data_9JBO
# 
_entry.id   9JBO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9JBO         pdb_00009jbo 10.2210/pdb9jbo/pdb 
WWPDB D_1300050787 ?            ?                   
EMDB  EMD-61321    ?            ?                   
# 
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 2025-01-15 
2 'Structure model' 1 1 2025-02-05 
# 
_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' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
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 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
# 
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  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
13 2 'Structure model' '_citation_author.identifier_ORCID' 
14 2 'Structure model' '_citation_author.name'             
15 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JBO 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of human SOD1 (WT) amyloid filament' 
_pdbx_database_related.db_id          EMD-61321 
_pdbx_database_related.content_type   'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 shroh@snu.ac.kr   Soung-Hun Roh ? 'principal investigator/group leader' 0000-0003-3851-7200 
4 hanc210@snu.ac.kr Nam-Chul  Ha  ? 'principal investigator/group leader' 0000-0003-4813-748X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Baek, Y.'   1 0000-0001-5119-1829 
'Kim, H.'    2 0000-0001-5227-4319 
'Lee, D.'    3 ?                   
'Kim, D.'    4 ?                   
'Jo, E.'     5 ?                   
'Roh, S.-H.' 6 0000-0003-3851-7200 
'Ha, N.-C.'  7 0000-0003-4813-748X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2408582122 
_citation.page_last                 e2408582122 
_citation.title                     
'Structural insights into the role of reduced cysteine residues in SOD1 amyloid filament formation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2408582122 
_citation.pdbx_database_id_PubMed   39874287 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Baek, Y.'  1 0000-0001-5119-1829 
primary 'Kim, H.'   2 ?                   
primary 'Lee, D.'   3 ?                   
primary 'Kim, D.'   4 0009-0000-7960-0401 
primary 'Jo, E.'    5 0009-0001-6533-6643 
primary 'Roh, S.H.' 6 0000-0003-3851-7200 
primary 'Ha, N.C.'  7 0000-0003-4813-748X 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Superoxide dismutase [Cu-Zn]' 
_entity.formula_weight             16706.570 
_entity.pdbx_number_of_molecules   3 
_entity.pdbx_ec                    1.15.1.1 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_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       
;GAMDPEFMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIA
Q
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMDPEFMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIA
Q
;
_entity_poly.pdbx_strand_id                 C,B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ASP n 
1 5   PRO n 
1 6   GLU n 
1 7   PHE n 
1 8   MET n 
1 9   ALA n 
1 10  THR n 
1 11  LYS n 
1 12  ALA n 
1 13  VAL n 
1 14  CYS n 
1 15  VAL n 
1 16  LEU n 
1 17  LYS n 
1 18  GLY n 
1 19  ASP n 
1 20  GLY n 
1 21  PRO n 
1 22  VAL n 
1 23  GLN n 
1 24  GLY n 
1 25  ILE n 
1 26  ILE n 
1 27  ASN n 
1 28  PHE n 
1 29  GLU n 
1 30  GLN n 
1 31  LYS n 
1 32  GLU n 
1 33  SER n 
1 34  ASN n 
1 35  GLY n 
1 36  PRO n 
1 37  VAL n 
1 38  LYS n 
1 39  VAL n 
1 40  TRP n 
1 41  GLY n 
1 42  SER n 
1 43  ILE n 
1 44  LYS n 
1 45  GLY n 
1 46  LEU n 
1 47  THR n 
1 48  GLU n 
1 49  GLY n 
1 50  LEU n 
1 51  HIS n 
1 52  GLY n 
1 53  PHE n 
1 54  HIS n 
1 55  VAL n 
1 56  HIS n 
1 57  GLU n 
1 58  PHE n 
1 59  GLY n 
1 60  ASP n 
1 61  ASN n 
1 62  THR n 
1 63  ALA n 
1 64  GLY n 
1 65  CYS n 
1 66  THR n 
1 67  SER n 
1 68  ALA n 
1 69  GLY n 
1 70  PRO n 
1 71  HIS n 
1 72  PHE n 
1 73  ASN n 
1 74  PRO n 
1 75  LEU n 
1 76  SER n 
1 77  ARG n 
1 78  LYS n 
1 79  HIS n 
1 80  GLY n 
1 81  GLY n 
1 82  PRO n 
1 83  LYS n 
1 84  ASP n 
1 85  GLU n 
1 86  GLU n 
1 87  ARG n 
1 88  HIS n 
1 89  VAL n 
1 90  GLY n 
1 91  ASP n 
1 92  LEU n 
1 93  GLY n 
1 94  ASN n 
1 95  VAL n 
1 96  THR n 
1 97  ALA n 
1 98  ASP n 
1 99  LYS n 
1 100 ASP n 
1 101 GLY n 
1 102 VAL n 
1 103 ALA n 
1 104 ASP n 
1 105 VAL n 
1 106 SER n 
1 107 ILE n 
1 108 GLU n 
1 109 ASP n 
1 110 SER n 
1 111 VAL n 
1 112 ILE n 
1 113 SER n 
1 114 LEU n 
1 115 SER n 
1 116 GLY n 
1 117 ASP n 
1 118 HIS n 
1 119 CYS n 
1 120 ILE n 
1 121 ILE n 
1 122 GLY n 
1 123 ARG n 
1 124 THR n 
1 125 LEU n 
1 126 VAL n 
1 127 VAL n 
1 128 HIS n 
1 129 GLU n 
1 130 LYS n 
1 131 ALA n 
1 132 ASP n 
1 133 ASP n 
1 134 LEU n 
1 135 GLY n 
1 136 LYS n 
1 137 GLY n 
1 138 GLY n 
1 139 ASN n 
1 140 GLU n 
1 141 GLU n 
1 142 SER n 
1 143 THR n 
1 144 LYS n 
1 145 THR n 
1 146 GLY n 
1 147 ASN n 
1 148 ALA n 
1 149 GLY n 
1 150 SER n 
1 151 ARG n 
1 152 LEU n 
1 153 ALA n 
1 154 CYS n 
1 155 GLY n 
1 156 VAL n 
1 157 ILE n 
1 158 GLY n 
1 159 ILE n 
1 160 ALA n 
1 161 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   161 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -7  ?   ?   ?   C . n 
A 1 2   ALA 2   -6  ?   ?   ?   C . n 
A 1 3   MET 3   -5  ?   ?   ?   C . n 
A 1 4   ASP 4   -4  ?   ?   ?   C . n 
A 1 5   PRO 5   -3  ?   ?   ?   C . n 
A 1 6   GLU 6   -2  ?   ?   ?   C . n 
A 1 7   PHE 7   -1  ?   ?   ?   C . n 
A 1 8   MET 8   0   ?   ?   ?   C . n 
A 1 9   ALA 9   1   1   ALA ALA C . n 
A 1 10  THR 10  2   2   THR THR C . n 
A 1 11  LYS 11  3   3   LYS LYS C . n 
A 1 12  ALA 12  4   4   ALA ALA C . n 
A 1 13  VAL 13  5   5   VAL VAL C . n 
A 1 14  CYS 14  6   6   CYS CYS C . n 
A 1 15  VAL 15  7   7   VAL VAL C . n 
A 1 16  LEU 16  8   8   LEU LEU C . n 
A 1 17  LYS 17  9   9   LYS LYS C . n 
A 1 18  GLY 18  10  10  GLY GLY C . n 
A 1 19  ASP 19  11  11  ASP ASP C . n 
A 1 20  GLY 20  12  12  GLY GLY C . n 
A 1 21  PRO 21  13  13  PRO PRO C . n 
A 1 22  VAL 22  14  14  VAL VAL C . n 
A 1 23  GLN 23  15  15  GLN GLN C . n 
A 1 24  GLY 24  16  16  GLY GLY C . n 
A 1 25  ILE 25  17  17  ILE ILE C . n 
A 1 26  ILE 26  18  18  ILE ILE C . n 
A 1 27  ASN 27  19  19  ASN ASN C . n 
A 1 28  PHE 28  20  20  PHE PHE C . n 
A 1 29  GLU 29  21  21  GLU GLU C . n 
A 1 30  GLN 30  22  22  GLN GLN C . n 
A 1 31  LYS 31  23  23  LYS LYS C . n 
A 1 32  GLU 32  24  24  GLU GLU C . n 
A 1 33  SER 33  25  25  SER SER C . n 
A 1 34  ASN 34  26  26  ASN ASN C . n 
A 1 35  GLY 35  27  27  GLY GLY C . n 
A 1 36  PRO 36  28  28  PRO PRO C . n 
A 1 37  VAL 37  29  29  VAL VAL C . n 
A 1 38  LYS 38  30  30  LYS LYS C . n 
A 1 39  VAL 39  31  31  VAL VAL C . n 
A 1 40  TRP 40  32  32  TRP TRP C . n 
A 1 41  GLY 41  33  33  GLY GLY C . n 
A 1 42  SER 42  34  34  SER SER C . n 
A 1 43  ILE 43  35  35  ILE ILE C . n 
A 1 44  LYS 44  36  36  LYS LYS C . n 
A 1 45  GLY 45  37  37  GLY GLY C . n 
A 1 46  LEU 46  38  38  LEU LEU C . n 
A 1 47  THR 47  39  39  THR THR C . n 
A 1 48  GLU 48  40  40  GLU GLU C . n 
A 1 49  GLY 49  41  41  GLY GLY C . n 
A 1 50  LEU 50  42  42  LEU LEU C . n 
A 1 51  HIS 51  43  43  HIS HIS C . n 
A 1 52  GLY 52  44  44  GLY GLY C . n 
A 1 53  PHE 53  45  45  PHE PHE C . n 
A 1 54  HIS 54  46  ?   ?   ?   C . n 
A 1 55  VAL 55  47  ?   ?   ?   C . n 
A 1 56  HIS 56  48  ?   ?   ?   C . n 
A 1 57  GLU 57  49  ?   ?   ?   C . n 
A 1 58  PHE 58  50  ?   ?   ?   C . n 
A 1 59  GLY 59  51  ?   ?   ?   C . n 
A 1 60  ASP 60  52  ?   ?   ?   C . n 
A 1 61  ASN 61  53  ?   ?   ?   C . n 
A 1 62  THR 62  54  ?   ?   ?   C . n 
A 1 63  ALA 63  55  ?   ?   ?   C . n 
A 1 64  GLY 64  56  ?   ?   ?   C . n 
A 1 65  CYS 65  57  ?   ?   ?   C . n 
A 1 66  THR 66  58  ?   ?   ?   C . n 
A 1 67  SER 67  59  ?   ?   ?   C . n 
A 1 68  ALA 68  60  ?   ?   ?   C . n 
A 1 69  GLY 69  61  ?   ?   ?   C . n 
A 1 70  PRO 70  62  ?   ?   ?   C . n 
A 1 71  HIS 71  63  ?   ?   ?   C . n 
A 1 72  PHE 72  64  ?   ?   ?   C . n 
A 1 73  ASN 73  65  ?   ?   ?   C . n 
A 1 74  PRO 74  66  ?   ?   ?   C . n 
A 1 75  LEU 75  67  ?   ?   ?   C . n 
A 1 76  SER 76  68  ?   ?   ?   C . n 
A 1 77  ARG 77  69  ?   ?   ?   C . n 
A 1 78  LYS 78  70  ?   ?   ?   C . n 
A 1 79  HIS 79  71  ?   ?   ?   C . n 
A 1 80  GLY 80  72  ?   ?   ?   C . n 
A 1 81  GLY 81  73  ?   ?   ?   C . n 
A 1 82  PRO 82  74  ?   ?   ?   C . n 
A 1 83  LYS 83  75  ?   ?   ?   C . n 
A 1 84  ASP 84  76  ?   ?   ?   C . n 
A 1 85  GLU 85  77  ?   ?   ?   C . n 
A 1 86  GLU 86  78  ?   ?   ?   C . n 
A 1 87  ARG 87  79  ?   ?   ?   C . n 
A 1 88  HIS 88  80  ?   ?   ?   C . n 
A 1 89  VAL 89  81  81  VAL VAL C . n 
A 1 90  GLY 90  82  82  GLY GLY C . n 
A 1 91  ASP 91  83  83  ASP ASP C . n 
A 1 92  LEU 92  84  84  LEU LEU C . n 
A 1 93  GLY 93  85  85  GLY GLY C . n 
A 1 94  ASN 94  86  86  ASN ASN C . n 
A 1 95  VAL 95  87  87  VAL VAL C . n 
A 1 96  THR 96  88  88  THR THR C . n 
A 1 97  ALA 97  89  89  ALA ALA C . n 
A 1 98  ASP 98  90  90  ASP ASP C . n 
A 1 99  LYS 99  91  91  LYS LYS C . n 
A 1 100 ASP 100 92  92  ASP ASP C . n 
A 1 101 GLY 101 93  93  GLY GLY C . n 
A 1 102 VAL 102 94  94  VAL VAL C . n 
A 1 103 ALA 103 95  95  ALA ALA C . n 
A 1 104 ASP 104 96  96  ASP ASP C . n 
A 1 105 VAL 105 97  97  VAL VAL C . n 
A 1 106 SER 106 98  98  SER SER C . n 
A 1 107 ILE 107 99  99  ILE ILE C . n 
A 1 108 GLU 108 100 100 GLU GLU C . n 
A 1 109 ASP 109 101 101 ASP ASP C . n 
A 1 110 SER 110 102 102 SER SER C . n 
A 1 111 VAL 111 103 103 VAL VAL C . n 
A 1 112 ILE 112 104 104 ILE ILE C . n 
A 1 113 SER 113 105 105 SER SER C . n 
A 1 114 LEU 114 106 106 LEU LEU C . n 
A 1 115 SER 115 107 107 SER SER C . n 
A 1 116 GLY 116 108 108 GLY GLY C . n 
A 1 117 ASP 117 109 109 ASP ASP C . n 
A 1 118 HIS 118 110 110 HIS HIS C . n 
A 1 119 CYS 119 111 111 CYS CYS C . n 
A 1 120 ILE 120 112 112 ILE ILE C . n 
A 1 121 ILE 121 113 113 ILE ILE C . n 
A 1 122 GLY 122 114 114 GLY GLY C . n 
A 1 123 ARG 123 115 115 ARG ARG C . n 
A 1 124 THR 124 116 116 THR THR C . n 
A 1 125 LEU 125 117 117 LEU LEU C . n 
A 1 126 VAL 126 118 118 VAL VAL C . n 
A 1 127 VAL 127 119 119 VAL VAL C . n 
A 1 128 HIS 128 120 120 HIS HIS C . n 
A 1 129 GLU 129 121 121 GLU GLU C . n 
A 1 130 LYS 130 122 ?   ?   ?   C . n 
A 1 131 ALA 131 123 ?   ?   ?   C . n 
A 1 132 ASP 132 124 ?   ?   ?   C . n 
A 1 133 ASP 133 125 ?   ?   ?   C . n 
A 1 134 LEU 134 126 ?   ?   ?   C . n 
A 1 135 GLY 135 127 ?   ?   ?   C . n 
A 1 136 LYS 136 128 ?   ?   ?   C . n 
A 1 137 GLY 137 129 ?   ?   ?   C . n 
A 1 138 GLY 138 130 ?   ?   ?   C . n 
A 1 139 ASN 139 131 ?   ?   ?   C . n 
A 1 140 GLU 140 132 ?   ?   ?   C . n 
A 1 141 GLU 141 133 ?   ?   ?   C . n 
A 1 142 SER 142 134 ?   ?   ?   C . n 
A 1 143 THR 143 135 ?   ?   ?   C . n 
A 1 144 LYS 144 136 ?   ?   ?   C . n 
A 1 145 THR 145 137 ?   ?   ?   C . n 
A 1 146 GLY 146 138 ?   ?   ?   C . n 
A 1 147 ASN 147 139 ?   ?   ?   C . n 
A 1 148 ALA 148 140 ?   ?   ?   C . n 
A 1 149 GLY 149 141 ?   ?   ?   C . n 
A 1 150 SER 150 142 ?   ?   ?   C . n 
A 1 151 ARG 151 143 ?   ?   ?   C . n 
A 1 152 LEU 152 144 ?   ?   ?   C . n 
A 1 153 ALA 153 145 ?   ?   ?   C . n 
A 1 154 CYS 154 146 ?   ?   ?   C . n 
A 1 155 GLY 155 147 ?   ?   ?   C . n 
A 1 156 VAL 156 148 ?   ?   ?   C . n 
A 1 157 ILE 157 149 ?   ?   ?   C . n 
A 1 158 GLY 158 150 ?   ?   ?   C . n 
A 1 159 ILE 159 151 ?   ?   ?   C . n 
A 1 160 ALA 160 152 ?   ?   ?   C . n 
A 1 161 GLN 161 153 ?   ?   ?   C . n 
B 1 1   GLY 1   -7  ?   ?   ?   B . n 
B 1 2   ALA 2   -6  ?   ?   ?   B . n 
B 1 3   MET 3   -5  ?   ?   ?   B . n 
B 1 4   ASP 4   -4  ?   ?   ?   B . n 
B 1 5   PRO 5   -3  ?   ?   ?   B . n 
B 1 6   GLU 6   -2  ?   ?   ?   B . n 
B 1 7   PHE 7   -1  ?   ?   ?   B . n 
B 1 8   MET 8   0   ?   ?   ?   B . n 
B 1 9   ALA 9   1   1   ALA ALA B . n 
B 1 10  THR 10  2   2   THR THR B . n 
B 1 11  LYS 11  3   3   LYS LYS B . n 
B 1 12  ALA 12  4   4   ALA ALA B . n 
B 1 13  VAL 13  5   5   VAL VAL B . n 
B 1 14  CYS 14  6   6   CYS CYS B . n 
B 1 15  VAL 15  7   7   VAL VAL B . n 
B 1 16  LEU 16  8   8   LEU LEU B . n 
B 1 17  LYS 17  9   9   LYS LYS B . n 
B 1 18  GLY 18  10  10  GLY GLY B . n 
B 1 19  ASP 19  11  11  ASP ASP B . n 
B 1 20  GLY 20  12  12  GLY GLY B . n 
B 1 21  PRO 21  13  13  PRO PRO B . n 
B 1 22  VAL 22  14  14  VAL VAL B . n 
B 1 23  GLN 23  15  15  GLN GLN B . n 
B 1 24  GLY 24  16  16  GLY GLY B . n 
B 1 25  ILE 25  17  17  ILE ILE B . n 
B 1 26  ILE 26  18  18  ILE ILE B . n 
B 1 27  ASN 27  19  19  ASN ASN B . n 
B 1 28  PHE 28  20  20  PHE PHE B . n 
B 1 29  GLU 29  21  21  GLU GLU B . n 
B 1 30  GLN 30  22  22  GLN GLN B . n 
B 1 31  LYS 31  23  23  LYS LYS B . n 
B 1 32  GLU 32  24  24  GLU GLU B . n 
B 1 33  SER 33  25  25  SER SER B . n 
B 1 34  ASN 34  26  26  ASN ASN B . n 
B 1 35  GLY 35  27  27  GLY GLY B . n 
B 1 36  PRO 36  28  28  PRO PRO B . n 
B 1 37  VAL 37  29  29  VAL VAL B . n 
B 1 38  LYS 38  30  30  LYS LYS B . n 
B 1 39  VAL 39  31  31  VAL VAL B . n 
B 1 40  TRP 40  32  32  TRP TRP B . n 
B 1 41  GLY 41  33  33  GLY GLY B . n 
B 1 42  SER 42  34  34  SER SER B . n 
B 1 43  ILE 43  35  35  ILE ILE B . n 
B 1 44  LYS 44  36  36  LYS LYS B . n 
B 1 45  GLY 45  37  37  GLY GLY B . n 
B 1 46  LEU 46  38  38  LEU LEU B . n 
B 1 47  THR 47  39  39  THR THR B . n 
B 1 48  GLU 48  40  40  GLU GLU B . n 
B 1 49  GLY 49  41  41  GLY GLY B . n 
B 1 50  LEU 50  42  42  LEU LEU B . n 
B 1 51  HIS 51  43  43  HIS HIS B . n 
B 1 52  GLY 52  44  44  GLY GLY B . n 
B 1 53  PHE 53  45  45  PHE PHE B . n 
B 1 54  HIS 54  46  ?   ?   ?   B . n 
B 1 55  VAL 55  47  ?   ?   ?   B . n 
B 1 56  HIS 56  48  ?   ?   ?   B . n 
B 1 57  GLU 57  49  ?   ?   ?   B . n 
B 1 58  PHE 58  50  ?   ?   ?   B . n 
B 1 59  GLY 59  51  ?   ?   ?   B . n 
B 1 60  ASP 60  52  ?   ?   ?   B . n 
B 1 61  ASN 61  53  ?   ?   ?   B . n 
B 1 62  THR 62  54  ?   ?   ?   B . n 
B 1 63  ALA 63  55  ?   ?   ?   B . n 
B 1 64  GLY 64  56  ?   ?   ?   B . n 
B 1 65  CYS 65  57  ?   ?   ?   B . n 
B 1 66  THR 66  58  ?   ?   ?   B . n 
B 1 67  SER 67  59  ?   ?   ?   B . n 
B 1 68  ALA 68  60  ?   ?   ?   B . n 
B 1 69  GLY 69  61  ?   ?   ?   B . n 
B 1 70  PRO 70  62  ?   ?   ?   B . n 
B 1 71  HIS 71  63  ?   ?   ?   B . n 
B 1 72  PHE 72  64  ?   ?   ?   B . n 
B 1 73  ASN 73  65  ?   ?   ?   B . n 
B 1 74  PRO 74  66  ?   ?   ?   B . n 
B 1 75  LEU 75  67  ?   ?   ?   B . n 
B 1 76  SER 76  68  ?   ?   ?   B . n 
B 1 77  ARG 77  69  ?   ?   ?   B . n 
B 1 78  LYS 78  70  ?   ?   ?   B . n 
B 1 79  HIS 79  71  ?   ?   ?   B . n 
B 1 80  GLY 80  72  ?   ?   ?   B . n 
B 1 81  GLY 81  73  ?   ?   ?   B . n 
B 1 82  PRO 82  74  ?   ?   ?   B . n 
B 1 83  LYS 83  75  ?   ?   ?   B . n 
B 1 84  ASP 84  76  ?   ?   ?   B . n 
B 1 85  GLU 85  77  ?   ?   ?   B . n 
B 1 86  GLU 86  78  ?   ?   ?   B . n 
B 1 87  ARG 87  79  ?   ?   ?   B . n 
B 1 88  HIS 88  80  ?   ?   ?   B . n 
B 1 89  VAL 89  81  81  VAL VAL B . n 
B 1 90  GLY 90  82  82  GLY GLY B . n 
B 1 91  ASP 91  83  83  ASP ASP B . n 
B 1 92  LEU 92  84  84  LEU LEU B . n 
B 1 93  GLY 93  85  85  GLY GLY B . n 
B 1 94  ASN 94  86  86  ASN ASN B . n 
B 1 95  VAL 95  87  87  VAL VAL B . n 
B 1 96  THR 96  88  88  THR THR B . n 
B 1 97  ALA 97  89  89  ALA ALA B . n 
B 1 98  ASP 98  90  90  ASP ASP B . n 
B 1 99  LYS 99  91  91  LYS LYS B . n 
B 1 100 ASP 100 92  92  ASP ASP B . n 
B 1 101 GLY 101 93  93  GLY GLY B . n 
B 1 102 VAL 102 94  94  VAL VAL B . n 
B 1 103 ALA 103 95  95  ALA ALA B . n 
B 1 104 ASP 104 96  96  ASP ASP B . n 
B 1 105 VAL 105 97  97  VAL VAL B . n 
B 1 106 SER 106 98  98  SER SER B . n 
B 1 107 ILE 107 99  99  ILE ILE B . n 
B 1 108 GLU 108 100 100 GLU GLU B . n 
B 1 109 ASP 109 101 101 ASP ASP B . n 
B 1 110 SER 110 102 102 SER SER B . n 
B 1 111 VAL 111 103 103 VAL VAL B . n 
B 1 112 ILE 112 104 104 ILE ILE B . n 
B 1 113 SER 113 105 105 SER SER B . n 
B 1 114 LEU 114 106 106 LEU LEU B . n 
B 1 115 SER 115 107 107 SER SER B . n 
B 1 116 GLY 116 108 108 GLY GLY B . n 
B 1 117 ASP 117 109 109 ASP ASP B . n 
B 1 118 HIS 118 110 110 HIS HIS B . n 
B 1 119 CYS 119 111 111 CYS CYS B . n 
B 1 120 ILE 120 112 112 ILE ILE B . n 
B 1 121 ILE 121 113 113 ILE ILE B . n 
B 1 122 GLY 122 114 114 GLY GLY B . n 
B 1 123 ARG 123 115 115 ARG ARG B . n 
B 1 124 THR 124 116 116 THR THR B . n 
B 1 125 LEU 125 117 117 LEU LEU B . n 
B 1 126 VAL 126 118 118 VAL VAL B . n 
B 1 127 VAL 127 119 119 VAL VAL B . n 
B 1 128 HIS 128 120 120 HIS HIS B . n 
B 1 129 GLU 129 121 121 GLU GLU B . n 
B 1 130 LYS 130 122 ?   ?   ?   B . n 
B 1 131 ALA 131 123 ?   ?   ?   B . n 
B 1 132 ASP 132 124 ?   ?   ?   B . n 
B 1 133 ASP 133 125 ?   ?   ?   B . n 
B 1 134 LEU 134 126 ?   ?   ?   B . n 
B 1 135 GLY 135 127 ?   ?   ?   B . n 
B 1 136 LYS 136 128 ?   ?   ?   B . n 
B 1 137 GLY 137 129 ?   ?   ?   B . n 
B 1 138 GLY 138 130 ?   ?   ?   B . n 
B 1 139 ASN 139 131 ?   ?   ?   B . n 
B 1 140 GLU 140 132 ?   ?   ?   B . n 
B 1 141 GLU 141 133 ?   ?   ?   B . n 
B 1 142 SER 142 134 ?   ?   ?   B . n 
B 1 143 THR 143 135 ?   ?   ?   B . n 
B 1 144 LYS 144 136 ?   ?   ?   B . n 
B 1 145 THR 145 137 ?   ?   ?   B . n 
B 1 146 GLY 146 138 ?   ?   ?   B . n 
B 1 147 ASN 147 139 ?   ?   ?   B . n 
B 1 148 ALA 148 140 ?   ?   ?   B . n 
B 1 149 GLY 149 141 ?   ?   ?   B . n 
B 1 150 SER 150 142 ?   ?   ?   B . n 
B 1 151 ARG 151 143 ?   ?   ?   B . n 
B 1 152 LEU 152 144 ?   ?   ?   B . n 
B 1 153 ALA 153 145 ?   ?   ?   B . n 
B 1 154 CYS 154 146 ?   ?   ?   B . n 
B 1 155 GLY 155 147 ?   ?   ?   B . n 
B 1 156 VAL 156 148 ?   ?   ?   B . n 
B 1 157 ILE 157 149 ?   ?   ?   B . n 
B 1 158 GLY 158 150 ?   ?   ?   B . n 
B 1 159 ILE 159 151 ?   ?   ?   B . n 
B 1 160 ALA 160 152 ?   ?   ?   B . n 
B 1 161 GLN 161 153 ?   ?   ?   B . n 
C 1 1   GLY 1   -7  ?   ?   ?   A . n 
C 1 2   ALA 2   -6  ?   ?   ?   A . n 
C 1 3   MET 3   -5  ?   ?   ?   A . n 
C 1 4   ASP 4   -4  ?   ?   ?   A . n 
C 1 5   PRO 5   -3  ?   ?   ?   A . n 
C 1 6   GLU 6   -2  ?   ?   ?   A . n 
C 1 7   PHE 7   -1  ?   ?   ?   A . n 
C 1 8   MET 8   0   ?   ?   ?   A . n 
C 1 9   ALA 9   1   1   ALA ALA A . n 
C 1 10  THR 10  2   2   THR THR A . n 
C 1 11  LYS 11  3   3   LYS LYS A . n 
C 1 12  ALA 12  4   4   ALA ALA A . n 
C 1 13  VAL 13  5   5   VAL VAL A . n 
C 1 14  CYS 14  6   6   CYS CYS A . n 
C 1 15  VAL 15  7   7   VAL VAL A . n 
C 1 16  LEU 16  8   8   LEU LEU A . n 
C 1 17  LYS 17  9   9   LYS LYS A . n 
C 1 18  GLY 18  10  10  GLY GLY A . n 
C 1 19  ASP 19  11  11  ASP ASP A . n 
C 1 20  GLY 20  12  12  GLY GLY A . n 
C 1 21  PRO 21  13  13  PRO PRO A . n 
C 1 22  VAL 22  14  14  VAL VAL A . n 
C 1 23  GLN 23  15  15  GLN GLN A . n 
C 1 24  GLY 24  16  16  GLY GLY A . n 
C 1 25  ILE 25  17  17  ILE ILE A . n 
C 1 26  ILE 26  18  18  ILE ILE A . n 
C 1 27  ASN 27  19  19  ASN ASN A . n 
C 1 28  PHE 28  20  20  PHE PHE A . n 
C 1 29  GLU 29  21  21  GLU GLU A . n 
C 1 30  GLN 30  22  22  GLN GLN A . n 
C 1 31  LYS 31  23  23  LYS LYS A . n 
C 1 32  GLU 32  24  24  GLU GLU A . n 
C 1 33  SER 33  25  25  SER SER A . n 
C 1 34  ASN 34  26  26  ASN ASN A . n 
C 1 35  GLY 35  27  27  GLY GLY A . n 
C 1 36  PRO 36  28  28  PRO PRO A . n 
C 1 37  VAL 37  29  29  VAL VAL A . n 
C 1 38  LYS 38  30  30  LYS LYS A . n 
C 1 39  VAL 39  31  31  VAL VAL A . n 
C 1 40  TRP 40  32  32  TRP TRP A . n 
C 1 41  GLY 41  33  33  GLY GLY A . n 
C 1 42  SER 42  34  34  SER SER A . n 
C 1 43  ILE 43  35  35  ILE ILE A . n 
C 1 44  LYS 44  36  36  LYS LYS A . n 
C 1 45  GLY 45  37  37  GLY GLY A . n 
C 1 46  LEU 46  38  38  LEU LEU A . n 
C 1 47  THR 47  39  39  THR THR A . n 
C 1 48  GLU 48  40  40  GLU GLU A . n 
C 1 49  GLY 49  41  41  GLY GLY A . n 
C 1 50  LEU 50  42  42  LEU LEU A . n 
C 1 51  HIS 51  43  43  HIS HIS A . n 
C 1 52  GLY 52  44  44  GLY GLY A . n 
C 1 53  PHE 53  45  45  PHE PHE A . n 
C 1 54  HIS 54  46  ?   ?   ?   A . n 
C 1 55  VAL 55  47  ?   ?   ?   A . n 
C 1 56  HIS 56  48  ?   ?   ?   A . n 
C 1 57  GLU 57  49  ?   ?   ?   A . n 
C 1 58  PHE 58  50  ?   ?   ?   A . n 
C 1 59  GLY 59  51  ?   ?   ?   A . n 
C 1 60  ASP 60  52  ?   ?   ?   A . n 
C 1 61  ASN 61  53  ?   ?   ?   A . n 
C 1 62  THR 62  54  ?   ?   ?   A . n 
C 1 63  ALA 63  55  ?   ?   ?   A . n 
C 1 64  GLY 64  56  ?   ?   ?   A . n 
C 1 65  CYS 65  57  ?   ?   ?   A . n 
C 1 66  THR 66  58  ?   ?   ?   A . n 
C 1 67  SER 67  59  ?   ?   ?   A . n 
C 1 68  ALA 68  60  ?   ?   ?   A . n 
C 1 69  GLY 69  61  ?   ?   ?   A . n 
C 1 70  PRO 70  62  ?   ?   ?   A . n 
C 1 71  HIS 71  63  ?   ?   ?   A . n 
C 1 72  PHE 72  64  ?   ?   ?   A . n 
C 1 73  ASN 73  65  ?   ?   ?   A . n 
C 1 74  PRO 74  66  ?   ?   ?   A . n 
C 1 75  LEU 75  67  ?   ?   ?   A . n 
C 1 76  SER 76  68  ?   ?   ?   A . n 
C 1 77  ARG 77  69  ?   ?   ?   A . n 
C 1 78  LYS 78  70  ?   ?   ?   A . n 
C 1 79  HIS 79  71  ?   ?   ?   A . n 
C 1 80  GLY 80  72  ?   ?   ?   A . n 
C 1 81  GLY 81  73  ?   ?   ?   A . n 
C 1 82  PRO 82  74  ?   ?   ?   A . n 
C 1 83  LYS 83  75  ?   ?   ?   A . n 
C 1 84  ASP 84  76  ?   ?   ?   A . n 
C 1 85  GLU 85  77  ?   ?   ?   A . n 
C 1 86  GLU 86  78  ?   ?   ?   A . n 
C 1 87  ARG 87  79  ?   ?   ?   A . n 
C 1 88  HIS 88  80  ?   ?   ?   A . n 
C 1 89  VAL 89  81  81  VAL VAL A . n 
C 1 90  GLY 90  82  82  GLY GLY A . n 
C 1 91  ASP 91  83  83  ASP ASP A . n 
C 1 92  LEU 92  84  84  LEU LEU A . n 
C 1 93  GLY 93  85  85  GLY GLY A . n 
C 1 94  ASN 94  86  86  ASN ASN A . n 
C 1 95  VAL 95  87  87  VAL VAL A . n 
C 1 96  THR 96  88  88  THR THR A . n 
C 1 97  ALA 97  89  89  ALA ALA A . n 
C 1 98  ASP 98  90  90  ASP ASP A . n 
C 1 99  LYS 99  91  91  LYS LYS A . n 
C 1 100 ASP 100 92  92  ASP ASP A . n 
C 1 101 GLY 101 93  93  GLY GLY A . n 
C 1 102 VAL 102 94  94  VAL VAL A . n 
C 1 103 ALA 103 95  95  ALA ALA A . n 
C 1 104 ASP 104 96  96  ASP ASP A . n 
C 1 105 VAL 105 97  97  VAL VAL A . n 
C 1 106 SER 106 98  98  SER SER A . n 
C 1 107 ILE 107 99  99  ILE ILE A . n 
C 1 108 GLU 108 100 100 GLU GLU A . n 
C 1 109 ASP 109 101 101 ASP ASP A . n 
C 1 110 SER 110 102 102 SER SER A . n 
C 1 111 VAL 111 103 103 VAL VAL A . n 
C 1 112 ILE 112 104 104 ILE ILE A . n 
C 1 113 SER 113 105 105 SER SER A . n 
C 1 114 LEU 114 106 106 LEU LEU A . n 
C 1 115 SER 115 107 107 SER SER A . n 
C 1 116 GLY 116 108 108 GLY GLY A . n 
C 1 117 ASP 117 109 109 ASP ASP A . n 
C 1 118 HIS 118 110 110 HIS HIS A . n 
C 1 119 CYS 119 111 111 CYS CYS A . n 
C 1 120 ILE 120 112 112 ILE ILE A . n 
C 1 121 ILE 121 113 113 ILE ILE A . n 
C 1 122 GLY 122 114 114 GLY GLY A . n 
C 1 123 ARG 123 115 115 ARG ARG A . n 
C 1 124 THR 124 116 116 THR THR A . n 
C 1 125 LEU 125 117 117 LEU LEU A . n 
C 1 126 VAL 126 118 118 VAL VAL A . n 
C 1 127 VAL 127 119 119 VAL VAL A . n 
C 1 128 HIS 128 120 120 HIS HIS A . n 
C 1 129 GLU 129 121 121 GLU GLU A . n 
C 1 130 LYS 130 122 ?   ?   ?   A . n 
C 1 131 ALA 131 123 ?   ?   ?   A . n 
C 1 132 ASP 132 124 ?   ?   ?   A . n 
C 1 133 ASP 133 125 ?   ?   ?   A . n 
C 1 134 LEU 134 126 ?   ?   ?   A . n 
C 1 135 GLY 135 127 ?   ?   ?   A . n 
C 1 136 LYS 136 128 ?   ?   ?   A . n 
C 1 137 GLY 137 129 ?   ?   ?   A . n 
C 1 138 GLY 138 130 ?   ?   ?   A . n 
C 1 139 ASN 139 131 ?   ?   ?   A . n 
C 1 140 GLU 140 132 ?   ?   ?   A . n 
C 1 141 GLU 141 133 ?   ?   ?   A . n 
C 1 142 SER 142 134 ?   ?   ?   A . n 
C 1 143 THR 143 135 ?   ?   ?   A . n 
C 1 144 LYS 144 136 ?   ?   ?   A . n 
C 1 145 THR 145 137 ?   ?   ?   A . n 
C 1 146 GLY 146 138 ?   ?   ?   A . n 
C 1 147 ASN 147 139 ?   ?   ?   A . n 
C 1 148 ALA 148 140 ?   ?   ?   A . n 
C 1 149 GLY 149 141 ?   ?   ?   A . n 
C 1 150 SER 150 142 ?   ?   ?   A . n 
C 1 151 ARG 151 143 ?   ?   ?   A . n 
C 1 152 LEU 152 144 ?   ?   ?   A . n 
C 1 153 ALA 153 145 ?   ?   ?   A . n 
C 1 154 CYS 154 146 ?   ?   ?   A . n 
C 1 155 GLY 155 147 ?   ?   ?   A . n 
C 1 156 VAL 156 148 ?   ?   ?   A . n 
C 1 157 ILE 157 149 ?   ?   ?   A . n 
C 1 158 GLY 158 150 ?   ?   ?   A . n 
C 1 159 ILE 159 151 ?   ?   ?   A . n 
C 1 160 ALA 160 152 ?   ?   ?   A . n 
C 1 161 GLN 161 153 ?   ?   ?   A . n 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JBO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JBO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JBO 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9JBO 
_struct.title                        'Cryo-EM structure of human SOD1 (WT) amyloid filament' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9JBO 
_struct_keywords.text            'amyloid, filament, superoxide dismutase 1, amyotrophic lateral sclerosis, PROTEIN FIBRIL' 
_struct_keywords.pdbx_keywords   'PROTEIN FIBRIL' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JBO C 8 ? 161 ? P00441 1 ? 154 ? 0 153 
2 1 9JBO B 8 ? 161 ? P00441 1 ? 154 ? 0 153 
3 1 9JBO A 8 ? 161 ? P00441 1 ? 154 ? 0 153 
# 
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 9JBO GLY C 1 ? UNP P00441 ? ? 'expression tag' -7 1  
1 9JBO ALA C 2 ? UNP P00441 ? ? 'expression tag' -6 2  
1 9JBO MET C 3 ? UNP P00441 ? ? 'expression tag' -5 3  
1 9JBO ASP C 4 ? UNP P00441 ? ? 'expression tag' -4 4  
1 9JBO PRO C 5 ? UNP P00441 ? ? 'expression tag' -3 5  
1 9JBO GLU C 6 ? UNP P00441 ? ? 'expression tag' -2 6  
1 9JBO PHE C 7 ? UNP P00441 ? ? 'expression tag' -1 7  
2 9JBO GLY B 1 ? UNP P00441 ? ? 'expression tag' -7 8  
2 9JBO ALA B 2 ? UNP P00441 ? ? 'expression tag' -6 9  
2 9JBO MET B 3 ? UNP P00441 ? ? 'expression tag' -5 10 
2 9JBO ASP B 4 ? UNP P00441 ? ? 'expression tag' -4 11 
2 9JBO PRO B 5 ? UNP P00441 ? ? 'expression tag' -3 12 
2 9JBO GLU B 6 ? UNP P00441 ? ? 'expression tag' -2 13 
2 9JBO PHE B 7 ? UNP P00441 ? ? 'expression tag' -1 14 
3 9JBO GLY A 1 ? UNP P00441 ? ? 'expression tag' -7 15 
3 9JBO ALA A 2 ? UNP P00441 ? ? 'expression tag' -6 16 
3 9JBO MET A 3 ? UNP P00441 ? ? 'expression tag' -5 17 
3 9JBO ASP A 4 ? UNP P00441 ? ? 'expression tag' -4 18 
3 9JBO PRO A 5 ? UNP P00441 ? ? 'expression tag' -3 19 
