HOH HOH B . 
J 4 HOH 57  425 425 HOH HOH B . 
J 4 HOH 58  426 426 HOH HOH B . 
J 4 HOH 59  427 427 HOH HOH B . 
J 4 HOH 60  436 436 HOH HOH B . 
J 4 HOH 61  437 437 HOH HOH B . 
J 4 HOH 62  438 438 HOH HOH B . 
J 4 HOH 63  446 446 HOH HOH B . 
J 4 HOH 64  447 447 HOH HOH B . 
J 4 HOH 65  448 448 HOH HOH B . 
J 4 HOH 66  449 449 HOH HOH B . 
J 4 HOH 67  450 450 HOH HOH B . 
J 4 HOH 68  451 451 HOH HOH B . 
J 4 HOH 69  452 452 HOH HOH B . 
J 4 HOH 70  464 464 HOH HOH B . 
J 4 HOH 71  465 465 HOH HOH B . 
J 4 HOH 72  467 467 HOH HOH B . 
J 4 HOH 73  468 468 HOH HOH B . 
J 4 HOH 74  470 470 HOH HOH B . 
J 4 HOH 75  471 471 HOH HOH B . 
J 4 HOH 76  472 472 HOH HOH B . 
J 4 HOH 77  474 474 HOH HOH B . 
J 4 HOH 78  475 475 HOH HOH B . 
J 4 HOH 79  476 476 HOH HOH B . 
J 4 HOH 80  477 477 HOH HOH B . 
J 4 HOH 81  478 478 HOH HOH B . 
J 4 HOH 82  479 479 HOH HOH B . 
J 4 HOH 83  480 480 HOH HOH B . 
J 4 HOH 84  483 483 HOH HOH B . 
J 4 HOH 85  484 484 HOH HOH B . 
J 4 HOH 86  485 485 HOH HOH B . 
J 4 HOH 87  486 486 HOH HOH B . 
J 4 HOH 88  487 487 HOH HOH B . 
J 4 HOH 89  488 488 HOH HOH B . 
J 4 HOH 90  489 489 HOH HOH B . 
J 4 HOH 91  490 490 HOH HOH B . 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .       ?              program 'Murshudov, G.N.' ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html  Fortran_77 ? 1 
PDB_EXTRACT 3.000   'July 2, 2007' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/ C++        ? 2 
ADSC        Quantum ?              ?       ?                 ?                        'data collection' ? ?          ? 3 
DENZO       .       ?              ?       ?                 ?                        'data reduction'  ? ?          ? 4 
SCALEPACK   .       ?              ?       ?                 ?                        'data scaling'    ? ?          ? 5 
HKL-2000    .       ?              ?       ?                 ?                        'data scaling'    ? ?          ? 6 
MOLREP      .       ?              ?       ?                 ?                        phasing           ? ?          ? 7 
# 
_cell.length_a           132.531 
_cell.length_b           132.531 
_cell.length_c           82.762 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.entry_id           2QSQ 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              18 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.entry_id                         2QSQ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                146 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.crystals_number   1 
_exptl.entry_id          2QSQ 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      5.63 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   78.14 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '3.0 M NaCl, 100 mM Tris-HCl pH 7.0, temperature 277K, VAPOR DIFFUSION' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2006-04-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 5.0.1' 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   5.0.1 
# 
_reflns.entry_id                     2QSQ 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            1.95 
_reflns.d_resolution_low             50. 
_reflns.number_all                   38912 
_reflns.number_obs                   38912 
_reflns.percent_possible_obs         97.8 
_reflns.pdbx_Rmerge_I_obs            0.094 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15. 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.4 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.95 
_reflns_shell.d_res_low              2.02 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   83.4 
_reflns_shell.Rmerge_I_obs           0.802 
_reflns_shell.meanI_over_sigI_obs    1. 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        2.5 
_reflns_shell.number_unique_all      3283 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2QSQ 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             10.00 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    97.970 
_refine.ls_number_reflns_obs                     38432 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.181 
_refine.ls_R_factor_R_work                       0.180 
_refine.ls_R_factor_R_free                       0.203 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  1936 
_refine.B_iso_mean                               41.014 
_refine.aniso_B[1][1]                            -0.300 
_refine.aniso_B[2][2]                            -0.300 
_refine.aniso_B[3][3]                            0.460 
_refine.aniso_B[1][2]                            -0.150 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.pdbx_overall_ESU_R                       0.096 
_refine.pdbx_overall_ESU_R_Free                  0.096 
_refine.overall_SU_ML                            0.073 
_refine.overall_SU_B                             2.600 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_number_reflns_all                     38432 
_refine.ls_R_factor_all                          0.181 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1743 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             193 
_refine_hist.number_atoms_total               1962 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        10.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         1888 0.013  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2559 1.340  1.960  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   220  6.215  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   101  36.758 24.752 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   320  14.568 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   11   18.371 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           276  0.102  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1447 0.005  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            786  0.202  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1277 0.309  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    182  0.157  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   76   0.209  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 15   0.257  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1146 0.834  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             1797 1.396  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              863  1.925  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             762  2.902  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.95 
_refine_ls_shell.d_res_low                        1.999 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               82.640 
_refine_ls_shell.number_reflns_R_work             2214 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.288 
_refine_ls_shell.R_factor_R_free                  0.324 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             123 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2337 
_refine_ls_shell.number_reflns_obs                3283 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2QSQ 
_struct.title                     'Crystal structure of the N-terminal domain of carcinoembryonic antigen (CEA)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2QSQ 
_struct_keywords.text            'cell adhesion, Glycoprotein, GPI-anchor, Immunoglobulin domain, Lipoprotein, Membrane' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 2 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CEAM5_HUMAN 
_struct_ref.pdbx_db_accession          P06731 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNII
QNDTGFYTLHVIKSDLVNEEATGQFRVYPEL
;
_struct_ref.pdbx_align_begin           34 
_struct_ref.pdbx_db_isoform            ? 
# 
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 2QSQ A 1 ? 111 ? P06731 34 ? 144 ? 0 110 
2 1 2QSQ B 1 ? 111 ? P06731 34 ? 144 ? 0 110 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2QSQ ALA A 84 ? UNP P06731 THR 117 'SEE REMARK 999' 83 1 
2 2QSQ ALA B 84 ? UNP P06731 THR 117 'SEE REMARK 999' 83 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_prop.biol_id   1 
_pdbx_struct_assembly_prop.type      'ABSA (A^2)' 
_pdbx_struct_assembly_prop.value     2610 
_pdbx_struct_assembly_prop.details   ? 
# 
_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 
# 
_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 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ASP A 41 ? ASN A 43 ? ASP A 40 ASN A 42 5 ? 3 
HELX_P HELX_P2 2 ILE A 80 ? ALA A 84 ? ILE A 79 ALA A 83 5 ? 5 
HELX_P HELX_P3 3 ASP B 41 ? ASN B 43 ? ASP B 40 ASN B 42 5 ? 3 
HELX_P HELX_P4 4 ILE B 80 ? ALA B 84 ? ILE B 79 ALA B 83 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 8 A . ? THR 7 A PRO 9 A ? PRO 8 A 1 -3.36 
2 THR 8 B . ? THR 7 B PRO 9 B ? PRO 8 B 1 -4.85 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 6 ? 
C ? 4 ? 
D ? 6 ? 
# 
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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
B 5 6 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
D 1 2 ? parallel      
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
D 5 6 ? 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 
A 1 THR A 4  ? THR A 8   ? THR A 3  THR A 7   
A 2 VAL A 18 ? HIS A 23  ? VAL A 17 HIS A 22  
A 3 LEU A 74 ? ILE A 76  ? LEU A 73 ILE A 75  
A 4 GLU A 66 ? ILE A 68  ? GLU A 65 ILE A 67  
B 1 ASN A 11 ? ALA A 13  ? ASN A 10 ALA A 12  
B 2 GLU A 99 ? TYR A 108 ? GLU A 98 TYR A 107 
B 3 GLY A 85 ? LYS A 93  ? GLY A 84 LYS A 92  
B 4 LEU A 29 ? LYS A 36  ? LEU A 28 LYS A 35  
B 5 GLN A 45 ? VAL A 50  ? GLN A 44 VAL A 49  
B 6 GLN A 55 ? PRO A 58  ? GLN A 54 PRO A 57  
C 1 THR B 4  ? THR B 8   ? THR B 3  THR B 7   
C 2 VAL B 18 ? HIS B 23  ? VAL B 17 HIS B 22  
C 3 LEU B 74 ? ILE B 76  ? LEU B 73 ILE B 75  
C 4 GLU B 66 ? ILE B 68  ? GLU B 65 ILE B 67  
D 1 ASN B 11 ? ALA B 13  ? ASN B 10 ALA B 12  
D 2 GLU B 99 ? TYR B 108 ? GLU B 98 TYR B 107 
D 3 GLY B 85 ? LYS B 93  ? GLY B 84 LYS B 92  
D 4 LEU B 29 ? LYS B 36  ? LEU B 28 LYS B 35  
D 5 GLN B 45 ? VAL B 50  ? GLN B 44 VAL B 49  
D 6 THR B 57 ? PRO B 58  ? THR B 56 PRO B 57  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N THR A 4  ? N THR A 3  O HIS A 23  ? O HIS A 22  
A 2 3 N LEU A 20 ? N LEU A 19 O LEU A 74  ? O LEU A 73  
A 3 4 O LEU A 75 ? O LEU A 74 N ILE A 67  ? N ILE A 66  
B 1 2 N VAL A 12 ? N VAL A 11 O ARG A 106 ? O ARG A 105 
B 2 3 O GLU A 99 ? O GLU A 98 N VAL A 91  ? N VAL A 90  
B 3 4 O ILE A 92 ? O ILE A 91 N PHE A 30  ? N PHE A 29  
B 4 5 N TYR A 32 ? N TYR A 31 O TYR A 49  ? O TYR A 48  
B 5 6 N GLY A 48 ? N GLY A 47 O THR A 57  ? O THR A 56  
C 1 2 N THR B 4  ? N THR B 3  O HIS B 23  ? O HIS B 22  
C 2 3 N LEU B 20 ? N LEU B 19 O LEU B 74  ? O LEU B 73  
C 3 4 O LEU B 75 ? O LEU B 74 N ILE B 67  ? N ILE B 66  
D 1 2 N VAL B 12 ? N VAL B 11 O ARG B 106 ? O ARG B 105 
D 2 3 O GLU B 99 ? O GLU B 98 N VAL B 91  ? N VAL B 90  
D 3 4 O ILE B 92 ? O ILE B 91 N PHE B 30  ? N PHE B 29  
D 4 5 N TRP B 34 ? N TRP B 33 O ILE B 46  ? O ILE B 45  
D 5 6 N GLY B 48 ? N GLY B 47 O THR B 57  ? O THR B 56  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software B GOL 201 ? 6 'BINDING SITE FOR RESIDUE GOL B 201' 
AC2 Software A CL  502 ? 3 'BINDING SITE FOR RESIDUE CL A 502'  
AC3 Software A GOL 202 ? 7 'BINDING SITE FOR RESIDUE GOL A 202' 
AC4 Software B CL  501 ? 2 'BINDING SITE FOR RESIDUE CL B 501'  
AC5 Software A GOL 203 ? 5 'BINDING SITE FOR RESIDUE GOL A 203' 
AC6 Software A GOL 204 ? 8 'BINDING SITE FOR RESIDUE GOL A 204' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 6 SER A 94 ? SER A 93  . ? 1_555 ? 
2  AC1 6 TYR B 49 ? TYR B 48  . ? 1_555 ? 
3  AC1 6 VAL B 50 ? VAL B 49  . ? 1_555 ? 
4  AC1 6 THR B 53 ? THR B 52  . ? 1_555 ? 
5  AC1 6 GLN B 55 ? GLN B 54  . ? 1_555 ? 
6  AC1 6 THR B 57 ? THR B 56  . ? 1_555 ? 
7  AC2 3 LYS A 36 ? LYS A 35  . ? 1_555 ? 
8  AC2 3 PHE A 86 ? PHE A 85  . ? 1_555 ? 
9  AC2 3 HOH I .  ? HOH A 443 . ? 1_555 ? 
10 AC3 7 VAL A 22 ? VAL A 21  . ? 1_555 ? 
11 AC3 7 HIS A 23 ? HIS A 22  . ? 1_555 ? 
12 AC3 7 ASN A 24 ? ASN A 23  . ? 1_555 ? 
13 AC3 7 HOH I .  ? HOH A 382 . ? 1_555 ? 
14 AC3 7 GLN B 77 ? GLN B 76  . ? 9_554 ? 
15 AC3 7 ASN B 78 ? ASN B 77  . ? 9_554 ? 
16 AC3 7 HOH J .  ? HOH B 480 . ? 9_554 ? 
17 AC4 2 LYS B 36 ? LYS B 35  . ? 1_555 ? 
18 AC4 2 PHE B 86 ? PHE B 85  . ? 1_555 ? 
19 AC5 5 GLU A 17 ? GLU A 16  . ? 1_555 ? 
20 AC5 5 HOH I .  ? HOH A 311 . ? 1_555 ? 
21 AC5 5 TYR B 69 ? TYR B 68  . ? 9_554 ? 
22 AC5 5 ASN B 71 ? ASN B 70  . ? 9_554 ? 
23 AC5 5 SER B 73 ? SER B 72  . ? 9_554 ? 
24 AC6 8 TYR A 62 ? TYR A 61  . ? 1_555 ? 
25 AC6 8 GLY A 64 ? GLY A 63  . ? 1_555 ? 
26 AC6 8 ARG A 65 ? ARG A 64  . ? 1_555 ? 
27 AC6 8 GLU A 66 ? GLU A 65  . ? 1_555 ? 
28 AC6 8 GLN A 77 ? GLN A 76  . ? 1_555 ? 
29 AC6 8 TYR B 49 ? TYR B 48  . ? 9_554 ? 
30 AC6 8 GLY B 52 ? GLY B 51  . ? 9_554 ? 
31 AC6 8 THR B 53 ? THR B 52  . ? 9_554 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    38 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    422 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.08 
# 
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 ALA A 71 ? ? 84.23 -7.34 
2 1 LEU A 95 ? ? 59.60 18.84 
3 1 HIS B 27 ? ? 67.65 73.83 
4 1 ALA B 71 ? ? 82.48 -7.98 
# 
_pdbx_database_remark.id     999 
_pdbx_database_remark.text   
;Sequence 
 
The sequence was obtained from human cDNA  
and the authors confirmed that ALA is the 
correct sequence. However, the authors do 
not know if it is a mutation introduced by  
PCR or whether it is an SNP that results in 
the different amino acid. 
;
# 
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 B GLU 109 ? B GLU 110 
2 1 Y 1 B LEU 110 ? B LEU 111 
# 
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  
CL  CL   CL N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
GOL C1   C  N N 124 
GOL O1   O  N N 125 
GOL C2   C  N N 126 
GOL O2   O  N N 127 
GOL C3   C  N N 128 
GOL O3   O  N N 129 
GOL H11  H  N N 130 
GOL H12  H  N N 131 
GOL HO1  H  N N 132 
GOL H2   H  N N 133 
GOL HO2  H  N N 134 
GOL H31  H  N N 135 
GOL H32  H  N N 136 
GOL HO3  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  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 
# 
_atom_sites.entry_id                    2QSQ 
_atom_sites.fract_transf_matrix[1][1]   0.007545 
_atom_sites.fract_transf_matrix[1][2]   0.004356 
_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]   0.008713 
_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]   0.012083 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
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   . ALA A 1 1   ? 11.451 19.821 15.475  1.00 54.27  ? 0   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 11.957 21.217 15.693  1.00 53.41  ? 0   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 13.400 21.379 15.214  1.00 52.45  ? 0   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 13.902 22.503 15.063  1.00 52.97  ? 0   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 11.853 21.585 17.171  1.00 54.18  ? 0   ALA A CB  1 
ATOM   6    N  N   . LYS A 1 2   ? 14.058 20.245 14.997  1.00 50.26  ? 1   LYS A N   1 
ATOM   7    C  CA  . LYS A 1 2   ? 15.476 20.196 14.682  1.00 48.39  ? 1   LYS A CA  1 
ATOM   8    C  C   . LYS A 1 2   ? 15.664 20.152 13.160  1.00 45.72  ? 1   LYS A C   1 
ATOM   9    O  O   . LYS A 1 2   ? 14.842 19.563 12.452  1.00 45.02  ? 1   LYS A O   1 
ATOM   10   C  CB  . LYS A 1 2   ? 16.069 18.982 15.410  1.00 48.86  ? 1   LYS A CB  1 
ATOM   11   C  CG  . LYS A 1 2   ? 17.292 18.320 14.825  1.00 49.76  ? 1   LYS A CG  1 
ATOM   12   C  CD  . LYS A 1 2   ? 17.732 17.122 15.695  1.00 50.21  ? 1   LYS A CD  1 
ATOM   13   C  CE  . LYS A 1 2   ? 18.379 17.568 17.008  0.10 49.87  ? 1   LYS A CE  1 
ATOM   14   N  NZ  . LYS A 1 2   ? 18.681 16.423 17.914  0.10 49.59  ? 1   LYS A NZ  1 
ATOM   15   N  N   . LEU A 1 3   ? 16.712 20.815 12.664  1.00 42.73  ? 2   LEU A N   1 
ATOM   16   C  CA  . LEU A 1 3   ? 17.024 20.827 11.230  1.00 40.21  ? 2   LEU A CA  1 
ATOM   17   C  C   . LEU A 1 3   ? 17.133 19.381 10.735  1.00 39.15  ? 2   LEU A C   1 
ATOM   18   O  O   . LEU A 1 3   ? 17.868 18.581 11.329  1.00 38.35  ? 2   LEU A O   1 
ATOM   19   C  CB  . LEU A 1 3   ? 18.346 21.575 10.965  1.00 39.62  ? 2   LEU A CB  1 
ATOM   20   C  CG  . LEU A 1 3   ? 18.789 21.709 9.506   1.00 38.75  ? 2   LEU A CG  1 
ATOM   21   C  CD1 . LEU A 1 3   ? 17.961 22.751 8.787   1.00 35.85  ? 2   LEU A CD1 1 
ATOM   22   C  CD2 . LEU A 1 3   ? 20.249 22.071 9.423   1.00 38.11  ? 2   LEU A CD2 1 
ATOM   23   N  N   . THR A 1 4   ? 16.399 19.050 9.672   1.00 38.71  ? 3   THR A N   1 
ATOM   24   C  CA  . THR A 1 4   ? 16.419 17.677 9.106   1.00 38.36  ? 3   THR A CA  1 
ATOM   25   C  C   . THR A 1 4   ? 16.395 17.671 7.583   1.00 38.32  ? 3   THR A C   1 
ATOM   26   O  O   . THR A 1 4   ? 15.815 18.566 6.961   1.00 38.26  ? 3   THR A O   1 
ATOM   27   C  CB  . THR A 1 4   ? 15.183 16.825 9.564   1.00 38.92  ? 3   THR A CB  1 
ATOM   28   O  OG1 A THR A 1 4   ? 13.957 17.474 9.211   0.50 36.80  ? 3   THR A OG1 1 
ATOM   29   O  OG1 B THR A 1 4   ? 14.780 17.245 10.878  0.50 39.65  ? 3   THR A OG1 1 
ATOM   30   C  CG2 A THR A 1 4   ? 15.252 16.512 11.068  0.50 38.96  ? 3   THR A CG2 1 
ATOM   31   C  CG2 B THR A 1 4   ? 15.449 15.337 9.531   0.50 37.78  ? 3   THR A CG2 1 
ATOM   32   N  N   . ILE A 1 5   ? 16.989 16.624 7.007   1.00 37.71  ? 4   ILE A N   1 
ATOM   33   C  CA  . ILE A 1 5   ? 17.015 16.409 5.571   1.00 37.97  ? 4   ILE A CA  1 
ATOM   34   C  C   . ILE A 1 5   ? 16.185 15.166 5.214   1.00 39.45  ? 4   ILE A C   1 
ATOM   35   O  O   . ILE A 1 5   ? 16.404 14.080 5.780   1.00 39.70  ? 4   ILE A O   1 
ATOM   36   C  CB  . ILE A 1 5   ? 18.466 16.176 5.070   1.00 37.63  ? 4   ILE A CB  1 
ATOM   37   C  CG1 . ILE A 1 5   ? 19.432 17.305 5.535   1.00 37.00  ? 4   ILE A CG1 1 
ATOM   38   C  CG2 . ILE A 1 5   ? 18.480 15.901 3.540   1.00 36.64  ? 4   ILE A CG2 1 
ATOM   39   C  CD1 A ILE A 1 5   ? 18.956 18.702 5.361   0.50 35.63  ? 4   ILE A CD1 1 
ATOM   40   C  CD1 B ILE A 1 5   ? 20.851 17.183 5.065   0.50 37.17  ? 4   ILE A CD1 1 
ATOM   41   N  N   . GLU A 1 6   ? 15.253 15.300 4.276   1.00 39.78  ? 5   GLU A N   1 
ATOM   42   C  CA  . GLU A 1 6   ? 14.617 14.092 3.747   1.00 40.96  ? 5   GLU A CA  1 
ATOM   43   C  C   . GLU A 1 6   ? 14.696 13.954 2.218   1.00 40.13  ? 5   GLU A C   1 
ATOM   44   O  O   . GLU A 1 6   ? 14.213 14.815 1.461   1.00 39.21  ? 5   GLU A O   1 
ATOM   45   C  CB  . GLU A 1 6   ? 13.201 13.895 4.280   1.00 41.76  ? 5   GLU A CB  1 
ATOM   46   C  CG  . GLU A 1 6   ? 12.185 14.861 3.781   1.00 47.24  ? 5   GLU A CG  1 
ATOM   47   C  CD  . GLU A 1 6   ? 10.767 14.281 3.708   1.00 51.36  ? 5   GLU A CD  1 
ATOM   48   O  OE1 . GLU A 1 6   ? 10.609 13.083 3.377   1.00 54.43  ? 5   GLU A OE1 1 
ATOM   49   O  OE2 . GLU A 1 6   ? 9.809  15.046 3.934   1.00 51.62  ? 5   GLU A OE2 1 
ATOM   50   N  N   . SER A 1 7   ? 15.340 12.877 1.774   1.00 39.85  ? 6   SER A N   1 
ATOM   51   C  CA  . SER A 1 7   ? 15.471 12.629 0.339   1.00 40.15  ? 6   SER A CA  1 
ATOM   52   C  C   . SER A 1 7   ? 14.148 12.180 -0.233  1.00 40.58  ? 6   SER A C   1 
ATOM   53   O  O   . SER A 1 7   ? 13.372 11.440 0.421   1.00 40.20  ? 6   SER A O   1 
ATOM   54   C  CB  . SER A 1 7   ? 16.570 11.628 0.038   1.00 40.46  ? 6   SER A CB  1 
ATOM   55   O  OG  . SER A 1 7   ? 16.359 10.422 0.757   1.00 41.97  ? 6   SER A OG  1 
ATOM   56   N  N   . THR A 1 8   ? 13.866 12.664 -1.436  1.00 40.40  ? 7   THR A N   1 
ATOM   57   C  CA  . THR A 1 8   ? 12.701 12.211 -2.189  1.00 41.14  ? 7   THR A CA  1 
ATOM   58   C  C   . THR A 1 8   ? 13.006 12.112 -3.691  1.00 41.14  ? 7   THR A C   1 
ATOM   59   O  O   . THR A 1 8   ? 13.386 13.099 -4.323  1.00 40.15  ? 7   THR A O   1 
ATOM   60   C  CB  . THR A 1 8   ? 11.443 13.046 -1.899  1.00 42.34  ? 7   THR A CB  1 
ATOM   61   O  OG1 . THR A 1 8   ? 10.316 12.482 -2.597  1.00 44.82  ? 7   THR A OG1 1 
ATOM   62   C  CG2 . THR A 1 8   ? 11.617 14.512 -2.306  1.00 41.94  ? 7   THR A CG2 1 
ATOM   63   N  N   . PRO A 1 9   ? 12.880 10.897 -4.261  1.00 41.40  ? 8   PRO A N   1 
ATOM   64   C  CA  . PRO A 1 9   ? 12.544 9.675  -3.526  1.00 41.23  ? 8   PRO A CA  1 
ATOM   65   C  C   . PRO A 1 9   ? 13.803 9.177  -2.804  1.00 41.14  ? 8   PRO A C   1 
ATOM   66   O  O   . PRO A 1 9   ? 14.908 9.631  -3.118  1.00 40.98  ? 8   PRO A O   1 
ATOM   67   C  CB  . PRO A 1 9   ? 12.124 8.718  -4.648  1.00 41.30  ? 8   PRO A CB  1 
ATOM   68   C  CG  . PRO A 1 9   ? 13.012 9.108  -5.794  1.00 41.89  ? 8   PRO A CG  1 
ATOM   69   C  CD  . PRO A 1 9   ? 13.083 10.636 -5.701  1.00 41.11  ? 8   PRO A CD  1 
ATOM   70   N  N   . PHE A 1 10  ? 13.649 8.263  -1.848  1.00 40.98  ? 9   PHE A N   1 
ATOM   71   C  CA  . PHE A 1 10  ? 14.798 7.733  -1.108  1.00 40.92  ? 9   PHE A CA  1 
ATOM   72   C  C   . PHE A 1 10  ? 15.644 6.781  -1.960  1.00 40.85  ? 9   PHE A C   1 
ATOM   73   O  O   . PHE A 1 10  ? 16.878 6.709  -1.808  1.00 39.67  ? 9   PHE A O   1 
ATOM   74   C  CB  . PHE A 1 10  ? 14.323 7.034  0.182   1.00 42.04  ? 9   PHE A CB  1 
ATOM   75   C  CG  . PHE A 1 10  ? 15.450 6.507  1.025   1.00 43.80  ? 9   PHE A CG  1 
ATOM   76   C  CD1 . PHE A 1 10  ? 16.107 7.329  1.927   1.00 44.23  ? 9   PHE A CD1 1 
ATOM   77   C  CD2 . PHE A 1 10  ? 15.862 5.187  0.908   1.00 46.90  ? 9   PHE A CD2 1 
ATOM   78   C  CE1 . PHE A 1 10  ? 17.170 6.849  2.693   1.00 44.96  ? 9   PHE A CE1 1 
ATOM   79   C  CE2 . PHE A 1 10  ? 16.924 4.704  1.674   1.00 47.72  ? 9   PHE A CE2 1 
ATOM   80   C  CZ  . PHE A 1 10  ? 17.579 5.538  2.561   1.00 46.13  ? 9   PHE A CZ  1 
ATOM   81   N  N   . ASN A 1 11  ? 14.972 6.028  -2.840  1.00 40.81  ? 10  ASN A N   1 
ATOM   82   C  CA  . ASN A 1 11  ? 15.662 5.164  -3.814  1.00 41.78  ? 10  ASN A CA  1 
ATOM   83   C  C   . ASN A 1 11  ? 15.482 5.760  -5.195  1.00 41.20  ? 10  ASN A C   1 
ATOM   84   O  O   . ASN A 1 11  ? 14.353 5.972  -5.624  1.00 40.99  ? 10  ASN A O   1 
ATOM   85   C  CB  . ASN A 1 11  ? 15.103 3.722  -3.798  1.00 42.57  ? 10  ASN A CB  1 
ATOM   86   C  CG  . ASN A 1 11  ? 15.297 3.026  -2.456  1.00 44.47  ? 10  ASN A CG  1 
ATOM   87   O  OD1 . ASN A 1 11  ? 14.334 2.831  -1.707  1.00 48.92  ? 10  ASN A OD1 1 
ATOM   88   N  ND2 . ASN A 1 11  ? 16.535 2.654  -2.145  1.00 45.20  ? 10  ASN A ND2 1 
ATOM   89   N  N   . VAL A 1 12  ? 16.591 6.051  -5.864  1.00 41.18  ? 11  VAL A N   1 
ATOM   90   C  CA  . VAL A 1 12  ? 16.572 6.855  -7.089  1.00 41.63  ? 11  VAL A CA  1 
ATOM   91   C  C   . VAL A 1 12  ? 17.067 6.075  -8.299  1.00 42.04  ? 11  VAL A C   1 
ATOM   92   O  O   . VAL A 1 12  ? 18.140 5.490  -8.249  1.00 41.89  ? 11  VAL A O   1 
ATOM   93   C  CB  . VAL A 1 12  ? 17.517 8.100  -6.991  1.00 41.24  ? 11  VAL A CB  1 
ATOM   94   C  CG1 . VAL A 1 12  ? 17.219 9.055  -8.139  1.00 39.93  ? 11  VAL A CG1 1 
ATOM   95   C  CG2 . VAL A 1 12  ? 17.365 8.812  -5.644  1.00 41.98  ? 11  VAL A CG2 1 
ATOM   96   N  N   . ALA A 1 13  ? 16.326 6.139  -9.401  1.00 43.56  ? 12  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 13  ? 16.776 5.502  -10.653 1.00 44.98  ? 12  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 13  ? 17.952 6.246  -11.283 1.00 46.40  ? 12  ALA A C   1 
ATOM   99   O  O   . ALA A 1 13  ? 17.955 7.488  -11.324 1.00 46.89  ? 12  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 13  ? 15.615 5.409  -11.636 1.00 44.93  ? 12  ALA A CB  1 
ATOM   101  N  N   . GLU A 1 14  ? 18.959 5.512  -11.764 1.00 47.15  ? 13  GLU A N   1 
ATOM   102  C  CA  . GLU A 1 14  ? 20.030 6.120  -12.555 1.00 48.71  ? 13  GLU A CA  1 
ATOM   103  C  C   . GLU A 1 14  ? 19.453 6.962  -13.693 1.00 47.92  ? 13  GLU A C   1 
ATOM   104  O  O   . GLU A 1 14  ? 18.475 6.566  -14.342 1.00 48.00  ? 13  GLU A O   1 
ATOM   105  C  CB  . GLU A 1 14  ? 20.995 5.072  -13.116 1.00 48.68  ? 13  GLU A CB  1 
ATOM   106  C  CG  . GLU A 1 14  ? 22.123 4.713  -12.156 1.00 51.25  ? 13  GLU A CG  1 
ATOM   107  C  CD  . GLU A 1 14  ? 23.254 3.909  -12.809 1.00 52.46  ? 13  GLU A CD  1 
ATOM   108  O  OE1 . GLU A 1 14  ? 24.460 4.258  -12.589 1.00 57.64  ? 13  GLU A OE1 1 
ATOM   109  O  OE2 . GLU A 1 14  ? 22.936 2.948  -13.546 1.00 54.66  ? 13  GLU A OE2 1 
ATOM   110  N  N   . GLY A 1 15  ? 20.039 8.139  -13.910 1.00 47.33  ? 14  GLY A N   1 
ATOM   111  C  CA  . GLY A 1 15  ? 19.568 9.045  -14.947 1.00 45.52  ? 14  GLY A CA  1 
