data_9JBP
# 
_entry.id   9JBP 
# 
_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   9JBP         pdb_00009jbp 10.2210/pdb9jbp/pdb 
WWPDB D_1300050531 ?            ?                   
EMDB  EMD-61322    ?            ?                   
# 
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                        9JBP 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  '9JBO contains the wild-type SOD1 filament structure, while the current deposition is the mutant SOD1 structure.' 9JBO      
unspecified            
EMDB 'EMD-61321 contains the wild-type SOD1 data, while the current deposition is the mutant SOD1 data.'               EMD-61321 
'other EM volume'      
EMDB 'Cryo-EM structure of human SOD1 (C6A/C111A) amyloid filament'                                                    EMD-61322 
'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 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Superoxide dismutase [Cu-Zn]'  16642.439 6 1.15.1.1 C6A,C111A ? ?                                     
2 polymer man 'Unassigned poly-alanine model' 698.854   6 ?        ?         ? 'superoxide dismutase[Cu-Zn](P00441)' 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GAMDPEFMATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIA
Q
;
;GAMDPEFMATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIA
Q
;
A,B,C,D,E,F ? 
2 'polypeptide(L)' no no '(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)' XXXXXXXX G,H,I,J,K,L ? 
# 
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  ALA 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 ALA 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 
2 1   UNK n 
2 2   UNK n 
2 3   UNK n 
2 4   UNK n 
2 5   UNK n 
2 6   UNK n 
2 7   UNK n 
2 8   UNK n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 161 human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 8   ?     ? ?    ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
UNK 'L-peptide linking' . UNKNOWN         ? 'C4 H9 N O2'     103.120 
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  ?  ?   ?   A . n 
A 1 2   ALA 2   -6  ?  ?   ?   A . n 
A 1 3   MET 3   -5  ?  ?   ?   A . n 
A 1 4   ASP 4   -4  ?  ?   ?   A . n 
A 1 5   PRO 5   -3  ?  ?   ?   A . n 
A 1 6   GLU 6   -2  ?  ?   ?   A . n 
A 1 7   PHE 7   -1  ?  ?   ?   A . n 
A 1 8   MET 8   0   ?  ?   ?   A . n 
A 1 9   ALA 9   1   1  ALA ALA A . n 
A 1 10  THR 10  2   2  THR THR A . n 
A 1 11  LYS 11  3   3  LYS LYS A . n 
A 1 12  ALA 12  4   4  ALA ALA A . n 
A 1 13  VAL 13  5   5  VAL VAL A . n 
A 1 14  ALA 14  6   6  ALA ALA A . n 
A 1 15  VAL 15  7   7  VAL VAL A . n 
A 1 16  LEU 16  8   8  LEU LEU A . n 
A 1 17  LYS 17  9   9  LYS LYS A . n 
A 1 18  GLY 18  10  10 GLY GLY A . n 
A 1 19  ASP 19  11  11 ASP ASP A . n 
A 1 20  GLY 20  12  12 GLY GLY A . n 
A 1 21  PRO 21  13  13 PRO PRO A . n 
A 1 22  VAL 22  14  14 VAL VAL A . n 
A 1 23  GLN 23  15  15 GLN GLN A . n 
A 1 24  GLY 24  16  16 GLY GLY A . n 
A 1 25  ILE 25  17  17 ILE ILE A . n 
A 1 26  ILE 26  18  18 ILE ILE A . n 
A 1 27  ASN 27  19  19 ASN ASN A . n 
A 1 28  PHE 28  20  20 PHE PHE A . n 
A 1 29  GLU 29  21  21 GLU GLU A . n 
A 1 30  GLN 30  22  22 GLN GLN A . n 
A 1 31  LYS 31  23  23 LYS LYS A . n 
A 1 32  GLU 32  24  24 GLU GLU A . n 
A 1 33  SER 33  25  25 SER SER A . n 
A 1 34  ASN 34  26  26 ASN ASN A . n 
A 1 35  GLY 35  27  27 GLY GLY A . n 
A 1 36  PRO 36  28  28 PRO PRO A . n 
A 1 37  VAL 37  29  29 VAL VAL A . n 
A 1 38  LYS 38  30  30 LYS LYS A . n 
A 1 39  VAL 39  31  31 VAL VAL A . n 
A 1 40  TRP 40  32  32 TRP TRP A . n 
A 1 41  GLY 41  33  33 GLY GLY A . n 
A 1 42  SER 42  34  34 SER SER A . n 
A 1 43  ILE 43  35  35 ILE ILE A . n 
A 1 44  LYS 44  36  36 LYS LYS A . n 
A 1 45  GLY 45  37  37 GLY GLY A . n 
A 1 46  LEU 46  38  38 LEU LEU A . n 
A 1 47  THR 47  39  39 THR THR A . n 
A 1 48  GLU 48  40  40 GLU GLU A . n 
A 1 49  GLY 49  41  41 GLY GLY A . n 
A 1 50  LEU 50  42  ?  ?   ?   A . n 
A 1 51  HIS 51  43  ?  ?   ?   A . n 
A 1 52  GLY 52  44  ?  ?   ?   A . n 
A 1 53  PHE 53  45  ?  ?   ?   A . n 
A 1 54  HIS 54  46  ?  ?   ?   A . n 
A 1 55  VAL 55  47  ?  ?   ?   A . n 
A 1 56  HIS 56  48  ?  ?   ?   A . n 
A 1 57  GLU 57  49  ?  ?   ?   A . n 
A 1 58  PHE 58  50  ?  ?   ?   A . n 
A 1 59  GLY 59  51  ?  ?   ?   A . n 
A 1 60  ASP 60  52  ?  ?   ?   A . n 
A 1 61  ASN 61  53  ?  ?   ?   A . n 
A 1 62  THR 62  54  ?  ?   ?   A . n 
A 1 63  ALA 63  55  ?  ?   ?   A . n 
A 1 64  GLY 64  56  ?  ?   ?   A . n 
A 1 65  CYS 65  57  ?  ?   ?   A . n 
A 1 66  THR 66  58  ?  ?   ?   A . n 
A 1 67  SER 67  59  ?  ?   ?   A . n 
A 1 68  ALA 68  60  ?  ?   ?   A . n 
A 1 69  GLY 69  61  ?  ?   ?   A . n 
A 1 70  PRO 70  62  ?  ?   ?   A . n 
A 1 71  HIS 71  63  ?  ?   ?   A . n 
A 1 72  PHE 72  64  ?  ?   ?   A . n 
A 1 73  ASN 73  65  ?  ?   ?   A . n 