3 9JBO GLU A 6 ? UNP P00441 ? ? 'expression tag' -2 20 
3 9JBO PHE A 7 ? UNP P00441 ? ? 'expression tag' -1 21 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'filaments were observed in EM images' 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 3 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA4 1 2 ? parallel 
AA4 2 3 ? parallel 
AA5 1 2 ? parallel 
AA5 2 3 ? parallel 
AA6 1 2 ? parallel 
AA6 2 3 ? parallel 
AA7 1 2 ? parallel 
AA7 2 3 ? parallel 
AA8 1 2 ? parallel 
AA8 2 3 ? parallel 
AA9 1 2 ? parallel 
AA9 2 3 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 15  ? GLY A 18  ? VAL C 7   GLY C 10  
AA1 2 VAL B 15  ? GLY B 18  ? VAL B 7   GLY B 10  
AA1 3 VAL C 15  ? GLY C 18  ? VAL A 7   GLY A 10  
AA2 1 VAL A 22  ? LYS A 31  ? VAL C 14  LYS C 23  
AA2 2 VAL B 22  ? LYS B 31  ? VAL B 14  LYS B 23  
AA2 3 VAL C 22  ? LYS C 31  ? VAL A 14  LYS A 23  
AA3 1 VAL A 37  ? VAL A 39  ? VAL C 29  VAL C 31  
AA3 2 VAL B 37  ? VAL B 39  ? VAL B 29  VAL B 31  
AA3 3 VAL C 37  ? VAL C 39  ? VAL A 29  VAL A 31  
AA4 1 ILE A 43  ? THR A 47  ? ILE C 35  THR C 39  
AA4 2 ILE B 43  ? THR B 47  ? ILE B 35  THR B 39  
AA4 3 ILE C 43  ? THR C 47  ? ILE A 35  THR A 39  
AA5 1 VAL A 95  ? THR A 96  ? VAL C 87  THR C 88  
AA5 2 VAL B 95  ? THR B 96  ? VAL B 87  THR B 88  
AA5 3 VAL C 95  ? THR C 96  ? VAL A 87  THR A 88  
AA6 1 VAL A 105 ? GLU A 108 ? VAL C 97  GLU C 100 
AA6 2 VAL B 105 ? GLU B 108 ? VAL B 97  GLU B 100 
AA6 3 VAL C 105 ? GLU C 108 ? VAL A 97  GLU A 100 
AA7 1 VAL A 111 ? SER A 113 ? VAL C 103 SER C 105 
AA7 2 VAL B 111 ? SER B 113 ? VAL B 103 SER B 105 
AA7 3 VAL C 111 ? SER C 113 ? VAL A 103 SER A 105 
AA8 1 CYS A 119 ? ILE A 121 ? CYS C 111 ILE C 113 
AA8 2 CYS B 119 ? ILE B 121 ? CYS B 111 ILE B 113 
AA8 3 CYS C 119 ? ILE C 121 ? CYS A 111 ILE A 113 
AA9 1 VAL A 126 ? HIS A 128 ? VAL C 118 HIS C 120 
AA9 2 VAL B 126 ? HIS B 128 ? VAL B 118 HIS B 120 
AA9 3 VAL C 126 ? HIS C 128 ? VAL A 118 HIS A 120 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 18  ? N GLY C 10  O LYS B 17  ? O LYS B 9   
AA1 2 3 N GLY B 18  ? N GLY B 10  O LYS C 17  ? O LYS A 9   
AA2 1 2 N ILE A 25  ? N ILE C 17  O GLY B 24  ? O GLY B 16  
AA2 2 3 N ILE B 25  ? N ILE B 17  O GLY C 24  ? O GLY A 16  
AA3 1 2 N LYS A 38  ? N LYS C 30  O VAL B 39  ? O VAL B 31  
AA3 2 3 N LYS B 38  ? N LYS B 30  O VAL C 39  ? O VAL A 31  
AA4 1 2 N LYS A 44  ? N LYS C 36  O GLY B 45  ? O GLY B 37  
AA4 2 3 N LYS B 44  ? N LYS B 36  O GLY C 45  ? O GLY A 37  
AA5 1 2 N VAL A 95  ? N VAL C 87  O THR B 96  ? O THR B 88  
AA5 2 3 N VAL B 95  ? N VAL B 87  O THR C 96  ? O THR A 88  
AA6 1 2 N SER A 106 ? N SER C 98  O ILE B 107 ? O ILE B 99  
AA6 2 3 N SER B 106 ? N SER B 98  O ILE C 107 ? O ILE A 99  
AA7 1 2 N VAL A 111 ? N VAL C 103 O ILE B 112 ? O ILE B 104 
AA7 2 3 N VAL B 111 ? N VAL B 103 O ILE C 112 ? O ILE A 104 
AA8 1 2 N ILE A 120 ? N ILE C 112 O ILE B 121 ? O ILE B 113 
AA8 2 3 N ILE B 120 ? N ILE B 112 O ILE C 121 ? O ILE A 113 
AA9 1 2 N HIS A 128 ? N HIS C 120 O VAL B 127 ? O VAL B 119 
AA9 2 3 N HIS B 128 ? N HIS B 120 O VAL C 127 ? O VAL A 119 
# 
_pdbx_entry_details.entry_id                   9JBO 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR C 2  ? ? 50.06   -100.42 
2 1 CYS C 6  ? ? 61.51   63.83   
3 1 ALA C 89 ? ? -142.30 47.55   
4 1 THR B 2  ? ? 50.04   -100.37 
5 1 CYS B 6  ? ? 61.45   63.87   
6 1 ALA B 89 ? ? -142.33 47.55   
7 1 THR A 2  ? ? 50.05   -100.37 
8 1 CYS A 6  ? ? 61.47   63.87   
9 1 ALA A 89 ? ? -142.32 47.53   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9JBO 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'AB INITIO MODEL' 
# 
_em_3d_reconstruction.entry_id                    9JBO 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.39 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               92864 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               HELICAL 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Amyloid filament of human wild-type SOD1 protein' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9JBO 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             1400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           165000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9JBO 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9JBO 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   HELICAL 
_em_experiment.aggregation_state       'HELICAL ARRAY' 
_em_experiment.entity_assembly_id      1 
# 
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 C GLY -7  ? A GLY 1   
2   1 Y 1 C ALA -6  ? A ALA 2   
3   1 Y 1 C MET -5  ? A MET 3   
4   1 Y 1 C ASP -4  ? A ASP 4   
5   1 Y 1 C PRO -3  ? A PRO 5   
6   1 Y 1 C GLU -2  ? A GLU 6   
7   1 Y 1 C PHE -1  ? A PHE 7   
8   1 Y 1 C MET 0   ? A MET 8   
9   1 Y 1 C HIS 46  ? A HIS 54  
10  1 Y 1 C VAL 47  ? A VAL 55  
11  1 Y 1 C HIS 48  ? A HIS 56  
12  1 Y 1 C GLU 49  ? A GLU 57  
13  1 Y 1 C PHE 50  ? A PHE 58  
14  1 Y 1 C GLY 51  ? A GLY 59  
15  1 Y 1 C ASP 52  ? A ASP 60  
16  1 Y 1 C ASN 53  ? A ASN 61  
17  1 Y 1 C THR 54  ? A THR 62  
18  1 Y 1 C ALA 55  ? A ALA 63  
19  1 Y 1 C GLY 56  ? A GLY 64  
20  1 Y 1 C CYS 57  ? A CYS 65  
21  1 Y 1 C THR 58  ? A THR 66  
22  1 Y 1 C SER 59  ? A SER 67  
23  1 Y 1 C ALA 60  ? A ALA 68  
24  1 Y 1 C GLY 61  ? A GLY 69  
25  1 Y 1 C PRO 62  ? A PRO 70  
26  1 Y 1 C HIS 63  ? A HIS 71  
27  1 Y 1 C PHE 64  ? A PHE 72  
28  1 Y 1 C ASN 65  ? A ASN 73  
29  1 Y 1 C PRO 66  ? A PRO 74  
30  1 Y 1 C LEU 67  ? A LEU 75  
31  1 Y 1 C SER 68  ? A SER 76  
32  1 Y 1 C ARG 69  ? A ARG 77  
33  1 Y 1 C LYS 70  ? A LYS 78  
34  1 Y 1 C HIS 71  ? A HIS 79  
35  1 Y 1 C GLY 72  ? A GLY 80  
36  1 Y 1 C GLY 73  ? A GLY 81  
37  1 Y 1 C PRO 74  ? A PRO 82  
38  1 Y 1 C LYS 75  ? A LYS 83  
39  1 Y 1 C ASP 76  ? A ASP 84  
40  1 Y 1 C GLU 77  ? A GLU 85  
41  1 Y 1 C GLU 78  ? A GLU 86  
42  1 Y 1 C ARG 79  ? A ARG 87  
43  1 Y 1 C HIS 80  ? A HIS 88  
44  1 Y 1 C LYS 122 ? A LYS 130 
45  1 Y 1 C ALA 123 ? A ALA 131 
46  1 Y 1 C ASP 124 ? A ASP 132 
47  1 Y 1 C ASP 125 ? A ASP 133 
48  1 Y 1 C LEU 126 ? A LEU 134 
49  1 Y 1 C GLY 127 ? A GLY 135 
50  1 Y 1 C LYS 128 ? A LYS 136 
51  1 Y 1 C GLY 129 ? A GLY 137 
52  1 Y 1 C GLY 130 ? A GLY 138 
53  1 Y 1 C ASN 131 ? A ASN 139 
54  1 Y 1 C GLU 132 ? A GLU 140 
55  1 Y 1 C GLU 133 ? A GLU 141 
56  1 Y 1 C SER 134 ? A SER 142 
57  1 Y 1 C THR 135 ? A THR 143 
58  1 Y 1 C LYS 136 ? A LYS 144 
59  1 Y 1 C THR 137 ? A THR 145 
60  1 Y 1 C GLY 138 ? A GLY 146 
61  1 Y 1 C ASN 139 ? A ASN 147 
62  1 Y 1 C ALA 140 ? A ALA 148 
63  1 Y 1 C GLY 141 ? A GLY 149 
64  1 Y 1 C SER 142 ? A SER 150 
65  1 Y 1 C ARG 143 ? A ARG 151 
66  1 Y 1 C LEU 144 ? A LEU 152 
67  1 Y 1 C ALA 145 ? A ALA 153 
68  1 Y 1 C CYS 146 ? A CYS 154 
69  1 Y 1 C GLY 147 ? A GLY 155 
70  1 Y 1 C VAL 148 ? A VAL 156 
71  1 Y 1 C ILE 149 ? A ILE 157 
72  1 Y 1 C GLY 150 ? A GLY 158 
73  1 Y 1 C ILE 151 ? A ILE 159 
74  1 Y 1 C ALA 152 ? A ALA 160 
75  1 Y 1 C GLN 153 ? A GLN 161 
76  1 Y 1 B GLY -7  ? B GLY 1   
77  1 Y 1 B ALA -6  ? B ALA 2   
78  1 Y 1 B MET -5  ? B MET 3   
79  1 Y 1 B ASP -4  ? B ASP 4   
80  1 Y 1 B PRO -3  ? B PRO 5   
81  1 Y 1 B GLU -2  ? B GLU 6   
82  1 Y 1 B PHE -1  ? B PHE 7   
83  1 Y 1 B MET 0   ? B MET 8   
84  1 Y 1 B HIS 46  ? B HIS 54  
85  1 Y 1 B VAL 47  ? B VAL 55  
86  1 Y 1 B HIS 48  ? B HIS 56  
87  1 Y 1 B GLU 49  ? B GLU 57  
88  1 Y 1 B PHE 50  ? B PHE 58  
89  1 Y 1 B GLY 51  ? B GLY 59  
90  1 Y 1 B ASP 52  ? B ASP 60  
91  1 Y 1 B ASN 53  ? B ASN 61  
92  1 Y 1 B THR 54  ? B THR 62  
93  1 Y 1 B ALA 55  ? B ALA 63  
94  1 Y 1 B GLY 56  ? B GLY 64  
95  1 Y 1 B CYS 57  ? B CYS 65  
96  1 Y 1 B THR 58  ? B THR 66  
97  1 Y 1 B SER 59  ? B SER 67  
98  1 Y 1 B ALA 60  ? B ALA 68  
99  1 Y 1 B GLY 61  ? B GLY 69  
100 1 Y 1 B PRO 62  ? B PRO 70  
101 1 Y 1 B HIS 63  ? B HIS 71  
102 1 Y 1 B PHE 64  ? B PHE 72  
103 1 Y 1 B ASN 65  ? B ASN 73  
104 1 Y 1 B PRO 66  ? B PRO 74  
105 1 Y 1 B LEU 67  ? B LEU 75  
106 1 Y 1 B SER 68  ? B SER 76  
107 1 Y 1 B ARG 69  ? B ARG 77  
108 1 Y 1 B LYS 70  ? B LYS 78  
109 1 Y 1 B HIS 71  ? B HIS 79  
110 1 Y 1 B GLY 72  ? B GLY 80  
111 1 Y 1 B GLY 73  ? B GLY 81  
112 1 Y 1 B PRO 74  ? B PRO 82  
113 1 Y 1 B LYS 75  ? B LYS 83  
114 1 Y 1 B ASP 76  ? B ASP 84  
115 1 Y 1 B GLU 77  ? B GLU 85  
116 1 Y 1 B GLU 78  ? B GLU 86  
117 1 Y 1 B ARG 79  ? B ARG 87  
118 1 Y 1 B HIS 80  ? B HIS 88  
119 1 Y 1 B LYS 122 ? B LYS 130 
120 1 Y 1 B ALA 123 ? B ALA 131 
121 1 Y 1 B ASP 124 ? B ASP 132 
122 1 Y 1 B ASP 125 ? B ASP 133 
123 1 Y 1 B LEU 126 ? B LEU 134 
124 1 Y 1 B GLY 127 ? B GLY 135 
125 1 Y 1 B LYS 128 ? B LYS 136 
126 1 Y 1 B GLY 129 ? B GLY 137 
127 1 Y 1 B GLY 130 ? B GLY 138 
128 1 Y 1 B ASN 131 ? B ASN 139 
129 1 Y 1 B GLU 132 ? B GLU 140 
130 1 Y 1 B GLU 133 ? B GLU 141 
131 1 Y 1 B SER 134 ? B SER 142 
132 1 Y 1 B THR 135 ? B THR 143 
133 1 Y 1 B LYS 136 ? B LYS 144 
134 1 Y 1 B THR 137 ? B THR 145 
135 1 Y 1 B GLY 138 ? B GLY 146 
136 1 Y 1 B ASN 139 ? B ASN 147 
137 1 Y 1 B ALA 140 ? B ALA 148 
138 1 Y 1 B GLY 141 ? B GLY 149 
139 1 Y 1 B SER 142 ? B SER 150 
140 1 Y 1 B ARG 143 ? B ARG 151 
141 1 Y 1 B LEU 144 ? B LEU 152 
142 1 Y 1 B ALA 145 ? B ALA 153 
143 1 Y 1 B CYS 146 ? B CYS 154 
144 1 Y 1 B GLY 147 ? B GLY 155 
145 1 Y 1 B VAL 148 ? B VAL 156 
146 1 Y 1 B ILE 149 ? B ILE 157 
147 1 Y 1 B GLY 150 ? B GLY 158 
148 1 Y 1 B ILE 151 ? B ILE 159 
149 1 Y 1 B ALA 152 ? B ALA 160 
150 1 Y 1 B GLN 153 ? B GLN 161 
151 1 Y 1 A GLY -7  ? C GLY 1   
152 1 Y 1 A ALA -6  ? C ALA 2   
153 1 Y 1 A MET -5  ? C MET 3   
154 1 Y 1 A ASP -4  ? C ASP 4   
155 1 Y 1 A PRO -3  ? C PRO 5   
156 1 Y 1 A GLU -2  ? C GLU 6   
157 1 Y 1 A PHE -1  ? C PHE 7   
158 1 Y 1 A MET 0   ? C MET 8   
159 1 Y 1 A HIS 46  ? C HIS 54  
160 1 Y 1 A VAL 47  ? C VAL 55  
161 1 Y 1 A HIS 48  ? C HIS 56  
162 1 Y 1 A GLU 49  ? C GLU 57  
163 1 Y 1 A PHE 50  ? C PHE 58  
164 1 Y 1 A GLY 51  ? C GLY 59  
165 1 Y 1 A ASP 52  ? C ASP 60  
166 1 Y 1 A ASN 53  ? C ASN 61  
167 1 Y 1 A THR 54  ? C THR 62  
168 1 Y 1 A ALA 55  ? C ALA 63  
169 1 Y 1 A GLY 56  ? C GLY 64  
170 1 Y 1 A CYS 57  ? C CYS 65  
171 1 Y 1 A THR 58  ? C THR 66  
172 1 Y 1 A SER 59  ? C SER 67  
173 1 Y 1 A ALA 60  ? C ALA 68  
174 1 Y 1 A GLY 61  ? C GLY 69  
175 1 Y 1 A PRO 62  ? C PRO 70  
176 1 Y 1 A HIS 63  ? C HIS 71  
177 1 Y 1 A PHE 64  ? C PHE 72  
178 1 Y 1 A ASN 65  ? C ASN 73  
179 1 Y 1 A PRO 66  ? C PRO 74  
180 1 Y 1 A LEU 67  ? C LEU 75  
181 1 Y 1 A SER 68  ? C SER 76  
182 1 Y 1 A ARG 69  ? C ARG 77  
183 1 Y 1 A LYS 70  ? C LYS 78  
184 1 Y 1 A HIS 71  ? C HIS 79  
185 1 Y 1 A GLY 72  ? C GLY 80  
186 1 Y 1 A GLY 73  ? C GLY 81  
187 1 Y 1 A PRO 74  ? C PRO 82  
188 1 Y 1 A LYS 75  ? C LYS 83  
189 1 Y 1 A ASP 76  ? C ASP 84  
190 1 Y 1 A GLU 77  ? C GLU 85  
191 1 Y 1 A GLU 78  ? C GLU 86  
192 1 Y 1 A ARG 79  ? C ARG 87  
193 1 Y 1 A HIS 80  ? C HIS 88  
194 1 Y 1 A LYS 122 ? C LYS 130 
195 1 Y 1 A ALA 123 ? C ALA 131 
196 1 Y 1 A ASP 124 ? C ASP 132 
197 1 Y 1 A ASP 125 ? C ASP 133 
198 1 Y 1 A LEU 126 ? C LEU 134 
199 1 Y 1 A GLY 127 ? C GLY 135 
200 1 Y 1 A LYS 128 ? C LYS 136 
201 1 Y 1 A GLY 129 ? C GLY 137 
202 1 Y 1 A GLY 130 ? C GLY 138 
203 1 Y 1 A ASN 131 ? C ASN 139 
204 1 Y 1 A GLU 132 ? C GLU 140 
205 1 Y 1 A GLU 133 ? C GLU 141 
206 1 Y 1 A SER 134 ? C SER 142 
207 1 Y 1 A THR 135 ? C THR 143 
208 1 Y 1 A LYS 136 ? C LYS 144 
209 1 Y 1 A THR 137 ? C THR 145 
210 1 Y 1 A GLY 138 ? C GLY 146 
211 1 Y 1 A ASN 139 ? C ASN 147 
212 1 Y 1 A ALA 140 ? C ALA 148 
213 1 Y 1 A GLY 141 ? C GLY 149 
214 1 Y 1 A SER 142 ? C SER 150 
215 1 Y 1 A ARG 143 ? C ARG 151 
216 1 Y 1 A LEU 144 ? C LEU 152 
217 1 Y 1 A ALA 145 ? C ALA 153 
218 1 Y 1 A CYS 146 ? C CYS 154 
219 1 Y 1 A GLY 147 ? C GLY 155 
220 1 Y 1 A VAL 148 ? C VAL 156 
221 1 Y 1 A ILE 149 ? C ILE 157 
222 1 Y 1 A GLY 150 ? C GLY 158 
223 1 Y 1 A ILE 151 ? C ILE 159 
224 1 Y 1 A ALA 152 ? C ALA 160 
225 1 Y 1 A GLN 153 ? C GLN 161 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
VAL N    N N N 345 
VAL CA   C N S 346 
VAL C    C N N 347 
VAL O    O N N 348 
VAL CB   C N N 349 
VAL CG1  C N N 350 
VAL CG2  C N N 351 
VAL OXT  O N N 352 
VAL H    H N N 353 
VAL H2   H N N 354 
VAL HA   H N N 355 
VAL HB   H N N 356 
VAL HG11 H N N 357 
VAL HG12 H N N 358 
VAL HG13 H N N 359 
VAL HG21 H N N 360 
VAL HG22 H N N 361 
VAL HG23 H N N 362 
VAL HXT  H N N 363 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
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 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
VAL N   CA   sing N N 332 
VAL N   H    sing N N 333 
VAL N   H2   sing N N 334 
VAL CA  C    sing N N 335 
VAL CA  CB   sing N N 336 
VAL CA  HA   sing N N 337 
VAL C   O    doub N N 338 
VAL C   OXT  sing N N 339 
VAL CB  CG1  sing N N 340 
VAL CB  CG2  sing N N 341 
VAL CB  HB   sing N N 342 
VAL CG1 HG11 sing N N 343 
VAL CG1 HG12 sing N N 344 
VAL CG1 HG13 sing N N 345 
VAL CG2 HG21 sing N N 346 
VAL CG2 HG22 sing N N 347 
VAL CG2 HG23 sing N N 348 
VAL OXT HXT  sing N N 349 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-27 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9JBO 
_em_admin.last_update        2025-02-05 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'Cryo-EM structure of human SOD1 (WT) amyloid filament' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                KILODALTONS/NANOMETER 
_em_entity_assembly_molwt.value                34.6 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_helical_entity.id                             1 
_em_helical_entity.image_processing_id            1 
_em_helical_entity.details                        ? 
_em_helical_entity.axial_symmetry                 C1 
_em_helical_entity.angular_rotation_per_subunit   -1.91 
_em_helical_entity.axial_rise_per_subunit         4.82 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'TFS FALCON 4i (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     3102 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    10 
_em_imaging_optics.energyfilter_name          'TFS Selectris X' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   99812 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       'start-end manual picking' 1  1 ? ? RELION 4.0  
'IMAGE ACQUISITION'        ?                          2  1 ? 1 ?      ?    
MASKING                    ?                          3  1 1 1 ?      ?    
'CTF CORRECTION'           Gctf                       4  1 ? ? RELION 4.0  
'LAYERLINE INDEXING'       ?                          5  1 1 1 ?      ?    
'DIFFRACTION INDEXING'     ?                          6  1 1 1 ?      ?    
'MODEL FITTING'            ?                          7  1 1 ? Coot   ?    
OTHER                      ?                          8  1 1 1 ?      ?    
'MODEL REFINEMENT'         ?                          9  ? 1 ? PHENIX 1.21 
'INITIAL EULER ASSIGNMENT' ?                          10 1 ? ? RELION 4.0  
'FINAL EULER ASSIGNMENT'   ?                          11 1 ? ? RELION 4.0  
CLASSIFICATION             ?                          12 1 ? ? RELION 4.0  
RECONSTRUCTION             ?                          13 1 ? ? RELION 4.0  
# 
_em_specimen.concentration           4.4 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9JBO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . ALA A 1 9   ? 93.740  145.771 105.853 1.00 55.72  ?  1   ALA C N   1 
ATOM 2    C CA  . ALA A 1 9   ? 94.671  144.915 105.129 1.00 56.34  ?  1   ALA C CA  1 
ATOM 3    C C   . ALA A 1 9   ? 94.410  143.444 105.433 1.00 54.10  ?  1   ALA C C   1 
ATOM 4    O O   . ALA A 1 9   ? 95.037  142.565 104.843 1.00 51.98  ?  1   ALA C O   1 
ATOM 5    C CB  . ALA A 1 9   ? 96.107  145.282 105.475 1.00 53.70  ?  1   ALA C CB  1 
ATOM 6    N N   . THR A 1 10  ? 93.473  143.194 106.351 1.00 55.69  ?  2   THR C N   1 
ATOM 7    C CA  . THR A 1 10  ? 93.096  141.853 106.791 1.00 57.85  ?  2   THR C CA  1 
ATOM 8    C C   . THR A 1 10  ? 94.348  141.058 107.162 1.00 60.11  ?  2   THR C C   1 
ATOM 9    O O   . THR A 1 10  ? 94.883  141.227 108.261 1.00 62.57  ?  2   THR C O   1 
ATOM 10   C CB  . THR A 1 10  ? 92.258  141.143 105.721 1.00 57.79  ?  2   THR C CB  1 
ATOM 11   O OG1 . THR A 1 10  ? 91.057  141.888 105.498 1.00 57.08  ?  2   THR C OG1 1 
ATOM 12   C CG2 . THR A 1 10  ? 91.835  139.752 106.196 1.00 57.16  ?  2   THR C CG2 1 
ATOM 13   N N   . LYS A 1 11  ? 94.820  140.185 106.274 1.00 56.21  ?  3   LYS C N   1 
ATOM 14   C CA  . LYS A 1 11  ? 96.037  139.415 106.502 1.00 50.38  ?  3   LYS C CA  1 
ATOM 15   C C   . LYS A 1 11  ? 97.131  139.950 105.590 1.00 45.18  ?  3   LYS C C   1 
ATOM 16   O O   . LYS A 1 11  ? 96.992  139.917 104.363 1.00 48.01  ?  3   LYS C O   1 
ATOM 17   C CB  . LYS A 1 11  ? 95.798  137.927 106.252 1.00 51.67  ?  3   LYS C CB  1 
ATOM 18   C CG  . LYS A 1 11  ? 96.725  137.009 107.033 1.00 52.43  ?  3   LYS C CG  1 
ATOM 19   C CD  . LYS A 1 11  ? 96.627  135.575 106.538 1.00 53.78  ?  3   LYS C CD  1 
ATOM 20   C CE  . LYS A 1 11  ? 97.713  134.703 107.149 1.00 58.89  ?  3   LYS C CE  1 
ATOM 21   N NZ  . LYS A 1 11  ? 99.059  135.330 107.038 1.00 61.87  1  3   LYS C NZ  1 
ATOM 22   N N   . ALA A 1 12  ? 98.221  140.437 106.180 1.00 41.44  ?  4   ALA C N   1 
ATOM 23   C CA  . ALA A 1 12  ? 99.257  141.093 105.388 1.00 36.97  ?  4   ALA C CA  1 
ATOM 24   C C   . ALA A 1 12  ? 100.592 140.988 106.114 1.00 31.73  ?  4   ALA C C   1 
ATOM 25   O O   . ALA A 1 12  ? 100.795 141.653 107.132 1.00 34.38  ?  4   ALA C O   1 
ATOM 26   C CB  . ALA A 1 12  ? 98.886  142.546 105.124 1.00 41.09  ?  4   ALA C CB  1 
ATOM 27   N N   . VAL A 1 13  ? 101.492 140.170 105.581 1.00 28.38  ?  5   VAL C N   1 
ATOM 28   C CA  . VAL A 1 13  ? 102.851 140.047 106.097 1.00 28.15  ?  5   VAL C CA  1 
ATOM 29   C C   . VAL A 1 13  ? 103.786 140.915 105.263 1.00 26.99  ?  5   VAL C C   1 
ATOM 30   O O   . VAL A 1 13  ? 103.655 140.983 104.034 1.00 27.51  ?  5   VAL C O   1 
ATOM 31   C CB  . VAL A 1 13  ? 103.300 138.575 106.111 1.00 30.26  ?  5   VAL C CB  1 
ATOM 32   C CG1 . VAL A 1 13  ? 102.965 137.907 104.816 1.00 31.24  ?  5   VAL C CG1 1 
ATOM 33   C CG2 . VAL A 1 13  ? 104.802 138.466 106.367 1.00 24.72  ?  5   VAL C CG2 1 
ATOM 34   N N   . CYS A 1 14  ? 104.719 141.590 105.938 1.00 26.06  ?  6   CYS C N   1 
ATOM 35   C CA  . CYS A 1 14  ? 105.689 142.498 105.322 1.00 23.51  ?  6   CYS C CA  1 
ATOM 36   C C   . CYS A 1 14  ? 104.984 143.667 104.627 1.00 24.07  ?  6   CYS C C   1 
ATOM 37   O O   . CYS A 1 14  ? 105.044 143.849 103.410 1.00 27.95  ?  6   CYS C O   1 
ATOM 38   C CB  . CYS A 1 14  ? 106.610 141.751 104.352 1.00 24.39  ?  6   CYS C CB  1 
ATOM 39   S SG  . CYS A 1 14  ? 108.240 142.505 104.154 1.00 26.80  ?  6   CYS C SG  1 
ATOM 40   N N   . VAL A 1 15  ? 104.306 144.459 105.452 1.00 22.94  ?  7   VAL C N   1 
ATOM 41   C CA  . VAL A 1 15  ? 103.680 145.706 105.025 1.00 24.99  ?  7   VAL C CA  1 
ATOM 42   C C   . VAL A 1 15  ? 104.504 146.856 105.586 1.00 26.21  ?  7   VAL C C   1 
ATOM 43   O O   . VAL A 1 15  ? 104.757 146.914 106.795 1.00 30.94  ?  7   VAL C O   1 
ATOM 44   C CB  . VAL A 1 15  ? 102.217 145.786 105.486 1.00 25.56  ?  7   VAL C CB  1 
ATOM 45   C CG1 . VAL A 1 15  ? 101.771 147.231 105.605 1.00 24.48  ?  7   VAL C CG1 1 
ATOM 46   C CG2 . VAL A 1 15  ? 101.327 145.041 104.515 1.00 25.36  ?  7   VAL C CG2 1 
ATOM 47   N N   . LEU A 1 16  ? 104.943 147.768 104.719 1.00 24.46  ?  8   LEU C N   1 
ATOM 48   C CA  . LEU A 1 16  ? 105.809 148.844 105.172 1.00 28.74  ?  8   LEU C CA  1 
ATOM 49   C C   . LEU A 1 16  ? 105.725 150.029 104.220 1.00 31.40  ?  8   LEU C C   1 
ATOM 50   O O   . LEU A 1 16  ? 105.293 149.903 103.071 1.00 38.14  ?  8   LEU C O   1 
ATOM 51   C CB  . LEU A 1 16  ? 107.262 148.371 105.307 1.00 28.94  ?  8   LEU C CB  1 
ATOM 52   C CG  . LEU A 1 16  ? 107.965 147.935 104.019 1.00 26.95  ?  8   LEU C CG  1 
ATOM 53   C CD1 . LEU A 1 16  ? 108.973 148.982 103.568 1.00 26.80  ?  8   LEU C CD1 1 
ATOM 54   C CD2 . LEU A 1 16  ? 108.632 146.582 104.206 1.00 25.59  ?  8   LEU C CD2 1 
ATOM 55   N N   . LYS A 1 17  ? 106.140 151.190 104.725 1.00 30.63  ?  9   LYS C N   1 
ATOM 56   C CA  . LYS A 1 17  ? 106.290 152.400 103.930 1.00 33.89  ?  9   LYS C CA  1 
ATOM 57   C C   . LYS A 1 17  ? 107.601 153.077 104.298 1.00 35.38  ?  9   LYS C C   1 
ATOM 58   O O   . LYS A 1 17  ? 107.978 153.119 105.472 1.00 37.54  ?  9   LYS C O   1 
ATOM 59   C CB  . LYS A 1 17  ? 105.132 153.386 104.139 1.00 31.42  ?  9   LYS C CB  1 
ATOM 60   C CG  . LYS A 1 17  ? 103.773 152.910 103.651 1.00 29.83  ?  9   LYS C CG  1 
ATOM 61   C CD  . LYS A 1 17  ? 102.977 152.232 104.752 1.00 30.45  ?  9   LYS C CD  1 
ATOM 62   C CE  . LYS A 1 17  ? 101.766 151.511 104.183 1.00 30.67  ?  9   LYS C CE  1 
ATOM 63   N NZ  . LYS A 1 17  ? 101.328 150.390 105.053 1.00 32.46  1  9   LYS C NZ  1 
ATOM 64   N N   . GLY A 1 18  ? 108.294 153.603 103.292 1.00 35.35  ?  10  GLY C N   1 
ATOM 65   C CA  . GLY A 1 18  ? 109.527 154.323 103.532 1.00 41.06  ?  10  GLY C CA  1 
ATOM 66   C C   . GLY A 1 18  ? 110.727 153.727 102.828 1.00 47.17  ?  10  GLY C C   1 
ATOM 67   O O   . GLY A 1 18  ? 110.650 153.364 101.650 1.00 48.28  ?  10  GLY C O   1 
ATOM 68   N N   . ASP A 1 19  ? 111.845 153.621 103.540 1.00 48.64  ?  11  ASP C N   1 
ATOM 69   C CA  . ASP A 1 19  ? 113.079 153.090 102.979 1.00 48.52  ?  11  ASP C CA  1 
ATOM 70   C C   . ASP A 1 19  ? 113.646 152.062 103.954 1.00 46.49  ?  11  ASP C C   1 
ATOM 71   O O   . ASP A 1 19  ? 113.006 151.692 104.943 1.00 49.98  ?  11  ASP C O   1 
ATOM 72   C CB  . ASP A 1 19  ? 114.069 154.225 102.681 1.00 48.64  ?  11  ASP C CB  1 
ATOM 73   C CG  . ASP A 1 19  ? 114.743 154.756 103.927 1.00 50.33  ?  11  ASP C CG  1 
ATOM 74   O OD1 . ASP A 1 19  ? 115.783 154.192 104.328 1.00 54.07  ?  11  ASP C OD1 1 
ATOM 75   O OD2 . ASP A 1 19  ? 114.237 155.742 104.504 1.00 46.67  -1 11  ASP C OD2 1 
ATOM 76   N N   . GLY A 1 20  ? 114.860 151.597 103.670 1.00 40.40  ?  12  GLY C N   1 
ATOM 77   C CA  . GLY A 1 20  ? 115.501 150.592 104.479 1.00 35.56  ?  12  GLY C CA  1 
ATOM 78   C C   . GLY A 1 20  ? 115.379 149.214 103.861 1.00 35.56  ?  12  GLY C C   1 
ATOM 79   O O   . GLY A 1 20  ? 114.292 148.779 103.466 1.00 36.41  ?  12  GLY C O   1 
ATOM 80   N N   . PRO A 1 21  ? 116.500 148.501 103.757 1.00 33.92  ?  13  PRO C N   1 
ATOM 81   C CA  . PRO A 1 21  ? 116.466 147.171 103.139 1.00 30.41  ?  13  PRO C CA  1 
ATOM 82   C C   . PRO A 1 21  ? 115.690 146.176 103.989 1.00 28.35  ?  13  PRO C C   1 
ATOM 83   O O   . PRO A 1 21  ? 115.788 146.169 105.218 1.00 30.32  ?  13  PRO C O   1 
ATOM 84   C CB  . PRO A 1 21  ? 117.947 146.789 103.038 1.00 28.15  ?  13  PRO C CB  1 
ATOM 85   C CG  . PRO A 1 21  ? 118.608 147.573 104.120 1.00 27.72  ?  13  PRO C CG  1 
ATOM 86   C CD  . PRO A 1 21  ? 117.850 148.868 104.217 1.00 30.27  ?  13  PRO C CD  1 
ATOM 87   N N   . VAL A 1 22  ? 114.912 145.333 103.317 1.00 26.60  ?  14  VAL C N   1 
ATOM 88   C CA  . VAL A 1 22  ? 114.138 144.278 103.959 1.00 24.81  ?  14  VAL C CA  1 
ATOM 89   C C   . VAL A 1 22  ? 114.602 142.949 103.380 1.00 24.76  ?  14  VAL C C   1 
ATOM 90   O O   . VAL A 1 22  ? 114.573 142.754 102.158 1.00 27.69  ?  14  VAL C O   1 
ATOM 91   C CB  . VAL A 1 22  ? 112.627 144.467 103.754 1.00 24.47  ?  14  VAL C CB  1 
ATOM 92   C CG1 . VAL A 1 22  ? 111.850 143.458 104.585 1.00 27.39  ?  14  VAL C CG1 1 
ATOM 93   C CG2 . VAL A 1 22  ? 112.221 145.889 104.113 1.00 23.89  ?  14  VAL C CG2 1 
ATOM 94   N N   . GLN A 1 23  ? 115.029 142.039 104.252 1.00 21.92  ?  15  GLN C N   1 
ATOM 95   C CA  . GLN A 1 23  ? 115.602 140.770 103.824 1.00 22.66  ?  15  GLN C CA  1 
ATOM 96   C C   . GLN A 1 23  ? 115.036 139.643 104.673 1.00 22.28  ?  15  GLN C C   1 
ATOM 97   O O   . GLN A 1 23  ? 114.825 139.817 105.876 1.00 22.91  ?  15  GLN C O   1 
ATOM 98   C CB  . GLN A 1 23  ? 117.132 140.796 103.932 1.00 24.25  ?  15  GLN C CB  1 
ATOM 99   C CG  . GLN A 1 23  ? 117.658 141.633 105.085 1.00 22.14  ?  15  GLN C CG  1 
ATOM 100  C CD  . GLN A 1 23  ? 119.016 142.241 104.794 1.00 17.91  ?  15  GLN C CD  1 
ATOM 101  O OE1 . GLN A 1 23  ? 119.445 142.314 103.644 1.00 16.55  ?  15  GLN C OE1 1 
ATOM 102  N NE2 . GLN A 1 23  ? 119.701 142.681 105.843 1.00 17.47  ?  15  GLN C NE2 1 
ATOM 103  N N   . GLY A 1 24  ? 114.788 138.497 104.043 1.00 21.29  ?  16  GLY C N   1 
ATOM 104  C CA  . GLY A 1 24  ? 114.336 137.323 104.764 1.00 22.93  ?  16  GLY C CA  1 
ATOM 105  C C   . GLY A 1 24  ? 112.879 137.368 105.171 1.00 24.98  ?  16  GLY C C   1 
ATOM 106  O O   . GLY A 1 24  ? 112.562 137.390 106.363 1.00 29.08  ?  16  GLY C O   1 
ATOM 107  N N   . ILE A 1 25  ? 111.981 137.381 104.191 1.00 22.38  ?  17  ILE C N   1 
ATOM 108  C CA  . ILE A 1 25  ? 110.543 137.367 104.431 1.00 23.61  ?  17  ILE C CA  1 
ATOM 109  C C   . ILE A 1 25  ? 110.024 135.989 104.048 1.00 25.42  ?  17  ILE C C   1 
ATOM 110  O O   . ILE A 1 25  ? 110.098 135.593 102.880 1.00 27.17  ?  17  ILE C O   1 
ATOM 111  C CB  . ILE A 1 25  ? 109.822 138.468 103.640 1.00 24.33  ?  17  ILE C CB  1 
ATOM 112  C CG1 . ILE A 1 25  ? 110.591 139.783 103.746 1.00 22.88  ?  17  ILE C CG1 1 
ATOM 113  C CG2 . ILE A 1 25  ? 108.397 138.625 104.137 1.00 21.54  ?  17  ILE C CG2 1 
ATOM 114  C CD1 . ILE A 1 25  ? 111.210 140.231 102.445 1.00 26.06  ?  17  ILE C CD1 1 
ATOM 115  N N   . ILE A 1 26  ? 109.566 135.245 105.061 1.00 24.51  ?  18  ILE C N   1 
ATOM 116  C CA  . ILE A 1 26  ? 109.128 133.842 104.802 1.00 24.36  ?  18  ILE C CA  1 
ATOM 117  C C   . ILE A 1 26  ? 107.718 133.606 105.362 1.00 24.62  ?  18  ILE C C   1 
ATOM 118  O O   . ILE A 1 26  ? 107.493 133.911 106.553 1.00 27.94  ?  18  ILE C O   1 
ATOM 119  C CB  . ILE A 1 26  ? 110.151 132.832 105.355 1.00 24.43  ?  18  ILE C CB  1 