ATOM   112  C  C   . GLY A 1 15  ? 18.439 9.950  -14.482 1.00 45.11  ? 14  GLY A C   1 
ATOM   113  O  O   . GLY A 1 15  ? 18.107 10.926 -15.164 1.00 45.11  ? 14  GLY A O   1 
ATOM   114  N  N   . LYS A 1 16  ? 17.840 9.652  -13.331 1.00 43.64  ? 15  LYS A N   1 
ATOM   115  C  CA  . LYS A 1 16  ? 16.757 10.496 -12.815 1.00 42.75  ? 15  LYS A CA  1 
ATOM   116  C  C   . LYS A 1 16  ? 17.277 11.556 -11.794 1.00 40.96  ? 15  LYS A C   1 
ATOM   117  O  O   . LYS A 1 16  ? 18.460 11.829 -11.773 1.00 40.28  ? 15  LYS A O   1 
ATOM   118  C  CB  . LYS A 1 16  ? 15.619 9.644  -12.261 1.00 43.66  ? 15  LYS A CB  1 
ATOM   119  C  CG  . LYS A 1 16  ? 14.953 8.717  -13.306 1.00 46.23  ? 15  LYS A CG  1 
ATOM   120  C  CD  . LYS A 1 16  ? 14.107 9.501  -14.316 1.00 51.12  ? 15  LYS A CD  1 
ATOM   121  C  CE  . LYS A 1 16  ? 13.669 8.616  -15.505 1.00 53.12  ? 15  LYS A CE  1 
ATOM   122  N  NZ  . LYS A 1 16  ? 12.621 7.579  -15.129 1.00 57.59  ? 15  LYS A NZ  1 
ATOM   123  N  N   . GLU A 1 17  ? 16.390 12.136 -10.985 1.00 39.50  ? 16  GLU A N   1 
ATOM   124  C  CA  . GLU A 1 17  ? 16.736 13.240 -10.051 1.00 39.27  ? 16  GLU A CA  1 
ATOM   125  C  C   . GLU A 1 17  ? 16.364 12.876 -8.604  1.00 38.69  ? 16  GLU A C   1 
ATOM   126  O  O   . GLU A 1 17  ? 15.388 12.147 -8.371  1.00 38.52  ? 16  GLU A O   1 
ATOM   127  C  CB  . GLU A 1 17  ? 15.981 14.531 -10.421 1.00 39.14  ? 16  GLU A CB  1 
ATOM   128  C  CG  A GLU A 1 17  ? 14.529 14.501 -10.054 0.50 40.80  ? 16  GLU A CG  1 
ATOM   129  C  CG  B GLU A 1 17  ? 15.669 14.759 -11.917 0.30 40.00  ? 16  GLU A CG  1 
ATOM   130  C  CG  C GLU A 1 17  ? 16.253 14.998 -11.853 0.20 39.29  ? 16  GLU A CG  1 
ATOM   131  C  CD  A GLU A 1 17  ? 13.692 15.451 -10.858 0.50 44.33  ? 16  GLU A CD  1 
ATOM   132  C  CD  B GLU A 1 17  ? 14.427 14.012 -12.416 0.30 40.95  ? 16  GLU A CD  1 
ATOM   133  C  CD  C GLU A 1 17  ? 15.486 16.244 -12.265 0.20 39.08  ? 16  GLU A CD  1 
ATOM   134  O  OE1 A GLU A 1 17  ? 14.248 16.269 -11.627 0.50 45.42  ? 16  GLU A OE1 1 
ATOM   135  O  OE1 B GLU A 1 17  ? 13.498 13.759 -11.612 0.30 41.52  ? 16  GLU A OE1 1 
ATOM   136  O  OE1 C GLU A 1 17  ? 14.505 16.614 -11.588 0.20 39.49  ? 16  GLU A OE1 1 
ATOM   137  O  OE2 A GLU A 1 17  ? 12.458 15.366 -10.723 0.50 46.39  ? 16  GLU A OE2 1 
ATOM   138  O  OE2 B GLU A 1 17  ? 14.381 13.679 -13.624 0.30 41.35  ? 16  GLU A OE2 1 
ATOM   139  O  OE2 C GLU A 1 17  ? 15.867 16.851 -13.289 0.20 38.47  ? 16  GLU A OE2 1 
ATOM   140  N  N   . VAL A 1 18  ? 17.106 13.408 -7.630  1.00 36.98  ? 17  VAL A N   1 
ATOM   141  C  CA  . VAL A 1 18  ? 16.679 13.301 -6.235  1.00 36.06  ? 17  VAL A CA  1 
ATOM   142  C  C   . VAL A 1 18  ? 16.610 14.730 -5.665  1.00 35.85  ? 17  VAL A C   1 
ATOM   143  O  O   . VAL A 1 18  ? 17.438 15.579 -6.024  1.00 35.35  ? 17  VAL A O   1 
ATOM   144  C  CB  . VAL A 1 18  ? 17.673 12.440 -5.399  1.00 36.08  ? 17  VAL A CB  1 
ATOM   145  C  CG1 . VAL A 1 18  ? 19.059 13.095 -5.348  1.00 36.05  ? 17  VAL A CG1 1 
ATOM   146  C  CG2 . VAL A 1 18  ? 17.159 12.172 -3.969  1.00 34.73  ? 17  VAL A CG2 1 
ATOM   147  N  N   . LEU A 1 19  ? 15.627 14.972 -4.799  1.00 34.09  ? 18  LEU A N   1 
ATOM   148  C  CA  . LEU A 1 19  ? 15.527 16.206 -4.035  1.00 33.64  ? 18  LEU A CA  1 
ATOM   149  C  C   . LEU A 1 19  ? 15.839 15.939 -2.560  1.00 34.14  ? 18  LEU A C   1 
ATOM   150  O  O   . LEU A 1 19  ? 15.129 15.135 -1.917  1.00 34.60  ? 18  LEU A O   1 
ATOM   151  C  CB  . LEU A 1 19  ? 14.123 16.779 -4.172  1.00 32.92  ? 18  LEU A CB  1 
ATOM   152  C  CG  . LEU A 1 19  ? 13.817 18.108 -3.477  1.00 34.07  ? 18  LEU A CG  1 
ATOM   153  C  CD1 . LEU A 1 19  ? 14.763 19.222 -3.999  1.00 32.83  ? 18  LEU A CD1 1 
ATOM   154  C  CD2 . LEU A 1 19  ? 12.396 18.482 -3.733  1.00 32.78  ? 18  LEU A CD2 1 
ATOM   155  N  N   . LEU A 1 20  ? 16.888 16.586 -2.032  1.00 33.46  ? 19  LEU A N   1 
ATOM   156  C  CA  . LEU A 1 20  ? 17.144 16.602 -0.595  1.00 34.12  ? 19  LEU A CA  1 
ATOM   157  C  C   . LEU A 1 20  ? 16.347 17.757 0.003   1.00 34.83  ? 19  LEU A C   1 
ATOM   158  O  O   . LEU A 1 20  ? 16.783 18.910 -0.055  1.00 33.96  ? 19  LEU A O   1 
ATOM   159  C  CB  . LEU A 1 20  ? 18.639 16.734 -0.304  1.00 34.13  ? 19  LEU A CB  1 
ATOM   160  C  CG  . LEU A 1 20  ? 19.499 15.680 -1.035  1.00 34.89  ? 19  LEU A CG  1 
ATOM   161  C  CD1 . LEU A 1 20  ? 20.992 15.983 -0.994  1.00 33.39  ? 19  LEU A CD1 1 
ATOM   162  C  CD2 . LEU A 1 20  ? 19.243 14.303 -0.429  1.00 36.87  ? 19  LEU A CD2 1 
ATOM   163  N  N   . LEU A 1 21  ? 15.151 17.439 0.517   1.00 34.63  ? 20  LEU A N   1 
ATOM   164  C  CA  . LEU A 1 21  ? 14.261 18.423 1.128   1.00 35.07  ? 20  LEU A CA  1 
ATOM   165  C  C   . LEU A 1 21  ? 14.780 18.803 2.497   1.00 34.59  ? 20  LEU A C   1 
ATOM   166  O  O   . LEU A 1 21  ? 15.158 17.933 3.269   1.00 35.13  ? 20  LEU A O   1 
ATOM   167  C  CB  . LEU A 1 21  ? 12.866 17.825 1.326   1.00 35.32  ? 20  LEU A CB  1 
ATOM   168  C  CG  . LEU A 1 21  ? 11.824 17.889 0.218   1.00 38.66  ? 20  LEU A CG  1 
ATOM   169  C  CD1 . LEU A 1 21  ? 10.572 17.106 0.663   1.00 39.60  ? 20  LEU A CD1 1 
ATOM   170  C  CD2 . LEU A 1 21  ? 11.460 19.334 -0.109  1.00 38.57  ? 20  LEU A CD2 1 
ATOM   171  N  N   . VAL A 1 22  ? 14.767 20.093 2.811   1.00 34.09  ? 21  VAL A N   1 
ATOM   172  C  CA  . VAL A 1 22  ? 15.241 20.581 4.099   1.00 33.12  ? 21  VAL A CA  1 
ATOM   173  C  C   . VAL A 1 22  ? 14.053 21.094 4.956   1.00 33.74  ? 21  VAL A C   1 
ATOM   174  O  O   . VAL A 1 22  ? 13.236 21.904 4.487   1.00 33.11  ? 21  VAL A O   1 
ATOM   175  C  CB  . VAL A 1 22  ? 16.332 21.679 3.891   1.00 33.12  ? 21  VAL A CB  1 
ATOM   176  C  CG1 . VAL A 1 22  ? 16.695 22.332 5.211   1.00 33.17  ? 21  VAL A CG1 1 
ATOM   177  C  CG2 . VAL A 1 22  ? 17.567 21.055 3.227   1.00 30.53  ? 21  VAL A CG2 1 
ATOM   178  N  N   . HIS A 1 23  ? 13.941 20.593 6.192   1.00 34.45  ? 22  HIS A N   1 
ATOM   179  C  CA  . HIS A 1 23  ? 12.840 20.967 7.084   1.00 35.39  ? 22  HIS A CA  1 
ATOM   180  C  C   . HIS A 1 23  ? 13.413 21.668 8.316   1.00 35.95  ? 22  HIS A C   1 
ATOM   181  O  O   . HIS A 1 23  ? 14.545 21.388 8.703   1.00 36.62  ? 22  HIS A O   1 
ATOM   182  C  CB  . HIS A 1 23  ? 12.058 19.718 7.541   1.00 36.56  ? 22  HIS A CB  1 
ATOM   183  C  CG  . HIS A 1 23  ? 11.494 18.908 6.412   1.00 36.62  ? 22  HIS A CG  1 
ATOM   184  N  ND1 . HIS A 1 23  ? 10.476 19.366 5.606   1.00 38.35  ? 22  HIS A ND1 1 
ATOM   185  C  CD2 . HIS A 1 23  ? 11.810 17.673 5.956   1.00 37.78  ? 22  HIS A CD2 1 
ATOM   186  C  CE1 . HIS A 1 23  ? 10.200 18.456 4.687   1.00 38.67  ? 22  HIS A CE1 1 
ATOM   187  N  NE2 . HIS A 1 23  ? 10.994 17.417 4.882   1.00 36.38  ? 22  HIS A NE2 1 
ATOM   188  N  N   . ASN A 1 24  ? 12.623 22.549 8.931   1.00 36.78  ? 23  ASN A N   1 
ATOM   189  C  CA  . ASN A 1 24  ? 12.986 23.228 10.182  1.00 37.01  ? 23  ASN A CA  1 
ATOM   190  C  C   . ASN A 1 24  ? 14.232 24.106 10.064  1.00 37.08  ? 23  ASN A C   1 
ATOM   191  O  O   . ASN A 1 24  ? 15.128 24.052 10.904  1.00 36.81  ? 23  ASN A O   1 
ATOM   192  C  CB  . ASN A 1 24  ? 13.129 22.209 11.329  1.00 37.41  ? 23  ASN A CB  1 
ATOM   193  C  CG  . ASN A 1 24  ? 11.928 21.273 11.429  1.00 39.44  ? 23  ASN A CG  1 
ATOM   194  O  OD1 . ASN A 1 24  ? 12.082 20.061 11.628  1.00 42.67  ? 23  ASN A OD1 1 
ATOM   195  N  ND2 . ASN A 1 24  ? 10.737 21.824 11.262  1.00 35.95  ? 23  ASN A ND2 1 
ATOM   196  N  N   . LEU A 1 25  ? 14.273 24.920 9.014   1.00 37.91  ? 24  LEU A N   1 
ATOM   197  C  CA  . LEU A 1 25  ? 15.357 25.878 8.805   1.00 39.17  ? 24  LEU A CA  1 
ATOM   198  C  C   . LEU A 1 25  ? 15.279 26.957 9.889   1.00 40.20  ? 24  LEU A C   1 
ATOM   199  O  O   . LEU A 1 25  ? 14.198 27.491 10.122  1.00 39.89  ? 24  LEU A O   1 
ATOM   200  C  CB  . LEU A 1 25  ? 15.178 26.521 7.434   1.00 39.37  ? 24  LEU A CB  1 
ATOM   201  C  CG  . LEU A 1 25  ? 16.337 27.133 6.645   1.00 39.61  ? 24  LEU A CG  1 
ATOM   202  C  CD1 . LEU A 1 25  ? 17.475 26.126 6.408   1.00 36.55  ? 24  LEU A CD1 1 
ATOM   203  C  CD2 . LEU A 1 25  ? 15.797 27.706 5.339   1.00 39.06  ? 24  LEU A CD2 1 
ATOM   204  N  N   . PRO A 1 26  ? 16.413 27.278 10.556  1.00 40.53  ? 25  PRO A N   1 
ATOM   205  C  CA  . PRO A 1 26  ? 16.422 28.319 11.584  1.00 41.23  ? 25  PRO A CA  1 
ATOM   206  C  C   . PRO A 1 26  ? 16.321 29.740 11.023  1.00 42.17  ? 25  PRO A C   1 
ATOM   207  O  O   . PRO A 1 26  ? 16.235 29.935 9.813   1.00 41.60  ? 25  PRO A O   1 
ATOM   208  C  CB  . PRO A 1 26  ? 17.781 28.113 12.269  1.00 41.13  ? 25  PRO A CB  1 
ATOM   209  C  CG  . PRO A 1 26  ? 18.633 27.566 11.204  1.00 40.55  ? 25  PRO A CG  1 
ATOM   210  C  CD  . PRO A 1 26  ? 17.748 26.675 10.385  1.00 40.59  ? 25  PRO A CD  1 
ATOM   211  N  N   . GLN A 1 27  ? 16.327 30.720 11.917  1.00 43.90  ? 26  GLN A N   1 
ATOM   212  C  CA  . GLN A 1 27  ? 16.339 32.138 11.540  1.00 45.71  ? 26  GLN A CA  1 
ATOM   213  C  C   . GLN A 1 27  ? 17.775 32.682 11.591  1.00 44.93  ? 26  GLN A C   1 
ATOM   214  O  O   . GLN A 1 27  ? 18.706 31.940 11.917  1.00 45.79  ? 26  GLN A O   1 
ATOM   215  C  CB  . GLN A 1 27  ? 15.414 32.932 12.482  1.00 46.44  ? 26  GLN A CB  1 
ATOM   216  C  CG  A GLN A 1 27  ? 13.942 32.488 12.453  0.50 48.86  ? 26  GLN A CG  1 
ATOM   217  C  CG  B GLN A 1 27  ? 13.956 32.441 12.480  0.50 47.59  ? 26  GLN A CG  1 
ATOM   218  C  CD  A GLN A 1 27  ? 13.236 32.816 11.143  0.50 50.95  ? 26  GLN A CD  1 
ATOM   219  C  CD  B GLN A 1 27  ? 12.994 33.422 13.132  0.50 47.36  ? 26  GLN A CD  1 
ATOM   220  O  OE1 A GLN A 1 27  ? 12.529 31.974 10.581  0.50 52.53  ? 26  GLN A OE1 1 
ATOM   221  O  OE1 B GLN A 1 27  ? 13.140 33.769 14.310  0.50 50.09  ? 26  GLN A OE1 1 
ATOM   222  N  NE2 A GLN A 1 27  ? 13.421 34.044 10.653  0.50 52.25  ? 26  GLN A NE2 1 
ATOM   223  N  NE2 B GLN A 1 27  ? 12.000 33.870 12.368  0.50 47.55  ? 26  GLN A NE2 1 
ATOM   224  N  N   . HIS A 1 28  ? 17.961 33.958 11.261  1.00 44.17  ? 27  HIS A N   1 
ATOM   225  C  CA  . HIS A 1 28  ? 19.275 34.621 11.365  1.00 43.29  ? 27  HIS A CA  1 
ATOM   226  C  C   . HIS A 1 28  ? 20.236 34.067 10.332  1.00 41.32  ? 27  HIS A C   1 
ATOM   227  O  O   . HIS A 1 28  ? 21.430 33.931 10.625  1.00 41.88  ? 27  HIS A O   1 
ATOM   228  C  CB  . HIS A 1 28  ? 19.948 34.420 12.759  1.00 43.76  ? 27  HIS A CB  1 
ATOM   229  C  CG  . HIS A 1 28  ? 19.105 34.833 13.928  0.50 44.83  ? 27  HIS A CG  1 
ATOM   230  N  ND1 . HIS A 1 28  ? 18.881 34.005 15.008  0.50 45.80  ? 27  HIS A ND1 1 
ATOM   231  C  CD2 . HIS A 1 28  ? 18.441 35.984 14.193  0.50 45.87  ? 27  HIS A CD2 1 
ATOM   232  C  CE1 . HIS A 1 28  ? 18.115 34.626 15.887  0.50 46.01  ? 27  HIS A CE1 1 
ATOM   233  N  NE2 . HIS A 1 28  ? 17.831 35.828 15.415  0.50 46.38  ? 27  HIS A NE2 1 
ATOM   234  N  N   . LEU A 1 29  ? 19.751 33.758 9.137   1.00 39.14  ? 28  LEU A N   1 
ATOM   235  C  CA  A LEU A 1 29  ? 20.566 33.005 8.177   0.50 38.84  ? 28  LEU A CA  1 
ATOM   236  C  CA  B LEU A 1 29  ? 20.542 32.990 8.168   0.50 38.22  ? 28  LEU A CA  1 
ATOM   237  C  C   A LEU A 1 29  ? 21.482 33.868 7.328   0.50 37.87  ? 28  LEU A C   1 
ATOM   238  C  C   B LEU A 1 29  ? 21.481 33.868 7.344   0.50 37.53  ? 28  LEU A C   1 
ATOM   239  O  O   A LEU A 1 29  ? 21.077 34.926 6.849   0.50 38.11  ? 28  LEU A O   1 
ATOM   240  O  O   B LEU A 1 29  ? 21.090 34.949 6.907   0.50 37.75  ? 28  LEU A O   1 
ATOM   241  C  CB  A LEU A 1 29  ? 19.663 32.178 7.259   0.50 39.35  ? 28  LEU A CB  1 
ATOM   242  C  CB  B LEU A 1 29  ? 19.604 32.223 7.223   0.50 38.33  ? 28  LEU A CB  1 
ATOM   243  C  CG  A LEU A 1 29  ? 19.562 30.654 7.375   0.50 39.96  ? 28  LEU A CG  1 
ATOM   244  C  CG  B LEU A 1 29  ? 18.442 31.392 7.788   0.50 36.82  ? 28  LEU A CG  1 
ATOM   245  C  CD1 A LEU A 1 29  ? 19.720 30.121 8.794   0.50 39.61  ? 28  LEU A CD1 1 
ATOM   246  C  CD1 B LEU A 1 29  ? 17.260 31.390 6.818   0.50 35.08  ? 28  LEU A CD1 1 
ATOM   247  C  CD2 A LEU A 1 29  ? 18.239 30.222 6.764   0.50 40.31  ? 28  LEU A CD2 1 
ATOM   248  C  CD2 B LEU A 1 29  ? 18.889 29.950 8.127   0.50 34.90  ? 28  LEU A CD2 1 
ATOM   249  N  N   . PHE A 1 30  ? 22.712 33.400 7.127   1.00 36.27  ? 29  PHE A N   1 
ATOM   250  C  CA  . PHE A 1 30  ? 23.616 34.012 6.175   1.00 34.64  ? 29  PHE A CA  1 
ATOM   251  C  C   . PHE A 1 30  ? 23.676 33.174 4.882   1.00 33.92  ? 29  PHE A C   1 
ATOM   252  O  O   . PHE A 1 30  ? 23.680 33.719 3.774   1.00 32.34  ? 29  PHE A O   1 
ATOM   253  C  CB  . PHE A 1 30  ? 25.045 34.185 6.740   1.00 34.80  ? 29  PHE A CB  1 
ATOM   254  C  CG  . PHE A 1 30  ? 26.020 34.785 5.743   1.00 35.00  ? 29  PHE A CG  1 
ATOM   255  C  CD1 . PHE A 1 30  ? 25.849 36.091 5.281   1.00 38.12  ? 29  PHE A CD1 1 
ATOM   256  C  CD2 . PHE A 1 30  ? 27.093 34.058 5.265   1.00 36.75  ? 29  PHE A CD2 1 
ATOM   257  C  CE1 . PHE A 1 30  ? 26.734 36.647 4.371   1.00 38.55  ? 29  PHE A CE1 1 
ATOM   258  C  CE2 . PHE A 1 30  ? 27.990 34.600 4.350   1.00 36.40  ? 29  PHE A CE2 1 
ATOM   259  C  CZ  . PHE A 1 30  ? 27.809 35.896 3.893   1.00 38.05  ? 29  PHE A CZ  1 
ATOM   260  N  N   . GLY A 1 31  ? 23.788 31.853 5.028   1.00 32.46  ? 30  GLY A N   1 
ATOM   261  C  CA  . GLY A 1 31  ? 23.730 30.966 3.856   1.00 31.77  ? 30  GLY A CA  1 
ATOM   262  C  C   . GLY A 1 31  ? 23.966 29.490 4.162   1.00 31.11  ? 30  GLY A C   1 
ATOM   263  O  O   . GLY A 1 31  ? 23.903 29.082 5.331   1.00 29.93  ? 30  GLY A O   1 
ATOM   264  N  N   . TYR A 1 32  ? 24.252 28.717 3.099   1.00 30.37  ? 31  TYR A N   1 
ATOM   265  C  CA  . TYR A 1 32  ? 24.231 27.260 3.127   1.00 30.08  ? 31  TYR A CA  1 
ATOM   266  C  C   . TYR A 1 32  ? 25.493 26.696 2.502   1.00 30.82  ? 31  TYR A C   1 
ATOM   267  O  O   . TYR A 1 32  ? 25.996 27.229 1.492   1.00 30.19  ? 31  TYR A O   1 
ATOM   268  C  CB  . TYR A 1 32  ? 23.030 26.699 2.325   1.00 30.59  ? 31  TYR A CB  1 
ATOM   269  C  CG  . TYR A 1 32  ? 21.703 27.403 2.568   1.00 30.69  ? 31  TYR A CG  1 
ATOM   270  C  CD1 . TYR A 1 32  ? 20.899 27.790 1.499   1.00 29.44  ? 31  TYR A CD1 1 
ATOM   271  C  CD2 . TYR A 1 32  ? 21.253 27.674 3.874   1.00 29.89  ? 31  TYR A CD2 1 
ATOM   272  C  CE1 . TYR A 1 32  ? 19.669 28.424 1.713   1.00 28.48  ? 31  TYR A CE1 1 
ATOM   273  C  CE2 . TYR A 1 32  ? 20.032 28.320 4.097   1.00 30.83  ? 31  TYR A CE2 1 
ATOM   274  C  CZ  . TYR A 1 32  ? 19.263 28.701 3.006   1.00 30.99  ? 31  TYR A CZ  1 
ATOM   275  O  OH  . TYR A 1 32  ? 18.066 29.336 3.205   1.00 33.35  ? 31  TYR A OH  1 
ATOM   276  N  N   . SER A 1 33  ? 25.982 25.599 3.089   1.00 30.59  ? 32  SER A N   1 
ATOM   277  C  CA  . SER A 1 33  ? 27.151 24.879 2.598   1.00 30.76  ? 32  SER A CA  1 
ATOM   278  C  C   . SER A 1 33  ? 26.788 23.386 2.562   1.00 31.05  ? 32  SER A C   1 
ATOM   279  O  O   . SER A 1 33  ? 26.430 22.813 3.597   1.00 30.91  ? 32  SER A O   1 
ATOM   280  C  CB  . SER A 1 33  ? 28.349 25.125 3.528   1.00 30.97  ? 32  SER A CB  1 
ATOM   281  O  OG  . SER A 1 33  ? 28.670 26.509 3.589   1.00 32.77  ? 32  SER A OG  1 
ATOM   282  N  N   . TRP A 1 34  ? 26.859 22.769 1.386   1.00 30.43  ? 33  TRP A N   1 
ATOM   283  C  CA  . TRP A 1 34  ? 26.464 21.356 1.254   1.00 30.88  ? 33  TRP A CA  1 
ATOM   284  C  C   . TRP A 1 34  ? 27.682 20.470 0.979   1.00 31.35  ? 33  TRP A C   1 
ATOM   285  O  O   . TRP A 1 34  ? 28.596 20.884 0.240   1.00 30.89  ? 33  TRP A O   1 
ATOM   286  C  CB  . TRP A 1 34  ? 25.472 21.175 0.098   1.00 30.37  ? 33  TRP A CB  1 
ATOM   287  C  CG  . TRP A 1 34  ? 24.003 21.317 0.418   1.00 31.02  ? 33  TRP A CG  1 
ATOM   288  C  CD1 . TRP A 1 34  ? 23.210 22.404 0.164   1.00 29.45  ? 33  TRP A CD1 1 
ATOM   289  C  CD2 . TRP A 1 34  ? 23.139 20.313 0.984   1.00 31.58  ? 33  TRP A CD2 1 
ATOM   290  N  NE1 . TRP A 1 34  ? 21.912 22.142 0.542   1.00 30.36  ? 33  TRP A NE1 1 
ATOM   291  C  CE2 . TRP A 1 34  ? 21.841 20.869 1.054   1.00 31.07  ? 33  TRP A CE2 1 
ATOM   292  C  CE3 . TRP A 1 34  ? 23.337 18.996 1.435   1.00 31.63  ? 33  TRP A CE3 1 
ATOM   293  C  CZ2 . TRP A 1 34  ? 20.742 20.157 1.562   1.00 30.30  ? 33  TRP A CZ2 1 
ATOM   294  C  CZ3 . TRP A 1 34  ? 22.230 18.283 1.956   1.00 31.15  ? 33  TRP A CZ3 1 
ATOM   295  C  CH2 . TRP A 1 34  ? 20.959 18.867 2.008   1.00 31.19  ? 33  TRP A CH2 1 
ATOM   296  N  N   . TYR A 1 35  ? 27.670 19.255 1.539   1.00 32.33  ? 34  TYR A N   1 
ATOM   297  C  CA  . TYR A 1 35  ? 28.801 18.299 1.455   1.00 32.74  ? 34  TYR A CA  1 
ATOM   298  C  C   . TYR A 1 35  ? 28.330 16.884 1.088   1.00 33.18  ? 34  TYR A C   1 
ATOM   299  O  O   . TYR A 1 35  ? 27.212 16.496 1.427   1.00 33.10  ? 34  TYR A O   1 
ATOM   300  C  CB  . TYR A 1 35  ? 29.521 18.197 2.821   1.00 32.28  ? 34  TYR A CB  1 
ATOM   301  C  CG  . TYR A 1 35  ? 29.997 19.538 3.340   1.00 30.78  ? 34  TYR A CG  1 
ATOM   302  C  CD1 . TYR A 1 35  ? 29.131 20.400 4.030   1.00 31.48  ? 34  TYR A CD1 1 
ATOM   303  C  CD2 . TYR A 1 35  ? 31.308 19.956 3.121   1.00 30.17  ? 34  TYR A CD2 1 
ATOM   304  C  CE1 . TYR A 1 35  ? 29.578 21.659 4.480   1.00 30.62  ? 34  TYR A CE1 1 
ATOM   305  C  CE2 . TYR A 1 35  ? 31.769 21.212 3.565   1.00 30.09  ? 34  TYR A CE2 1 
ATOM   306  C  CZ  . TYR A 1 35  ? 30.879 22.060 4.228   1.00 30.76  ? 34  TYR A CZ  1 
ATOM   307  O  OH  . TYR A 1 35  ? 31.322 23.290 4.666   1.00 32.49  ? 34  TYR A OH  1 
ATOM   308  N  N   . LYS A 1 36  ? 29.205 16.117 0.434   1.00 34.25  ? 35  LYS A N   1 
ATOM   309  C  CA  . LYS A 1 36  ? 29.053 14.663 0.341   1.00 35.51  ? 35  LYS A CA  1 
ATOM   310  C  C   . LYS A 1 36  ? 29.653 14.066 1.617   1.00 35.85  ? 35  LYS A C   1 
ATOM   311  O  O   . LYS A 1 36  ? 30.702 14.515 2.085   1.00 35.98  ? 35  LYS A O   1 
ATOM   312  C  CB  . LYS A 1 36  ? 29.775 14.103 -0.897  1.00 36.09  ? 35  LYS A CB  1 
ATOM   313  C  CG  . LYS A 1 36  ? 29.513 12.590 -1.142  1.00 37.63  ? 35  LYS A CG  1 
ATOM   314  C  CD  . LYS A 1 36  ? 28.079 12.331 -1.590  1.00 38.45  ? 35  LYS A CD  1 
ATOM   315  C  CE  . LYS A 1 36  ? 27.672 10.837 -1.565  1.00 39.15  ? 35  LYS A CE  1 
ATOM   316  N  NZ  A LYS A 1 36  ? 27.781 10.310 -0.180  0.50 41.46  ? 35  LYS A NZ  1 
ATOM   317  N  NZ  B LYS A 1 36  ? 28.364 9.992  -2.598  0.50 33.23  ? 35  LYS A NZ  1 
ATOM   318  N  N   . GLY A 1 37  ? 28.975 13.079 2.194   1.00 36.76  ? 36  GLY A N   1 
ATOM   319  C  CA  . GLY A 1 37  ? 29.471 12.455 3.413   1.00 37.49  ? 36  GLY A CA  1 
ATOM   320  C  C   . GLY A 1 37  ? 28.673 12.877 4.630   1.00 38.19  ? 36  GLY A C   1 
ATOM   321  O  O   . GLY A 1 37  ? 27.620 13.511 4.508   1.00 37.24  ? 36  GLY A O   1 
ATOM   322  N  N   . GLU A 1 38  ? 29.199 12.552 5.806   1.00 38.55  ? 37  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 38  ? 28.428 12.650 7.034   1.00 40.00  ? 37  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 38  ? 28.867 13.814 7.911   1.00 40.19  ? 37  GLU A C   1 
ATOM   325  O  O   . GLU A 1 38  ? 28.336 13.984 9.010   1.00 40.71  ? 37  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 38  ? 28.517 11.336 7.823   1.00 39.75  ? 37  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 38  ? 27.830 10.167 7.114   1.00 39.78  ? 37  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 38  ? 27.978 8.865  7.879   1.00 42.44  ? 37  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 38  ? 28.888 8.081  7.533   1.00 47.41  ? 37  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 38  ? 27.199 8.644  8.825   1.00 45.13  ? 37  GLU A OE2 1 
ATOM   331  N  N   . ARG A 1 39  ? 29.835 14.591 7.435   1.00 40.31  ? 38  ARG A N   1 
ATOM   332  C  CA  . ARG A 1 39  ? 30.313 15.738 8.192   1.00 41.39  ? 38  ARG A CA  1 
ATOM   333  C  C   . ARG A 1 39  ? 30.673 16.957 7.334   1.00 40.21  ? 38  ARG A C   1 
ATOM   334  O  O   . ARG A 1 39  ? 30.775 16.883 6.114   1.00 40.13  ? 38  ARG A O   1 
ATOM   335  C  CB  . ARG A 1 39  ? 31.508 15.340 9.074   1.00 41.41  ? 38  ARG A CB  1 
ATOM   336  C  CG  . ARG A 1 39  ? 32.803 15.019 8.323   1.00 42.55  ? 38  ARG A CG  1 
ATOM   337  C  CD  . ARG A 1 39  ? 33.973 14.740 9.298   1.00 43.85  ? 38  ARG A CD  1 
ATOM   338  N  NE  A ARG A 1 39  ? 35.288 14.912 8.657   0.40 45.49  ? 38  ARG A NE  1 
ATOM   339  N  NE  B ARG A 1 39  ? 33.699 13.630 10.221  0.40 44.58  ? 38  ARG A NE  1 
ATOM   340  N  NE  C ARG A 1 39  ? 35.006 13.876 8.731   0.20 44.42  ? 38  ARG A NE  1 
ATOM   341  C  CZ  A ARG A 1 39  ? 35.884 14.022 7.854   0.40 46.66  ? 38  ARG A CZ  1 
ATOM   342  C  CZ  B ARG A 1 39  ? 34.556 13.159 11.133  0.40 44.86  ? 38  ARG A CZ  1 
ATOM   343  C  CZ  C ARG A 1 39  ? 36.228 13.730 9.243   0.20 44.81  ? 38  ARG A CZ  1 
ATOM   344  N  NH1 A ARG A 1 39  ? 35.300 12.863 7.558   0.40 46.33  ? 38  ARG A NH1 1 
ATOM   345  N  NH1 B ARG A 1 39  ? 35.767 13.691 11.270  0.40 45.03  ? 38  ARG A NH1 1 
ATOM   346  N  NH1 C ARG A 1 39  ? 36.589 14.402 10.334  0.20 44.39  ? 38  ARG A NH1 1 
ATOM   347  N  NH2 A ARG A 1 39  ? 37.080 14.293 7.339   0.40 46.54  ? 38  ARG A NH2 1 
ATOM   348  N  NH2 B ARG A 1 39  ? 34.196 12.151 11.920  0.40 44.57  ? 38  ARG A NH2 1 
ATOM   349  N  NH2 C ARG A 1 39  ? 37.096 12.915 8.654   0.20 44.63  ? 38  ARG A NH2 1 
ATOM   350  N  N   . VAL A 1 40  ? 30.879 18.077 8.010   1.00 39.31  ? 39  VAL A N   1 
ATOM   351  C  CA  . VAL A 1 40  ? 31.431 19.262 7.396   1.00 38.12  ? 39  VAL A CA  1 
ATOM   352  C  C   . VAL A 1 40  ? 32.893 19.023 7.098   1.00 38.42  ? 39  VAL A C   1 
ATOM   353  O  O   . VAL A 1 40  ? 33.677 18.781 8.003   1.00 39.59  ? 39  VAL A O   1 
ATOM   354  C  CB  . VAL A 1 40  ? 31.263 20.498 8.350   1.00 37.99  ? 39  VAL A CB  1 
ATOM   355  C  CG1 . VAL A 1 40  ? 31.957 21.714 7.774   1.00 34.96  ? 39  VAL A CG1 1 
ATOM   356  C  CG2 . VAL A 1 40  ? 29.767 20.755 8.618   1.00 36.37  ? 39  VAL A CG2 1 
ATOM   357  N  N   . ASP A 1 41  ? 33.273 19.117 5.831   1.00 38.28  ? 40  ASP A N   1 
ATOM   358  C  CA  . ASP A 1 41  ? 34.641 18.811 5.408   1.00 37.90  ? 40  ASP A CA  1 
ATOM   359  C  C   . ASP A 1 41  ? 34.849 19.491 4.074   1.00 37.46  ? 40  ASP A C   1 
ATOM   360  O  O   . ASP A 1 41  ? 34.304 19.050 3.070   1.00 37.67  ? 40  ASP A O   1 
ATOM   361  C  CB  . ASP A 1 41  ? 34.786 17.283 5.266   1.00 37.90  ? 40  ASP A CB  1 
ATOM   362  C  CG  . ASP A 1 41  ? 36.165 16.828 4.747   1.00 39.39  ? 40  ASP A CG  1 
ATOM   363  O  OD1 . ASP A 1 41  ? 37.046 17.640 4.394   1.00 37.91  ? 40  ASP A OD1 1 
ATOM   364  O  OD2 . ASP A 1 41  ? 36.342 15.591 4.671   1.00 44.09  ? 40  ASP A OD2 1 
ATOM   365  N  N   . GLY A 1 42  ? 35.636 20.560 4.072   1.00 37.01  ? 41  GLY A N   1 
ATOM   366  C  CA  . GLY A 1 42  ? 35.874 21.370 2.876   1.00 37.31  ? 41  GLY A CA  1 
ATOM   367  C  C   . GLY A 1 42  ? 36.293 20.596 1.637   1.00 38.38  ? 41  GLY A C   1 
ATOM   368  O  O   . GLY A 1 42  ? 35.974 20.993 0.502   1.00 38.32  ? 41  GLY A O   1 
ATOM   369  N  N   . ASN A 1 43  ? 37.018 19.498 1.839   1.00 38.52  ? 42  ASN A N   1 
ATOM   370  C  CA  . ASN A 1 43  ? 37.494 18.687 0.713   1.00 39.00  ? 42  ASN A CA  1 
ATOM   371  C  C   . ASN A 1 43  ? 36.340 17.998 0.007   1.00 38.27  ? 42  ASN A C   1 
ATOM   372  O  O   . ASN A 1 43  ? 36.462 17.633 -1.155  1.00 37.86  ? 42  ASN A O   1 
ATOM   373  C  CB  . ASN A 1 43  ? 38.502 17.613 1.173   1.00 40.46  ? 42  ASN A CB  1 
ATOM   374  C  CG  . ASN A 1 43  ? 39.731 18.197 1.827   1.00 42.61  ? 42  ASN A CG  1 
ATOM   375  O  OD1 . ASN A 1 43  ? 40.350 19.131 1.314   1.00 47.13  ? 42  ASN A OD1 1 
ATOM   376  N  ND2 . ASN A 1 43  ? 40.095 17.643 2.974   1.00 49.55  ? 42  ASN A ND2 1 
ATOM   377  N  N   . ARG A 1 44  ? 35.221 17.820 0.708   1.00 37.28  ? 43  ARG A N   1 
ATOM   378  C  CA  . ARG A 1 44  ? 34.047 17.177 0.122   1.00 37.17  ? 43  ARG A CA  1 
ATOM   379  C  C   . ARG A 1 44  ? 32.862 18.144 -0.144  1.00 36.00  ? 43  ARG A C   1 
ATOM   380  O  O   . ARG A 1 44  ? 31.719 17.694 -0.294  1.00 35.02  ? 43  ARG A O   1 
ATOM   381  C  CB  . ARG A 1 44  ? 33.597 15.997 0.997   1.00 37.08  ? 43  ARG A CB  1 
ATOM   382  C  CG  . ARG A 1 44  ? 34.741 15.005 1.354   1.00 38.84  ? 43  ARG A CG  1 
ATOM   383  C  CD  . ARG A 1 44  ? 34.191 13.627 1.763   1.00 39.49  ? 43  ARG A CD  1 
ATOM   384  N  NE  . ARG A 1 44  ? 33.668 12.919 0.597   1.00 45.57  ? 43  ARG A NE  1 
ATOM   385  C  CZ  . ARG A 1 44  ? 32.925 11.818 0.635   1.00 46.42  ? 43  ARG A CZ  1 
ATOM   386  N  NH1 . ARG A 1 44  ? 32.595 11.253 1.795   1.00 47.26  ? 43  ARG A NH1 1 