A 1 74  PRO 74  66  ?  ?   ?   A . n 
A 1 75  LEU 75  67  ?  ?   ?   A . n 
A 1 76  SER 76  68  ?  ?   ?   A . n 
A 1 77  ARG 77  69  ?  ?   ?   A . n 
A 1 78  LYS 78  70  ?  ?   ?   A . n 
A 1 79  HIS 79  71  ?  ?   ?   A . n 
A 1 80  GLY 80  72  ?  ?   ?   A . n 
A 1 81  GLY 81  73  ?  ?   ?   A . n 
A 1 82  PRO 82  74  ?  ?   ?   A . n 
A 1 83  LYS 83  75  ?  ?   ?   A . n 
A 1 84  ASP 84  76  ?  ?   ?   A . n 
A 1 85  GLU 85  77  ?  ?   ?   A . n 
A 1 86  GLU 86  78  ?  ?   ?   A . n 
A 1 87  ARG 87  79  ?  ?   ?   A . n 
A 1 88  HIS 88  80  ?  ?   ?   A . n 
A 1 89  VAL 89  81  ?  ?   ?   A . n 
A 1 90  GLY 90  82  ?  ?   ?   A . n 
A 1 91  ASP 91  83  ?  ?   ?   A . n 
A 1 92  LEU 92  84  ?  ?   ?   A . n 
A 1 93  GLY 93  85  ?  ?   ?   A . n 
A 1 94  ASN 94  86  ?  ?   ?   A . n 
A 1 95  VAL 95  87  ?  ?   ?   A . n 
A 1 96  THR 96  88  ?  ?   ?   A . n 
A 1 97  ALA 97  89  ?  ?   ?   A . n 
A 1 98  ASP 98  90  ?  ?   ?   A . n 
A 1 99  LYS 99  91  ?  ?   ?   A . n 
A 1 100 ASP 100 92  ?  ?   ?   A . n 
A 1 101 GLY 101 93  ?  ?   ?   A . n 
A 1 102 VAL 102 94  ?  ?   ?   A . n 
A 1 103 ALA 103 95  ?  ?   ?   A . n 
A 1 104 ASP 104 96  ?  ?   ?   A . n 
A 1 105 VAL 105 97  ?  ?   ?   A . n 
A 1 106 SER 106 98  ?  ?   ?   A . n 
A 1 107 ILE 107 99  ?  ?   ?   A . n 
A 1 108 GLU 108 100 ?  ?   ?   A . n 
A 1 109 ASP 109 101 ?  ?   ?   A . n 
A 1 110 SER 110 102 ?  ?   ?   A . n 
A 1 111 VAL 111 103 ?  ?   ?   A . n 
A 1 112 ILE 112 104 ?  ?   ?   A . n 
A 1 113 SER 113 105 ?  ?   ?   A . n 
A 1 114 LEU 114 106 ?  ?   ?   A . n 
A 1 115 SER 115 107 ?  ?   ?   A . n 
A 1 116 GLY 116 108 ?  ?   ?   A . n 
A 1 117 ASP 117 109 ?  ?   ?   A . n 
A 1 118 HIS 118 110 ?  ?   ?   A . n 
A 1 119 ALA 119 111 ?  ?   ?   A . n 
A 1 120 ILE 120 112 ?  ?   ?   A . n 
A 1 121 ILE 121 113 ?  ?   ?   A . n 
A 1 122 GLY 122 114 ?  ?   ?   A . n 
A 1 123 ARG 123 115 ?  ?   ?   A . n 
A 1 124 THR 124 116 ?  ?   ?   A . n 
A 1 125 LEU 125 117 ?  ?   ?   A . n 
A 1 126 VAL 126 118 ?  ?   ?   A . n 
A 1 127 VAL 127 119 ?  ?   ?   A . n 
A 1 128 HIS 128 120 ?  ?   ?   A . n 
A 1 129 GLU 129 121 ?  ?   ?   A . n 
A 1 130 LYS 130 122 ?  ?   ?   A . n 
A 1 131 ALA 131 123 ?  ?   ?   A . n 
A 1 132 ASP 132 124 ?  ?   ?   A . n 
A 1 133 ASP 133 125 ?  ?   ?   A . n 
A 1 134 LEU 134 126 ?  ?   ?   A . n 
A 1 135 GLY 135 127 ?  ?   ?   A . n 
A 1 136 LYS 136 128 ?  ?   ?   A . n 
A 1 137 GLY 137 129 ?  ?   ?   A . n 
A 1 138 GLY 138 130 ?  ?   ?   A . n 
A 1 139 ASN 139 131 ?  ?   ?   A . n 
A 1 140 GLU 140 132 ?  ?   ?   A . n 
A 1 141 GLU 141 133 ?  ?   ?   A . n 
A 1 142 SER 142 134 ?  ?   ?   A . n 
A 1 143 THR 143 135 ?  ?   ?   A . n 
A 1 144 LYS 144 136 ?  ?   ?   A . n 
A 1 145 THR 145 137 ?  ?   ?   A . n 
A 1 146 GLY 146 138 ?  ?   ?   A . n 
A 1 147 ASN 147 139 ?  ?   ?   A . n 
A 1 148 ALA 148 140 ?  ?   ?   A . n 
A 1 149 GLY 149 141 ?  ?   ?   A . n 
A 1 150 SER 150 142 ?  ?   ?   A . n 
A 1 151 ARG 151 143 ?  ?   ?   A . n 
A 1 152 LEU 152 144 ?  ?   ?   A . n 
A 1 153 ALA 153 145 ?  ?   ?   A . n 
A 1 154 CYS 154 146 ?  ?   ?   A . n 
A 1 155 GLY 155 147 ?  ?   ?   A . n 
A 1 156 VAL 156 148 ?  ?   ?   A . n 
A 1 157 ILE 157 149 ?  ?   ?   A . n 
A 1 158 GLY 158 150 ?  ?   ?   A . n 
A 1 159 ILE 159 151 ?  ?   ?   A . n 
A 1 160 ALA 160 152 ?  ?   ?   A . n 
A 1 161 GLN 161 153 ?  ?   ?   A . n 
B 2 1   UNK 1   1   1  UNK UNK G . n 
B 2 2   UNK 2   2   2  UNK UNK G . n 
B 2 3   UNK 3   3   3  UNK UNK G . n 
B 2 4   UNK 4   4   4  UNK UNK G . n 
B 2 5   UNK 5   5   5  UNK UNK G . n 
B 2 6   UNK 6   6   6  UNK UNK G . n 
B 2 7   UNK 7   7   7  UNK UNK G . n 
B 2 8   UNK 8   8   8  UNK UNK G . n 
C 1 1   GLY 1   -7  ?  ?   ?   B . n 
C 1 2   ALA 2   -6  ?  ?   ?   B . n 
C 1 3   MET 3   -5  ?  ?   ?   B . n 
C 1 4   ASP 4   -4  ?  ?   ?   B . n 
C 1 5   PRO 5   -3  ?  ?   ?   B . n 
C 1 6   GLU 6   -2  ?  ?   ?   B . n 
C 1 7   PHE 7   -1  ?  ?   ?   B . n 
C 1 8   MET 8   0   ?  ?   ?   B . n 
C 1 9   ALA 9   1   1  ALA ALA B . n 
C 1 10  THR 10  2   2  THR THR B . n 
C 1 11  LYS 11  3   3  LYS LYS B . n 
C 1 12  ALA 12  4   4  ALA ALA B . n 
C 1 13  VAL 13  5   5  VAL VAL B . n 
C 1 14  ALA 14  6   6  ALA ALA B . n 
C 1 15  VAL 15  7   7  VAL VAL B . n 
C 1 16  LEU 16  8   8  LEU LEU B . n 
C 1 17  LYS 17  9   9  LYS LYS B . n 
C 1 18  GLY 18  10  10 GLY GLY B . n 
C 1 19  ASP 19  11  11 ASP ASP B . n 
C 1 20  GLY 20  12  12 GLY GLY B . n 
C 1 21  PRO 21  13  13 PRO PRO B . n 
C 1 22  VAL 22  14  14 VAL VAL B . n 
C 1 23  GLN 23  15  15 GLN GLN B . n 
C 1 24  GLY 24  16  16 GLY GLY B . n 
C 1 25  ILE 25  17  17 ILE ILE B . n 
C 1 26  ILE 26  18  18 ILE ILE B . n 
C 1 27  ASN 27  19  19 ASN ASN B . n 
C 1 28  PHE 28  20  20 PHE PHE B . n 
C 1 29  GLU 29  21  21 GLU GLU B . n 
C 1 30  GLN 30  22  22 GLN GLN B . n 
C 1 31  LYS 31  23  23 LYS LYS B . n 