ATOM 120  C CG1 . ILE A 1 26  ? 111.499 132.968 104.650 1.00 22.03  ?  18  ILE C CG1 1 
ATOM 121  C CG2 . ILE A 1 26  ? 109.615 131.405 105.265 1.00 25.26  ?  18  ILE C CG2 1 
ATOM 122  C CD1 . ILE A 1 26  ? 112.410 131.768 104.821 1.00 22.02  ?  18  ILE C CD1 1 
ATOM 123  N N   . ASN A 1 27  ? 106.820 133.090 104.528 1.00 24.34  ?  19  ASN C N   1 
ATOM 124  C CA  . ASN A 1 27  ? 105.444 132.774 104.900 1.00 28.83  ?  19  ASN C CA  1 
ATOM 125  C C   . ASN A 1 27  ? 105.222 131.283 104.682 1.00 32.93  ?  19  ASN C C   1 
ATOM 126  O O   . ASN A 1 27  ? 105.315 130.797 103.551 1.00 33.84  ?  19  ASN C O   1 
ATOM 127  C CB  . ASN A 1 27  ? 104.453 133.603 104.084 1.00 29.86  ?  19  ASN C CB  1 
ATOM 128  C CG  . ASN A 1 27  ? 103.013 133.212 104.346 1.00 29.12  ?  19  ASN C CG  1 
ATOM 129  O OD1 . ASN A 1 27  ? 102.548 133.232 105.485 1.00 29.88  ?  19  ASN C OD1 1 
ATOM 130  N ND2 . ASN A 1 27  ? 102.299 132.849 103.286 1.00 26.34  ?  19  ASN C ND2 1 
ATOM 131  N N   . PHE A 1 28  ? 104.930 130.559 105.762 1.00 34.71  ?  20  PHE C N   1 
ATOM 132  C CA  . PHE A 1 28  ? 104.673 129.124 105.709 1.00 38.96  ?  20  PHE C CA  1 
ATOM 133  C C   . PHE A 1 28  ? 103.239 128.847 106.141 1.00 43.50  ?  20  PHE C C   1 
ATOM 134  O O   . PHE A 1 28  ? 102.826 129.253 107.234 1.00 47.56  ?  20  PHE C O   1 
ATOM 135  C CB  . PHE A 1 28  ? 105.649 128.353 106.597 1.00 44.73  ?  20  PHE C CB  1 
ATOM 136  C CG  . PHE A 1 28  ? 106.839 127.804 105.862 1.00 43.10  ?  20  PHE C CG  1 
ATOM 137  C CD1 . PHE A 1 28  ? 106.704 126.720 105.013 1.00 43.98  ?  20  PHE C CD1 1 
ATOM 138  C CD2 . PHE A 1 28  ? 108.094 128.357 106.041 1.00 38.33  ?  20  PHE C CD2 1 
ATOM 139  C CE1 . PHE A 1 28  ? 107.799 126.209 104.339 1.00 47.10  ?  20  PHE C CE1 1 
ATOM 140  C CE2 . PHE A 1 28  ? 109.192 127.850 105.374 1.00 38.50  ?  20  PHE C CE2 1 
ATOM 141  C CZ  . PHE A 1 28  ? 109.045 126.777 104.519 1.00 43.62  ?  20  PHE C CZ  1 
ATOM 142  N N   . GLU A 1 29  ? 102.491 128.146 105.292 1.00 44.08  ?  21  GLU C N   1 
ATOM 143  C CA  . GLU A 1 29  ? 101.120 127.739 105.592 1.00 49.54  ?  21  GLU C CA  1 
ATOM 144  C C   . GLU A 1 29  ? 100.956 126.286 105.166 1.00 48.82  ?  21  GLU C C   1 
ATOM 145  O O   . GLU A 1 29  ? 100.859 125.994 103.969 1.00 47.51  ?  21  GLU C O   1 
ATOM 146  C CB  . GLU A 1 29  ? 100.108 128.640 104.883 1.00 53.29  ?  21  GLU C CB  1 
ATOM 147  C CG  . GLU A 1 29  ? 98.669  128.158 104.976 1.00 60.45  ?  21  GLU C CG  1 
ATOM 148  C CD  . GLU A 1 29  ? 97.690  129.131 104.352 1.00 65.14  ?  21  GLU C CD  1 
ATOM 149  O OE1 . GLU A 1 29  ? 98.105  130.264 104.025 1.00 64.22  ?  21  GLU C OE1 1 
ATOM 150  O OE2 . GLU A 1 29  ? 96.507  128.767 104.188 1.00 64.00  -1 21  GLU C OE2 1 
ATOM 151  N N   . GLN A 1 30  ? 100.920 125.378 106.138 1.00 48.04  ?  22  GLN C N   1 
ATOM 152  C CA  . GLN A 1 30  ? 100.861 123.948 105.877 1.00 50.83  ?  22  GLN C CA  1 
ATOM 153  C C   . GLN A 1 30  ? 99.586  123.354 106.458 1.00 54.87  ?  22  GLN C C   1 
ATOM 154  O O   . GLN A 1 30  ? 99.181  123.696 107.573 1.00 53.25  ?  22  GLN C O   1 
ATOM 155  C CB  . GLN A 1 30  ? 102.078 123.225 106.465 1.00 49.29  ?  22  GLN C CB  1 
ATOM 156  C CG  . GLN A 1 30  ? 103.341 123.342 105.631 1.00 48.84  ?  22  GLN C CG  1 
ATOM 157  C CD  . GLN A 1 30  ? 104.600 123.290 106.473 1.00 49.90  ?  22  GLN C CD  1 
ATOM 158  O OE1 . GLN A 1 30  ? 104.594 122.766 107.588 1.00 49.86  ?  22  GLN C OE1 1 
ATOM 159  N NE2 . GLN A 1 30  ? 105.690 123.831 105.944 1.00 48.78  ?  22  GLN C NE2 1 
ATOM 160  N N   . LYS A 1 31  ? 98.962  122.460 105.694 1.00 55.39  ?  23  LYS C N   1 
ATOM 161  C CA  . LYS A 1 31  ? 97.790  121.709 106.129 1.00 53.82  ?  23  LYS C CA  1 
ATOM 162  C C   . LYS A 1 31  ? 98.143  120.229 106.084 1.00 53.95  ?  23  LYS C C   1 
ATOM 163  O O   . LYS A 1 31  ? 98.242  119.645 104.998 1.00 54.78  ?  23  LYS C O   1 
ATOM 164  C CB  . LYS A 1 31  ? 96.580  122.015 105.245 1.00 53.83  ?  23  LYS C CB  1 
ATOM 165  C CG  . LYS A 1 31  ? 95.827  123.278 105.636 1.00 52.24  ?  23  LYS C CG  1 
ATOM 166  C CD  . LYS A 1 31  ? 94.394  123.259 105.121 1.00 55.54  ?  23  LYS C CD  1 
ATOM 167  C CE  . LYS A 1 31  ? 93.728  121.912 105.358 1.00 57.07  ?  23  LYS C CE  1 
ATOM 168  N NZ  . LYS A 1 31  ? 93.669  121.562 106.804 1.00 56.48  1  23  LYS C NZ  1 
ATOM 169  N N   . GLU A 1 32  ? 98.332  119.627 107.258 1.00 53.98  ?  24  GLU C N   1 
ATOM 170  C CA  . GLU A 1 32  ? 98.764  118.236 107.388 1.00 55.86  ?  24  GLU C CA  1 
ATOM 171  C C   . GLU A 1 32  ? 100.077 118.007 106.635 1.00 58.44  ?  24  GLU C C   1 
ATOM 172  O O   . GLU A 1 32  ? 100.163 117.229 105.684 1.00 62.27  ?  24  GLU C O   1 
ATOM 173  C CB  . GLU A 1 32  ? 97.672  117.276 106.905 1.00 56.67  ?  24  GLU C CB  1 
ATOM 174  C CG  . GLU A 1 32  ? 96.345  117.426 107.631 1.00 62.98  ?  24  GLU C CG  1 
ATOM 175  C CD  . GLU A 1 32  ? 95.222  117.853 106.706 1.00 65.14  ?  24  GLU C CD  1 
ATOM 176  O OE1 . GLU A 1 32  ? 95.301  118.966 106.145 1.00 63.46  ?  24  GLU C OE1 1 
ATOM 177  O OE2 . GLU A 1 32  ? 94.260  117.074 106.537 1.00 66.01  -1 24  GLU C OE2 1 
ATOM 178  N N   . SER A 1 33  ? 101.109 118.715 107.094 1.00 55.32  ?  25  SER C N   1 
ATOM 179  C CA  . SER A 1 33  ? 102.394 118.726 106.403 1.00 56.02  ?  25  SER C CA  1 
ATOM 180  C C   . SER A 1 33  ? 103.062 117.357 106.442 1.00 59.63  ?  25  SER C C   1 
ATOM 181  O O   . SER A 1 33  ? 103.266 116.737 105.393 1.00 61.97  ?  25  SER C O   1 
ATOM 182  C CB  . SER A 1 33  ? 103.322 119.779 107.013 1.00 57.72  ?  25  SER C CB  1 
ATOM 183  O OG  . SER A 1 33  ? 103.719 119.413 108.322 1.00 60.40  ?  25  SER C OG  1 
ATOM 184  N N   . ASN A 1 34  ? 103.392 116.877 107.641 1.00 59.77  ?  26  ASN C N   1 
ATOM 185  C CA  . ASN A 1 34  ? 104.051 115.584 107.835 1.00 58.66  ?  26  ASN C CA  1 
ATOM 186  C C   . ASN A 1 34  ? 105.342 115.495 107.017 1.00 59.61  ?  26  ASN C C   1 
ATOM 187  O O   . ASN A 1 34  ? 105.540 114.588 106.205 1.00 59.31  ?  26  ASN C O   1 
ATOM 188  C CB  . ASN A 1 34  ? 103.099 114.431 107.500 1.00 59.30  ?  26  ASN C CB  1 
ATOM 189  C CG  . ASN A 1 34  ? 102.241 114.021 108.679 1.00 64.47  ?  26  ASN C CG  1 
ATOM 190  O OD1 . ASN A 1 34  ? 101.097 114.459 108.811 1.00 69.26  ?  26  ASN C OD1 1 
ATOM 191  N ND2 . ASN A 1 34  ? 102.787 113.175 109.544 1.00 61.99  ?  26  ASN C ND2 1 
ATOM 192  N N   . GLY A 1 35  ? 106.228 116.460 107.251 1.00 58.45  ?  27  GLY C N   1 
ATOM 193  C CA  . GLY A 1 35  ? 107.486 116.520 106.547 1.00 54.06  ?  27  GLY C CA  1 
ATOM 194  C C   . GLY A 1 35  ? 108.466 117.489 107.179 1.00 56.87  ?  27  GLY C C   1 
ATOM 195  O O   . GLY A 1 35  ? 108.099 118.339 107.995 1.00 55.15  ?  27  GLY C O   1 
ATOM 196  N N   . PRO A 1 36  ? 109.740 117.374 106.809 1.00 60.77  ?  28  PRO C N   1 
ATOM 197  C CA  . PRO A 1 36  ? 110.764 118.258 107.378 1.00 57.27  ?  28  PRO C CA  1 
ATOM 198  C C   . PRO A 1 36  ? 110.959 119.538 106.581 1.00 52.53  ?  28  PRO C C   1 
ATOM 199  O O   . PRO A 1 36  ? 110.895 119.563 105.351 1.00 53.35  ?  28  PRO C O   1 
ATOM 200  C CB  . PRO A 1 36  ? 112.025 117.386 107.331 1.00 52.87  ?  28  PRO C CB  1 
ATOM 201  C CG  . PRO A 1 36  ? 111.816 116.488 106.152 1.00 47.86  ?  28  PRO C CG  1 
ATOM 202  C CD  . PRO A 1 36  ? 110.323 116.353 105.921 1.00 54.45  ?  28  PRO C CD  1 
ATOM 203  N N   . VAL A 1 37  ? 111.197 120.621 107.317 1.00 48.48  ?  29  VAL C N   1 
ATOM 204  C CA  . VAL A 1 37  ? 111.441 121.943 106.754 1.00 47.21  ?  29  VAL C CA  1 
ATOM 205  C C   . VAL A 1 37  ? 112.684 122.541 107.401 1.00 46.15  ?  29  VAL C C   1 
ATOM 206  O O   . VAL A 1 37  ? 112.845 122.489 108.626 1.00 49.39  ?  29  VAL C O   1 
ATOM 207  C CB  . VAL A 1 37  ? 110.218 122.868 106.912 1.00 46.90  ?  29  VAL C CB  1 
ATOM 208  C CG1 . VAL A 1 37  ? 109.779 122.937 108.331 1.00 44.83  ?  29  VAL C CG1 1 
ATOM 209  C CG2 . VAL A 1 37  ? 110.564 124.276 106.443 1.00 44.88  ?  29  VAL C CG2 1 
ATOM 210  N N   . LYS A 1 38  ? 113.565 123.099 106.572 1.00 44.07  ?  30  LYS C N   1 
ATOM 211  C CA  . LYS A 1 38  ? 114.853 123.616 107.016 1.00 41.23  ?  30  LYS C CA  1 
ATOM 212  C C   . LYS A 1 38  ? 115.079 124.990 106.404 1.00 38.56  ?  30  LYS C C   1 
ATOM 213  O O   . LYS A 1 38  ? 115.184 125.120 105.182 1.00 38.56  ?  30  LYS C O   1 
ATOM 214  C CB  . LYS A 1 38  ? 115.983 122.659 106.631 1.00 42.71  ?  30  LYS C CB  1 
ATOM 215  C CG  . LYS A 1 38  ? 117.379 123.212 106.849 1.00 40.00  ?  30  LYS C CG  1 
ATOM 216  C CD  . LYS A 1 38  ? 117.725 123.310 108.312 1.00 40.23  ?  30  LYS C CD  1 
ATOM 217  C CE  . LYS A 1 38  ? 119.221 123.492 108.529 1.00 40.83  ?  30  LYS C CE  1 
ATOM 218  N NZ  . LYS A 1 38  ? 120.012 122.344 108.005 1.00 39.78  1  30  LYS C NZ  1 
ATOM 219  N N   . VAL A 1 39  ? 115.144 126.007 107.259 1.00 38.13  ?  31  VAL C N   1 
ATOM 220  C CA  . VAL A 1 39  ? 115.504 127.366 106.871 1.00 40.08  ?  31  VAL C CA  1 
ATOM 221  C C   . VAL A 1 39  ? 116.822 127.740 107.539 1.00 40.96  ?  31  VAL C C   1 
ATOM 222  O O   . VAL A 1 39  ? 117.024 127.481 108.731 1.00 42.68  ?  31  VAL C O   1 
ATOM 223  C CB  . VAL A 1 39  ? 114.370 128.368 107.178 1.00 39.42  ?  31  VAL C CB  1 
ATOM 224  C CG1 . VAL A 1 39  ? 114.172 128.510 108.610 1.00 38.01  ?  31  VAL C CG1 1 
ATOM 225  C CG2 . VAL A 1 39  ? 114.737 129.753 106.645 1.00 36.32  ?  31  VAL C CG2 1 
ATOM 226  N N   . TRP A 1 40  ? 117.729 128.314 106.748 1.00 39.62  ?  32  TRP C N   1 
ATOM 227  C CA  . TRP A 1 40  ? 119.120 128.503 107.125 1.00 41.94  ?  32  TRP C CA  1 
ATOM 228  C C   . TRP A 1 40  ? 119.790 129.508 106.200 1.00 47.10  ?  32  TRP C C   1 
ATOM 229  O O   . TRP A 1 40  ? 119.367 129.708 105.060 1.00 52.87  ?  32  TRP C O   1 
ATOM 230  C CB  . TRP A 1 40  ? 119.843 127.146 107.163 1.00 43.21  ?  32  TRP C CB  1 
ATOM 231  C CG  . TRP A 1 40  ? 121.118 127.145 107.940 1.00 46.40  ?  32  TRP C CG  1 
ATOM 232  C CD1 . TRP A 1 40  ? 121.389 127.836 109.076 1.00 48.02  ?  32  TRP C CD1 1 
ATOM 233  C CD2 . TRP A 1 40  ? 122.247 126.292 107.715 1.00 44.13  ?  32  TRP C CD2 1 
ATOM 234  N NE1 . TRP A 1 40  ? 122.660 127.551 109.516 1.00 51.88  ?  32  TRP C NE1 1 
ATOM 235  C CE2 . TRP A 1 40  ? 123.199 126.588 108.705 1.00 46.70  ?  32  TRP C CE2 1 
ATOM 236  C CE3 . TRP A 1 40  ? 122.553 125.325 106.754 1.00 42.91  ?  32  TRP C CE3 1 
ATOM 237  C CZ2 . TRP A 1 40  ? 124.438 125.958 108.760 1.00 49.52  ?  32  TRP C CZ2 1 
ATOM 238  C CZ3 . TRP A 1 40  ? 123.782 124.701 106.807 1.00 43.59  ?  32  TRP C CZ3 1 
ATOM 239  C CH2 . TRP A 1 40  ? 124.710 125.018 107.804 1.00 48.13  ?  32  TRP C CH2 1 
ATOM 240  N N   . GLY A 1 41  ? 120.823 130.146 106.721 1.00 43.38  ?  33  GLY C N   1 
ATOM 241  C CA  . GLY A 1 41  ? 121.521 131.225 106.048 1.00 41.37  ?  33  GLY C CA  1 
ATOM 242  C C   . GLY A 1 41  ? 121.749 132.370 107.017 1.00 42.12  ?  33  GLY C C   1 
ATOM 243  O O   . GLY A 1 41  ? 121.011 132.566 107.982 1.00 41.68  ?  33  GLY C O   1 
ATOM 244  N N   . SER A 1 42  ? 122.791 133.151 106.746 1.00 41.19  ?  34  SER C N   1 
ATOM 245  C CA  . SER A 1 42  ? 123.197 134.246 107.615 1.00 37.65  ?  34  SER C CA  1 
ATOM 246  C C   . SER A 1 42  ? 122.919 135.592 106.956 1.00 34.43  ?  34  SER C C   1 
ATOM 247  O O   . SER A 1 42  ? 123.079 135.755 105.743 1.00 35.63  ?  34  SER C O   1 
ATOM 248  C CB  . SER A 1 42  ? 124.680 134.143 107.978 1.00 39.91  ?  34  SER C CB  1 
ATOM 249  O OG  . SER A 1 42  ? 124.910 133.068 108.873 1.00 45.22  ?  34  SER C OG  1 
ATOM 250  N N   . ILE A 1 43  ? 122.506 136.557 107.776 1.00 31.84  ?  35  ILE C N   1 
ATOM 251  C CA  . ILE A 1 43  ? 122.111 137.882 107.313 1.00 31.37  ?  35  ILE C CA  1 
ATOM 252  C C   . ILE A 1 43  ? 122.992 138.929 107.980 1.00 29.80  ?  35  ILE C C   1 
ATOM 253  O O   . ILE A 1 43  ? 123.290 138.835 109.175 1.00 30.62  ?  35  ILE C O   1 
ATOM 254  C CB  . ILE A 1 43  ? 120.623 138.172 107.607 1.00 29.17  ?  35  ILE C CB  1 
ATOM 255  C CG1 . ILE A 1 43  ? 119.765 136.936 107.330 1.00 29.56  ?  35  ILE C CG1 1 
ATOM 256  C CG2 . ILE A 1 43  ? 120.140 139.345 106.774 1.00 27.12  ?  35  ILE C CG2 1 
ATOM 257  C CD1 . ILE A 1 43  ? 118.291 137.159 107.573 1.00 28.44  ?  35  ILE C CD1 1 
ATOM 258  N N   . LYS A 1 44  ? 123.406 139.930 107.202 1.00 27.94  ?  36  LYS C N   1 
ATOM 259  C CA  . LYS A 1 44  ? 124.186 141.052 107.708 1.00 28.09  ?  36  LYS C CA  1 
ATOM 260  C C   . LYS A 1 44  ? 123.544 142.348 107.233 1.00 29.75  ?  36  LYS C C   1 
ATOM 261  O O   . LYS A 1 44  ? 123.291 142.513 106.034 1.00 30.05  ?  36  LYS C O   1 
ATOM 262  C CB  . LYS A 1 44  ? 125.644 140.970 107.243 1.00 31.37  ?  36  LYS C CB  1 
ATOM 263  C CG  . LYS A 1 44  ? 126.478 142.198 107.587 1.00 32.18  ?  36  LYS C CG  1 
ATOM 264  C CD  . LYS A 1 44  ? 126.879 142.980 106.345 1.00 31.06  ?  36  LYS C CD  1 
ATOM 265  C CE  . LYS A 1 44  ? 128.069 143.886 106.622 1.00 29.17  ?  36  LYS C CE  1 
ATOM 266  N NZ  . LYS A 1 44  ? 129.339 143.119 106.766 1.00 28.74  1  36  LYS C NZ  1 
ATOM 267  N N   . GLY A 1 45  ? 123.288 143.259 108.162 1.00 31.51  ?  37  GLY C N   1 
ATOM 268  C CA  . GLY A 1 45  ? 122.679 144.531 107.830 1.00 33.19  ?  37  GLY C CA  1 
ATOM 269  C C   . GLY A 1 45  ? 123.426 145.686 108.462 1.00 38.65  ?  37  GLY C C   1 
ATOM 270  O O   . GLY A 1 45  ? 123.991 145.569 109.549 1.00 43.33  ?  37  GLY C O   1 
ATOM 271  N N   . LEU A 1 46  ? 123.419 146.817 107.758 1.00 40.57  ?  38  LEU C N   1 
ATOM 272  C CA  . LEU A 1 46  ? 124.107 148.011 108.226 1.00 49.70  ?  38  LEU C CA  1 
ATOM 273  C C   . LEU A 1 46  ? 123.410 149.243 107.667 1.00 49.34  ?  38  LEU C C   1 
ATOM 274  O O   . LEU A 1 46  ? 122.989 149.254 106.506 1.00 49.78  ?  38  LEU C O   1 
ATOM 275  C CB  . LEU A 1 46  ? 125.591 147.984 107.823 1.00 50.64  ?  38  LEU C CB  1 
ATOM 276  C CG  . LEU A 1 46  ? 126.479 149.236 107.852 1.00 50.83  ?  38  LEU C CG  1 
ATOM 277  C CD1 . LEU A 1 46  ? 127.930 148.817 108.009 1.00 50.18  ?  38  LEU C CD1 1 
ATOM 278  C CD2 . LEU A 1 46  ? 126.336 150.088 106.595 1.00 53.75  ?  38  LEU C CD2 1 
ATOM 279  N N   . THR A 1 47  ? 123.291 150.274 108.501 1.00 51.59  ?  39  THR C N   1 
ATOM 280  C CA  . THR A 1 47  ? 122.759 151.567 108.091 1.00 60.01  ?  39  THR C CA  1 
ATOM 281  C C   . THR A 1 47  ? 123.683 152.665 108.594 1.00 68.73  ?  39  THR C C   1 
ATOM 282  O O   . THR A 1 47  ? 124.086 152.655 109.762 1.00 74.58  ?  39  THR C O   1 
ATOM 283  C CB  . THR A 1 47  ? 121.329 151.779 108.609 1.00 60.26  ?  39  THR C CB  1 
ATOM 284  O OG1 . THR A 1 47  ? 120.953 153.153 108.446 1.00 59.95  ?  39  THR C OG1 1 
ATOM 285  C CG2 . THR A 1 47  ? 121.208 151.378 110.065 1.00 63.57  ?  39  THR C CG2 1 
ATOM 286  N N   . GLU A 1 48  ? 124.025 153.601 107.710 1.00 69.61  ?  40  GLU C N   1 
ATOM 287  C CA  . GLU A 1 48  ? 124.952 154.677 108.033 1.00 73.72  ?  40  GLU C CA  1 
ATOM 288  C C   . GLU A 1 48  ? 124.395 155.985 107.489 1.00 81.48  ?  40  GLU C C   1 
ATOM 289  O O   . GLU A 1 48  ? 123.344 156.017 106.839 1.00 86.68  ?  40  GLU C O   1 
ATOM 290  C CB  . GLU A 1 48  ? 126.348 154.388 107.468 1.00 73.85  ?  40  GLU C CB  1 
ATOM 291  C CG  . GLU A 1 48  ? 127.488 154.738 108.410 1.00 79.73  ?  40  GLU C CG  1 
ATOM 292  C CD  . GLU A 1 48  ? 128.795 154.083 108.010 1.00 83.99  ?  40  GLU C CD  1 
ATOM 293  O OE1 . GLU A 1 48  ? 128.824 153.402 106.965 1.00 80.86  ?  40  GLU C OE1 1 
ATOM 294  O OE2 . GLU A 1 48  ? 129.794 154.250 108.742 1.00 88.46  -1 40  GLU C OE2 1 
ATOM 295  N N   . GLY A 1 49  ? 125.109 157.075 107.758 1.00 82.55  ?  41  GLY C N   1 
ATOM 296  C CA  . GLY A 1 49  ? 124.685 158.386 107.305 1.00 86.07  ?  41  GLY C CA  1 
ATOM 297  C C   . GLY A 1 49  ? 123.448 158.884 108.021 1.00 92.08  ?  41  GLY C C   1 
ATOM 298  O O   . GLY A 1 49  ? 123.508 159.240 109.202 1.00 94.69  ?  41  GLY C O   1 
ATOM 299  N N   . LEU A 1 50  ? 122.320 158.917 107.306 1.00 96.07  ?  42  LEU C N   1 
ATOM 300  C CA  . LEU A 1 50  ? 121.029 159.316 107.870 1.00 101.18 ?  42  LEU C CA  1 
ATOM 301  C C   . LEU A 1 50  ? 121.083 160.735 108.433 1.00 107.80 ?  42  LEU C C   1 
ATOM 302  O O   . LEU A 1 50  ? 120.480 161.036 109.466 1.00 110.50 ?  42  LEU C O   1 
ATOM 303  C CB  . LEU A 1 50  ? 120.567 158.322 108.937 1.00 98.30  ?  42  LEU C CB  1 
ATOM 304  C CG  . LEU A 1 50  ? 119.421 157.380 108.558 1.00 97.12  ?  42  LEU C CG  1 
ATOM 305  C CD1 . LEU A 1 50  ? 119.332 156.232 109.550 1.00 96.01  ?  42  LEU C CD1 1 
ATOM 306  C CD2 . LEU A 1 50  ? 118.102 158.128 108.477 1.00 103.05 ?  42  LEU C CD2 1 
ATOM 307  N N   . HIS A 1 51  ? 121.810 161.613 107.749 1.00 108.75 ?  43  HIS C N   1 
ATOM 308  C CA  . HIS A 1 51  ? 121.958 162.986 108.211 1.00 111.41 ?  43  HIS C CA  1 
ATOM 309  C C   . HIS A 1 51  ? 120.693 163.789 107.928 1.00 113.81 ?  43  HIS C C   1 
ATOM 310  O O   . HIS A 1 51  ? 120.086 163.670 106.860 1.00 112.58 ?  43  HIS C O   1 
ATOM 311  C CB  . HIS A 1 51  ? 123.160 163.645 107.534 1.00 112.44 ?  43  HIS C CB  1 
ATOM 312  C CG  . HIS A 1 51  ? 123.279 165.113 107.803 1.00 116.99 ?  43  HIS C CG  1 
ATOM 313  N ND1 . HIS A 1 51  ? 122.616 166.063 107.056 1.00 117.69 ?  43  HIS C ND1 1 
ATOM 314  C CD2 . HIS A 1 51  ? 123.988 165.794 108.732 1.00 118.15 ?  43  HIS C CD2 1 
ATOM 315  C CE1 . HIS A 1 51  ? 122.910 167.266 107.517 1.00 116.72 ?  43  HIS C CE1 1 
ATOM 316  N NE2 . HIS A 1 51  ? 123.740 167.131 108.534 1.00 118.74 ?  43  HIS C NE2 1 
ATOM 317  N N   . GLY A 1 52  ? 120.300 164.612 108.898 1.00 116.05 ?  44  GLY C N   1 
ATOM 318  C CA  . GLY A 1 52  ? 119.157 165.488 108.716 1.00 117.65 ?  44  GLY C CA  1 
ATOM 319  C C   . GLY A 1 52  ? 117.822 164.789 108.650 1.00 118.87 ?  44  GLY C C   1 
ATOM 320  O O   . GLY A 1 52  ? 116.873 165.337 108.084 1.00 118.82 ?  44  GLY C O   1 
ATOM 321  N N   . PHE A 1 53  ? 117.715 163.590 109.212 1.00 116.85 ?  45  PHE C N   1 
ATOM 322  C CA  . PHE A 1 53  ? 116.464 162.844 109.183 1.00 115.25 ?  45  PHE C CA  1 
ATOM 323  C C   . PHE A 1 53  ? 115.535 163.399 110.260 1.00 116.82 ?  45  PHE C C   1 
ATOM 324  O O   . PHE A 1 53  ? 114.539 164.055 109.957 1.00 113.10 ?  45  PHE C O   1 
ATOM 325  C CB  . PHE A 1 53  ? 116.724 161.347 109.393 1.00 112.45 ?  45  PHE C CB  1 
ATOM 326  C CG  . PHE A 1 53  ? 115.499 160.544 109.754 1.00 117.95 ?  45  PHE C CG  1 
ATOM 327  C CD1 . PHE A 1 53  ? 114.274 160.794 109.149 1.00 118.95 ?  45  PHE C CD1 1 
ATOM 328  C CD2 . PHE A 1 53  ? 115.576 159.534 110.700 1.00 117.85 ?  45  PHE C CD2 1 
ATOM 329  C CE1 . PHE A 1 53  ? 113.155 160.054 109.484 1.00 115.98 ?  45  PHE C CE1 1 
ATOM 330  C CE2 . PHE A 1 53  ? 114.460 158.792 111.037 1.00 117.16 ?  45  PHE C CE2 1 
ATOM 331  C CZ  . PHE A 1 53  ? 113.249 159.053 110.428 1.00 116.13 ?  45  PHE C CZ  1 
ATOM 332  N N   . VAL A 1 89  ? 137.071 154.014 111.048 1.00 104.10 ?  81  VAL C N   1 
ATOM 333  C CA  . VAL A 1 89  ? 136.078 153.416 111.930 1.00 103.42 ?  81  VAL C CA  1 
ATOM 334  C C   . VAL A 1 89  ? 135.666 152.043 111.408 1.00 102.49 ?  81  VAL C C   1 
ATOM 335  O O   . VAL A 1 89  ? 134.786 151.391 111.973 1.00 100.27 ?  81  VAL C O   1 
ATOM 336  C CB  . VAL A 1 89  ? 134.851 154.333 112.092 1.00 100.20 ?  81  VAL C CB  1 
ATOM 337  C CG1 . VAL A 1 89  ? 135.292 155.762 112.366 1.00 94.61  ?  81  VAL C CG1 1 
ATOM 338  C CG2 . VAL A 1 89  ? 133.971 154.272 110.855 1.00 99.35  ?  81  VAL C CG2 1 
ATOM 339  N N   . GLY A 1 90  ? 136.312 151.612 110.326 1.00 104.32 ?  82  GLY C N   1 
ATOM 340  C CA  . GLY A 1 90  ? 136.025 150.323 109.726 1.00 102.79 ?  82  GLY C CA  1 
ATOM 341  C C   . GLY A 1 90  ? 136.240 149.160 110.671 1.00 99.38  ?  82  GLY C C   1 
ATOM 342  O O   . GLY A 1 90  ? 137.274 149.076 111.341 1.00 98.08  ?  82  GLY C O   1 
ATOM 343  N N   . ASP A 1 91  ? 135.269 148.254 110.734 1.00 97.40  ?  83  ASP C N   1 
ATOM 344  C CA  . ASP A 1 91  ? 135.304 147.109 111.638 1.00 93.97  ?  83  ASP C CA  1 
ATOM 345  C C   . ASP A 1 91  ? 135.479 145.838 110.815 1.00 86.96  ?  83  ASP C C   1 
ATOM 346  O O   . ASP A 1 91  ? 134.607 145.483 110.016 1.00 87.12  ?  83  ASP C O   1 
ATOM 347  C CB  . ASP A 1 91  ? 134.034 147.048 112.485 1.00 98.51  ?  83  ASP C CB  1 
ATOM 348  C CG  . ASP A 1 91  ? 132.773 147.230 111.662 1.00 101.66 ?  83  ASP C CG  1 
ATOM 349  O OD1 . ASP A 1 91  ? 132.516 148.365 111.210 1.00 103.27 ?  83  ASP C OD1 1 
ATOM 350  O OD2 . ASP A 1 91  ? 132.040 146.238 111.468 1.00 99.30  -1 83  ASP C OD2 1 
ATOM 351  N N   . LEU A 1 92  ? 136.604 145.157 111.012 1.00 83.64  ?  84  LEU C N   1 
ATOM 352  C CA  . LEU A 1 92  ? 136.848 143.881 110.355 1.00 83.25  ?  84  LEU C CA  1 
ATOM 353  C C   . LEU A 1 92  ? 136.043 142.798 111.066 1.00 83.87  ?  84  LEU C C   1 
ATOM 354  O O   . LEU A 1 92  ? 136.217 142.577 112.269 1.00 86.74  ?  84  LEU C O   1 
ATOM 355  C CB  . LEU A 1 92  ? 138.338 143.551 110.364 1.00 82.44  ?  84  LEU C CB  1 
ATOM 356  C CG  . LEU A 1 92  ? 138.755 142.085 110.200 1.00 83.01  ?  84  LEU C CG  1 
ATOM 357  C CD1 . LEU A 1 92  ? 138.322 141.536 108.849 1.00 83.81  ?  84  LEU C CD1 1 
ATOM 358  C CD2 . LEU A 1 92  ? 140.257 141.932 110.388 1.00 79.77  ?  84  LEU C CD2 1 
ATOM 359  N N   . GLY A 1 93  ? 135.159 142.129 110.327 1.00 78.35  ?  85  GLY C N   1 
ATOM 360  C CA  . GLY A 1 93  ? 134.289 141.133 110.918 1.00 71.14  ?  85  GLY C CA  1 
ATOM 361  C C   . GLY A 1 93  ? 133.927 140.051 109.927 1.00 66.38  ?  85  GLY C C   1 
ATOM 362  O O   . GLY A 1 93  ? 134.292 140.106 108.750 1.00 67.07  ?  85  GLY C O   1 
ATOM 363  N N   . ASN A 1 94  ? 133.207 139.049 110.428 1.00 62.95  ?  86  ASN C N   1 
ATOM 364  C CA  . ASN A 1 94  ? 132.729 137.949 109.599 1.00 57.34  ?  86  ASN C CA  1 
ATOM 365  C C   . ASN A 1 94  ? 131.713 137.124 110.376 1.00 53.91  ?  86  ASN C C   1 
ATOM 366  O O   . ASN A 1 94  ? 131.947 136.778 111.537 1.00 55.84  ?  86  ASN C O   1 
ATOM 367  C CB  . ASN A 1 94  ? 133.888 137.055 109.142 1.00 57.30  ?  86  ASN C CB  1 
ATOM 368  C CG  . ASN A 1 94  ? 134.832 136.699 110.275 1.00 54.05  ?  86  ASN C CG  1 
ATOM 369  O OD1 . ASN A 1 94  ? 135.361 137.575 110.959 1.00 55.15  ?  86  ASN C OD1 1 
ATOM 370  N ND2 . ASN A 1 94  ? 135.047 135.404 110.480 1.00 51.29  ?  86  ASN C ND2 1 
ATOM 371  N N   . VAL A 1 95  ? 130.590 136.801 109.740 1.00 53.01  ?  87  VAL C N   1 
ATOM 372  C CA  . VAL A 1 95  ? 129.605 135.901 110.325 1.00 52.38  ?  87  VAL C CA  1 
ATOM 373  C C   . VAL A 1 95  ? 129.864 134.506 109.773 1.00 58.67  ?  87  VAL C C   1 
ATOM 374  O O   . VAL A 1 95  ? 130.219 134.335 108.601 1.00 62.80  ?  87  VAL C O   1 
ATOM 375  C CB  . VAL A 1 95  ? 128.154 136.366 110.063 1.00 47.00  ?  87  VAL C CB  1 
ATOM 376  C CG1 . VAL A 1 95  ? 128.008 137.853 110.369 1.00 41.34  ?  87  VAL C CG1 1 
ATOM 377  C CG2 . VAL A 1 95  ? 127.713 136.057 108.656 1.00 46.98  ?  87  VAL C CG2 1 
ATOM 378  N N   . THR A 1 96  ? 129.725 133.503 110.639 1.00 60.00  ?  88  THR C N   1 
ATOM 379  C CA  . THR A 1 96  ? 130.202 132.161 110.344 1.00 64.49  ?  88  THR C CA  1 
ATOM 380  C C   . THR A 1 96  ? 129.176 131.133 110.799 1.00 68.43  ?  88  THR C C   1 
ATOM 381  O O   . THR A 1 96  ? 128.806 131.100 111.976 1.00 69.23  ?  88  THR C O   1 
ATOM 382  C CB  . THR A 1 96  ? 131.551 131.913 111.029 1.00 68.10  ?  88  THR C CB  1 
ATOM 383  O OG1 . THR A 1 96  ? 132.453 132.978 110.702 1.00 63.64  ?  88  THR C OG1 1 
ATOM 384  C CG2 . THR A 1 96  ? 132.154 130.614 110.564 1.00 70.67  ?  88  THR C CG2 1 
ATOM 385  N N   . ALA A 1 97  ? 128.716 130.297 109.863 1.00 70.62  ?  89  ALA C N   1 
ATOM 386  C CA  . ALA A 1 97  ? 127.700 129.281 110.137 1.00 69.18  ?  89  ALA C CA  1 
ATOM 387  C C   . ALA A 1 97  ? 128.008 127.998 109.354 1.00 73.53  ?  89  ALA C C   1 
ATOM 388  O O   . ALA A 1 97  ? 127.141 127.423 108.699 1.00 71.42  ?  89  ALA C O   1 
ATOM 389  C CB  . ALA A 1 97  ? 126.304 129.810 109.811 1.00 55.21  ?  89  ALA C CB  1 
ATOM 390  N N   . ASP A 1 98  ? 129.259 127.550 109.412 1.00 75.25  ?  90  ASP C N   1 
ATOM 391  C CA  . ASP A 1 98  ? 129.687 126.332 108.736 1.00 77.12  ?  90  ASP C CA  1 
ATOM 392  C C   . ASP A 1 98  ? 129.587 125.108 109.644 1.00 76.53  ?  90  ASP C C   1 
ATOM 393  O O   . ASP A 1 98  ? 128.918 125.115 110.681 1.00 74.45  ?  90  ASP C O   1 
ATOM 394  C CB  . ASP A 1 98  ? 131.107 126.465 108.178 1.00 82.61  ?  90  ASP C CB  1 
ATOM 395  C CG  . ASP A 1 98  ? 131.399 127.849 107.659 1.00 83.75  ?  90  ASP C CG  1 
ATOM 396  O OD1 . ASP A 1 98  ? 132.237 128.549 108.257 1.00 82.56  ?  90  ASP C OD1 1 
ATOM 397  O OD2 . ASP A 1 98  ? 130.782 128.231 106.643 1.00 82.26  -1 90  ASP C OD2 1 
ATOM 398  N N   . LYS A 1 99  ? 130.147 124.003 109.143 1.00 79.82  ?  91  LYS C N   1 
ATOM 399  C CA  . LYS A 1 99  ? 130.053 122.725 109.891 1.00 79.00  ?  91  LYS C CA  1 
ATOM 400  C C   . LYS A 1 99  ? 131.137 121.756 109.402 1.00 83.57  ?  91  LYS C C   1 
ATOM 401  O O   . LYS A 1 99  ? 131.620 121.936 108.264 1.00 89.29  ?  91  LYS C O   1 
ATOM 402  C CB  . LYS A 1 99  ? 128.654 122.126 109.715 1.00 75.53  ?  91  LYS C CB  1 
ATOM 403  C CG  . LYS A 1 99  ? 128.268 121.067 110.737 1.00 80.00  ?  91  LYS C CG  1 
ATOM 404  C CD  . LYS A 1 99  ? 126.778 120.748 110.727 1.00 79.46  ?  91  LYS C CD  1 
ATOM 405  C CE  . LYS A 1 99  ? 126.298 120.340 109.371 1.00 84.72  ?  91  LYS C CE  1 
ATOM 406  N NZ  . LYS A 1 99  ? 124.854 120.091 109.360 1.00 97.74  1  91  LYS C NZ  1 
ATOM 407  N N   . ASP A 1 100 ? 131.487 120.799 110.264 1.00 81.87  ?  92  ASP C N   1 
ATOM 408  C CA  . ASP A 1 100 ? 132.516 119.791 109.907 1.00 83.84  ?  92  ASP C CA  1 
ATOM 409  C C   . ASP A 1 100 ? 132.246 118.509 110.692 1.00 85.39  ?  92  ASP C C   1 
ATOM 410  O O   . ASP A 1 100 ? 131.408 118.543 111.619 1.00 89.15  ?  92  ASP C O   1 
ATOM 411  C CB  . ASP A 1 100 ? 133.923 120.328 110.122 1.00 86.42  ?  92  ASP C CB  1 