ATOM   387  N  NH2 . ARG A 1 44  ? 32.508 11.282 -0.508  1.00 47.93  ? 43  ARG A NH2 1 
ATOM   388  N  N   . GLN A 1 45  ? 33.135 19.454 -0.191  1.00 35.92  ? 44  GLN A N   1 
ATOM   389  C  CA  . GLN A 1 45  ? 32.063 20.444 -0.349  1.00 35.09  ? 44  GLN A CA  1 
ATOM   390  C  C   . GLN A 1 45  ? 31.538 20.529 -1.782  1.00 34.61  ? 44  GLN A C   1 
ATOM   391  O  O   . GLN A 1 45  ? 32.296 20.734 -2.719  1.00 35.59  ? 44  GLN A O   1 
ATOM   392  C  CB  . GLN A 1 45  ? 32.450 21.844 0.154   1.00 34.78  ? 44  GLN A CB  1 
ATOM   393  C  CG  . GLN A 1 45  ? 31.224 22.757 0.224   1.00 34.70  ? 44  GLN A CG  1 
ATOM   394  C  CD  . GLN A 1 45  ? 31.456 24.104 0.870   1.00 35.05  ? 44  GLN A CD  1 
ATOM   395  O  OE1 . GLN A 1 45  ? 32.468 24.332 1.541   1.00 34.37  ? 44  GLN A OE1 1 
ATOM   396  N  NE2 . GLN A 1 45  ? 30.501 25.016 0.671   1.00 32.01  ? 44  GLN A NE2 1 
ATOM   397  N  N   . ILE A 1 46  ? 30.230 20.376 -1.922  1.00 33.70  ? 45  ILE A N   1 
ATOM   398  C  CA  . ILE A 1 46  ? 29.562 20.410 -3.222  1.00 33.10  ? 45  ILE A CA  1 
ATOM   399  C  C   . ILE A 1 46  ? 29.356 21.849 -3.692  1.00 33.41  ? 45  ILE A C   1 
ATOM   400  O  O   . ILE A 1 46  ? 29.699 22.212 -4.833  1.00 33.37  ? 45  ILE A O   1 
ATOM   401  C  CB  . ILE A 1 46  ? 28.198 19.688 -3.121  1.00 32.88  ? 45  ILE A CB  1 
ATOM   402  C  CG1 . ILE A 1 46  ? 28.400 18.202 -2.787  1.00 32.88  ? 45  ILE A CG1 1 
ATOM   403  C  CG2 . ILE A 1 46  ? 27.400 19.849 -4.399  1.00 32.20  ? 45  ILE A CG2 1 
ATOM   404  C  CD1 . ILE A 1 46  ? 27.135 17.493 -2.338  1.00 30.64  ? 45  ILE A CD1 1 
ATOM   405  N  N   . ILE A 1 47  ? 28.810 22.682 -2.802  1.00 32.76  ? 46  ILE A N   1 
ATOM   406  C  CA  . ILE A 1 47  ? 28.371 24.021 -3.208  1.00 33.09  ? 46  ILE A CA  1 
ATOM   407  C  C   . ILE A 1 47  ? 28.192 24.905 -1.975  1.00 33.18  ? 46  ILE A C   1 
ATOM   408  O  O   . ILE A 1 47  ? 27.950 24.384 -0.870  1.00 32.90  ? 46  ILE A O   1 
ATOM   409  C  CB  . ILE A 1 47  ? 27.059 23.923 -4.056  1.00 33.42  ? 46  ILE A CB  1 
ATOM   410  C  CG1 . ILE A 1 47  ? 26.809 25.199 -4.874  1.00 33.94  ? 46  ILE A CG1 1 
ATOM   411  C  CG2 . ILE A 1 47  ? 25.829 23.506 -3.195  1.00 34.17  ? 46  ILE A CG2 1 
ATOM   412  C  CD1 . ILE A 1 47  ? 25.722 25.024 -5.990  1.00 33.63  ? 46  ILE A CD1 1 
ATOM   413  N  N   . GLY A 1 48  ? 28.370 26.214 -2.156  1.00 32.13  ? 47  GLY A N   1 
ATOM   414  C  CA  . GLY A 1 48  ? 28.074 27.212 -1.118  1.00 32.88  ? 47  GLY A CA  1 
ATOM   415  C  C   . GLY A 1 48  ? 27.068 28.214 -1.663  1.00 33.38  ? 47  GLY A C   1 
ATOM   416  O  O   . GLY A 1 48  ? 27.111 28.545 -2.847  1.00 33.33  ? 47  GLY A O   1 
ATOM   417  N  N   . TYR A 1 49  ? 26.163 28.698 -0.823  1.00 32.67  ? 48  TYR A N   1 
ATOM   418  C  CA  . TYR A 1 49  ? 25.097 29.607 -1.314  1.00 33.01  ? 48  TYR A CA  1 
ATOM   419  C  C   . TYR A 1 49  ? 24.813 30.729 -0.330  1.00 32.71  ? 48  TYR A C   1 
ATOM   420  O  O   . TYR A 1 49  ? 24.449 30.474 0.821   1.00 31.72  ? 48  TYR A O   1 
ATOM   421  C  CB  . TYR A 1 49  ? 23.808 28.824 -1.594  1.00 32.42  ? 48  TYR A CB  1 
ATOM   422  C  CG  . TYR A 1 49  ? 22.604 29.672 -2.012  1.00 34.02  ? 48  TYR A CG  1 
ATOM   423  C  CD1 . TYR A 1 49  ? 22.428 30.060 -3.342  1.00 33.35  ? 48  TYR A CD1 1 
ATOM   424  C  CD2 . TYR A 1 49  ? 21.661 30.092 -1.071  1.00 33.38  ? 48  TYR A CD2 1 
ATOM   425  C  CE1 . TYR A 1 49  ? 21.320 30.841 -3.728  1.00 34.56  ? 48  TYR A CE1 1 
ATOM   426  C  CE2 . TYR A 1 49  ? 20.546 30.862 -1.450  1.00 32.33  ? 48  TYR A CE2 1 
ATOM   427  C  CZ  . TYR A 1 49  ? 20.396 31.235 -2.770  1.00 33.55  ? 48  TYR A CZ  1 
ATOM   428  O  OH  . TYR A 1 49  ? 19.285 31.981 -3.134  1.00 34.42  ? 48  TYR A OH  1 
ATOM   429  N  N   . VAL A 1 50  ? 24.958 31.964 -0.805  1.00 32.98  ? 49  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 50  ? 24.726 33.161 0.013   1.00 33.56  ? 49  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 50  ? 23.314 33.665 -0.230  1.00 34.16  ? 49  VAL A C   1 
ATOM   432  O  O   . VAL A 1 50  ? 22.965 34.021 -1.348  1.00 33.28  ? 49  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 50  ? 25.763 34.302 -0.319  1.00 33.91  ? 49  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 50  ? 25.547 35.525 0.612   1.00 33.96  ? 49  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 50  ? 27.189 33.802 -0.203  1.00 33.94  ? 49  VAL A CG2 1 
ATOM   436  N  N   . ILE A 1 51  ? 22.519 33.726 0.823   1.00 35.02  ? 50  ILE A N   1 
ATOM   437  C  CA  . ILE A 1 51  ? 21.121 34.098 0.691   1.00 36.75  ? 50  ILE A CA  1 
ATOM   438  C  C   . ILE A 1 51  ? 20.917 35.524 0.159   1.00 37.94  ? 50  ILE A C   1 
ATOM   439  O  O   . ILE A 1 51  ? 20.137 35.728 -0.781  1.00 37.46  ? 50  ILE A O   1 
ATOM   440  C  CB  . ILE A 1 51  ? 20.376 33.880 2.019   1.00 36.62  ? 50  ILE A CB  1 
ATOM   441  C  CG1 . ILE A 1 51  ? 20.282 32.372 2.302   1.00 35.42  ? 50  ILE A CG1 1 
ATOM   442  C  CG2 . ILE A 1 51  ? 18.972 34.500 1.965   1.00 38.57  ? 50  ILE A CG2 1 
ATOM   443  C  CD1 . ILE A 1 51  ? 20.013 32.051 3.738   1.00 34.61  ? 50  ILE A CD1 1 
ATOM   444  N  N   . GLY A 1 52  ? 21.639 36.489 0.736   1.00 38.76  ? 51  GLY A N   1 
ATOM   445  C  CA  . GLY A 1 52  ? 21.413 37.901 0.438   1.00 40.05  ? 51  GLY A CA  1 
ATOM   446  C  C   . GLY A 1 52  ? 21.749 38.283 -0.985  1.00 40.41  ? 51  GLY A C   1 
ATOM   447  O  O   . GLY A 1 52  ? 21.094 39.139 -1.578  1.00 42.69  ? 51  GLY A O   1 
ATOM   448  N  N   . THR A 1 53  ? 22.757 37.653 -1.553  1.00 40.68  ? 52  THR A N   1 
ATOM   449  C  CA  . THR A 1 53  ? 23.215 37.995 -2.890  1.00 40.51  ? 52  THR A CA  1 
ATOM   450  C  C   . THR A 1 53  ? 22.776 36.960 -3.912  1.00 40.30  ? 52  THR A C   1 
ATOM   451  O  O   . THR A 1 53  ? 23.020 37.132 -5.106  1.00 39.79  ? 52  THR A O   1 
ATOM   452  C  CB  . THR A 1 53  ? 24.733 38.043 -2.943  1.00 41.87  ? 52  THR A CB  1 
ATOM   453  O  OG1 . THR A 1 53  ? 25.256 36.728 -2.656  1.00 41.42  ? 52  THR A OG1 1 
ATOM   454  C  CG2 . THR A 1 53  ? 25.295 39.065 -1.915  1.00 41.58  ? 52  THR A CG2 1 
ATOM   455  N  N   . GLN A 1 54  ? 22.192 35.858 -3.430  1.00 39.75  ? 53  GLN A N   1 
ATOM   456  C  CA  . GLN A 1 54  ? 21.831 34.710 -4.273  1.00 39.81  ? 53  GLN A CA  1 
ATOM   457  C  C   . GLN A 1 54  ? 22.960 34.098 -5.098  1.00 40.19  ? 53  GLN A C   1 
ATOM   458  O  O   . GLN A 1 54  ? 22.712 33.571 -6.189  1.00 40.06  ? 53  GLN A O   1 
ATOM   459  C  CB  . GLN A 1 54  ? 20.644 35.066 -5.172  1.00 39.18  ? 53  GLN A CB  1 
ATOM   460  C  CG  . GLN A 1 54  ? 19.398 35.435 -4.383  1.00 39.46  ? 53  GLN A CG  1 
ATOM   461  C  CD  . GLN A 1 54  ? 18.195 35.726 -5.277  1.00 41.29  ? 53  GLN A CD  1 
ATOM   462  O  OE1 . GLN A 1 54  ? 17.728 34.864 -6.023  1.00 42.11  ? 53  GLN A OE1 1 
ATOM   463  N  NE2 . GLN A 1 54  ? 17.691 36.939 -5.197  1.00 44.80  ? 53  GLN A NE2 1 
ATOM   464  N  N   . GLN A 1 55  ? 24.198 34.144 -4.598  1.00 39.65  ? 54  GLN A N   1 
ATOM   465  C  CA  . GLN A 1 55  ? 25.299 33.581 -5.353  1.00 40.29  ? 54  GLN A CA  1 
ATOM   466  C  C   . GLN A 1 55  ? 25.649 32.175 -4.882  1.00 40.12  ? 54  GLN A C   1 
ATOM   467  O  O   . GLN A 1 55  ? 25.887 31.951 -3.682  1.00 38.25  ? 54  GLN A O   1 
ATOM   468  C  CB  . GLN A 1 55  ? 26.555 34.464 -5.292  1.00 41.64  ? 54  GLN A CB  1 
ATOM   469  C  CG  . GLN A 1 55  ? 26.433 35.835 -5.983  1.00 45.44  ? 54  GLN A CG  1 
ATOM   470  C  CD  . GLN A 1 55  ? 25.956 35.741 -7.430  1.00 50.54  ? 54  GLN A CD  1 
ATOM   471  O  OE1 . GLN A 1 55  ? 24.811 36.104 -7.745  1.00 54.91  ? 54  GLN A OE1 1 
ATOM   472  N  NE2 . GLN A 1 55  ? 26.815 35.235 -8.309  1.00 50.81  ? 54  GLN A NE2 1 
ATOM   473  N  N   . ALA A 1 56  ? 25.700 31.259 -5.849  1.00 39.88  ? 55  ALA A N   1 
ATOM   474  C  CA  . ALA A 1 56  ? 26.139 29.888 -5.635  1.00 39.96  ? 55  ALA A CA  1 
ATOM   475  C  C   . ALA A 1 56  ? 27.551 29.714 -6.175  1.00 40.09  ? 55  ALA A C   1 
ATOM   476  O  O   . ALA A 1 56  ? 27.875 30.196 -7.272  1.00 40.38  ? 55  ALA A O   1 
ATOM   477  C  CB  . ALA A 1 56  ? 25.167 28.896 -6.301  1.00 39.56  ? 55  ALA A CB  1 
ATOM   478  N  N   . THR A 1 57  ? 28.404 29.048 -5.397  1.00 39.14  ? 56  THR A N   1 
ATOM   479  C  CA  . THR A 1 57  ? 29.769 28.814 -5.808  1.00 38.99  ? 56  THR A CA  1 
ATOM   480  C  C   . THR A 1 57  ? 30.076 27.335 -5.621  1.00 39.66  ? 56  THR A C   1 
ATOM   481  O  O   . THR A 1 57  ? 29.823 26.777 -4.544  1.00 39.47  ? 56  THR A O   1 
ATOM   482  C  CB  . THR A 1 57  ? 30.741 29.704 -4.990  1.00 39.31  ? 56  THR A CB  1 
ATOM   483  O  OG1 . THR A 1 57  ? 30.336 31.073 -5.108  1.00 37.35  ? 56  THR A OG1 1 
ATOM   484  C  CG2 . THR A 1 57  ? 32.199 29.564 -5.445  1.00 39.04  ? 56  THR A CG2 1 
ATOM   485  N  N   . PRO A 1 58  ? 30.605 26.683 -6.673  1.00 39.76  ? 57  PRO A N   1 
ATOM   486  C  CA  . PRO A 1 58  ? 31.022 25.281 -6.570  1.00 39.71  ? 57  PRO A CA  1 
ATOM   487  C  C   . PRO A 1 58  ? 32.132 25.060 -5.550  1.00 39.50  ? 57  PRO A C   1 
ATOM   488  O  O   . PRO A 1 58  ? 33.053 25.891 -5.427  1.00 39.24  ? 57  PRO A O   1 
ATOM   489  C  CB  . PRO A 1 58  ? 31.552 24.951 -7.980  1.00 39.93  ? 57  PRO A CB  1 
ATOM   490  C  CG  . PRO A 1 58  ? 31.713 26.248 -8.672  1.00 41.16  ? 57  PRO A CG  1 
ATOM   491  C  CD  . PRO A 1 58  ? 30.806 27.234 -8.028  1.00 40.29  ? 57  PRO A CD  1 
ATOM   492  N  N   . GLY A 1 59  ? 32.035 23.952 -4.818  1.00 38.85  ? 58  GLY A N   1 
ATOM   493  C  CA  . GLY A 1 59  ? 33.155 23.465 -4.013  1.00 39.04  ? 58  GLY A CA  1 
ATOM   494  C  C   . GLY A 1 59  ? 33.875 22.356 -4.773  1.00 39.46  ? 58  GLY A C   1 
ATOM   495  O  O   . GLY A 1 59  ? 33.512 22.049 -5.916  1.00 38.68  ? 58  GLY A O   1 
ATOM   496  N  N   . PRO A 1 60  ? 34.892 21.730 -4.143  1.00 40.10  ? 59  PRO A N   1 
ATOM   497  C  CA  . PRO A 1 60  ? 35.627 20.600 -4.758  1.00 40.16  ? 59  PRO A CA  1 
ATOM   498  C  C   . PRO A 1 60  ? 34.775 19.433 -5.273  1.00 40.63  ? 59  PRO A C   1 
ATOM   499  O  O   . PRO A 1 60  ? 35.172 18.785 -6.254  1.00 41.48  ? 59  PRO A O   1 
ATOM   500  C  CB  . PRO A 1 60  ? 36.548 20.119 -3.625  1.00 40.25  ? 59  PRO A CB  1 
ATOM   501  C  CG  . PRO A 1 60  ? 36.785 21.373 -2.801  1.00 40.25  ? 59  PRO A CG  1 
ATOM   502  C  CD  . PRO A 1 60  ? 35.458 22.109 -2.834  1.00 39.59  ? 59  PRO A CD  1 
ATOM   503  N  N   . ALA A 1 61  ? 33.639 19.147 -4.634  1.00 39.86  ? 60  ALA A N   1 
ATOM   504  C  CA  . ALA A 1 61  ? 32.807 18.009 -5.029  1.00 39.96  ? 60  ALA A CA  1 
ATOM   505  C  C   . ALA A 1 61  ? 31.657 18.357 -5.986  1.00 39.79  ? 60  ALA A C   1 
ATOM   506  O  O   . ALA A 1 61  ? 30.813 17.519 -6.265  1.00 40.20  ? 60  ALA A O   1 
ATOM   507  C  CB  . ALA A 1 61  ? 32.262 17.291 -3.787  1.00 39.78  ? 60  ALA A CB  1 
ATOM   508  N  N   . TYR A 1 62  ? 31.621 19.594 -6.471  1.00 40.10  ? 61  TYR A N   1 
ATOM   509  C  CA  . TYR A 1 62  ? 30.593 20.060 -7.413  1.00 40.22  ? 61  TYR A CA  1 
ATOM   510  C  C   . TYR A 1 62  ? 30.592 19.224 -8.698  1.00 40.68  ? 61  TYR A C   1 
ATOM   511  O  O   . TYR A 1 62  ? 31.644 19.017 -9.282  1.00 40.57  ? 61  TYR A O   1 
ATOM   512  C  CB  . TYR A 1 62  ? 30.911 21.514 -7.776  1.00 40.74  ? 61  TYR A CB  1 
ATOM   513  C  CG  . TYR A 1 62  ? 29.961 22.187 -8.753  1.00 40.89  ? 61  TYR A CG  1 
ATOM   514  C  CD1 . TYR A 1 62  ? 28.707 22.628 -8.342  1.00 41.21  ? 61  TYR A CD1 1 
ATOM   515  C  CD2 . TYR A 1 62  ? 30.339 22.414 -10.081 1.00 41.63  ? 61  TYR A CD2 1 
ATOM   516  C  CE1 . TYR A 1 62  ? 27.844 23.268 -9.236  1.00 41.81  ? 61  TYR A CE1 1 
ATOM   517  C  CE2 . TYR A 1 62  ? 29.494 23.059 -10.980 1.00 41.55  ? 61  TYR A CE2 1 
ATOM   518  C  CZ  . TYR A 1 62  ? 28.250 23.475 -10.550 1.00 43.16  ? 61  TYR A CZ  1 
ATOM   519  O  OH  . TYR A 1 62  ? 27.397 24.104 -11.438 1.00 44.00  ? 61  TYR A OH  1 
ATOM   520  N  N   . SER A 1 63  ? 29.425 18.766 -9.145  1.00 40.20  ? 62  SER A N   1 
ATOM   521  C  CA  . SER A 1 63  ? 29.340 17.968 -10.369 1.00 40.61  ? 62  SER A CA  1 
ATOM   522  C  C   . SER A 1 63  ? 28.790 18.735 -11.564 1.00 40.51  ? 62  SER A C   1 
ATOM   523  O  O   . SER A 1 63  ? 28.930 18.282 -12.693 1.00 40.93  ? 62  SER A O   1 
ATOM   524  C  CB  . SER A 1 63  ? 28.495 16.702 -10.156 1.00 40.73  ? 62  SER A CB  1 
ATOM   525  O  OG  . SER A 1 63  ? 27.113 17.021 -10.065 1.00 41.83  ? 62  SER A OG  1 
ATOM   526  N  N   . GLY A 1 64  ? 28.152 19.878 -11.334 1.00 39.54  ? 63  GLY A N   1 
ATOM   527  C  CA  . GLY A 1 64  ? 27.447 20.568 -12.412 1.00 39.01  ? 63  GLY A CA  1 
ATOM   528  C  C   . GLY A 1 64  ? 26.019 20.057 -12.603 1.00 38.28  ? 63  GLY A C   1 
ATOM   529  O  O   . GLY A 1 64  ? 25.303 20.507 -13.499 1.00 39.18  ? 63  GLY A O   1 
ATOM   530  N  N   . ARG A 1 65  ? 25.585 19.134 -11.759 1.00 36.28  ? 64  ARG A N   1 
ATOM   531  C  CA  . ARG A 1 65  ? 24.235 18.589 -11.900 1.00 35.39  ? 64  ARG A CA  1 
ATOM   532  C  C   . ARG A 1 65  ? 23.293 19.061 -10.786 1.00 35.07  ? 64  ARG A C   1 
ATOM   533  O  O   . ARG A 1 65  ? 22.129 18.672 -10.744 1.00 33.86  ? 64  ARG A O   1 
ATOM   534  C  CB  . ARG A 1 65  ? 24.300 17.060 -11.943 1.00 34.95  ? 64  ARG A CB  1 
ATOM   535  C  CG  . ARG A 1 65  ? 25.032 16.539 -13.190 1.00 35.41  ? 64  ARG A CG  1 
ATOM   536  C  CD  . ARG A 1 65  ? 25.204 14.997 -13.158 1.00 36.90  ? 64  ARG A CD  1 
ATOM   537  N  NE  . ARG A 1 65  ? 26.207 14.579 -12.177 1.00 37.72  ? 64  ARG A NE  1 
ATOM   538  C  CZ  . ARG A 1 65  ? 25.955 13.820 -11.113 1.00 40.20  ? 64  ARG A CZ  1 
ATOM   539  N  NH1 . ARG A 1 65  ? 24.717 13.409 -10.854 1.00 40.85  ? 64  ARG A NH1 1 
ATOM   540  N  NH2 . ARG A 1 65  ? 26.937 13.504 -10.284 1.00 40.61  ? 64  ARG A NH2 1 
ATOM   541  N  N   . GLU A 1 66  ? 23.803 19.918 -9.901  1.00 34.85  ? 65  GLU A N   1 
ATOM   542  C  CA  . GLU A 1 66  ? 23.045 20.344 -8.717  1.00 34.93  ? 65  GLU A CA  1 
ATOM   543  C  C   . GLU A 1 66  ? 22.250 21.638 -8.904  1.00 35.39  ? 65  GLU A C   1 
ATOM   544  O  O   . GLU A 1 66  ? 22.632 22.522 -9.702  1.00 34.74  ? 65  GLU A O   1 
ATOM   545  C  CB  . GLU A 1 66  ? 23.946 20.438 -7.454  1.00 35.99  ? 65  GLU A CB  1 
ATOM   546  C  CG  A GLU A 1 66  ? 24.802 19.201 -7.127  0.50 32.51  ? 65  GLU A CG  1 
ATOM   547  C  CG  B GLU A 1 66  ? 25.282 21.104 -7.604  0.50 38.10  ? 65  GLU A CG  1 
ATOM   548  C  CD  A GLU A 1 66  ? 26.096 19.101 -7.932  0.50 35.58  ? 65  GLU A CD  1 
ATOM   549  C  CD  B GLU A 1 66  ? 26.293 20.244 -8.326  0.50 40.56  ? 65  GLU A CD  1 
ATOM   550  O  OE1 A GLU A 1 66  ? 26.374 19.998 -8.758  0.50 36.17  ? 65  GLU A OE1 1 
ATOM   551  O  OE1 B GLU A 1 66  ? 26.901 19.333 -7.717  0.50 40.74  ? 65  GLU A OE1 1 
ATOM   552  O  OE2 A GLU A 1 66  ? 26.849 18.115 -7.747  0.50 34.36  ? 65  GLU A OE2 1 
ATOM   553  O  OE2 B GLU A 1 66  ? 26.485 20.511 -9.519  0.50 41.54  ? 65  GLU A OE2 1 
ATOM   554  N  N   . ILE A 1 67  ? 21.117 21.733 -8.203  1.00 33.69  ? 66  ILE A N   1 
ATOM   555  C  CA  . ILE A 1 67  ? 20.382 22.989 -8.114  1.00 32.94  ? 66  ILE A CA  1 
ATOM   556  C  C   . ILE A 1 67  ? 20.070 23.233 -6.655  1.00 32.81  ? 66  ILE A C   1 
ATOM   557  O  O   . ILE A 1 67  ? 19.454 22.367 -6.010  1.00 32.70  ? 66  ILE A O   1 
ATOM   558  C  CB  . ILE A 1 67  ? 19.030 22.959 -8.887  1.00 32.68  ? 66  ILE A CB  1 
ATOM   559  C  CG1 . ILE A 1 67  ? 19.246 22.627 -10.360 1.00 32.35  ? 66  ILE A CG1 1 
ATOM   560  C  CG2 . ILE A 1 67  ? 18.303 24.327 -8.738  1.00 31.87  ? 66  ILE A CG2 1 
ATOM   561  C  CD1 . ILE A 1 67  ? 17.979 22.467 -11.142 1.00 33.22  ? 66  ILE A CD1 1 
ATOM   562  N  N   . ILE A 1 68  ? 20.488 24.388 -6.136  1.00 31.41  ? 67  ILE A N   1 
ATOM   563  C  CA  . ILE A 1 68  ? 20.175 24.761 -4.760  1.00 31.32  ? 67  ILE A CA  1 
ATOM   564  C  C   . ILE A 1 68  ? 18.963 25.702 -4.695  1.00 31.98  ? 67  ILE A C   1 
ATOM   565  O  O   . ILE A 1 68  ? 18.808 26.571 -5.552  1.00 31.38  ? 67  ILE A O   1 
ATOM   566  C  CB  . ILE A 1 68  ? 21.407 25.359 -4.022  1.00 31.79  ? 67  ILE A CB  1 
ATOM   567  C  CG1 . ILE A 1 68  ? 21.067 25.687 -2.565  1.00 31.17  ? 67  ILE A CG1 1 
ATOM   568  C  CG2 . ILE A 1 68  ? 21.930 26.659 -4.714  1.00 31.28  ? 67  ILE A CG2 1 
ATOM   569  C  CD1 A ILE A 1 68  ? 20.979 24.548 -1.666  0.50 26.98  ? 67  ILE A CD1 1 
ATOM   570  C  CD1 B ILE A 1 68  ? 22.169 25.363 -1.603  0.50 26.29  ? 67  ILE A CD1 1 
ATOM   571  N  N   . TYR A 1 69  ? 18.112 25.535 -3.671  1.00 31.69  ? 68  TYR A N   1 
ATOM   572  C  CA  . TYR A 1 69  ? 16.896 26.337 -3.539  1.00 31.40  ? 68  TYR A CA  1 
ATOM   573  C  C   . TYR A 1 69  ? 17.029 27.338 -2.388  1.00 30.81  ? 68  TYR A C   1 
ATOM   574  O  O   . TYR A 1 69  ? 17.891 27.166 -1.507  1.00 31.11  ? 68  TYR A O   1 
ATOM   575  C  CB  . TYR A 1 69  ? 15.660 25.415 -3.355  1.00 32.39  ? 68  TYR A CB  1 
ATOM   576  C  CG  . TYR A 1 69  ? 15.418 24.622 -4.628  1.00 32.65  ? 68  TYR A CG  1 
ATOM   577  C  CD1 . TYR A 1 69  ? 14.651 25.151 -5.652  1.00 31.64  ? 68  TYR A CD1 1 
ATOM   578  C  CD2 . TYR A 1 69  ? 16.035 23.388 -4.830  1.00 33.58  ? 68  TYR A CD2 1 
ATOM   579  C  CE1 . TYR A 1 69  ? 14.470 24.451 -6.863  1.00 32.87  ? 68  TYR A CE1 1 
ATOM   580  C  CE2 . TYR A 1 69  ? 15.863 22.660 -6.046  1.00 31.90  ? 68  TYR A CE2 1 
ATOM   581  C  CZ  . TYR A 1 69  ? 15.068 23.205 -7.043  1.00 32.72  ? 68  TYR A CZ  1 
ATOM   582  O  OH  . TYR A 1 69  ? 14.875 22.521 -8.238  1.00 34.69  ? 68  TYR A OH  1 
ATOM   583  N  N   . PRO A 1 70  ? 16.203 28.398 -2.397  1.00 30.42  ? 69  PRO A N   1 
ATOM   584  C  CA  . PRO A 1 70  ? 16.326 29.439 -1.369  1.00 30.21  ? 69  PRO A CA  1 
ATOM   585  C  C   . PRO A 1 70  ? 16.134 28.954 0.061   1.00 30.21  ? 69  PRO A C   1 
ATOM   586  O  O   . PRO A 1 70  ? 16.605 29.620 0.992   1.00 31.07  ? 69  PRO A O   1 
ATOM   587  C  CB  . PRO A 1 70  ? 15.206 30.429 -1.738  1.00 30.45  ? 69  PRO A CB  1 
ATOM   588  C  CG  . PRO A 1 70  ? 15.024 30.242 -3.198  1.00 30.87  ? 69  PRO A CG  1 
ATOM   589  C  CD  . PRO A 1 70  ? 15.134 28.741 -3.366  1.00 30.52  ? 69  PRO A CD  1 
ATOM   590  N  N   . ASN A 1 71  ? 15.431 27.827 0.238   1.00 30.66  ? 70  ASN A N   1 
ATOM   591  C  CA  . ASN A 1 71  ? 15.211 27.230 1.563   1.00 30.40  ? 70  ASN A CA  1 
ATOM   592  C  C   . ASN A 1 71  ? 16.208 26.103 1.886   1.00 30.47  ? 70  ASN A C   1 
ATOM   593  O  O   . ASN A 1 71  ? 15.986 25.301 2.812   1.00 30.56  ? 70  ASN A O   1 
ATOM   594  C  CB  . ASN A 1 71  ? 13.751 26.752 1.694   1.00 31.53  ? 70  ASN A CB  1 
ATOM   595  C  CG  . ASN A 1 71  ? 13.435 25.514 0.828   1.00 33.85  ? 70  ASN A CG  1 
ATOM   596  O  OD1 . ASN A 1 71  ? 14.275 25.041 0.053   1.00 34.70  ? 70  ASN A OD1 1 
ATOM   597  N  ND2 . ASN A 1 71  ? 12.195 25.001 0.951   1.00 34.30  ? 70  ASN A ND2 1 
ATOM   598  N  N   . ALA A 1 72  ? 17.301 26.065 1.113   1.00 29.52  ? 71  ALA A N   1 
ATOM   599  C  CA  . ALA A 1 72  ? 18.468 25.177 1.295   1.00 29.67  ? 71  ALA A CA  1 
ATOM   600  C  C   . ALA A 1 72  ? 18.323 23.782 0.689   1.00 29.83  ? 71  ALA A C   1 
ATOM   601  O  O   . ALA A 1 72  ? 19.299 23.040 0.656   1.00 28.87  ? 71  ALA A O   1 
ATOM   602  C  CB  . ALA A 1 72  ? 18.936 25.085 2.754   1.00 29.86  ? 71  ALA A CB  1 
ATOM   603  N  N   . SER A 1 73  ? 17.127 23.444 0.195   1.00 29.89  ? 72  SER A N   1 
ATOM   604  C  CA  . SER A 1 73  ? 16.904 22.125 -0.413  1.00 30.21  ? 72  SER A CA  1 
ATOM   605  C  C   . SER A 1 73  ? 17.806 21.982 -1.622  1.00 31.10  ? 72  SER A C   1 
ATOM   606  O  O   . SER A 1 73  ? 18.050 22.983 -2.320  1.00 31.31  ? 72  SER A O   1 
ATOM   607  C  CB  . SER A 1 73  ? 15.444 21.962 -0.828  1.00 30.63  ? 72  SER A CB  1 
ATOM   608  O  OG  . SER A 1 73  ? 14.611 21.917 0.331   1.00 31.37  ? 72  SER A OG  1 
ATOM   609  N  N   . LEU A 1 74  ? 18.268 20.760 -1.909  1.00 30.56  ? 73  LEU A N   1 
ATOM   610  C  CA  . LEU A 1 74  ? 19.230 20.548 -2.980  1.00 30.51  ? 73  LEU A CA  1 
ATOM   611  C  C   . LEU A 1 74  ? 18.739 19.443 -3.900  1.00 32.41  ? 73  LEU A C   1 
ATOM   612  O  O   . LEU A 1 74  ? 18.432 18.326 -3.438  1.00 31.61  ? 73  LEU A O   1 
ATOM   613  C  CB  . LEU A 1 74  ? 20.624 20.182 -2.418  1.00 30.93  ? 73  LEU A CB  1 
ATOM   614  C  CG  . LEU A 1 74  ? 21.787 19.993 -3.407  1.00 30.25  ? 73  LEU A CG  1 
ATOM   615  C  CD1 . LEU A 1 74  ? 22.276 21.344 -3.982  1.00 30.40  ? 73  LEU A CD1 1 
ATOM   616  C  CD2 . LEU A 1 74  ? 22.960 19.224 -2.768  1.00 30.68  ? 73  LEU A CD2 1 
ATOM   617  N  N   . LEU A 1 75  ? 18.626 19.769 -5.185  1.00 31.86  ? 74  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 75  ? 18.296 18.763 -6.198  1.00 33.43  ? 74  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 75  ? 19.546 18.334 -6.949  1.00 34.63  ? 74  LEU A C   1 
ATOM   620  O  O   . LEU A 1 75  ? 20.402 19.178 -7.276  1.00 34.68  ? 74  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 75  ? 17.285 19.328 -7.186  1.00 33.58  ? 74  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 75  ? 16.801 18.328 -8.239  1.00 33.77  ? 74  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 75  ? 15.387 18.000 -7.952  1.00 36.06  ? 74  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 75  ? 16.899 18.930 -9.598  1.00 35.73  ? 74  LEU A CD2 1 
ATOM   625  N  N   . ILE A 1 76  ? 19.667 17.030 -7.227  1.00 35.67  ? 75  ILE A N   1 
ATOM   626  C  CA  . ILE A 1 76  ? 20.768 16.500 -8.063  1.00 36.00  ? 75  ILE A CA  1 
ATOM   627  C  C   . ILE A 1 76  ? 20.147 15.758 -9.261  1.00 36.84  ? 75  ILE A C   1 
ATOM   628  O  O   . ILE A 1 76  ? 19.312 14.887 -9.073  1.00 36.53  ? 75  ILE A O   1 
ATOM   629  C  CB  . ILE A 1 76  ? 21.722 15.583 -7.246  1.00 35.95  ? 75  ILE A CB  1 
ATOM   630  C  CG1 . ILE A 1 76  ? 22.208 16.321 -5.986  1.00 36.01  ? 75  ILE A CG1 1 
ATOM   631  C  CG2 . ILE A 1 76  ? 22.948 15.086 -8.091  1.00 36.18  ? 75  ILE A CG2 1 
ATOM   632  C  CD1 . ILE A 1 76  ? 22.917 15.439 -4.956  1.00 37.06  ? 75  ILE A CD1 1 
ATOM   633  N  N   . GLN A 1 77  ? 20.539 16.134 -10.477 1.00 36.66  ? 76  GLN A N   1 
ATOM   634  C  CA  . GLN A 1 77  ? 19.963 15.579 -11.704 1.00 37.97  ? 76  GLN A CA  1 
ATOM   635  C  C   . GLN A 1 77  ? 20.865 14.493 -12.304 1.00 38.31  ? 76  GLN A C   1 
ATOM   636  O  O   . GLN A 1 77  ? 22.038 14.373 -11.930 1.00 37.28  ? 76  GLN A O   1 
ATOM   637  C  CB  . GLN A 1 77  ? 19.805 16.685 -12.755 1.00 37.31  ? 76  GLN A CB  1 
ATOM   638  C  CG  . GLN A 1 77  ? 19.046 17.894 -12.280 1.00 38.84  ? 76  GLN A CG  1 
ATOM   639  C  CD  . GLN A 1 77  ? 19.195 19.056 -13.214 1.00 40.02  ? 76  GLN A CD  1 
ATOM   640  O  OE1 . GLN A 1 77  ? 20.167 19.824 -13.135 1.00 43.63  ? 76  GLN A OE1 1 
ATOM   641  N  NE2 . GLN A 1 77  ? 18.239 19.205 -14.106 1.00 39.62  ? 76  GLN A NE2 1 
ATOM   642  N  N   . ASN A 1 78  ? 20.315 13.737 -13.267 1.00 39.56  ? 77  ASN A N   1 
ATOM   643  C  CA  . ASN A 1 78  ? 21.105 12.772 -14.046 1.00 40.78  ? 77  ASN A CA  1 
ATOM   644  C  C   . ASN A 1 78  ? 21.975 11.956 -13.109 1.00 41.02  ? 77  ASN A C   1 
ATOM   645  O  O   . ASN A 1 78  ? 23.201 11.883 -13.244 1.00 40.92  ? 77  ASN A O   1 
ATOM   646  C  CB  . ASN A 1 78  ? 21.902 13.488 -15.158 1.00 41.49  ? 77  ASN A CB  1 
ATOM   647  C  CG  A ASN A 1 78  ? 22.425 12.520 -16.264 0.50 43.32  ? 77  ASN A CG  1 
ATOM   648  C  CG  B ASN A 1 78  ? 20.990 14.285 -16.108 0.50 42.04  ? 77  ASN A CG  1 
ATOM   649  O  OD1 A ASN A 1 78  ? 21.942 11.388 -16.425 0.50 45.76  ? 77  ASN A OD1 1 
ATOM   650  O  OD1 B ASN A 1 78  ? 20.028 13.744 -16.658 0.50 43.68  ? 77  ASN A OD1 1 
ATOM   651  N  ND2 A ASN A 1 78  ? 23.411 12.985 -17.028 0.50 43.88  ? 77  ASN A ND2 1 
ATOM   652  N  ND2 B ASN A 1 78  ? 21.287 15.576 -16.291 0.50 42.93  ? 77  ASN A ND2 1 
ATOM   653  N  N   . ILE A 1 79  ? 21.300 11.360 -12.128 1.00 41.89  ? 78  ILE A N   1 
ATOM   654  C  CA  . ILE A 1 79  ? 21.934 10.593 -11.056 1.00 42.68  ? 78  ILE A CA  1 
ATOM   655  C  C   . ILE A 1 79  ? 22.742 9.401  -11.593 1.00 44.63  ? 78  ILE A C   1 
ATOM   656  O  O   . ILE A 1 79  ? 22.319 8.738  -12.551 1.00 44.28  ? 78  ILE A O   1 
ATOM   657  C  CB  . ILE A 1 79  ? 20.839 10.123 -10.024 1.00 42.63  ? 78  ILE A CB  1 
ATOM   658  C  CG1 . ILE A 1 79  ? 20.379 11.307 -9.143  1.00 41.31  ? 78  ILE A CG1 1 
ATOM   659  C  CG2 . ILE A 1 79  ? 21.325 8.959  -9.162  1.00 41.69  ? 78  ILE A CG2 1 
ATOM   660  C  CD1 . ILE A 1 79  ? 21.400 11.724 -8.091  1.00 38.29  ? 78  ILE A CD1 1 
ATOM   661  N  N   . ILE A 1 80  ? 23.902 9.157  -10.980 1.00 45.40  ? 79  ILE A N   1 