C 1 32  GLU 32  24  24 GLU GLU B . n 
C 1 33  SER 33  25  25 SER SER B . n 
C 1 34  ASN 34  26  26 ASN ASN B . n 
C 1 35  GLY 35  27  27 GLY GLY B . n 
C 1 36  PRO 36  28  28 PRO PRO B . n 
C 1 37  VAL 37  29  29 VAL VAL B . n 
C 1 38  LYS 38  30  30 LYS LYS B . n 
C 1 39  VAL 39  31  31 VAL VAL B . n 
C 1 40  TRP 40  32  32 TRP TRP B . n 
C 1 41  GLY 41  33  33 GLY GLY B . n 
C 1 42  SER 42  34  34 SER SER B . n 
C 1 43  ILE 43  35  35 ILE ILE B . n 
C 1 44  LYS 44  36  36 LYS LYS B . n 
C 1 45  GLY 45  37  37 GLY GLY B . n 
C 1 46  LEU 46  38  38 LEU LEU B . n 
C 1 47  THR 47  39  39 THR THR B . n 
C 1 48  GLU 48  40  40 GLU GLU B . n 
C 1 49  GLY 49  41  41 GLY GLY B . n 
C 1 50  LEU 50  42  ?  ?   ?   B . n 
C 1 51  HIS 51  43  ?  ?   ?   B . n 
C 1 52  GLY 52  44  ?  ?   ?   B . n 
C 1 53  PHE 53  45  ?  ?   ?   B . n 
C 1 54  HIS 54  46  ?  ?   ?   B . n 
C 1 55  VAL 55  47  ?  ?   ?   B . n 
C 1 56  HIS 56  48  ?  ?   ?   B . n 
C 1 57  GLU 57  49  ?  ?   ?   B . n 
C 1 58  PHE 58  50  ?  ?   ?   B . n 
C 1 59  GLY 59  51  ?  ?   ?   B . n 
C 1 60  ASP 60  52  ?  ?   ?   B . n 
C 1 61  ASN 61  53  ?  ?   ?   B . n 
C 1 62  THR 62  54  ?  ?   ?   B . n 
C 1 63  ALA 63  55  ?  ?   ?   B . n 
C 1 64  GLY 64  56  ?  ?   ?   B . n 
C 1 65  CYS 65  57  ?  ?   ?   B . n 
C 1 66  THR 66  58  ?  ?   ?   B . n 
C 1 67  SER 67  59  ?  ?   ?   B . n 
C 1 68  ALA 68  60  ?  ?   ?   B . n 
C 1 69  GLY 69  61  ?  ?   ?   B . n 
C 1 70  PRO 70  62  ?  ?   ?   B . n 
C 1 71  HIS 71  63  ?  ?   ?   B . n 
C 1 72  PHE 72  64  ?  ?   ?   B . n 
C 1 73  ASN 73  65  ?  ?   ?   B . n 
C 1 74  PRO 74  66  ?  ?   ?   B . n 
C 1 75  LEU 75  67  ?  ?   ?   B . n 
C 1 76  SER 76  68  ?  ?   ?   B . n 
C 1 77  ARG 77  69  ?  ?   ?   B . n 
C 1 78  LYS 78  70  ?  ?   ?   B . n 
C 1 79  HIS 79  71  ?  ?   ?   B . n 
C 1 80  GLY 80  72  ?  ?   ?   B . n 
C 1 81  GLY 81  73  ?  ?   ?   B . n 
C 1 82  PRO 82  74  ?  ?   ?   B . n 
C 1 83  LYS 83  75  ?  ?   ?   B . n 
C 1 84  ASP 84  76  ?  ?   ?   B . n 
C 1 85  GLU 85  77  ?  ?   ?   B . n 
C 1 86  GLU 86  78  ?  ?   ?   B . n 
C 1 87  ARG 87  79  ?  ?   ?   B . n 
C 1 88  HIS 88  80  ?  ?   ?   B . n 
C 1 89  VAL 89  81  ?  ?   ?   B . n 
C 1 90  GLY 90  82  ?  ?   ?   B . n 
C 1 91  ASP 91  83  ?  ?   ?   B . n 
C 1 92  LEU 92  84  ?  ?   ?   B . n 
C 1 93  GLY 93  85  ?  ?   ?   B . n 
C 1 94  ASN 94  86  ?  ?   ?   B . n 
C 1 95  VAL 95  87  ?  ?   ?   B . n 
C 1 96  THR 96  88  ?  ?   ?   B . n 
C 1 97  ALA 97  89  ?  ?   ?   B . n 
C 1 98  ASP 98  90  ?  ?   ?   B . n 
C 1 99  LYS 99  91  ?  ?   ?   B . n 
C 1 100 ASP 100 92  ?  ?   ?   B . n 
C 1 101 GLY 101 93  ?  ?   ?   B . n 
C 1 102 VAL 102 94  ?  ?   ?   B . n 
C 1 103 ALA 103 95  ?  ?   ?   B . n 
C 1 104 ASP 104 96  ?  ?   ?   B . n 
C 1 105 VAL 105 97  ?  ?   ?   B . n 
C 1 106 SER 106 98  ?  ?   ?   B . n 
C 1 107 ILE 107 99  ?  ?   ?   B . n 
C 1 108 GLU 108 100 ?  ?   ?   B . n 
C 1 109 ASP 109 101 ?  ?   ?   B . n 
C 1 110 SER 110 102 ?  ?   ?   B . n 
C 1 111 VAL 111 103 ?  ?   ?   B . n 
C 1 112 ILE 112 104 ?  ?   ?   B . n 
C 1 113 SER 113 105 ?  ?   ?   B . n 
C 1 114 LEU 114 106 ?  ?   ?   B . n 
C 1 115 SER 115 107 ?  ?   ?   B . n 
C 1 116 GLY 116 108 ?  ?   ?   B . n 
C 1 117 ASP 117 109 ?  ?   ?   B . n 
C 1 118 HIS 118 110 ?  ?   ?   B . n 
C 1 119 ALA 119 111 ?  ?   ?   B . n 
C 1 120 ILE 120 112 ?  ?   ?   B . n 
C 1 121 ILE 121 113 ?  ?   ?   B . n 
C 1 122 GLY 122 114 ?  ?   ?   B . n 
C 1 123 ARG 123 115 ?  ?   ?   B . n 
C 1 124 THR 124 116 ?  ?   ?   B . n 
C 1 125 LEU 125 117 ?  ?   ?   B . n 
C 1 126 VAL 126 118 ?  ?   ?   B . n 
C 1 127 VAL 127 119 ?  ?   ?   B . n 
C 1 128 HIS 128 120 ?  ?   ?   B . n 
C 1 129 GLU 129 121 ?  ?   ?   B . n 
C 1 130 LYS 130 122 ?  ?   ?   B . n 
C 1 131 ALA 131 123 ?  ?   ?   B . n 
C 1 132 ASP 132 124 ?  ?   ?   B . n 
C 1 133 ASP 133 125 ?  ?   ?   B . n 
C 1 134 LEU 134 126 ?  ?   ?   B . n 
C 1 135 GLY 135 127 ?  ?   ?   B . n 
C 1 136 LYS 136 128 ?  ?   ?   B . n 
C 1 137 GLY 137 129 ?  ?   ?   B . n 
C 1 138 GLY 138 130 ?  ?   ?   B . n 
C 1 139 ASN 139 131 ?  ?   ?   B . n 
C 1 140 GLU 140 132 ?  ?   ?   B . n 
C 1 141 GLU 141 133 ?  ?   ?   B . n 
C 1 142 SER 142 134 ?  ?   ?   B . n 
C 1 143 THR 143 135 ?  ?   ?   B . n 
C 1 144 LYS 144 136 ?  ?   ?   B . n 
C 1 145 THR 145 137 ?  ?   ?   B . n 
C 1 146 GLY 146 138 ?  ?   ?   B . n 
C 1 147 ASN 147 139 ?  ?   ?   B . n 
C 1 148 ALA 148 140 ?  ?   ?   B . n 
C 1 149 GLY 149 141 ?  ?   ?   B . n 
C 1 150 SER 150 142 ?  ?   ?   B . n 
C 1 151 ARG 151 143 ?  ?   ?   B . n 
C 1 152 LEU 152 144 ?  ?   ?   B . n 
C 1 153 ALA 153 145 ?  ?   ?   B . n 
C 1 154 CYS 154 146 ?  ?   ?   B . n 
C 1 155 GLY 155 147 ?  ?   ?   B . n 
C 1 156 VAL 156 148 ?  ?   ?   B . n 
C 1 157 ILE 157 149 ?  ?   ?   B . n 
C 1 158 GLY 158 150 ?  ?   ?   B . n 