ATOM 412  C CG  . ASP A 1 100 ? 134.404 120.393 111.564 1.00 91.06  ?  92  ASP C CG  1 
ATOM 413  O OD1 . ASP A 1 100 ? 134.626 119.319 112.160 1.00 88.87  ?  92  ASP C OD1 1 
ATOM 414  O OD2 . ASP A 1 100 ? 134.549 121.520 112.083 1.00 93.76  -1 92  ASP C OD2 1 
ATOM 415  N N   . GLY A 1 101 ? 132.932 117.431 110.334 1.00 79.29  ?  93  GLY C N   1 
ATOM 416  C CA  . GLY A 1 101 ? 132.801 116.144 110.989 1.00 71.84  ?  93  GLY C CA  1 
ATOM 417  C C   . GLY A 1 101 ? 132.757 115.017 109.975 1.00 69.42  ?  93  GLY C C   1 
ATOM 418  O O   . GLY A 1 101 ? 132.100 115.108 108.934 1.00 69.13  ?  93  GLY C O   1 
ATOM 419  N N   . VAL A 1 102 ? 133.456 113.928 110.283 1.00 68.71  ?  94  VAL C N   1 
ATOM 420  C CA  . VAL A 1 102 ? 133.618 112.829 109.339 1.00 67.28  ?  94  VAL C CA  1 
ATOM 421  C C   . VAL A 1 102 ? 132.878 111.613 109.879 1.00 68.78  ?  94  VAL C C   1 
ATOM 422  O O   . VAL A 1 102 ? 132.888 111.349 111.088 1.00 71.47  ?  94  VAL C O   1 
ATOM 423  C CB  . VAL A 1 102 ? 135.107 112.514 109.082 1.00 66.89  ?  94  VAL C CB  1 
ATOM 424  C CG1 . VAL A 1 102 ? 135.811 113.740 108.510 1.00 71.34  ?  94  VAL C CG1 1 
ATOM 425  C CG2 . VAL A 1 102 ? 135.800 112.004 110.326 1.00 66.12  ?  94  VAL C CG2 1 
ATOM 426  N N   . ALA A 1 103 ? 132.205 110.890 108.986 1.00 68.23  ?  95  ALA C N   1 
ATOM 427  C CA  . ALA A 1 103 ? 131.417 109.729 109.371 1.00 68.77  ?  95  ALA C CA  1 
ATOM 428  C C   . ALA A 1 103 ? 131.427 108.724 108.230 1.00 72.34  ?  95  ALA C C   1 
ATOM 429  O O   . ALA A 1 103 ? 132.233 108.831 107.304 1.00 73.15  ?  95  ALA C O   1 
ATOM 430  C CB  . ALA A 1 103 ? 129.976 110.116 109.724 1.00 67.48  ?  95  ALA C CB  1 
ATOM 431  N N   . ASP A 1 104 ? 130.545 107.726 108.323 1.00 72.34  ?  96  ASP C N   1 
ATOM 432  C CA  . ASP A 1 104 ? 130.306 106.845 107.184 1.00 70.64  ?  96  ASP C CA  1 
ATOM 433  C C   . ASP A 1 104 ? 128.820 106.758 106.851 1.00 70.01  ?  96  ASP C C   1 
ATOM 434  O O   . ASP A 1 104 ? 128.448 106.700 105.676 1.00 71.59  ?  96  ASP C O   1 
ATOM 435  C CB  . ASP A 1 104 ? 130.903 105.455 107.435 1.00 68.86  ?  96  ASP C CB  1 
ATOM 436  C CG  . ASP A 1 104 ? 130.417 104.816 108.725 1.00 69.61  ?  96  ASP C CG  1 
ATOM 437  O OD1 . ASP A 1 104 ? 131.226 104.124 109.377 1.00 70.65  ?  96  ASP C OD1 1 
ATOM 438  O OD2 . ASP A 1 104 ? 129.232 104.974 109.078 1.00 71.40  -1 96  ASP C OD2 1 
ATOM 439  N N   . VAL A 1 105 ? 127.957 106.757 107.863 1.00 64.12  ?  97  VAL C N   1 
ATOM 440  C CA  . VAL A 1 105 ? 126.511 106.793 107.666 1.00 60.56  ?  97  VAL C CA  1 
ATOM 441  C C   . VAL A 1 105 ? 125.999 108.111 108.234 1.00 61.90  ?  97  VAL C C   1 
ATOM 442  O O   . VAL A 1 105 ? 126.075 108.341 109.447 1.00 63.73  ?  97  VAL C O   1 
ATOM 443  C CB  . VAL A 1 105 ? 125.802 105.599 108.326 1.00 59.54  ?  97  VAL C CB  1 
ATOM 444  C CG1 . VAL A 1 105 ? 124.309 105.870 108.463 1.00 61.30  ?  97  VAL C CG1 1 
ATOM 445  C CG2 . VAL A 1 105 ? 126.044 104.330 107.528 1.00 59.51  ?  97  VAL C CG2 1 
ATOM 446  N N   . SER A 1 106 ? 125.484 108.973 107.360 1.00 60.17  ?  98  SER C N   1 
ATOM 447  C CA  . SER A 1 106 ? 125.004 110.292 107.756 1.00 58.65  ?  98  SER C CA  1 
ATOM 448  C C   . SER A 1 106 ? 123.692 110.576 107.040 1.00 60.75  ?  98  SER C C   1 
ATOM 449  O O   . SER A 1 106 ? 123.647 110.593 105.807 1.00 67.09  ?  98  SER C O   1 
ATOM 450  C CB  . SER A 1 106 ? 126.036 111.376 107.435 1.00 62.75  ?  98  SER C CB  1 
ATOM 451  O OG  . SER A 1 106 ? 125.549 112.663 107.776 1.00 65.82  ?  98  SER C OG  1 
ATOM 452  N N   . ILE A 1 107 ? 122.634 110.798 107.815 1.00 56.92  ?  99  ILE C N   1 
ATOM 453  C CA  . ILE A 1 107 ? 121.314 111.122 107.286 1.00 58.31  ?  99  ILE C CA  1 
ATOM 454  C C   . ILE A 1 107 ? 120.838 112.402 107.956 1.00 59.95  ?  99  ILE C C   1 
ATOM 455  O O   . ILE A 1 107 ? 120.836 112.498 109.189 1.00 63.35  ?  99  ILE C O   1 
ATOM 456  C CB  . ILE A 1 107 ? 120.312 109.975 107.513 1.00 58.58  ?  99  ILE C CB  1 
ATOM 457  C CG1 . ILE A 1 107 ? 120.515 108.877 106.467 1.00 56.46  ?  99  ILE C CG1 1 
ATOM 458  C CG2 . ILE A 1 107 ? 118.882 110.491 107.469 1.00 57.79  ?  99  ILE C CG2 1 
ATOM 459  C CD1 . ILE A 1 107 ? 120.095 107.501 106.935 1.00 51.99  ?  99  ILE C CD1 1 
ATOM 460  N N   . GLU A 1 108 ? 120.443 113.386 107.150 1.00 57.62  ?  100 GLU C N   1 
ATOM 461  C CA  . GLU A 1 108 ? 120.005 114.675 107.670 1.00 58.25  ?  100 GLU C CA  1 
ATOM 462  C C   . GLU A 1 108 ? 118.795 115.161 106.890 1.00 62.05  ?  100 GLU C C   1 
ATOM 463  O O   . GLU A 1 108 ? 118.796 115.131 105.656 1.00 62.23  ?  100 GLU C O   1 
ATOM 464  C CB  . GLU A 1 108 ? 121.132 115.713 107.594 1.00 61.43  ?  100 GLU C CB  1 
ATOM 465  C CG  . GLU A 1 108 ? 121.980 115.800 108.853 1.00 68.72  ?  100 GLU C CG  1 
ATOM 466  C CD  . GLU A 1 108 ? 123.373 116.335 108.582 1.00 76.46  ?  100 GLU C CD  1 
ATOM 467  O OE1 . GLU A 1 108 ? 123.488 117.495 108.133 1.00 76.22  ?  100 GLU C OE1 1 
ATOM 468  O OE2 . GLU A 1 108 ? 124.352 115.595 108.816 1.00 76.18  -1 100 GLU C OE2 1 
ATOM 469  N N   . ASP A 1 109 ? 117.770 115.610 107.619 1.00 63.82  ?  101 ASP C N   1 
ATOM 470  C CA  . ASP A 1 109 ? 116.560 116.192 107.031 1.00 57.98  ?  101 ASP C CA  1 
ATOM 471  C C   . ASP A 1 109 ? 115.901 115.237 106.037 1.00 55.19  ?  101 ASP C C   1 
ATOM 472  O O   . ASP A 1 109 ? 115.378 115.654 105.004 1.00 56.07  ?  101 ASP C O   1 
ATOM 473  C CB  . ASP A 1 109 ? 116.861 117.538 106.367 1.00 61.33  ?  101 ASP C CB  1 
ATOM 474  C CG  . ASP A 1 109 ? 117.922 118.330 107.104 1.00 64.04  ?  101 ASP C CG  1 
ATOM 475  O OD1 . ASP A 1 109 ? 117.724 118.625 108.302 1.00 65.84  ?  101 ASP C OD1 1 
ATOM 476  O OD2 . ASP A 1 109 ? 118.957 118.658 106.488 1.00 62.09  -1 101 ASP C OD2 1 
ATOM 477  N N   . SER A 1 110 ? 115.910 113.945 106.359 1.00 53.07  ?  102 SER C N   1 
ATOM 478  C CA  . SER A 1 110 ? 115.393 112.917 105.468 1.00 50.43  ?  102 SER C CA  1 
ATOM 479  C C   . SER A 1 110 ? 114.249 112.176 106.154 1.00 45.76  ?  102 SER C C   1 
ATOM 480  O O   . SER A 1 110 ? 113.999 112.339 107.351 1.00 49.36  ?  102 SER C O   1 
ATOM 481  C CB  . SER A 1 110 ? 116.502 111.943 105.048 1.00 56.20  ?  102 SER C CB  1 
ATOM 482  O OG  . SER A 1 110 ? 117.283 112.484 103.997 1.00 66.02  ?  102 SER C OG  1 
ATOM 483  N N   . VAL A 1 111 ? 113.547 111.357 105.376 1.00 42.69  ?  103 VAL C N   1 
ATOM 484  C CA  . VAL A 1 111 ? 112.455 110.529 105.873 1.00 43.70  ?  103 VAL C CA  1 
ATOM 485  C C   . VAL A 1 111 ? 112.726 109.094 105.446 1.00 43.90  ?  103 VAL C C   1 
ATOM 486  O O   . VAL A 1 111 ? 112.755 108.796 104.245 1.00 46.53  ?  103 VAL C O   1 
ATOM 487  C CB  . VAL A 1 111 ? 111.086 110.998 105.351 1.00 41.76  ?  103 VAL C CB  1 
ATOM 488  C CG1 . VAL A 1 111 ? 109.988 110.059 105.825 1.00 41.31  ?  103 VAL C CG1 1 
ATOM 489  C CG2 . VAL A 1 111 ? 110.804 112.424 105.803 1.00 39.91  ?  103 VAL C CG2 1 
ATOM 490  N N   . ILE A 1 112 ? 112.924 108.208 106.421 1.00 41.15  ?  104 ILE C N   1 
ATOM 491  C CA  . ILE A 1 112 ? 113.229 106.806 106.171 1.00 44.16  ?  104 ILE C CA  1 
ATOM 492  C C   . ILE A 1 112 ? 112.167 105.952 106.849 1.00 47.34  ?  104 ILE C C   1 
ATOM 493  O O   . ILE A 1 112 ? 111.739 106.251 107.969 1.00 47.97  ?  104 ILE C O   1 
ATOM 494  C CB  . ILE A 1 112 ? 114.636 106.423 106.678 1.00 45.87  ?  104 ILE C CB  1 
ATOM 495  C CG1 . ILE A 1 112 ? 115.609 107.595 106.529 1.00 46.46  ?  104 ILE C CG1 1 
ATOM 496  C CG2 . ILE A 1 112 ? 115.154 105.203 105.935 1.00 42.68  ?  104 ILE C CG2 1 
ATOM 497  C CD1 . ILE A 1 112 ? 115.997 107.904 105.113 1.00 43.99  ?  104 ILE C CD1 1 
ATOM 498  N N   . SER A 1 113 ? 111.742 104.891 106.165 1.00 48.70  ?  105 SER C N   1 
ATOM 499  C CA  . SER A 1 113 ? 110.748 103.963 106.702 1.00 50.12  ?  105 SER C CA  1 
ATOM 500  C C   . SER A 1 113 ? 111.107 102.561 106.234 1.00 50.68  ?  105 SER C C   1 
ATOM 501  O O   . SER A 1 113 ? 110.925 102.232 105.056 1.00 51.76  ?  105 SER C O   1 
ATOM 502  C CB  . SER A 1 113 ? 109.336 104.344 106.260 1.00 51.75  ?  105 SER C CB  1 
ATOM 503  O OG  . SER A 1 113 ? 109.221 104.325 104.847 1.00 56.08  ?  105 SER C OG  1 
ATOM 504  N N   . LEU A 1 114 ? 111.611 101.735 107.149 1.00 51.90  ?  106 LEU C N   1 
ATOM 505  C CA  . LEU A 1 114 ? 111.996 100.355 106.851 1.00 54.88  ?  106 LEU C CA  1 
ATOM 506  C C   . LEU A 1 114 ? 111.227 99.443  107.801 1.00 58.03  ?  106 LEU C C   1 
ATOM 507  O O   . LEU A 1 114 ? 111.683 99.177  108.917 1.00 59.34  ?  106 LEU C O   1 
ATOM 508  C CB  . LEU A 1 114 ? 113.503 100.148 106.990 1.00 51.99  ?  106 LEU C CB  1 
ATOM 509  C CG  . LEU A 1 114 ? 114.460 101.276 106.591 1.00 43.98  ?  106 LEU C CG  1 
ATOM 510  C CD1 . LEU A 1 114 ? 115.902 100.835 106.780 1.00 38.32  ?  106 LEU C CD1 1 
ATOM 511  C CD2 . LEU A 1 114 ? 114.226 101.728 105.164 1.00 46.48  ?  106 LEU C CD2 1 
ATOM 512  N N   . SER A 1 115 ? 110.069 98.962  107.361 1.00 60.00  ?  107 SER C N   1 
ATOM 513  C CA  . SER A 1 115 ? 109.221 98.102  108.176 1.00 57.45  ?  107 SER C CA  1 
ATOM 514  C C   . SER A 1 115 ? 109.415 96.645  107.776 1.00 57.98  ?  107 SER C C   1 
ATOM 515  O O   . SER A 1 115 ? 109.423 96.311  106.588 1.00 58.97  ?  107 SER C O   1 
ATOM 516  C CB  . SER A 1 115 ? 107.750 98.493  108.031 1.00 61.13  ?  107 SER C CB  1 
ATOM 517  O OG  . SER A 1 115 ? 106.922 97.660  108.825 1.00 66.11  ?  107 SER C OG  1 
ATOM 518  N N   . GLY A 1 116 ? 109.567 95.786  108.772 1.00 56.34  ?  108 GLY C N   1 
ATOM 519  C CA  . GLY A 1 116 ? 109.756 94.371  108.541 1.00 55.95  ?  108 GLY C CA  1 
ATOM 520  C C   . GLY A 1 116 ? 110.608 93.766  109.639 1.00 54.04  ?  108 GLY C C   1 
ATOM 521  O O   . GLY A 1 116 ? 110.665 94.279  110.752 1.00 55.80  ?  108 GLY C O   1 
ATOM 522  N N   . ASP A 1 117 ? 111.254 92.653  109.272 1.00 53.28  ?  109 ASP C N   1 
ATOM 523  C CA  . ASP A 1 117 ? 112.107 91.924  110.240 1.00 56.24  ?  109 ASP C CA  1 
ATOM 524  C C   . ASP A 1 117 ? 113.576 92.263  109.995 1.00 54.97  ?  109 ASP C C   1 
ATOM 525  O O   . ASP A 1 117 ? 113.960 92.423  108.815 1.00 58.57  ?  109 ASP C O   1 
ATOM 526  C CB  . ASP A 1 117 ? 111.854 90.427  110.182 1.00 59.64  ?  109 ASP C CB  1 
ATOM 527  C CG  . ASP A 1 117 ? 110.425 90.001  110.484 1.00 64.19  ?  109 ASP C CG  1 
ATOM 528  O OD1 . ASP A 1 117 ? 109.517 90.433  109.744 1.00 64.97  ?  109 ASP C OD1 1 
ATOM 529  O OD2 . ASP A 1 117 ? 110.233 89.245  111.460 1.00 65.83  -1 109 ASP C OD2 1 
ATOM 530  N N   . HIS A 1 118 ? 114.351 92.367  111.065 1.00 54.12  ?  110 HIS C N   1 
ATOM 531  C CA  . HIS A 1 118 ? 115.783 92.673  111.029 1.00 54.88  ?  110 HIS C CA  1 
ATOM 532  C C   . HIS A 1 118 ? 116.035 94.025  110.351 1.00 53.17  ?  110 HIS C C   1 
ATOM 533  O O   . HIS A 1 118 ? 116.706 94.134  109.323 1.00 56.45  ?  110 HIS C O   1 
ATOM 534  C CB  . HIS A 1 118 ? 116.567 91.550  110.340 1.00 58.25  ?  110 HIS C CB  1 
ATOM 535  C CG  . HIS A 1 118 ? 116.338 90.198  110.940 1.00 61.96  ?  110 HIS C CG  1 
ATOM 536  N ND1 . HIS A 1 118 ? 115.901 89.120  110.200 1.00 63.66  ?  110 HIS C ND1 1 
ATOM 537  C CD2 . HIS A 1 118 ? 116.485 89.748  112.209 1.00 64.08  ?  110 HIS C CD2 1 
ATOM 538  C CE1 . HIS A 1 118 ? 115.790 88.064  110.987 1.00 66.25  ?  110 HIS C CE1 1 
ATOM 539  N NE2 . HIS A 1 118 ? 116.138 88.419  112.211 1.00 65.97  ?  110 HIS C NE2 1 
ATOM 540  N N   . CYS A 1 119 ? 115.470 95.059  110.968 1.00 50.28  ?  111 CYS C N   1 
ATOM 541  C CA  . CYS A 1 119 ? 115.668 96.440  110.541 1.00 47.95  ?  111 CYS C CA  1 
ATOM 542  C C   . CYS A 1 119 ? 116.734 97.060  111.435 1.00 49.91  ?  111 CYS C C   1 
ATOM 543  O O   . CYS A 1 119 ? 116.445 97.474  112.563 1.00 54.61  ?  111 CYS C O   1 
ATOM 544  C CB  . CYS A 1 119 ? 114.360 97.225  110.609 1.00 48.90  ?  111 CYS C CB  1 
ATOM 545  S SG  . CYS A 1 119 ? 112.956 96.395  109.830 1.00 52.14  ?  111 CYS C SG  1 
ATOM 546  N N   . ILE A 1 120 ? 117.963 97.127  110.930 1.00 47.41  ?  112 ILE C N   1 
ATOM 547  C CA  . ILE A 1 120 ? 119.120 97.559  111.707 1.00 46.51  ?  112 ILE C CA  1 
ATOM 548  C C   . ILE A 1 120 ? 119.749 98.762  111.019 1.00 49.01  ?  112 ILE C C   1 
ATOM 549  O O   . ILE A 1 120 ? 119.890 98.780  109.792 1.00 54.47  ?  112 ILE C O   1 
ATOM 550  C CB  . ILE A 1 120 ? 120.148 96.426  111.870 1.00 49.70  ?  112 ILE C CB  1 
ATOM 551  C CG1 . ILE A 1 120 ? 119.440 95.084  112.076 1.00 54.70  ?  112 ILE C CG1 1 
ATOM 552  C CG2 . ILE A 1 120 ? 121.089 96.721  113.029 1.00 50.02  ?  112 ILE C CG2 1 
ATOM 553  C CD1 . ILE A 1 120 ? 120.370 93.894  112.084 1.00 54.77  ?  112 ILE C CD1 1 
ATOM 554  N N   . ILE A 1 121 ? 120.123 99.763  111.812 1.00 47.94  ?  113 ILE C N   1 
ATOM 555  C CA  . ILE A 1 121 ? 120.836 100.940 111.330 1.00 45.58  ?  113 ILE C CA  1 
ATOM 556  C C   . ILE A 1 121 ? 122.222 100.925 111.955 1.00 45.63  ?  113 ILE C C   1 
ATOM 557  O O   . ILE A 1 121 ? 122.356 100.972 113.185 1.00 47.62  ?  113 ILE C O   1 
ATOM 558  C CB  . ILE A 1 121 ? 120.093 102.241 111.670 1.00 42.73  ?  113 ILE C CB  1 
ATOM 559  C CG1 . ILE A 1 121 ? 118.806 102.351 110.849 1.00 41.00  ?  113 ILE C CG1 1 
ATOM 560  C CG2 . ILE A 1 121 ? 120.989 103.447 111.426 1.00 41.28  ?  113 ILE C CG2 1 
ATOM 561  C CD1 . ILE A 1 121 ? 118.092 103.676 111.003 1.00 34.55  ?  113 ILE C CD1 1 
ATOM 562  N N   . GLY A 1 122 ? 123.247 100.861 111.118 1.00 44.91  ?  114 GLY C N   1 
ATOM 563  C CA  . GLY A 1 122 ? 124.618 100.760 111.568 1.00 48.20  ?  114 GLY C CA  1 
ATOM 564  C C   . GLY A 1 122 ? 125.197 99.376  111.319 1.00 55.05  ?  114 GLY C C   1 
ATOM 565  O O   . GLY A 1 122 ? 124.577 98.503  110.711 1.00 60.26  ?  114 GLY C O   1 
ATOM 566  N N   . ARG A 1 123 ? 126.422 99.195  111.807 1.00 56.45  ?  115 ARG C N   1 
ATOM 567  C CA  . ARG A 1 123 ? 127.096 97.913  111.656 1.00 60.05  ?  115 ARG C CA  1 
ATOM 568  C C   . ARG A 1 123 ? 126.377 96.831  112.452 1.00 63.05  ?  115 ARG C C   1 
ATOM 569  O O   . ARG A 1 123 ? 125.832 97.087  113.529 1.00 67.17  ?  115 ARG C O   1 
ATOM 570  C CB  . ARG A 1 123 ? 128.558 98.022  112.095 1.00 60.37  ?  115 ARG C CB  1 
ATOM 571  C CG  . ARG A 1 123 ? 128.760 98.316  113.571 1.00 62.22  ?  115 ARG C CG  1 
ATOM 572  C CD  . ARG A 1 123 ? 130.237 98.304  113.934 1.00 63.70  ?  115 ARG C CD  1 
ATOM 573  N NE  . ARG A 1 123 ? 130.856 99.613  113.755 1.00 68.41  ?  115 ARG C NE  1 
ATOM 574  C CZ  . ARG A 1 123 ? 131.551 100.245 114.689 1.00 69.03  ?  115 ARG C CZ  1 
ATOM 575  N NH1 . ARG A 1 123 ? 131.742 99.717  115.887 1.00 66.49  1  115 ARG C NH1 1 
ATOM 576  N NH2 . ARG A 1 123 ? 132.071 101.438 114.414 1.00 71.22  ?  115 ARG C NH2 1 
ATOM 577  N N   . THR A 1 124 ? 126.363 95.618  111.907 1.00 62.52  ?  116 THR C N   1 
ATOM 578  C CA  . THR A 1 124 ? 125.690 94.491  112.541 1.00 62.73  ?  116 THR C CA  1 
ATOM 579  C C   . THR A 1 124 ? 126.244 93.197  111.959 1.00 64.55  ?  116 THR C C   1 
ATOM 580  O O   . THR A 1 124 ? 127.074 93.205  111.046 1.00 68.81  ?  116 THR C O   1 
ATOM 581  C CB  . THR A 1 124 ? 124.171 94.574  112.365 1.00 62.54  ?  116 THR C CB  1 
ATOM 582  O OG1 . THR A 1 124 ? 123.552 93.460  113.020 1.00 67.18  ?  116 THR C OG1 1 
ATOM 583  C CG2 . THR A 1 124 ? 123.796 94.573  110.899 1.00 62.11  ?  116 THR C CG2 1 
ATOM 584  N N   . LEU A 1 125 ? 125.771 92.078  112.502 1.00 66.11  ?  117 LEU C N   1 
ATOM 585  C CA  . LEU A 1 125 ? 126.203 90.756  112.057 1.00 69.44  ?  117 LEU C CA  1 
ATOM 586  C C   . LEU A 1 125 ? 125.073 89.782  112.354 1.00 74.04  ?  117 LEU C C   1 
ATOM 587  O O   . LEU A 1 125 ? 124.749 89.551  113.524 1.00 78.90  ?  117 LEU C O   1 
ATOM 588  C CB  . LEU A 1 125 ? 127.494 90.340  112.755 1.00 69.18  ?  117 LEU C CB  1 
ATOM 589  C CG  . LEU A 1 125 ? 128.506 89.525  111.945 1.00 67.69  ?  117 LEU C CG  1 
ATOM 590  C CD1 . LEU A 1 125 ? 129.843 89.474  112.668 1.00 64.04  ?  117 LEU C CD1 1 
ATOM 591  C CD2 . LEU A 1 125 ? 127.990 88.120  111.672 1.00 69.31  ?  117 LEU C CD2 1 
ATOM 592  N N   . VAL A 1 126 ? 124.478 89.217  111.306 1.00 75.25  ?  118 VAL C N   1 
ATOM 593  C CA  . VAL A 1 126 ? 123.351 88.301  111.429 1.00 77.60  ?  118 VAL C CA  1 
ATOM 594  C C   . VAL A 1 126 ? 123.779 86.939  110.904 1.00 78.22  ?  118 VAL C C   1 
ATOM 595  O O   . VAL A 1 126 ? 124.274 86.829  109.777 1.00 79.51  ?  118 VAL C O   1 
ATOM 596  C CB  . VAL A 1 126 ? 122.115 88.816  110.668 1.00 78.76  ?  118 VAL C CB  1 
ATOM 597  C CG1 . VAL A 1 126 ? 120.944 87.860  110.847 1.00 78.09  ?  118 VAL C CG1 1 
ATOM 598  C CG2 . VAL A 1 126 ? 121.748 90.216  111.136 1.00 73.56  ?  118 VAL C CG2 1 
ATOM 599  N N   . VAL A 1 127 ? 123.589 85.907  111.723 1.00 78.07  ?  119 VAL C N   1 
ATOM 600  C CA  . VAL A 1 127 ? 123.937 84.535  111.366 1.00 80.37  ?  119 VAL C CA  1 
ATOM 601  C C   . VAL A 1 127 ? 122.705 83.664  111.562 1.00 83.95  ?  119 VAL C C   1 
ATOM 602  O O   . VAL A 1 127 ? 122.104 83.664  112.642 1.00 85.60  ?  119 VAL C O   1 
ATOM 603  C CB  . VAL A 1 127 ? 125.115 84.007  112.207 1.00 79.15  ?  119 VAL C CB  1 
ATOM 604  C CG1 . VAL A 1 127 ? 125.263 82.504  112.033 1.00 78.97  ?  119 VAL C CG1 1 
ATOM 605  C CG2 . VAL A 1 127 ? 126.401 84.722  111.825 1.00 78.38  ?  119 VAL C CG2 1 
ATOM 606  N N   . HIS A 1 128 ? 122.333 82.922  110.522 1.00 86.95  ?  120 HIS C N   1 
ATOM 607  C CA  . HIS A 1 128 ? 121.190 82.019  110.566 1.00 88.45  ?  120 HIS C CA  1 
ATOM 608  C C   . HIS A 1 128 ? 121.695 80.585  110.660 1.00 90.30  ?  120 HIS C C   1 
ATOM 609  O O   . HIS A 1 128 ? 122.491 80.149  109.821 1.00 89.93  ?  120 HIS C O   1 
ATOM 610  C CB  . HIS A 1 128 ? 120.304 82.201  109.334 1.00 87.72  ?  120 HIS C CB  1 
ATOM 611  C CG  . HIS A 1 128 ? 119.283 83.285  109.478 1.00 88.59  ?  120 HIS C CG  1 
ATOM 612  N ND1 . HIS A 1 128 ? 119.178 84.332  108.587 1.00 88.11  ?  120 HIS C ND1 1 
ATOM 613  C CD2 . HIS A 1 128 ? 118.320 83.487  110.409 1.00 87.73  ?  120 HIS C CD2 1 
ATOM 614  C CE1 . HIS A 1 128 ? 118.195 85.131  108.962 1.00 83.30  ?  120 HIS C CE1 1 
ATOM 615  N NE2 . HIS A 1 128 ? 117.657 84.641  110.065 1.00 82.92  ?  120 HIS C NE2 1 
ATOM 616  N N   . GLU A 1 129 ? 121.228 79.862  111.676 1.00 92.63  ?  121 GLU C N   1 
ATOM 617  C CA  . GLU A 1 129 ? 121.621 78.473  111.912 1.00 95.14  ?  121 GLU C CA  1 
ATOM 618  C C   . GLU A 1 129 ? 123.136 78.316  112.001 1.00 91.48  ?  121 GLU C C   1 
ATOM 619  O O   . GLU A 1 129 ? 123.830 79.185  112.530 1.00 89.98  ?  121 GLU C O   1 
ATOM 620  C CB  . GLU A 1 129 ? 121.062 77.562  110.815 1.00 95.66  ?  121 GLU C CB  1 
ATOM 621  C CG  . GLU A 1 129 ? 119.578 77.750  110.546 1.00 98.85  ?  121 GLU C CG  1 
ATOM 622  C CD  . GLU A 1 129 ? 118.865 76.439  110.278 1.00 103.82 ?  121 GLU C CD  1 
ATOM 623  O OE1 . GLU A 1 129 ? 119.395 75.380  110.677 1.00 99.75  ?  121 GLU C OE1 1 
ATOM 624  O OE2 . GLU A 1 129 ? 117.776 76.468  109.668 1.00 106.63 -1 121 GLU C OE2 1 
ATOM 625  N N   . ALA B 1 9   ? 93.125  144.723 101.326 1.00 55.72  ?  1   ALA B N   1 
ATOM 626  C CA  . ALA B 1 9   ? 94.077  143.897 100.594 1.00 56.34  ?  1   ALA B CA  1 
ATOM 627  C C   . ALA B 1 9   ? 93.865  142.418 100.897 1.00 54.10  ?  1   ALA B C   1 
ATOM 628  O O   . ALA B 1 9   ? 94.515  141.560 100.301 1.00 51.98  ?  1   ALA B O   1 
ATOM 629  C CB  . ALA B 1 9   ? 95.504  144.309 100.930 1.00 53.70  ?  1   ALA B CB  1 
ATOM 630  N N   . THR B 1 10  ? 92.943  142.138 101.822 1.00 55.69  ?  2   THR B N   1 
ATOM 631  C CA  . THR B 1 10  ? 92.612  140.785 102.263 1.00 57.85  ?  2   THR B CA  1 
ATOM 632  C C   . THR B 1 10  ? 93.891  140.029 102.623 1.00 60.11  ?  2   THR B C   1 
ATOM 633  O O   . THR B 1 10  ? 94.429  140.213 103.718 1.00 62.57  ?  2   THR B O   1 
ATOM 634  C CB  . THR B 1 10  ? 91.789  140.051 101.198 1.00 57.79  ?  2   THR B CB  1 
ATOM 635  O OG1 . THR B 1 10  ? 90.563  140.758 100.985 1.00 57.08  ?  2   THR B OG1 1 
ATOM 636  C CG2 . THR B 1 10  ? 91.413  138.646 101.674 1.00 57.16  ?  2   THR B CG2 1 
ATOM 637  N N   . LYS B 1 11  ? 94.384  139.173 101.730 1.00 56.21  ?  3   LYS B N   1 
ATOM 638  C CA  . LYS B 1 11  ? 95.626  138.441 101.948 1.00 50.38  ?  3   LYS B CA  1 
ATOM 639  C C   . LYS B 1 11  ? 96.696  139.012 101.028 1.00 45.18  ?  3   LYS B C   1 
ATOM 640  O O   . LYS B 1 11  ? 96.548  138.976 99.802  1.00 48.01  ?  3   LYS B O   1 
ATOM 641  C CB  . LYS B 1 11  ? 95.432  136.947 101.697 1.00 51.67  ?  3   LYS B CB  1 
ATOM 642  C CG  . LYS B 1 11  ? 96.393  136.057 102.470 1.00 52.43  ?  3   LYS B CG  1 
ATOM 643  C CD  . LYS B 1 11  ? 96.336  134.622 101.973 1.00 53.78  ?  3   LYS B CD  1 
ATOM 644  C CE  . LYS B 1 11  ? 97.454  133.783 102.574 1.00 58.89  ?  3   LYS B CE  1 
ATOM 645  N NZ  . LYS B 1 11  ? 98.779  134.452 102.454 1.00 61.87  1  3   LYS B NZ  1 
ATOM 646  N N   . ALA B 1 12  ? 97.774  139.532 101.611 1.00 41.44  ?  4   ALA B N   1 
ATOM 647  C CA  . ALA B 1 12  ? 98.783  140.221 100.812 1.00 36.97  ?  4   ALA B CA  1 
ATOM 648  C C   . ALA B 1 12  ? 100.126 140.157 101.528 1.00 31.73  ?  4   ALA B C   1 
ATOM 649  O O   . ALA B 1 12  ? 100.316 140.827 102.546 1.00 34.38  ?  4   ALA B O   1 
ATOM 650  C CB  . ALA B 1 12  ? 98.365  141.662 100.553 1.00 41.09  ?  4   ALA B CB  1 
ATOM 651  N N   . VAL B 1 13  ? 101.047 139.369 100.987 1.00 28.38  ?  5   VAL B N   1 
ATOM 652  C CA  . VAL B 1 13  ? 102.413 139.288 101.493 1.00 28.15  ?  5   VAL B CA  1 
ATOM 653  C C   . VAL B 1 13  ? 103.314 140.186 100.653 1.00 26.99  ?  5   VAL B C   1 
ATOM 654  O O   . VAL B 1 13  ? 103.172 140.251 99.425  1.00 27.51  ?  5   VAL B O   1 
ATOM 655  C CB  . VAL B 1 13  ? 102.908 137.830 101.501 1.00 30.26  ?  5   VAL B CB  1 
ATOM 656  C CG1 . VAL B 1 13  ? 102.585 137.154 100.207 1.00 31.24  ?  5   VAL B CG1 1 
ATOM 657  C CG2 . VAL B 1 13  ? 104.415 137.768 101.746 1.00 24.72  ?  5   VAL B CG2 1 
ATOM 658  N N   . CYS B 1 14  ? 104.231 140.889 101.322 1.00 26.06  ?  6   CYS B N   1 
ATOM 659  C CA  . CYS B 1 14  ? 105.167 141.828 100.701 1.00 23.51  ?  6   CYS B CA  1 
ATOM 660  C C   . CYS B 1 14  ? 104.420 142.975 100.013 1.00 24.07  ?  6   CYS B C   1 
ATOM 661  O O   . CYS B 1 14  ? 104.466 143.160 98.796  1.00 27.95  ?  6   CYS B O   1 
ATOM 662  C CB  . CYS B 1 14  ? 106.104 141.111 99.722  1.00 24.39  ?  6   CYS B CB  1 
ATOM 663  S SG  . CYS B 1 14  ? 107.708 141.917 99.514  1.00 26.80  ?  6   CYS B SG  1 
ATOM 664  N N   . VAL B 1 15  ? 103.724 143.744 100.844 1.00 22.94  ?  7   VAL B N   1 
ATOM 665  C CA  . VAL B 1 15  ? 103.056 144.971 100.424 1.00 24.99  ?  7   VAL B CA  1 
ATOM 666  C C   . VAL B 1 15  ? 103.848 146.146 100.981 1.00 26.21  ?  7   VAL B C   1 
ATOM 667  O O   . VAL B 1 15  ? 104.108 146.210 102.188 1.00 30.94  ?  7   VAL B O   1 
ATOM 668  C CB  . VAL B 1 15  ? 101.595 145.005 100.896 1.00 25.56  ?  7   VAL B CB  1 
ATOM 669  C CG1 . VAL B 1 15  ? 101.104 146.435 101.021 1.00 24.48  ?  7   VAL B CG1 1 
ATOM 670  C CG2 . VAL B 1 15  ? 100.721 144.233 99.930  1.00 25.36  ?  7   VAL B CG2 1 
ATOM 671  N N   . LEU B 1 16  ? 104.251 147.072 100.112 1.00 24.46  ?  8   LEU B N   1 
ATOM 672  C CA  . LEU B 1 16  ? 105.086 148.175 100.560 1.00 28.74  ?  8   LEU B CA  1 
ATOM 673  C C   . LEU B 1 16  ? 104.958 149.358 99.611  1.00 31.40  ?  8   LEU B C   1 
ATOM 674  O O   . LEU B 1 16  ? 104.522 149.220 98.465  1.00 38.14  ?  8   LEU B O   1 
ATOM 675  C CB  . LEU B 1 16  ? 106.555 147.747 100.683 1.00 28.94  ?  8   LEU B CB  1 
ATOM 676  C CG  . LEU B 1 16  ? 107.261 147.335 99.389  1.00 26.95  ?  8   LEU B CG  1 
ATOM 677  C CD1 . LEU B 1 16  ? 108.232 148.414 98.933  1.00 26.80  ?  8   LEU B CD1 1 
ATOM 678  C CD2 . LEU B 1 16  ? 107.972 146.004 99.569  1.00 25.59  ?  8   LEU B CD2 1 
ATOM 679  N N   . LYS B 1 17  ? 105.340 150.530 100.114 1.00 30.63  ?  9   LYS B N   1 
ATOM 680  C CA  . LYS B 1 17  ? 105.446 151.746 99.320  1.00 33.89  ?  9   LYS B CA  1 
ATOM 681  C C   . LYS B 1 17  ? 106.738 152.463 99.680  1.00 35.38  ?  9   LYS B C   1 
ATOM 682  O O   . LYS B 1 17  ? 107.122 152.515 100.851 1.00 37.54  ?  9   LYS B O   1 
ATOM 683  C CB  . LYS B 1 17  ? 104.259 152.694 99.540  1.00 31.42  ?  9   LYS B CB  1 
ATOM 684  C CG  . LYS B 1 17  ? 102.912 152.177 99.061  1.00 29.83  ?  9   LYS B CG  1 
ATOM 685  C CD  . LYS B 1 17  ? 102.146 151.472 100.167 1.00 30.45  ?  9   LYS B CD  1 
ATOM 686  C CE  . LYS B 1 17  ? 100.954 150.714 99.606  1.00 30.67  ?  9   LYS B CE  1 
ATOM 687  N NZ  . LYS B 1 17  ? 100.558 149.579 100.477 1.00 32.46  1  9   LYS B NZ  1 
ATOM 688  N N   . GLY B 1 18  ? 107.406 153.012 98.669  1.00 35.35  ?  10  GLY B N   1 
ATOM 689  C CA  . GLY B 1 18  ? 108.618 153.770 98.901  1.00 41.06  ?  10  GLY B CA  1 
ATOM 690  C C   . GLY B 1 18  ? 109.831 153.213 98.187  1.00 47.17  ?  10  GLY B C   1 
ATOM 691  O O   . GLY B 1 18  ? 109.756 152.849 97.009  1.00 48.28  ?  10  GLY B O   1 
ATOM 692  N N   . ASP B 1 19  ? 110.957 153.141 98.891  1.00 48.64  ?  11  ASP B N   1 
ATOM 693  C CA  . ASP B 1 19  ? 112.203 152.650 98.320  1.00 48.52  ?  11  ASP B CA  1 
ATOM 694  C C   . ASP B 1 19  ? 112.809 151.639 99.289  1.00 46.49  ?  11  ASP B C   1 
ATOM 695  O O   . ASP B 1 19  ? 112.188 151.248 100.282 1.00 49.98  ?  11  ASP B O   1 
ATOM 696  C CB  . ASP B 1 19  ? 113.154 153.816 98.016  1.00 48.64  ?  11  ASP B CB  1 
ATOM 697  C CG  . ASP B 1 19  ? 113.821 154.366 99.258  1.00 50.33  ?  11  ASP B CG  1 
ATOM 698  O OD1 . ASP B 1 19  ? 114.881 153.835 99.650  1.00 54.07  ?  11  ASP B OD1 1 
ATOM 699  O OD2 . ASP B 1 19  ? 113.288 155.335 99.840  1.00 46.67  -1 11  ASP B OD2 1 
ATOM 700  N N   . GLY B 1 20  ? 114.035 151.213 98.995  1.00 40.40  ?  12  GLY B N   1 
ATOM 701  C CA  . GLY B 1 20  ? 114.713 150.227 99.797  1.00 35.56  ?  12  GLY B CA  1 
ATOM 702  C C   . GLY B 1 20  ? 114.630 148.847 99.178  1.00 35.56  ?  12  GLY B C   1 
ATOM 703  O O   . GLY B 1 20  ? 113.554 148.379 98.791  1.00 36.41  ?  12  GLY B O   1 