ATOM   662  C  CA  . ILE A 1 80  ? 24.684 7.936  -11.206 1.00 47.16  ? 79  ILE A CA  1 
ATOM   663  C  C   . ILE A 1 80  ? 24.838 7.186  -9.872  1.00 47.59  ? 79  ILE A C   1 
ATOM   664  O  O   . ILE A 1 80  ? 24.607 7.776  -8.805  1.00 46.84  ? 79  ILE A O   1 
ATOM   665  C  CB  . ILE A 1 80  ? 26.079 8.254  -11.793 1.00 46.94  ? 79  ILE A CB  1 
ATOM   666  C  CG1 . ILE A 1 80  ? 26.829 9.242  -10.893 1.00 47.46  ? 79  ILE A CG1 1 
ATOM   667  C  CG2 . ILE A 1 80  ? 25.944 8.817  -13.220 1.00 48.20  ? 79  ILE A CG2 1 
ATOM   668  C  CD1 . ILE A 1 80  ? 28.258 9.503  -11.322 1.00 48.66  ? 79  ILE A CD1 1 
ATOM   669  N  N   . GLN A 1 81  ? 25.235 5.909  -9.918  1.00 47.89  ? 80  GLN A N   1 
ATOM   670  C  CA  . GLN A 1 81  ? 25.413 5.117  -8.693  1.00 48.46  ? 80  GLN A CA  1 
ATOM   671  C  C   . GLN A 1 81  ? 26.349 5.750  -7.696  1.00 48.29  ? 80  GLN A C   1 
ATOM   672  O  O   . GLN A 1 81  ? 26.145 5.614  -6.489  1.00 48.68  ? 80  GLN A O   1 
ATOM   673  C  CB  . GLN A 1 81  ? 25.936 3.696  -8.967  1.00 48.64  ? 80  GLN A CB  1 
ATOM   674  C  CG  . GLN A 1 81  ? 24.887 2.619  -8.849  1.00 50.57  ? 80  GLN A CG  1 
ATOM   675  C  CD  . GLN A 1 81  ? 24.352 2.372  -7.447  1.00 51.58  ? 80  GLN A CD  1 
ATOM   676  O  OE1 . GLN A 1 81  ? 25.084 2.385  -6.452  1.00 53.96  ? 80  GLN A OE1 1 
ATOM   677  N  NE2 . GLN A 1 81  ? 23.062 2.104  -7.372  1.00 50.95  ? 80  GLN A NE2 1 
ATOM   678  N  N   . ASN A 1 82  ? 27.388 6.405  -8.199  1.00 48.14  ? 81  ASN A N   1 
ATOM   679  C  CA  . ASN A 1 82  ? 28.377 7.036  -7.338  1.00 48.40  ? 81  ASN A CA  1 
ATOM   680  C  C   . ASN A 1 82  ? 27.796 8.149  -6.457  1.00 47.43  ? 81  ASN A C   1 
ATOM   681  O  O   . ASN A 1 82  ? 28.393 8.512  -5.426  1.00 47.58  ? 81  ASN A O   1 
ATOM   682  C  CB  . ASN A 1 82  ? 29.529 7.592  -8.163  1.00 48.80  ? 81  ASN A CB  1 
ATOM   683  C  CG  . ASN A 1 82  ? 30.767 7.820  -7.331  1.00 52.99  ? 81  ASN A CG  1 
ATOM   684  O  OD1 . ASN A 1 82  ? 31.247 6.904  -6.645  1.00 57.03  ? 81  ASN A OD1 1 
ATOM   685  N  ND2 . ASN A 1 82  ? 31.293 9.046  -7.365  1.00 55.36  ? 81  ASN A ND2 1 
ATOM   686  N  N   . ASP A 1 83  ? 26.648 8.686  -6.875  1.00 45.98  ? 82  ASP A N   1 
ATOM   687  C  CA  . ASP A 1 83  ? 25.918 9.708  -6.106  1.00 45.16  ? 82  ASP A CA  1 
ATOM   688  C  C   . ASP A 1 83  ? 25.315 9.167  -4.806  1.00 44.30  ? 82  ASP A C   1 
ATOM   689  O  O   . ASP A 1 83  ? 25.096 9.934  -3.860  1.00 44.73  ? 82  ASP A O   1 
ATOM   690  C  CB  . ASP A 1 83  ? 24.806 10.345 -6.946  1.00 44.07  ? 82  ASP A CB  1 
ATOM   691  C  CG  . ASP A 1 83  ? 25.334 11.166 -8.111  1.00 43.98  ? 82  ASP A CG  1 
ATOM   692  O  OD1 . ASP A 1 83  ? 26.455 11.721 -8.042  1.00 41.37  ? 82  ASP A OD1 1 
ATOM   693  O  OD2 . ASP A 1 83  ? 24.598 11.269 -9.116  1.00 43.32  ? 82  ASP A OD2 1 
ATOM   694  N  N   . ALA A 1 84  ? 25.032 7.864  -4.756  1.00 43.34  ? 83  ALA A N   1 
ATOM   695  C  CA  . ALA A 1 84  ? 24.451 7.254  -3.554  1.00 42.51  ? 83  ALA A CA  1 
ATOM   696  C  C   . ALA A 1 84  ? 25.322 7.518  -2.324  1.00 41.79  ? 83  ALA A C   1 
ATOM   697  O  O   . ALA A 1 84  ? 26.548 7.581  -2.432  1.00 41.76  ? 83  ALA A O   1 
ATOM   698  C  CB  . ALA A 1 84  ? 24.248 5.751  -3.734  1.00 42.72  ? 83  ALA A CB  1 
ATOM   699  N  N   . GLY A 1 85  ? 24.676 7.694  -1.171  1.00 40.69  ? 84  GLY A N   1 
ATOM   700  C  CA  . GLY A 1 85  ? 25.395 7.888  0.082   1.00 39.69  ? 84  GLY A CA  1 
ATOM   701  C  C   . GLY A 1 85  ? 24.779 9.000  0.915   1.00 39.00  ? 84  GLY A C   1 
ATOM   702  O  O   . GLY A 1 85  ? 23.611 9.366  0.728   1.00 38.61  ? 84  GLY A O   1 
ATOM   703  N  N   . PHE A 1 86  ? 25.587 9.527  1.825   1.00 38.07  ? 85  PHE A N   1 
ATOM   704  C  CA  . PHE A 1 86  ? 25.162 10.570 2.761   1.00 37.93  ? 85  PHE A CA  1 
ATOM   705  C  C   . PHE A 1 86  ? 25.517 11.963 2.229   1.00 36.61  ? 85  PHE A C   1 
ATOM   706  O  O   . PHE A 1 86  ? 26.548 12.147 1.551   1.00 35.73  ? 85  PHE A O   1 
ATOM   707  C  CB  . PHE A 1 86  ? 25.838 10.362 4.122   1.00 38.12  ? 85  PHE A CB  1 
ATOM   708  C  CG  . PHE A 1 86  ? 25.405 9.094  4.840   1.00 38.96  ? 85  PHE A CG  1 
ATOM   709  C  CD1 . PHE A 1 86  ? 26.194 7.939  4.777   1.00 42.80  ? 85  PHE A CD1 1 
ATOM   710  C  CD2 . PHE A 1 86  ? 24.230 9.066  5.590   1.00 40.86  ? 85  PHE A CD2 1 
ATOM   711  C  CE1 . PHE A 1 86  ? 25.806 6.764  5.439   1.00 42.69  ? 85  PHE A CE1 1 
ATOM   712  C  CE2 . PHE A 1 86  ? 23.820 7.902  6.265   1.00 41.83  ? 85  PHE A CE2 1 
ATOM   713  C  CZ  . PHE A 1 86  ? 24.612 6.745  6.186   1.00 42.10  ? 85  PHE A CZ  1 
ATOM   714  N  N   . TYR A 1 87  ? 24.665 12.931 2.583   1.00 35.77  ? 86  TYR A N   1 
ATOM   715  C  CA  . TYR A 1 87  ? 24.852 14.337 2.233   1.00 34.51  ? 86  TYR A CA  1 
ATOM   716  C  C   . TYR A 1 87  ? 24.604 15.180 3.485   1.00 33.77  ? 86  TYR A C   1 
ATOM   717  O  O   . TYR A 1 87  ? 23.641 14.944 4.197   1.00 34.60  ? 86  TYR A O   1 
ATOM   718  C  CB  . TYR A 1 87  ? 23.852 14.733 1.148   1.00 34.67  ? 86  TYR A CB  1 
ATOM   719  C  CG  . TYR A 1 87  ? 24.195 14.140 -0.198  1.00 36.13  ? 86  TYR A CG  1 
ATOM   720  C  CD1 . TYR A 1 87  ? 23.876 12.811 -0.496  1.00 37.13  ? 86  TYR A CD1 1 
ATOM   721  C  CD2 . TYR A 1 87  ? 24.856 14.905 -1.175  1.00 35.50  ? 86  TYR A CD2 1 
ATOM   722  C  CE1 . TYR A 1 87  ? 24.220 12.249 -1.728  1.00 36.52  ? 86  TYR A CE1 1 
ATOM   723  C  CE2 . TYR A 1 87  ? 25.198 14.354 -2.408  1.00 38.06  ? 86  TYR A CE2 1 
ATOM   724  C  CZ  . TYR A 1 87  ? 24.878 13.024 -2.678  1.00 37.75  ? 86  TYR A CZ  1 
ATOM   725  O  OH  . TYR A 1 87  ? 25.203 12.477 -3.912  1.00 38.69  ? 86  TYR A OH  1 
ATOM   726  N  N   . THR A 1 88  ? 25.475 16.142 3.744   1.00 33.10  ? 87  THR A N   1 
ATOM   727  C  CA  . THR A 1 88  ? 25.391 16.941 4.957   1.00 32.79  ? 87  THR A CA  1 
ATOM   728  C  C   . THR A 1 88  ? 25.257 18.418 4.591   1.00 32.48  ? 87  THR A C   1 
ATOM   729  O  O   . THR A 1 88  ? 26.001 18.930 3.742   1.00 33.18  ? 87  THR A O   1 
ATOM   730  C  CB  . THR A 1 88  ? 26.629 16.675 5.850   1.00 33.48  ? 87  THR A CB  1 
ATOM   731  O  OG1 . THR A 1 88  ? 26.557 15.328 6.350   1.00 34.89  ? 87  THR A OG1 1 
ATOM   732  C  CG2 . THR A 1 88  ? 26.696 17.642 7.065   1.00 33.37  ? 87  THR A CG2 1 
ATOM   733  N  N   . LEU A 1 89  ? 24.317 19.092 5.252   1.00 32.22  ? 88  LEU A N   1 
ATOM   734  C  CA  . LEU A 1 89  ? 24.097 20.531 5.112   1.00 31.06  ? 88  LEU A CA  1 
ATOM   735  C  C   . LEU A 1 89  ? 24.624 21.250 6.361   1.00 31.26  ? 88  LEU A C   1 
ATOM   736  O  O   . LEU A 1 89  ? 24.304 20.843 7.470   1.00 31.05  ? 88  LEU A O   1 
ATOM   737  C  CB  . LEU A 1 89  ? 22.580 20.793 5.017   1.00 30.63  ? 88  LEU A CB  1 
ATOM   738  C  CG  . LEU A 1 89  ? 22.111 22.253 5.163   1.00 31.45  ? 88  LEU A CG  1 
ATOM   739  C  CD1 . LEU A 1 89  ? 22.702 23.160 4.059   1.00 28.70  ? 88  LEU A CD1 1 
ATOM   740  C  CD2 . LEU A 1 89  ? 20.602 22.362 5.157   1.00 29.87  ? 88  LEU A CD2 1 
ATOM   741  N  N   . HIS A 1 90  ? 25.410 22.314 6.172   1.00 30.38  ? 89  HIS A N   1 
ATOM   742  C  CA  . HIS A 1 90  ? 25.783 23.239 7.253   1.00 30.38  ? 89  HIS A CA  1 
ATOM   743  C  C   . HIS A 1 90  ? 25.083 24.586 6.991   1.00 30.52  ? 89  HIS A C   1 
ATOM   744  O  O   . HIS A 1 90  ? 25.260 25.172 5.908   1.00 30.62  ? 89  HIS A O   1 
ATOM   745  C  CB  . HIS A 1 90  ? 27.302 23.435 7.258   1.00 29.99  ? 89  HIS A CB  1 
ATOM   746  C  CG  . HIS A 1 90  ? 27.877 23.828 8.586   1.00 30.57  ? 89  HIS A CG  1 
ATOM   747  N  ND1 . HIS A 1 90  ? 29.111 24.429 8.699   1.00 29.02  ? 89  HIS A ND1 1 
ATOM   748  C  CD2 . HIS A 1 90  ? 27.400 23.697 9.850   1.00 30.01  ? 89  HIS A CD2 1 
ATOM   749  C  CE1 . HIS A 1 90  ? 29.372 24.657 9.978   1.00 30.24  ? 89  HIS A CE1 1 
ATOM   750  N  NE2 . HIS A 1 90  ? 28.355 24.207 10.700  1.00 30.21  ? 89  HIS A NE2 1 
ATOM   751  N  N   . VAL A 1 91  ? 24.288 25.047 7.956   1.00 30.03  ? 90  VAL A N   1 
ATOM   752  C  CA  . VAL A 1 91  ? 23.592 26.336 7.855   1.00 30.66  ? 90  VAL A CA  1 
ATOM   753  C  C   . VAL A 1 91  ? 24.356 27.361 8.684   1.00 31.40  ? 90  VAL A C   1 
ATOM   754  O  O   . VAL A 1 91  ? 24.537 27.172 9.885   1.00 30.87  ? 90  VAL A O   1 
ATOM   755  C  CB  . VAL A 1 91  ? 22.076 26.272 8.288   1.00 31.05  ? 90  VAL A CB  1 
ATOM   756  C  CG1 A VAL A 1 91  ? 21.450 27.669 8.325   0.50 28.91  ? 90  VAL A CG1 1 
ATOM   757  C  CG1 B VAL A 1 91  ? 21.364 25.078 7.641   0.50 30.44  ? 90  VAL A CG1 1 
ATOM   758  C  CG2 A VAL A 1 91  ? 21.281 25.306 7.400   0.50 30.65  ? 90  VAL A CG2 1 
ATOM   759  C  CG2 B VAL A 1 91  ? 21.914 26.223 9.764   0.50 33.00  ? 90  VAL A CG2 1 
ATOM   760  N  N   . ILE A 1 92  ? 24.844 28.401 8.003   1.00 30.15  ? 91  ILE A N   1 
ATOM   761  C  CA  . ILE A 1 92  ? 25.688 29.426 8.586   1.00 30.76  ? 91  ILE A CA  1 
ATOM   762  C  C   . ILE A 1 92  ? 24.786 30.590 9.009   1.00 31.73  ? 91  ILE A C   1 
ATOM   763  O  O   . ILE A 1 92  ? 24.023 31.137 8.194   1.00 31.20  ? 91  ILE A O   1 
ATOM   764  C  CB  . ILE A 1 92  ? 26.777 29.924 7.579   1.00 30.17  ? 91  ILE A CB  1 
ATOM   765  C  CG1 . ILE A 1 92  ? 27.605 28.751 7.011   1.00 29.25  ? 91  ILE A CG1 1 
ATOM   766  C  CG2 . ILE A 1 92  ? 27.679 31.004 8.216   1.00 29.20  ? 91  ILE A CG2 1 
ATOM   767  C  CD1 . ILE A 1 92  ? 28.236 27.835 8.082   1.00 29.53  ? 91  ILE A CD1 1 
ATOM   768  N  N   . LYS A 1 93  ? 24.861 30.933 10.286  1.00 32.99  ? 92  LYS A N   1 
ATOM   769  C  CA  . LYS A 1 93  ? 24.024 31.980 10.862  1.00 35.10  ? 92  LYS A CA  1 
ATOM   770  C  C   . LYS A 1 93  ? 24.883 33.154 11.303  1.00 35.94  ? 92  LYS A C   1 
ATOM   771  O  O   . LYS A 1 93  ? 26.049 32.974 11.663  1.00 35.82  ? 92  LYS A O   1 
ATOM   772  C  CB  . LYS A 1 93  ? 23.230 31.409 12.047  1.00 34.37  ? 92  LYS A CB  1 
ATOM   773  C  CG  . LYS A 1 93  ? 22.032 30.516 11.607  1.00 37.75  ? 92  LYS A CG  1 
ATOM   774  C  CD  . LYS A 1 93  ? 21.667 29.399 12.615  1.00 37.13  ? 92  LYS A CD  1 
ATOM   775  C  CE  . LYS A 1 93  ? 21.007 29.924 13.877  1.00 41.26  ? 92  LYS A CE  1 
ATOM   776  N  NZ  . LYS A 1 93  ? 20.894 28.793 14.880  1.00 41.30  ? 92  LYS A NZ  1 
ATOM   777  N  N   . SER A 1 94  ? 24.290 34.351 11.317  1.00 36.51  ? 93  SER A N   1 
ATOM   778  C  CA  . SER A 1 94  ? 24.971 35.578 11.791  1.00 37.20  ? 93  SER A CA  1 
ATOM   779  C  C   . SER A 1 94  ? 25.437 35.512 13.242  1.00 37.20  ? 93  SER A C   1 
ATOM   780  O  O   . SER A 1 94  ? 26.348 36.240 13.628  1.00 38.26  ? 93  SER A O   1 
ATOM   781  C  CB  . SER A 1 94  ? 24.035 36.789 11.627  1.00 38.17  ? 93  SER A CB  1 
ATOM   782  O  OG  A SER A 1 94  ? 23.336 36.703 10.393  0.50 38.98  ? 93  SER A OG  1 
ATOM   783  O  OG  B SER A 1 94  ? 22.909 36.657 12.474  0.50 35.80  ? 93  SER A OG  1 
ATOM   784  N  N   . ASP A 1 95  ? 24.807 34.670 14.059  1.00 36.35  ? 94  ASP A N   1 
ATOM   785  C  CA  . ASP A 1 95  ? 25.221 34.521 15.448  1.00 36.25  ? 94  ASP A CA  1 
ATOM   786  C  C   . ASP A 1 95  ? 26.198 33.336 15.614  1.00 36.35  ? 94  ASP A C   1 
ATOM   787  O  O   . ASP A 1 95  ? 26.588 33.015 16.753  1.00 37.45  ? 94  ASP A O   1 
ATOM   788  C  CB  . ASP A 1 95  ? 24.012 34.388 16.395  1.00 36.11  ? 94  ASP A CB  1 
ATOM   789  C  CG  . ASP A 1 95  ? 23.163 33.170 16.100  1.00 39.39  ? 94  ASP A CG  1 
ATOM   790  O  OD1 . ASP A 1 95  ? 22.095 32.974 16.754  1.00 42.34  ? 94  ASP A OD1 1 
ATOM   791  O  OD2 . ASP A 1 95  ? 23.553 32.391 15.205  1.00 38.22  ? 94  ASP A OD2 1 
ATOM   792  N  N   . LEU A 1 96  ? 26.560 32.692 14.489  1.00 35.27  ? 95  LEU A N   1 
ATOM   793  C  CA  . LEU A 1 96  ? 27.514 31.562 14.452  1.00 35.33  ? 95  LEU A CA  1 
ATOM   794  C  C   . LEU A 1 96  ? 27.060 30.369 15.295  1.00 35.04  ? 95  LEU A C   1 
ATOM   795  O  O   . LEU A 1 96  ? 27.870 29.495 15.658  1.00 34.51  ? 95  LEU A O   1 
ATOM   796  C  CB  . LEU A 1 96  ? 28.912 32.038 14.886  1.00 35.21  ? 95  LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 96  ? 30.000 32.359 13.846  1.00 37.85  ? 95  LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 96  ? 29.537 32.544 12.396  1.00 36.09  ? 95  LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 96  ? 30.949 33.449 14.313  1.00 35.27  ? 95  LEU A CD2 1 
ATOM   800  N  N   . VAL A 1 97  ? 25.763 30.321 15.614  1.00 34.61  ? 96  VAL A N   1 
ATOM   801  C  CA  . VAL A 1 97  ? 25.196 29.124 16.202  1.00 34.81  ? 96  VAL A CA  1 
ATOM   802  C  C   . VAL A 1 97  ? 24.780 28.260 15.012  1.00 35.37  ? 96  VAL A C   1 
ATOM   803  O  O   . VAL A 1 97  ? 23.600 28.139 14.700  1.00 36.32  ? 96  VAL A O   1 
ATOM   804  C  CB  . VAL A 1 97  ? 23.991 29.438 17.143  1.00 34.88  ? 96  VAL A CB  1 
ATOM   805  C  CG1 . VAL A 1 97  ? 23.470 28.169 17.767  1.00 35.00  ? 96  VAL A CG1 1 
ATOM   806  C  CG2 . VAL A 1 97  ? 24.422 30.448 18.244  1.00 35.10  ? 96  VAL A CG2 1 
ATOM   807  N  N   . ASN A 1 98  ? 25.767 27.725 14.301  1.00 35.18  ? 97  ASN A N   1 
ATOM   808  C  CA  . ASN A 1 98  ? 25.537 27.083 13.013  1.00 35.19  ? 97  ASN A CA  1 
ATOM   809  C  C   . ASN A 1 98  ? 24.928 25.696 13.211  1.00 36.34  ? 97  ASN A C   1 
ATOM   810  O  O   . ASN A 1 98  ? 25.233 25.043 14.200  1.00 37.24  ? 97  ASN A O   1 
ATOM   811  C  CB  . ASN A 1 98  ? 26.846 27.029 12.238  1.00 34.68  ? 97  ASN A CB  1 
ATOM   812  C  CG  . ASN A 1 98  ? 27.425 28.429 11.979  1.00 33.86  ? 97  ASN A CG  1 
ATOM   813  O  OD1 . ASN A 1 98  ? 26.678 29.416 11.857  1.00 33.49  ? 97  ASN A OD1 1 
ATOM   814  N  ND2 . ASN A 1 98  ? 28.748 28.522 11.900  1.00 31.31  ? 97  ASN A ND2 1 
ATOM   815  N  N   . GLU A 1 99  ? 24.049 25.270 12.299  1.00 35.53  ? 98  GLU A N   1 
ATOM   816  C  CA  . GLU A 1 99  ? 23.333 24.018 12.458  1.00 35.75  ? 98  GLU A CA  1 
ATOM   817  C  C   . GLU A 1 99  ? 23.694 23.058 11.321  1.00 35.18  ? 98  GLU A C   1 
ATOM   818  O  O   . GLU A 1 99  ? 23.966 23.478 10.191  1.00 34.40  ? 98  GLU A O   1 
ATOM   819  C  CB  . GLU A 1 99  ? 21.823 24.273 12.506  1.00 35.28  ? 98  GLU A CB  1 
ATOM   820  C  CG  . GLU A 1 99  ? 21.428 25.184 13.699  1.00 37.32  ? 98  GLU A CG  1 
ATOM   821  C  CD  . GLU A 1 99  ? 19.929 25.405 13.842  1.00 38.53  ? 98  GLU A CD  1 
ATOM   822  O  OE1 . GLU A 1 99  ? 19.565 26.360 14.572  1.00 40.04  ? 98  GLU A OE1 1 
ATOM   823  O  OE2 . GLU A 1 99  ? 19.125 24.638 13.249  1.00 39.44  ? 98  GLU A OE2 1 
ATOM   824  N  N   . GLU A 1 100 ? 23.688 21.772 11.638  1.00 35.34  ? 99  GLU A N   1 
ATOM   825  C  CA  . GLU A 1 100 ? 24.134 20.719 10.727  1.00 35.97  ? 99  GLU A CA  1 
ATOM   826  C  C   . GLU A 1 100 ? 23.055 19.639 10.659  1.00 35.90  ? 99  GLU A C   1 
ATOM   827  O  O   . GLU A 1 100 ? 22.431 19.327 11.676  1.00 35.13  ? 99  GLU A O   1 
ATOM   828  C  CB  . GLU A 1 100 ? 25.393 20.112 11.334  1.00 37.44  ? 99  GLU A CB  1 
ATOM   829  C  CG  . GLU A 1 100 ? 26.155 19.218 10.444  1.00 42.22  ? 99  GLU A CG  1 
ATOM   830  C  CD  . GLU A 1 100 ? 27.215 18.414 11.200  1.00 46.84  ? 99  GLU A CD  1 
ATOM   831  O  OE1 . GLU A 1 100 ? 27.908 18.985 12.096  1.00 44.99  ? 99  GLU A OE1 1 
ATOM   832  O  OE2 . GLU A 1 100 ? 27.334 17.208 10.872  1.00 49.01  ? 99  GLU A OE2 1 
ATOM   833  N  N   . ALA A 1 101 ? 22.815 19.076 9.473   1.00 34.94  ? 100 ALA A N   1 
ATOM   834  C  CA  . ALA A 1 101 ? 21.984 17.879 9.380   1.00 34.57  ? 100 ALA A CA  1 
ATOM   835  C  C   . ALA A 1 101 ? 22.515 17.011 8.271   1.00 34.35  ? 100 ALA A C   1 
ATOM   836  O  O   . ALA A 1 101 ? 23.164 17.500 7.359   1.00 32.23  ? 100 ALA A O   1 
ATOM   837  C  CB  . ALA A 1 101 ? 20.524 18.216 9.122   1.00 34.11  ? 100 ALA A CB  1 
ATOM   838  N  N   . THR A 1 102 ? 22.180 15.729 8.348   1.00 34.89  ? 101 THR A N   1 
ATOM   839  C  CA  . THR A 1 102 ? 22.632 14.754 7.366   1.00 35.53  ? 101 THR A CA  1 
ATOM   840  C  C   . THR A 1 102 ? 21.437 13.952 6.856   1.00 36.38  ? 101 THR A C   1 
ATOM   841  O  O   . THR A 1 102 ? 20.548 13.588 7.640   1.00 36.55  ? 101 THR A O   1 
ATOM   842  C  CB  . THR A 1 102 ? 23.688 13.819 7.961   1.00 35.76  ? 101 THR A CB  1 
ATOM   843  O  OG1 . THR A 1 102 ? 24.849 14.574 8.304   1.00 34.28  ? 101 THR A OG1 1 
ATOM   844  C  CG2 . THR A 1 102 ? 24.113 12.739 6.932   1.00 36.51  ? 101 THR A CG2 1 
ATOM   845  N  N   . GLY A 1 103 ? 21.402 13.703 5.542   1.00 36.74  ? 102 GLY A N   1 
ATOM   846  C  CA  . GLY A 1 103 ? 20.415 12.798 4.962   1.00 36.58  ? 102 GLY A CA  1 
ATOM   847  C  C   . GLY A 1 103 ? 21.109 11.792 4.050   1.00 37.43  ? 102 GLY A C   1 
ATOM   848  O  O   . GLY A 1 103 ? 22.331 11.813 3.915   1.00 36.67  ? 102 GLY A O   1 
ATOM   849  N  N   . GLN A 1 104 ? 20.331 10.912 3.414   1.00 38.33  ? 103 GLN A N   1 
ATOM   850  C  CA  . GLN A 1 104 ? 20.920 9.937  2.488   1.00 40.00  ? 103 GLN A CA  1 
ATOM   851  C  C   . GLN A 1 104 ? 19.936 9.485  1.421   1.00 38.56  ? 103 GLN A C   1 
ATOM   852  O  O   . GLN A 1 104 ? 18.724 9.646  1.564   1.00 38.24  ? 103 GLN A O   1 
ATOM   853  C  CB  . GLN A 1 104 ? 21.527 8.719  3.230   1.00 40.75  ? 103 GLN A CB  1 
ATOM   854  C  CG  . GLN A 1 104 ? 20.549 7.643  3.621   1.00 43.09  ? 103 GLN A CG  1 
ATOM   855  C  CD  . GLN A 1 104 ? 21.205 6.409  4.292   1.00 43.40  ? 103 GLN A CD  1 
ATOM   856  O  OE1 . GLN A 1 104 ? 20.883 6.096  5.434   1.00 49.51  ? 103 GLN A OE1 1 
ATOM   857  N  NE2 . GLN A 1 104 ? 22.095 5.712  3.582   1.00 46.53  ? 103 GLN A NE2 1 
ATOM   858  N  N   . PHE A 1 105 ? 20.482 8.958  0.329   1.00 38.97  ? 104 PHE A N   1 
ATOM   859  C  CA  . PHE A 1 105 ? 19.660 8.255  -0.649  1.00 39.52  ? 104 PHE A CA  1 
ATOM   860  C  C   . PHE A 1 105 ? 20.436 7.093  -1.281  1.00 40.80  ? 104 PHE A C   1 
ATOM   861  O  O   . PHE A 1 105 ? 21.670 7.017  -1.177  1.00 39.85  ? 104 PHE A O   1 
ATOM   862  C  CB  . PHE A 1 105 ? 19.078 9.200  -1.717  1.00 38.84  ? 104 PHE A CB  1 
ATOM   863  C  CG  . PHE A 1 105 ? 20.111 9.875  -2.586  1.00 38.81  ? 104 PHE A CG  1 
ATOM   864  C  CD1 . PHE A 1 105 ? 20.603 11.138 -2.255  1.00 39.32  ? 104 PHE A CD1 1 
ATOM   865  C  CD2 . PHE A 1 105 ? 20.566 9.268  -3.754  1.00 39.06  ? 104 PHE A CD2 1 
ATOM   866  C  CE1 . PHE A 1 105 ? 21.548 11.773 -3.067  1.00 38.30  ? 104 PHE A CE1 1 
ATOM   867  C  CE2 . PHE A 1 105 ? 21.510 9.889  -4.574  1.00 38.34  ? 104 PHE A CE2 1 
ATOM   868  C  CZ  . PHE A 1 105 ? 22.004 11.150 -4.227  1.00 38.61  ? 104 PHE A CZ  1 
ATOM   869  N  N   . ARG A 1 106 ? 19.687 6.200  -1.926  1.00 42.40  ? 105 ARG A N   1 
ATOM   870  C  CA  . ARG A 1 106 ? 20.283 5.091  -2.689  1.00 44.44  ? 105 ARG A CA  1 
ATOM   871  C  C   . ARG A 1 106 ? 19.899 5.166  -4.160  1.00 44.73  ? 105 ARG A C   1 
ATOM   872  O  O   . ARG A 1 106 ? 18.915 5.818  -4.534  1.00 44.71  ? 105 ARG A O   1 
ATOM   873  C  CB  . ARG A 1 106 ? 19.880 3.744  -2.070  1.00 45.10  ? 105 ARG A CB  1 
ATOM   874  C  CG  . ARG A 1 106 ? 20.451 3.578  -0.671  1.00 47.62  ? 105 ARG A CG  1 
ATOM   875  C  CD  . ARG A 1 106 ? 19.708 2.560  0.173   1.00 51.10  ? 105 ARG A CD  1 
ATOM   876  N  NE  . ARG A 1 106 ? 20.322 2.503  1.500   1.00 54.48  ? 105 ARG A NE  1 
ATOM   877  C  CZ  . ARG A 1 106 ? 19.675 2.182  2.612   1.00 54.65  ? 105 ARG A CZ  1 
ATOM   878  N  NH1 . ARG A 1 106 ? 18.387 1.872  2.558   1.00 56.52  ? 105 ARG A NH1 1 
ATOM   879  N  NH2 . ARG A 1 106 ? 20.316 2.166  3.778   1.00 54.83  ? 105 ARG A NH2 1 
ATOM   880  N  N   . VAL A 1 107 ? 20.699 4.511  -4.992  1.00 45.35  ? 106 VAL A N   1 
ATOM   881  C  CA  . VAL A 1 107 ? 20.539 4.574  -6.441  1.00 46.61  ? 106 VAL A CA  1 
ATOM   882  C  C   . VAL A 1 107 ? 20.339 3.144  -6.992  1.00 48.09  ? 106 VAL A C   1 
ATOM   883  O  O   . VAL A 1 107 ? 20.937 2.195  -6.486  1.00 47.79  ? 106 VAL A O   1 
ATOM   884  C  CB  . VAL A 1 107 ? 21.770 5.236  -7.087  1.00 46.12  ? 106 VAL A CB  1 
ATOM   885  C  CG1 . VAL A 1 107 ? 21.627 5.317  -8.604  1.00 45.82  ? 106 VAL A CG1 1 
ATOM   886  C  CG2 . VAL A 1 107 ? 21.996 6.651  -6.492  1.00 45.78  ? 106 VAL A CG2 1 
ATOM   887  N  N   . TYR A 1 108 ? 19.482 2.994  -7.994  1.00 49.55  ? 107 TYR A N   1 
ATOM   888  C  CA  . TYR A 1 108 ? 19.370 1.709  -8.696  1.00 51.57  ? 107 TYR A CA  1 
ATOM   889  C  C   . TYR A 1 108 ? 19.401 1.898  -10.213 1.00 53.10  ? 107 TYR A C   1 
ATOM   890  O  O   . TYR A 1 108 ? 18.917 2.909  -10.714 1.00 52.72  ? 107 TYR A O   1 
ATOM   891  C  CB  . TYR A 1 108 ? 18.106 0.964  -8.265  1.00 50.76  ? 107 TYR A CB  1 
ATOM   892  C  CG  . TYR A 1 108 ? 16.809 1.685  -8.544  1.00 50.58  ? 107 TYR A CG  1 
ATOM   893  C  CD1 . TYR A 1 108 ? 16.144 1.537  -9.765  1.00 49.35  ? 107 TYR A CD1 1 
ATOM   894  C  CD2 . TYR A 1 108 ? 16.229 2.495  -7.572  1.00 50.22  ? 107 TYR A CD2 1 
ATOM   895  C  CE1 . TYR A 1 108 ? 14.931 2.193  -10.010 1.00 50.13  ? 107 TYR A CE1 1 
ATOM   896  C  CE2 . TYR A 1 108 ? 15.026 3.144  -7.796  1.00 50.16  ? 107 TYR A CE2 1 
ATOM   897  C  CZ  . TYR A 1 108 ? 14.382 2.998  -9.012  1.00 50.42  ? 107 TYR A CZ  1 
ATOM   898  O  OH  . TYR A 1 108 ? 13.195 3.659  -9.209  1.00 50.48  ? 107 TYR A OH  1 
ATOM   899  N  N   . PRO A 1 109 ? 19.972 0.919  -10.950 1.00 55.20  ? 108 PRO A N   1 
ATOM   900  C  CA  . PRO A 1 109 ? 19.996 0.996  -12.412 1.00 56.58  ? 108 PRO A CA  1 
ATOM   901  C  C   . PRO A 1 109 ? 18.625 0.717  -13.017 1.00 58.40  ? 108 PRO A C   1 
ATOM   902  O  O   . PRO A 1 109 ? 17.780 0.095  -12.375 1.00 58.43  ? 108 PRO A O   1 
ATOM   903  C  CB  . PRO A 1 109 ? 20.975 -0.111 -12.796 1.00 56.64  ? 108 PRO A CB  1 
ATOM   904  C  CG  . PRO A 1 109 ? 20.818 -1.129 -11.708 1.00 55.99  ? 108 PRO A CG  1 
ATOM   905  C  CD  . PRO A 1 109 ? 20.627 -0.308 -10.454 1.00 55.18  ? 108 PRO A CD  1 
ATOM   906  N  N   . GLU A 1 110 ? 18.391 1.174  -14.243 1.00 60.93  ? 109 GLU A N   1 
ATOM   907  C  CA  . GLU A 1 110 ? 17.142 0.800  -14.927 1.00 63.38  ? 109 GLU A CA  1 
ATOM   908  C  C   . GLU A 1 110 ? 17.346 -0.039 -16.195 1.00 63.97  ? 109 GLU A C   1 
ATOM   909  O  O   . GLU A 1 110 ? 18.397 0.049  -16.845 1.00 64.81  ? 109 GLU A O   1 
ATOM   910  C  CB  . GLU A 1 110 ? 16.232 2.011  -15.170 1.00 63.52  ? 109 GLU A CB  1 
ATOM   911  C  CG  . GLU A 1 110 ? 15.214 2.206  -14.029 1.00 65.03  ? 109 GLU A CG  1 
ATOM   912  C  CD  . GLU A 1 110 ? 14.171 3.284  -14.300 1.00 65.08  ? 109 GLU A CD  1 
ATOM   913  O  OE1 . GLU A 1 110 ? 13.067 3.194  -13.703 1.00 66.96  ? 109 GLU A OE1 1 
ATOM   914  O  OE2 . GLU A 1 110 ? 14.448 4.220  -15.092 1.00 67.06  ? 109 GLU A OE2 1 
ATOM   915  N  N   . LEU A 1 111 ? 16.347 -0.872 -16.502 0.50 64.59  ? 110 LEU A N   1 
ATOM   916  C  CA  . LEU A 1 111 ? 16.280 -1.656 -17.748 0.50 65.01  ? 110 LEU A CA  1 
ATOM   917  C  C   . LEU A 1 111 ? 17.536 -2.497 -18.020 0.50 65.19  ? 110 LEU A C   1 
ATOM   918  O  O   . LEU A 1 111 ? 18.437 -2.084 -18.760 0.50 65.37  ? 110 LEU A O   1 
ATOM   919  C  CB  . LEU A 1 111 ? 15.949 -0.751 -18.949 0.50 65.07  ? 110 LEU A CB  1 
ATOM   920  C  CG  . LEU A 1 111 ? 14.827 0.282  -18.759 0.50 65.80  ? 110 LEU A CG  1 
ATOM   921  C  CD1 . LEU A 1 111 ? 14.903 1.386  -19.818 0.50 66.48  ? 110 LEU A CD1 1 
ATOM   922  C  CD2 . LEU A 1 111 ? 13.437 -0.362 -18.732 0.50 66.79  ? 110 LEU A CD2 1 
ATOM   923  N  N   . ALA B 1 1   ? 50.080 28.921 0.101   1.00 56.54  ? 0   ALA B N   1 
ATOM   924  C  CA  . ALA B 1 1   ? 50.108 27.472 0.477   1.00 55.82  ? 0   ALA B CA  1 
ATOM   925  C  C   . ALA B 1 1   ? 48.802 27.074 1.181   1.00 54.93  ? 0   ALA B C   1 
ATOM   926  O  O   . ALA B 1 1   ? 47.789 27.773 1.053   1.00 55.82  ? 0   ALA B O   1 
ATOM   927  C  CB  . ALA B 1 1   ? 51.334 27.170 1.352   1.00 56.58  ? 0   ALA B CB  1 
ATOM   928  N  N   . LYS B 1 2   ? 48.794 25.951 1.894   1.00 52.89  ? 1   LYS B N   1 
ATOM   929  C  CA  . LYS B 1 2   ? 47.566 25.536 2.557   1.00 50.78  ? 1   LYS B CA  1 
ATOM   930  C  C   . LYS B 1 2   ? 47.416 26.256 3.898   1.00 49.40  ? 1   LYS B C   1 
ATOM   931  O  O   . LYS B 1 2   ? 48.416 26.670 4.517   1.00 48.84  ? 1   LYS B O   1 
ATOM   932  C  CB  . LYS B 1 2   ? 47.467 24.012 2.700   1.00 50.77  ? 1   LYS B CB  1 
ATOM   933  C  CG  . LYS B 1 2   ? 48.456 23.368 3.667   0.10 50.70  ? 1   LYS B CG  1 
ATOM   934  C  CD  . LYS B 1 2   ? 48.387 21.840 3.554   0.10 50.56  ? 1   LYS B CD  1 
ATOM   935  C  CE  . LYS B 1 2   ? 49.131 21.181 4.754   0.10 50.57  ? 1   LYS B CE  1 
ATOM   936  N  NZ  . LYS B 1 2   ? 48.281 21.091 5.973   0.10 50.43  ? 1   LYS B NZ  1 
ATOM   937  N  N   . LEU B 1 3   ? 46.157 26.442 4.306   1.00 47.19  ? 2   LEU B N   1 