C 1 159 ILE 159 151 ?  ?   ?   B . n 
C 1 160 ALA 160 152 ?  ?   ?   B . n 
C 1 161 GLN 161 153 ?  ?   ?   B . n 
D 2 1   UNK 1   1   1  UNK UNK H . n 
D 2 2   UNK 2   2   2  UNK UNK H . n 
D 2 3   UNK 3   3   3  UNK UNK H . n 
D 2 4   UNK 4   4   4  UNK UNK H . n 
D 2 5   UNK 5   5   5  UNK UNK H . n 
D 2 6   UNK 6   6   6  UNK UNK H . n 
D 2 7   UNK 7   7   7  UNK UNK H . n 
D 2 8   UNK 8   8   8  UNK UNK H . n 
E 1 1   GLY 1   -7  ?  ?   ?   C . n 
E 1 2   ALA 2   -6  ?  ?   ?   C . n 
E 1 3   MET 3   -5  ?  ?   ?   C . n 
E 1 4   ASP 4   -4  ?  ?   ?   C . n 
E 1 5   PRO 5   -3  ?  ?   ?   C . n 
E 1 6   GLU 6   -2  ?  ?   ?   C . n 
E 1 7   PHE 7   -1  ?  ?   ?   C . n 
E 1 8   MET 8   0   ?  ?   ?   C . n 
E 1 9   ALA 9   1   1  ALA ALA C . n 
E 1 10  THR 10  2   2  THR THR C . n 
E 1 11  LYS 11  3   3  LYS LYS C . n 
E 1 12  ALA 12  4   4  ALA ALA C . n 
E 1 13  VAL 13  5   5  VAL VAL C . n 
E 1 14  ALA 14  6   6  ALA ALA C . n 
E 1 15  VAL 15  7   7  VAL VAL C . n 
E 1 16  LEU 16  8   8  LEU LEU C . n 
E 1 17  LYS 17  9   9  LYS LYS C . n 
E 1 18  GLY 18  10  10 GLY GLY C . n 
E 1 19  ASP 19  11  11 ASP ASP C . n 
E 1 20  GLY 20  12  12 GLY GLY C . n 
E 1 21  PRO 21  13  13 PRO PRO C . n 
E 1 22  VAL 22  14  14 VAL VAL C . n 
E 1 23  GLN 23  15  15 GLN GLN C . n 
E 1 24  GLY 24  16  16 GLY GLY C . n 
E 1 25  ILE 25  17  17 ILE ILE C . n 
E 1 26  ILE 26  18  18 ILE ILE C . n 
E 1 27  ASN 27  19  19 ASN ASN C . n 
E 1 28  PHE 28  20  20 PHE PHE C . n 
E 1 29  GLU 29  21  21 GLU GLU C . n 
E 1 30  GLN 30  22  22 GLN GLN C . n 
E 1 31  LYS 31  23  23 LYS LYS C . n 
E 1 32  GLU 32  24  24 GLU GLU C . n 
E 1 33  SER 33  25  25 SER SER C . n 
E 1 34  ASN 34  26  26 ASN ASN C . n 
E 1 35  GLY 35  27  27 GLY GLY C . n 
E 1 36  PRO 36  28  28 PRO PRO C . n 
E 1 37  VAL 37  29  29 VAL VAL C . n 
E 1 38  LYS 38  30  30 LYS LYS C . n 
E 1 39  VAL 39  31  31 VAL VAL C . n 
E 1 40  TRP 40  32  32 TRP TRP C . n 
E 1 41  GLY 41  33  33 GLY GLY C . n 
E 1 42  SER 42  34  34 SER SER C . n 
E 1 43  ILE 43  35  35 ILE ILE C . n 
E 1 44  LYS 44  36  36 LYS LYS C . n 
E 1 45  GLY 45  37  37 GLY GLY C . n 
E 1 46  LEU 46  38  38 LEU LEU C . n 
E 1 47  THR 47  39  39 THR THR C . n 
E 1 48  GLU 48  40  40 GLU GLU C . n 
E 1 49  GLY 49  41  41 GLY GLY C . n 
E 1 50  LEU 50  42  ?  ?   ?   C . n 
E 1 51  HIS 51  43  ?  ?   ?   C . n 
E 1 52  GLY 52  44  ?  ?   ?   C . n 
E 1 53  PHE 53  45  ?  ?   ?   C . n 
E 1 54  HIS 54  46  ?  ?   ?   C . n 
E 1 55  VAL 55  47  ?  ?   ?   C . n 
E 1 56  HIS 56  48  ?  ?   ?   C . n 
E 1 57  GLU 57  49  ?  ?   ?   C . n 
E 1 58  PHE 58  50  ?  ?   ?   C . n 
E 1 59  GLY 59  51  ?  ?   ?   C . n 
E 1 60  ASP 60  52  ?  ?   ?   C . n 
E 1 61  ASN 61  53  ?  ?   ?   C . n 
E 1 62  THR 62  54  ?  ?   ?   C . n 
E 1 63  ALA 63  55  ?  ?   ?   C . n 
E 1 64  GLY 64  56  ?  ?   ?   C . n 
E 1 65  CYS 65  57  ?  ?   ?   C . n 
E 1 66  THR 66  58  ?  ?   ?   C . n 
E 1 67  SER 67  59  ?  ?   ?   C . n 
E 1 68  ALA 68  60  ?  ?   ?   C . n 
E 1 69  GLY 69  61  ?  ?   ?   C . n 
E 1 70  PRO 70  62  ?  ?   ?   C . n 
E 1 71  HIS 71  63  ?  ?   ?   C . n 
E 1 72  PHE 72  64  ?  ?   ?   C . n 
E 1 73  ASN 73  65  ?  ?   ?   C . n 
E 1 74  PRO 74  66  ?  ?   ?   C . n 
E 1 75  LEU 75  67  ?  ?   ?   C . n 
E 1 76  SER 76  68  ?  ?   ?   C . n 
E 1 77  ARG 77  69  ?  ?   ?   C . n 
E 1 78  LYS 78  70  ?  ?   ?   C . n 
E 1 79  HIS 79  71  ?  ?   ?   C . n 
E 1 80  GLY 80  72  ?  ?   ?   C . n 
E 1 81  GLY 81  73  ?  ?   ?   C . n 
E 1 82  PRO 82  74  ?  ?   ?   C . n 
E 1 83  LYS 83  75  ?  ?   ?   C . n 
E 1 84  ASP 84  76  ?  ?   ?   C . n 
E 1 85  GLU 85  77  ?  ?   ?   C . n 
E 1 86  GLU 86  78  ?  ?   ?   C . n 
E 1 87  ARG 87  79  ?  ?   ?   C . n 
E 1 88  HIS 88  80  ?  ?   ?   C . n 
E 1 89  VAL 89  81  ?  ?   ?   C . n 
E 1 90  GLY 90  82  ?  ?   ?   C . n 
E 1 91  ASP 91  83  ?  ?   ?   C . n 
E 1 92  LEU 92  84  ?  ?   ?   C . n 
E 1 93  GLY 93  85  ?  ?   ?   C . n 
E 1 94  ASN 94  86  ?  ?   ?   C . n 
E 1 95  VAL 95  87  ?  ?   ?   C . n 
E 1 96  THR 96  88  ?  ?   ?   C . n 
E 1 97  ALA 97  89  ?  ?   ?   C . n 
E 1 98  ASP 98  90  ?  ?   ?   C . n 
E 1 99  LYS 99  91  ?  ?   ?   C . n 
E 1 100 ASP 100 92  ?  ?   ?   C . n 
E 1 101 GLY 101 93  ?  ?   ?   C . n 
E 1 102 VAL 102 94  ?  ?   ?   C . n 
E 1 103 ALA 103 95  ?  ?   ?   C . n 
E 1 104 ASP 104 96  ?  ?   ?   C . n 
E 1 105 VAL 105 97  ?  ?   ?   C . n 
E 1 106 SER 106 98  ?  ?   ?   C . n 
E 1 107 ILE 107 99  ?  ?   ?   C . n 
E 1 108 GLU 108 100 ?  ?   ?   C . n 
E 1 109 ASP 109 101 ?  ?   ?   C . n 
E 1 110 SER 110 102 ?  ?   ?   C . n 
E 1 111 VAL 111 103 ?  ?   ?   C . n 
E 1 112 ILE 112 104 ?  ?   ?   C . n 
E 1 113 SER 113 105 ?  ?   ?   C . n 
E 1 114 LEU 114 106 ?  ?   ?   C . n 
E 1 115 SER 115 107 ?  ?   ?   C . n 
E 1 116 GLY 116 108 ?  ?   ?   C . n 