ATOM 704  N N   . PRO B 1 21  ? 115.772 148.170 99.065  1.00 33.92  ?  13  PRO B N   1 
ATOM 705  C CA  . PRO B 1 21  ? 115.775 146.840 98.445  1.00 30.41  ?  13  PRO B CA  1 
ATOM 706  C C   . PRO B 1 21  ? 115.037 145.820 99.299  1.00 28.35  ?  13  PRO B C   1 
ATOM 707  O O   . PRO B 1 21  ? 115.145 145.815 100.527 1.00 30.32  ?  13  PRO B O   1 
ATOM 708  C CB  . PRO B 1 21  ? 117.267 146.505 98.332  1.00 28.15  ?  13  PRO B CB  1 
ATOM 709  C CG  . PRO B 1 21  ? 117.911 147.308 99.410  1.00 27.72  ?  13  PRO B CG  1 
ATOM 710  C CD  . PRO B 1 21  ? 117.113 148.578 99.515  1.00 30.27  ?  13  PRO B CD  1 
ATOM 711  N N   . VAL B 1 22  ? 114.281 144.954 98.631  1.00 26.60  ?  14  VAL B N   1 
ATOM 712  C CA  . VAL B 1 22  ? 113.545 143.874 99.277  1.00 24.81  ?  14  VAL B CA  1 
ATOM 713  C C   . VAL B 1 22  ? 114.047 142.561 98.693  1.00 24.76  ?  14  VAL B C   1 
ATOM 714  O O   . VAL B 1 22  ? 114.015 142.367 97.471  1.00 27.69  ?  14  VAL B O   1 
ATOM 715  C CB  . VAL B 1 22  ? 112.028 144.016 99.084  1.00 24.47  ?  14  VAL B CB  1 
ATOM 716  C CG1 . VAL B 1 22  ? 111.289 142.982 99.919  1.00 27.39  ?  14  VAL B CG1 1 
ATOM 717  C CG2 . VAL B 1 22  ? 111.580 145.424 99.448  1.00 23.89  ?  14  VAL B CG2 1 
ATOM 718  N N   . GLN B 1 23  ? 114.509 141.664 99.560  1.00 21.92  ?  15  GLN B N   1 
ATOM 719  C CA  . GLN B 1 23  ? 115.118 140.414 99.126  1.00 22.66  ?  15  GLN B CA  1 
ATOM 720  C C   . GLN B 1 23  ? 114.594 139.269 99.977  1.00 22.28  ?  15  GLN B C   1 
ATOM 721  O O   . GLN B 1 23  ? 114.387 139.434 101.182 1.00 22.91  ?  15  GLN B O   1 
ATOM 722  C CB  . GLN B 1 23  ? 116.647 140.488 99.222  1.00 24.25  ?  15  GLN B CB  1 
ATOM 723  C CG  . GLN B 1 23  ? 117.155 141.340 100.373 1.00 22.14  ?  15  GLN B CG  1 
ATOM 724  C CD  . GLN B 1 23  ? 118.491 141.990 100.073 1.00 17.91  ?  15  GLN B CD  1 
ATOM 725  O OE1 . GLN B 1 23  ? 118.909 142.079 98.919  1.00 16.55  ?  15  GLN B OE1 1 
ATOM 726  N NE2 . GLN B 1 23  ? 119.170 142.450 101.117 1.00 17.47  ?  15  GLN B NE2 1 
ATOM 727  N N   . GLY B 1 24  ? 114.377 138.116 99.347  1.00 21.29  ?  16  GLY B N   1 
ATOM 728  C CA  . GLY B 1 24  ? 113.968 136.928 100.069 1.00 22.93  ?  16  GLY B CA  1 
ATOM 729  C C   . GLY B 1 24  ? 112.513 136.926 100.487 1.00 24.98  ?  16  GLY B C   1 
ATOM 730  O O   . GLY B 1 24  ? 112.205 136.937 101.682 1.00 29.08  ?  16  GLY B O   1 
ATOM 731  N N   . ILE B 1 25  ? 111.608 136.913 99.514  1.00 22.38  ?  17  ILE B N   1 
ATOM 732  C CA  . ILE B 1 25  ? 110.173 136.853 99.765  1.00 23.61  ?  17  ILE B CA  1 
ATOM 733  C C   . ILE B 1 25  ? 109.695 135.460 99.384  1.00 25.42  ?  17  ILE B C   1 
ATOM 734  O O   . ILE B 1 25  ? 109.772 135.068 98.214  1.00 27.17  ?  17  ILE B O   1 
ATOM 735  C CB  . ILE B 1 25  ? 109.412 137.932 98.981  1.00 24.33  ?  17  ILE B CB  1 
ATOM 736  C CG1 . ILE B 1 25  ? 110.140 139.270 99.084  1.00 22.88  ?  17  ILE B CG1 1 
ATOM 737  C CG2 . ILE B 1 25  ? 107.986 138.043 99.489  1.00 21.54  ?  17  ILE B CG2 1 
ATOM 738  C CD1 . ILE B 1 25  ? 110.735 139.739 97.779  1.00 26.06  ?  17  ILE B CD1 1 
ATOM 739  N N   . ILE B 1 26  ? 109.268 134.701 100.399 1.00 24.51  ?  18  ILE B N   1 
ATOM 740  C CA  . ILE B 1 26  ? 108.872 133.285 100.141 1.00 24.36  ?  18  ILE B CA  1 
ATOM 741  C C   . ILE B 1 26  ? 107.475 133.004 100.711 1.00 24.62  ?  18  ILE B C   1 
ATOM 742  O O   . ILE B 1 26  ? 107.249 133.300 101.904 1.00 27.94  ?  18  ILE B O   1 
ATOM 743  C CB  . ILE B 1 26  ? 109.931 132.307 100.684 1.00 24.43  ?  18  ILE B CB  1 
ATOM 744  C CG1 . ILE B 1 26  ? 111.268 132.486 99.970  1.00 22.03  ?  18  ILE B CG1 1 
ATOM 745  C CG2 . ILE B 1 26  ? 109.439 130.864 100.596 1.00 25.26  ?  18  ILE B CG2 1 
ATOM 746  C CD1 . ILE B 1 26  ? 112.218 131.315 100.132 1.00 22.02  ?  18  ILE B CD1 1 
ATOM 747  N N   . ASN B 1 27  ? 106.587 132.461 99.883  1.00 24.34  ?  19  ASN B N   1 
ATOM 748  C CA  . ASN B 1 27  ? 105.225 132.101 100.264 1.00 28.83  ?  19  ASN B CA  1 
ATOM 749  C C   . ASN B 1 27  ? 105.048 130.604 100.046 1.00 32.93  ?  19  ASN B C   1 
ATOM 750  O O   . ASN B 1 27  ? 105.148 130.123 98.913  1.00 33.84  ?  19  ASN B O   1 
ATOM 751  C CB  . ASN B 1 27  ? 104.202 132.900 99.457  1.00 29.86  ?  19  ASN B CB  1 
ATOM 752  C CG  . ASN B 1 27  ? 102.777 132.464 99.729  1.00 29.12  ?  19  ASN B CG  1 
ATOM 753  O OD1 . ASN B 1 27  ? 102.320 132.467 100.872 1.00 29.88  ?  19  ASN B OD1 1 
ATOM 754  N ND2 . ASN B 1 27  ? 102.067 132.080 98.674  1.00 26.34  ?  19  ASN B ND2 1 
ATOM 755  N N   . PHE B 1 28  ? 104.787 129.870 101.127 1.00 34.71  ?  20  PHE B N   1 
ATOM 756  C CA  . PHE B 1 28  ? 104.575 128.428 101.073 1.00 38.96  ?  20  PHE B CA  1 
ATOM 757  C C   . PHE B 1 28  ? 103.153 128.105 101.516 1.00 43.50  ?  20  PHE B C   1 
ATOM 758  O O   . PHE B 1 28  ? 102.736 128.497 102.612 1.00 47.56  ?  20  PHE B O   1 
ATOM 759  C CB  . PHE B 1 28  ? 105.581 127.687 101.953 1.00 44.73  ?  20  PHE B CB  1 
ATOM 760  C CG  . PHE B 1 28  ? 106.782 127.176 101.208 1.00 43.10  ?  20  PHE B CG  1 
ATOM 761  C CD1 . PHE B 1 28  ? 106.675 126.090 100.358 1.00 43.98  ?  20  PHE B CD1 1 
ATOM 762  C CD2 . PHE B 1 28  ? 108.021 127.768 101.378 1.00 38.33  ?  20  PHE B CD2 1 
ATOM 763  C CE1 . PHE B 1 28  ? 107.780 125.614 99.675  1.00 47.10  ?  20  PHE B CE1 1 
ATOM 764  C CE2 . PHE B 1 28  ? 109.129 127.297 100.702 1.00 38.50  ?  20  PHE B CE2 1 
ATOM 765  C CZ  . PHE B 1 28  ? 109.009 126.221 99.847  1.00 43.62  ?  20  PHE B CZ  1 
ATOM 766  N N   . GLU B 1 29  ? 102.421 127.382 100.671 1.00 44.08  ?  21  GLU B N   1 
ATOM 767  C CA  . GLU B 1 29  ? 101.066 126.932 100.981 1.00 49.54  ?  21  GLU B CA  1 
ATOM 768  C C   . GLU B 1 29  ? 100.945 125.475 100.553 1.00 48.82  ?  21  GLU B C   1 
ATOM 769  O O   . GLU B 1 29  ? 100.848 125.182 99.357  1.00 47.51  ?  21  GLU B O   1 
ATOM 770  C CB  . GLU B 1 29  ? 100.021 127.802 100.281 1.00 53.29  ?  21  GLU B CB  1 
ATOM 771  C CG  . GLU B 1 29  ? 98.599  127.275 100.384 1.00 60.45  ?  21  GLU B CG  1 
ATOM 772  C CD  . GLU B 1 29  ? 97.585  128.217 99.769  1.00 65.14  ?  21  GLU B CD  1 
ATOM 773  O OE1 . GLU B 1 29  ? 97.962  129.363 99.440  1.00 64.22  ?  21  GLU B OE1 1 
ATOM 774  O OE2 . GLU B 1 29  ? 96.413  127.816 99.613  1.00 64.00  -1 21  GLU B OE2 1 
ATOM 775  N N   . GLN B 1 30  ? 100.945 124.565 101.524 1.00 48.04  ?  22  GLN B N   1 
ATOM 776  C CA  . GLN B 1 30  ? 100.929 123.134 101.261 1.00 50.83  ?  22  GLN B CA  1 
ATOM 777  C C   . GLN B 1 30  ? 99.677  122.500 101.851 1.00 54.87  ?  22  GLN B C   1 
ATOM 778  O O   . GLN B 1 30  ? 99.270  122.827 102.969 1.00 53.25  ?  22  GLN B O   1 
ATOM 779  C CB  . GLN B 1 30  ? 102.172 122.449 101.839 1.00 49.29  ?  22  GLN B CB  1 
ATOM 780  C CG  . GLN B 1 30  ? 103.425 122.607 100.996 1.00 48.84  ?  22  GLN B CG  1 
ATOM 781  C CD  . GLN B 1 30  ? 104.691 122.593 101.828 1.00 49.90  ?  22  GLN B CD  1 
ATOM 782  O OE1 . GLN B 1 30  ? 104.710 122.068 102.942 1.00 49.86  ?  22  GLN B OE1 1 
ATOM 783  N NE2 . GLN B 1 30  ? 105.759 123.169 101.292 1.00 48.78  ?  22  GLN B NE2 1 
ATOM 784  N N   . LYS B 1 31  ? 99.076  121.588 101.090 1.00 55.39  ?  23  LYS B N   1 
ATOM 785  C CA  . LYS B 1 31  ? 97.931  120.800 101.533 1.00 53.82  ?  23  LYS B CA  1 
ATOM 786  C C   . LYS B 1 31  ? 98.331  119.331 101.483 1.00 53.95  ?  23  LYS B C   1 
ATOM 787  O O   . LYS B 1 31  ? 98.440  118.752 100.395 1.00 54.78  ?  23  LYS B O   1 
ATOM 788  C CB  . LYS B 1 31  ? 96.706  121.069 100.658 1.00 53.83  ?  23  LYS B CB  1 
ATOM 789  C CG  . LYS B 1 31  ? 95.917  122.307 101.057 1.00 52.24  ?  23  LYS B CG  1 
ATOM 790  C CD  . LYS B 1 31  ? 94.481  122.243 100.553 1.00 55.54  ?  23  LYS B CD  1 
ATOM 791  C CE  . LYS B 1 31  ? 93.859  120.876 100.792 1.00 57.07  ?  23  LYS B CE  1 
ATOM 792  N NZ  . LYS B 1 31  ? 93.822  120.522 102.238 1.00 56.48  1  23  LYS B NZ  1 
ATOM 793  N N   . GLU B 1 32  ? 98.547  118.734 102.654 1.00 53.98  ?  24  GLU B N   1 
ATOM 794  C CA  . GLU B 1 32  ? 99.024  117.357 102.779 1.00 55.86  ?  24  GLU B CA  1 
ATOM 795  C C   . GLU B 1 32  ? 100.337 117.171 102.015 1.00 58.44  ?  24  GLU B C   1 
ATOM 796  O O   . GLU B 1 32  ? 100.441 116.397 101.063 1.00 62.27  ?  24  GLU B O   1 
ATOM 797  C CB  . GLU B 1 32  ? 97.959  116.364 102.302 1.00 56.67  ?  24  GLU B CB  1 
ATOM 798  C CG  . GLU B 1 32  ? 96.633  116.471 103.038 1.00 62.98  ?  24  GLU B CG  1 
ATOM 799  C CD  . GLU B 1 32  ? 95.490  116.864 102.122 1.00 65.14  ?  24  GLU B CD  1 
ATOM 800  O OE1 . GLU B 1 32  ? 95.530  117.980 101.563 1.00 63.46  ?  24  GLU B OE1 1 
ATOM 801  O OE2 . GLU B 1 32  ? 94.552  116.055 101.959 1.00 66.01  -1 24  GLU B OE2 1 
ATOM 802  N N   . SER B 1 33  ? 101.350 117.910 102.468 1.00 55.32  ?  25  SER B N   1 
ATOM 803  C CA  . SER B 1 33  ? 102.629 117.962 101.767 1.00 56.02  ?  25  SER B CA  1 
ATOM 804  C C   . SER B 1 33  ? 103.340 116.615 101.799 1.00 59.63  ?  25  SER B C   1 
ATOM 805  O O   . SER B 1 33  ? 103.555 116.003 100.748 1.00 61.97  ?  25  SER B O   1 
ATOM 806  C CB  . SER B 1 33  ? 103.528 119.043 102.372 1.00 57.72  ?  25  SER B CB  1 
ATOM 807  O OG  . SER B 1 33  ? 103.946 118.688 103.677 1.00 60.40  ?  25  SER B OG  1 
ATOM 808  N N   . ASN B 1 34  ? 103.694 116.144 102.995 1.00 59.77  ?  26  ASN B N   1 
ATOM 809  C CA  . ASN B 1 34  ? 104.395 114.872 103.182 1.00 58.66  ?  26  ASN B CA  1 
ATOM 810  C C   . ASN B 1 34  ? 105.682 114.825 102.354 1.00 59.61  ?  26  ASN B C   1 
ATOM 811  O O   . ASN B 1 34  ? 105.902 113.926 101.539 1.00 59.31  ?  26  ASN B O   1 
ATOM 812  C CB  . ASN B 1 34  ? 103.477 113.690 102.852 1.00 59.30  ?  26  ASN B CB  1 
ATOM 813  C CG  . ASN B 1 34  ? 102.641 113.252 104.037 1.00 64.47  ?  26  ASN B CG  1 
ATOM 814  O OD1 . ASN B 1 34  ? 101.485 113.653 104.178 1.00 69.26  ?  26  ASN B OD1 1 
ATOM 815  N ND2 . ASN B 1 34  ? 103.220 112.422 104.896 1.00 61.99  ?  26  ASN B ND2 1 
ATOM 816  N N   . GLY B 1 35  ? 106.538 115.817 102.583 1.00 58.45  ?  27  GLY B N   1 
ATOM 817  C CA  . GLY B 1 35  ? 107.789 115.917 101.870 1.00 54.06  ?  27  GLY B CA  1 
ATOM 818  C C   . GLY B 1 35  ? 108.742 116.916 102.496 1.00 56.87  ?  27  GLY B C   1 
ATOM 819  O O   . GLY B 1 35  ? 108.355 117.753 103.316 1.00 55.15  ?  27  GLY B O   1 
ATOM 820  N N   . PRO B 1 36  ? 110.017 116.841 102.116 1.00 60.77  ?  28  PRO B N   1 
ATOM 821  C CA  . PRO B 1 36  ? 111.017 117.756 102.679 1.00 57.27  ?  28  PRO B CA  1 
ATOM 822  C C   . PRO B 1 36  ? 111.165 119.043 101.883 1.00 52.53  ?  28  PRO B C   1 
ATOM 823  O O   . PRO B 1 36  ? 111.091 119.068 100.653 1.00 53.35  ?  28  PRO B O   1 
ATOM 824  C CB  . PRO B 1 36  ? 112.304 116.924 102.621 1.00 52.87  ?  28  PRO B CB  1 
ATOM 825  C CG  . PRO B 1 36  ? 112.114 116.022 101.442 1.00 47.86  ?  28  PRO B CG  1 
ATOM 826  C CD  . PRO B 1 36  ? 110.625 115.840 101.222 1.00 54.45  ?  28  PRO B CD  1 
ATOM 827  N N   . VAL B 1 37  ? 111.375 120.132 102.619 1.00 48.48  ?  29  VAL B N   1 
ATOM 828  C CA  . VAL B 1 37  ? 111.573 121.462 102.056 1.00 47.21  ?  29  VAL B CA  1 
ATOM 829  C C   . VAL B 1 37  ? 112.801 122.098 102.695 1.00 46.15  ?  29  VAL B C   1 
ATOM 830  O O   . VAL B 1 37  ? 112.973 122.049 103.918 1.00 49.39  ?  29  VAL B O   1 
ATOM 831  C CB  . VAL B 1 37  ? 110.322 122.348 102.225 1.00 46.90  ?  29  VAL B CB  1 
ATOM 832  C CG1 . VAL B 1 37  ? 109.892 122.401 103.647 1.00 44.83  ?  29  VAL B CG1 1 
ATOM 833  C CG2 . VAL B 1 37  ? 110.621 123.766 101.755 1.00 44.88  ?  29  VAL B CG2 1 
ATOM 834  N N   . LYS B 1 38  ? 113.658 122.684 101.860 1.00 44.07  ?  30  LYS B N   1 
ATOM 835  C CA  . LYS B 1 38  ? 114.932 123.241 102.295 1.00 41.23  ?  30  LYS B CA  1 
ATOM 836  C C   . LYS B 1 38  ? 115.110 124.622 101.684 1.00 38.56  ?  30  LYS B C   1 
ATOM 837  O O   . LYS B 1 38  ? 115.202 124.757 100.461 1.00 38.56  ?  30  LYS B O   1 
ATOM 838  C CB  . LYS B 1 38  ? 116.089 122.320 101.900 1.00 42.71  ?  30  LYS B CB  1 
ATOM 839  C CG  . LYS B 1 38  ? 117.468 122.917 102.109 1.00 40.00  ?  30  LYS B CG  1 
ATOM 840  C CD  . LYS B 1 38  ? 117.822 123.023 103.569 1.00 40.23  ?  30  LYS B CD  1 
ATOM 841  C CE  . LYS B 1 38  ? 119.313 123.252 103.775 1.00 40.83  ?  30  LYS B CE  1 
ATOM 842  N NZ  . LYS B 1 38  ? 120.136 122.130 103.243 1.00 39.78  1  30  LYS B NZ  1 
ATOM 843  N N   . VAL B 1 39  ? 115.150 125.639 102.540 1.00 38.13  ?  31  VAL B N   1 
ATOM 844  C CA  . VAL B 1 39  ? 115.464 127.010 102.151 1.00 40.08  ?  31  VAL B CA  1 
ATOM 845  C C   . VAL B 1 39  ? 116.775 127.424 102.810 1.00 40.96  ?  31  VAL B C   1 
ATOM 846  O O   . VAL B 1 39  ? 116.994 127.170 104.000 1.00 42.68  ?  31  VAL B O   1 
ATOM 847  C CB  . VAL B 1 39  ? 114.301 127.975 102.468 1.00 39.42  ?  31  VAL B CB  1 
ATOM 848  C CG1 . VAL B 1 39  ? 114.110 128.109 103.902 1.00 38.01  ?  31  VAL B CG1 1 
ATOM 849  C CG2 . VAL B 1 39  ? 114.621 129.372 101.935 1.00 36.32  ?  31  VAL B CG2 1 
ATOM 850  N N   . TRP B 1 40  ? 117.657 128.027 102.013 1.00 39.62  ?  32  TRP B N   1 
ATOM 851  C CA  . TRP B 1 40  ? 119.044 128.259 102.380 1.00 41.94  ?  32  TRP B CA  1 
ATOM 852  C C   . TRP B 1 40  ? 119.675 129.286 101.452 1.00 47.10  ?  32  TRP B C   1 
ATOM 853  O O   . TRP B 1 40  ? 119.238 129.474 100.315 1.00 52.87  ?  32  TRP B O   1 
ATOM 854  C CB  . TRP B 1 40  ? 119.810 126.926 102.411 1.00 43.21  ?  32  TRP B CB  1 
ATOM 855  C CG  . TRP B 1 40  ? 121.090 126.964 103.178 1.00 46.40  ?  32  TRP B CG  1 
ATOM 856  C CD1 . TRP B 1 40  ? 121.348 127.661 104.313 1.00 48.02  ?  32  TRP B CD1 1 
ATOM 857  C CD2 . TRP B 1 40  ? 122.244 126.147 102.943 1.00 44.13  ?  32  TRP B CD2 1 
ATOM 858  N NE1 . TRP B 1 40  ? 122.630 127.416 104.743 1.00 51.88  ?  32  TRP B NE1 1 
ATOM 859  C CE2 . TRP B 1 40  ? 123.193 126.471 103.927 1.00 46.70  ?  32  TRP B CE2 1 
ATOM 860  C CE3 . TRP B 1 40  ? 122.573 125.191 101.978 1.00 42.91  ?  32  TRP B CE3 1 
ATOM 861  C CZ2 . TRP B 1 40  ? 124.452 125.880 103.971 1.00 49.52  ?  32  TRP B CZ2 1 
ATOM 862  C CZ3 . TRP B 1 40  ? 123.821 124.606 102.021 1.00 43.59  ?  32  TRP B CZ3 1 
ATOM 863  C CH2 . TRP B 1 40  ? 124.746 124.951 103.012 1.00 48.13  ?  32  TRP B CH2 1 
ATOM 864  N N   . GLY B 1 41  ? 120.692 129.956 101.966 1.00 43.38  ?  33  GLY B N   1 
ATOM 865  C CA  . GLY B 1 41  ? 121.350 131.057 101.290 1.00 41.37  ?  33  GLY B CA  1 
ATOM 866  C C   . GLY B 1 41  ? 121.550 132.207 102.259 1.00 42.12  ?  33  GLY B C   1 
ATOM 867  O O   . GLY B 1 41  ? 120.813 132.379 103.230 1.00 41.68  ?  33  GLY B O   1 
ATOM 868  N N   . SER B 1 42  ? 122.565 133.021 101.981 1.00 41.19  ?  34  SER B N   1 
ATOM 869  C CA  . SER B 1 42  ? 122.942 134.127 102.849 1.00 37.65  ?  34  SER B CA  1 
ATOM 870  C C   . SER B 1 42  ? 122.617 135.464 102.194 1.00 34.43  ?  34  SER B C   1 
ATOM 871  O O   . SER B 1 42  ? 122.763 135.634 100.981 1.00 35.63  ?  34  SER B O   1 
ATOM 872  C CB  . SER B 1 42  ? 124.431 134.070 103.201 1.00 39.91  ?  34  SER B CB  1 
ATOM 873  O OG  . SER B 1 42  ? 124.701 133.002 104.092 1.00 45.22  ?  34  SER B OG  1 
ATOM 874  N N   . ILE B 1 43  ? 122.180 136.415 103.019 1.00 31.84  ?  35  ILE B N   1 
ATOM 875  C CA  . ILE B 1 43  ? 121.740 137.727 102.561 1.00 31.37  ?  35  ILE B CA  1 
ATOM 876  C C   . ILE B 1 43  ? 122.593 138.801 103.223 1.00 29.80  ?  35  ILE B C   1 
ATOM 877  O O   . ILE B 1 43  ? 122.903 138.714 104.416 1.00 30.62  ?  35  ILE B O   1 
ATOM 878  C CB  . ILE B 1 43  ? 120.246 137.970 102.867 1.00 29.17  ?  35  ILE B CB  1 
ATOM 879  C CG1 . ILE B 1 43  ? 119.426 136.708 102.594 1.00 29.56  ?  35  ILE B CG1 1 
ATOM 880  C CG2 . ILE B 1 43  ? 119.720 139.128 102.039 1.00 27.12  ?  35  ILE B CG2 1 
ATOM 881  C CD1 . ILE B 1 43  ? 117.947 136.884 102.849 1.00 28.44  ?  35  ILE B CD1 1 
ATOM 882  N N   . LYS B 1 44  ? 122.970 139.815 102.444 1.00 27.94  ?  36  LYS B N   1 
ATOM 883  C CA  . LYS B 1 44  ? 123.718 140.961 102.946 1.00 28.09  ?  36  LYS B CA  1 
ATOM 884  C C   . LYS B 1 44  ? 123.032 142.236 102.478 1.00 29.75  ?  36  LYS B C   1 
ATOM 885  O O   . LYS B 1 44  ? 122.765 142.395 101.281 1.00 30.05  ?  36  LYS B O   1 
ATOM 886  C CB  . LYS B 1 44  ? 125.174 140.925 102.470 1.00 31.37  ?  36  LYS B CB  1 
ATOM 887  C CG  . LYS B 1 44  ? 125.972 142.178 102.810 1.00 32.18  ?  36  LYS B CG  1 
ATOM 888  C CD  . LYS B 1 44  ? 126.338 142.974 101.566 1.00 31.06  ?  36  LYS B CD  1 
ATOM 889  C CE  . LYS B 1 44  ? 127.501 143.917 101.835 1.00 29.17  ?  36  LYS B CE  1 
ATOM 890  N NZ  . LYS B 1 44  ? 128.796 143.190 101.969 1.00 28.74  1  36  LYS B NZ  1 
ATOM 891  N N   . GLY B 1 45  ? 122.754 143.138 103.410 1.00 31.51  ?  37  GLY B N   1 
ATOM 892  C CA  . GLY B 1 45  ? 122.103 144.390 103.085 1.00 33.19  ?  37  GLY B CA  1 
ATOM 893  C C   . GLY B 1 45  ? 122.818 145.567 103.713 1.00 38.65  ?  37  GLY B C   1 
ATOM 894  O O   . GLY B 1 45  ? 123.395 145.467 104.796 1.00 43.33  ?  37  GLY B O   1 
ATOM 895  N N   . LEU B 1 46  ? 122.770 146.698 103.011 1.00 40.57  ?  38  LEU B N   1 
ATOM 896  C CA  . LEU B 1 46  ? 123.424 147.913 103.476 1.00 49.70  ?  38  LEU B CA  1 
ATOM 897  C C   . LEU B 1 46  ? 122.684 149.123 102.924 1.00 49.34  ?  38  LEU B C   1 
ATOM 898  O O   . LEU B 1 46  ? 122.255 149.123 101.766 1.00 49.78  ?  38  LEU B O   1 
ATOM 899  C CB  . LEU B 1 46  ? 124.905 147.933 103.062 1.00 50.64  ?  38  LEU B CB  1 
ATOM 900  C CG  . LEU B 1 46  ? 125.753 149.212 103.086 1.00 50.83  ?  38  LEU B CG  1 
ATOM 901  C CD1 . LEU B 1 46  ? 127.218 148.839 103.232 1.00 50.18  ?  38  LEU B CD1 1 
ATOM 902  C CD2 . LEU B 1 46  ? 125.574 150.061 101.832 1.00 53.75  ?  38  LEU B CD2 1 
ATOM 903  N N   . THR B 1 47  ? 122.539 150.149 103.761 1.00 51.59  ?  39  THR B N   1 
ATOM 904  C CA  . THR B 1 47  ? 121.964 151.425 103.357 1.00 60.01  ?  39  THR B CA  1 
ATOM 905  C C   . THR B 1 47  ? 122.857 152.551 103.855 1.00 68.73  ?  39  THR B C   1 
ATOM 906  O O   . THR B 1 47  ? 123.269 152.552 105.019 1.00 74.58  ?  39  THR B O   1 
ATOM 907  C CB  . THR B 1 47  ? 120.532 151.591 103.886 1.00 60.26  ?  39  THR B CB  1 
ATOM 908  O OG1 . THR B 1 47  ? 120.112 152.953 103.728 1.00 59.95  ?  39  THR B OG1 1 
ATOM 909  C CG2 . THR B 1 47  ? 120.435 151.185 105.342 1.00 63.57  ?  39  THR B CG2 1 
ATOM 910  N N   . GLU B 1 48  ? 123.163 153.498 102.970 1.00 69.61  ?  40  GLU B N   1 
ATOM 911  C CA  . GLU B 1 48  ? 124.058 154.602 103.287 1.00 73.72  ?  40  GLU B CA  1 
ATOM 912  C C   . GLU B 1 48  ? 123.456 155.893 102.750 1.00 81.48  ?  40  GLU B C   1 
ATOM 913  O O   . GLU B 1 48  ? 122.399 155.893 102.108 1.00 86.68  ?  40  GLU B O   1 
ATOM 914  C CB  . GLU B 1 48  ? 125.458 154.358 102.711 1.00 73.85  ?  40  GLU B CB  1 
ATOM 915  C CG  . GLU B 1 48  ? 126.593 154.743 103.646 1.00 79.73  ?  40  GLU B CG  1 
ATOM 916  C CD  . GLU B 1 48  ? 127.917 154.130 103.235 1.00 83.99  ?  40  GLU B CD  1 
ATOM 917  O OE1 . GLU B 1 48  ? 127.960 153.451 102.188 1.00 80.86  ?  40  GLU B OE1 1 
ATOM 918  O OE2 . GLU B 1 48  ? 128.916 154.327 103.959 1.00 88.46  -1 40  GLU B OE2 1 
ATOM 919  N N   . GLY B 1 49  ? 124.137 157.005 103.015 1.00 82.55  ?  41  GLY B N   1 
ATOM 920  C CA  . GLY B 1 49  ? 123.669 158.302 102.567 1.00 86.07  ?  41  GLY B CA  1 
ATOM 921  C C   . GLY B 1 49  ? 122.422 158.760 103.294 1.00 92.08  ?  41  GLY B C   1 
ATOM 922  O O   . GLY B 1 49  ? 122.480 159.116 104.475 1.00 94.69  ?  41  GLY B O   1 
ATOM 923  N N   . LEU B 1 50  ? 121.288 158.759 102.587 1.00 96.07  ?  42  LEU B N   1 
ATOM 924  C CA  . LEU B 1 50  ? 119.990 159.116 103.161 1.00 101.18 ?  42  LEU B CA  1 
ATOM 925  C C   . LEU B 1 50  ? 120.003 160.535 103.726 1.00 107.80 ?  42  LEU B C   1 
ATOM 926  O O   . LEU B 1 50  ? 119.399 160.816 104.764 1.00 110.50 ?  42  LEU B O   1 
ATOM 927  C CB  . LEU B 1 50  ? 119.567 158.106 104.230 1.00 98.30  ?  42  LEU B CB  1 
ATOM 928  C CG  . LEU B 1 50  ? 118.449 157.129 103.858 1.00 97.12  ?  42  LEU B CG  1 
ATOM 929  C CD1 . LEU B 1 50  ? 118.403 155.978 104.849 1.00 96.01  ?  42  LEU B CD1 1 
ATOM 930  C CD2 . LEU B 1 50  ? 117.106 157.836 103.788 1.00 103.05 ?  42  LEU B CD2 1 
ATOM 931  N N   . HIS B 1 51  ? 120.697 161.437 103.038 1.00 108.75 ?  43  HIS B N   1 
ATOM 932  C CA  . HIS B 1 51  ? 120.805 162.813 103.501 1.00 111.41 ?  43  HIS B CA  1 
ATOM 933  C C   . HIS B 1 51  ? 119.514 163.576 103.229 1.00 113.81 ?  43  HIS B C   1 
ATOM 934  O O   . HIS B 1 51  ? 118.903 163.440 102.166 1.00 112.58 ?  43  HIS B O   1 
ATOM 935  C CB  . HIS B 1 51  ? 121.981 163.510 102.816 1.00 112.44 ?  43  HIS B CB  1 
ATOM 936  C CG  . HIS B 1 51  ? 122.056 164.981 103.087 1.00 116.99 ?  43  HIS B CG  1 
ATOM 937  N ND1 . HIS B 1 51  ? 121.358 165.911 102.346 1.00 117.69 ?  43  HIS B ND1 1 
ATOM 938  C CD2 . HIS B 1 51  ? 122.750 165.683 104.012 1.00 118.15 ?  43  HIS B CD2 1 
ATOM 939  C CE1 . HIS B 1 51  ? 121.617 167.122 102.807 1.00 116.72 ?  43  HIS B CE1 1 
ATOM 940  N NE2 . HIS B 1 51  ? 122.459 167.011 103.818 1.00 118.74 ?  43  HIS B NE2 1 
ATOM 941  N N   . GLY B 1 52  ? 119.102 164.385 104.203 1.00 116.05 ?  44  GLY B N   1 
ATOM 942  C CA  . GLY B 1 52  ? 117.931 165.225 104.031 1.00 117.65 ?  44  GLY B CA  1 
ATOM 943  C C   . GLY B 1 52  ? 116.618 164.484 103.974 1.00 118.87 ?  44  GLY B C   1 
ATOM 944  O O   . GLY B 1 52  ? 115.648 165.003 103.416 1.00 118.82 ?  44  GLY B O   1 
ATOM 945  N N   . PHE B 1 53  ? 116.553 163.282 104.535 1.00 116.85 ?  45  PHE B N   1 
ATOM 946  C CA  . PHE B 1 53  ? 115.326 162.497 104.514 1.00 115.25 ?  45  PHE B CA  1 
ATOM 947  C C   . PHE B 1 53  ? 114.388 163.021 105.599 1.00 116.82 ?  45  PHE B C   1 
ATOM 948  O O   . PHE B 1 53  ? 113.370 163.646 105.305 1.00 113.10 ?  45  PHE B O   1 
ATOM 949  C CB  . PHE B 1 53  ? 115.635 161.009 104.720 1.00 112.45 ?  45  PHE B CB  1 
ATOM 950  C CG  . PHE B 1 53  ? 114.438 160.167 105.089 1.00 117.95 ?  45  PHE B CG  1 
ATOM 951  C CD1 . PHE B 1 53  ? 113.201 160.379 104.493 1.00 118.95 ?  45  PHE B CD1 1 
ATOM 952  C CD2 . PHE B 1 53  ? 114.554 159.159 106.032 1.00 117.85 ?  45  PHE B CD2 1 
ATOM 953  C CE1 . PHE B 1 53  ? 112.109 159.604 104.835 1.00 115.98 ?  45  PHE B CE1 1 
ATOM 954  C CE2 . PHE B 1 53  ? 113.464 158.381 106.376 1.00 117.16 ?  45  PHE B CE2 1 
ATOM 955  C CZ  . PHE B 1 53  ? 112.241 158.605 105.777 1.00 116.13 ?  45  PHE B CZ  1 
ATOM 956  N N   . VAL B 1 89  ? 136.214 154.317 106.211 1.00 104.10 ?  81  VAL B N   1 
ATOM 957  C CA  . VAL B 1 89  ? 135.247 153.686 107.099 1.00 103.42 ?  81  VAL B CA  1 
ATOM 958  C C   . VAL B 1 89  ? 134.874 152.302 106.578 1.00 102.49 ?  81  VAL B C   1 
ATOM 959  O O   . VAL B 1 89  ? 134.019 151.622 107.148 1.00 100.27 ?  81  VAL B O   1 
ATOM 960  C CB  . VAL B 1 89  ? 133.993 154.564 107.272 1.00 100.20 ?  81  VAL B CB  1 
ATOM 961  C CG1 . VAL B 1 89  ? 134.391 156.006 107.545 1.00 94.61  ?  81  VAL B CG1 1 
ATOM 962  C CG2 . VAL B 1 89  ? 133.106 154.477 106.041 1.00 99.35  ?  81  VAL B CG2 1 
ATOM 963  N N   . GLY B 1 90  ? 135.525 151.893 105.490 1.00 104.32 ?  82  GLY B N   1 
ATOM 964  C CA  . GLY B 1 90  ? 135.274 150.596 104.890 1.00 102.79 ?  82  GLY B CA  1 
ATOM 965  C C   . GLY B 1 90  ? 135.533 149.439 105.832 1.00 99.38  ?  82  GLY B C   1 
ATOM 966  O O   . GLY B 1 90  ? 136.574 149.387 106.494 1.00 98.08  ?  82  GLY B O   1 
ATOM 967  N N   . ASP B 1 91  ? 134.591 148.503 105.901 1.00 97.40  ?  83  ASP B N   1 
ATOM 968  C CA  . ASP B 1 91  ? 134.669 147.359 106.803 1.00 93.97  ?  83  ASP B CA  1 
ATOM 969  C C   . ASP B 1 91  ? 134.878 146.095 105.976 1.00 86.96  ?  83  ASP B C   1 
ATOM 970  O O   . ASP B 1 91  ? 134.011 145.714 105.183 1.00 87.12  ?  83  ASP B O   1 
ATOM 971  C CB  . ASP B 1 91  ? 133.408 147.256 107.659 1.00 98.51  ?  83  ASP B CB  1 
ATOM 972  C CG  . ASP B 1 91  ? 132.136 147.400 106.846 1.00 101.66 ?  83  ASP B CG  1 
ATOM 973  O OD1 . ASP B 1 91  ? 131.840 148.527 106.397 1.00 103.27 ?  83  ASP B OD1 1 
ATOM 974  O OD2 . ASP B 1 91  ? 131.433 146.386 106.655 1.00 99.30  -1 83  ASP B OD2 1 
ATOM 975  N N   . LEU B 1 92  ? 136.025 145.449 106.164 1.00 83.64  ?  84  LEU B N   1 
ATOM 976  C CA  . LEU B 1 92  ? 136.304 144.182 105.503 1.00 83.25  ?  84  LEU B CA  1 
ATOM 977  C C   . LEU B 1 92  ? 135.539 143.074 106.218 1.00 83.87  ?  84  LEU B C   1 
ATOM 978  O O   . LEU B 1 92  ? 135.729 142.857 107.419 1.00 86.74  ?  84  LEU B O   1 
ATOM 979  C CB  . LEU B 1 92  ? 137.804 143.899 105.500 1.00 82.44  ?  84  LEU B CB  1 
ATOM 980  C CG  . LEU B 1 92  ? 138.265 142.448 105.331 1.00 83.01  ?  84  LEU B CG  1 
ATOM 981  C CD1 . LEU B 1 92  ? 137.840 141.887 103.982 1.00 83.81  ?  84  LEU B CD1 1 
ATOM 982  C CD2 . LEU B 1 92  ? 139.773 142.342 105.507 1.00 79.77  ?  84  LEU B CD2 1 
ATOM 983  N N   . GLY B 1 93  ? 134.671 142.378 105.484 1.00 78.35  ?  85  GLY B N   1 
ATOM 984  C CA  . GLY B 1 93  ? 133.837 141.355 106.080 1.00 71.14  ?  85  GLY B CA  1 
ATOM 985  C C   . GLY B 1 93  ? 133.502 140.263 105.090 1.00 66.38  ?  85  GLY B C   1 
ATOM 986  O O   . GLY B 1 93  ? 133.856 140.331 103.911 1.00 67.07  ?  85  GLY B O   1 
ATOM 987  N N   . ASN B 1 94  ? 132.817 139.238 105.595 1.00 62.95  ?  86  ASN B N   1 
ATOM 988  C CA  . ASN B 1 94  ? 132.368 138.125 104.768 1.00 57.34  ?  86  ASN B CA  1 
ATOM 989  C C   . ASN B 1 94  ? 131.384 137.267 105.551 1.00 53.91  ?  86  ASN B C   1 
ATOM 990  O O   . ASN B 1 94  ? 131.638 136.927 106.710 1.00 55.84  ?  86  ASN B O   1 
ATOM 991  C CB  . ASN B 1 94  ? 133.551 137.269 104.301 1.00 57.30  ?  86  ASN B CB  1 
ATOM 992  C CG  . ASN B 1 94  ? 134.514 136.941 105.426 1.00 54.05  ?  86  ASN B CG  1 
ATOM 993  O OD1 . ASN B 1 94  ? 135.021 137.832 106.107 1.00 55.15  ?  86  ASN B OD1 1 
ATOM 994  N ND2 . ASN B 1 94  ? 134.771 135.653 105.627 1.00 51.29  ?  86  ASN B ND2 1 
ATOM 995  N N   . VAL B 1 95  ? 130.267 136.910 104.923 1.00 53.01  ?  87  VAL B N   1 
ATOM 996  C CA  . VAL B 1 95  ? 129.315 135.979 105.514 1.00 52.38  ?  87  VAL B CA  1 