ATOM   938  C  CA  . LEU B 1 3   ? 45.811 26.979 5.622   1.00 44.23  ? 2   LEU B CA  1 
ATOM   939  C  C   . LEU B 1 3   ? 46.434 26.053 6.681   1.00 43.57  ? 2   LEU B C   1 
ATOM   940  O  O   . LEU B 1 3   ? 46.262 24.841 6.600   1.00 43.04  ? 2   LEU B O   1 
ATOM   941  C  CB  . LEU B 1 3   ? 44.288 26.982 5.761   1.00 43.98  ? 2   LEU B CB  1 
ATOM   942  C  CG  . LEU B 1 3   ? 43.685 27.402 7.100   1.00 42.70  ? 2   LEU B CG  1 
ATOM   943  C  CD1 . LEU B 1 3   ? 43.931 28.865 7.324   1.00 40.23  ? 2   LEU B CD1 1 
ATOM   944  C  CD2 . LEU B 1 3   ? 42.183 27.043 7.134   1.00 42.05  ? 2   LEU B CD2 1 
ATOM   945  N  N   . THR B 1 4   ? 47.163 26.619 7.642   1.00 42.65  ? 3   THR B N   1 
ATOM   946  C  CA  . THR B 1 4   ? 47.875 25.813 8.652   1.00 42.73  ? 3   THR B CA  1 
ATOM   947  C  C   . THR B 1 4   ? 47.852 26.487 10.012  1.00 41.94  ? 3   THR B C   1 
ATOM   948  O  O   . THR B 1 4   ? 47.980 27.699 10.101  1.00 42.62  ? 3   THR B O   1 
ATOM   949  C  CB  . THR B 1 4   ? 49.328 25.590 8.318   1.00 42.44  ? 3   THR B CB  1 
ATOM   950  O  OG1 A THR B 1 4   ? 49.412 25.086 6.982   0.50 43.24  ? 3   THR B OG1 1 
ATOM   951  O  OG1 B THR B 1 4   ? 50.010 26.834 8.154   0.50 43.18  ? 3   THR B OG1 1 
ATOM   952  C  CG2 A THR B 1 4   ? 50.021 24.650 9.275   0.50 41.58  ? 3   THR B CG2 1 
ATOM   953  C  CG2 B THR B 1 4   ? 49.450 24.747 7.060   0.50 43.33  ? 3   THR B CG2 1 
ATOM   954  N  N   . ILE B 1 5   ? 47.714 25.677 11.059  1.00 41.81  ? 4   ILE B N   1 
ATOM   955  C  CA  . ILE B 1 5   ? 47.738 26.153 12.433  1.00 41.71  ? 4   ILE B CA  1 
ATOM   956  C  C   . ILE B 1 5   ? 49.108 25.884 13.049  1.00 42.51  ? 4   ILE B C   1 
ATOM   957  O  O   . ILE B 1 5   ? 49.630 24.776 12.907  1.00 42.79  ? 4   ILE B O   1 
ATOM   958  C  CB  . ILE B 1 5   ? 46.674 25.424 13.307  1.00 41.47  ? 4   ILE B CB  1 
ATOM   959  C  CG1 . ILE B 1 5   ? 45.284 25.406 12.623  1.00 40.21  ? 4   ILE B CG1 1 
ATOM   960  C  CG2 . ILE B 1 5   ? 46.624 26.029 14.724  1.00 40.49  ? 4   ILE B CG2 1 
ATOM   961  C  CD1 . ILE B 1 5   ? 44.794 26.773 12.136  1.00 38.05  ? 4   ILE B CD1 1 
ATOM   962  N  N   . GLU B 1 6   ? 49.663 26.886 13.729  1.00 42.65  ? 5   GLU B N   1 
ATOM   963  C  CA  . GLU B 1 6   ? 50.918 26.745 14.469  1.00 44.33  ? 5   GLU B CA  1 
ATOM   964  C  C   . GLU B 1 6   ? 50.738 27.121 15.949  1.00 43.78  ? 5   GLU B C   1 
ATOM   965  O  O   . GLU B 1 6   ? 50.572 28.286 16.285  1.00 42.98  ? 5   GLU B O   1 
ATOM   966  C  CB  . GLU B 1 6   ? 52.003 27.628 13.841  1.00 44.31  ? 5   GLU B CB  1 
ATOM   967  C  CG  . GLU B 1 6   ? 53.411 27.354 14.370  1.00 45.85  ? 5   GLU B CG  1 
ATOM   968  C  CD  . GLU B 1 6   ? 54.388 28.492 14.083  1.00 47.04  ? 5   GLU B CD  1 
ATOM   969  O  OE1 . GLU B 1 6   ? 54.111 29.340 13.201  1.00 49.02  ? 5   GLU B OE1 1 
ATOM   970  O  OE2 . GLU B 1 6   ? 55.437 28.558 14.768  1.00 52.52  ? 5   GLU B OE2 1 
ATOM   971  N  N   . SER B 1 7   ? 50.776 26.115 16.819  1.00 44.18  ? 6   SER B N   1 
ATOM   972  C  CA  . SER B 1 7   ? 50.725 26.303 18.266  1.00 44.30  ? 6   SER B CA  1 
ATOM   973  C  C   . SER B 1 7   ? 51.989 26.988 18.784  1.00 45.31  ? 6   SER B C   1 
ATOM   974  O  O   . SER B 1 7   ? 53.106 26.535 18.480  1.00 44.80  ? 6   SER B O   1 
ATOM   975  C  CB  . SER B 1 7   ? 50.597 24.941 18.927  1.00 44.49  ? 6   SER B CB  1 
ATOM   976  O  OG  A SER B 1 7   ? 49.412 24.297 18.522  0.50 44.33  ? 6   SER B OG  1 
ATOM   977  O  OG  B SER B 1 7   ? 49.916 25.050 20.157  0.50 46.60  ? 6   SER B OG  1 
ATOM   978  N  N   . THR B 1 8   ? 51.832 28.068 19.559  1.00 44.83  ? 7   THR B N   1 
ATOM   979  C  CA  . THR B 1 8   ? 52.980 28.733 20.160  1.00 45.88  ? 7   THR B CA  1 
ATOM   980  C  C   . THR B 1 8   ? 52.749 29.050 21.639  1.00 46.10  ? 7   THR B C   1 
ATOM   981  O  O   . THR B 1 8   ? 51.953 29.930 21.954  1.00 45.96  ? 7   THR B O   1 
ATOM   982  C  CB  . THR B 1 8   ? 53.419 30.029 19.396  1.00 46.00  ? 7   THR B CB  1 
ATOM   983  O  OG1 . THR B 1 8   ? 52.528 31.105 19.693  1.00 48.26  ? 7   THR B OG1 1 
ATOM   984  C  CG2 . THR B 1 8   ? 53.447 29.817 17.898  1.00 46.86  ? 7   THR B CG2 1 
ATOM   985  N  N   . PRO B 1 9   ? 53.432 28.324 22.556  1.00 46.38  ? 8   PRO B N   1 
ATOM   986  C  CA  . PRO B 1 9   ? 54.319 27.176 22.312  1.00 46.24  ? 8   PRO B CA  1 
ATOM   987  C  C   . PRO B 1 9   ? 53.543 25.896 22.080  1.00 45.81  ? 8   PRO B C   1 
ATOM   988  O  O   . PRO B 1 9   ? 52.356 25.826 22.410  1.00 45.65  ? 8   PRO B O   1 
ATOM   989  C  CB  . PRO B 1 9   ? 55.101 27.057 23.633  1.00 46.57  ? 8   PRO B CB  1 
ATOM   990  C  CG  . PRO B 1 9   ? 54.116 27.532 24.682  1.00 46.94  ? 8   PRO B CG  1 
ATOM   991  C  CD  . PRO B 1 9   ? 53.351 28.656 23.997  1.00 46.42  ? 8   PRO B CD  1 
ATOM   992  N  N   . PHE B 1 10  ? 54.201 24.891 21.511  1.00 45.04  ? 9   PHE B N   1 
ATOM   993  C  CA  . PHE B 1 10  ? 53.579 23.587 21.332  1.00 44.82  ? 9   PHE B CA  1 
ATOM   994  C  C   . PHE B 1 10  ? 53.455 22.844 22.659  1.00 45.26  ? 9   PHE B C   1 
ATOM   995  O  O   . PHE B 1 10  ? 52.506 22.072 22.859  1.00 44.86  ? 9   PHE B O   1 
ATOM   996  C  CB  . PHE B 1 10  ? 54.373 22.753 20.318  1.00 44.55  ? 9   PHE B CB  1 
ATOM   997  C  CG  . PHE B 1 10  ? 53.800 21.384 20.079  1.00 44.82  ? 9   PHE B CG  1 
ATOM   998  C  CD1 . PHE B 1 10  ? 54.279 20.282 20.788  1.00 44.85  ? 9   PHE B CD1 1 
ATOM   999  C  CD2 . PHE B 1 10  ? 52.758 21.191 19.151  1.00 43.68  ? 9   PHE B CD2 1 
ATOM   1000 C  CE1 . PHE B 1 10  ? 53.747 19.008 20.585  1.00 43.44  ? 9   PHE B CE1 1 
ATOM   1001 C  CE2 . PHE B 1 10  ? 52.229 19.921 18.933  1.00 43.28  ? 9   PHE B CE2 1 
ATOM   1002 C  CZ  . PHE B 1 10  ? 52.721 18.822 19.649  1.00 44.85  ? 9   PHE B CZ  1 
ATOM   1003 N  N   . ASN B 1 11  ? 54.439 23.057 23.544  1.00 45.09  ? 10  ASN B N   1 
ATOM   1004 C  CA  . ASN B 1 11  ? 54.488 22.408 24.863  1.00 45.44  ? 10  ASN B CA  1 
ATOM   1005 C  C   . ASN B 1 11  ? 54.208 23.487 25.886  1.00 45.49  ? 10  ASN B C   1 
ATOM   1006 O  O   . ASN B 1 11  ? 55.050 24.352 26.104  1.00 45.81  ? 10  ASN B O   1 
ATOM   1007 C  CB  . ASN B 1 11  ? 55.899 21.812 25.129  1.00 45.39  ? 10  ASN B CB  1 
ATOM   1008 C  CG  . ASN B 1 11  ? 56.250 20.680 24.185  1.00 44.56  ? 10  ASN B CG  1 
ATOM   1009 O  OD1 . ASN B 1 11  ? 57.101 20.825 23.290  1.00 49.30  ? 10  ASN B OD1 1 
ATOM   1010 N  ND2 . ASN B 1 11  ? 55.593 19.553 24.362  1.00 43.86  ? 10  ASN B ND2 1 
ATOM   1011 N  N   . VAL B 1 12  ? 53.021 23.465 26.491  1.00 46.03  ? 11  VAL B N   1 
ATOM   1012 C  CA  . VAL B 1 12  ? 52.600 24.600 27.328  1.00 46.00  ? 11  VAL B CA  1 
ATOM   1013 C  C   . VAL B 1 12  ? 52.649 24.230 28.811  1.00 46.95  ? 11  VAL B C   1 
ATOM   1014 O  O   . VAL B 1 12  ? 52.160 23.179 29.196  1.00 47.38  ? 11  VAL B O   1 
ATOM   1015 C  CB  . VAL B 1 12  ? 51.167 25.130 26.947  1.00 45.72  ? 11  VAL B CB  1 
ATOM   1016 C  CG1 A VAL B 1 12  ? 50.130 24.075 27.139  0.50 46.14  ? 11  VAL B CG1 1 
ATOM   1017 C  CG1 B VAL B 1 12  ? 50.889 26.466 27.620  0.50 45.16  ? 11  VAL B CG1 1 
ATOM   1018 C  CG2 A VAL B 1 12  ? 50.815 26.367 27.765  0.50 45.26  ? 11  VAL B CG2 1 
ATOM   1019 C  CG2 B VAL B 1 12  ? 50.992 25.215 25.432  0.50 43.78  ? 11  VAL B CG2 1 
ATOM   1020 N  N   . ALA B 1 13  ? 53.234 25.100 29.631  1.00 48.02  ? 12  ALA B N   1 
ATOM   1021 C  CA  . ALA B 1 13  ? 53.206 24.914 31.085  1.00 49.16  ? 12  ALA B CA  1 
ATOM   1022 C  C   . ALA B 1 13  ? 51.821 25.187 31.662  1.00 49.95  ? 12  ALA B C   1 
ATOM   1023 O  O   . ALA B 1 13  ? 51.209 26.220 31.357  1.00 49.84  ? 12  ALA B O   1 
ATOM   1024 C  CB  . ALA B 1 13  ? 54.244 25.825 31.765  1.00 49.30  ? 12  ALA B CB  1 
ATOM   1025 N  N   . GLU B 1 14  ? 51.337 24.271 32.500  1.00 50.27  ? 13  GLU B N   1 
ATOM   1026 C  CA  . GLU B 1 14  ? 50.133 24.507 33.301  1.00 51.39  ? 13  GLU B CA  1 
ATOM   1027 C  C   . GLU B 1 14  ? 50.126 25.936 33.879  1.00 51.05  ? 13  GLU B C   1 
ATOM   1028 O  O   . GLU B 1 14  ? 51.137 26.414 34.421  1.00 51.21  ? 13  GLU B O   1 
ATOM   1029 C  CB  . GLU B 1 14  ? 50.041 23.464 34.418  1.00 51.94  ? 13  GLU B CB  1 
ATOM   1030 C  CG  . GLU B 1 14  ? 48.630 23.023 34.781  1.00 56.75  ? 13  GLU B CG  1 
ATOM   1031 C  CD  . GLU B 1 14  ? 48.551 21.557 35.263  1.00 63.61  ? 13  GLU B CD  1 
ATOM   1032 O  OE1 . GLU B 1 14  ? 47.506 20.890 34.984  1.00 65.87  ? 13  GLU B OE1 1 
ATOM   1033 O  OE2 . GLU B 1 14  ? 49.526 21.074 35.908  1.00 64.43  ? 13  GLU B OE2 1 
ATOM   1034 N  N   . GLY B 1 15  ? 48.998 26.629 33.727  1.00 50.01  ? 14  GLY B N   1 
ATOM   1035 C  CA  . GLY B 1 15  ? 48.848 27.986 34.238  1.00 48.78  ? 14  GLY B CA  1 
ATOM   1036 C  C   . GLY B 1 15  ? 49.374 29.069 33.319  1.00 48.30  ? 14  GLY B C   1 
ATOM   1037 O  O   . GLY B 1 15  ? 49.119 30.256 33.548  1.00 48.59  ? 14  GLY B O   1 
ATOM   1038 N  N   . LYS B 1 16  ? 50.120 28.693 32.283  1.00 47.37  ? 15  LYS B N   1 
ATOM   1039 C  CA  . LYS B 1 16  ? 50.564 29.688 31.303  1.00 47.26  ? 15  LYS B CA  1 
ATOM   1040 C  C   . LYS B 1 16  ? 49.551 29.796 30.124  1.00 46.49  ? 15  LYS B C   1 
ATOM   1041 O  O   . LYS B 1 16  ? 48.413 29.353 30.238  1.00 45.74  ? 15  LYS B O   1 
ATOM   1042 C  CB  . LYS B 1 16  ? 51.998 29.404 30.825  1.00 47.72  ? 15  LYS B CB  1 
ATOM   1043 C  CG  . LYS B 1 16  ? 53.047 29.331 31.974  1.00 51.02  ? 15  LYS B CG  1 
ATOM   1044 C  CD  . LYS B 1 16  ? 53.262 30.708 32.604  1.00 57.11  ? 15  LYS B CD  1 
ATOM   1045 C  CE  . LYS B 1 16  ? 53.893 30.627 33.996  1.00 61.30  ? 15  LYS B CE  1 
ATOM   1046 N  NZ  . LYS B 1 16  ? 53.986 31.988 34.629  1.00 63.10  ? 15  LYS B NZ  1 
ATOM   1047 N  N   . GLU B 1 17  ? 49.976 30.395 29.018  1.00 45.94  ? 16  GLU B N   1 
ATOM   1048 C  CA  . GLU B 1 17  ? 49.079 30.692 27.908  1.00 44.99  ? 16  GLU B CA  1 
ATOM   1049 C  C   . GLU B 1 17  ? 49.549 30.010 26.622  1.00 44.19  ? 16  GLU B C   1 
ATOM   1050 O  O   . GLU B 1 17  ? 50.731 29.655 26.491  1.00 43.64  ? 16  GLU B O   1 
ATOM   1051 C  CB  . GLU B 1 17  ? 49.013 32.211 27.678  1.00 45.32  ? 16  GLU B CB  1 
ATOM   1052 C  CG  A GLU B 1 17  ? 48.921 33.108 28.936  0.50 46.37  ? 16  GLU B CG  1 
ATOM   1053 C  CG  B GLU B 1 17  ? 50.289 32.876 27.186  0.50 45.55  ? 16  GLU B CG  1 
ATOM   1054 C  CD  A GLU B 1 17  ? 50.209 33.150 29.785  0.50 48.30  ? 16  GLU B CD  1 
ATOM   1055 C  CD  B GLU B 1 17  ? 50.079 34.344 26.903  0.50 45.85  ? 16  GLU B CD  1 
ATOM   1056 O  OE1 A GLU B 1 17  ? 51.312 32.918 29.236  0.50 49.38  ? 16  GLU B OE1 1 
ATOM   1057 O  OE1 B GLU B 1 17  ? 49.129 34.926 27.468  0.50 48.10  ? 16  GLU B OE1 1 
ATOM   1058 O  OE2 A GLU B 1 17  ? 50.113 33.417 31.007  0.50 46.93  ? 16  GLU B OE2 1 
ATOM   1059 O  OE2 B GLU B 1 17  ? 50.854 34.926 26.115  0.50 48.12  ? 16  GLU B OE2 1 
ATOM   1060 N  N   . VAL B 1 18  ? 48.639 29.849 25.660  1.00 41.87  ? 17  VAL B N   1 
ATOM   1061 C  CA  . VAL B 1 18  ? 49.023 29.366 24.335  1.00 40.37  ? 17  VAL B CA  1 
ATOM   1062 C  C   . VAL B 1 18  ? 48.395 30.271 23.268  1.00 40.12  ? 17  VAL B C   1 
ATOM   1063 O  O   . VAL B 1 18  ? 47.286 30.785 23.476  1.00 39.03  ? 17  VAL B O   1 
ATOM   1064 C  CB  . VAL B 1 18  ? 48.660 27.873 24.153  1.00 40.58  ? 17  VAL B CB  1 
ATOM   1065 C  CG1 . VAL B 1 18  ? 47.146 27.667 24.065  1.00 40.40  ? 17  VAL B CG1 1 
ATOM   1066 C  CG2 . VAL B 1 18  ? 49.385 27.260 22.943  1.00 38.63  ? 17  VAL B CG2 1 
ATOM   1067 N  N   . LEU B 1 19  ? 49.124 30.514 22.179  1.00 39.26  ? 18  LEU B N   1 
ATOM   1068 C  CA  . LEU B 1 19  ? 48.586 31.230 21.015  1.00 38.89  ? 18  LEU B CA  1 
ATOM   1069 C  C   . LEU B 1 19  ? 48.635 30.317 19.782  1.00 39.61  ? 18  LEU B C   1 
ATOM   1070 O  O   . LEU B 1 19  ? 49.729 29.862 19.376  1.00 39.10  ? 18  LEU B O   1 
ATOM   1071 C  CB  . LEU B 1 19  ? 49.374 32.517 20.760  1.00 38.55  ? 18  LEU B CB  1 
ATOM   1072 C  CG  . LEU B 1 19  ? 48.989 33.395 19.563  1.00 38.90  ? 18  LEU B CG  1 
ATOM   1073 C  CD1 . LEU B 1 19  ? 47.574 33.996 19.751  1.00 35.28  ? 18  LEU B CD1 1 
ATOM   1074 C  CD2 . LEU B 1 19  ? 50.024 34.519 19.403  1.00 39.34  ? 18  LEU B CD2 1 
ATOM   1075 N  N   . LEU B 1 20  ? 47.464 30.046 19.193  1.00 38.44  ? 19  LEU B N   1 
ATOM   1076 C  CA  . LEU B 1 20  ? 47.386 29.262 17.966  1.00 38.89  ? 19  LEU B CA  1 
ATOM   1077 C  C   . LEU B 1 20  ? 47.418 30.201 16.778  1.00 39.59  ? 19  LEU B C   1 
ATOM   1078 O  O   . LEU B 1 20  ? 46.437 30.882 16.489  1.00 38.18  ? 19  LEU B O   1 
ATOM   1079 C  CB  . LEU B 1 20  ? 46.120 28.393 17.929  1.00 38.63  ? 19  LEU B CB  1 
ATOM   1080 C  CG  . LEU B 1 20  ? 45.879 27.527 19.173  1.00 39.21  ? 19  LEU B CG  1 
ATOM   1081 C  CD1 . LEU B 1 20  ? 44.647 26.695 18.974  1.00 36.15  ? 19  LEU B CD1 1 
ATOM   1082 C  CD2 . LEU B 1 20  ? 47.086 26.647 19.483  1.00 39.85  ? 19  LEU B CD2 1 
ATOM   1083 N  N   . LEU B 1 21  ? 48.567 30.245 16.105  1.00 39.70  ? 20  LEU B N   1 
ATOM   1084 C  CA  . LEU B 1 21  ? 48.760 31.073 14.915  1.00 40.87  ? 20  LEU B CA  1 
ATOM   1085 C  C   . LEU B 1 21  ? 48.097 30.456 13.704  1.00 39.48  ? 20  LEU B C   1 
ATOM   1086 O  O   . LEU B 1 21  ? 48.045 29.233 13.572  1.00 39.87  ? 20  LEU B O   1 
ATOM   1087 C  CB  . LEU B 1 21  ? 50.253 31.198 14.625  1.00 41.31  ? 20  LEU B CB  1 
ATOM   1088 C  CG  . LEU B 1 21  ? 51.046 32.420 15.075  1.00 43.85  ? 20  LEU B CG  1 
ATOM   1089 C  CD1 . LEU B 1 21  ? 50.421 33.200 16.186  1.00 45.33  ? 20  LEU B CD1 1 
ATOM   1090 C  CD2 . LEU B 1 21  ? 52.531 32.056 15.373  1.00 43.31  ? 20  LEU B CD2 1 
ATOM   1091 N  N   . VAL B 1 22  ? 47.605 31.308 12.812  1.00 38.56  ? 21  VAL B N   1 
ATOM   1092 C  CA  . VAL B 1 22  ? 46.912 30.846 11.621  1.00 38.35  ? 21  VAL B CA  1 
ATOM   1093 C  C   . VAL B 1 22  ? 47.656 31.368 10.390  1.00 39.42  ? 21  VAL B C   1 
ATOM   1094 O  O   . VAL B 1 22  ? 47.724 32.579 10.162  1.00 40.24  ? 21  VAL B O   1 
ATOM   1095 C  CB  . VAL B 1 22  ? 45.430 31.317 11.608  1.00 37.94  ? 21  VAL B CB  1 
ATOM   1096 C  CG1 . VAL B 1 22  ? 44.709 30.796 10.354  1.00 35.86  ? 21  VAL B CG1 1 
ATOM   1097 C  CG2 . VAL B 1 22  ? 44.720 30.807 12.871  1.00 35.49  ? 21  VAL B CG2 1 
ATOM   1098 N  N   . HIS B 1 23  ? 48.232 30.452 9.621   1.00 40.26  ? 22  HIS B N   1 
ATOM   1099 C  CA  . HIS B 1 23  ? 48.980 30.832 8.413   1.00 41.32  ? 22  HIS B CA  1 
ATOM   1100 C  C   . HIS B 1 23  ? 48.177 30.550 7.151   1.00 41.52  ? 22  HIS B C   1 
ATOM   1101 O  O   . HIS B 1 23  ? 47.487 29.534 7.070   1.00 42.11  ? 22  HIS B O   1 
ATOM   1102 C  CB  . HIS B 1 23  ? 50.321 30.079 8.336   1.00 41.83  ? 22  HIS B CB  1 
ATOM   1103 C  CG  . HIS B 1 23  ? 51.183 30.252 9.549   1.00 41.53  ? 22  HIS B CG  1 
ATOM   1104 N  ND1 . HIS B 1 23  ? 51.744 31.463 9.900   1.00 43.96  ? 22  HIS B ND1 1 
ATOM   1105 C  CD2 . HIS B 1 23  ? 51.569 29.369 10.500  1.00 41.65  ? 22  HIS B CD2 1 
ATOM   1106 C  CE1 . HIS B 1 23  ? 52.432 31.320 11.020  1.00 42.31  ? 22  HIS B CE1 1 
ATOM   1107 N  NE2 . HIS B 1 23  ? 52.343 30.059 11.402  1.00 41.56  ? 22  HIS B NE2 1 
ATOM   1108 N  N   . ASN B 1 24  ? 48.307 31.454 6.174   1.00 42.22  ? 23  ASN B N   1 
ATOM   1109 C  CA  . ASN B 1 24  ? 47.725 31.324 4.839   1.00 42.32  ? 23  ASN B CA  1 
ATOM   1110 C  C   . ASN B 1 24  ? 46.195 31.390 4.810   1.00 41.82  ? 23  ASN B C   1 
ATOM   1111 O  O   . ASN B 1 24  ? 45.546 30.590 4.137   1.00 41.49  ? 23  ASN B O   1 
ATOM   1112 C  CB  . ASN B 1 24  ? 48.249 30.071 4.114   1.00 42.91  ? 23  ASN B CB  1 
ATOM   1113 C  CG  . ASN B 1 24  ? 49.781 30.006 4.082   1.00 45.04  ? 23  ASN B CG  1 
ATOM   1114 O  OD1 . ASN B 1 24  ? 50.360 28.946 4.272   1.00 48.03  ? 23  ASN B OD1 1 
ATOM   1115 N  ND2 . ASN B 1 24  ? 50.427 31.143 3.871   1.00 45.84  ? 23  ASN B ND2 1 
ATOM   1116 N  N   . LEU B 1 25  ? 45.617 32.348 5.533   1.00 41.61  ? 24  LEU B N   1 
ATOM   1117 C  CA  . LEU B 1 25  ? 44.184 32.617 5.403   1.00 41.79  ? 24  LEU B CA  1 
ATOM   1118 C  C   . LEU B 1 25  ? 43.843 32.980 3.965   1.00 42.77  ? 24  LEU B C   1 
ATOM   1119 O  O   . LEU B 1 25  ? 44.575 33.758 3.330   1.00 42.84  ? 24  LEU B O   1 
ATOM   1120 C  CB  . LEU B 1 25  ? 43.767 33.780 6.302   1.00 41.23  ? 24  LEU B CB  1 
ATOM   1121 C  CG  . LEU B 1 25  ? 43.371 33.519 7.741   1.00 41.22  ? 24  LEU B CG  1 
ATOM   1122 C  CD1 . LEU B 1 25  ? 43.020 34.864 8.346   1.00 39.64  ? 24  LEU B CD1 1 
ATOM   1123 C  CD2 . LEU B 1 25  ? 42.193 32.526 7.839   1.00 38.54  ? 24  LEU B CD2 1 
ATOM   1124 N  N   . PRO B 1 26  ? 42.732 32.433 3.436   1.00 43.16  ? 25  PRO B N   1 
ATOM   1125 C  CA  . PRO B 1 26  ? 42.274 32.888 2.127   1.00 43.31  ? 25  PRO B CA  1 
ATOM   1126 C  C   . PRO B 1 26  ? 41.776 34.324 2.206   1.00 43.46  ? 25  PRO B C   1 
ATOM   1127 O  O   . PRO B 1 26  ? 41.555 34.852 3.297   1.00 43.24  ? 25  PRO B O   1 
ATOM   1128 C  CB  . PRO B 1 26  ? 41.097 31.955 1.804   1.00 43.95  ? 25  PRO B CB  1 
ATOM   1129 C  CG  . PRO B 1 26  ? 41.127 30.874 2.826   1.00 43.70  ? 25  PRO B CG  1 
ATOM   1130 C  CD  . PRO B 1 26  ? 41.884 31.367 4.003   1.00 43.17  ? 25  PRO B CD  1 
ATOM   1131 N  N   . GLN B 1 27  ? 41.621 34.960 1.050   1.00 44.16  ? 26  GLN B N   1 
ATOM   1132 C  CA  . GLN B 1 27  ? 41.023 36.284 0.982   1.00 44.85  ? 26  GLN B CA  1 
ATOM   1133 C  C   . GLN B 1 27  ? 39.500 36.161 0.949   1.00 43.84  ? 26  GLN B C   1 
ATOM   1134 O  O   . GLN B 1 27  ? 38.969 35.092 0.634   1.00 44.39  ? 26  GLN B O   1 
ATOM   1135 C  CB  . GLN B 1 27  ? 41.547 37.056 -0.249  1.00 45.37  ? 26  GLN B CB  1 
ATOM   1136 C  CG  A GLN B 1 27  ? 42.572 38.172 0.071   0.50 46.16  ? 26  GLN B CG  1 
ATOM   1137 C  CG  B GLN B 1 27  ? 43.083 37.039 -0.354  0.50 44.91  ? 26  GLN B CG  1 
ATOM   1138 C  CD  A GLN B 1 27  ? 42.538 39.345 -0.927  0.50 46.54  ? 26  GLN B CD  1 
ATOM   1139 C  CD  B GLN B 1 27  ? 43.611 37.801 -1.549  0.50 45.65  ? 26  GLN B CD  1 
ATOM   1140 O  OE1 A GLN B 1 27  ? 42.482 40.515 -0.528  0.50 49.08  ? 26  GLN B OE1 1 
ATOM   1141 O  OE1 B GLN B 1 27  ? 43.231 37.534 -2.693  0.50 47.33  ? 26  GLN B OE1 1 
ATOM   1142 N  NE2 A GLN B 1 27  ? 42.569 39.031 -2.225  0.50 47.85  ? 26  GLN B NE2 1 
ATOM   1143 N  NE2 B GLN B 1 27  ? 44.501 38.757 -1.290  0.50 46.92  ? 26  GLN B NE2 1 
ATOM   1144 N  N   . HIS B 1 28  ? 38.820 37.256 1.286   1.00 42.73  ? 27  HIS B N   1 
ATOM   1145 C  CA  . HIS B 1 28  ? 37.363 37.411 1.158   1.00 41.82  ? 27  HIS B CA  1 
ATOM   1146 C  C   . HIS B 1 28  ? 36.584 36.508 2.116   1.00 39.68  ? 27  HIS B C   1 
ATOM   1147 O  O   . HIS B 1 28  ? 35.963 35.519 1.715   1.00 39.14  ? 27  HIS B O   1 
ATOM   1148 C  CB  . HIS B 1 28  ? 36.908 37.287 -0.314  1.00 42.71  ? 27  HIS B CB  1 
ATOM   1149 C  CG  . HIS B 1 28  ? 37.723 38.124 -1.255  1.00 46.84  ? 27  HIS B CG  1 
ATOM   1150 N  ND1 . HIS B 1 28  ? 38.465 37.584 -2.287  1.00 49.97  ? 27  HIS B ND1 1 
ATOM   1151 C  CD2 . HIS B 1 28  ? 37.958 39.459 -1.279  1.00 48.85  ? 27  HIS B CD2 1 
ATOM   1152 C  CE1 . HIS B 1 28  ? 39.101 38.554 -2.922  1.00 49.14  ? 27  HIS B CE1 1 
ATOM   1153 N  NE2 . HIS B 1 28  ? 38.815 39.699 -2.327  1.00 50.04  ? 27  HIS B NE2 1 
ATOM   1154 N  N   . LEU B 1 29  ? 36.610 36.895 3.383   1.00 37.83  ? 28  LEU B N   1 
ATOM   1155 C  CA  . LEU B 1 29  ? 36.111 36.056 4.465   1.00 36.69  ? 28  LEU B CA  1 
ATOM   1156 C  C   . LEU B 1 29  ? 34.905 36.654 5.161   1.00 35.97  ? 28  LEU B C   1 
ATOM   1157 O  O   . LEU B 1 29  ? 34.788 37.891 5.283   1.00 35.01  ? 28  LEU B O   1 
ATOM   1158 C  CB  . LEU B 1 29  ? 37.231 35.822 5.488   1.00 36.71  ? 28  LEU B CB  1 
ATOM   1159 C  CG  . LEU B 1 29  ? 38.516 35.156 4.974   1.00 37.43  ? 28  LEU B CG  1 
ATOM   1160 C  CD1 . LEU B 1 29  ? 39.497 34.900 6.124   1.00 36.88  ? 28  LEU B CD1 1 
ATOM   1161 C  CD2 . LEU B 1 29  ? 38.246 33.855 4.215   1.00 35.67  ? 28  LEU B CD2 1 
ATOM   1162 N  N   . PHE B 1 30  ? 34.019 35.762 5.627   1.00 34.28  ? 29  PHE B N   1 
ATOM   1163 C  CA  . PHE B 1 30  ? 32.873 36.138 6.439   1.00 32.76  ? 29  PHE B CA  1 
ATOM   1164 C  C   . PHE B 1 30  ? 33.241 36.068 7.918   1.00 32.42  ? 29  PHE B C   1 
ATOM   1165 O  O   . PHE B 1 30  ? 32.888 36.967 8.699   1.00 31.25  ? 29  PHE B O   1 
ATOM   1166 C  CB  . PHE B 1 30  ? 31.660 35.239 6.130   1.00 32.25  ? 29  PHE B CB  1 
ATOM   1167 C  CG  . PHE B 1 30  ? 30.490 35.433 7.061   1.00 32.98  ? 29  PHE B CG  1 
ATOM   1168 C  CD1 . PHE B 1 30  ? 29.602 36.493 6.888   1.00 31.77  ? 29  PHE B CD1 1 
ATOM   1169 C  CD2 . PHE B 1 30  ? 30.261 34.546 8.105   1.00 32.53  ? 29  PHE B CD2 1 
ATOM   1170 C  CE1 . PHE B 1 30  ? 28.509 36.653 7.735   1.00 31.97  ? 29  PHE B CE1 1 
ATOM   1171 C  CE2 . PHE B 1 30  ? 29.169 34.714 8.962   1.00 32.64  ? 29  PHE B CE2 1 
ATOM   1172 C  CZ  . PHE B 1 30  ? 28.295 35.761 8.770   1.00 31.69  ? 29  PHE B CZ  1 
ATOM   1173 N  N   . GLY B 1 31  ? 33.945 35.009 8.317   1.00 31.75  ? 30  GLY B N   1 
ATOM   1174 C  CA  . GLY B 1 31  ? 34.314 34.877 9.724   1.00 31.59  ? 30  GLY B CA  1 
ATOM   1175 C  C   . GLY B 1 31  ? 34.903 33.519 10.055  1.00 31.84  ? 30  GLY B C   1 
ATOM   1176 O  O   . GLY B 1 31  ? 35.260 32.753 9.145   1.00 31.01  ? 30  GLY B O   1 
ATOM   1177 N  N   . TYR B 1 32  ? 35.001 33.228 11.357  1.00 31.20  ? 31  TYR B N   1 
ATOM   1178 C  CA  . TYR B 1 32  ? 35.657 32.001 11.812  1.00 31.88  ? 31  TYR B CA  1 
ATOM   1179 C  C   . TYR B 1 32  ? 35.030 31.434 13.063  1.00 31.58  ? 31  TYR B C   1 
ATOM   1180 O  O   . TYR B 1 32  ? 34.487 32.183 13.874  1.00 31.07  ? 31  TYR B O   1 
ATOM   1181 C  CB  . TYR B 1 32  ? 37.103 32.267 12.222  1.00 32.47  ? 31  TYR B CB  1 
ATOM   1182 C  CG  . TYR B 1 32  ? 37.831 33.422 11.584  1.00 33.63  ? 31  TYR B CG  1 
ATOM   1183 C  CD1 . TYR B 1 32  ? 38.062 34.590 12.295  1.00 32.78  ? 31  TYR B CD1 1 
ATOM   1184 C  CD2 . TYR B 1 32  ? 38.364 33.305 10.304  1.00 33.93  ? 31  TYR B CD2 1 
ATOM   1185 C  CE1 . TYR B 1 32  ? 38.781 35.660 11.723  1.00 34.05  ? 31  TYR B CE1 1 
ATOM   1186 C  CE2 . TYR B 1 32  ? 39.080 34.348 9.736   1.00 34.76  ? 31  TYR B CE2 1 
ATOM   1187 C  CZ  . TYR B 1 32  ? 39.277 35.513 10.438  1.00 33.15  ? 31  TYR B CZ  1 
ATOM   1188 O  OH  . TYR B 1 32  ? 40.009 36.534 9.869   1.00 34.84  ? 31  TYR B OH  1 
ATOM   1189 N  N   . SER B 1 33  ? 35.182 30.126 13.246  1.00 31.29  ? 32  SER B N   1 
ATOM   1190 C  CA  . SER B 1 33  ? 34.855 29.455 14.518  1.00 31.64  ? 32  SER B CA  1 
ATOM   1191 C  C   . SER B 1 33  ? 36.004 28.524 14.913  1.00 31.55  ? 32  SER B C   1 
ATOM   1192 O  O   . SER B 1 33  ? 36.537 27.816 14.056  1.00 31.31  ? 32  SER B O   1 
ATOM   1193 C  CB  . SER B 1 33  ? 33.622 28.582 14.376  1.00 30.98  ? 32  SER B CB  1 
ATOM   1194 O  OG  . SER B 1 33  ? 32.456 29.332 14.168  1.00 32.85  ? 32  SER B OG  1 
ATOM   1195 N  N   . TRP B 1 34  ? 36.371 28.527 16.197  1.00 31.22  ? 33  TRP B N   1 
ATOM   1196 C  CA  . TRP B 1 34  ? 37.267 27.496 16.754  1.00 32.18  ? 33  TRP B CA  1 
ATOM   1197 C  C   . TRP B 1 34  ? 36.483 26.418 17.517  1.00 32.55  ? 33  TRP B C   1 
ATOM   1198 O  O   . TRP B 1 34  ? 35.528 26.741 18.265  1.00 31.53  ? 33  TRP B O   1 
ATOM   1199 C  CB  . TRP B 1 34  ? 38.302 28.124 17.703  1.00 31.89  ? 33  TRP B CB  1 
ATOM   1200 C  CG  . TRP B 1 34  ? 39.471 28.797 17.014  1.00 31.61  ? 33  TRP B CG  1 
ATOM   1201 C  CD1 . TRP B 1 34  ? 39.612 30.119 16.774  1.00 32.25  ? 33  TRP B CD1 1 
ATOM   1202 C  CD2 . TRP B 1 34  ? 40.673 28.166 16.524  1.00 31.69  ? 33  TRP B CD2 1 
ATOM   1203 N  NE1 . TRP B 1 34  ? 40.829 30.371 16.142  1.00 33.63  ? 33  TRP B NE1 1 
ATOM   1204 C  CE2 . TRP B 1 34  ? 41.492 29.183 15.976  1.00 32.67  ? 33  TRP B CE2 1 
ATOM   1205 C  CE3 . TRP B 1 34  ? 41.129 26.846 16.497  1.00 31.11  ? 33  TRP B CE3 1 
ATOM   1206 C  CZ2 . TRP B 1 34  ? 42.763 28.918 15.416  1.00 32.80  ? 33  TRP B CZ2 1 
ATOM   1207 C  CZ3 . TRP B 1 34  ? 42.386 26.574 15.919  1.00 32.82  ? 33  TRP B CZ3 1 
ATOM   1208 C  CH2 . TRP B 1 34  ? 43.181 27.609 15.389  1.00 32.31  ? 33  TRP B CH2 1 
ATOM   1209 N  N   . TYR B 1 35  ? 36.927 25.161 17.345  1.00 32.72  ? 34  TYR B N   1 
ATOM   1210 C  CA  . TYR B 1 35  ? 36.334 23.972 17.959  1.00 33.39  ? 34  TYR B CA  1 
ATOM   1211 C  C   . TYR B 1 35  ? 37.416 23.225 18.749  1.00 34.39  ? 34  TYR B C   1 
ATOM   1212 O  O   . TYR B 1 35  ? 38.571 23.200 18.319  1.00 34.82  ? 34  TYR B O   1 
ATOM   1213 C  CB  . TYR B 1 35  ? 35.788 23.035 16.877  1.00 32.99  ? 34  TYR B CB  1 
ATOM   1214 C  CG  . TYR B 1 35  ? 34.647 23.652 16.087  1.00 32.42  ? 34  TYR B CG  1 