E 1 117 ASP 117 109 ?  ?   ?   C . n 
E 1 118 HIS 118 110 ?  ?   ?   C . n 
E 1 119 ALA 119 111 ?  ?   ?   C . n 
E 1 120 ILE 120 112 ?  ?   ?   C . n 
E 1 121 ILE 121 113 ?  ?   ?   C . n 
E 1 122 GLY 122 114 ?  ?   ?   C . n 
E 1 123 ARG 123 115 ?  ?   ?   C . n 
E 1 124 THR 124 116 ?  ?   ?   C . n 
E 1 125 LEU 125 117 ?  ?   ?   C . n 
E 1 126 VAL 126 118 ?  ?   ?   C . n 
E 1 127 VAL 127 119 ?  ?   ?   C . n 
E 1 128 HIS 128 120 ?  ?   ?   C . n 
E 1 129 GLU 129 121 ?  ?   ?   C . n 
E 1 130 LYS 130 122 ?  ?   ?   C . n 
E 1 131 ALA 131 123 ?  ?   ?   C . n 
E 1 132 ASP 132 124 ?  ?   ?   C . n 
E 1 133 ASP 133 125 ?  ?   ?   C . n 
E 1 134 LEU 134 126 ?  ?   ?   C . n 
E 1 135 GLY 135 127 ?  ?   ?   C . n 
E 1 136 LYS 136 128 ?  ?   ?   C . n 
E 1 137 GLY 137 129 ?  ?   ?   C . n 
E 1 138 GLY 138 130 ?  ?   ?   C . n 
E 1 139 ASN 139 131 ?  ?   ?   C . n 
E 1 140 GLU 140 132 ?  ?   ?   C . n 
E 1 141 GLU 141 133 ?  ?   ?   C . n 
E 1 142 SER 142 134 ?  ?   ?   C . n 
E 1 143 THR 143 135 ?  ?   ?   C . n 
E 1 144 LYS 144 136 ?  ?   ?   C . n 
E 1 145 THR 145 137 ?  ?   ?   C . n 
E 1 146 GLY 146 138 ?  ?   ?   C . n 
E 1 147 ASN 147 139 ?  ?   ?   C . n 
E 1 148 ALA 148 140 ?  ?   ?   C . n 
E 1 149 GLY 149 141 ?  ?   ?   C . n 
E 1 150 SER 150 142 ?  ?   ?   C . n 
E 1 151 ARG 151 143 ?  ?   ?   C . n 
E 1 152 LEU 152 144 ?  ?   ?   C . n 
E 1 153 ALA 153 145 ?  ?   ?   C . n 
E 1 154 CYS 154 146 ?  ?   ?   C . n 
E 1 155 GLY 155 147 ?  ?   ?   C . n 
E 1 156 VAL 156 148 ?  ?   ?   C . n 
E 1 157 ILE 157 149 ?  ?   ?   C . n 
E 1 158 GLY 158 150 ?  ?   ?   C . n 
E 1 159 ILE 159 151 ?  ?   ?   C . n 
E 1 160 ALA 160 152 ?  ?   ?   C . n 
E 1 161 GLN 161 153 ?  ?   ?   C . n 
F 2 1   UNK 1   1   1  UNK UNK I . n 
F 2 2   UNK 2   2   2  UNK UNK I . n 
F 2 3   UNK 3   3   3  UNK UNK I . n 
F 2 4   UNK 4   4   4  UNK UNK I . n 
F 2 5   UNK 5   5   5  UNK UNK I . n 
F 2 6   UNK 6   6   6  UNK UNK I . n 
F 2 7   UNK 7   7   7  UNK UNK I . n 
F 2 8   UNK 8   8   8  UNK UNK I . n 
G 1 1   GLY 1   -7  ?  ?   ?   D . n 
G 1 2   ALA 2   -6  ?  ?   ?   D . n 
G 1 3   MET 3   -5  ?  ?   ?   D . n 
G 1 4   ASP 4   -4  ?  ?   ?   D . n 
G 1 5   PRO 5   -3  ?  ?   ?   D . n 
G 1 6   GLU 6   -2  ?  ?   ?   D . n 
G 1 7   PHE 7   -1  ?  ?   ?   D . n 
G 1 8   MET 8   0   ?  ?   ?   D . n 
G 1 9   ALA 9   1   1  ALA ALA D . n 
G 1 10  THR 10  2   2  THR THR D . n 
G 1 11  LYS 11  3   3  LYS LYS D . n 
G 1 12  ALA 12  4   4  ALA ALA D . n 
G 1 13  VAL 13  5   5  VAL VAL D . n 
G 1 14  ALA 14  6   6  ALA ALA D . n 
G 1 15  VAL 15  7   7  VAL VAL D . n 
G 1 16  LEU 16  8   8  LEU LEU D . n 
G 1 17  LYS 17  9   9  LYS LYS D . n 
G 1 18  GLY 18  10  10 GLY GLY D . n 
G 1 19  ASP 19  11  11 ASP ASP D . n 
G 1 20  GLY 20  12  12 GLY GLY D . n 
G 1 21  PRO 21  13  13 PRO PRO D . n 
G 1 22  VAL 22  14  14 VAL VAL D . n 
G 1 23  GLN 23  15  15 GLN GLN D . n 
G 1 24  GLY 24  16  16 GLY GLY D . n 
G 1 25  ILE 25  17  17 ILE ILE D . n 
G 1 26  ILE 26  18  18 ILE ILE D . n 
G 1 27  ASN 27  19  19 ASN ASN D . n 
G 1 28  PHE 28  20  20 PHE PHE D . n 
G 1 29  GLU 29  21  21 GLU GLU D . n 
G 1 30  GLN 30  22  22 GLN GLN D . n 
G 1 31  LYS 31  23  23 LYS LYS D . n 
G 1 32  GLU 32  24  24 GLU GLU D . n 
G 1 33  SER 33  25  25 SER SER D . n 
G 1 34  ASN 34  26  26 ASN ASN D . n 
G 1 35  GLY 35  27  27 GLY GLY D . n 
G 1 36  PRO 36  28  28 PRO PRO D . n 
G 1 37  VAL 37  29  29 VAL VAL D . n 
G 1 38  LYS 38  30  30 LYS LYS D . n 
G 1 39  VAL 39  31  31 VAL VAL D . n 
G 1 40  TRP 40  32  32 TRP TRP D . n 
G 1 41  GLY 41  33  33 GLY GLY D . n 
G 1 42  SER 42  34  34 SER SER D . n 
G 1 43  ILE 43  35  35 ILE ILE D . n 
G 1 44  LYS 44  36  36 LYS LYS D . n 
G 1 45  GLY 45  37  37 GLY GLY D . n 
G 1 46  LEU 46  38  38 LEU LEU D . n 
G 1 47  THR 47  39  39 THR THR D . n 
G 1 48  GLU 48  40  40 GLU GLU D . n 
G 1 49  GLY 49  41  41 GLY GLY D . n 
G 1 50  LEU 50  42  ?  ?   ?   D . n 
G 1 51  HIS 51  43  ?  ?   ?   D . n 
G 1 52  GLY 52  44  ?  ?   ?   D . n 
G 1 53  PHE 53  45  ?  ?   ?   D . n 
G 1 54  HIS 54  46  ?  ?   ?   D . n 
G 1 55  VAL 55  47  ?  ?   ?   D . n 
G 1 56  HIS 56  48  ?  ?   ?   D . n 
G 1 57  GLU 57  49  ?  ?   ?   D . n 
G 1 58  PHE 58  50  ?  ?   ?   D . n 
G 1 59  GLY 59  51  ?  ?   ?   D . n 
G 1 60  ASP 60  52  ?  ?   ?   D . n 
G 1 61  ASN 61  53  ?  ?   ?   D . n 
G 1 62  THR 62  54  ?  ?   ?   D . n 
G 1 63  ALA 63  55  ?  ?   ?   D . n 
G 1 64  GLY 64  56  ?  ?   ?   D . n 
G 1 65  CYS 65  57  ?  ?   ?   D . n 
G 1 66  THR 66  58  ?  ?   ?   D . n 
G 1 67  SER 67  59  ?  ?   ?   D . n 
G 1 68  ALA 68  60  ?  ?   ?   D . n 
G 1 69  GLY 69  61  ?  ?   ?   D . n 
G 1 70  PRO 70  62  ?  ?   ?   D . n 
G 1 71  HIS 71  63  ?  ?   ?   D . n 
G 1 72  PHE 72  64  ?  ?   ?   D . n 
G 1 73  ASN 73  65  ?  ?   ?   D . n 