ATOM 997  C C   . VAL B 1 95  ? 129.614 134.593 104.958 1.00 58.67  ?  87  VAL B C   1 
ATOM 998  O O   . VAL B 1 95  ? 129.965 134.435 103.783 1.00 62.80  ?  87  VAL B O   1 
ATOM 999  C CB  . VAL B 1 95  ? 127.849 136.398 105.263 1.00 47.00  ?  87  VAL B CB  1 
ATOM 1000 C CG1 . VAL B 1 95  ? 127.658 137.880 105.573 1.00 41.34  ?  87  VAL B CG1 1 
ATOM 1001 C CG2 . VAL B 1 95  ? 127.407 136.078 103.859 1.00 46.98  ?  87  VAL B CG2 1 
ATOM 1002 N N   . THR B 1 96  ? 129.513 133.585 105.823 1.00 60.00  ?  88  THR B N   1 
ATOM 1003 C CA  . THR B 1 96  ? 130.030 132.259 105.522 1.00 64.49  ?  88  THR B CA  1 
ATOM 1004 C C   . THR B 1 96  ? 129.040 131.199 105.983 1.00 68.43  ?  88  THR B C   1 
ATOM 1005 O O   . THR B 1 96  ? 128.680 131.153 107.163 1.00 69.23  ?  88  THR B O   1 
ATOM 1006 C CB  . THR B 1 96  ? 131.391 132.053 106.197 1.00 68.10  ?  88  THR B CB  1 
ATOM 1007 O OG1 . THR B 1 96  ? 132.257 133.146 105.865 1.00 63.64  ?  88  THR B OG1 1 
ATOM 1008 C CG2 . THR B 1 96  ? 132.031 130.774 105.725 1.00 70.67  ?  88  THR B CG2 1 
ATOM 1009 N N   . ALA B 1 97  ? 128.600 130.350 105.049 1.00 70.62  ?  89  ALA B N   1 
ATOM 1010 C CA  . ALA B 1 97  ? 127.618 129.302 105.329 1.00 69.18  ?  89  ALA B CA  1 
ATOM 1011 C C   . ALA B 1 97  ? 127.960 128.031 104.542 1.00 73.53  ?  89  ALA B C   1 
ATOM 1012 O O   . ALA B 1 97  ? 127.107 127.430 103.892 1.00 71.42  ?  89  ALA B O   1 
ATOM 1013 C CB  . ALA B 1 97  ? 126.204 129.788 105.015 1.00 55.21  ?  89  ALA B CB  1 
ATOM 1014 N N   . ASP B 1 98  ? 129.225 127.622 104.590 1.00 75.25  ?  90  ASP B N   1 
ATOM 1015 C CA  . ASP B 1 98  ? 129.686 126.419 103.909 1.00 77.12  ?  90  ASP B CA  1 
ATOM 1016 C C   . ASP B 1 98  ? 129.632 125.192 104.815 1.00 76.53  ?  90  ASP B C   1 
ATOM 1017 O O   . ASP B 1 98  ? 128.970 125.176 105.857 1.00 74.45  ?  90  ASP B O   1 
ATOM 1018 C CB  . ASP B 1 98  ? 131.097 126.598 103.340 1.00 82.61  ?  90  ASP B CB  1 
ATOM 1019 C CG  . ASP B 1 98  ? 131.342 127.991 102.821 1.00 83.75  ?  90  ASP B CG  1 
ATOM 1020 O OD1 . ASP B 1 98  ? 132.162 128.716 103.414 1.00 82.56  ?  90  ASP B OD1 1 
ATOM 1021 O OD2 . ASP B 1 98  ? 130.705 128.355 101.811 1.00 82.26  -1 90  ASP B OD2 1 
ATOM 1022 N N   . LYS B 1 99  ? 130.222 124.105 104.308 1.00 79.82  ?  91  LYS B N   1 
ATOM 1023 C CA  . LYS B 1 99  ? 130.174 122.824 105.055 1.00 79.00  ?  91  LYS B CA  1 
ATOM 1024 C C   . LYS B 1 99  ? 131.284 121.890 104.556 1.00 83.57  ?  91  LYS B C   1 
ATOM 1025 O O   . LYS B 1 99  ? 131.753 122.087 103.415 1.00 89.29  ?  91  LYS B O   1 
ATOM 1026 C CB  . LYS B 1 99  ? 128.793 122.182 104.888 1.00 75.53  ?  91  LYS B CB  1 
ATOM 1027 C CG  . LYS B 1 99  ? 128.448 121.110 105.912 1.00 80.00  ?  91  LYS B CG  1 
ATOM 1028 C CD  . LYS B 1 99  ? 126.969 120.744 105.912 1.00 79.46  ?  91  LYS B CD  1 
ATOM 1029 C CE  . LYS B 1 99  ? 126.492 120.323 104.559 1.00 84.72  ?  91  LYS B CE  1 
ATOM 1030 N NZ  . LYS B 1 99  ? 125.057 120.029 104.559 1.00 97.74  1  91  LYS B NZ  1 
ATOM 1031 N N   . ASP B 1 100 ? 131.671 120.944 105.414 1.00 81.87  ?  92  ASP B N   1 
ATOM 1032 C CA  . ASP B 1 100 ? 132.728 119.969 105.048 1.00 83.84  ?  92  ASP B CA  1 
ATOM 1033 C C   . ASP B 1 100 ? 132.504 118.678 105.833 1.00 85.39  ?  92  ASP B C   1 
ATOM 1034 O O   . ASP B 1 100 ? 131.673 118.684 106.766 1.00 89.15  ?  92  ASP B O   1 
ATOM 1035 C CB  . ASP B 1 100 ? 134.119 120.550 105.253 1.00 86.42  ?  92  ASP B CB  1 
ATOM 1036 C CG  . ASP B 1 100 ? 134.609 120.628 106.692 1.00 91.06  ?  92  ASP B CG  1 
ATOM 1037 O OD1 . ASP B 1 100 ? 134.869 119.560 107.284 1.00 88.87  ?  92  ASP B OD1 1 
ATOM 1038 O OD2 . ASP B 1 100 ? 134.722 121.758 107.211 1.00 93.76  -1 92  ASP B OD2 1 
ATOM 1039 N N   . GLY B 1 101 ? 133.221 117.622 105.468 1.00 79.29  ?  93  GLY B N   1 
ATOM 1040 C CA  . GLY B 1 101 ? 133.136 116.331 106.122 1.00 71.84  ?  93  GLY B CA  1 
ATOM 1041 C C   . GLY B 1 101 ? 133.119 115.205 105.106 1.00 69.42  ?  93  GLY B C   1 
ATOM 1042 O O   . GLY B 1 101 ? 132.452 115.276 104.070 1.00 69.13  ?  93  GLY B O   1 
ATOM 1043 N N   . VAL B 1 102 ? 133.855 114.138 105.407 1.00 68.71  ?  94  VAL B N   1 
ATOM 1044 C CA  . VAL B 1 102 ? 134.044 113.046 104.460 1.00 67.28  ?  94  VAL B CA  1 
ATOM 1045 C C   . VAL B 1 102 ? 133.347 111.806 105.004 1.00 68.78  ?  94  VAL B C   1 
ATOM 1046 O O   . VAL B 1 102 ? 133.374 111.541 106.212 1.00 71.47  ?  94  VAL B O   1 
ATOM 1047 C CB  . VAL B 1 102 ? 135.540 112.778 104.191 1.00 66.89  ?  94  VAL B CB  1 
ATOM 1048 C CG1 . VAL B 1 102 ? 136.201 114.026 103.616 1.00 71.34  ?  94  VAL B CG1 1 
ATOM 1049 C CG2 . VAL B 1 102 ? 136.258 112.288 105.429 1.00 66.12  ?  94  VAL B CG2 1 
ATOM 1050 N N   . ALA B 1 103 ? 132.690 111.064 104.115 1.00 68.23  ?  95  ALA B N   1 
ATOM 1051 C CA  . ALA B 1 103 ? 131.942 109.878 104.503 1.00 68.77  ?  95  ALA B CA  1 
ATOM 1052 C C   . ALA B 1 103 ? 131.975 108.875 103.361 1.00 72.34  ?  95  ALA B C   1 
ATOM 1053 O O   . ALA B 1 103 ? 132.770 109.009 102.429 1.00 73.15  ?  95  ALA B O   1 
ATOM 1054 C CB  . ALA B 1 103 ? 130.492 110.219 104.868 1.00 67.48  ?  95  ALA B CB  1 
ATOM 1055 N N   . ASP B 1 104 ? 131.125 107.850 103.459 1.00 72.34  ?  96  ASP B N   1 
ATOM 1056 C CA  . ASP B 1 104 ? 130.906 106.964 102.320 1.00 70.64  ?  96  ASP B CA  1 
ATOM 1057 C C   . ASP B 1 104 ? 129.421 106.830 101.998 1.00 70.01  ?  96  ASP B C   1 
ATOM 1058 O O   . ASP B 1 104 ? 129.042 106.762 100.826 1.00 71.59  ?  96  ASP B O   1 
ATOM 1059 C CB  . ASP B 1 104 ? 131.548 105.593 102.564 1.00 68.86  ?  96  ASP B CB  1 
ATOM 1060 C CG  . ASP B 1 104 ? 131.092 104.937 103.857 1.00 69.61  ?  96  ASP B CG  1 
ATOM 1061 O OD1 . ASP B 1 104 ? 131.927 104.270 104.502 1.00 70.65  ?  96  ASP B OD1 1 
ATOM 1062 O OD2 . ASP B 1 104 ? 129.905 105.057 104.219 1.00 71.40  -1 96  ASP B OD2 1 
ATOM 1063 N N   . VAL B 1 105 ? 128.566 106.801 103.017 1.00 64.12  ?  97  VAL B N   1 
ATOM 1064 C CA  . VAL B 1 105 ? 127.118 106.792 102.830 1.00 60.56  ?  97  VAL B CA  1 
ATOM 1065 C C   . VAL B 1 105 ? 126.569 108.092 103.404 1.00 61.90  ?  97  VAL B C   1 
ATOM 1066 O O   . VAL B 1 105 ? 126.647 108.323 104.617 1.00 63.73  ?  97  VAL B O   1 
ATOM 1067 C CB  . VAL B 1 105 ? 126.452 105.575 103.494 1.00 59.54  ?  97  VAL B CB  1 
ATOM 1068 C CG1 . VAL B 1 105 ? 124.952 105.799 103.642 1.00 61.30  ?  97  VAL B CG1 1 
ATOM 1069 C CG2 . VAL B 1 105 ? 126.727 104.315 102.692 1.00 59.51  ?  97  VAL B CG2 1 
ATOM 1070 N N   . SER B 1 106 ? 126.021 108.939 102.536 1.00 60.17  ?  98  SER B N   1 
ATOM 1071 C CA  . SER B 1 106 ? 125.502 110.241 102.937 1.00 58.65  ?  98  SER B CA  1 
ATOM 1072 C C   . SER B 1 106 ? 124.177 110.485 102.232 1.00 60.75  ?  98  SER B C   1 
ATOM 1073 O O   . SER B 1 106 ? 124.122 110.502 100.999 1.00 67.09  ?  98  SER B O   1 
ATOM 1074 C CB  . SER B 1 106 ? 126.497 111.358 102.610 1.00 62.75  ?  98  SER B CB  1 
ATOM 1075 O OG  . SER B 1 106 ? 125.973 112.628 102.957 1.00 65.82  ?  98  SER B OG  1 
ATOM 1076 N N   . ILE B 1 107 ? 123.118 110.673 103.015 1.00 56.92  ?  99  ILE B N   1 
ATOM 1077 C CA  . ILE B 1 107 ? 121.785 110.956 102.496 1.00 58.31  ?  99  ILE B CA  1 
ATOM 1078 C C   . ILE B 1 107 ? 121.274 112.219 103.172 1.00 59.95  ?  99  ILE B C   1 
ATOM 1079 O O   . ILE B 1 107 ? 121.278 112.313 104.405 1.00 63.35  ?  99  ILE B O   1 
ATOM 1080 C CB  . ILE B 1 107 ? 120.821 109.777 102.729 1.00 58.58  ?  99  ILE B CB  1 
ATOM 1081 C CG1 . ILE B 1 107 ? 121.050 108.688 101.680 1.00 56.46  ?  99  ILE B CG1 1 
ATOM 1082 C CG2 . ILE B 1 107 ? 119.375 110.248 102.697 1.00 57.79  ?  99  ILE B CG2 1 
ATOM 1083 C CD1 . ILE B 1 107 ? 120.677 107.299 102.149 1.00 51.99  ?  99  ILE B CD1 1 
ATOM 1084 N N   . GLU B 1 108 ? 120.842 113.191 102.371 1.00 57.62  ?  100 GLU B N   1 
ATOM 1085 C CA  . GLU B 1 108 ? 120.368 114.465 102.896 1.00 58.25  ?  100 GLU B CA  1 
ATOM 1086 C C   . GLU B 1 108 ? 119.137 114.914 102.126 1.00 62.05  ?  100 GLU B C   1 
ATOM 1087 O O   . GLU B 1 108 ? 119.130 114.886 100.892 1.00 62.23  ?  100 GLU B O   1 
ATOM 1088 C CB  . GLU B 1 108 ? 121.461 115.538 102.813 1.00 61.43  ?  100 GLU B CB  1 
ATOM 1089 C CG  . GLU B 1 108 ? 122.315 115.650 104.066 1.00 68.72  ?  100 GLU B CG  1 
ATOM 1090 C CD  . GLU B 1 108 ? 123.688 116.229 103.785 1.00 76.46  ?  100 GLU B CD  1 
ATOM 1091 O OE1 . GLU B 1 108 ? 123.764 117.393 103.338 1.00 76.22  ?  100 GLU B OE1 1 
ATOM 1092 O OE2 . GLU B 1 108 ? 124.692 115.520 104.011 1.00 76.18  -1 100 GLU B OE2 1 
ATOM 1093 N N   . ASP B 1 109 ? 118.104 115.330 102.863 1.00 63.82  ?  101 ASP B N   1 
ATOM 1094 C CA  . ASP B 1 109 ? 116.872 115.874 102.285 1.00 57.98  ?  101 ASP B CA  1 
ATOM 1095 C C   . ASP B 1 109 ? 116.236 114.900 101.295 1.00 55.19  ?  101 ASP B C   1 
ATOM 1096 O O   . ASP B 1 109 ? 115.692 115.302 100.266 1.00 56.07  ?  101 ASP B O   1 
ATOM 1097 C CB  . ASP B 1 109 ? 117.125 117.230 101.621 1.00 61.33  ?  101 ASP B CB  1 
ATOM 1098 C CG  . ASP B 1 109 ? 118.167 118.054 102.352 1.00 64.04  ?  101 ASP B CG  1 
ATOM 1099 O OD1 . ASP B 1 109 ? 117.968 118.341 103.551 1.00 65.84  ?  101 ASP B OD1 1 
ATOM 1100 O OD2 . ASP B 1 109 ? 119.186 118.415 101.728 1.00 62.09  -1 101 ASP B OD2 1 
ATOM 1101 N N   . SER B 1 110 ? 116.288 113.609 101.614 1.00 53.07  ?  102 SER B N   1 
ATOM 1102 C CA  . SER B 1 110 ? 115.797 112.566 100.726 1.00 50.43  ?  102 SER B CA  1 
ATOM 1103 C C   . SER B 1 110 ? 114.682 111.789 101.419 1.00 45.76  ?  102 SER B C   1 
ATOM 1104 O O   . SER B 1 110 ? 114.436 111.942 102.618 1.00 49.36  ?  102 SER B O   1 
ATOM 1105 C CB  . SER B 1 110 ? 116.933 111.628 100.296 1.00 56.20  ?  102 SER B CB  1 
ATOM 1106 O OG  . SER B 1 110 ? 117.688 112.195 99.240  1.00 66.02  ?  102 SER B OG  1 
ATOM 1107 N N   . VAL B 1 111 ? 114.000 110.949 100.645 1.00 42.69  ?  103 VAL B N   1 
ATOM 1108 C CA  . VAL B 1 111 ? 112.938 110.086 101.149 1.00 43.70  ?  103 VAL B CA  1 
ATOM 1109 C C   . VAL B 1 111 ? 113.251 108.661 100.717 1.00 43.90  ?  103 VAL B C   1 
ATOM 1110 O O   . VAL B 1 111 ? 113.280 108.366 99.516  1.00 46.53  ?  103 VAL B O   1 
ATOM 1111 C CB  . VAL B 1 111 ? 111.551 110.513 100.638 1.00 41.76  ?  103 VAL B CB  1 
ATOM 1112 C CG1 . VAL B 1 111 ? 110.487 109.539 101.118 1.00 41.31  ?  103 VAL B CG1 1 
ATOM 1113 C CG2 . VAL B 1 111 ? 111.228 111.929 101.094 1.00 39.91  ?  103 VAL B CG2 1 
ATOM 1114 N N   . ILE B 1 112 ? 113.484 107.781 101.689 1.00 41.15  ?  104 ILE B N   1 
ATOM 1115 C CA  . ILE B 1 112 ? 113.831 106.389 101.435 1.00 44.16  ?  104 ILE B CA  1 
ATOM 1116 C C   . ILE B 1 112 ? 112.802 105.501 102.119 1.00 47.34  ?  104 ILE B C   1 
ATOM 1117 O O   . ILE B 1 112 ? 112.373 105.785 103.243 1.00 47.97  ?  104 ILE B O   1 
ATOM 1118 C CB  . ILE B 1 112 ? 115.253 106.050 101.931 1.00 45.87  ?  104 ILE B CB  1 
ATOM 1119 C CG1 . ILE B 1 112 ? 116.188 107.252 101.776 1.00 46.46  ?  104 ILE B CG1 1 
ATOM 1120 C CG2 . ILE B 1 112 ? 115.804 104.848 101.182 1.00 42.68  ?  104 ILE B CG2 1 
ATOM 1121 C CD1 . ILE B 1 112 ? 116.555 107.575 100.358 1.00 43.99  ?  104 ILE B CD1 1 
ATOM 1122 N N   . SER B 1 113 ? 112.405 104.428 101.437 1.00 48.70  ?  105 SER B N   1 
ATOM 1123 C CA  . SER B 1 113 ? 111.445 103.469 101.980 1.00 50.12  ?  105 SER B CA  1 
ATOM 1124 C C   . SER B 1 113 ? 111.844 102.079 101.507 1.00 50.68  ?  105 SER B C   1 
ATOM 1125 O O   . SER B 1 113 ? 111.664 101.747 100.330 1.00 51.76  ?  105 SER B O   1 
ATOM 1126 C CB  . SER B 1 113 ? 110.018 103.806 101.549 1.00 51.75  ?  105 SER B CB  1 
ATOM 1127 O OG  . SER B 1 113 ? 109.893 103.785 100.137 1.00 56.08  ?  105 SER B OG  1 
ATOM 1128 N N   . LEU B 1 114 ? 112.381 101.268 102.417 1.00 51.90  ?  106 LEU B N   1 
ATOM 1129 C CA  . LEU B 1 114 ? 112.807 99.902  102.113 1.00 54.88  ?  106 LEU B CA  1 
ATOM 1130 C C   . LEU B 1 114 ? 112.074 98.965  103.068 1.00 58.03  ?  106 LEU B C   1 
ATOM 1131 O O   . LEU B 1 114 ? 112.546 98.712  104.180 1.00 59.34  ?  106 LEU B O   1 
ATOM 1132 C CB  . LEU B 1 114 ? 114.320 99.742  102.241 1.00 51.99  ?  106 LEU B CB  1 
ATOM 1133 C CG  . LEU B 1 114 ? 115.238 100.900 101.837 1.00 43.98  ?  106 LEU B CG  1 
ATOM 1134 C CD1 . LEU B 1 114 ? 116.695 100.504 102.014 1.00 38.32  ?  106 LEU B CD1 1 
ATOM 1135 C CD2 . LEU B 1 114 ? 114.980 101.346 100.412 1.00 46.48  ?  106 LEU B CD2 1 
ATOM 1136 N N   . SER B 1 115 ? 110.928 98.448  102.636 1.00 60.00  ?  107 SER B N   1 
ATOM 1137 C CA  . SER B 1 115 ? 110.114 97.561  103.455 1.00 57.45  ?  107 SER B CA  1 
ATOM 1138 C C   . SER B 1 115 ? 110.350 96.111  103.052 1.00 57.98  ?  107 SER B C   1 
ATOM 1139 O O   . SER B 1 115 ? 110.360 95.779  101.863 1.00 58.97  ?  107 SER B O   1 
ATOM 1140 C CB  . SER B 1 115 ? 108.630 97.905  103.322 1.00 61.13  ?  107 SER B CB  1 
ATOM 1141 O OG  . SER B 1 115 ? 107.835 97.046  104.121 1.00 66.11  ?  107 SER B OG  1 
ATOM 1142 N N   . GLY B 1 116 ? 110.537 95.256  104.045 1.00 56.34  ?  108 GLY B N   1 
ATOM 1143 C CA  . GLY B 1 116 ? 110.768 93.848  103.810 1.00 55.95  ?  108 GLY B CA  1 
ATOM 1144 C C   . GLY B 1 116 ? 111.647 93.268  104.901 1.00 54.04  ?  108 GLY B C   1 
ATOM 1145 O O   . GLY B 1 116 ? 111.697 93.781  106.014 1.00 55.80  ?  108 GLY B O   1 
ATOM 1146 N N   . ASP B 1 117 ? 112.325 92.177  104.527 1.00 53.28  ?  109 ASP B N   1 
ATOM 1147 C CA  . ASP B 1 117 ? 113.208 91.474  105.488 1.00 56.24  ?  109 ASP B CA  1 
ATOM 1148 C C   . ASP B 1 117 ? 114.664 91.859  105.232 1.00 54.97  ?  109 ASP B C   1 
ATOM 1149 O O   . ASP B 1 117 ? 115.034 92.033  104.050 1.00 58.57  ?  109 ASP B O   1 
ATOM 1150 C CB  . ASP B 1 117 ? 113.002 89.969  105.429 1.00 59.64  ?  109 ASP B CB  1 
ATOM 1151 C CG  . ASP B 1 117 ? 111.589 89.498  105.741 1.00 64.19  ?  109 ASP B CG  1 
ATOM 1152 O OD1 . ASP B 1 117 ? 110.662 89.903  105.009 1.00 64.97  ?  109 ASP B OD1 1 
ATOM 1153 O OD2 . ASP B 1 117 ? 111.428 88.735  106.717 1.00 65.83  -1 109 ASP B OD2 1 
ATOM 1154 N N   . HIS B 1 118 ? 115.443 91.986  106.297 1.00 54.12  ?  110 HIS B N   1 
ATOM 1155 C CA  . HIS B 1 118 ? 116.864 92.337  106.250 1.00 54.88  ?  110 HIS B CA  1 
ATOM 1156 C C   . HIS B 1 118 ? 117.069 93.697  105.573 1.00 53.17  ?  110 HIS B C   1 
ATOM 1157 O O   . HIS B 1 118 ? 117.728 93.828  104.540 1.00 56.45  ?  110 HIS B O   1 
ATOM 1158 C CB  . HIS B 1 118 ? 117.678 91.240  105.554 1.00 58.25  ?  110 HIS B CB  1 
ATOM 1159 C CG  . HIS B 1 118 ? 117.496 89.880  106.153 1.00 61.96  ?  110 HIS B CG  1 
ATOM 1160 N ND1 . HIS B 1 118 ? 117.088 88.790  105.415 1.00 63.66  ?  110 HIS B ND1 1 
ATOM 1161 C CD2 . HIS B 1 118 ? 117.667 89.434  107.420 1.00 64.08  ?  110 HIS B CD2 1 
ATOM 1162 C CE1 . HIS B 1 118 ? 117.016 87.730  106.201 1.00 66.25  ?  110 HIS B CE1 1 
ATOM 1163 N NE2 . HIS B 1 118 ? 117.362 88.094  107.423 1.00 65.97  ?  110 HIS B NE2 1 
ATOM 1164 N N   . CYS B 1 119 ? 116.476 94.712  106.196 1.00 50.28  ?  111 CYS B N   1 
ATOM 1165 C CA  . CYS B 1 119 ? 116.627 96.099  105.769 1.00 47.95  ?  111 CYS B CA  1 
ATOM 1166 C C   . CYS B 1 119 ? 117.680 96.751  106.656 1.00 49.91  ?  111 CYS B C   1 
ATOM 1167 O O   . CYS B 1 119 ? 117.387 97.154  107.787 1.00 54.61  ?  111 CYS B O   1 
ATOM 1168 C CB  . CYS B 1 119 ? 115.296 96.842  105.849 1.00 48.90  ?  111 CYS B CB  1 
ATOM 1169 S SG  . CYS B 1 119 ? 113.913 95.970  105.079 1.00 52.14  ?  111 CYS B SG  1 
ATOM 1170 N N   . ILE B 1 120 ? 118.903 96.857  106.142 1.00 47.41  ?  112 ILE B N   1 
ATOM 1171 C CA  . ILE B 1 120 ? 120.051 97.324  106.911 1.00 46.51  ?  112 ILE B CA  1 
ATOM 1172 C C   . ILE B 1 120 ? 120.637 98.547  106.221 1.00 49.01  ?  112 ILE B C   1 
ATOM 1173 O O   . ILE B 1 120 ? 120.768 98.571  104.993 1.00 54.47  ?  112 ILE B O   1 
ATOM 1174 C CB  . ILE B 1 120 ? 121.116 96.224  107.065 1.00 49.70  ?  112 ILE B CB  1 
ATOM 1175 C CG1 . ILE B 1 120 ? 120.452 94.860  107.274 1.00 54.70  ?  112 ILE B CG1 1 
ATOM 1176 C CG2 . ILE B 1 120 ? 122.055 96.547  108.217 1.00 50.02  ?  112 ILE B CG2 1 
ATOM 1177 C CD1 . ILE B 1 120 ? 121.419 93.700  107.273 1.00 54.77  ?  112 ILE B CD1 1 
ATOM 1178 N N   . ILE B 1 121 ? 120.985 99.559  107.013 1.00 47.94  ?  113 ILE B N   1 
ATOM 1179 C CA  . ILE B 1 121 ? 121.657 100.758 106.527 1.00 45.58  ?  113 ILE B CA  1 
ATOM 1180 C C   . ILE B 1 121 ? 123.048 100.786 107.142 1.00 45.63  ?  113 ILE B C   1 
ATOM 1181 O O   . ILE B 1 121 ? 123.189 100.835 108.371 1.00 47.62  ?  113 ILE B O   1 
ATOM 1182 C CB  . ILE B 1 121 ? 120.876 102.035 106.875 1.00 42.73  ?  113 ILE B CB  1 
ATOM 1183 C CG1 . ILE B 1 121 ? 119.580 102.105 106.064 1.00 41.00  ?  113 ILE B CG1 1 
ATOM 1184 C CG2 . ILE B 1 121 ? 121.732 103.268 106.626 1.00 41.28  ?  113 ILE B CG2 1 
ATOM 1185 C CD1 . ILE B 1 121 ? 118.826 103.407 106.225 1.00 34.55  ?  113 ILE B CD1 1 
ATOM 1186 N N   . GLY B 1 122 ? 124.068 100.755 106.297 1.00 44.91  ?  114 GLY B N   1 
ATOM 1187 C CA  . GLY B 1 122 ? 125.445 100.697 106.737 1.00 48.20  ?  114 GLY B CA  1 
ATOM 1188 C C   . GLY B 1 122 ? 126.065 99.332  106.481 1.00 55.05  ?  114 GLY B C   1 
ATOM 1189 O O   . GLY B 1 122 ? 125.468 98.441  105.876 1.00 60.26  ?  114 GLY B O   1 
ATOM 1190 N N   . ARG B 1 123 ? 127.299 99.189  106.960 1.00 56.45  ?  115 ARG B N   1 
ATOM 1191 C CA  . ARG B 1 123 ? 128.012 97.929  106.801 1.00 60.05  ?  115 ARG B CA  1 
ATOM 1192 C C   . ARG B 1 123 ? 127.333 96.824  107.601 1.00 63.05  ?  115 ARG B C   1 
ATOM 1193 O O   . ARG B 1 123 ? 126.788 97.061  108.682 1.00 67.17  ?  115 ARG B O   1 
ATOM 1194 C CB  . ARG B 1 123 ? 129.473 98.083  107.230 1.00 60.37  ?  115 ARG B CB  1 
ATOM 1195 C CG  . ARG B 1 123 ? 129.676 98.381  108.705 1.00 62.22  ?  115 ARG B CG  1 
ATOM 1196 C CD  . ARG B 1 123 ? 131.156 98.415  109.056 1.00 63.70  ?  115 ARG B CD  1 
ATOM 1197 N NE  . ARG B 1 123 ? 131.732 99.743  108.875 1.00 68.41  ?  115 ARG B NE  1 
ATOM 1198 C CZ  . ARG B 1 123 ? 132.414 100.396 109.805 1.00 69.03  ?  115 ARG B CZ  1 
ATOM 1199 N NH1 . ARG B 1 123 ? 132.630 99.872  111.000 1.00 66.49  1  115 ARG B NH1 1 
ATOM 1200 N NH2 . ARG B 1 123 ? 132.894 101.605 109.528 1.00 71.22  ?  115 ARG B NH2 1 
ATOM 1201 N N   . THR B 1 124 ? 127.353 95.612  107.054 1.00 62.52  ?  116 THR B N   1 
ATOM 1202 C CA  . THR B 1 124 ? 126.721 94.463  107.691 1.00 62.73  ?  116 THR B CA  1 
ATOM 1203 C C   . THR B 1 124 ? 127.311 93.188  107.103 1.00 64.55  ?  116 THR B C   1 
ATOM 1204 O O   . THR B 1 124 ? 128.133 93.223  106.184 1.00 68.81  ?  116 THR B O   1 
ATOM 1205 C CB  . THR B 1 124 ? 125.198 94.499  107.527 1.00 62.54  ?  116 THR B CB  1 
ATOM 1206 O OG1 . THR B 1 124 ? 124.620 93.365  108.185 1.00 67.18  ?  116 THR B OG1 1 
ATOM 1207 C CG2 . THR B 1 124 ? 124.813 94.488  106.064 1.00 62.11  ?  116 THR B CG2 1 
ATOM 1208 N N   . LEU B 1 125 ? 126.877 92.054  107.648 1.00 66.11  ?  117 LEU B N   1 
ATOM 1209 C CA  . LEU B 1 125 ? 127.347 90.747  107.197 1.00 69.44  ?  117 LEU B CA  1 
ATOM 1210 C C   . LEU B 1 125 ? 126.250 89.737  107.501 1.00 74.04  ?  117 LEU B C   1 
ATOM 1211 O O   . LEU B 1 125 ? 125.943 89.495  108.673 1.00 78.90  ?  117 LEU B O   1 
ATOM 1212 C CB  . LEU B 1 125 ? 128.656 90.371  107.885 1.00 69.18  ?  117 LEU B CB  1 
ATOM 1213 C CG  . LEU B 1 125 ? 129.687 89.589  107.066 1.00 67.69  ?  117 LEU B CG  1 
ATOM 1214 C CD1 . LEU B 1 125 ? 131.030 89.579  107.779 1.00 64.04  ?  117 LEU B CD1 1 
ATOM 1215 C CD2 . LEU B 1 125 ? 129.213 88.169  106.795 1.00 69.31  ?  117 LEU B CD2 1 
ATOM 1216 N N   . VAL B 1 126 ? 125.666 89.155  106.457 1.00 75.25  ?  118 VAL B N   1 
ATOM 1217 C CA  . VAL B 1 126 ? 124.569 88.204  106.587 1.00 77.60  ?  118 VAL B CA  1 
ATOM 1218 C C   . VAL B 1 126 ? 125.036 86.857  106.056 1.00 78.22  ?  118 VAL B C   1 
ATOM 1219 O O   . VAL B 1 126 ? 125.525 86.764  104.925 1.00 79.51  ?  118 VAL B O   1 
ATOM 1220 C CB  . VAL B 1 126 ? 123.312 88.681  105.836 1.00 78.76  ?  118 VAL B CB  1 
ATOM 1221 C CG1 . VAL B 1 126 ? 122.173 87.689  106.022 1.00 78.09  ?  118 VAL B CG1 1 
ATOM 1222 C CG2 . VAL B 1 126 ? 122.904 90.068  106.309 1.00 73.56  ?  118 VAL B CG2 1 
ATOM 1223 N N   . VAL B 1 127 ? 124.884 85.818  106.875 1.00 78.07  ?  119 VAL B N   1 
ATOM 1224 C CA  . VAL B 1 127 ? 125.272 84.459  106.513 1.00 80.37  ?  119 VAL B CA  1 
ATOM 1225 C C   . VAL B 1 127 ? 124.070 83.549  106.717 1.00 83.95  ?  119 VAL B C   1 
ATOM 1226 O O   . VAL B 1 127 ? 123.477 83.529  107.801 1.00 85.60  ?  119 VAL B O   1 
ATOM 1227 C CB  . VAL B 1 127 ? 126.473 83.967  107.344 1.00 79.15  ?  119 VAL B CB  1 
ATOM 1228 C CG1 . VAL B 1 127 ? 126.667 82.469  107.167 1.00 78.97  ?  119 VAL B CG1 1 
ATOM 1229 C CG2 . VAL B 1 127 ? 127.733 84.722  106.954 1.00 78.38  ?  119 VAL B CG2 1 
ATOM 1230 N N   . HIS B 1 128 ? 123.714 82.797  105.679 1.00 86.95  ?  120 HIS B N   1 
ATOM 1231 C CA  . HIS B 1 128 ? 122.600 81.859  105.730 1.00 88.45  ?  120 HIS B CA  1 
ATOM 1232 C C   . HIS B 1 128 ? 123.150 80.441  105.817 1.00 90.30  ?  120 HIS B C   1 
ATOM 1233 O O   . HIS B 1 128 ? 123.953 80.031  104.972 1.00 89.93  ?  120 HIS B O   1 
ATOM 1234 C CB  . HIS B 1 128 ? 121.699 82.014  104.505 1.00 87.72  ?  120 HIS B CB  1 
ATOM 1235 C CG  . HIS B 1 128 ? 120.646 83.066  104.658 1.00 88.59  ?  120 HIS B CG  1 
ATOM 1236 N ND1 . HIS B 1 128 ? 120.501 84.110  103.769 1.00 88.11  ?  120 HIS B ND1 1 
ATOM 1237 C CD2 . HIS B 1 128 ? 119.684 83.236  105.596 1.00 87.73  ?  120 HIS B CD2 1 
ATOM 1238 C CE1 . HIS B 1 128 ? 119.497 84.877  104.153 1.00 83.30  ?  120 HIS B CE1 1 
ATOM 1239 N NE2 . HIS B 1 128 ? 118.983 84.369  105.259 1.00 82.92  ?  120 HIS B NE2 1 
ATOM 1240 N N   . GLU B 1 129 ? 122.714 79.702  106.836 1.00 92.63  ?  121 GLU B N   1 
ATOM 1241 C CA  . GLU B 1 129 ? 123.152 78.326  107.067 1.00 95.14  ?  121 GLU B CA  1 
ATOM 1242 C C   . GLU B 1 129 ? 124.672 78.217  107.144 1.00 91.48  ?  121 GLU B C   1 
ATOM 1243 O O   . GLU B 1 129 ? 125.342 79.106  107.669 1.00 89.98  ?  121 GLU B O   1 
ATOM 1244 C CB  . GLU B 1 129 ? 122.614 77.399  105.972 1.00 95.66  ?  121 GLU B CB  1 
ATOM 1245 C CG  . GLU B 1 129 ? 121.123 77.541  105.715 1.00 98.85  ?  121 GLU B CG  1 
ATOM 1246 C CD  . GLU B 1 129 ? 120.449 76.209  105.450 1.00 103.82 ?  121 GLU B CD  1 
ATOM 1247 O OE1 . GLU B 1 129 ? 121.015 75.166  105.843 1.00 99.75  ?  121 GLU B OE1 1 
ATOM 1248 O OE2 . GLU B 1 129 ? 119.355 76.204  104.848 1.00 106.63 -1 121 GLU B OE2 1 
ATOM 1249 N N   . ALA C 1 9   ? 92.491  143.770 96.634  1.00 55.72  ?  1   ALA A N   1 
ATOM 1250 C CA  . ALA C 1 9   ? 93.467  142.976 95.898  1.00 56.34  ?  1   ALA A CA  1 
ATOM 1251 C C   . ALA C 1 9   ? 93.304  141.490 96.200  1.00 54.10  ?  1   ALA A C   1 
ATOM 1252 O O   . ALA C 1 9   ? 93.979  140.654 95.601  1.00 51.98  ?  1   ALA A O   1 
ATOM 1253 C CB  . ALA C 1 9   ? 94.881  143.433 96.229  1.00 53.70  ?  1   ALA A CB  1 
ATOM 1254 N N   . THR C 1 10  ? 92.395  141.180 97.129  1.00 55.69  ?  2   THR A N   1 
ATOM 1255 C CA  . THR C 1 10  ? 92.109  139.817 97.570  1.00 57.85  ?  2   THR A CA  1 
ATOM 1256 C C   . THR C 1 10  ? 93.413  139.102 97.924  1.00 60.11  ?  2   THR A C   1 
ATOM 1257 O O   . THR C 1 10  ? 93.949  139.303 99.018  1.00 62.57  ?  2   THR A O   1 
ATOM 1258 C CB  . THR C 1 10  ? 91.306  139.058 96.507  1.00 57.79  ?  2   THR A CB  1 
ATOM 1259 O OG1 . THR C 1 10  ? 90.057  139.725 96.299  1.00 57.08  ?  2   THR A OG1 1 
ATOM 1260 C CG2 . THR C 1 10  ? 90.978  137.641 96.983  1.00 57.16  ?  2   THR A CG2 1 
ATOM 1261 N N   . LYS C 1 11  ? 93.930  138.263 97.029  1.00 56.21  ?  3   LYS A N   1 
ATOM 1262 C CA  . LYS C 1 11  ? 95.196  137.572 97.242  1.00 50.38  ?  3   LYS A CA  1 
ATOM 1263 C C   . LYS C 1 11  ? 96.244  138.177 96.319  1.00 45.18  ?  3   LYS A C   1 
ATOM 1264 O O   . LYS C 1 11  ? 96.092  138.137 95.093  1.00 48.01  ?  3   LYS A O   1 
ATOM 1265 C CB  . LYS C 1 11  ? 95.049  136.072 96.991  1.00 51.67  ?  3   LYS A CB  1 
ATOM 1266 C CG  . LYS C 1 11  ? 96.041  135.213 97.759  1.00 52.43  ?  3   LYS A CG  1 
ATOM 1267 C CD  . LYS C 1 11  ? 96.029  133.778 97.261  1.00 53.78  ?  3   LYS A CD  1 
ATOM 1268 C CE  . LYS C 1 11  ? 97.176  132.975 97.858  1.00 58.89  ?  3   LYS A CE  1 
ATOM 1269 N NZ  . LYS C 1 11  ? 98.478  133.686 97.733  1.00 61.87  1  3   LYS A NZ  1 
ATOM 1270 N N   . ALA C 1 12  ? 97.306  138.732 96.898  1.00 41.44  ?  4   ALA A N   1 
ATOM 1271 C CA  . ALA C 1 12  ? 98.290  139.453 96.096  1.00 36.97  ?  4   ALA A CA  1 
ATOM 1272 C C   . ALA C 1 12  ? 99.637  139.432 96.807  1.00 31.73  ?  4   ALA A C   1 
ATOM 1273 O O   . ALA C 1 12  ? 99.809  140.107 97.825  1.00 34.38  ?  4   ALA A O   1 
ATOM 1274 C CB  . ALA C 1 12  ? 97.825  140.880 95.840  1.00 41.09  ?  4   ALA A CB  1 
ATOM 1275 N N   . VAL C 1 13  ? 100.581 138.675 96.262  1.00 28.38  ?  5   VAL A N   1 
ATOM 1276 C CA  . VAL C 1 13  ? 101.950 138.637 96.763  1.00 28.15  ?  5   VAL A CA  1 
ATOM 1277 C C   . VAL C 1 13  ? 102.819 139.565 95.920  1.00 26.99  ?  5   VAL A C   1 
ATOM 1278 O O   . VAL C 1 13  ? 102.670 139.626 94.693  1.00 27.51  ?  5   VAL A O   1 
ATOM 1279 C CB  . VAL C 1 13  ? 102.492 137.196 96.768  1.00 30.26  ?  5   VAL A CB  1 
ATOM 1280 C CG1 . VAL C 1 13  ? 102.186 136.511 95.475  1.00 31.24  ?  5   VAL A CG1 1 
ATOM 1281 C CG2 . VAL C 1 13  ? 104.001 137.183 97.008  1.00 24.72  ?  5   VAL A CG2 1 
ATOM 1282 N N   . CYS C 1 14  ? 103.715 140.296 96.587  1.00 26.06  ?  6   CYS A N   1 
ATOM 1283 C CA  . CYS C 1 14  ? 104.618 141.265 95.963  1.00 23.51  ?  6   CYS A CA  1 
ATOM 1284 C C   . CYS C 1 14  ? 103.832 142.388 95.279  1.00 24.07  ?  6   CYS A C   1 
ATOM 1285 O O   . CYS C 1 14  ? 103.868 142.575 94.062  1.00 27.95  ?  6   CYS A O   1 
ATOM 1286 C CB  . CYS C 1 14  ? 105.574 140.580 94.980  1.00 24.39  ?  6   CYS A CB  1 
ATOM 1287 S SG  . CYS C 1 14  ? 107.151 141.437 94.767  1.00 26.80  ?  6   CYS A SG  1 
ATOM 1288 N N   . VAL C 1 15  ? 103.115 143.134 96.113  1.00 22.94  ?  7   VAL A N   1 