ATOM   1215 C  CD1 . TYR B 1 35  ? 33.328 23.489 16.501  1.00 33.34  ? 34  TYR B CD1 1 
ATOM   1216 C  CD2 . TYR B 1 35  ? 34.896 24.432 14.957  1.00 32.96  ? 34  TYR B CD2 1 
ATOM   1217 C  CE1 . TYR B 1 35  ? 32.267 24.068 15.799  1.00 32.00  ? 34  TYR B CE1 1 
ATOM   1218 C  CE2 . TYR B 1 35  ? 33.860 25.016 14.256  1.00 32.78  ? 34  TYR B CE2 1 
ATOM   1219 C  CZ  . TYR B 1 35  ? 32.542 24.837 14.695  1.00 33.25  ? 34  TYR B CZ  1 
ATOM   1220 O  OH  . TYR B 1 35  ? 31.498 25.421 13.987  1.00 33.16  ? 34  TYR B OH  1 
ATOM   1221 N  N   . LYS B 1 36  ? 37.053 22.615 19.875  1.00 35.00  ? 35  LYS B N   1 
ATOM   1222 C  CA  . LYS B 1 36  ? 37.954 21.617 20.502  1.00 35.45  ? 35  LYS B CA  1 
ATOM   1223 C  C   . LYS B 1 36  ? 37.774 20.306 19.735  1.00 35.26  ? 35  LYS B C   1 
ATOM   1224 O  O   . LYS B 1 36  ? 36.649 19.905 19.445  1.00 35.27  ? 35  LYS B O   1 
ATOM   1225 C  CB  . LYS B 1 36  ? 37.658 21.422 21.997  1.00 35.73  ? 35  LYS B CB  1 
ATOM   1226 C  CG  . LYS B 1 36  ? 38.682 20.511 22.735  1.00 36.37  ? 35  LYS B CG  1 
ATOM   1227 C  CD  . LYS B 1 36  ? 40.086 21.159 22.819  1.00 36.82  ? 35  LYS B CD  1 
ATOM   1228 C  CE  . LYS B 1 36  ? 41.184 20.170 23.321  1.00 37.41  ? 35  LYS B CE  1 
ATOM   1229 N  NZ  A LYS B 1 36  ? 40.824 19.479 24.600  0.50 31.89  ? 35  LYS B NZ  1 
ATOM   1230 N  NZ  B LYS B 1 36  ? 41.303 19.016 22.415  0.50 40.53  ? 35  LYS B NZ  1 
ATOM   1231 N  N   . GLY B 1 37  ? 38.878 19.663 19.368  1.00 35.20  ? 36  GLY B N   1 
ATOM   1232 C  CA  . GLY B 1 37  ? 38.787 18.399 18.644  1.00 35.16  ? 36  GLY B CA  1 
ATOM   1233 C  C   . GLY B 1 37  ? 39.199 18.529 17.205  1.00 36.02  ? 36  GLY B C   1 
ATOM   1234 O  O   . GLY B 1 37  ? 39.740 19.568 16.795  1.00 35.71  ? 36  GLY B O   1 
ATOM   1235 N  N   . GLU B 1 38  ? 38.946 17.468 16.435  1.00 35.98  ? 37  GLU B N   1 
ATOM   1236 C  CA  . GLU B 1 38  ? 39.484 17.364 15.104  1.00 37.14  ? 37  GLU B CA  1 
ATOM   1237 C  C   . GLU B 1 38  ? 38.434 17.663 14.031  1.00 38.32  ? 37  GLU B C   1 
ATOM   1238 O  O   . GLU B 1 38  ? 38.732 17.545 12.837  1.00 39.09  ? 37  GLU B O   1 
ATOM   1239 C  CB  . GLU B 1 38  ? 40.117 15.984 14.877  1.00 36.69  ? 37  GLU B CB  1 
ATOM   1240 C  CG  A GLU B 1 38  ? 41.537 15.921 15.481  0.50 37.05  ? 37  GLU B CG  1 
ATOM   1241 C  CG  B GLU B 1 38  ? 40.988 15.459 16.006  0.50 36.56  ? 37  GLU B CG  1 
ATOM   1242 C  CD  A GLU B 1 38  ? 42.321 14.665 15.118  0.50 37.55  ? 37  GLU B CD  1 
ATOM   1243 C  CD  B GLU B 1 38  ? 41.297 13.980 15.849  0.50 37.20  ? 37  GLU B CD  1 
ATOM   1244 O  OE1 A GLU B 1 38  ? 42.365 13.742 15.954  0.50 38.68  ? 37  GLU B OE1 1 
ATOM   1245 O  OE1 B GLU B 1 38  ? 41.055 13.234 16.819  0.50 37.64  ? 37  GLU B OE1 1 
ATOM   1246 O  OE2 A GLU B 1 38  ? 42.895 14.602 14.012  0.50 37.50  ? 37  GLU B OE2 1 
ATOM   1247 O  OE2 B GLU B 1 38  ? 41.778 13.565 14.762  0.50 36.38  ? 37  GLU B OE2 1 
ATOM   1248 N  N   . ARG B 1 39  ? 37.225 18.044 14.446  1.00 38.42  ? 38  ARG B N   1 
ATOM   1249 C  CA  . ARG B 1 39  ? 36.183 18.351 13.466  1.00 39.86  ? 38  ARG B CA  1 
ATOM   1250 C  C   . ARG B 1 39  ? 35.308 19.547 13.816  1.00 39.48  ? 38  ARG B C   1 
ATOM   1251 O  O   . ARG B 1 39  ? 35.295 20.020 14.951  1.00 38.54  ? 38  ARG B O   1 
ATOM   1252 C  CB  . ARG B 1 39  ? 35.283 17.143 13.226  1.00 40.90  ? 38  ARG B CB  1 
ATOM   1253 C  CG  . ARG B 1 39  ? 34.503 16.667 14.423  1.00 43.31  ? 38  ARG B CG  1 
ATOM   1254 C  CD  . ARG B 1 39  ? 33.581 15.500 14.010  1.00 49.43  ? 38  ARG B CD  1 
ATOM   1255 N  NE  A ARG B 1 39  ? 32.604 15.150 15.049  0.50 51.51  ? 38  ARG B NE  1 
ATOM   1256 N  NE  B ARG B 1 39  ? 32.306 15.963 13.475  0.50 48.31  ? 38  ARG B NE  1 
ATOM   1257 C  CZ  A ARG B 1 39  ? 31.801 14.084 15.016  0.50 53.42  ? 38  ARG B CZ  1 
ATOM   1258 C  CZ  B ARG B 1 39  ? 31.398 15.170 12.914  0.50 49.70  ? 38  ARG B CZ  1 
ATOM   1259 N  NH1 A ARG B 1 39  ? 30.951 13.857 16.015  0.50 53.64  ? 38  ARG B NH1 1 
ATOM   1260 N  NH1 B ARG B 1 39  ? 30.277 15.686 12.452  0.50 48.64  ? 38  ARG B NH1 1 
ATOM   1261 N  NH2 A ARG B 1 39  ? 31.843 13.240 13.993  0.50 53.78  ? 38  ARG B NH2 1 
ATOM   1262 N  NH2 B ARG B 1 39  ? 31.612 13.860 12.807  0.50 49.88  ? 38  ARG B NH2 1 
ATOM   1263 N  N   . VAL B 1 40  ? 34.561 20.001 12.816  1.00 39.06  ? 39  VAL B N   1 
ATOM   1264 C  CA  . VAL B 1 40  ? 33.513 20.973 13.032  1.00 38.72  ? 39  VAL B CA  1 
ATOM   1265 C  C   . VAL B 1 40  ? 32.375 20.225 13.717  1.00 39.01  ? 39  VAL B C   1 
ATOM   1266 O  O   . VAL B 1 40  ? 31.831 19.252 13.168  1.00 40.60  ? 39  VAL B O   1 
ATOM   1267 C  CB  . VAL B 1 40  ? 33.082 21.600 11.696  1.00 38.74  ? 39  VAL B CB  1 
ATOM   1268 C  CG1 . VAL B 1 40  ? 31.799 22.437 11.860  1.00 38.99  ? 39  VAL B CG1 1 
ATOM   1269 C  CG2 . VAL B 1 40  ? 34.218 22.431 11.139  1.00 37.01  ? 39  VAL B CG2 1 
ATOM   1270 N  N   . ASP B 1 41  ? 32.031 20.657 14.920  1.00 37.60  ? 40  ASP B N   1 
ATOM   1271 C  CA  . ASP B 1 41  ? 30.960 20.024 15.697  1.00 37.78  ? 40  ASP B CA  1 
ATOM   1272 C  C   . ASP B 1 41  ? 30.385 21.106 16.611  1.00 37.11  ? 40  ASP B C   1 
ATOM   1273 O  O   . ASP B 1 41  ? 31.075 21.579 17.501  1.00 36.32  ? 40  ASP B O   1 
ATOM   1274 C  CB  . ASP B 1 41  ? 31.531 18.857 16.529  1.00 37.38  ? 40  ASP B CB  1 
ATOM   1275 C  CG  . ASP B 1 41  ? 30.524 18.284 17.552  1.00 40.29  ? 40  ASP B CG  1 
ATOM   1276 O  OD1 . ASP B 1 41  ? 29.463 18.893 17.820  1.00 39.70  ? 40  ASP B OD1 1 
ATOM   1277 O  OD2 . ASP B 1 41  ? 30.819 17.212 18.114  1.00 42.80  ? 40  ASP B OD2 1 
ATOM   1278 N  N   . GLY B 1 42  ? 29.131 21.474 16.392  1.00 36.63  ? 41  GLY B N   1 
ATOM   1279 C  CA  . GLY B 1 42  ? 28.526 22.599 17.104  1.00 37.63  ? 41  GLY B CA  1 
ATOM   1280 C  C   . GLY B 1 42  ? 28.611 22.506 18.608  1.00 37.23  ? 41  GLY B C   1 
ATOM   1281 O  O   . GLY B 1 42  ? 28.744 23.521 19.288  1.00 37.44  ? 41  GLY B O   1 
ATOM   1282 N  N   . ASN B 1 43  ? 28.552 21.287 19.141  1.00 38.23  ? 42  ASN B N   1 
ATOM   1283 C  CA  . ASN B 1 43  ? 28.616 21.105 20.601  1.00 38.50  ? 42  ASN B CA  1 
ATOM   1284 C  C   . ASN B 1 43  ? 29.979 21.474 21.176  1.00 37.24  ? 42  ASN B C   1 
ATOM   1285 O  O   . ASN B 1 43  ? 30.110 21.668 22.393  1.00 36.64  ? 42  ASN B O   1 
ATOM   1286 C  CB  . ASN B 1 43  ? 28.260 19.666 21.010  1.00 39.64  ? 42  ASN B CB  1 
ATOM   1287 C  CG  . ASN B 1 43  ? 26.844 19.276 20.621  1.00 43.59  ? 42  ASN B CG  1 
ATOM   1288 O  OD1 . ASN B 1 43  ? 25.894 20.024 20.846  1.00 47.08  ? 42  ASN B OD1 1 
ATOM   1289 N  ND2 . ASN B 1 43  ? 26.702 18.091 20.029  1.00 46.71  ? 42  ASN B ND2 1 
ATOM   1290 N  N   . ARG B 1 44  ? 30.993 21.567 20.309  1.00 35.97  ? 43  ARG B N   1 
ATOM   1291 C  CA  . ARG B 1 44  ? 32.370 21.823 20.763  1.00 35.21  ? 43  ARG B CA  1 
ATOM   1292 C  C   . ARG B 1 44  ? 32.945 23.165 20.265  1.00 34.35  ? 43  ARG B C   1 
ATOM   1293 O  O   . ARG B 1 44  ? 34.162 23.396 20.357  1.00 33.51  ? 43  ARG B O   1 
ATOM   1294 C  CB  . ARG B 1 44  ? 33.290 20.649 20.379  1.00 35.27  ? 43  ARG B CB  1 
ATOM   1295 C  CG  . ARG B 1 44  ? 32.700 19.266 20.696  1.00 37.60  ? 43  ARG B CG  1 
ATOM   1296 C  CD  . ARG B 1 44  ? 33.768 18.148 20.635  1.00 36.34  ? 43  ARG B CD  1 
ATOM   1297 N  NE  . ARG B 1 44  ? 34.727 18.265 21.734  1.00 40.10  ? 43  ARG B NE  1 
ATOM   1298 C  CZ  . ARG B 1 44  ? 35.862 17.569 21.836  1.00 42.84  ? 43  ARG B CZ  1 
ATOM   1299 N  NH1 . ARG B 1 44  ? 36.202 16.697 20.895  1.00 42.81  ? 43  ARG B NH1 1 
ATOM   1300 N  NH2 . ARG B 1 44  ? 36.660 17.756 22.881  1.00 42.72  ? 43  ARG B NH2 1 
ATOM   1301 N  N   . GLN B 1 45  ? 32.073 24.060 19.782  1.00 32.51  ? 44  GLN B N   1 
ATOM   1302 C  CA  . GLN B 1 45  ? 32.506 25.403 19.416  1.00 31.90  ? 44  GLN B CA  1 
ATOM   1303 C  C   . GLN B 1 45  ? 32.933 26.162 20.664  1.00 31.85  ? 44  GLN B C   1 
ATOM   1304 O  O   . GLN B 1 45  ? 32.179 26.272 21.645  1.00 32.01  ? 44  GLN B O   1 
ATOM   1305 C  CB  . GLN B 1 45  ? 31.433 26.194 18.620  1.00 31.79  ? 44  GLN B CB  1 
ATOM   1306 C  CG  A GLN B 1 45  ? 31.969 27.586 18.210  0.50 30.91  ? 44  GLN B CG  1 
ATOM   1307 C  CG  B GLN B 1 45  ? 31.938 27.529 18.028  0.50 30.47  ? 44  GLN B CG  1 
ATOM   1308 C  CD  A GLN B 1 45  ? 31.167 28.307 17.144  0.50 32.61  ? 44  GLN B CD  1 
ATOM   1309 C  CD  B GLN B 1 45  ? 30.817 28.451 17.554  0.50 31.73  ? 44  GLN B CD  1 
ATOM   1310 O  OE1 A GLN B 1 45  ? 31.678 29.467 16.720  0.50 33.80  ? 44  GLN B OE1 1 
ATOM   1311 O  OE1 B GLN B 1 45  ? 30.943 29.124 16.521  0.50 32.97  ? 44  GLN B OE1 1 
ATOM   1312 N  NE2 A GLN B 1 45  ? 30.107 27.844 16.701  0.50 30.71  ? 44  GLN B NE2 1 
ATOM   1313 N  NE2 B GLN B 1 45  ? 29.719 28.491 18.304  0.50 28.74  ? 44  GLN B NE2 1 
ATOM   1314 N  N   . ILE B 1 46  ? 34.155 26.666 20.618  1.00 31.69  ? 45  ILE B N   1 
ATOM   1315 C  CA  . ILE B 1 46  ? 34.716 27.462 21.690  1.00 31.63  ? 45  ILE B CA  1 
ATOM   1316 C  C   . ILE B 1 46  ? 34.301 28.929 21.578  1.00 32.41  ? 45  ILE B C   1 
ATOM   1317 O  O   . ILE B 1 46  ? 33.745 29.512 22.526  1.00 31.28  ? 45  ILE B O   1 
ATOM   1318 C  CB  . ILE B 1 46  ? 36.259 27.354 21.690  1.00 32.54  ? 45  ILE B CB  1 
ATOM   1319 C  CG1 . ILE B 1 46  ? 36.700 25.878 21.798  1.00 31.30  ? 45  ILE B CG1 1 
ATOM   1320 C  CG2 . ILE B 1 46  ? 36.869 28.204 22.825  1.00 32.00  ? 45  ILE B CG2 1 
ATOM   1321 C  CD1 . ILE B 1 46  ? 38.204 25.679 21.606  1.00 32.31  ? 45  ILE B CD1 1 
ATOM   1322 N  N   . ILE B 1 47  ? 34.596 29.523 20.419  1.00 32.18  ? 46  ILE B N   1 
ATOM   1323 C  CA  . ILE B 1 47  ? 34.399 30.955 20.202  1.00 32.36  ? 46  ILE B CA  1 
ATOM   1324 C  C   . ILE B 1 47  ? 34.407 31.177 18.714  1.00 32.59  ? 46  ILE B C   1 
ATOM   1325 O  O   . ILE B 1 47  ? 34.976 30.367 17.964  1.00 32.60  ? 46  ILE B O   1 
ATOM   1326 C  CB  . ILE B 1 47  ? 35.503 31.815 20.940  1.00 32.48  ? 46  ILE B CB  1 
ATOM   1327 C  CG1 . ILE B 1 47  ? 35.134 33.305 21.008  1.00 32.26  ? 46  ILE B CG1 1 
ATOM   1328 C  CG2 . ILE B 1 47  ? 36.923 31.585 20.339  1.00 31.50  ? 46  ILE B CG2 1 
ATOM   1329 C  CD1 . ILE B 1 47  ? 36.085 34.119 21.889  1.00 32.58  ? 46  ILE B CD1 1 
ATOM   1330 N  N   . GLY B 1 48  ? 33.728 32.225 18.269  1.00 32.46  ? 47  GLY B N   1 
ATOM   1331 C  CA  . GLY B 1 48  ? 33.656 32.541 16.838  1.00 32.58  ? 47  GLY B CA  1 
ATOM   1332 C  C   . GLY B 1 48  ? 33.659 34.037 16.637  1.00 32.60  ? 47  GLY B C   1 
ATOM   1333 O  O   . GLY B 1 48  ? 33.378 34.795 17.592  1.00 32.13  ? 47  GLY B O   1 
ATOM   1334 N  N   . TYR B 1 49  ? 33.974 34.483 15.415  1.00 32.01  ? 48  TYR B N   1 
ATOM   1335 C  CA  . TYR B 1 49  ? 34.019 35.923 15.145  1.00 31.62  ? 48  TYR B CA  1 
ATOM   1336 C  C   . TYR B 1 49  ? 33.558 36.202 13.711  1.00 31.47  ? 48  TYR B C   1 
ATOM   1337 O  O   . TYR B 1 49  ? 34.055 35.592 12.762  1.00 30.75  ? 48  TYR B O   1 
ATOM   1338 C  CB  . TYR B 1 49  ? 35.435 36.507 15.375  1.00 31.90  ? 48  TYR B CB  1 
ATOM   1339 C  CG  . TYR B 1 49  ? 35.497 37.971 15.034  1.00 32.77  ? 48  TYR B CG  1 
ATOM   1340 C  CD1 . TYR B 1 49  ? 34.727 38.898 15.756  1.00 33.97  ? 48  TYR B CD1 1 
ATOM   1341 C  CD2 . TYR B 1 49  ? 36.290 38.443 13.975  1.00 33.92  ? 48  TYR B CD2 1 
ATOM   1342 C  CE1 . TYR B 1 49  ? 34.731 40.249 15.428  1.00 34.24  ? 48  TYR B CE1 1 
ATOM   1343 C  CE2 . TYR B 1 49  ? 36.306 39.813 13.644  1.00 33.44  ? 48  TYR B CE2 1 
ATOM   1344 C  CZ  . TYR B 1 49  ? 35.529 40.694 14.371  1.00 34.68  ? 48  TYR B CZ  1 
ATOM   1345 O  OH  . TYR B 1 49  ? 35.499 42.045 14.054  1.00 37.75  ? 48  TYR B OH  1 
ATOM   1346 N  N   . VAL B 1 50  ? 32.591 37.097 13.568  1.00 30.44  ? 49  VAL B N   1 
ATOM   1347 C  CA  . VAL B 1 50  ? 32.112 37.529 12.264  1.00 30.55  ? 49  VAL B CA  1 
ATOM   1348 C  C   . VAL B 1 50  ? 32.855 38.828 11.933  1.00 31.48  ? 49  VAL B C   1 
ATOM   1349 O  O   . VAL B 1 50  ? 32.756 39.839 12.660  1.00 31.37  ? 49  VAL B O   1 
ATOM   1350 C  CB  . VAL B 1 50  ? 30.575 37.767 12.259  1.00 30.42  ? 49  VAL B CB  1 
ATOM   1351 C  CG1 . VAL B 1 50  ? 30.128 38.332 10.919  1.00 29.64  ? 49  VAL B CG1 1 
ATOM   1352 C  CG2 . VAL B 1 50  ? 29.840 36.441 12.585  1.00 30.17  ? 49  VAL B CG2 1 
ATOM   1353 N  N   . ILE B 1 51  ? 33.622 38.783 10.859  1.00 32.40  ? 50  ILE B N   1 
ATOM   1354 C  CA  . ILE B 1 51  ? 34.489 39.914 10.475  1.00 33.93  ? 50  ILE B CA  1 
ATOM   1355 C  C   . ILE B 1 51  ? 33.701 41.218 10.319  1.00 34.88  ? 50  ILE B C   1 
ATOM   1356 O  O   . ILE B 1 51  ? 32.626 41.238 9.709   1.00 34.76  ? 50  ILE B O   1 
ATOM   1357 C  CB  . ILE B 1 51  ? 35.278 39.542 9.217   1.00 34.56  ? 50  ILE B CB  1 
ATOM   1358 C  CG1 . ILE B 1 51  ? 36.318 38.471 9.591   1.00 34.75  ? 50  ILE B CG1 1 
ATOM   1359 C  CG2 . ILE B 1 51  ? 35.968 40.785 8.593   1.00 35.34  ? 50  ILE B CG2 1 
ATOM   1360 C  CD1 . ILE B 1 51  ? 36.913 37.762 8.403   1.00 37.58  ? 50  ILE B CD1 1 
ATOM   1361 N  N   . GLY B 1 52  ? 34.199 42.288 10.926  1.00 35.07  ? 51  GLY B N   1 
ATOM   1362 C  CA  . GLY B 1 52  ? 33.543 43.574 10.840  1.00 36.48  ? 51  GLY B CA  1 
ATOM   1363 C  C   . GLY B 1 52  ? 32.543 43.892 11.934  1.00 36.98  ? 51  GLY B C   1 
ATOM   1364 O  O   . GLY B 1 52  ? 31.983 44.991 11.940  1.00 37.75  ? 51  GLY B O   1 
ATOM   1365 N  N   . THR B 1 53  ? 32.307 42.953 12.857  1.00 36.05  ? 52  THR B N   1 
ATOM   1366 C  CA  . THR B 1 53  ? 31.351 43.180 13.921  1.00 36.12  ? 52  THR B CA  1 
ATOM   1367 C  C   . THR B 1 53  ? 32.084 43.617 15.207  1.00 36.54  ? 52  THR B C   1 
ATOM   1368 O  O   . THR B 1 53  ? 33.330 43.565 15.270  1.00 35.91  ? 52  THR B O   1 
ATOM   1369 C  CB  . THR B 1 53  ? 30.443 41.936 14.152  1.00 36.49  ? 52  THR B CB  1 
ATOM   1370 O  OG1 . THR B 1 53  ? 31.227 40.849 14.656  1.00 36.78  ? 52  THR B OG1 1 
ATOM   1371 C  CG2 . THR B 1 53  ? 29.740 41.523 12.823  1.00 35.38  ? 52  THR B CG2 1 
ATOM   1372 N  N   . GLN B 1 54  ? 31.311 44.056 16.203  1.00 35.91  ? 53  GLN B N   1 
ATOM   1373 C  CA  . GLN B 1 54  ? 31.870 44.679 17.414  1.00 36.46  ? 53  GLN B CA  1 
ATOM   1374 C  C   . GLN B 1 54  ? 32.251 43.669 18.513  1.00 35.36  ? 53  GLN B C   1 
ATOM   1375 O  O   . GLN B 1 54  ? 32.820 44.052 19.531  1.00 34.50  ? 53  GLN B O   1 
ATOM   1376 C  CB  . GLN B 1 54  ? 30.863 45.683 17.991  1.00 36.87  ? 53  GLN B CB  1 
ATOM   1377 C  CG  . GLN B 1 54  ? 30.426 46.767 16.996  1.00 41.36  ? 53  GLN B CG  1 
ATOM   1378 C  CD  . GLN B 1 54  ? 29.077 47.391 17.351  1.00 43.44  ? 53  GLN B CD  1 
ATOM   1379 O  OE1 . GLN B 1 54  ? 28.956 48.616 17.452  1.00 45.96  ? 53  GLN B OE1 1 
ATOM   1380 N  NE2 . GLN B 1 54  ? 28.063 46.556 17.528  1.00 43.83  ? 53  GLN B NE2 1 
ATOM   1381 N  N   . GLN B 1 55  ? 31.906 42.396 18.318  1.00 34.47  ? 54  GLN B N   1 
ATOM   1382 C  CA  . GLN B 1 55  ? 32.090 41.395 19.369  1.00 34.38  ? 54  GLN B CA  1 
ATOM   1383 C  C   . GLN B 1 55  ? 32.385 40.018 18.780  1.00 33.83  ? 54  GLN B C   1 
ATOM   1384 O  O   . GLN B 1 55  ? 32.095 39.747 17.614  1.00 33.22  ? 54  GLN B O   1 
ATOM   1385 C  CB  . GLN B 1 55  ? 30.874 41.347 20.319  1.00 34.46  ? 54  GLN B CB  1 
ATOM   1386 C  CG  . GLN B 1 55  ? 29.485 40.873 19.697  1.00 37.11  ? 54  GLN B CG  1 
ATOM   1387 C  CD  . GLN B 1 55  ? 28.784 41.953 18.857  1.00 41.24  ? 54  GLN B CD  1 
ATOM   1388 O  OE1 . GLN B 1 55  ? 28.512 43.097 19.463  1.00 44.93  ? 54  GLN B OE1 1 
ATOM   1389 N  NE2 . GLN B 1 55  ? 28.523 41.762 17.669  1.00 39.90  ? 54  GLN B NE2 1 
ATOM   1390 N  N   . ALA B 1 56  ? 32.985 39.170 19.610  1.00 34.00  ? 55  ALA B N   1 
ATOM   1391 C  CA  . ALA B 1 56  ? 33.205 37.777 19.301  1.00 32.97  ? 55  ALA B CA  1 
ATOM   1392 C  C   . ALA B 1 56  ? 32.102 37.080 20.069  1.00 33.42  ? 55  ALA B C   1 
ATOM   1393 O  O   . ALA B 1 56  ? 31.564 37.643 21.024  1.00 31.77  ? 55  ALA B O   1 
ATOM   1394 C  CB  . ALA B 1 56  ? 34.544 37.358 19.828  1.00 33.03  ? 55  ALA B CB  1 
ATOM   1395 N  N   . THR B 1 57  ? 31.760 35.862 19.681  1.00 33.20  ? 56  THR B N   1 
ATOM   1396 C  CA  . THR B 1 57  ? 30.651 35.176 20.351  1.00 33.67  ? 56  THR B CA  1 
ATOM   1397 C  C   . THR B 1 57  ? 31.077 33.825 20.933  1.00 33.26  ? 56  THR B C   1 
ATOM   1398 O  O   . THR B 1 57  ? 31.764 33.064 20.260  1.00 33.69  ? 56  THR B O   1 
ATOM   1399 C  CB  . THR B 1 57  ? 29.448 34.970 19.390  1.00 34.83  ? 56  THR B CB  1 
ATOM   1400 O  OG1 A THR B 1 57  ? 28.404 34.225 20.042  0.50 31.81  ? 56  THR B OG1 1 
ATOM   1401 O  OG1 B THR B 1 57  ? 29.823 34.026 18.384  0.50 35.46  ? 56  THR B OG1 1 
ATOM   1402 C  CG2 A THR B 1 57  ? 29.853 34.304 18.091  0.50 34.51  ? 56  THR B CG2 1 
ATOM   1403 C  CG2 B THR B 1 57  ? 29.086 36.236 18.723  0.50 35.29  ? 56  THR B CG2 1 
ATOM   1404 N  N   . PRO B 1 58  ? 30.632 33.511 22.166  1.00 33.75  ? 57  PRO B N   1 
ATOM   1405 C  CA  . PRO B 1 58  ? 31.038 32.253 22.803  1.00 33.23  ? 57  PRO B CA  1 
ATOM   1406 C  C   . PRO B 1 58  ? 30.239 31.063 22.271  1.00 33.47  ? 57  PRO B C   1 
ATOM   1407 O  O   . PRO B 1 58  ? 29.052 31.210 21.918  1.00 32.99  ? 57  PRO B O   1 
ATOM   1408 C  CB  . PRO B 1 58  ? 30.726 32.498 24.269  1.00 33.62  ? 57  PRO B CB  1 
ATOM   1409 C  CG  . PRO B 1 58  ? 29.501 33.431 24.220  1.00 33.32  ? 57  PRO B CG  1 
ATOM   1410 C  CD  . PRO B 1 58  ? 29.728 34.314 23.025  1.00 32.47  ? 57  PRO B CD  1 
ATOM   1411 N  N   . GLY B 1 59  ? 30.879 29.898 22.182  1.00 32.87  ? 58  GLY B N   1 
ATOM   1412 C  CA  . GLY B 1 59  ? 30.125 28.674 21.875  1.00 33.52  ? 58  GLY B CA  1 
ATOM   1413 C  C   . GLY B 1 59  ? 29.949 27.846 23.139  1.00 34.39  ? 58  GLY B C   1 
ATOM   1414 O  O   . GLY B 1 59  ? 30.371 28.277 24.226  1.00 34.47  ? 58  GLY B O   1 
ATOM   1415 N  N   . PRO B 1 60  ? 29.338 26.650 23.018  1.00 35.36  ? 59  PRO B N   1 
ATOM   1416 C  CA  . PRO B 1 60  ? 29.138 25.797 24.197  1.00 36.14  ? 59  PRO B CA  1 
ATOM   1417 C  C   . PRO B 1 60  ? 30.427 25.409 24.933  1.00 36.67  ? 59  PRO B C   1 
ATOM   1418 O  O   . PRO B 1 60  ? 30.371 25.128 26.135  1.00 36.31  ? 59  PRO B O   1 
ATOM   1419 C  CB  . PRO B 1 60  ? 28.465 24.548 23.608  1.00 36.57  ? 59  PRO B CB  1 
ATOM   1420 C  CG  . PRO B 1 60  ? 27.764 25.049 22.366  1.00 36.51  ? 59  PRO B CG  1 
ATOM   1421 C  CD  . PRO B 1 60  ? 28.737 26.051 21.803  1.00 34.98  ? 59  PRO B CD  1 
ATOM   1422 N  N   . ALA B 1 61  ? 31.569 25.389 24.238  1.00 36.04  ? 60  ALA B N   1 
ATOM   1423 C  CA  . ALA B 1 61  ? 32.844 25.023 24.877  1.00 36.57  ? 60  ALA B CA  1 
ATOM   1424 C  C   . ALA B 1 61  ? 33.641 26.201 25.428  1.00 37.21  ? 60  ALA B C   1 
ATOM   1425 O  O   . ALA B 1 61  ? 34.769 26.041 25.923  1.00 37.91  ? 60  ALA B O   1 
ATOM   1426 C  CB  . ALA B 1 61  ? 33.712 24.156 23.931  1.00 35.92  ? 60  ALA B CB  1 
ATOM   1427 N  N   . TYR B 1 62  ? 33.058 27.394 25.363  1.00 37.63  ? 61  TYR B N   1 
ATOM   1428 C  CA  . TYR B 1 62  ? 33.716 28.590 25.882  1.00 37.29  ? 61  TYR B CA  1 
ATOM   1429 C  C   . TYR B 1 62  ? 33.977 28.449 27.376  1.00 37.56  ? 61  TYR B C   1 
ATOM   1430 O  O   . TYR B 1 62  ? 33.124 27.940 28.115  1.00 35.91  ? 61  TYR B O   1 
ATOM   1431 C  CB  . TYR B 1 62  ? 32.836 29.799 25.640  1.00 37.72  ? 61  TYR B CB  1 
ATOM   1432 C  CG  . TYR B 1 62  ? 33.437 31.091 26.091  1.00 38.75  ? 61  TYR B CG  1 
ATOM   1433 C  CD1 . TYR B 1 62  ? 34.514 31.676 25.394  1.00 37.79  ? 61  TYR B CD1 1 
ATOM   1434 C  CD2 . TYR B 1 62  ? 32.928 31.744 27.217  1.00 40.13  ? 61  TYR B CD2 1 
ATOM   1435 C  CE1 . TYR B 1 62  ? 35.062 32.877 25.825  1.00 41.06  ? 61  TYR B CE1 1 
ATOM   1436 C  CE2 . TYR B 1 62  ? 33.467 32.943 27.651  1.00 40.67  ? 61  TYR B CE2 1 
ATOM   1437 C  CZ  . TYR B 1 62  ? 34.520 33.491 26.961  1.00 40.61  ? 61  TYR B CZ  1 
ATOM   1438 O  OH  . TYR B 1 62  ? 35.018 34.672 27.415  1.00 44.27  ? 61  TYR B OH  1 
ATOM   1439 N  N   . SER B 1 63  ? 35.141 28.905 27.837  1.00 37.73  ? 62  SER B N   1 
ATOM   1440 C  CA  . SER B 1 63  ? 35.427 28.746 29.273  1.00 38.07  ? 62  SER B CA  1 
ATOM   1441 C  C   . SER B 1 63  ? 35.847 30.027 29.955  1.00 38.08  ? 62  SER B C   1 
ATOM   1442 O  O   . SER B 1 63  ? 36.301 29.995 31.095  1.00 38.74  ? 62  SER B O   1 
ATOM   1443 C  CB  . SER B 1 63  ? 36.458 27.636 29.511  1.00 37.94  ? 62  SER B CB  1 
ATOM   1444 O  OG  . SER B 1 63  ? 37.732 28.041 29.035  1.00 39.34  ? 62  SER B OG  1 
ATOM   1445 N  N   . GLY B 1 64  ? 35.697 31.161 29.272  1.00 37.55  ? 63  GLY B N   1 
ATOM   1446 C  CA  . GLY B 1 64  ? 36.027 32.458 29.876  1.00 37.22  ? 63  GLY B CA  1 
ATOM   1447 C  C   . GLY B 1 64  ? 37.491 32.854 29.749  1.00 37.25  ? 63  GLY B C   1 
ATOM   1448 O  O   . GLY B 1 64  ? 37.897 33.892 30.262  1.00 37.03  ? 63  GLY B O   1 
ATOM   1449 N  N   . ARG B 1 65  ? 38.271 32.024 29.056  1.00 36.94  ? 64  ARG B N   1 
ATOM   1450 C  CA  . ARG B 1 65  ? 39.731 32.169 28.982  1.00 37.41  ? 64  ARG B CA  1 
ATOM   1451 C  C   . ARG B 1 65  ? 40.236 32.450 27.557  1.00 37.76  ? 64  ARG B C   1 
ATOM   1452 O  O   . ARG B 1 65  ? 41.438 32.683 27.364  1.00 38.50  ? 64  ARG B O   1 
ATOM   1453 C  CB  . ARG B 1 65  ? 40.409 30.897 29.521  1.00 37.24  ? 64  ARG B CB  1 
ATOM   1454 C  CG  . ARG B 1 65  ? 40.086 30.576 31.004  1.00 38.22  ? 64  ARG B CG  1 
ATOM   1455 C  CD  . ARG B 1 65  ? 40.705 29.255 31.434  1.00 37.79  ? 64  ARG B CD  1 
ATOM   1456 N  NE  . ARG B 1 65  ? 40.125 28.177 30.623  1.00 38.82  ? 64  ARG B NE  1 
ATOM   1457 C  CZ  . ARG B 1 65  ? 40.773 27.082 30.230  1.00 40.43  ? 64  ARG B CZ  1 
ATOM   1458 N  NH1 . ARG B 1 65  ? 40.144 26.184 29.487  1.00 40.60  ? 64  ARG B NH1 1 
ATOM   1459 N  NH2 . ARG B 1 65  ? 42.045 26.876 30.566  1.00 41.81  ? 64  ARG B NH2 1 
ATOM   1460 N  N   . GLU B 1 66  ? 39.324 32.438 26.574  1.00 36.65  ? 65  GLU B N   1 
ATOM   1461 C  CA  . GLU B 1 66  ? 39.692 32.437 25.157  1.00 36.69  ? 65  GLU B CA  1 
ATOM   1462 C  C   . GLU B 1 66  ? 39.339 33.733 24.434  1.00 36.95  ? 65  GLU B C   1 
ATOM   1463 O  O   . GLU B 1 66  ? 38.263 34.323 24.652  1.00 36.70  ? 65  GLU B O   1 
ATOM   1464 C  CB  . GLU B 1 66  ? 39.033 31.266 24.430  1.00 36.35  ? 65  GLU B CB  1 
ATOM   1465 C  CG  . GLU B 1 66  ? 39.293 29.907 25.074  1.00 36.03  ? 65  GLU B CG  1 
ATOM   1466 C  CD  . GLU B 1 66  ? 38.224 29.509 26.113  1.00 36.75  ? 65  GLU B CD  1 
ATOM   1467 O  OE1 . GLU B 1 66  ? 37.377 30.341 26.505  1.00 37.19  ? 65  GLU B OE1 1 
ATOM   1468 O  OE2 . GLU B 1 66  ? 38.239 28.349 26.535  1.00 36.63  ? 65  GLU B OE2 1 
ATOM   1469 N  N   . ILE B 1 67  ? 40.257 34.176 23.580  1.00 36.94  ? 66  ILE B N   1 
ATOM   1470 C  CA  . ILE B 1 67  ? 40.051 35.334 22.727  1.00 37.17  ? 66  ILE B CA  1 
ATOM   1471 C  C   . ILE B 1 67  ? 40.414 34.937 21.306  1.00 37.08  ? 66  ILE B C   1 
ATOM   1472 O  O   . ILE B 1 67  ? 41.373 34.183 21.093  1.00 37.24  ? 66  ILE B O   1 
ATOM   1473 C  CB  . ILE B 1 67  ? 40.890 36.526 23.247  1.00 39.02  ? 66  ILE B CB  1 
ATOM   1474 C  CG1 . ILE B 1 67  ? 40.051 37.333 24.252  1.00 40.59  ? 66  ILE B CG1 1 
ATOM   1475 C  CG2 . ILE B 1 67  ? 41.436 37.423 22.113  1.00 38.52  ? 66  ILE B CG2 1 
ATOM   1476 C  CD1 . ILE B 1 67  ? 40.636 37.315 25.565  1.00 45.06  ? 66  ILE B CD1 1 
ATOM   1477 N  N   . ILE B 1 68  ? 39.620 35.387 20.335  1.00 36.32  ? 67  ILE B N   1 
ATOM   1478 C  CA  . ILE B 1 68  ? 39.934 35.142 18.943  1.00 35.29  ? 67  ILE B CA  1 
ATOM   1479 C  C   . ILE B 1 68  ? 40.264 36.485 18.298  1.00 36.53  ? 67  ILE B C   1 
ATOM   1480 O  O   . ILE B 1 68  ? 39.431 37.421 18.305  1.00 36.54  ? 67  ILE B O   1 
ATOM   1481 C  CB  . ILE B 1 68  ? 38.772 34.399 18.199  1.00 35.24  ? 67  ILE B CB  1 
ATOM   1482 C  CG1 . ILE B 1 68  ? 39.161 34.084 16.747  1.00 35.08  ? 67  ILE B CG1 1 
ATOM   1483 C  CG2 . ILE B 1 68  ? 37.418 35.177 18.316  1.00 33.45  ? 67  ILE B CG2 1 
ATOM   1484 C  CD1 . ILE B 1 68  ? 38.105 33.269 15.972  1.00 34.71  ? 67  ILE B CD1 1 
ATOM   1485 N  N   . TYR B 1 69  ? 41.487 36.589 17.765  1.00 36.27  ? 68  TYR B N   1 
ATOM   1486 C  CA  . TYR B 1 69  ? 41.929 37.794 17.049  1.00 36.55  ? 68  TYR B CA  1 
ATOM   1487 C  C   . TYR B 1 69  ? 41.242 37.904 15.675  1.00 36.68  ? 68  TYR B C   1 
ATOM   1488 O  O   . TYR B 1 69  ? 40.789 36.904 15.112  1.00 36.32  ? 68  TYR B O   1 
ATOM   1489 C  CB  . TYR B 1 69  ? 43.455 37.772 16.873  1.00 37.07  ? 68  TYR B CB  1 
ATOM   1490 C  CG  . TYR B 1 69  ? 44.260 38.101 18.122  1.00 37.71  ? 68  TYR B CG  1 