G 1 74  PRO 74  66  ?  ?   ?   D . n 
G 1 75  LEU 75  67  ?  ?   ?   D . n 
G 1 76  SER 76  68  ?  ?   ?   D . n 
G 1 77  ARG 77  69  ?  ?   ?   D . n 
G 1 78  LYS 78  70  ?  ?   ?   D . n 
G 1 79  HIS 79  71  ?  ?   ?   D . n 
G 1 80  GLY 80  72  ?  ?   ?   D . n 
G 1 81  GLY 81  73  ?  ?   ?   D . n 
G 1 82  PRO 82  74  ?  ?   ?   D . n 
G 1 83  LYS 83  75  ?  ?   ?   D . n 
G 1 84  ASP 84  76  ?  ?   ?   D . n 
G 1 85  GLU 85  77  ?  ?   ?   D . n 
G 1 86  GLU 86  78  ?  ?   ?   D . n 
G 1 87  ARG 87  79  ?  ?   ?   D . n 
G 1 88  HIS 88  80  ?  ?   ?   D . n 
G 1 89  VAL 89  81  ?  ?   ?   D . n 
G 1 90  GLY 90  82  ?  ?   ?   D . n 
G 1 91  ASP 91  83  ?  ?   ?   D . n 
G 1 92  LEU 92  84  ?  ?   ?   D . n 
G 1 93  GLY 93  85  ?  ?   ?   D . n 
G 1 94  ASN 94  86  ?  ?   ?   D . n 
G 1 95  VAL 95  87  ?  ?   ?   D . n 
G 1 96  THR 96  88  ?  ?   ?   D . n 
G 1 97  ALA 97  89  ?  ?   ?   D . n 
G 1 98  ASP 98  90  ?  ?   ?   D . n 
G 1 99  LYS 99  91  ?  ?   ?   D . n 
G 1 100 ASP 100 92  ?  ?   ?   D . n 
G 1 101 GLY 101 93  ?  ?   ?   D . n 
G 1 102 VAL 102 94  ?  ?   ?   D . n 
G 1 103 ALA 103 95  ?  ?   ?   D . n 
G 1 104 ASP 104 96  ?  ?   ?   D . n 
G 1 105 VAL 105 97  ?  ?   ?   D . n 
G 1 106 SER 106 98  ?  ?   ?   D . n 
G 1 107 ILE 107 99  ?  ?   ?   D . n 
G 1 108 GLU 108 100 ?  ?   ?   D . n 
G 1 109 ASP 109 101 ?  ?   ?   D . n 
G 1 110 SER 110 102 ?  ?   ?   D . n 
G 1 111 VAL 111 103 ?  ?   ?   D . n 
G 1 112 ILE 112 104 ?  ?   ?   D . n 
G 1 113 SER 113 105 ?  ?   ?   D . n 
G 1 114 LEU 114 106 ?  ?   ?   D . n 
G 1 115 SER 115 107 ?  ?   ?   D . n 
G 1 116 GLY 116 108 ?  ?   ?   D . n 
G 1 117 ASP 117 109 ?  ?   ?   D . n 
G 1 118 HIS 118 110 ?  ?   ?   D . n 
G 1 119 ALA 119 111 ?  ?   ?   D . n 
G 1 120 ILE 120 112 ?  ?   ?   D . n 
G 1 121 ILE 121 113 ?  ?   ?   D . n 
G 1 122 GLY 122 114 ?  ?   ?   D . n 
G 1 123 ARG 123 115 ?  ?   ?   D . n 
G 1 124 THR 124 116 ?  ?   ?   D . n 
G 1 125 LEU 125 117 ?  ?   ?   D . n 
G 1 126 VAL 126 118 ?  ?   ?   D . n 
G 1 127 VAL 127 119 ?  ?   ?   D . n 
G 1 128 HIS 128 120 ?  ?   ?   D . n 
G 1 129 GLU 129 121 ?  ?   ?   D . n 
G 1 130 LYS 130 122 ?  ?   ?   D . n 
G 1 131 ALA 131 123 ?  ?   ?   D . n 
G 1 132 ASP 132 124 ?  ?   ?   D . n 
G 1 133 ASP 133 125 ?  ?   ?   D . n 
G 1 134 LEU 134 126 ?  ?   ?   D . n 
G 1 135 GLY 135 127 ?  ?   ?   D . n 
G 1 136 LYS 136 128 ?  ?   ?   D . n 
G 1 137 GLY 137 129 ?  ?   ?   D . n 
G 1 138 GLY 138 130 ?  ?   ?   D . n 
G 1 139 ASN 139 131 ?  ?   ?   D . n 
G 1 140 GLU 140 132 ?  ?   ?   D . n 
G 1 141 GLU 141 133 ?  ?   ?   D . n 
G 1 142 SER 142 134 ?  ?   ?   D . n 
G 1 143 THR 143 135 ?  ?   ?   D . n 
G 1 144 LYS 144 136 ?  ?   ?   D . n 
G 1 145 THR 145 137 ?  ?   ?   D . n 
G 1 146 GLY 146 138 ?  ?   ?   D . n 
G 1 147 ASN 147 139 ?  ?   ?   D . n 
G 1 148 ALA 148 140 ?  ?   ?   D . n 
G 1 149 GLY 149 141 ?  ?   ?   D . n 
G 1 150 SER 150 142 ?  ?   ?   D . n 
G 1 151 ARG 151 143 ?  ?   ?   D . n 
G 1 152 LEU 152 144 ?  ?   ?   D . n 
G 1 153 ALA 153 145 ?  ?   ?   D . n 
G 1 154 CYS 154 146 ?  ?   ?   D . n 
G 1 155 GLY 155 147 ?  ?   ?   D . n 
G 1 156 VAL 156 148 ?  ?   ?   D . n 
G 1 157 ILE 157 149 ?  ?   ?   D . n 
G 1 158 GLY 158 150 ?  ?   ?   D . n 
G 1 159 ILE 159 151 ?  ?   ?   D . n 
G 1 160 ALA 160 152 ?  ?   ?   D . n 
G 1 161 GLN 161 153 ?  ?   ?   D . n 
H 2 1   UNK 1   1   1  UNK UNK J . n 
H 2 2   UNK 2   2   2  UNK UNK J . n 
H 2 3   UNK 3   3   3  UNK UNK J . n 
H 2 4   UNK 4   4   4  UNK UNK J . n 
H 2 5   UNK 5   5   5  UNK UNK J . n 
H 2 6   UNK 6   6   6  UNK UNK J . n 
H 2 7   UNK 7   7   7  UNK UNK J . n 
H 2 8   UNK 8   8   8  UNK UNK J . n 
I 1 1   GLY 1   -7  ?  ?   ?   E . n 
I 1 2   ALA 2   -6  ?  ?   ?   E . n 
I 1 3   MET 3   -5  ?  ?   ?   E . n 
I 1 4   ASP 4   -4  ?  ?   ?   E . n 
I 1 5   PRO 5   -3  ?  ?   ?   E . n 
I 1 6   GLU 6   -2  ?  ?   ?   E . n 
I 1 7   PHE 7   -1  ?  ?   ?   E . n 
I 1 8   MET 8   0   ?  ?   ?   E . n 
I 1 9   ALA 9   1   1  ALA ALA E . n 
I 1 10  THR 10  2   2  THR THR E . n 
I 1 11  LYS 11  3   3  LYS LYS E . n 
I 1 12  ALA 12  4   4  ALA ALA E . n 
I 1 13  VAL 13  5   5  VAL VAL E . n 
I 1 14  ALA 14  6   6  ALA ALA E . n 
I 1 15  VAL 15  7   7  VAL VAL E . n 
I 1 16  LEU 16  8   8  LEU LEU E . n 
I 1 17  LYS 17  9   9  LYS LYS E . n 
I 1 18  GLY 18  10  10 GLY GLY E . n 
I 1 19  ASP 19  11  11 ASP ASP E . n 
I 1 20  GLY 20  12  12 GLY GLY E . n 
I 1 21  PRO 21  13  13 PRO PRO E . n 
I 1 22  VAL 22  14  14 VAL VAL E . n 
I 1 23  GLN 23  15  15 GLN GLN E . n 
I 1 24  GLY 24  16  16 GLY GLY E . n 
I 1 25  ILE 25  17  17 ILE ILE E . n 
I 1 26  ILE 26  18  18 ILE ILE E . n 
I 1 27  ASN 27  19  19 ASN ASN E . n 
I 1 28  PHE 28  20  20 PHE PHE E . n 
I 1 29  GLU 29  21  21 GLU GLU E . n 
I 1 30  GLN 30  22  22 GLN GLN E . n 
I 1 31  LYS 31  23  23 LYS LYS E . n 