ATOM 1289 C CA  . VAL C 1 15  ? 102.406 144.339 95.696  1.00 24.99  ?  7   VAL A CA  1 
ATOM 1290 C C   . VAL C 1 15  ? 103.162 145.538 96.251  1.00 26.21  ?  7   VAL A C   1 
ATOM 1291 O O   . VAL C 1 15  ? 103.424 145.610 97.457  1.00 30.94  ?  7   VAL A O   1 
ATOM 1292 C CB  . VAL C 1 15  ? 100.946 144.325 96.173  1.00 25.56  ?  7   VAL A CB  1 
ATOM 1293 C CG1 . VAL C 1 15  ? 100.410 145.739 96.301  1.00 24.48  ?  7   VAL A CG1 1 
ATOM 1294 C CG2 . VAL C 1 15  ? 100.094 143.526 95.210  1.00 25.36  ?  7   VAL A CG2 1 
ATOM 1295 N N   . LEU C 1 16  ? 103.531 146.478 95.381  1.00 24.46  ?  8   LEU A N   1 
ATOM 1296 C CA  . LEU C 1 16  ? 104.332 147.607 95.827  1.00 28.74  ?  8   LEU A CA  1 
ATOM 1297 C C   . LEU C 1 16  ? 104.162 148.785 94.880  1.00 31.40  ?  8   LEU A C   1 
ATOM 1298 O O   . LEU C 1 16  ? 103.727 148.634 93.735  1.00 38.14  ?  8   LEU A O   1 
ATOM 1299 C CB  . LEU C 1 16  ? 105.815 147.226 95.945  1.00 28.94  ?  8   LEU A CB  1 
ATOM 1300 C CG  . LEU C 1 16  ? 106.529 146.838 94.648  1.00 26.95  ?  8   LEU A CG  1 
ATOM 1301 C CD1 . LEU C 1 16  ? 107.463 147.948 94.189  1.00 26.80  ?  8   LEU A CD1 1 
ATOM 1302 C CD2 . LEU C 1 16  ? 107.283 145.530 94.824  1.00 25.59  ?  8   LEU A CD2 1 
ATOM 1303 N N   . LYS C 1 17  ? 104.508 149.969 95.382  1.00 30.63  ?  9   LYS A N   1 
ATOM 1304 C CA  . LYS C 1 17  ? 104.572 151.188 94.589  1.00 33.89  ?  9   LYS A CA  1 
ATOM 1305 C C   . LYS C 1 17  ? 105.842 151.946 94.945  1.00 35.38  ?  9   LYS A C   1 
ATOM 1306 O O   . LYS C 1 17  ? 106.228 152.010 96.114  1.00 37.54  ?  9   LYS A O   1 
ATOM 1307 C CB  . LYS C 1 17  ? 103.356 152.097 94.814  1.00 31.42  ?  9   LYS A CB  1 
ATOM 1308 C CG  . LYS C 1 17  ? 102.025 151.537 94.339  1.00 29.83  ?  9   LYS A CG  1 
ATOM 1309 C CD  . LYS C 1 17  ? 101.286 150.807 95.447  1.00 30.45  ?  9   LYS A CD  1 
ATOM 1310 C CE  . LYS C 1 17  ? 100.117 150.012 94.890  1.00 30.67  ?  9   LYS A CE  1 
ATOM 1311 N NZ  . LYS C 1 17  ? 99.761  148.864 95.762  1.00 32.46  1  9   LYS A NZ  1 
ATOM 1312 N N   . GLY C 1 18  ? 106.488 152.517 93.932  1.00 35.35  ?  10  GLY A N   1 
ATOM 1313 C CA  . GLY C 1 18  ? 107.676 153.314 94.160  1.00 41.06  ?  10  GLY A CA  1 
ATOM 1314 C C   . GLY C 1 18  ? 108.903 152.797 93.441  1.00 47.17  ?  10  GLY A C   1 
ATOM 1315 O O   . GLY C 1 18  ? 108.836 152.431 92.263  1.00 48.28  ?  10  GLY A O   1 
ATOM 1316 N N   . ASP C 1 19  ? 110.034 152.760 94.141  1.00 48.64  ?  11  ASP A N   1 
ATOM 1317 C CA  . ASP C 1 19  ? 111.293 152.310 93.565  1.00 48.52  ?  11  ASP A CA  1 
ATOM 1318 C C   . ASP C 1 19  ? 111.935 151.319 94.531  1.00 46.49  ?  11  ASP A C   1 
ATOM 1319 O O   . ASP C 1 19  ? 111.330 150.907 95.526  1.00 49.98  ?  11  ASP A O   1 
ATOM 1320 C CB  . ASP C 1 19  ? 112.205 153.506 93.258  1.00 48.64  ?  11  ASP A CB  1 
ATOM 1321 C CG  . ASP C 1 19  ? 112.858 154.077 94.498  1.00 50.33  ?  11  ASP A CG  1 
ATOM 1322 O OD1 . ASP C 1 19  ? 113.936 153.580 94.886  1.00 54.07  ?  11  ASP A OD1 1 
ATOM 1323 O OD2 . ASP C 1 19  ? 112.296 155.028 95.083  1.00 46.67  -1 11  ASP A OD2 1 
ATOM 1324 N N   . GLY C 1 20  ? 113.173 150.933 94.232  1.00 40.40  ?  12  GLY A N   1 
ATOM 1325 C CA  . GLY C 1 20  ? 113.885 149.968 95.031  1.00 35.56  ?  12  GLY A CA  1 
ATOM 1326 C C   . GLY C 1 20  ? 113.844 148.587 94.411  1.00 35.56  ?  12  GLY A C   1 
ATOM 1327 O O   . GLY C 1 20  ? 112.783 148.085 94.028  1.00 36.41  ?  12  GLY A O   1 
ATOM 1328 N N   . PRO C 1 21  ? 115.007 147.947 94.293  1.00 33.92  ?  13  PRO A N   1 
ATOM 1329 C CA  . PRO C 1 21  ? 115.051 146.618 93.672  1.00 30.41  ?  13  PRO A CA  1 
ATOM 1330 C C   . PRO C 1 21  ? 114.349 145.575 94.528  1.00 28.35  ?  13  PRO A C   1 
ATOM 1331 O O   . PRO C 1 21  ? 114.462 145.572 95.756  1.00 30.32  ?  13  PRO A O   1 
ATOM 1332 C CB  . PRO C 1 21  ? 116.552 146.332 93.554  1.00 28.15  ?  13  PRO A CB  1 
ATOM 1333 C CG  . PRO C 1 21  ? 117.174 147.154 94.630  1.00 27.72  ?  13  PRO A CG  1 
ATOM 1334 C CD  . PRO C 1 21  ? 116.336 148.398 94.739  1.00 30.27  ?  13  PRO A CD  1 
ATOM 1335 N N   . VAL C 1 22  ? 113.619 144.685 93.862  1.00 26.60  ?  14  VAL A N   1 
ATOM 1336 C CA  . VAL C 1 22  ? 112.921 143.581 94.510  1.00 24.81  ?  14  VAL A CA  1 
ATOM 1337 C C   . VAL C 1 22  ? 113.463 142.286 93.923  1.00 24.76  ?  14  VAL A C   1 
ATOM 1338 O O   . VAL C 1 22  ? 113.432 142.092 92.701  1.00 27.69  ?  14  VAL A O   1 
ATOM 1339 C CB  . VAL C 1 22  ? 111.399 143.675 94.323  1.00 24.47  ?  14  VAL A CB  1 
ATOM 1340 C CG1 . VAL C 1 22  ? 110.697 142.617 95.160  1.00 27.39  ?  14  VAL A CG1 1 
ATOM 1341 C CG2 . VAL C 1 22  ? 110.907 145.067 94.690  1.00 23.89  ?  14  VAL A CG2 1 
ATOM 1342 N N   . GLN C 1 23  ? 113.956 141.404 94.788  1.00 21.92  ?  15  GLN A N   1 
ATOM 1343 C CA  . GLN C 1 23  ? 114.604 140.174 94.351  1.00 22.66  ?  15  GLN A CA  1 
ATOM 1344 C C   . GLN C 1 23  ? 114.120 139.012 95.203  1.00 22.28  ?  15  GLN A C   1 
ATOM 1345 O O   . GLN C 1 23  ? 113.912 139.170 96.409  1.00 22.91  ?  15  GLN A O   1 
ATOM 1346 C CB  . GLN C 1 23  ? 116.130 140.297 94.441  1.00 24.25  ?  15  GLN A CB  1 
ATOM 1347 C CG  . GLN C 1 23  ? 116.614 141.164 95.591  1.00 22.14  ?  15  GLN A CG  1 
ATOM 1348 C CD  . GLN C 1 23  ? 117.928 141.857 95.287  1.00 17.91  ?  15  GLN A CD  1 
ATOM 1349 O OE1 . GLN C 1 23  ? 118.338 141.961 94.131  1.00 16.55  ?  15  GLN A OE1 1 
ATOM 1350 N NE2 . GLN C 1 23  ? 118.595 142.338 96.329  1.00 17.47  ?  15  GLN A NE2 1 
ATOM 1351 N N   . GLY C 1 24  ? 113.938 137.853 94.573  1.00 21.29  ?  16  GLY A N   1 
ATOM 1352 C CA  . GLY C 1 24  ? 113.570 136.652 95.295  1.00 22.93  ?  16  GLY A CA  1 
ATOM 1353 C C   . GLY C 1 24  ? 112.118 136.603 95.719  1.00 24.98  ?  16  GLY A C   1 
ATOM 1354 O O   . GLY C 1 24  ? 111.814 136.603 96.915  1.00 29.08  ?  16  GLY A O   1 
ATOM 1355 N N   . ILE C 1 25  ? 111.210 136.561 94.749  1.00 22.38  ?  17  ILE A N   1 
ATOM 1356 C CA  . ILE C 1 25  ? 109.779 136.455 95.005  1.00 23.61  ?  17  ILE A CA  1 
ATOM 1357 C C   . ILE C 1 25  ? 109.344 135.048 94.625  1.00 25.42  ?  17  ILE A C   1 
ATOM 1358 O O   . ILE C 1 25  ? 109.430 134.659 93.454  1.00 27.17  ?  17  ILE A O   1 
ATOM 1359 C CB  . ILE C 1 25  ? 108.980 137.509 94.225  1.00 24.33  ?  17  ILE A CB  1 
ATOM 1360 C CG1 . ILE C 1 25  ? 109.665 138.870 94.326  1.00 22.88  ?  17  ILE A CG1 1 
ATOM 1361 C CG2 . ILE C 1 25  ? 107.553 137.574 94.738  1.00 21.54  ?  17  ILE A CG2 1 
ATOM 1362 C CD1 . ILE C 1 25  ? 110.240 139.359 93.019  1.00 26.06  ?  17  ILE A CD1 1 
ATOM 1363 N N   . ILE C 1 26  ? 108.946 134.275 95.641  1.00 24.51  ?  18  ILE A N   1 
ATOM 1364 C CA  . ILE C 1 26  ? 108.595 132.847 95.383  1.00 24.36  ?  18  ILE A CA  1 
ATOM 1365 C C   . ILE C 1 26  ? 107.210 132.520 95.958  1.00 24.62  ?  18  ILE A C   1 
ATOM 1366 O O   . ILE C 1 26  ? 106.978 132.808 97.152  1.00 27.94  ?  18  ILE A O   1 
ATOM 1367 C CB  . ILE C 1 26  ? 109.687 131.903 95.921  1.00 24.43  ?  18  ILE A CB  1 
ATOM 1368 C CG1 . ILE C 1 26  ? 111.015 132.125 95.203  1.00 22.03  ?  18  ILE A CG1 1 
ATOM 1369 C CG2 . ILE C 1 26  ? 109.241 130.445 95.834  1.00 25.26  ?  18  ILE A CG2 1 
ATOM 1370 C CD1 . ILE C 1 26  ? 112.002 130.986 95.360  1.00 22.02  ?  18  ILE A CD1 1 
ATOM 1371 N N   . ASN C 1 27  ? 106.337 131.950 95.133  1.00 24.34  ?  19  ASN A N   1 
ATOM 1372 C CA  . ASN C 1 27  ? 104.988 131.546 95.518  1.00 28.83  ?  19  ASN A CA  1 
ATOM 1373 C C   . ASN C 1 27  ? 104.859 130.044 95.300  1.00 32.93  ?  19  ASN A C   1 
ATOM 1374 O O   . ASN C 1 27  ? 104.970 129.567 94.166  1.00 33.84  ?  19  ASN A O   1 
ATOM 1375 C CB  . ASN C 1 27  ? 103.937 132.312 94.716  1.00 29.86  ?  19  ASN A CB  1 
ATOM 1376 C CG  . ASN C 1 27  ? 102.528 131.830 94.992  1.00 29.12  ?  19  ASN A CG  1 
ATOM 1377 O OD1 . ASN C 1 27  ? 102.075 131.817 96.137  1.00 29.88  ?  19  ASN A OD1 1 
ATOM 1378 N ND2 . ASN C 1 27  ? 101.827 131.424 93.940  1.00 26.34  ?  19  ASN A ND2 1 
ATOM 1379 N N   . PHE C 1 28  ? 104.626 129.301 96.381  1.00 34.71  ?  20  PHE A N   1 
ATOM 1380 C CA  . PHE C 1 28  ? 104.460 127.853 96.327  1.00 38.96  ?  20  PHE A CA  1 
ATOM 1381 C C   . PHE C 1 28  ? 103.051 127.484 96.775  1.00 43.50  ?  20  PHE A C   1 
ATOM 1382 O O   . PHE C 1 28  ? 102.625 127.862 97.873  1.00 47.56  ?  20  PHE A O   1 
ATOM 1383 C CB  . PHE C 1 28  ? 105.493 127.144 97.203  1.00 44.73  ?  20  PHE A CB  1 
ATOM 1384 C CG  . PHE C 1 28  ? 106.707 126.673 96.453  1.00 43.10  ?  20  PHE A CG  1 
ATOM 1385 C CD1 . PHE C 1 28  ? 106.632 125.584 95.602  1.00 43.98  ?  20  PHE A CD1 1 
ATOM 1386 C CD2 . PHE C 1 28  ? 107.927 127.304 96.619  1.00 38.33  ?  20  PHE A CD2 1 
ATOM 1387 C CE1 . PHE C 1 28  ? 107.749 125.145 94.915  1.00 47.10  ?  20  PHE A CE1 1 
ATOM 1388 C CE2 . PHE C 1 28  ? 109.047 126.870 95.938  1.00 38.50  ?  20  PHE A CE2 1 
ATOM 1389 C CZ  . PHE C 1 28  ? 108.958 125.791 95.083  1.00 43.62  ?  20  PHE A CZ  1 
ATOM 1390 N N   . GLU C 1 29  ? 102.339 126.738 95.932  1.00 44.08  ?  21  GLU A N   1 
ATOM 1391 C CA  . GLU C 1 29  ? 101.001 126.245 96.246  1.00 49.54  ?  21  GLU A CA  1 
ATOM 1392 C C   . GLU C 1 29  ? 100.925 124.785 95.818  1.00 48.82  ?  21  GLU A C   1 
ATOM 1393 O O   . GLU C 1 29  ? 100.833 124.490 94.622  1.00 47.51  ?  21  GLU A O   1 
ATOM 1394 C CB  . GLU C 1 29  ? 99.926  127.081 95.551  1.00 53.29  ?  21  GLU A CB  1 
ATOM 1395 C CG  . GLU C 1 29  ? 98.522  126.508 95.659  1.00 60.45  ?  21  GLU A CG  1 
ATOM 1396 C CD  . GLU C 1 29  ? 97.476  127.418 95.048  1.00 65.14  ?  21  GLU A CD  1 
ATOM 1397 O OE1 . GLU C 1 29  ? 97.814  128.575 94.719  1.00 64.22  ?  21  GLU A OE1 1 
ATOM 1398 O OE2 . GLU C 1 29  ? 96.317  126.979 94.896  1.00 64.00  -1 21  GLU A OE2 1 
ATOM 1399 N N   . GLN C 1 30  ? 100.958 123.875 96.788  1.00 48.04  ?  22  GLN A N   1 
ATOM 1400 C CA  . GLN C 1 30  ? 100.987 122.444 96.524  1.00 50.83  ?  22  GLN A CA  1 
ATOM 1401 C C   . GLN C 1 30  ? 99.759  121.770 97.118  1.00 54.87  ?  22  GLN A C   1 
ATOM 1402 O O   . GLN C 1 30  ? 99.345  122.083 98.238  1.00 53.25  ?  22  GLN A O   1 
ATOM 1403 C CB  . GLN C 1 30  ? 102.254 121.799 97.097  1.00 49.29  ?  22  GLN A CB  1 
ATOM 1404 C CG  . GLN C 1 30  ? 103.498 121.998 96.250  1.00 48.84  ?  22  GLN A CG  1 
ATOM 1405 C CD  . GLN C 1 30  ? 104.767 122.024 97.077  1.00 49.90  ?  22  GLN A CD  1 
ATOM 1406 O OE1 . GLN C 1 30  ? 104.807 121.499 98.190  1.00 49.86  ?  22  GLN A OE1 1 
ATOM 1407 N NE2 . GLN C 1 30  ? 105.814 122.635 96.537  1.00 48.78  ?  22  GLN A NE2 1 
ATOM 1408 N N   . LYS C 1 31  ? 99.185  120.839 96.358  1.00 55.39  ?  23  LYS A N   1 
ATOM 1409 C CA  . LYS C 1 31  ? 98.067  120.014 96.805  1.00 53.82  ?  23  LYS A CA  1 
ATOM 1410 C C   . LYS C 1 31  ? 98.514  118.559 96.752  1.00 53.95  ?  23  LYS A C   1 
ATOM 1411 O O   . LYS C 1 31  ? 98.638  117.985 95.664  1.00 54.78  ?  23  LYS A O   1 
ATOM 1412 C CB  . LYS C 1 31  ? 96.831  120.244 95.935  1.00 53.83  ?  23  LYS A CB  1 
ATOM 1413 C CG  . LYS C 1 31  ? 96.004  121.456 96.338  1.00 52.24  ?  23  LYS A CG  1 
ATOM 1414 C CD  . LYS C 1 31  ? 94.569  121.346 95.839  1.00 55.54  ?  23  LYS A CD  1 
ATOM 1415 C CE  . LYS C 1 31  ? 93.992  119.960 96.079  1.00 57.07  ?  23  LYS A CE  1 
ATOM 1416 N NZ  . LYS C 1 31  ? 93.972  119.604 97.525  1.00 56.48  1  23  LYS A NZ  1 
ATOM 1417 N N   . GLU C 1 32  ? 98.754  117.969 97.922  1.00 53.98  ?  24  GLU A N   1 
ATOM 1418 C CA  . GLU C 1 32  ? 99.275  116.608 98.044  1.00 55.86  ?  24  GLU A CA  1 
ATOM 1419 C C   . GLU C 1 32  ? 100.591 116.465 97.276  1.00 58.44  ?  24  GLU A C   1 
ATOM 1420 O O   . GLU C 1 32  ? 100.716 115.695 96.323  1.00 62.27  ?  24  GLU A O   1 
ATOM 1421 C CB  . GLU C 1 32  ? 98.241  115.581 97.571  1.00 56.67  ?  24  GLU A CB  1 
ATOM 1422 C CG  . GLU C 1 32  ? 96.915  115.645 98.311  1.00 62.98  ?  24  GLU A CG  1 
ATOM 1423 C CD  . GLU C 1 32  ? 95.756  116.001 97.400  1.00 65.14  ?  24  GLU A CD  1 
ATOM 1424 O OE1 . GLU C 1 32  ? 95.758  117.118 96.842  1.00 63.46  ?  24  GLU A OE1 1 
ATOM 1425 O OE2 . GLU C 1 32  ? 94.844  115.163 97.240  1.00 66.01  -1 24  GLU A OE2 1 
ATOM 1426 N N   . SER C 1 33  ? 101.581 117.236 97.725  1.00 55.32  ?  25  SER A N   1 
ATOM 1427 C CA  . SER C 1 33  ? 102.855 117.329 97.020  1.00 56.02  ?  25  SER A CA  1 
ATOM 1428 C C   . SER C 1 33  ? 103.609 116.006 97.048  1.00 59.63  ?  25  SER A C   1 
ATOM 1429 O O   . SER C 1 33  ? 103.840 115.402 95.996  1.00 61.97  ?  25  SER A O   1 
ATOM 1430 C CB  . SER C 1 33  ? 103.721 118.438 97.622  1.00 57.72  ?  25  SER A CB  1 
ATOM 1431 O OG  . SER C 1 33  ? 104.155 118.096 98.926  1.00 60.40  ?  25  SER A OG  1 
ATOM 1432 N N   . ASN C 1 34  ? 103.983 115.546 98.243  1.00 59.77  ?  26  ASN A N   1 
ATOM 1433 C CA  . ASN C 1 34  ? 104.725 114.297 98.426  1.00 58.66  ?  26  ASN A CA  1 
ATOM 1434 C C   . ASN C 1 34  ? 106.010 114.292 97.593  1.00 59.61  ?  26  ASN A C   1 
ATOM 1435 O O   . ASN C 1 34  ? 106.256 113.401 96.777  1.00 59.31  ?  26  ASN A O   1 
ATOM 1436 C CB  . ASN C 1 34  ? 103.844 113.086 98.098  1.00 59.30  ?  26  ASN A CB  1 
ATOM 1437 C CG  . ASN C 1 34  ? 103.027 112.621 99.286  1.00 64.47  ?  26  ASN A CG  1 
ATOM 1438 O OD1 . ASN C 1 34  ? 101.859 112.984 99.432  1.00 69.26  ?  26  ASN A OD1 1 
ATOM 1439 N ND2 . ASN C 1 34  ? 103.636 111.809 100.142 1.00 61.99  ?  26  ASN A ND2 1 
ATOM 1440 N N   . GLY C 1 35  ? 106.834 115.311 97.820  1.00 58.45  ?  27  GLY A N   1 
ATOM 1441 C CA  . GLY C 1 35  ? 108.079 115.452 97.103  1.00 54.06  ?  27  GLY A CA  1 
ATOM 1442 C C   . GLY C 1 35  ? 109.001 116.480 97.726  1.00 56.87  ?  27  GLY A C   1 
ATOM 1443 O O   . GLY C 1 35  ? 108.590 117.304 98.548  1.00 55.15  ?  27  GLY A O   1 
ATOM 1444 N N   . PRO C 1 36  ? 110.277 116.447 97.341  1.00 60.77  ?  28  PRO A N   1 
ATOM 1445 C CA  . PRO C 1 36  ? 111.249 117.393 97.901  1.00 57.27  ?  28  PRO A CA  1 
ATOM 1446 C C   . PRO C 1 36  ? 111.352 118.685 97.106  1.00 52.53  ?  28  PRO A C   1 
ATOM 1447 O O   . PRO C 1 36  ? 111.273 118.708 95.876  1.00 53.35  ?  28  PRO A O   1 
ATOM 1448 C CB  . PRO C 1 36  ? 112.562 116.603 97.838  1.00 52.87  ?  28  PRO A CB  1 
ATOM 1449 C CG  . PRO C 1 36  ? 112.396 115.696 96.659  1.00 47.86  ?  28  PRO A CG  1 
ATOM 1450 C CD  . PRO C 1 36  ? 110.913 115.467 96.444  1.00 54.45  ?  28  PRO A CD  1 
ATOM 1451 N N   . VAL C 1 37  ? 111.530 119.780 97.842  1.00 48.48  ?  29  VAL A N   1 
ATOM 1452 C CA  . VAL C 1 37  ? 111.683 121.116 97.279  1.00 47.21  ?  29  VAL A CA  1 
ATOM 1453 C C   . VAL C 1 37  ? 112.892 121.791 97.914  1.00 46.15  ?  29  VAL A C   1 
ATOM 1454 O O   . VAL C 1 37  ? 113.070 121.746 99.136  1.00 49.39  ?  29  VAL A O   1 
ATOM 1455 C CB  . VAL C 1 37  ? 110.404 121.961 97.453  1.00 46.90  ?  29  VAL A CB  1 
ATOM 1456 C CG1 . VAL C 1 37  ? 109.978 121.999 98.877  1.00 44.83  ?  29  VAL A CG1 1 
ATOM 1457 C CG2 . VAL C 1 37  ? 110.656 123.388 96.983  1.00 44.88  ?  29  VAL A CG2 1 
ATOM 1458 N N   . LYS C 1 38  ? 113.726 122.404 97.076  1.00 44.07  ?  30  LYS A N   1 
ATOM 1459 C CA  . LYS C 1 38  ? 114.983 123.002 97.507  1.00 41.23  ?  30  LYS A CA  1 
ATOM 1460 C C   . LYS C 1 38  ? 115.114 124.388 96.897  1.00 38.56  ?  30  LYS A C   1 
ATOM 1461 O O   . LYS C 1 38  ? 115.198 124.527 95.673  1.00 38.56  ?  30  LYS A O   1 
ATOM 1462 C CB  . LYS C 1 38  ? 116.168 122.119 97.107  1.00 42.71  ?  30  LYS A CB  1 
ATOM 1463 C CG  . LYS C 1 38  ? 117.528 122.760 97.312  1.00 40.00  ?  30  LYS A CG  1 
ATOM 1464 C CD  . LYS C 1 38  ? 117.883 122.876 98.771  1.00 40.23  ?  30  LYS A CD  1 
ATOM 1465 C CE  . LYS C 1 38  ? 119.367 123.153 98.971  1.00 40.83  ?  30  LYS A CE  1 
ATOM 1466 N NZ  . LYS C 1 38  ? 120.224 122.059 98.436  1.00 39.78  1  30  LYS A NZ  1 
ATOM 1467 N N   . VAL C 1 39  ? 115.125 125.406 97.753  1.00 38.13  ?  31  VAL A N   1 
ATOM 1468 C CA  . VAL C 1 39  ? 115.393 126.786 97.364  1.00 40.08  ?  31  VAL A CA  1 
ATOM 1469 C C   . VAL C 1 39  ? 116.692 127.242 98.019  1.00 40.96  ?  31  VAL A C   1 
ATOM 1470 O O   . VAL C 1 39  ? 116.924 126.994 99.208  1.00 42.68  ?  31  VAL A O   1 
ATOM 1471 C CB  . VAL C 1 39  ? 114.201 127.713 97.686  1.00 39.42  ?  31  VAL A CB  1 
ATOM 1472 C CG1 . VAL C 1 39  ? 114.011 127.840 99.121  1.00 38.01  ?  31  VAL A CG1 1 
ATOM 1473 C CG2 . VAL C 1 39  ? 114.473 129.120 97.153  1.00 36.32  ?  31  VAL A CG2 1 
ATOM 1474 N N   . TRP C 1 40  ? 117.551 127.874 97.219  1.00 39.62  ?  32  TRP A N   1 
ATOM 1475 C CA  . TRP C 1 40  ? 118.932 128.150 97.581  1.00 41.94  ?  32  TRP A CA  1 
ATOM 1476 C C   . TRP C 1 40  ? 119.526 129.197 96.652  1.00 47.10  ?  32  TRP A C   1 
ATOM 1477 O O   . TRP C 1 40  ? 119.079 129.372 95.516  1.00 52.87  ?  32  TRP A O   1 
ATOM 1478 C CB  . TRP C 1 40  ? 119.740 126.842 97.608  1.00 43.21  ?  32  TRP A CB  1 
ATOM 1479 C CG  . TRP C 1 40  ? 121.021 126.921 98.371  1.00 46.40  ?  32  TRP A CG  1 
ATOM 1480 C CD1 . TRP C 1 40  ? 121.261 127.625 99.505  1.00 48.02  ?  32  TRP A CD1 1 
ATOM 1481 C CD2 . TRP C 1 40  ? 122.200 126.142 98.131  1.00 44.13  ?  32  TRP A CD2 1 
ATOM 1482 N NE1 . TRP C 1 40  ? 122.551 127.421 99.931  1.00 51.88  ?  32  TRP A NE1 1 
ATOM 1483 C CE2 . TRP C 1 40  ? 123.142 126.496 99.112  1.00 46.70  ?  32  TRP A CE2 1 
ATOM 1484 C CE3 . TRP C 1 40  ? 122.556 125.198 97.164  1.00 42.91  ?  32  TRP A CE3 1 
ATOM 1485 C CZ2 . TRP C 1 40  ? 124.419 125.945 99.151  1.00 49.52  ?  32  TRP A CZ2 1 
ATOM 1486 C CZ3 . TRP C 1 40  ? 123.823 124.653 97.202  1.00 43.59  ?  32  TRP A CZ3 1 
ATOM 1487 C CH2 . TRP C 1 40  ? 124.740 125.027 98.190  1.00 48.13  ?  32  TRP A CH2 1 
ATOM 1488 N N   . GLY C 1 41  ? 120.522 129.899 97.163  1.00 43.38  ?  33  GLY A N   1 
ATOM 1489 C CA  . GLY C 1 41  ? 121.142 131.022 96.485  1.00 41.37  ?  33  GLY A CA  1 
ATOM 1490 C C   . GLY C 1 41  ? 121.309 132.177 97.454  1.00 42.12  ?  33  GLY A C   1 
ATOM 1491 O O   . GLY C 1 41  ? 120.570 132.324 98.428  1.00 41.68  ?  33  GLY A O   1 
ATOM 1492 N N   . SER C 1 42  ? 122.296 133.023 97.173  1.00 41.19  ?  34  SER A N   1 
ATOM 1493 C CA  . SER C 1 42  ? 122.640 134.140 98.041  1.00 37.65  ?  34  SER A CA  1 
ATOM 1494 C C   . SER C 1 42  ? 122.270 135.466 97.388  1.00 34.43  ?  34  SER A C   1 
ATOM 1495 O O   . SER C 1 42  ? 122.406 135.642 96.174  1.00 35.63  ?  34  SER A O   1 
ATOM 1496 C CB  . SER C 1 42  ? 124.131 134.131 98.387  1.00 39.91  ?  34  SER A CB  1 
ATOM 1497 O OG  . SER C 1 42  ? 124.439 133.072 99.276  1.00 45.22  ?  34  SER A OG  1 
ATOM 1498 N N   . ILE C 1 43  ? 121.805 136.402 98.215  1.00 31.84  ?  35  ILE A N   1 
ATOM 1499 C CA  . ILE C 1 43  ? 121.321 137.700 97.760  1.00 31.37  ?  35  ILE A CA  1 
ATOM 1500 C C   . ILE C 1 43  ? 122.142 138.800 98.419  1.00 29.80  ?  35  ILE A C   1 
ATOM 1501 O O   . ILE C 1 43  ? 122.459 138.723 99.611  1.00 30.62  ?  35  ILE A O   1 
ATOM 1502 C CB  . ILE C 1 43  ? 119.822 137.894 98.071  1.00 29.17  ?  35  ILE A CB  1 
ATOM 1503 C CG1 . ILE C 1 43  ? 119.042 136.607 97.800  1.00 29.56  ?  35  ILE A CG1 1 
ATOM 1504 C CG2 . ILE C 1 43  ? 119.255 139.035 97.246  1.00 27.12  ?  35  ILE A CG2 1 
ATOM 1505 C CD1 . ILE C 1 43  ? 117.559 136.735 98.061  1.00 28.44  ?  35  ILE A CD1 1 
ATOM 1506 N N   . LYS C 1 44  ? 122.483 139.826 97.640  1.00 27.94  ?  36  LYS A N   1 
ATOM 1507 C CA  . LYS C 1 44  ? 123.196 140.996 98.140  1.00 28.09  ?  36  LYS A CA  1 
ATOM 1508 C C   . LYS C 1 44  ? 122.467 142.248 97.676  1.00 29.75  ?  36  LYS A C   1 
ATOM 1509 O O   . LYS C 1 44  ? 122.191 142.399 96.480  1.00 30.05  ?  36  LYS A O   1 
ATOM 1510 C CB  . LYS C 1 44  ? 124.650 141.007 97.659  1.00 31.37  ?  36  LYS A CB  1 
ATOM 1511 C CG  . LYS C 1 44  ? 125.409 142.285 97.997  1.00 32.18  ?  36  LYS A CG  1 
ATOM 1512 C CD  . LYS C 1 44  ? 125.744 143.093 96.752  1.00 31.06  ?  36  LYS A CD  1 
ATOM 1513 C CE  . LYS C 1 44  ? 126.877 144.073 97.018  1.00 29.17  ?  36  LYS A CE  1 
ATOM 1514 N NZ  . LYS C 1 44  ? 128.195 143.388 97.146  1.00 28.74  1  36  LYS A NZ  1 
ATOM 1515 N N   . GLY C 1 45  ? 122.164 143.140 98.609  1.00 31.51  ?  37  GLY A N   1 
ATOM 1516 C CA  . GLY C 1 45  ? 121.471 144.371 98.288  1.00 33.19  ?  37  GLY A CA  1 
ATOM 1517 C C   . GLY C 1 45  ? 122.150 145.570 98.914  1.00 38.65  ?  37  GLY A C   1 
ATOM 1518 O O   . GLY C 1 45  ? 122.734 145.488 99.995  1.00 43.33  ?  37  GLY A O   1 
ATOM 1519 N N   . LEU C 1 46  ? 122.063 146.699 98.213  1.00 40.57  ?  38  LEU A N   1 
ATOM 1520 C CA  . LEU C 1 46  ? 122.679 147.934 98.676  1.00 49.70  ?  38  LEU A CA  1 
ATOM 1521 C C   . LEU C 1 46  ? 121.899 149.120 98.128  1.00 49.34  ?  38  LEU A C   1 
ATOM 1522 O O   . LEU C 1 46  ? 121.466 149.107 96.972  1.00 49.78  ?  38  LEU A O   1 
ATOM 1523 C CB  . LEU C 1 46  ? 124.158 148.002 98.257  1.00 50.64  ?  38  LEU A CB  1 
ATOM 1524 C CG  . LEU C 1 46  ? 124.964 149.308 98.279  1.00 50.83  ?  38  LEU A CG  1 
ATOM 1525 C CD1 . LEU C 1 46  ? 126.441 148.982 98.419  1.00 50.18  ?  38  LEU A CD1 1 
ATOM 1526 C CD2 . LEU C 1 46  ? 124.753 150.152 97.026  1.00 53.75  ?  38  LEU A CD2 1 
ATOM 1527 N N   . THR C 1 47  ? 121.724 150.140 98.966  1.00 51.59  ?  39  THR A N   1 
ATOM 1528 C CA  . THR C 1 47  ? 121.107 151.397 98.565  1.00 60.01  ?  39  THR A CA  1 
ATOM 1529 C C   . THR C 1 47  ? 121.965 152.551 99.061  1.00 68.73  ?  39  THR A C   1 
ATOM 1530 O O   . THR C 1 47  ? 122.381 152.565 100.224 1.00 74.58  ?  39  THR A O   1 
ATOM 1531 C CB  . THR C 1 47  ? 119.672 151.517 99.100  1.00 60.26  ?  39  THR A CB  1 
ATOM 1532 O OG1 . THR C 1 47  ? 119.208 152.865 98.944  1.00 59.95  ?  39  THR A OG1 1 
ATOM 1533 C CG2 . THR C 1 47  ? 119.593 151.107 100.556 1.00 63.57  ?  39  THR A CG2 1 
ATOM 1534 N N   . GLU C 1 48  ? 122.237 153.508 98.176  1.00 69.61  ?  40  GLU A N   1 
ATOM 1535 C CA  . GLU C 1 48  ? 123.097 154.640 98.490  1.00 73.72  ?  40  GLU A CA  1 
ATOM 1536 C C   . GLU C 1 48  ? 122.451 155.912 97.957  1.00 81.48  ?  40  GLU A C   1 
ATOM 1537 O O   . GLU C 1 48  ? 121.393 155.878 97.318  1.00 86.68  ?  40  GLU A O   1 
ATOM 1538 C CB  . GLU C 1 48  ? 124.502 154.442 97.909  1.00 73.85  ?  40  GLU A CB  1 
ATOM 1539 C CG  . GLU C 1 48  ? 125.627 154.863 98.840  1.00 79.73  ?  40  GLU A CG  1 
ATOM 1540 C CD  . GLU C 1 48  ? 126.969 154.293 98.424  1.00 83.99  ?  40  GLU A CD  1 
ATOM 1541 O OE1 . GLU C 1 48  ? 127.030 153.616 97.376  1.00 80.86  ?  40  GLU A OE1 1 
ATOM 1542 O OE2 . GLU C 1 48  ? 127.964 154.522 99.144  1.00 88.46  -1 40  GLU A OE2 1 
ATOM 1543 N N   . GLY C 1 49  ? 123.097 157.045 98.220  1.00 82.55  ?  41  GLY A N   1 
ATOM 1544 C CA  . GLY C 1 49  ? 122.586 158.326 97.775  1.00 86.07  ?  41  GLY A CA  1 
ATOM 1545 C C   . GLY C 1 49  ? 121.328 158.743 98.506  1.00 92.08  ?  41  GLY A C   1 
ATOM 1546 O O   . GLY C 1 49  ? 121.378 159.100 99.688  1.00 94.69  ?  41  GLY A O   1 
ATOM 1547 N N   . LEU C 1 50  ? 120.192 158.706 97.804  1.00 96.07  ?  42  LEU A N   1 
ATOM 1548 C CA  . LEU C 1 50  ? 118.885 159.021 98.383  1.00 101.18 ?  42  LEU A CA  1 
ATOM 1549 C C   . LEU C 1 50  ? 118.854 160.439 98.949  1.00 107.80 ?  42  LEU A C   1 
ATOM 1550 O O   . LEU C 1 50  ? 118.245 160.700 99.989  1.00 110.50 ?  42  LEU A O   1 
ATOM 1551 C CB  . LEU C 1 50  ? 118.499 157.997 99.452  1.00 98.30  ?  42  LEU A CB  1 
ATOM 1552 C CG  . LEU C 1 50  ? 117.411 156.985 99.084  1.00 97.12  ?  42  LEU A CG  1 
ATOM 1553 C CD1 . LEU C 1 50  ? 117.406 155.832 100.074 1.00 96.01  ?  42  LEU A CD1 1 
ATOM 1554 C CD2 . LEU C 1 50  ? 116.046 157.648 99.019  1.00 103.05 ?  42  LEU A CD2 1 
ATOM 1555 N N   . HIS C 1 51  ? 119.516 161.363 98.259  1.00 108.75 ?  43  HIS A N   1 
ATOM 1556 C CA  . HIS C 1 51  ? 119.581 162.742 98.722  1.00 111.41 ?  43  HIS A CA  1 
ATOM 1557 C C   . HIS C 1 51  ? 118.266 163.463 98.456  1.00 113.81 ?  43  HIS A C   1 
ATOM 1558 O O   . HIS C 1 51  ? 117.655 163.308 97.395  1.00 112.58 ?  43  HIS A O   1 
ATOM 1559 C CB  . HIS C 1 51  ? 120.732 163.477 98.034  1.00 112.44 ?  43  HIS A CB  1 
ATOM 1560 C CG  . HIS C 1 51  ? 120.760 164.949 98.306  1.00 116.99 ?  43  HIS A CG  1 
ATOM 1561 N ND1 . HIS C 1 51  ? 120.030 165.857 97.568  1.00 117.69 ?  43  HIS A ND1 1 
ATOM 1562 C CD2 . HIS C 1 51  ? 121.435 165.673 99.229  1.00 118.15 ?  43  HIS A CD2 1 
ATOM 1563 C CE1 . HIS C 1 51  ? 120.252 167.075 98.029  1.00 116.72 ?  43  HIS A CE1 1 
ATOM 1564 N NE2 . HIS C 1 51  ? 121.100 166.991 99.037  1.00 118.74 ?  43  HIS A NE2 1 
ATOM 1565 N N   . GLY C 1 52  ? 117.831 164.258 99.432  1.00 116.05 ?  44  GLY A N   1 
ATOM 1566 C CA  . GLY C 1 52  ? 116.633 165.060 99.265  1.00 117.65 ?  44  GLY A CA  1 
ATOM 1567 C C   . GLY C 1 52  ? 115.345 164.277 99.212  1.00 118.87 ?  44  GLY A C   1 
ATOM 1568 O O   . GLY C 1 52  ? 114.356 164.765 98.658  1.00 118.82 ?  44  GLY A O   1 
ATOM 1569 N N   . PHE C 1 53  ? 115.320 163.073 99.772  1.00 116.85 ?  45  PHE A N   1 
ATOM 1570 C CA  . PHE C 1 53  ? 114.119 162.249 99.755  1.00 115.25 ?  45  PHE A CA  1 
ATOM 1571 C C   . PHE C 1 53  ? 113.169 162.742 100.844 1.00 116.82 ?  45  PHE A C   1 
ATOM 1572 O O   . PHE C 1 53  ? 112.130 163.334 100.554 1.00 113.10 ?  45  PHE A O   1 
ATOM 1573 C CB  . PHE C 1 53  ? 114.477 160.771 99.959  1.00 112.45 ?  45  PHE A CB  1 
ATOM 1574 C CG  . PHE C 1 53  ? 113.309 159.891 100.331 1.00 117.95 ?  45  PHE A CG  1 
ATOM 1575 C CD1 . PHE C 1 53  ? 112.064 160.063 99.740  1.00 118.95 ?  45  PHE A CD1 1 
ATOM 1576 C CD2 . PHE C 1 53  ? 113.461 158.887 101.273 1.00 117.85 ?  45  PHE A CD2 1 
ATOM 1577 C CE1 . PHE C 1 53  ? 110.998 159.253 100.085 1.00 115.98 ?  45  PHE A CE1 1 
ATOM 1578 C CE2 . PHE C 1 53  ? 112.398 158.074 101.621 1.00 117.16 ?  45  PHE A CE2 1 
ATOM 1579 C CZ  . PHE C 1 53  ? 111.166 158.258 101.026 1.00 116.13 ?  45  PHE A CZ  1 
ATOM 1580 N N   . VAL C 1 89  ? 135.266 154.746 101.370 1.00 104.10 ?  81  VAL A N   1 