ATOM   1491 C  CD1 . TYR B 1 69  ? 44.637 37.107 19.038  1.00 37.74  ? 68  TYR B CD1 1 
ATOM   1492 C  CD2 . TYR B 1 69  ? 44.641 39.410 18.392  1.00 38.64  ? 68  TYR B CD2 1 
ATOM   1493 C  CE1 . TYR B 1 69  ? 45.394 37.428 20.208  1.00 38.48  ? 68  TYR B CE1 1 
ATOM   1494 C  CE2 . TYR B 1 69  ? 45.385 39.733 19.542  1.00 38.12  ? 68  TYR B CE2 1 
ATOM   1495 C  CZ  . TYR B 1 69  ? 45.760 38.747 20.440  1.00 38.54  ? 68  TYR B CZ  1 
ATOM   1496 O  OH  . TYR B 1 69  ? 46.509 39.123 21.557  1.00 39.44  ? 68  TYR B OH  1 
ATOM   1497 N  N   . PRO B 1 70  ? 41.175 39.123 15.123  1.00 37.17  ? 69  PRO B N   1 
ATOM   1498 C  CA  . PRO B 1 70  ? 40.607 39.372 13.792  1.00 37.22  ? 69  PRO B CA  1 
ATOM   1499 C  C   . PRO B 1 70  ? 41.320 38.609 12.674  1.00 37.15  ? 69  PRO B C   1 
ATOM   1500 O  O   . PRO B 1 70  ? 40.725 38.404 11.611  1.00 37.41  ? 69  PRO B O   1 
ATOM   1501 C  CB  . PRO B 1 70  ? 40.804 40.877 13.604  1.00 37.87  ? 69  PRO B CB  1 
ATOM   1502 C  CG  . PRO B 1 70  ? 40.903 41.405 14.978  1.00 38.57  ? 69  PRO B CG  1 
ATOM   1503 C  CD  . PRO B 1 70  ? 41.599 40.370 15.778  1.00 37.27  ? 69  PRO B CD  1 
ATOM   1504 N  N   . ASN B 1 71  ? 42.575 38.197 12.907  1.00 35.97  ? 70  ASN B N   1 
ATOM   1505 C  CA  . ASN B 1 71  ? 43.297 37.327 11.954  1.00 35.44  ? 70  ASN B CA  1 
ATOM   1506 C  C   . ASN B 1 71  ? 43.116 35.825 12.246  1.00 34.56  ? 70  ASN B C   1 
ATOM   1507 O  O   . ASN B 1 71  ? 43.823 34.977 11.683  1.00 33.80  ? 70  ASN B O   1 
ATOM   1508 C  CB  . ASN B 1 71  ? 44.792 37.714 11.852  1.00 36.40  ? 70  ASN B CB  1 
ATOM   1509 C  CG  . ASN B 1 71  ? 45.609 37.285 13.075  1.00 38.73  ? 70  ASN B CG  1 
ATOM   1510 O  OD1 . ASN B 1 71  ? 45.093 36.673 14.013  1.00 37.95  ? 70  ASN B OD1 1 
ATOM   1511 N  ND2 . ASN B 1 71  ? 46.907 37.568 13.041  1.00 40.33  ? 70  ASN B ND2 1 
ATOM   1512 N  N   . ALA B 1 72  ? 42.144 35.514 13.114  1.00 33.41  ? 71  ALA B N   1 
ATOM   1513 C  CA  . ALA B 1 72  ? 41.741 34.144 13.475  1.00 33.04  ? 71  ALA B CA  1 
ATOM   1514 C  C   . ALA B 1 72  ? 42.596 33.474 14.540  1.00 33.25  ? 71  ALA B C   1 
ATOM   1515 O  O   . ALA B 1 72  ? 42.251 32.379 14.986  1.00 33.86  ? 71  ALA B O   1 
ATOM   1516 C  CB  . ALA B 1 72  ? 41.636 33.221 12.235  1.00 32.49  ? 71  ALA B CB  1 
ATOM   1517 N  N   . SER B 1 73  ? 43.708 34.078 14.943  1.00 33.24  ? 72  SER B N   1 
ATOM   1518 C  CA  . SER B 1 73  ? 44.534 33.409 15.970  1.00 34.03  ? 72  SER B CA  1 
ATOM   1519 C  C   . SER B 1 73  ? 43.770 33.273 17.289  1.00 34.47  ? 72  SER B C   1 
ATOM   1520 O  O   . SER B 1 73  ? 43.031 34.194 17.688  1.00 34.59  ? 72  SER B O   1 
ATOM   1521 C  CB  . SER B 1 73  ? 45.864 34.132 16.216  1.00 34.21  ? 72  SER B CB  1 
ATOM   1522 O  OG  A SER B 1 73  ? 45.710 35.524 16.351  0.50 32.92  ? 72  SER B OG  1 
ATOM   1523 O  OG  B SER B 1 73  ? 46.539 34.382 15.012  0.50 33.84  ? 72  SER B OG  1 
ATOM   1524 N  N   . LEU B 1 74  ? 43.970 32.145 17.975  1.00 34.08  ? 73  LEU B N   1 
ATOM   1525 C  CA  . LEU B 1 74  ? 43.269 31.885 19.234  1.00 33.40  ? 73  LEU B CA  1 
ATOM   1526 C  C   . LEU B 1 74  ? 44.254 32.001 20.411  1.00 35.13  ? 73  LEU B C   1 
ATOM   1527 O  O   . LEU B 1 74  ? 45.258 31.276 20.456  1.00 34.79  ? 73  LEU B O   1 
ATOM   1528 C  CB  . LEU B 1 74  ? 42.679 30.467 19.222  1.00 33.36  ? 73  LEU B CB  1 
ATOM   1529 C  CG  . LEU B 1 74  ? 41.848 30.068 20.459  1.00 32.71  ? 73  LEU B CG  1 
ATOM   1530 C  CD1 . LEU B 1 74  ? 40.549 30.916 20.511  1.00 30.06  ? 73  LEU B CD1 1 
ATOM   1531 C  CD2 . LEU B 1 74  ? 41.544 28.564 20.432  1.00 31.49  ? 73  LEU B CD2 1 
ATOM   1532 N  N   . LEU B 1 75  ? 43.958 32.881 21.364  1.00 34.93  ? 74  LEU B N   1 
ATOM   1533 C  CA  . LEU B 1 75  ? 44.734 32.958 22.591  1.00 36.68  ? 74  LEU B CA  1 
ATOM   1534 C  C   . LEU B 1 75  ? 43.943 32.336 23.750  1.00 37.49  ? 74  LEU B C   1 
ATOM   1535 O  O   . LEU B 1 75  ? 42.790 32.710 23.977  1.00 38.08  ? 74  LEU B O   1 
ATOM   1536 C  CB  . LEU B 1 75  ? 45.091 34.413 22.888  1.00 35.76  ? 74  LEU B CB  1 
ATOM   1537 C  CG  . LEU B 1 75  ? 45.816 34.686 24.207  1.00 37.98  ? 74  LEU B CG  1 
ATOM   1538 C  CD1 . LEU B 1 75  ? 47.268 34.196 24.122  1.00 39.39  ? 74  LEU B CD1 1 
ATOM   1539 C  CD2 . LEU B 1 75  ? 45.750 36.159 24.529  1.00 36.44  ? 74  LEU B CD2 1 
ATOM   1540 N  N   . ILE B 1 76  ? 44.545 31.382 24.469  1.00 38.49  ? 75  ILE B N   1 
ATOM   1541 C  CA  . ILE B 1 76  ? 43.931 30.799 25.685  1.00 38.72  ? 75  ILE B CA  1 
ATOM   1542 C  C   . ILE B 1 76  ? 44.821 31.058 26.909  1.00 40.49  ? 75  ILE B C   1 
ATOM   1543 O  O   . ILE B 1 76  ? 46.003 30.695 26.882  1.00 40.55  ? 75  ILE B O   1 
ATOM   1544 C  CB  . ILE B 1 76  ? 43.715 29.275 25.564  1.00 39.08  ? 75  ILE B CB  1 
ATOM   1545 C  CG1 . ILE B 1 76  ? 43.071 28.889 24.218  1.00 37.91  ? 75  ILE B CG1 1 
ATOM   1546 C  CG2 . ILE B 1 76  ? 42.896 28.733 26.785  1.00 38.94  ? 75  ILE B CG2 1 
ATOM   1547 C  CD1 . ILE B 1 76  ? 43.014 27.373 23.944  1.00 37.60  ? 75  ILE B CD1 1 
ATOM   1548 N  N   . GLN B 1 77  ? 44.255 31.662 27.965  1.00 40.97  ? 76  GLN B N   1 
ATOM   1549 C  CA  . GLN B 1 77  ? 44.953 31.928 29.233  1.00 41.88  ? 76  GLN B CA  1 
ATOM   1550 C  C   . GLN B 1 77  ? 44.790 30.778 30.222  1.00 41.69  ? 76  GLN B C   1 
ATOM   1551 O  O   . GLN B 1 77  ? 43.863 29.987 30.112  1.00 40.09  ? 76  GLN B O   1 
ATOM   1552 C  CB  . GLN B 1 77  ? 44.379 33.169 29.929  1.00 42.95  ? 76  GLN B CB  1 
ATOM   1553 C  CG  . GLN B 1 77  ? 44.352 34.472 29.159  1.00 46.45  ? 76  GLN B CG  1 
ATOM   1554 C  CD  . GLN B 1 77  ? 45.728 35.019 28.889  1.00 50.55  ? 76  GLN B CD  1 
ATOM   1555 O  OE1 . GLN B 1 77  ? 46.437 35.460 29.794  1.00 51.93  ? 76  GLN B OE1 1 
ATOM   1556 N  NE2 . GLN B 1 77  ? 46.117 35.002 27.627  1.00 53.87  ? 76  GLN B NE2 1 
ATOM   1557 N  N   . ASN B 1 78  ? 45.674 30.717 31.223  1.00 42.65  ? 77  ASN B N   1 
ATOM   1558 C  CA  . ASN B 1 78  ? 45.490 29.833 32.378  1.00 43.21  ? 77  ASN B CA  1 
ATOM   1559 C  C   . ASN B 1 78  ? 45.222 28.404 31.996  1.00 42.98  ? 77  ASN B C   1 
ATOM   1560 O  O   . ASN B 1 78  ? 44.212 27.818 32.386  1.00 42.50  ? 77  ASN B O   1 
ATOM   1561 C  CB  . ASN B 1 78  ? 44.375 30.363 33.288  1.00 44.59  ? 77  ASN B CB  1 
ATOM   1562 C  CG  . ASN B 1 78  ? 44.689 31.748 33.840  1.00 48.95  ? 77  ASN B CG  1 
ATOM   1563 O  OD1 . ASN B 1 78  ? 43.900 32.689 33.686  1.00 54.20  ? 77  ASN B OD1 1 
ATOM   1564 N  ND2 . ASN B 1 78  ? 45.859 31.888 34.469  1.00 53.34  ? 77  ASN B ND2 1 
ATOM   1565 N  N   . ILE B 1 79  ? 46.146 27.856 31.217  1.00 43.33  ? 78  ILE B N   1 
ATOM   1566 C  CA  . ILE B 1 79  ? 46.062 26.513 30.673  1.00 44.06  ? 78  ILE B CA  1 
ATOM   1567 C  C   . ILE B 1 79  ? 46.031 25.459 31.777  1.00 45.45  ? 78  ILE B C   1 
ATOM   1568 O  O   . ILE B 1 79  ? 46.718 25.594 32.786  1.00 45.30  ? 78  ILE B O   1 
ATOM   1569 C  CB  . ILE B 1 79  ? 47.267 26.262 29.729  1.00 43.58  ? 78  ILE B CB  1 
ATOM   1570 C  CG1 . ILE B 1 79  ? 47.131 27.126 28.463  1.00 43.00  ? 78  ILE B CG1 1 
ATOM   1571 C  CG2 . ILE B 1 79  ? 47.415 24.778 29.400  1.00 44.03  ? 78  ILE B CG2 1 
ATOM   1572 C  CD1 . ILE B 1 79  ? 46.056 26.642 27.475  1.00 40.55  ? 78  ILE B CD1 1 
ATOM   1573 N  N   . ILE B 1 80  ? 45.205 24.436 31.576  1.00 46.73  ? 79  ILE B N   1 
ATOM   1574 C  CA  . ILE B 1 80  ? 45.119 23.266 32.463  1.00 47.92  ? 79  ILE B CA  1 
ATOM   1575 C  C   . ILE B 1 80  ? 45.362 22.027 31.610  1.00 48.55  ? 79  ILE B C   1 
ATOM   1576 O  O   . ILE B 1 80  ? 45.250 22.088 30.378  1.00 48.12  ? 79  ILE B O   1 
ATOM   1577 C  CB  . ILE B 1 80  ? 43.735 23.158 33.172  1.00 47.77  ? 79  ILE B CB  1 
ATOM   1578 C  CG1 . ILE B 1 80  ? 42.589 23.154 32.142  1.00 48.22  ? 79  ILE B CG1 1 
ATOM   1579 C  CG2 . ILE B 1 80  ? 43.567 24.301 34.175  1.00 47.93  ? 79  ILE B CG2 1 
ATOM   1580 C  CD1 . ILE B 1 80  ? 41.228 22.696 32.667  1.00 48.34  ? 79  ILE B CD1 1 
ATOM   1581 N  N   . GLN B 1 81  ? 45.662 20.901 32.253  1.00 48.87  ? 80  GLN B N   1 
ATOM   1582 C  CA  . GLN B 1 81  ? 45.988 19.666 31.529  1.00 49.63  ? 80  GLN B CA  1 
ATOM   1583 C  C   . GLN B 1 81  ? 44.905 19.271 30.502  1.00 48.66  ? 80  GLN B C   1 
ATOM   1584 O  O   . GLN B 1 81  ? 45.214 18.845 29.398  1.00 48.17  ? 80  GLN B O   1 
ATOM   1585 C  CB  . GLN B 1 81  ? 46.249 18.520 32.519  1.00 50.39  ? 80  GLN B CB  1 
ATOM   1586 C  CG  . GLN B 1 81  ? 46.842 17.262 31.881  1.00 54.48  ? 80  GLN B CG  1 
ATOM   1587 C  CD  . GLN B 1 81  ? 48.271 17.467 31.371  1.00 59.84  ? 80  GLN B CD  1 
ATOM   1588 O  OE1 . GLN B 1 81  ? 49.084 18.160 32.005  1.00 62.28  ? 80  GLN B OE1 1 
ATOM   1589 N  NE2 . GLN B 1 81  ? 48.585 16.851 30.228  1.00 61.23  ? 80  GLN B NE2 1 
ATOM   1590 N  N   . ASN B 1 82  ? 43.643 19.431 30.893  1.00 48.11  ? 81  ASN B N   1 
ATOM   1591 C  CA  . ASN B 1 82  ? 42.481 19.133 30.047  1.00 47.77  ? 81  ASN B CA  1 
ATOM   1592 C  C   . ASN B 1 82  ? 42.388 19.930 28.728  1.00 46.59  ? 81  ASN B C   1 
ATOM   1593 O  O   . ASN B 1 82  ? 41.694 19.515 27.813  1.00 46.83  ? 81  ASN B O   1 
ATOM   1594 C  CB  . ASN B 1 82  ? 41.199 19.278 30.880  1.00 47.72  ? 81  ASN B CB  1 
ATOM   1595 C  CG  A ASN B 1 82  ? 39.969 18.705 30.198  0.50 48.64  ? 81  ASN B CG  1 
ATOM   1596 C  CG  B ASN B 1 82  ? 40.865 18.013 31.667  0.50 49.58  ? 81  ASN B CG  1 
ATOM   1597 O  OD1 A ASN B 1 82  ? 38.984 19.416 29.985  0.50 49.48  ? 81  ASN B OD1 1 
ATOM   1598 O  OD1 B ASN B 1 82  ? 41.624 16.932 31.432  0.50 51.77  ? 81  ASN B OD1 1 
ATOM   1599 N  ND2 A ASN B 1 82  ? 40.008 17.413 29.869  0.50 49.62  ? 81  ASN B ND2 1 
ATOM   1600 N  ND2 B ASN B 1 82  ? 39.929 18.006 32.476  0.50 49.50  ? 81  ASN B ND2 1 
ATOM   1601 N  N   . ASP B 1 83  ? 43.095 21.056 28.637  1.00 45.40  ? 82  ASP B N   1 
ATOM   1602 C  CA  . ASP B 1 83  ? 43.196 21.839 27.393  1.00 43.86  ? 82  ASP B CA  1 
ATOM   1603 C  C   . ASP B 1 83  ? 44.026 21.175 26.302  1.00 43.56  ? 82  ASP B C   1 
ATOM   1604 O  O   . ASP B 1 83  ? 43.921 21.539 25.120  1.00 42.56  ? 82  ASP B O   1 
ATOM   1605 C  CB  . ASP B 1 83  ? 43.793 23.206 27.696  1.00 43.31  ? 82  ASP B CB  1 
ATOM   1606 C  CG  . ASP B 1 83  ? 42.883 24.058 28.559  1.00 43.13  ? 82  ASP B CG  1 
ATOM   1607 O  OD1 . ASP B 1 83  ? 41.638 23.928 28.436  1.00 41.26  ? 82  ASP B OD1 1 
ATOM   1608 O  OD2 . ASP B 1 83  ? 43.412 24.866 29.351  1.00 41.83  ? 82  ASP B OD2 1 
ATOM   1609 N  N   . ALA B 1 84  ? 44.873 20.220 26.693  1.00 42.86  ? 83  ALA B N   1 
ATOM   1610 C  CA  . ALA B 1 84  ? 45.746 19.533 25.748  1.00 42.46  ? 83  ALA B CA  1 
ATOM   1611 C  C   . ALA B 1 84  ? 44.932 18.837 24.661  1.00 42.24  ? 83  ALA B C   1 
ATOM   1612 O  O   . ALA B 1 84  ? 43.825 18.343 24.913  1.00 42.85  ? 83  ALA B O   1 
ATOM   1613 C  CB  . ALA B 1 84  ? 46.656 18.502 26.488  1.00 42.39  ? 83  ALA B CB  1 
ATOM   1614 N  N   . GLY B 1 85  ? 45.480 18.798 23.453  1.00 41.82  ? 84  GLY B N   1 
ATOM   1615 C  CA  . GLY B 1 85  ? 44.851 18.061 22.362  1.00 41.13  ? 84  GLY B CA  1 
ATOM   1616 C  C   . GLY B 1 85  ? 44.690 18.899 21.103  1.00 40.63  ? 84  GLY B C   1 
ATOM   1617 O  O   . GLY B 1 85  ? 45.437 19.853 20.896  1.00 40.52  ? 84  GLY B O   1 
ATOM   1618 N  N   . PHE B 1 86  ? 43.695 18.534 20.285  1.00 40.11  ? 85  PHE B N   1 
ATOM   1619 C  CA  . PHE B 1 86  ? 43.489 19.119 18.949  1.00 39.88  ? 85  PHE B CA  1 
ATOM   1620 C  C   . PHE B 1 86  ? 42.491 20.268 18.984  1.00 38.64  ? 85  PHE B C   1 
ATOM   1621 O  O   . PHE B 1 86  ? 41.573 20.260 19.799  1.00 38.12  ? 85  PHE B O   1 
ATOM   1622 C  CB  . PHE B 1 86  ? 42.964 18.071 17.985  1.00 40.33  ? 85  PHE B CB  1 
ATOM   1623 C  CG  . PHE B 1 86  ? 43.940 16.961 17.696  1.00 42.47  ? 85  PHE B CG  1 
ATOM   1624 C  CD1 . PHE B 1 86  ? 43.784 15.707 18.298  1.00 45.12  ? 85  PHE B CD1 1 
ATOM   1625 C  CD2 . PHE B 1 86  ? 44.998 17.160 16.819  1.00 42.82  ? 85  PHE B CD2 1 
ATOM   1626 C  CE1 . PHE B 1 86  ? 44.681 14.659 18.023  1.00 46.01  ? 85  PHE B CE1 1 
ATOM   1627 C  CE2 . PHE B 1 86  ? 45.899 16.115 16.527  1.00 45.74  ? 85  PHE B CE2 1 
ATOM   1628 C  CZ  . PHE B 1 86  ? 45.733 14.869 17.140  1.00 44.85  ? 85  PHE B CZ  1 
ATOM   1629 N  N   . TYR B 1 87  ? 42.707 21.235 18.090  1.00 37.69  ? 86  TYR B N   1 
ATOM   1630 C  CA  . TYR B 1 87  ? 41.855 22.418 17.905  1.00 36.74  ? 86  TYR B CA  1 
ATOM   1631 C  C   . TYR B 1 87  ? 41.663 22.604 16.419  1.00 36.26  ? 86  TYR B C   1 
ATOM   1632 O  O   . TYR B 1 87  ? 42.631 22.557 15.671  1.00 36.15  ? 86  TYR B O   1 
ATOM   1633 C  CB  . TYR B 1 87  ? 42.505 23.667 18.501  1.00 36.62  ? 86  TYR B CB  1 
ATOM   1634 C  CG  . TYR B 1 87  ? 42.537 23.623 19.996  1.00 36.65  ? 86  TYR B CG  1 
ATOM   1635 C  CD1 . TYR B 1 87  ? 43.453 22.797 20.676  1.00 36.76  ? 86  TYR B CD1 1 
ATOM   1636 C  CD2 . TYR B 1 87  ? 41.639 24.370 20.746  1.00 35.97  ? 86  TYR B CD2 1 
ATOM   1637 C  CE1 . TYR B 1 87  ? 43.466 22.726 22.067  1.00 36.63  ? 86  TYR B CE1 1 
ATOM   1638 C  CE2 . TYR B 1 87  ? 41.636 24.309 22.123  1.00 35.95  ? 86  TYR B CE2 1 
ATOM   1639 C  CZ  . TYR B 1 87  ? 42.557 23.490 22.785  1.00 37.24  ? 86  TYR B CZ  1 
ATOM   1640 O  OH  . TYR B 1 87  ? 42.532 23.454 24.158  1.00 36.93  ? 86  TYR B OH  1 
ATOM   1641 N  N   . THR B 1 88  ? 40.418 22.815 15.997  1.00 35.49  ? 87  THR B N   1 
ATOM   1642 C  CA  . THR B 1 88  ? 40.080 22.946 14.575  1.00 35.23  ? 87  THR B CA  1 
ATOM   1643 C  C   . THR B 1 88  ? 39.463 24.314 14.256  1.00 34.78  ? 87  THR B C   1 
ATOM   1644 O  O   . THR B 1 88  ? 38.485 24.747 14.913  1.00 34.40  ? 87  THR B O   1 
ATOM   1645 C  CB  . THR B 1 88  ? 39.124 21.822 14.134  1.00 35.76  ? 87  THR B CB  1 
ATOM   1646 O  OG1 . THR B 1 88  ? 39.789 20.559 14.276  1.00 37.34  ? 87  THR B OG1 1 
ATOM   1647 C  CG2 . THR B 1 88  ? 38.699 21.984 12.655  1.00 33.55  ? 87  THR B CG2 1 
ATOM   1648 N  N   . LEU B 1 89  ? 40.049 24.992 13.272  1.00 33.40  ? 88  LEU B N   1 
ATOM   1649 C  CA  . LEU B 1 89  ? 39.548 26.284 12.823  1.00 33.10  ? 88  LEU B CA  1 
ATOM   1650 C  C   . LEU B 1 89  ? 38.668 26.057 11.613  1.00 33.06  ? 88  LEU B C   1 
ATOM   1651 O  O   . LEU B 1 89  ? 39.048 25.323 10.698  1.00 33.23  ? 88  LEU B O   1 
ATOM   1652 C  CB  . LEU B 1 89  ? 40.697 27.212 12.430  1.00 33.40  ? 88  LEU B CB  1 
ATOM   1653 C  CG  . LEU B 1 89  ? 40.346 28.546 11.777  1.00 32.11  ? 88  LEU B CG  1 
ATOM   1654 C  CD1 . LEU B 1 89  ? 39.626 29.505 12.756  1.00 31.07  ? 88  LEU B CD1 1 
ATOM   1655 C  CD2 . LEU B 1 89  ? 41.600 29.223 11.220  1.00 33.22  ? 88  LEU B CD2 1 
ATOM   1656 N  N   . HIS B 1 90  ? 37.483 26.671 11.623  1.00 32.01  ? 89  HIS B N   1 
ATOM   1657 C  CA  . HIS B 1 90  ? 36.567 26.628 10.482  1.00 31.39  ? 89  HIS B CA  1 
ATOM   1658 C  C   . HIS B 1 90  ? 36.589 28.051 9.910   1.00 31.86  ? 89  HIS B C   1 
ATOM   1659 O  O   . HIS B 1 90  ? 36.209 29.014 10.594  1.00 31.65  ? 89  HIS B O   1 
ATOM   1660 C  CB  . HIS B 1 90  ? 35.165 26.233 10.980  1.00 31.30  ? 89  HIS B CB  1 
ATOM   1661 C  CG  . HIS B 1 90  ? 34.111 26.180 9.909   1.00 31.24  ? 89  HIS B CG  1 
ATOM   1662 N  ND1 . HIS B 1 90  ? 32.869 26.752 10.071  1.00 30.73  ? 89  HIS B ND1 1 
ATOM   1663 C  CD2 . HIS B 1 90  ? 34.101 25.596 8.685   1.00 29.68  ? 89  HIS B CD2 1 
ATOM   1664 C  CE1 . HIS B 1 90  ? 32.134 26.530 8.994   1.00 30.14  ? 89  HIS B CE1 1 
ATOM   1665 N  NE2 . HIS B 1 90  ? 32.858 25.832 8.134   1.00 31.53  ? 89  HIS B NE2 1 
ATOM   1666 N  N   . VAL B 1 91  ? 37.094 28.188 8.688   1.00 31.76  ? 90  VAL B N   1 
ATOM   1667 C  CA  . VAL B 1 91  ? 37.170 29.482 8.022   1.00 31.98  ? 90  VAL B CA  1 
ATOM   1668 C  C   . VAL B 1 91  ? 35.963 29.583 7.098   1.00 32.27  ? 90  VAL B C   1 
ATOM   1669 O  O   . VAL B 1 91  ? 35.802 28.768 6.187   1.00 32.57  ? 90  VAL B O   1 
ATOM   1670 C  CB  . VAL B 1 91  ? 38.502 29.610 7.227   1.00 32.60  ? 90  VAL B CB  1 
ATOM   1671 C  CG1 . VAL B 1 91  ? 38.511 30.878 6.312   1.00 32.57  ? 90  VAL B CG1 1 
ATOM   1672 C  CG2 . VAL B 1 91  ? 39.688 29.661 8.216   1.00 31.87  ? 90  VAL B CG2 1 
ATOM   1673 N  N   . ILE B 1 92  ? 35.116 30.572 7.348   1.00 31.60  ? 91  ILE B N   1 
ATOM   1674 C  CA  . ILE B 1 92  ? 33.896 30.768 6.566   1.00 31.43  ? 91  ILE B CA  1 
ATOM   1675 C  C   . ILE B 1 92  ? 34.183 31.885 5.551   1.00 31.76  ? 91  ILE B C   1 
ATOM   1676 O  O   . ILE B 1 92  ? 34.325 33.058 5.923   1.00 31.20  ? 91  ILE B O   1 
ATOM   1677 C  CB  . ILE B 1 92  ? 32.676 31.128 7.477   1.00 31.21  ? 91  ILE B CB  1 
ATOM   1678 C  CG1 . ILE B 1 92  ? 32.462 30.031 8.542   1.00 31.30  ? 91  ILE B CG1 1 
ATOM   1679 C  CG2 . ILE B 1 92  ? 31.392 31.301 6.637   1.00 29.71  ? 91  ILE B CG2 1 
ATOM   1680 C  CD1 . ILE B 1 92  ? 31.681 30.459 9.837   1.00 32.61  ? 91  ILE B CD1 1 
ATOM   1681 N  N   . LYS B 1 93  ? 34.257 31.511 4.275   1.00 31.84  ? 92  LYS B N   1 
ATOM   1682 C  CA  . LYS B 1 93  ? 34.512 32.481 3.209   1.00 32.82  ? 92  LYS B CA  1 
ATOM   1683 C  C   . LYS B 1 93  ? 33.217 33.217 2.858   1.00 32.89  ? 92  LYS B C   1 
ATOM   1684 O  O   . LYS B 1 93  ? 32.106 32.723 3.129   1.00 32.80  ? 92  LYS B O   1 
ATOM   1685 C  CB  . LYS B 1 93  ? 35.085 31.797 1.961   1.00 32.49  ? 92  LYS B CB  1 
ATOM   1686 C  CG  . LYS B 1 93  ? 36.487 31.179 2.168   1.00 34.59  ? 92  LYS B CG  1 
ATOM   1687 C  CD  . LYS B 1 93  ? 37.430 31.455 0.954   1.00 37.00  ? 92  LYS B CD  1 
ATOM   1688 C  CE  . LYS B 1 93  ? 36.777 31.116 -0.404  1.00 37.58  ? 92  LYS B CE  1 
ATOM   1689 N  NZ  . LYS B 1 93  ? 36.548 29.639 -0.579  1.00 40.14  ? 92  LYS B NZ  1 
ATOM   1690 N  N   . SER B 1 94  ? 33.363 34.400 2.247   1.00 33.15  ? 93  SER B N   1 
ATOM   1691 C  CA  . SER B 1 94  ? 32.215 35.211 1.861   1.00 33.28  ? 93  SER B CA  1 
ATOM   1692 C  C   . SER B 1 94  ? 31.346 34.503 0.833   1.00 33.18  ? 93  SER B C   1 
ATOM   1693 O  O   . SER B 1 94  ? 30.157 34.793 0.756   1.00 33.37  ? 93  SER B O   1 
ATOM   1694 C  CB  . SER B 1 94  ? 32.647 36.592 1.335   1.00 34.06  ? 93  SER B CB  1 
ATOM   1695 O  OG  . SER B 1 94  ? 33.241 37.348 2.384   1.00 35.10  ? 93  SER B OG  1 
ATOM   1696 N  N   . ASP B 1 95  ? 31.924 33.574 0.067   1.00 32.74  ? 94  ASP B N   1 
ATOM   1697 C  CA  . ASP B 1 95  ? 31.139 32.784 -0.898  1.00 33.73  ? 94  ASP B CA  1 
ATOM   1698 C  C   . ASP B 1 95  ? 30.566 31.457 -0.332  1.00 33.88  ? 94  ASP B C   1 
ATOM   1699 O  O   . ASP B 1 95  ? 29.881 30.688 -1.055  1.00 33.30  ? 94  ASP B O   1 
ATOM   1700 C  CB  . ASP B 1 95  ? 31.929 32.553 -2.208  1.00 33.67  ? 94  ASP B CB  1 
ATOM   1701 C  CG  . ASP B 1 95  ? 33.146 31.649 -2.038  1.00 36.42  ? 94  ASP B CG  1 
ATOM   1702 O  OD1 . ASP B 1 95  ? 33.303 31.033 -0.956  1.00 37.31  ? 94  ASP B OD1 1 
ATOM   1703 O  OD2 . ASP B 1 95  ? 33.957 31.529 -3.000  1.00 36.72  ? 94  ASP B OD2 1 
ATOM   1704 N  N   . LEU B 1 96  ? 30.835 31.213 0.953   1.00 33.51  ? 95  LEU B N   1 
ATOM   1705 C  CA  . LEU B 1 96  ? 30.364 30.012 1.686   1.00 34.01  ? 95  LEU B CA  1 
ATOM   1706 C  C   . LEU B 1 96  ? 30.953 28.673 1.197   1.00 33.92  ? 95  LEU B C   1 
ATOM   1707 O  O   . LEU B 1 96  ? 30.450 27.592 1.542   1.00 33.72  ? 95  LEU B O   1 
ATOM   1708 C  CB  . LEU B 1 96  ? 28.835 29.995 1.797   1.00 33.69  ? 95  LEU B CB  1 
ATOM   1709 C  CG  . LEU B 1 96  ? 28.390 31.135 2.729   1.00 35.58  ? 95  LEU B CG  1 
ATOM   1710 C  CD1 . LEU B 1 96  ? 26.907 31.251 2.849   1.00 34.26  ? 95  LEU B CD1 1 
ATOM   1711 C  CD2 . LEU B 1 96  ? 28.978 30.911 4.124   1.00 37.53  ? 95  LEU B CD2 1 
ATOM   1712 N  N   . VAL B 1 97  ? 32.030 28.760 0.414   1.00 33.40  ? 96  VAL B N   1 
ATOM   1713 C  CA  . VAL B 1 97  ? 32.884 27.603 0.164   1.00 34.00  ? 96  VAL B CA  1 
ATOM   1714 C  C   . VAL B 1 97  ? 33.945 27.671 1.258   1.00 34.83  ? 96  VAL B C   1 
ATOM   1715 O  O   . VAL B 1 97  ? 34.845 28.515 1.207   1.00 35.60  ? 96  VAL B O   1 
ATOM   1716 C  CB  . VAL B 1 97  ? 33.461 27.626 -1.254  1.00 34.22  ? 96  VAL B CB  1 
ATOM   1717 C  CG1 . VAL B 1 97  ? 34.476 26.499 -1.467  1.00 33.43  ? 96  VAL B CG1 1 
ATOM   1718 C  CG2 . VAL B 1 97  ? 32.303 27.497 -2.279  1.00 34.67  ? 96  VAL B CG2 1 
ATOM   1719 N  N   . ASN B 1 98  ? 33.788 26.826 2.279   1.00 34.32  ? 97  ASN B N   1 
ATOM   1720 C  CA  . ASN B 1 98  ? 34.540 26.958 3.535   1.00 33.59  ? 97  ASN B CA  1 
ATOM   1721 C  C   . ASN B 1 98  ? 35.677 25.966 3.697   1.00 34.23  ? 97  ASN B C   1 
ATOM   1722 O  O   . ASN B 1 98  ? 35.704 24.935 3.003   1.00 34.09  ? 97  ASN B O   1 
ATOM   1723 C  CB  . ASN B 1 98  ? 33.545 26.883 4.711   1.00 33.33  ? 97  ASN B CB  1 
ATOM   1724 C  CG  . ASN B 1 98  ? 32.410 27.896 4.554   1.00 33.08  ? 97  ASN B CG  1 
ATOM   1725 O  OD1 . ASN B 1 98  ? 32.618 28.956 3.959   1.00 32.84  ? 97  ASN B OD1 1 
ATOM   1726 N  ND2 . ASN B 1 98  ? 31.206 27.559 5.035   1.00 30.30  ? 97  ASN B ND2 1 
ATOM   1727 N  N   . GLU B 1 99  ? 36.596 26.260 4.622   1.00 34.31  ? 98  GLU B N   1 
ATOM   1728 C  CA  . GLU B 1 99  ? 37.811 25.434 4.844   1.00 36.03  ? 98  GLU B CA  1 
ATOM   1729 C  C   . GLU B 1 99  ? 38.048 25.205 6.320   1.00 35.21  ? 98  GLU B C   1 
ATOM   1730 O  O   . GLU B 1 99  ? 37.663 26.047 7.138   1.00 34.60  ? 98  GLU B O   1 
ATOM   1731 C  CB  . GLU B 1 99  ? 39.046 26.228 4.417   1.00 36.64  ? 98  GLU B CB  1 
ATOM   1732 C  CG  . GLU B 1 99  ? 39.168 26.445 2.990   1.00 42.18  ? 98  GLU B CG  1 
ATOM   1733 C  CD  . GLU B 1 99  ? 40.496 27.063 2.650   1.00 46.91  ? 98  GLU B CD  1 
ATOM   1734 O  OE1 . GLU B 1 99  ? 40.511 27.926 1.761   1.00 49.37  ? 98  GLU B OE1 1 
ATOM   1735 O  OE2 . GLU B 1 99  ? 41.509 26.675 3.277   1.00 48.81  ? 98  GLU B OE2 1 
ATOM   1736 N  N   . GLU B 1 100 ? 38.776 24.129 6.642   1.00 34.96  ? 99  GLU B N   1 
ATOM   1737 C  CA  . GLU B 1 100 ? 39.196 23.826 8.021   1.00 35.28  ? 99  GLU B CA  1 
ATOM   1738 C  C   . GLU B 1 100 ? 40.709 23.548 8.098   1.00 35.94  ? 99  GLU B C   1 
ATOM   1739 O  O   . GLU B 1 100 ? 41.333 23.115 7.120   1.00 35.71  ? 99  GLU B O   1 
ATOM   1740 C  CB  . GLU B 1 100 ? 38.433 22.596 8.559   1.00 35.76  ? 99  GLU B CB  1 
ATOM   1741 C  CG  . GLU B 1 100 ? 36.898 22.662 8.483   1.00 36.87  ? 99  GLU B CG  1 
ATOM   1742 C  CD  . GLU B 1 100 ? 36.341 22.410 7.102   1.00 39.39  ? 99  GLU B CD  1 
ATOM   1743 O  OE1 . GLU B 1 100 ? 35.551 23.252 6.638   1.00 38.44  ? 99  GLU B OE1 1 
ATOM   1744 O  OE2 . GLU B 1 100 ? 36.691 21.383 6.472   1.00 40.71  ? 99  GLU B OE2 1 
ATOM   1745 N  N   . ALA B 1 101 ? 41.296 23.809 9.257   1.00 35.77  ? 100 ALA B N   1 
ATOM   1746 C  CA  . ALA B 1 101 ? 42.652 23.365 9.557   1.00 36.22  ? 100 ALA B CA  1 
ATOM   1747 C  C   . ALA B 1 101 ? 42.679 22.989 11.019  1.00 36.80  ? 100 ALA B C   1 
ATOM   1748 O  O   . ALA B 1 101 ? 41.979 23.604 11.826  1.00 36.22  ? 100 ALA B O   1 
ATOM   1749 C  CB  . ALA B 1 101 ? 43.646 24.447 9.292   1.00 36.06  ? 100 ALA B CB  1 
ATOM   1750 N  N   . THR B 1 102 ? 43.501 21.992 11.360  1.00 37.46  ? 101 THR B N   1 
ATOM   1751 C  CA  . THR B 1 102 ? 43.596 21.487 12.720  1.00 37.30  ? 101 THR B CA  1 
ATOM   1752 C  C   . THR B 1 102 ? 45.037 21.633 13.227  1.00 39.03  ? 101 THR B C   1 
ATOM   1753 O  O   . THR B 1 102 ? 46.013 21.402 12.476  1.00 38.50  ? 101 THR B O   1 
ATOM   1754 C  CB  . THR B 1 102 ? 43.142 20.018 12.769  1.00 37.59  ? 101 THR B CB  1 
ATOM   1755 O  OG1 . THR B 1 102 ? 41.777 19.916 12.337  1.00 37.29  ? 101 THR B OG1 1 
ATOM   1756 C  CG2 . THR B 1 102 ? 43.265 19.423 14.165  1.00 37.75  ? 101 THR B CG2 1 
ATOM   1757 N  N   . GLY B 1 103 ? 45.161 22.031 14.493  1.00 38.84  ? 102 GLY B N   1 
ATOM   1758 C  CA  . GLY B 1 103 ? 46.449 22.162 15.173  1.00 39.63  ? 102 GLY B CA  1 
ATOM   1759 C  C   . GLY B 1 103 ? 46.367 21.418 16.485  1.00 40.57  ? 102 GLY B C   1 
ATOM   1760 O  O   . GLY B 1 103 ? 45.312 20.873 16.829  1.00 39.53  ? 102 GLY B O   1 
ATOM   1761 N  N   . GLN B 1 104 ? 47.478 21.376 17.220  1.00 41.41  ? 103 GLN B N   1 
ATOM   1762 C  CA  . GLN B 1 104 ? 47.471 20.726 18.523  1.00 43.20  ? 103 GLN B CA  1 
ATOM   1763 C  C   . GLN B 1 104 ? 48.540 21.274 19.448  1.00 42.27  ? 103 GLN B C   1 
ATOM   1764 O  O   . GLN B 1 104 ? 49.502 21.902 19.011  1.00 41.72  ? 103 GLN B O   1 
ATOM   1765 C  CB  . GLN B 1 104 ? 47.590 19.192 18.399  1.00 43.74  ? 103 GLN B CB  1 
ATOM   1766 C  CG  . GLN B 1 104 ? 48.966 18.669 18.088  1.00 46.11  ? 103 GLN B CG  1 
ATOM   1767 C  CD  . GLN B 1 104 ? 49.067 17.140 18.219  1.00 46.67  ? 103 GLN B CD  1 