I 1 32  GLU 32  24  24 GLU GLU E . n 
I 1 33  SER 33  25  25 SER SER E . n 
I 1 34  ASN 34  26  26 ASN ASN E . n 
I 1 35  GLY 35  27  27 GLY GLY E . n 
I 1 36  PRO 36  28  28 PRO PRO E . n 
I 1 37  VAL 37  29  29 VAL VAL E . n 
I 1 38  LYS 38  30  30 LYS LYS E . n 
I 1 39  VAL 39  31  31 VAL VAL E . n 
I 1 40  TRP 40  32  32 TRP TRP E . n 
I 1 41  GLY 41  33  33 GLY GLY E . n 
I 1 42  SER 42  34  34 SER SER E . n 
I 1 43  ILE 43  35  35 ILE ILE E . n 
I 1 44  LYS 44  36  36 LYS LYS E . n 
I 1 45  GLY 45  37  37 GLY GLY E . n 
I 1 46  LEU 46  38  38 LEU LEU E . n 
I 1 47  THR 47  39  39 THR THR E . n 
I 1 48  GLU 48  40  40 GLU GLU E . n 
I 1 49  GLY 49  41  41 GLY GLY E . n 
I 1 50  LEU 50  42  ?  ?   ?   E . n 
I 1 51  HIS 51  43  ?  ?   ?   E . n 
I 1 52  GLY 52  44  ?  ?   ?   E . n 
I 1 53  PHE 53  45  ?  ?   ?   E . n 
I 1 54  HIS 54  46  ?  ?   ?   E . n 
I 1 55  VAL 55  47  ?  ?   ?   E . n 
I 1 56  HIS 56  48  ?  ?   ?   E . n 
I 1 57  GLU 57  49  ?  ?   ?   E . n 
I 1 58  PHE 58  50  ?  ?   ?   E . n 
I 1 59  GLY 59  51  ?  ?   ?   E . n 
I 1 60  ASP 60  52  ?  ?   ?   E . n 
I 1 61  ASN 61  53  ?  ?   ?   E . n 
I 1 62  THR 62  54  ?  ?   ?   E . n 
I 1 63  ALA 63  55  ?  ?   ?   E . n 
I 1 64  GLY 64  56  ?  ?   ?   E . n 
I 1 65  CYS 65  57  ?  ?   ?   E . n 
I 1 66  THR 66  58  ?  ?   ?   E . n 
I 1 67  SER 67  59  ?  ?   ?   E . n 
I 1 68  ALA 68  60  ?  ?   ?   E . n 
I 1 69  GLY 69  61  ?  ?   ?   E . n 
I 1 70  PRO 70  62  ?  ?   ?   E . n 
I 1 71  HIS 71  63  ?  ?   ?   E . n 
I 1 72  PHE 72  64  ?  ?   ?   E . n 
I 1 73  ASN 73  65  ?  ?   ?   E . n 
I 1 74  PRO 74  66  ?  ?   ?   E . n 
I 1 75  LEU 75  67  ?  ?   ?   E . n 
I 1 76  SER 76  68  ?  ?   ?   E . n 
I 1 77  ARG 77  69  ?  ?   ?   E . n 
I 1 78  LYS 78  70  ?  ?   ?   E . n 
I 1 79  HIS 79  71  ?  ?   ?   E . n 
I 1 80  GLY 80  72  ?  ?   ?   E . n 
I 1 81  GLY 81  73  ?  ?   ?   E . n 
I 1 82  PRO 82  74  ?  ?   ?   E . n 
I 1 83  LYS 83  75  ?  ?   ?   E . n 
I 1 84  ASP 84  76  ?  ?   ?   E . n 
I 1 85  GLU 85  77  ?  ?   ?   E . n 
I 1 86  GLU 86  78  ?  ?   ?   E . n 
I 1 87  ARG 87  79  ?  ?   ?   E . n 
I 1 88  HIS 88  80  ?  ?   ?   E . n 
I 1 89  VAL 89  81  ?  ?   ?   E . n 
I 1 90  GLY 90  82  ?  ?   ?   E . n 
I 1 91  ASP 91  83  ?  ?   ?   E . n 
I 1 92  LEU 92  84  ?  ?   ?   E . n 
I 1 93  GLY 93  85  ?  ?   ?   E . n 
I 1 94  ASN 94  86  ?  ?   ?   E . n 
I 1 95  VAL 95  87  ?  ?   ?   E . n 
I 1 96  THR 96  88  ?  ?   ?   E . n 
I 1 97  ALA 97  89  ?  ?   ?   E . n 
I 1 98  ASP 98  90  ?  ?   ?   E . n 
I 1 99  LYS 99  91  ?  ?   ?   E . n 
I 1 100 ASP 100 92  ?  ?   ?   E . n 
I 1 101 GLY 101 93  ?  ?   ?   E . n 
I 1 102 VAL 102 94  ?  ?   ?   E . n 
I 1 103 ALA 103 95  ?  ?   ?   E . n 
I 1 104 ASP 104 96  ?  ?   ?   E . n 
I 1 105 VAL 105 97  ?  ?   ?   E . n 
I 1 106 SER 106 98  ?  ?   ?   E . n 
I 1 107 ILE 107 99  ?  ?   ?   E . n 
I 1 108 GLU 108 100 ?  ?   ?   E . n 
I 1 109 ASP 109 101 ?  ?   ?   E . n 
I 1 110 SER 110 102 ?  ?   ?   E . n 
I 1 111 VAL 111 103 ?  ?   ?   E . n 
I 1 112 ILE 112 104 ?  ?   ?   E . n 
I 1 113 SER 113 105 ?  ?   ?   E . n 
I 1 114 LEU 114 106 ?  ?   ?   E . n 
I 1 115 SER 115 107 ?  ?   ?   E . n 
I 1 116 GLY 116 108 ?  ?   ?   E . n 
I 1 117 ASP 117 109 ?  ?   ?   E . n 
I 1 118 HIS 118 110 ?  ?   ?   E . n 
I 1 119 ALA 119 111 ?  ?   ?   E . n 
I 1 120 ILE 120 112 ?  ?   ?   E . n 
I 1 121 ILE 121 113 ?  ?   ?   E . n 
I 1 122 GLY 122 114 ?  ?   ?   E . n 
I 1 123 ARG 123 115 ?  ?   ?   E . n 
I 1 124 THR 124 116 ?  ?   ?   E . n 
I 1 125 LEU 125 117 ?  ?   ?   E . n 
I 1 126 VAL 126 118 ?  ?   ?   E . n 
I 1 127 VAL 127 119 ?  ?   ?   E . n 
I 1 128 HIS 128 120 ?  ?   ?   E . n 
I 1 129 GLU 129 121 ?  ?   ?   E . n 
I 1 130 LYS 130 122 ?  ?   ?   E . n 
I 1 131 ALA 131 123 ?  ?   ?   E . n 
I 1 132 ASP 132 124 ?  ?   ?   E . n 
I 1 133 ASP 133 125 ?  ?   ?   E . n 
I 1 134 LEU 134 126 ?  ?   ?   E . n 
I 1 135 GLY 135 127 ?  ?   ?   E . n 
I 1 136 LYS 136 128 ?  ?   ?   E . n 
I 1 137 GLY 137 129 ?  ?   ?   E . n 
I 1 138 GLY 138 130 ?  ?   ?   E . n 
I 1 139 ASN 139 131 ?  ?   ?   E . n 
I 1 140 GLU 140 132 ?  ?   ?   E . n 
I 1 141 GLU 141 133 ?  ?   ?   E . n 
I 1 142 SER 142 134 ?  ?   ?   E . n 
I 1 143 THR 143 135 ?  ?   ?   E . n 
I 1 144 LYS 144 136 ?  ?   ?   E . n 
I 1 145 THR 145 137 ?  ?   ?   E . n 
I 1 146 GLY 146 138 ?  ?   ?   E . n 
I 1 147 ASN 147 139 ?  ?   ?   E . n 
I 1 148 ALA 148 140 ?  ?   ?   E . n 
I 1 149 GLY 149 141 ?  ?   ?   E . n 
I 1 150 SER 150 142 ?  ?   ?   E . n 
I 1 151 ARG 151 143 ?  ?   ?   E . n 
I 1 152 LEU 152 144 ?  ?   ?   E . n 
I 1 153 ALA 153 145 ?  ?   ?   E . n 
I 1 154 CYS 154 146 ?  ?   ?   E . n 
I 1 155 GLY 155 147 ?  ?   ?   E . n 
I 1 156 VAL 156 148 ?  ?   ?   E . n 
I 1 157 ILE 157 149 ?  ?   ?   E . n 
I 1 158 GLY 158 150 ?  ?   ?   E . n 