ATOM 1581 C CA  . VAL C 1 89  ? 134.323 154.083 102.261 1.00 103.42 ?  81  VAL A CA  1 
ATOM 1582 C C   . VAL C 1 89  ? 133.993 152.688 101.740 1.00 102.49 ?  81  VAL A C   1 
ATOM 1583 O O   . VAL C 1 89  ? 133.163 151.981 102.313 1.00 100.27 ?  81  VAL A O   1 
ATOM 1584 C CB  . VAL C 1 89  ? 133.042 154.920 102.439 1.00 100.20 ?  81  VAL A CB  1 
ATOM 1585 C CG1 . VAL C 1 89  ? 133.395 156.374 102.712 1.00 94.61  ?  81  VAL A CG1 1 
ATOM 1586 C CG2 . VAL C 1 89  ? 132.154 154.805 101.211 1.00 99.35  ?  81  VAL A CG2 1 
ATOM 1587 N N   . GLY C 1 90  ? 134.653 152.301 100.650 1.00 104.32 ?  82  GLY A N   1 
ATOM 1588 C CA  . GLY C 1 90  ? 134.442 150.997 100.050 1.00 102.79 ?  82  GLY A CA  1 
ATOM 1589 C C   . GLY C 1 90  ? 134.741 149.848 100.990 1.00 99.38  ?  82  GLY A C   1 
ATOM 1590 O O   . GLY C 1 90  ? 135.786 149.830 101.648 1.00 98.08  ?  82  GLY A O   1 
ATOM 1591 N N   . ASP C 1 91  ? 133.830 148.882 101.061 1.00 97.40  ?  83  ASP A N   1 
ATOM 1592 C CA  . ASP C 1 91  ? 133.949 147.741 101.962 1.00 93.97  ?  83  ASP A CA  1 
ATOM 1593 C C   . ASP C 1 91  ? 134.195 146.485 101.134 1.00 86.96  ?  83  ASP A C   1 
ATOM 1594 O O   . ASP C 1 91  ? 133.338 146.077 100.343 1.00 87.12  ?  83  ASP A O   1 
ATOM 1595 C CB  . ASP C 1 91  ? 132.695 147.597 102.823 1.00 98.51  ?  83  ASP A CB  1 
ATOM 1596 C CG  . ASP C 1 91  ? 131.416 147.700 102.014 1.00 101.66 ?  83  ASP A CG  1 
ATOM 1597 O OD1 . ASP C 1 91  ? 131.082 148.817 101.567 1.00 103.27 ?  83  ASP A OD1 1 
ATOM 1598 O OD2 . ASP C 1 91  ? 130.745 146.664 101.825 1.00 99.30  -1 83  ASP A OD2 1 
ATOM 1599 N N   . LEU C 1 92  ? 135.363 145.876 101.317 1.00 83.64  ?  84  LEU A N   1 
ATOM 1600 C CA  . LEU C 1 92  ? 135.680 144.619 100.654 1.00 83.25  ?  84  LEU A CA  1 
ATOM 1601 C C   . LEU C 1 92  ? 134.954 143.487 101.371 1.00 83.87  ?  84  LEU A C   1 
ATOM 1602 O O   . LEU C 1 92  ? 135.155 143.275 102.571 1.00 86.74  ?  84  LEU A O   1 
ATOM 1603 C CB  . LEU C 1 92  ? 137.189 144.385 100.645 1.00 82.44  ?  84  LEU A CB  1 
ATOM 1604 C CG  . LEU C 1 92  ? 137.696 142.949 100.473 1.00 83.01  ?  84  LEU A CG  1 
ATOM 1605 C CD1 . LEU C 1 92  ? 137.284 142.376 99.126  1.00 83.81  ?  84  LEU A CD1 1 
ATOM 1606 C CD2 . LEU C 1 92  ? 139.207 142.892 100.644 1.00 79.77  ?  84  LEU A CD2 1 
ATOM 1607 N N   . GLY C 1 93  ? 134.106 142.763 100.639 1.00 78.35  ?  85  GLY A N   1 
ATOM 1608 C CA  . GLY C 1 93  ? 133.308 141.714 101.238 1.00 71.14  ?  85  GLY A CA  1 
ATOM 1609 C C   . GLY C 1 93  ? 133.005 140.612 100.248 1.00 66.38  ?  85  GLY A C   1 
ATOM 1610 O O   . GLY C 1 93  ? 133.352 140.692 99.068  1.00 67.07  ?  85  GLY A O   1 
ATOM 1611 N N   . ASN C 1 94  ? 132.355 139.565 100.755 1.00 62.95  ?  86  ASN A N   1 
ATOM 1612 C CA  . ASN C 1 94  ? 131.939 138.439 99.928  1.00 57.34  ?  86  ASN A CA  1 
ATOM 1613 C C   . ASN C 1 94  ? 130.986 137.549 100.714 1.00 53.91  ?  86  ASN A C   1 
ATOM 1614 O O   . ASN C 1 94  ? 131.255 137.217 101.872 1.00 55.84  ?  86  ASN A O   1 
ATOM 1615 C CB  . ASN C 1 94  ? 133.147 137.622 99.457  1.00 57.30  ?  86  ASN A CB  1 
ATOM 1616 C CG  . ASN C 1 94  ? 134.125 137.324 100.578 1.00 54.05  ?  86  ASN A CG  1 
ATOM 1617 O OD1 . ASN C 1 94  ? 134.605 138.231 101.258 1.00 55.15  ?  86  ASN A OD1 1 
ATOM 1618 N ND2 . ASN C 1 94  ? 134.424 136.045 100.777 1.00 51.29  ?  86  ASN A ND2 1 
ATOM 1619 N N   . VAL C 1 95  ? 129.879 137.157 100.090 1.00 53.01  ?  87  VAL A N   1 
ATOM 1620 C CA  . VAL C 1 95  ? 128.960 136.195 100.684 1.00 52.38  ?  87  VAL A CA  1 
ATOM 1621 C C   . VAL C 1 95  ? 129.301 134.820 100.126 1.00 58.67  ?  87  VAL A C   1 
ATOM 1622 O O   . VAL C 1 95  ? 129.653 134.674 98.949  1.00 62.80  ?  87  VAL A O   1 
ATOM 1623 C CB  . VAL C 1 95  ? 127.480 136.567 100.439 1.00 47.00  ?  87  VAL A CB  1 
ATOM 1624 C CG1 . VAL C 1 95  ? 127.242 138.042 100.750 1.00 41.34  ?  87  VAL A CG1 1 
ATOM 1625 C CG2 . VAL C 1 95  ? 127.043 136.234 99.036  1.00 46.98  ?  87  VAL A CG2 1 
ATOM 1626 N N   . THR C 1 96  ? 129.236 133.809 100.990 1.00 60.00  ?  88  THR A N   1 
ATOM 1627 C CA  . THR C 1 96  ? 129.794 132.500 100.686 1.00 64.49  ?  88  THR A CA  1 
ATOM 1628 C C   . THR C 1 96  ? 128.841 131.408 101.150 1.00 68.43  ?  88  THR A C   1 
ATOM 1629 O O   . THR C 1 96  ? 128.487 131.350 102.331 1.00 69.23  ?  88  THR A O   1 
ATOM 1630 C CB  . THR C 1 96  ? 131.164 132.338 101.356 1.00 68.10  ?  88  THR A CB  1 
ATOM 1631 O OG1 . THR C 1 96  ? 131.993 133.458 101.022 1.00 63.64  ?  88  THR A OG1 1 
ATOM 1632 C CG2 . THR C 1 96  ? 131.843 131.080 100.881 1.00 70.67  ?  88  THR A CG2 1 
ATOM 1633 N N   . ALA C 1 97  ? 128.425 130.546 100.217 1.00 70.62  ?  89  ALA A N   1 
ATOM 1634 C CA  . ALA C 1 97  ? 127.478 129.467 100.500 1.00 69.18  ?  89  ALA A CA  1 
ATOM 1635 C C   . ALA C 1 97  ? 127.858 128.208 99.711  1.00 73.53  ?  89  ALA A C   1 
ATOM 1636 O O   . ALA C 1 97  ? 127.023 127.580 99.063  1.00 71.42  ?  89  ALA A O   1 
ATOM 1637 C CB  . ALA C 1 97  ? 126.048 129.907 100.191 1.00 55.21  ?  89  ALA A CB  1 
ATOM 1638 N N   . ASP C 1 98  ? 129.136 127.840 99.754  1.00 75.25  ?  90  ASP A N   1 
ATOM 1639 C CA  . ASP C 1 98  ? 129.633 126.653 99.070  1.00 77.12  ?  90  ASP A CA  1 
ATOM 1640 C C   . ASP C 1 98  ? 129.622 125.424 99.975  1.00 76.53  ?  90  ASP A C   1 
ATOM 1641 O O   . ASP C 1 98  ? 128.964 125.386 101.020 1.00 74.45  ?  90  ASP A O   1 
ATOM 1642 C CB  . ASP C 1 98  ? 131.035 126.878 98.496  1.00 82.61  ?  90  ASP A CB  1 
ATOM 1643 C CG  . ASP C 1 98  ? 131.233 128.278 97.977  1.00 83.75  ?  90  ASP A CG  1 
ATOM 1644 O OD1 . ASP C 1 98  ? 132.032 129.029 98.568  1.00 82.56  ?  90  ASP A OD1 1 
ATOM 1645 O OD2 . ASP C 1 98  ? 130.581 128.622 96.970  1.00 82.26  -1 90  ASP A OD2 1 
ATOM 1646 N N   . LYS C 1 99  ? 130.245 124.357 99.465  1.00 79.82  ?  91  LYS A N   1 
ATOM 1647 C CA  . LYS C 1 99  ? 130.241 123.075 100.212 1.00 79.00  ?  91  LYS A CA  1 
ATOM 1648 C C   . LYS C 1 99  ? 131.378 122.178 99.708  1.00 83.57  ?  91  LYS A C   1 
ATOM 1649 O O   . LYS C 1 99  ? 131.837 122.390 98.565  1.00 89.29  ?  91  LYS A O   1 
ATOM 1650 C CB  . LYS C 1 99  ? 128.881 122.389 100.049 1.00 75.53  ?  91  LYS A CB  1 
ATOM 1651 C CG  . LYS C 1 99  ? 128.574 121.306 101.074 1.00 80.00  ?  91  LYS A CG  1 
ATOM 1652 C CD  . LYS C 1 99  ? 127.108 120.892 101.079 1.00 79.46  ?  91  LYS A CD  1 
ATOM 1653 C CE  . LYS C 1 99  ? 126.640 120.457 99.727  1.00 84.72  ?  91  LYS A CE  1 
ATOM 1654 N NZ  . LYS C 1 99  ? 125.215 120.117 99.732  1.00 97.74  1  91  LYS A NZ  1 
ATOM 1655 N N   . ASP C 1 100 ? 131.799 121.244 100.564 1.00 81.87  ?  92  ASP A N   1 
ATOM 1656 C CA  . ASP C 1 100 ? 132.885 120.304 100.193 1.00 83.84  ?  92  ASP A CA  1 
ATOM 1657 C C   . ASP C 1 100 ? 132.706 119.006 100.978 1.00 85.39  ?  92  ASP A C   1 
ATOM 1658 O O   . ASP C 1 100 ? 131.879 118.984 101.914 1.00 89.15  ?  92  ASP A O   1 
ATOM 1659 C CB  . ASP C 1 100 ? 134.258 120.929 100.394 1.00 86.42  ?  92  ASP A CB  1 
ATOM 1660 C CG  . ASP C 1 100 ? 134.750 121.022 101.831 1.00 91.06  ?  92  ASP A CG  1 
ATOM 1661 O OD1 . ASP C 1 100 ? 135.047 119.963 102.421 1.00 88.87  ?  92  ASP A OD1 1 
ATOM 1662 O OD2 . ASP C 1 100 ? 134.829 122.155 102.350 1.00 93.76  -1 92  ASP A OD2 1 
ATOM 1663 N N   . GLY C 1 101 ? 133.455 117.974 100.610 1.00 79.29  ?  93  GLY A N   1 
ATOM 1664 C CA  . GLY C 1 101 ? 133.414 116.680 101.263 1.00 71.84  ?  93  GLY A CA  1 
ATOM 1665 C C   . GLY C 1 101 ? 133.430 115.555 100.246 1.00 69.42  ?  93  GLY A C   1 
ATOM 1666 O O   . GLY C 1 101 ? 132.757 115.605 99.213  1.00 69.13  ?  93  GLY A O   1 
ATOM 1667 N N   . VAL C 1 102 ? 134.201 114.512 100.544 1.00 68.71  ?  94  VAL A N   1 
ATOM 1668 C CA  . VAL C 1 102 ? 134.422 113.427 99.595  1.00 67.28  ?  94  VAL A CA  1 
ATOM 1669 C C   . VAL C 1 102 ? 133.767 112.165 100.141 1.00 68.78  ?  94  VAL A C   1 
ATOM 1670 O O   . VAL C 1 102 ? 133.807 111.900 101.348 1.00 71.47  ?  94  VAL A O   1 
ATOM 1671 C CB  . VAL C 1 102 ? 135.925 113.208 99.320  1.00 66.89  ?  94  VAL A CB  1 
ATOM 1672 C CG1 . VAL C 1 102 ? 136.543 114.477 98.744  1.00 71.34  ?  94  VAL A CG1 1 
ATOM 1673 C CG2 . VAL C 1 102 ? 136.663 112.740 100.555 1.00 66.12  ?  94  VAL A CG2 1 
ATOM 1674 N N   . ALA C 1 103 ? 133.131 111.403 99.253  1.00 68.23  ?  95  ALA A N   1 
ATOM 1675 C CA  . ALA C 1 103 ? 132.423 110.193 99.643  1.00 68.77  ?  95  ALA A CA  1 
ATOM 1676 C C   . ALA C 1 103 ? 132.484 109.192 98.500  1.00 72.34  ?  95  ALA A C   1 
ATOM 1677 O O   . ALA C 1 103 ? 133.271 109.353 97.566  1.00 73.15  ?  95  ALA A O   1 
ATOM 1678 C CB  . ALA C 1 103 ? 130.964 110.487 100.014 1.00 67.48  ?  95  ALA A CB  1 
ATOM 1679 N N   . ASP C 1 104 ? 131.668 108.140 98.601  1.00 72.34  ?  96  ASP A N   1 
ATOM 1680 C CA  . ASP C 1 104 ? 131.474 107.249 97.462  1.00 70.64  ?  96  ASP A CA  1 
ATOM 1681 C C   . ASP C 1 104 ? 129.993 107.067 97.145  1.00 70.01  ?  96  ASP A C   1 
ATOM 1682 O O   . ASP C 1 104 ? 129.612 106.988 95.974  1.00 71.59  ?  96  ASP A O   1 
ATOM 1683 C CB  . ASP C 1 104 ? 132.161 105.899 97.702  1.00 68.86  ?  96  ASP A CB  1 
ATOM 1684 C CG  . ASP C 1 104 ? 131.731 105.228 98.997  1.00 69.61  ?  96  ASP A CG  1 
ATOM 1685 O OD1 . ASP C 1 104 ? 132.589 104.587 99.638  1.00 70.65  ?  96  ASP A OD1 1 
ATOM 1686 O OD2 . ASP C 1 104 ? 130.542 105.309 99.363  1.00 71.40  -1 96  ASP A OD2 1 
ATOM 1687 N N   . VAL C 1 105 ? 129.143 107.010 98.167  1.00 64.12  ?  97  VAL A N   1 
ATOM 1688 C CA  . VAL C 1 105 ? 127.695 106.954 97.985  1.00 60.56  ?  97  VAL A CA  1 
ATOM 1689 C C   . VAL C 1 105 ? 127.107 108.235 98.562  1.00 61.90  ?  97  VAL A C   1 
ATOM 1690 O O   . VAL C 1 105 ? 127.182 108.468 99.775  1.00 63.73  ?  97  VAL A O   1 
ATOM 1691 C CB  . VAL C 1 105 ? 127.071 105.716 98.651  1.00 59.54  ?  97  VAL A CB  1 
ATOM 1692 C CG1 . VAL C 1 105 ? 125.565 105.891 98.804  1.00 61.30  ?  97  VAL A CG1 1 
ATOM 1693 C CG2 . VAL C 1 105 ? 127.384 104.466 97.847  1.00 59.51  ?  97  VAL A CG2 1 
ATOM 1694 N N   . SER C 1 106 ? 126.528 109.065 97.697  1.00 60.17  ?  98  SER A N   1 
ATOM 1695 C CA  . SER C 1 106 ? 125.969 110.349 98.101  1.00 58.65  ?  98  SER A CA  1 
ATOM 1696 C C   . SER C 1 106 ? 124.634 110.551 97.401  1.00 60.75  ?  98  SER A C   1 
ATOM 1697 O O   . SER C 1 106 ? 124.574 110.567 96.168  1.00 67.09  ?  98  SER A O   1 
ATOM 1698 C CB  . SER C 1 106 ? 126.926 111.498 97.771  1.00 62.75  ?  98  SER A CB  1 
ATOM 1699 O OG  . SER C 1 106 ? 126.363 112.750 98.121  1.00 65.82  ?  98  SER A OG  1 
ATOM 1700 N N   . ILE C 1 107 ? 123.573 110.704 98.188  1.00 56.92  ?  99  ILE A N   1 
ATOM 1701 C CA  . ILE C 1 107 ? 122.230 110.944 97.674  1.00 58.31  ?  99  ILE A CA  1 
ATOM 1702 C C   . ILE C 1 107 ? 121.681 112.190 98.353  1.00 59.95  ?  99  ILE A C   1 
ATOM 1703 O O   . ILE C 1 107 ? 121.686 112.283 99.586  1.00 63.35  ?  99  ILE A O   1 
ATOM 1704 C CB  . ILE C 1 107 ? 121.305 109.735 97.910  1.00 58.58  ?  99  ILE A CB  1 
ATOM 1705 C CG1 . ILE C 1 107 ? 121.565 108.654 96.859  1.00 56.46  ?  99  ILE A CG1 1 
ATOM 1706 C CG2 . ILE C 1 107 ? 119.844 110.159 97.883  1.00 57.79  ?  99  ILE A CG2 1 
ATOM 1707 C CD1 . ILE C 1 107 ? 121.239 107.254 97.328  1.00 51.99  ?  99  ILE A CD1 1 
ATOM 1708 N N   . GLU C 1 108 ? 121.215 113.148 97.554  1.00 57.62  ?  100 GLU A N   1 
ATOM 1709 C CA  . GLU C 1 108 ? 120.702 114.405 98.082  1.00 58.25  ?  100 GLU A CA  1 
ATOM 1710 C C   . GLU C 1 108 ? 119.454 114.815 97.317  1.00 62.05  ?  100 GLU A C   1 
ATOM 1711 O O   . GLU C 1 108 ? 119.443 114.788 96.083  1.00 62.23  ?  100 GLU A O   1 
ATOM 1712 C CB  . GLU C 1 108 ? 121.759 115.513 97.996  1.00 61.43  ?  100 GLU A CB  1 
ATOM 1713 C CG  . GLU C 1 108 ? 122.614 115.652 99.246  1.00 68.72  ?  100 GLU A CG  1 
ATOM 1714 C CD  . GLU C 1 108 ? 123.966 116.275 98.960  1.00 76.46  ?  100 GLU A CD  1 
ATOM 1715 O OE1 . GLU C 1 108 ? 124.003 117.441 98.514  1.00 76.22  ?  100 GLU A OE1 1 
ATOM 1716 O OE2 . GLU C 1 108 ? 124.993 115.599 99.182  1.00 76.18  -1 100 GLU A OE2 1 
ATOM 1717 N N   . ASP C 1 109 ? 118.411 115.197 98.058  1.00 63.82  ?  101 ASP A N   1 
ATOM 1718 C CA  . ASP C 1 109 ? 117.160 115.701 97.485  1.00 57.98  ?  101 ASP A CA  1 
ATOM 1719 C C   . ASP C 1 109 ? 116.552 114.708 96.496  1.00 55.19  ?  101 ASP A C   1 
ATOM 1720 O O   . ASP C 1 109 ? 115.991 115.093 95.469  1.00 56.07  ?  101 ASP A O   1 
ATOM 1721 C CB  . ASP C 1 109 ? 117.366 117.065 96.821  1.00 61.33  ?  101 ASP A CB  1 
ATOM 1722 C CG  . ASP C 1 109 ? 118.384 117.922 97.549  1.00 64.04  ?  101 ASP A CG  1 
ATOM 1723 O OD1 . ASP C 1 109 ? 118.180 118.202 98.748  1.00 65.84  ?  101 ASP A OD1 1 
ATOM 1724 O OD2 . ASP C 1 109 ? 119.389 118.316 96.921  1.00 62.09  -1 101 ASP A OD2 1 
ATOM 1725 N N   . SER C 1 110 ? 116.647 113.419 96.814  1.00 53.07  ?  102 SER A N   1 
ATOM 1726 C CA  . SER C 1 110 ? 116.186 112.361 95.927  1.00 50.43  ?  102 SER A CA  1 
ATOM 1727 C C   . SER C 1 110 ? 115.099 111.548 96.623  1.00 45.76  ?  102 SER A C   1 
ATOM 1728 O O   . SER C 1 110 ? 114.853 111.693 97.823  1.00 49.36  ?  102 SER A O   1 
ATOM 1729 C CB  . SER C 1 110 ? 117.350 111.461 95.492  1.00 56.20  ?  102 SER A CB  1 
ATOM 1730 O OG  . SER C 1 110 ? 118.083 112.053 94.434  1.00 66.02  ?  102 SER A OG  1 
ATOM 1731 N N   . VAL C 1 111 ? 114.442 110.687 95.851  1.00 42.69  ?  103 VAL A N   1 
ATOM 1732 C CA  . VAL C 1 111 ? 113.410 109.790 96.358  1.00 43.70  ?  103 VAL A CA  1 
ATOM 1733 C C   . VAL C 1 111 ? 113.768 108.376 95.924  1.00 43.90  ?  103 VAL A C   1 
ATOM 1734 O O   . VAL C 1 111 ? 113.802 108.083 94.723  1.00 46.53  ?  103 VAL A O   1 
ATOM 1735 C CB  . VAL C 1 111 ? 112.008 110.173 95.853  1.00 41.76  ?  103 VAL A CB  1 
ATOM 1736 C CG1 . VAL C 1 111 ? 110.978 109.164 96.336  1.00 41.31  ?  103 VAL A CG1 1 
ATOM 1737 C CG2 . VAL C 1 111 ? 111.642 111.577 96.311  1.00 39.91  ?  103 VAL A CG2 1 
ATOM 1738 N N   . ILE C 1 112 ? 114.032 107.504 96.895  1.00 41.15  ?  104 ILE A N   1 
ATOM 1739 C CA  . ILE C 1 112 ? 114.423 106.124 96.638  1.00 44.16  ?  104 ILE A CA  1 
ATOM 1740 C C   . ILE C 1 112 ? 113.426 105.203 97.325  1.00 47.34  ?  104 ILE A C   1 
ATOM 1741 O O   . ILE C 1 112 ? 112.992 105.472 98.451  1.00 47.97  ?  104 ILE A O   1 
ATOM 1742 C CB  . ILE C 1 112 ? 115.857 105.830 97.129  1.00 45.87  ?  104 ILE A CB  1 
ATOM 1743 C CG1 . ILE C 1 112 ? 116.752 107.062 96.971  1.00 46.46  ?  104 ILE A CG1 1 
ATOM 1744 C CG2 . ILE C 1 112 ? 116.444 104.647 96.377  1.00 42.68  ?  104 ILE A CG2 1 
ATOM 1745 C CD1 . ILE C 1 112 ? 117.104 107.398 95.552  1.00 43.99  ?  104 ILE A CD1 1 
ATOM 1746 N N   . SER C 1 113 ? 113.061 104.118 96.644  1.00 48.70  ?  105 SER A N   1 
ATOM 1747 C CA  . SER C 1 113 ? 112.135 103.128 97.190  1.00 50.12  ?  105 SER A CA  1 
ATOM 1748 C C   . SER C 1 113 ? 112.576 101.752 96.714  1.00 50.68  ?  105 SER A C   1 
ATOM 1749 O O   . SER C 1 113 ? 112.403 101.415 95.538  1.00 51.76  ?  105 SER A O   1 
ATOM 1750 C CB  . SER C 1 113 ? 110.696 103.419 96.764  1.00 51.75  ?  105 SER A CB  1 
ATOM 1751 O OG  . SER C 1 113 ? 110.566 103.395 95.353  1.00 56.08  ?  105 SER A OG  1 
ATOM 1752 N N   . LEU C 1 114 ? 113.143 100.958 97.622  1.00 51.90  ?  106 LEU A N   1 
ATOM 1753 C CA  . LEU C 1 114 ? 113.611 99.607  97.315  1.00 54.88  ?  106 LEU A CA  1 
ATOM 1754 C C   . LEU C 1 114 ? 112.912 98.646  98.272  1.00 58.03  ?  106 LEU A C   1 
ATOM 1755 O O   . LEU C 1 114 ? 113.396 98.408  99.382  1.00 59.34  ?  106 LEU A O   1 
ATOM 1756 C CB  . LEU C 1 114 ? 115.129 99.495  97.437  1.00 51.99  ?  106 LEU A CB  1 
ATOM 1757 C CG  . LEU C 1 114 ? 116.008 100.683 97.031  1.00 43.98  ?  106 LEU A CG  1 
ATOM 1758 C CD1 . LEU C 1 114 ? 117.478 100.334 97.202  1.00 38.32  ?  106 LEU A CD1 1 
ATOM 1759 C CD2 . LEU C 1 114 ? 115.730 101.121 95.607  1.00 46.48  ?  106 LEU A CD2 1 
ATOM 1760 N N   . SER C 1 115 ? 111.782 98.092  97.844  1.00 60.00  ?  107 SER A N   1 
ATOM 1761 C CA  . SER C 1 115 ? 111.000 97.179  98.665  1.00 57.45  ?  107 SER A CA  1 
ATOM 1762 C C   . SER C 1 115 ? 111.281 95.738  98.260  1.00 57.98  ?  107 SER A C   1 
ATOM 1763 O O   . SER C 1 115 ? 111.298 95.407  97.071  1.00 58.97  ?  107 SER A O   1 
ATOM 1764 C CB  . SER C 1 115 ? 109.505 97.475  98.538  1.00 61.13  ?  107 SER A CB  1 
ATOM 1765 O OG  . SER C 1 115 ? 108.741 96.590  99.339  1.00 66.11  ?  107 SER A OG  1 
ATOM 1766 N N   . GLY C 1 116 ? 111.499 94.889  99.252  1.00 56.34  ?  108 GLY A N   1 
ATOM 1767 C CA  . GLY C 1 116 ? 111.775 93.489  99.015  1.00 55.95  ?  108 GLY A CA  1 
ATOM 1768 C C   . GLY C 1 116 ? 112.676 92.937  100.102 1.00 54.04  ?  108 GLY A C   1 
ATOM 1769 O O   . GLY C 1 116 ? 112.714 93.451  101.215 1.00 55.80  ?  108 GLY A O   1 
ATOM 1770 N N   . ASP C 1 117 ? 113.387 91.869  99.725  1.00 53.28  ?  109 ASP A N   1 
ATOM 1771 C CA  . ASP C 1 117 ? 114.296 91.194  100.682 1.00 56.24  ?  109 ASP A CA  1 
ATOM 1772 C C   . ASP C 1 117 ? 115.738 91.626  100.421 1.00 54.97  ?  109 ASP A C   1 
ATOM 1773 O O   . ASP C 1 117 ? 116.098 91.812  99.238  1.00 58.57  ?  109 ASP A O   1 
ATOM 1774 C CB  . ASP C 1 117 ? 114.139 89.683  100.623 1.00 59.64  ?  109 ASP A CB  1 
ATOM 1775 C CG  . ASP C 1 117 ? 112.743 89.166  100.939 1.00 64.19  ?  109 ASP A CG  1 
ATOM 1776 O OD1 . ASP C 1 117 ? 111.800 89.542  100.211 1.00 64.97  ?  109 ASP A OD1 1 
ATOM 1777 O OD2 . ASP C 1 117 ? 112.610 88.398  101.915 1.00 65.83  -1 109 ASP A OD2 1 
ATOM 1778 N N   . HIS C 1 118 ? 116.516 91.777  101.483 1.00 54.12  ?  110 HIS A N   1 
ATOM 1779 C CA  . HIS C 1 118 ? 117.925 92.174  101.431 1.00 54.88  ?  110 HIS A CA  1 
ATOM 1780 C C   . HIS C 1 118 ? 118.084 93.540  100.755 1.00 53.17  ?  110 HIS A C   1 
ATOM 1781 O O   . HIS C 1 118 ? 118.734 93.693  99.719  1.00 56.45  ?  110 HIS A O   1 
ATOM 1782 C CB  . HIS C 1 118 ? 118.772 91.104  100.732 1.00 58.25  ?  110 HIS A CB  1 
ATOM 1783 C CG  . HIS C 1 118 ? 118.636 89.738  101.330 1.00 61.96  ?  110 HIS A CG  1 
ATOM 1784 N ND1 . HIS C 1 118 ? 118.260 88.636  100.593 1.00 63.66  ?  110 HIS A ND1 1 
ATOM 1785 C CD2 . HIS C 1 118 ? 118.826 89.297  102.596 1.00 64.08  ?  110 HIS A CD2 1 
ATOM 1786 C CE1 . HIS C 1 118 ? 118.226 87.574  101.378 1.00 66.25  ?  110 HIS A CE1 1 
ATOM 1787 N NE2 . HIS C 1 118 ? 118.564 87.948  102.599 1.00 65.97  ?  110 HIS A NE2 1 
ATOM 1788 N N   . CYS C 1 119 ? 117.461 94.535  101.381 1.00 50.28  ?  111 CYS A N   1 
ATOM 1789 C CA  . CYS C 1 119 ? 117.565 95.926  100.954 1.00 47.95  ?  111 CYS A CA  1 
ATOM 1790 C C   . CYS C 1 119 ? 118.600 96.612  101.838 1.00 49.91  ?  111 CYS A C   1 
ATOM 1791 O O   . CYS C 1 119 ? 118.298 97.004  102.970 1.00 54.61  ?  111 CYS A O   1 
ATOM 1792 C CB  . CYS C 1 119 ? 116.211 96.626  101.040 1.00 48.90  ?  111 CYS A CB  1 
ATOM 1793 S SG  . CYS C 1 119 ? 114.854 95.710  100.274 1.00 52.14  ?  111 CYS A SG  1 
ATOM 1794 N N   . ILE C 1 120 ? 119.817 96.757  101.320 1.00 47.41  ?  112 ILE A N   1 
ATOM 1795 C CA  . ILE C 1 120 ? 120.952 97.261  102.085 1.00 46.51  ?  112 ILE A CA  1 
ATOM 1796 C C   . ILE C 1 120 ? 121.496 98.502  101.394 1.00 49.01  ?  112 ILE A C   1 
ATOM 1797 O O   . ILE C 1 120 ? 121.622 98.531  100.165 1.00 54.47  ?  112 ILE A O   1 
ATOM 1798 C CB  . ILE C 1 120 ? 122.053 96.195  102.234 1.00 49.70  ?  112 ILE A CB  1 
ATOM 1799 C CG1 . ILE C 1 120 ? 121.434 94.810  102.444 1.00 54.70  ?  112 ILE A CG1 1 
ATOM 1800 C CG2 . ILE C 1 120 ? 122.985 96.548  103.383 1.00 50.02  ?  112 ILE A CG2 1 
ATOM 1801 C CD1 . ILE C 1 120 ? 122.438 93.682  102.439 1.00 54.77  ?  112 ILE A CD1 1 
ATOM 1802 N N   . ILE C 1 121 ? 121.814 99.524  102.185 1.00 47.94  ?  113 ILE A N   1 
ATOM 1803 C CA  . ILE C 1 121 ? 122.445 100.745 101.698 1.00 45.58  ?  113 ILE A CA  1 
ATOM 1804 C C   . ILE C 1 121 ? 123.837 100.817 102.308 1.00 45.63  ?  113 ILE A C   1 
ATOM 1805 O O   . ILE C 1 121 ? 123.981 100.870 103.536 1.00 47.62  ?  113 ILE A O   1 
ATOM 1806 C CB  . ILE C 1 121 ? 121.625 101.996 102.049 1.00 42.73  ?  113 ILE A CB  1 
ATOM 1807 C CG1 . ILE C 1 121 ? 120.324 102.024 101.243 1.00 41.00  ?  113 ILE A CG1 1 
ATOM 1808 C CG2 . ILE C 1 121 ? 122.440 103.256 101.798 1.00 41.28  ?  113 ILE A CG2 1 
ATOM 1809 C CD1 . ILE C 1 121 ? 119.529 103.301 101.408 1.00 34.55  ?  113 ILE A CD1 1 
ATOM 1810 N N   . GLY C 1 122 ? 124.854 100.820 101.459 1.00 44.91  ?  114 GLY A N   1 
ATOM 1811 C CA  . GLY C 1 122 ? 126.234 100.806 101.894 1.00 48.20  ?  114 GLY A CA  1 
ATOM 1812 C C   . GLY C 1 122 ? 126.897 99.462  101.634 1.00 55.05  ?  114 GLY A C   1 
ATOM 1813 O O   . GLY C 1 122 ? 126.326 98.552  101.031 1.00 60.26  ?  114 GLY A O   1 
ATOM 1814 N N   . ARG C 1 123 ? 128.136 99.358  102.109 1.00 56.45  ?  115 ARG A N   1 
ATOM 1815 C CA  . ARG C 1 123 ? 128.889 98.122  101.946 1.00 60.05  ?  115 ARG A CA  1 
ATOM 1816 C C   . ARG C 1 123 ? 128.249 96.995  102.748 1.00 63.05  ?  115 ARG A C   1 
ATOM 1817 O O   . ARG C 1 123 ? 127.701 97.214  103.831 1.00 67.17  ?  115 ARG A O   1 
ATOM 1818 C CB  . ARG C 1 123 ? 130.346 98.323  102.370 1.00 60.37  ?  115 ARG A CB  1 
ATOM 1819 C CG  . ARG C 1 123 ? 130.545 98.626  103.845 1.00 62.22  ?  115 ARG A CG  1 
ATOM 1820 C CD  . ARG C 1 123 ? 132.024 98.708  104.190 1.00 63.70  ?  115 ARG A CD  1 
ATOM 1821 N NE  . ARG C 1 123 ? 132.556 100.054 104.008 1.00 68.41  ?  115 ARG A NE  1 
ATOM 1822 C CZ  . ARG C 1 123 ? 133.220 100.728 104.936 1.00 69.03  ?  115 ARG A CZ  1 
ATOM 1823 N NH1 . ARG C 1 123 ? 133.457 100.210 106.130 1.00 66.49  1  115 ARG A NH1 1 
ATOM 1824 N NH2 . ARG C 1 123 ? 133.660 101.952 104.658 1.00 71.22  ?  115 ARG A NH2 1 
ATOM 1825 N N   . THR C 1 124 ? 128.306 95.785  102.200 1.00 62.52  ?  116 THR A N   1 
ATOM 1826 C CA  . THR C 1 124 ? 127.714 94.616  102.838 1.00 62.73  ?  116 THR A CA  1 
ATOM 1827 C C   . THR C 1 124 ? 128.342 93.361  102.247 1.00 64.55  ?  116 THR A C   1 
ATOM 1828 O O   . THR C 1 124 ? 129.159 93.423  101.325 1.00 68.81  ?  116 THR A O   1 
ATOM 1829 C CB  . THR C 1 124 ? 126.190 94.603  102.680 1.00 62.54  ?  116 THR A CB  1 
ATOM 1830 O OG1 . THR C 1 124 ? 125.651 93.450  103.339 1.00 67.18  ?  116 THR A OG1 1 
ATOM 1831 C CG2 . THR C 1 124 ? 125.800 94.580  101.218 1.00 62.11  ?  116 THR A CG2 1 
ATOM 1832 N N   . LEU C 1 125 ? 127.947 92.213  102.793 1.00 66.11  ?  117 LEU A N   1 
ATOM 1833 C CA  . LEU C 1 125 ? 128.457 90.922  102.339 1.00 69.44  ?  117 LEU A CA  1 
ATOM 1834 C C   . LEU C 1 125 ? 127.395 89.877  102.646 1.00 74.04  ?  117 LEU A C   1 
ATOM 1835 O O   . LEU C 1 125 ? 127.100 89.624  103.819 1.00 78.90  ?  117 LEU A O   1 
ATOM 1836 C CB  . LEU C 1 125 ? 129.780 90.588  103.022 1.00 69.18  ?  117 LEU A CB  1 
ATOM 1837 C CG  . LEU C 1 125 ? 130.833 89.840  102.199 1.00 67.69  ?  117 LEU A CG  1 
ATOM 1838 C CD1 . LEU C 1 125 ? 132.178 89.873  102.907 1.00 64.04  ?  117 LEU A CD1 1 
ATOM 1839 C CD2 . LEU C 1 125 ? 130.404 88.406  101.928 1.00 69.31  ?  117 LEU A CD2 1 
ATOM 1840 N N   . VAL C 1 126 ? 126.826 89.277  101.604 1.00 75.25  ?  118 VAL A N   1 
ATOM 1841 C CA  . VAL C 1 126 ? 125.761 88.291  101.737 1.00 77.60  ?  118 VAL A CA  1 
ATOM 1842 C C   . VAL C 1 126 ? 126.269 86.960  101.204 1.00 78.22  ?  118 VAL A C   1 
ATOM 1843 O O   . VAL C 1 126 ? 126.757 86.884  100.071 1.00 79.51  ?  118 VAL A O   1 
ATOM 1844 C CB  . VAL C 1 126 ? 124.486 88.728  100.991 1.00 78.76  ?  118 VAL A CB  1 
ATOM 1845 C CG1 . VAL C 1 126 ? 123.380 87.700  101.181 1.00 78.09  ?  118 VAL A CG1 1 
ATOM 1846 C CG2 . VAL C 1 126 ? 124.035 90.101  101.467 1.00 73.56  ?  118 VAL A CG2 1 
ATOM 1847 N N   . VAL C 1 127 ? 126.154 85.916  102.022 1.00 78.07  ?  119 VAL A N   1 
ATOM 1848 C CA  . VAL C 1 127 ? 126.584 84.571  101.658 1.00 80.37  ?  119 VAL A CA  1 
ATOM 1849 C C   . VAL C 1 127 ? 125.413 83.622  101.866 1.00 83.95  ?  119 VAL A C   1 
ATOM 1850 O O   . VAL C 1 127 ? 124.824 83.583  102.952 1.00 85.60  ?  119 VAL A O   1 
ATOM 1851 C CB  . VAL C 1 127 ? 127.803 84.117  102.484 1.00 79.15  ?  119 VAL A CB  1 
ATOM 1852 C CG1 . VAL C 1 127 ? 128.045 82.626  102.305 1.00 78.97  ?  119 VAL A CG1 1 
ATOM 1853 C CG2 . VAL C 1 127 ? 129.037 84.913  102.090 1.00 78.38  ?  119 VAL A CG2 1 
ATOM 1854 N N   . HIS C 1 128 ? 125.077 82.860  100.828 1.00 86.95  ?  120 HIS A N   1 
ATOM 1855 C CA  . HIS C 1 128 ? 123.994 81.887  100.883 1.00 88.45  ?  120 HIS A CA  1 
ATOM 1856 C C   . HIS C 1 128 ? 124.590 80.487  100.966 1.00 90.30  ?  120 HIS A C   1 
ATOM 1857 O O   . HIS C 1 128 ? 125.403 80.104  100.118 1.00 89.93  ?  120 HIS A O   1 
ATOM 1858 C CB  . HIS C 1 128 ? 123.084 82.013  99.661  1.00 87.72  ?  120 HIS A CB  1 
ATOM 1859 C CG  . HIS C 1 128 ? 121.998 83.031  99.819  1.00 88.59  ?  120 HIS A CG  1 
ATOM 1860 N ND1 . HIS C 1 128 ? 121.817 84.070  98.931  1.00 88.11  ?  120 HIS A ND1 1 
ATOM 1861 C CD2 . HIS C 1 128 ? 121.035 83.169  100.760 1.00 87.73  ?  120 HIS A CD2 1 
ATOM 1862 C CE1 . HIS C 1 128 ? 120.790 84.804  99.319  1.00 83.30  ?  120 HIS A CE1 1 
ATOM 1863 N NE2 . HIS C 1 128 ? 120.296 84.279  100.427 1.00 82.92  ?  120 HIS A NE2 1 
ATOM 1864 N N   . GLU C 1 129 ? 124.182 79.734  101.986 1.00 92.63  ?  121 GLU A N   1 
ATOM 1865 C CA  . GLU C 1 129 ? 124.665 78.372  102.215 1.00 95.14  ?  121 GLU A CA  1 
ATOM 1866 C C   . GLU C 1 129 ? 126.188 78.312  102.286 1.00 91.48  ?  121 GLU A C   1 
ATOM 1867 O O   . GLU C 1 129 ? 126.831 79.222  102.809 1.00 89.98  ?  121 GLU A O   1 
ATOM 1868 C CB  . GLU C 1 129 ? 124.153 77.429  101.121 1.00 95.66  ?  121 GLU A CB  1 
ATOM 1869 C CG  . GLU C 1 129 ? 122.657 77.523  100.870 1.00 98.85  ?  121 GLU A CG  1 
ATOM 1870 C CD  . GLU C 1 129 ? 122.026 76.170  100.606 1.00 103.82 ?  121 GLU A CD  1 
ATOM 1871 O OE1 . GLU C 1 129 ? 122.626 75.146  100.996 1.00 99.75  ?  121 GLU A OE1 1 
ATOM 1872 O OE2 . GLU C 1 129 ? 120.930 76.130  100.008 1.00 106.63 -1 121 GLU A OE2 1 
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