ATOM   1768 O  OE1 . GLN B 1 104 ? 48.925 16.560 19.314  1.00 49.72  ? 103 GLN B OE1 1 
ATOM   1769 N  NE2 . GLN B 1 104 ? 49.312 16.486 17.093  1.00 49.84  ? 103 GLN B NE2 1 
ATOM   1770 N  N   . PHE B 1 105 ? 48.333 21.068 20.737  1.00 42.66  ? 104 PHE B N   1 
ATOM   1771 C  CA  . PHE B 1 105 ? 49.384 21.340 21.711  1.00 43.29  ? 104 PHE B CA  1 
ATOM   1772 C  C   . PHE B 1 105 ? 49.320 20.352 22.872  1.00 43.82  ? 104 PHE B C   1 
ATOM   1773 O  O   . PHE B 1 105 ? 48.327 19.649 23.044  1.00 42.93  ? 104 PHE B O   1 
ATOM   1774 C  CB  . PHE B 1 105 ? 49.407 22.815 22.174  1.00 42.27  ? 104 PHE B CB  1 
ATOM   1775 C  CG  . PHE B 1 105 ? 48.166 23.262 22.932  1.00 42.78  ? 104 PHE B CG  1 
ATOM   1776 C  CD1 . PHE B 1 105 ? 47.139 23.956 22.276  1.00 42.11  ? 104 PHE B CD1 1 
ATOM   1777 C  CD2 . PHE B 1 105 ? 48.045 23.028 24.304  1.00 41.81  ? 104 PHE B CD2 1 
ATOM   1778 C  CE1 . PHE B 1 105 ? 46.011 24.394 22.984  1.00 41.76  ? 104 PHE B CE1 1 
ATOM   1779 C  CE2 . PHE B 1 105 ? 46.926 23.457 25.018  1.00 42.13  ? 104 PHE B CE2 1 
ATOM   1780 C  CZ  . PHE B 1 105 ? 45.894 24.140 24.348  1.00 40.95  ? 104 PHE B CZ  1 
ATOM   1781 N  N   . ARG B 1 106 ? 50.414 20.305 23.638  1.00 45.28  ? 105 ARG B N   1 
ATOM   1782 C  CA  . ARG B 1 106 ? 50.556 19.424 24.801  1.00 46.54  ? 105 ARG B CA  1 
ATOM   1783 C  C   . ARG B 1 106 ? 50.662 20.300 26.044  1.00 46.21  ? 105 ARG B C   1 
ATOM   1784 O  O   . ARG B 1 106 ? 51.107 21.438 25.959  1.00 45.91  ? 105 ARG B O   1 
ATOM   1785 C  CB  . ARG B 1 106 ? 51.837 18.590 24.661  1.00 46.70  ? 105 ARG B CB  1 
ATOM   1786 C  CG  . ARG B 1 106 ? 51.884 17.639 23.464  1.00 48.54  ? 105 ARG B CG  1 
ATOM   1787 C  CD  . ARG B 1 106 ? 53.169 16.774 23.496  1.00 49.17  ? 105 ARG B CD  1 
ATOM   1788 N  NE  . ARG B 1 106 ? 53.092 15.701 24.499  1.00 55.39  ? 105 ARG B NE  1 
ATOM   1789 C  CZ  . ARG B 1 106 ? 53.891 14.625 24.554  1.00 57.85  ? 105 ARG B CZ  1 
ATOM   1790 N  NH1 . ARG B 1 106 ? 53.703 13.729 25.522  1.00 58.39  ? 105 ARG B NH1 1 
ATOM   1791 N  NH2 . ARG B 1 106 ? 54.865 14.422 23.653  1.00 55.17  ? 105 ARG B NH2 1 
ATOM   1792 N  N   . VAL B 1 107 ? 50.269 19.770 27.202  1.00 47.29  ? 106 VAL B N   1 
ATOM   1793 C  CA  . VAL B 1 107 ? 50.385 20.512 28.471  1.00 48.31  ? 106 VAL B CA  1 
ATOM   1794 C  C   . VAL B 1 107 ? 51.271 19.731 29.458  1.00 49.86  ? 106 VAL B C   1 
ATOM   1795 O  O   . VAL B 1 107 ? 51.100 18.515 29.619  1.00 50.14  ? 106 VAL B O   1 
ATOM   1796 C  CB  . VAL B 1 107 ? 49.002 20.766 29.105  1.00 48.15  ? 106 VAL B CB  1 
ATOM   1797 C  CG1 . VAL B 1 107 ? 49.127 21.564 30.414  1.00 47.60  ? 106 VAL B CG1 1 
ATOM   1798 C  CG2 . VAL B 1 107 ? 48.066 21.496 28.104  1.00 47.22  ? 106 VAL B CG2 1 
ATOM   1799 N  N   . TYR B 1 108 ? 52.206 20.430 30.099  1.00 51.03  ? 107 TYR B N   1 
ATOM   1800 C  CA  . TYR B 1 108 ? 53.089 19.816 31.105  1.00 52.57  ? 107 TYR B CA  1 
ATOM   1801 C  C   . TYR B 1 108 ? 52.916 20.495 32.465  1.00 54.26  ? 107 TYR B C   1 
ATOM   1802 O  O   . TYR B 1 108 ? 52.689 21.707 32.521  1.00 54.07  ? 107 TYR B O   1 
ATOM   1803 C  CB  . TYR B 1 108 ? 54.566 19.867 30.673  1.00 51.64  ? 107 TYR B CB  1 
ATOM   1804 C  CG  A TYR B 1 108 ? 55.005 18.941 29.534  0.50 52.64  ? 107 TYR B CG  1 
ATOM   1805 C  CG  B TYR B 1 108 ? 55.218 21.229 30.571  0.50 50.57  ? 107 TYR B CG  1 
ATOM   1806 C  CD1 A TYR B 1 108 ? 54.749 19.256 28.190  0.50 52.32  ? 107 TYR B CD1 1 
ATOM   1807 C  CD1 B TYR B 1 108 ? 55.841 21.815 31.677  0.50 48.63  ? 107 TYR B CD1 1 
ATOM   1808 C  CD2 A TYR B 1 108 ? 55.738 17.776 29.805  0.50 52.91  ? 107 TYR B CD2 1 
ATOM   1809 C  CD2 B TYR B 1 108 ? 55.272 21.904 29.349  0.50 49.96  ? 107 TYR B CD2 1 
ATOM   1810 C  CE1 A TYR B 1 108 ? 55.177 18.410 27.157  0.50 51.85  ? 107 TYR B CE1 1 
ATOM   1811 C  CE1 B TYR B 1 108 ? 56.473 23.046 31.575  0.50 48.39  ? 107 TYR B CE1 1 
ATOM   1812 C  CE2 A TYR B 1 108 ? 56.171 16.934 28.784  0.50 52.12  ? 107 TYR B CE2 1 
ATOM   1813 C  CE2 B TYR B 1 108 ? 55.903 23.138 29.238  0.50 49.15  ? 107 TYR B CE2 1 
ATOM   1814 C  CZ  A TYR B 1 108 ? 55.894 17.248 27.463  0.50 52.42  ? 107 TYR B CZ  1 
ATOM   1815 C  CZ  B TYR B 1 108 ? 56.498 23.704 30.353  0.50 49.44  ? 107 TYR B CZ  1 
ATOM   1816 O  OH  A TYR B 1 108 ? 56.342 16.393 26.465  0.50 51.42  ? 107 TYR B OH  1 
ATOM   1817 O  OH  B TYR B 1 108 ? 57.117 24.932 30.239  0.50 50.11  ? 107 TYR B OH  1 
ATOM   1818 N  N   . PRO B 1 109 ? 53.049 19.722 33.568  1.00 56.24  ? 108 PRO B N   1 
ATOM   1819 C  CA  . PRO B 1 109 ? 52.875 20.246 34.939  1.00 57.33  ? 108 PRO B CA  1 
ATOM   1820 C  C   . PRO B 1 109 ? 53.891 21.326 35.335  1.00 58.10  ? 108 PRO B C   1 
ATOM   1821 O  O   . PRO B 1 109 ? 55.000 21.361 34.792  1.00 59.33  ? 108 PRO B O   1 
ATOM   1822 C  CB  . PRO B 1 109 ? 53.060 19.000 35.818  1.00 57.68  ? 108 PRO B CB  1 
ATOM   1823 C  CG  . PRO B 1 109 ? 53.923 18.070 34.977  1.00 57.46  ? 108 PRO B CG  1 
ATOM   1824 C  CD  . PRO B 1 109 ? 53.381 18.282 33.579  1.00 56.62  ? 108 PRO B CD  1 
HETATM 1825 CL CL  . CL  C 2 .   ? 28.780 8.844  1.871   1.00 54.54  ? 502 CL  A CL  1 
HETATM 1826 C  C1  . GOL D 3 .   ? 9.951  23.467 6.313   1.00 65.61  ? 202 GOL A C1  1 
HETATM 1827 O  O1  . GOL D 3 .   ? 9.873  22.770 7.558   1.00 60.96  ? 202 GOL A O1  1 
HETATM 1828 C  C2  . GOL D 3 .   ? 9.498  22.702 5.051   1.00 64.18  ? 202 GOL A C2  1 
HETATM 1829 O  O2  . GOL D 3 .   ? 8.256  23.256 4.688   1.00 65.17  ? 202 GOL A O2  1 
HETATM 1830 C  C3  . GOL D 3 .   ? 10.407 23.057 3.867   1.00 65.17  ? 202 GOL A C3  1 
HETATM 1831 O  O3  . GOL D 3 .   ? 10.701 21.965 3.005   1.00 62.01  ? 202 GOL A O3  1 
HETATM 1832 C  C1  . GOL E 3 .   ? 8.370  15.666 -9.514  1.00 70.48  ? 203 GOL A C1  1 
HETATM 1833 O  O1  . GOL E 3 .   ? 8.318  14.378 -8.925  1.00 69.54  ? 203 GOL A O1  1 
HETATM 1834 C  C2  . GOL E 3 .   ? 8.549  15.572 -11.026 1.00 70.42  ? 203 GOL A C2  1 
HETATM 1835 O  O2  . GOL E 3 .   ? 7.419  16.055 -11.732 1.00 69.82  ? 203 GOL A O2  1 
HETATM 1836 C  C3  . GOL E 3 .   ? 9.758  16.410 -11.400 1.00 70.79  ? 203 GOL A C3  1 
HETATM 1837 O  O3  . GOL E 3 .   ? 10.649 15.657 -12.190 1.00 70.38  ? 203 GOL A O3  1 
HETATM 1838 C  C1  . GOL F 3 .   ? 23.996 23.720 -12.932 1.00 74.92  ? 204 GOL A C1  1 
HETATM 1839 O  O1  . GOL F 3 .   ? 24.665 23.231 -11.776 1.00 75.45  ? 204 GOL A O1  1 
HETATM 1840 C  C2  . GOL F 3 .   ? 22.960 22.695 -13.411 1.00 74.16  ? 204 GOL A C2  1 
HETATM 1841 O  O2  . GOL F 3 .   ? 22.559 21.895 -12.328 1.00 75.14  ? 204 GOL A O2  1 
HETATM 1842 C  C3  . GOL F 3 .   ? 21.700 23.336 -13.978 1.00 72.65  ? 204 GOL A C3  1 
HETATM 1843 O  O3  . GOL F 3 .   ? 20.849 22.331 -14.491 1.00 70.19  ? 204 GOL A O3  1 
HETATM 1844 C  C1  . GOL G 3 .   ? 27.568 37.713 16.244  1.00 46.30  ? 201 GOL B C1  1 
HETATM 1845 O  O1  . GOL G 3 .   ? 27.401 38.056 17.618  1.00 51.57  ? 201 GOL B O1  1 
HETATM 1846 C  C2  . GOL G 3 .   ? 28.895 38.239 15.696  1.00 43.70  ? 201 GOL B C2  1 
HETATM 1847 O  O2  . GOL G 3 .   ? 28.977 39.641 15.895  1.00 40.90  ? 201 GOL B O2  1 
HETATM 1848 C  C3  . GOL G 3 .   ? 30.085 37.515 16.373  1.00 40.55  ? 201 GOL B C3  1 
HETATM 1849 O  O3  . GOL G 3 .   ? 31.330 37.994 15.906  1.00 34.43  ? 201 GOL B O3  1 
HETATM 1850 CL CL  . CL  H 2 .   ? 41.380 16.474 21.215  1.00 50.20  ? 501 CL  B CL  1 
HETATM 1851 O  O   . HOH I 4 .   ? 30.658 25.085 6.332   1.00 29.58  ? 304 HOH A O   1 
HETATM 1852 O  O   . HOH I 4 .   ? 28.622 31.784 -3.172  1.00 32.74  ? 305 HOH A O   1 
HETATM 1853 O  O   . HOH I 4 .   ? 12.695 27.053 -1.647  1.00 44.32  ? 306 HOH A O   1 
HETATM 1854 O  O   . HOH I 4 .   ? 33.974 14.289 -2.690  0.50 24.27  ? 307 HOH A O   1 
HETATM 1855 O  O   . HOH I 4 .   ? 12.371 17.727 -13.201 1.00 38.71  ? 311 HOH A O   1 
HETATM 1856 O  O   . HOH I 4 .   ? 35.696 23.698 0.325   1.00 39.95  ? 313 HOH A O   1 
HETATM 1857 O  O   . HOH I 4 .   ? 18.647 32.209 -5.719  1.00 37.23  ? 314 HOH A O   1 
HETATM 1858 O  O   . HOH I 4 .   ? 31.707 14.834 4.586   1.00 33.45  ? 315 HOH A O   1 
HETATM 1859 O  O   . HOH I 4 .   ? 21.230 14.792 11.009  1.00 35.77  ? 316 HOH A O   1 
HETATM 1860 O  O   . HOH I 4 .   ? 23.072 21.199 14.638  1.00 38.74  ? 317 HOH A O   1 
HETATM 1861 O  O   . HOH I 4 .   ? 13.579 7.636  -9.606  1.00 38.27  ? 324 HOH A O   1 
HETATM 1862 O  O   . HOH I 4 .   ? 28.249 23.706 13.523  0.50 29.84  ? 325 HOH A O   1 
HETATM 1863 O  O   . HOH I 4 .   ? 13.334 10.487 -9.324  1.00 42.35  ? 326 HOH A O   1 
HETATM 1864 O  O   . HOH I 4 .   ? 11.977 14.332 -6.257  1.00 43.59  ? 327 HOH A O   1 
HETATM 1865 O  O   . HOH I 4 .   ? 31.600 10.875 5.741   1.00 45.59  ? 331 HOH A O   1 
HETATM 1866 O  O   . HOH I 4 .   ? 11.647 5.441  -2.724  1.00 45.13  ? 332 HOH A O   1 
HETATM 1867 O  O   . HOH I 4 .   ? 8.919  21.691 -1.497  1.00 48.97  ? 333 HOH A O   1 
HETATM 1868 O  O   . HOH I 4 .   ? 18.278 14.757 8.882   1.00 42.82  ? 334 HOH A O   1 
HETATM 1869 O  O   . HOH I 4 .   ? 24.827 16.200 10.534  1.00 46.33  ? 335 HOH A O   1 
HETATM 1870 O  O   . HOH I 4 .   ? 20.049 18.617 12.943  1.00 44.91  ? 336 HOH A O   1 
HETATM 1871 O  O   . HOH I 4 .   ? 16.344 24.815 13.245  1.00 40.60  ? 337 HOH A O   1 
HETATM 1872 O  O   . HOH I 4 .   ? 20.377 30.636 16.986  1.00 47.55  ? 338 HOH A O   1 
HETATM 1873 O  O   . HOH I 4 .   ? 7.725  15.342 -0.793  1.00 55.08  ? 350 HOH A O   1 
HETATM 1874 O  O   . HOH I 4 .   ? 25.189 31.766 -8.678  1.00 44.66  ? 351 HOH A O   1 
HETATM 1875 O  O   . HOH I 4 .   ? 23.101 36.324 3.217   1.00 31.95  ? 352 HOH A O   1 
HETATM 1876 O  O   . HOH I 4 .   ? 24.674 38.596 2.223   1.00 42.86  ? 353 HOH A O   1 
HETATM 1877 O  O   . HOH I 4 .   ? 28.041 36.582 -2.640  1.00 41.52  ? 356 HOH A O   1 
HETATM 1878 O  O   . HOH I 4 .   ? 29.514 34.531 -3.574  1.00 37.03  ? 357 HOH A O   1 
HETATM 1879 O  O   . HOH I 4 .   ? 27.436 30.839 -9.544  1.00 41.83  ? 358 HOH A O   1 
HETATM 1880 O  O   . HOH I 4 .   ? 17.779 14.066 -14.463 1.00 54.23  ? 361 HOH A O   1 
HETATM 1881 O  O   . HOH I 4 .   ? 11.838 13.525 -8.865  1.00 76.58  ? 362 HOH A O   1 
HETATM 1882 O  O   . HOH I 4 .   ? 25.108 11.955 -15.144 1.00 46.91  ? 363 HOH A O   1 
HETATM 1883 O  O   . HOH I 4 .   ? 29.445 11.447 -4.526  1.00 48.14  ? 364 HOH A O   1 
HETATM 1884 O  O   . HOH I 4 .   ? 28.652 5.659  -10.994 1.00 48.80  ? 365 HOH A O   1 
HETATM 1885 O  O   . HOH I 4 .   ? 13.259 9.849  2.686   1.00 47.86  ? 366 HOH A O   1 
HETATM 1886 O  O   . HOH I 4 .   ? 17.357 11.395 4.243   1.00 49.15  ? 373 HOH A O   1 
HETATM 1887 O  O   . HOH I 4 .   ? 18.636 22.180 14.342  1.00 43.25  ? 374 HOH A O   1 
HETATM 1888 O  O   . HOH I 4 .   ? 16.618 29.876 15.086  1.00 50.59  ? 375 HOH A O   1 
HETATM 1889 O  O   . HOH I 4 .   ? 26.617 39.484 9.717   1.00 47.14  ? 377 HOH A O   1 
HETATM 1890 O  O   . HOH I 4 .   ? 24.876 38.110 8.290   1.00 46.64  ? 378 HOH A O   1 
HETATM 1891 O  O   . HOH I 4 .   ? 10.511 22.642 0.424   1.00 61.36  ? 382 HOH A O   1 
HETATM 1892 O  O   . HOH I 4 .   ? 33.962 13.626 5.153   1.00 54.02  ? 383 HOH A O   1 
HETATM 1893 O  O   . HOH I 4 .   ? 25.995 12.811 10.466  1.00 45.71  ? 384 HOH A O   1 
HETATM 1894 O  O   . HOH I 4 .   ? 21.077 10.186 7.568   1.00 51.88  ? 385 HOH A O   1 
HETATM 1895 O  O   . HOH I 4 .   ? 16.779 34.533 8.488   1.00 54.48  ? 387 HOH A O   1 
HETATM 1896 O  O   . HOH I 4 .   ? 16.215 36.441 11.305  1.00 54.21  ? 388 HOH A O   1 
HETATM 1897 O  O   . HOH I 4 .   ? 12.591 6.070  -7.668  1.00 45.27  ? 389 HOH A O   1 
HETATM 1898 O  O   . HOH I 4 .   ? 15.273 10.212 4.321   1.00 59.66  ? 390 HOH A O   1 
HETATM 1899 O  O   . HOH I 4 .   ? 22.945 8.679  -15.304 1.00 60.66  ? 391 HOH A O   1 
HETATM 1900 O  O   . HOH I 4 .   ? 28.487 38.486 -4.517  1.00 50.56  ? 392 HOH A O   1 
HETATM 1901 O  O   . HOH I 4 .   ? 34.703 18.616 10.393  1.00 51.57  ? 394 HOH A O   1 
HETATM 1902 O  O   . HOH I 4 .   ? 28.583 21.535 11.794  1.00 284.49 ? 396 HOH A O   1 
HETATM 1903 O  O   . HOH I 4 .   ? 35.366 27.454 -5.074  1.00 52.85  ? 397 HOH A O   1 
HETATM 1904 O  O   . HOH I 4 .   ? 29.616 7.061  -3.341  1.00 50.74  ? 400 HOH A O   1 
HETATM 1905 O  O   . HOH I 4 .   ? 27.916 5.549  -2.200  1.00 51.75  ? 402 HOH A O   1 
HETATM 1906 O  O   . HOH I 4 .   ? 23.104 5.443  0.877   1.00 58.56  ? 403 HOH A O   1 
HETATM 1907 O  O   . HOH I 4 .   ? 16.682 1.036  0.227   1.00 72.13  ? 404 HOH A O   1 
HETATM 1908 O  O   . HOH I 4 .   ? 10.546 7.706  -1.026  1.00 50.67  ? 405 HOH A O   1 
HETATM 1909 O  O   . HOH I 4 .   ? 24.345 15.793 -16.840 1.00 58.48  ? 406 HOH A O   1 
HETATM 1910 O  O   . HOH I 4 .   ? 22.382 18.035 -15.600 1.00 57.33  ? 407 HOH A O   1 
HETATM 1911 O  O   . HOH I 4 .   ? 18.671 15.791 11.655  1.00 57.34  ? 414 HOH A O   1 
HETATM 1912 O  O   . HOH I 4 .   ? 27.507 4.425  -4.469  1.00 55.60  ? 415 HOH A O   1 
HETATM 1913 O  O   . HOH I 4 .   ? 28.287 33.108 -8.762  1.00 54.26  ? 416 HOH A O   1 
HETATM 1914 O  O   . HOH I 4 .   ? 27.101 31.711 -11.837 1.00 51.37  ? 417 HOH A O   1 
HETATM 1915 O  O   . HOH I 4 .   ? 29.550 29.906 -10.284 1.00 55.02  ? 418 HOH A O   1 
HETATM 1916 O  O   . HOH I 4 .   ? 30.747 32.571 -7.427  1.00 52.90  ? 419 HOH A O   1 
HETATM 1917 O  O   . HOH I 4 .   ? 31.660 11.417 9.980   1.00 56.33  ? 423 HOH A O   1 
HETATM 1918 O  O   . HOH I 4 .   ? 26.812 16.079 -6.217  1.00 64.38  ? 424 HOH A O   1 
HETATM 1919 O  O   . HOH I 4 .   ? 26.870 38.965 12.708  1.00 54.18  ? 428 HOH A O   1 
HETATM 1920 O  O   . HOH I 4 .   ? 8.029  19.721 8.069   0.50 40.45  ? 429 HOH A O   1 
HETATM 1921 O  O   . HOH I 4 .   ? 9.211  10.646 -1.034  1.00 69.60  ? 430 HOH A O   1 
HETATM 1922 O  O   . HOH I 4 .   ? 8.330  12.866 0.485   1.00 65.42  ? 431 HOH A O   1 
HETATM 1923 O  O   . HOH I 4 .   ? 18.647 11.613 -17.738 0.50 40.85  ? 432 HOH A O   1 
HETATM 1924 O  O   . HOH I 4 .   ? 24.371 9.939  -16.857 0.50 42.17  ? 433 HOH A O   1 
HETATM 1925 O  O   . HOH I 4 .   ? 21.254 37.098 4.620   1.00 56.57  ? 434 HOH A O   1 
HETATM 1926 O  O   . HOH I 4 .   ? 23.038 9.994  9.214   0.50 40.67  ? 435 HOH A O   1 
HETATM 1927 O  O   . HOH I 4 .   ? 19.396 39.579 -4.245  1.00 54.25  ? 439 HOH A O   1 
HETATM 1928 O  O   . HOH I 4 .   ? 20.480 20.527 14.757  1.00 55.31  ? 440 HOH A O   1 
HETATM 1929 O  O   . HOH I 4 .   ? 25.004 10.195 9.601   0.50 36.29  ? 441 HOH A O   1 
HETATM 1930 O  O   . HOH I 4 .   ? 30.597 9.281  -0.745  1.00 64.95  ? 442 HOH A O   1 
HETATM 1931 O  O   . HOH I 4 .   ? 31.443 8.868  3.024   0.50 38.68  ? 443 HOH A O   1 
HETATM 1932 O  O   . HOH I 4 .   ? 8.047  15.592 -5.410  1.00 54.05  ? 444 HOH A O   1 
HETATM 1933 O  O   . HOH I 4 .   ? 26.201 4.207  -0.959  1.00 54.52  ? 445 HOH A O   1 
HETATM 1934 O  O   . HOH I 4 .   ? 37.758 25.029 -0.995  1.00 55.20  ? 453 HOH A O   1 
HETATM 1935 O  O   . HOH I 4 .   ? 39.706 22.765 0.949   1.00 62.13  ? 454 HOH A O   1 
HETATM 1936 O  O   . HOH I 4 .   ? 37.195 25.220 -4.135  1.00 53.99  ? 455 HOH A O   1 
HETATM 1937 O  O   . HOH I 4 .   ? 37.279 23.650 -6.472  1.00 64.68  ? 456 HOH A O   1 
HETATM 1938 O  O   . HOH I 4 .   ? 38.906 21.214 -6.532  1.00 66.26  ? 457 HOH A O   1 
HETATM 1939 O  O   . HOH I 4 .   ? 40.025 20.826 -1.646  1.00 63.09  ? 458 HOH A O   1 
HETATM 1940 O  O   . HOH I 4 .   ? 34.542 22.348 -8.645  1.00 56.64  ? 459 HOH A O   1 
HETATM 1941 O  O   . HOH I 4 .   ? 23.200 38.091 15.079  1.00 56.03  ? 460 HOH A O   1 
HETATM 1942 O  O   . HOH I 4 .   ? 28.996 11.229 -7.816  1.00 52.99  ? 461 HOH A O   1 
HETATM 1943 O  O   . HOH I 4 .   ? 25.653 26.569 -14.216 1.00 62.37  ? 462 HOH A O   1 
HETATM 1944 O  O   . HOH I 4 .   ? 16.755 17.417 -14.938 0.50 39.80  ? 463 HOH A O   1 
HETATM 1945 O  O   . HOH I 4 .   ? 36.919 16.869 9.125   1.00 74.02  ? 466 HOH A O   1 
HETATM 1946 O  O   . HOH I 4 .   ? 25.327 24.766 17.084  1.00 56.31  ? 469 HOH A O   1 
HETATM 1947 O  O   . HOH I 4 .   ? 11.840 26.461 5.013   1.00 52.41  ? 473 HOH A O   1 
HETATM 1948 O  O   . HOH I 4 .   ? 13.929 24.533 4.312   1.00 32.40  ? 481 HOH A O   1 
HETATM 1949 O  O   . HOH I 4 .   ? 20.609 16.186 14.111  1.00 70.58  ? 482 HOH A O   1 
HETATM 1950 O  O   . HOH I 4 .   ? 33.319 13.549 -2.085  0.50 33.51  ? 491 HOH A O   1 
HETATM 1951 O  O   . HOH I 4 .   ? 23.297 15.549 12.401  1.00 58.83  ? 492 HOH A O   1 
HETATM 1952 O  O   . HOH I 4 .   ? 22.235 24.743 17.282  1.00 63.14  ? 493 HOH A O   1 
HETATM 1953 O  O   . HOH J 4 .   ? 33.569 36.291 -2.472  1.00 48.13  ? 301 HOH B O   1 
HETATM 1954 O  O   . HOH J 4 .   ? 34.034 23.390 4.611   1.00 33.63  ? 302 HOH B O   1 
HETATM 1955 O  O   . HOH J 4 .   ? 34.438 20.329 24.051  1.00 33.50  ? 303 HOH B O   1 
HETATM 1956 O  O   . HOH J 4 .   ? 28.300 44.415 15.632  1.00 41.84  ? 308 HOH B O   1 
HETATM 1957 O  O   . HOH J 4 .   ? 57.618 24.152 22.754  1.00 36.40  ? 309 HOH B O   1 
HETATM 1958 O  O   . HOH J 4 .   ? 44.732 20.402 9.055   1.00 36.54  ? 310 HOH B O   1 
HETATM 1959 O  O   . HOH J 4 .   ? 31.429 27.554 12.350  1.00 37.46  ? 312 HOH B O   1 
HETATM 1960 O  O   . HOH J 4 .   ? 31.256 38.275 3.963   1.00 39.70  ? 318 HOH B O   1 
HETATM 1961 O  O   . HOH J 4 .   ? 35.725 29.576 -3.401  1.00 43.07  ? 319 HOH B O   1 
HETATM 1962 O  O   . HOH J 4 .   ? 37.468 42.614 11.564  1.00 41.38  ? 320 HOH B O   1 
HETATM 1963 O  O   . HOH J 4 .   ? 30.580 18.114 11.029  1.00 42.45  ? 321 HOH B O   1 
HETATM 1964 O  O   . HOH J 4 .   ? 27.735 25.867 18.278  1.00 39.27  ? 322 HOH B O   1 
HETATM 1965 O  O   . HOH J 4 .   ? 38.951 26.197 25.133  1.00 45.88  ? 323 HOH B O   1 
HETATM 1966 O  O   . HOH J 4 .   ? 54.523 27.672 28.703  1.00 44.23  ? 328 HOH B O   1 
HETATM 1967 O  O   . HOH J 4 .   ? 46.360 34.739 10.546  1.00 39.74  ? 329 HOH B O   1 
HETATM 1968 O  O   . HOH J 4 .   ? 35.655 18.657 17.320  1.00 38.96  ? 330 HOH B O   1 
HETATM 1969 O  O   . HOH J 4 .   ? 27.887 30.967 18.915  1.00 44.74  ? 339 HOH B O   1 
HETATM 1970 O  O   . HOH J 4 .   ? 30.548 31.071 18.597  1.00 62.38  ? 340 HOH B O   1 
HETATM 1971 O  O   . HOH J 4 .   ? 34.534 39.488 1.430   1.00 44.84  ? 341 HOH B O   1 
HETATM 1972 O  O   . HOH J 4 .   ? 31.630 39.382 7.913   1.00 35.36  ? 342 HOH B O   1 
HETATM 1973 O  O   . HOH J 4 .   ? 32.750 40.103 5.573   1.00 45.12  ? 343 HOH B O   1 
HETATM 1974 O  O   . HOH J 4 .   ? 40.715 20.030 9.822   1.00 43.86  ? 344 HOH B O   1 
HETATM 1975 O  O   . HOH J 4 .   ? 39.189 22.159 4.353   1.00 39.72  ? 345 HOH B O   1 
HETATM 1976 O  O   . HOH J 4 .   ? 47.348 22.759 10.490  1.00 38.91  ? 346 HOH B O   1 
HETATM 1977 O  O   . HOH J 4 .   ? 56.182 17.468 16.830  1.00 68.85  ? 347 HOH B O   1 
HETATM 1978 O  O   . HOH J 4 .   ? 49.547 16.796 26.945  1.00 49.30  ? 348 HOH B O   1 
HETATM 1979 O  O   . HOH J 4 .   ? 57.204 17.319 23.830  1.00 49.34  ? 349 HOH B O   1 
HETATM 1980 O  O   . HOH J 4 .   ? 27.540 38.922 1.370   1.00 41.76  ? 354 HOH B O   1 
HETATM 1981 O  O   . HOH J 4 .   ? 29.084 37.200 -0.103  1.00 40.92  ? 355 HOH B O   1 
HETATM 1982 O  O   . HOH J 4 .   ? 50.012 33.926 6.521   1.00 46.72  ? 359 HOH B O   1 
HETATM 1983 O  O   . HOH J 4 .   ? 47.069 34.553 7.070   1.00 57.71  ? 360 HOH B O   1 
HETATM 1984 O  O   . HOH J 4 .   ? 42.233 27.912 34.313  1.00 49.94  ? 367 HOH B O   1 
HETATM 1985 O  O   . HOH J 4 .   ? 42.906 19.410 33.956  1.00 46.51  ? 368 HOH B O   1 
HETATM 1986 O  O   . HOH J 4 .   ? 52.175 23.362 15.949  1.00 48.06  ? 369 HOH B O   1 
HETATM 1987 O  O   . HOH J 4 .   ? 38.127 39.336 4.302   1.00 51.60  ? 370 HOH B O   1 
HETATM 1988 O  O   . HOH J 4 .   ? 27.173 28.211 19.516  1.00 41.08  ? 371 HOH B O   1 
HETATM 1989 O  O   . HOH J 4 .   ? 29.219 24.919 14.328  0.50 32.32  ? 372 HOH B O   1 
HETATM 1990 O  O   . HOH J 4 .   ? 28.884 40.143 8.112   1.00 46.53  ? 376 HOH B O   1 
HETATM 1991 O  O   . HOH J 4 .   ? 54.213 23.988 17.166  1.00 60.58  ? 379 HOH B O   1 
HETATM 1992 O  O   . HOH J 4 .   ? 34.880 16.176 18.132  1.00 49.14  ? 380 HOH B O   1 
HETATM 1993 O  O   . HOH J 4 .   ? 37.556 15.117 17.318  1.00 45.88  ? 381 HOH B O   1 
HETATM 1994 O  O   . HOH J 4 .   ? 52.362 16.176 27.726  0.50 52.07  ? 386 HOH B O   1 
HETATM 1995 O  O   . HOH J 4 .   ? 53.245 29.809 27.440  1.00 48.34  ? 393 HOH B O   1 
HETATM 1996 O  O   . HOH J 4 .   ? 29.276 16.302 20.138  1.00 55.52  ? 395 HOH B O   1 
HETATM 1997 O  O   . HOH J 4 .   ? 47.764 32.446 31.885  1.00 56.22  ? 398 HOH B O   1 
HETATM 1998 O  O   . HOH J 4 .   ? 27.581 21.015 14.117  1.00 48.61  ? 399 HOH B O   1 
HETATM 1999 O  O   . HOH J 4 .   ? 43.431 39.070 8.678   1.00 52.12  ? 401 HOH B O   1 
HETATM 2000 O  O   . HOH J 4 .   ? 39.243 33.606 -1.479  1.00 54.76  ? 408 HOH B O   1 
HETATM 2001 O  O   . HOH J 4 .   ? 42.179 23.752 4.232   1.00 47.74  ? 409 HOH B O   1 
HETATM 2002 O  O   . HOH J 4 .   ? 41.897 37.027 4.710   1.00 57.76  ? 410 HOH B O   1 
HETATM 2003 O  O   . HOH J 4 .   ? 40.512 24.190 25.829  1.00 50.41  ? 411 HOH B O   1 
HETATM 2004 O  O   . HOH J 4 .   ? 39.682 22.287 29.171  1.00 49.55  ? 412 HOH B O   1 
HETATM 2005 O  O   . HOH J 4 .   ? 48.533 15.419 24.829  1.00 60.05  ? 413 HOH B O   1 
HETATM 2006 O  O   . HOH J 4 .   ? 29.145 39.464 3.513   1.00 48.28  ? 420 HOH B O   1 
HETATM 2007 O  O   . HOH J 4 .   ? 29.075 17.333 14.225  1.00 63.68  ? 421 HOH B O   1 
HETATM 2008 O  O   . HOH J 4 .   ? 28.402 15.169 11.726  1.00 54.05  ? 422 HOH B O   1 
HETATM 2009 O  O   . HOH J 4 .   ? 39.564 21.425 26.162  1.00 53.79  ? 425 HOH B O   1 
HETATM 2010 O  O   . HOH J 4 .   ? 39.483 17.284 23.982  0.50 39.72  ? 426 HOH B O   1 
HETATM 2011 O  O   . HOH J 4 .   ? 36.622 21.815 25.533  1.00 51.07  ? 427 HOH B O   1 
HETATM 2012 O  O   . HOH J 4 .   ? 30.486 16.785 22.624  1.00 58.21  ? 436 HOH B O   1 
HETATM 2013 O  O   . HOH J 4 .   ? 45.740 16.953 12.893  1.00 67.04  ? 437 HOH B O   1 
HETATM 2014 O  O   . HOH J 4 .   ? 36.928 13.454 14.727  1.00 55.39  ? 438 HOH B O   1 
HETATM 2015 O  O   . HOH J 4 .   ? 49.661 22.850 15.672  1.00 68.13  ? 446 HOH B O   1 
HETATM 2016 O  O   . HOH J 4 .   ? 46.410 22.082 7.997   1.00 62.81  ? 447 HOH B O   1 
HETATM 2017 O  O   . HOH J 4 .   ? 45.913 26.324 35.609  1.00 61.93  ? 448 HOH B O   1 
HETATM 2018 O  O   . HOH J 4 .   ? 47.879 34.214 13.064  1.00 53.00  ? 449 HOH B O   1 
HETATM 2019 O  O   . HOH J 4 .   ? 45.935 29.376 36.105  1.00 71.82  ? 450 HOH B O   1 
HETATM 2020 O  O   . HOH J 4 .   ? 34.892 34.503 -0.697  1.00 42.61  ? 451 HOH B O   1 
HETATM 2021 O  O   . HOH J 4 .   ? 38.377 27.622 0.191   1.00 54.72  ? 452 HOH B O   1 
HETATM 2022 O  O   . HOH J 4 .   ? 38.371 18.879 10.067  1.00 56.14  ? 464 HOH B O   1 
HETATM 2023 O  O   . HOH J 4 .   ? 34.667 44.264 7.263   1.00 54.86  ? 465 HOH B O   1 
HETATM 2024 O  O   . HOH J 4 .   ? 42.700 33.589 -1.491  1.00 57.89  ? 467 HOH B O   1 
HETATM 2025 O  O   . HOH J 4 .   ? 27.949 40.461 5.369   1.00 53.20  ? 468 HOH B O   1 
HETATM 2026 O  O   . HOH J 4 .   ? 30.272 42.661 9.044   1.00 52.13  ? 470 HOH B O   1 
HETATM 2027 O  O   . HOH J 4 .   ? 58.060 18.833 12.373  1.00 65.34  ? 471 HOH B O   1 
HETATM 2028 O  O   . HOH J 4 .   ? 43.483 15.815 12.623  0.50 42.39  ? 472 HOH B O   1 
HETATM 2029 O  O   . HOH J 4 .   ? 25.717 33.171 19.640  0.50 28.38  ? 474 HOH B O   1 
HETATM 2030 O  O   . HOH J 4 .   ? 27.073 32.063 20.907  0.50 21.48  ? 475 HOH B O   1 
HETATM 2031 O  O   . HOH J 4 .   ? 28.906 29.588 26.203  1.00 48.17  ? 476 HOH B O   1 
HETATM 2032 O  O   . HOH J 4 .   ? 33.439 34.982 30.601  1.00 48.18  ? 477 HOH B O   1 
HETATM 2033 O  O   . HOH J 4 .   ? 28.370 36.971 25.967  1.00 40.83  ? 478 HOH B O   1 
HETATM 2034 O  O   . HOH J 4 .   ? 38.590 38.326 34.051  1.00 153.58 ? 479 HOH B O   1 
HETATM 2035 O  O   . HOH J 4 .   ? 38.306 35.812 34.885  1.00 54.73  ? 480 HOH B O   1 
HETATM 2036 O  O   . HOH J 4 .   ? 40.385 39.637 2.028   1.00 67.06  ? 483 HOH B O   1 
HETATM 2037 O  O   . HOH J 4 .   ? 36.588 33.807 -2.910  1.00 57.90  ? 484 HOH B O   1 
HETATM 2038 O  O   . HOH J 4 .   ? 33.977 33.044 -5.164  1.00 51.17  ? 485 HOH B O   1 
HETATM 2039 O  O   . HOH J 4 .   ? 26.676 30.415 24.475  1.00 61.46  ? 486 HOH B O   1 
HETATM 2040 O  O   . HOH J 4 .   ? 26.292 32.365 22.630  0.50 40.38  ? 487 HOH B O   1 
HETATM 2041 O  O   . HOH J 4 .   ? 37.032 24.583 26.178  1.00 55.74  ? 488 HOH B O   1 
HETATM 2042 O  O   . HOH J 4 .   ? 48.314 16.826 22.376  1.00 58.25  ? 489 HOH B O   1 
HETATM 2043 O  O   . HOH J 4 .   ? 41.462 17.011 11.400  1.00 50.79  ? 490 HOH B O   1 
# 