I 1 159 ILE 159 151 ?  ?   ?   E . n 
I 1 160 ALA 160 152 ?  ?   ?   E . n 
I 1 161 GLN 161 153 ?  ?   ?   E . n 
J 2 1   UNK 1   1   1  UNK UNK K . n 
J 2 2   UNK 2   2   2  UNK UNK K . n 
J 2 3   UNK 3   3   3  UNK UNK K . n 
J 2 4   UNK 4   4   4  UNK UNK K . n 
J 2 5   UNK 5   5   5  UNK UNK K . n 
J 2 6   UNK 6   6   6  UNK UNK K . n 
J 2 7   UNK 7   7   7  UNK UNK K . n 
J 2 8   UNK 8   8   8  UNK UNK K . n 
K 1 1   GLY 1   -7  ?  ?   ?   F . n 
K 1 2   ALA 2   -6  ?  ?   ?   F . n 
K 1 3   MET 3   -5  ?  ?   ?   F . n 
K 1 4   ASP 4   -4  ?  ?   ?   F . n 
K 1 5   PRO 5   -3  ?  ?   ?   F . n 
K 1 6   GLU 6   -2  ?  ?   ?   F . n 
K 1 7   PHE 7   -1  ?  ?   ?   F . n 
K 1 8   MET 8   0   ?  ?   ?   F . n 
K 1 9   ALA 9   1   1  ALA ALA F . n 
K 1 10  THR 10  2   2  THR THR F . n 
K 1 11  LYS 11  3   3  LYS LYS F . n 
K 1 12  ALA 12  4   4  ALA ALA F . n 
K 1 13  VAL 13  5   5  VAL VAL F . n 
K 1 14  ALA 14  6   6  ALA ALA F . n 
K 1 15  VAL 15  7   7  VAL VAL F . n 
K 1 16  LEU 16  8   8  LEU LEU F . n 
K 1 17  LYS 17  9   9  LYS LYS F . n 
K 1 18  GLY 18  10  10 GLY GLY F . n 
K 1 19  ASP 19  11  11 ASP ASP F . n 
K 1 20  GLY 20  12  12 GLY GLY F . n 
K 1 21  PRO 21  13  13 PRO PRO F . n 
K 1 22  VAL 22  14  14 VAL VAL F . n 
K 1 23  GLN 23  15  15 GLN GLN F . n 
K 1 24  GLY 24  16  16 GLY GLY F . n 
K 1 25  ILE 25  17  17 ILE ILE F . n 
K 1 26  ILE 26  18  18 ILE ILE F . n 
K 1 27  ASN 27  19  19 ASN ASN F . n 
K 1 28  PHE 28  20  20 PHE PHE F . n 
K 1 29  GLU 29  21  21 GLU GLU F . n 
K 1 30  GLN 30  22  22 GLN GLN F . n 
K 1 31  LYS 31  23  23 LYS LYS F . n 
K 1 32  GLU 32  24  24 GLU GLU F . n 
K 1 33  SER 33  25  25 SER SER F . n 
K 1 34  ASN 34  26  26 ASN ASN F . n 
K 1 35  GLY 35  27  27 GLY GLY F . n 
K 1 36  PRO 36  28  28 PRO PRO F . n 
K 1 37  VAL 37  29  29 VAL VAL F . n 
K 1 38  LYS 38  30  30 LYS LYS F . n 
K 1 39  VAL 39  31  31 VAL VAL F . n 
K 1 40  TRP 40  32  32 TRP TRP F . n 
K 1 41  GLY 41  33  33 GLY GLY F . n 
K 1 42  SER 42  34  34 SER SER F . n 
K 1 43  ILE 43  35  35 ILE ILE F . n 
K 1 44  LYS 44  36  36 LYS LYS F . n 
K 1 45  GLY 45  37  37 GLY GLY F . n 
K 1 46  LEU 46  38  38 LEU LEU F . n 
K 1 47  THR 47  39  39 THR THR F . n 
K 1 48  GLU 48  40  40 GLU GLU F . n 
K 1 49  GLY 49  41  41 GLY GLY F . n 
K 1 50  LEU 50  42  ?  ?   ?   F . n 
K 1 51  HIS 51  43  ?  ?   ?   F . n 
K 1 52  GLY 52  44  ?  ?   ?   F . n 
K 1 53  PHE 53  45  ?  ?   ?   F . n 
K 1 54  HIS 54  46  ?  ?   ?   F . n 
K 1 55  VAL 55  47  ?  ?   ?   F . n 
K 1 56  HIS 56  48  ?  ?   ?   F . n 
K 1 57  GLU 57  49  ?  ?   ?   F . n 
K 1 58  PHE 58  50  ?  ?   ?   F . n 
K 1 59  GLY 59  51  ?  ?   ?   F . n 
K 1 60  ASP 60  52  ?  ?   ?   F . n 
K 1 61  ASN 61  53  ?  ?   ?   F . n 
K 1 62  THR 62  54  ?  ?   ?   F . n 
K 1 63  ALA 63  55  ?  ?   ?   F . n 
K 1 64  GLY 64  56  ?  ?   ?   F . n 
K 1 65  CYS 65  57  ?  ?   ?   F . n 
K 1 66  THR 66  58  ?  ?   ?   F . n 
K 1 67  SER 67  59  ?  ?   ?   F . n 
K 1 68  ALA 68  60  ?  ?   ?   F . n 
K 1 69  GLY 69  61  ?  ?   ?   F . n 
K 1 70  PRO 70  62  ?  ?   ?   F . n 
K 1 71  HIS 71  63  ?  ?   ?   F . n 
K 1 72  PHE 72  64  ?  ?   ?   F . n 
K 1 73  ASN 73  65  ?  ?   ?   F . n 
K 1 74  PRO 74  66  ?  ?   ?   F . n 
K 1 75  LEU 75  67  ?  ?   ?   F . n 
K 1 76  SER 76  68  ?  ?   ?   F . n 
K 1 77  ARG 77  69  ?  ?   ?   F . n 
K 1 78  LYS 78  70  ?  ?   ?   F . n 
K 1 79  HIS 79  71  ?  ?   ?   F . n 
K 1 80  GLY 80  72  ?  ?   ?   F . n 
K 1 81  GLY 81  73  ?  ?   ?   F . n 
K 1 82  PRO 82  74  ?  ?   ?   F . n 
K 1 83  LYS 83  75  ?  ?   ?   F . n 
K 1 84  ASP 84  76  ?  ?   ?   F . n 
K 1 85  GLU 85  77  ?  ?   ?   F . n 
K 1 86  GLU 86  78  ?  ?   ?   F . n 
K 1 87  ARG 87  79  ?  ?   ?   F . n 
K 1 88  HIS 88  80  ?  ?   ?   F . n 
K 1 89  VAL 89  81  ?  ?   ?   F . n 
K 1 90  GLY 90  82  ?  ?   ?   F . n 
K 1 91  ASP 91  83  ?  ?   ?   F . n 
K 1 92  LEU 92  84  ?  ?   ?   F . n 
K 1 93  GLY 93  85  ?  ?   ?   F . n 
K 1 94  ASN 94  86  ?  ?   ?   F . n 
K 1 95  VAL 95  87  ?  ?   ?   F . n 
K 1 96  THR 96  88  ?  ?   ?   F . n 
K 1 97  ALA 97  89  ?  ?   ?   F . n 
K 1 98  ASP 98  90  ?  ?   ?   F . n 
K 1 99  LYS 99  91  ?  ?   ?   F . n 
K 1 100 ASP 100 92  ?  ?   ?   F . n 
K 1 101 GLY 101 93  ?  ?   ?   F . n 
K 1 102 VAL 102 94  ?  ?   ?   F . n 
K 1 103 ALA 103 95  ?  ?   ?   F . n 
K 1 104 ASP 104 96  ?  ?   ?   F . n 
K 1 105 VAL 105 97  ?  ?   ?   F . n 
K 1 106 SER 106 98  ?  ?   ?   F . n 
K 1 107 ILE 107 99  ?  ?   ?   F . n 
K 1 108 GLU 108 100 ?  ?   ?   F . n 
K 1 109 ASP 109 101 ?  ?   ?   F . n 
K 1 110 SER 110 102 ?  ?   ?   F . n 
K 1 111 VAL 111 103 ?  ?   ?   F . n 
K 1 112 ILE 112 104 ?  ?   ?   F . n 
K 1 113 SER 113 105 ?  ?   ?   F . n 
K 1 114 LEU 114 106 ?  ?   ?   F . n 
K 1 115 SER 115 107 ?  ?   ?   F . n 
K 1 116 GLY 116 108 ?  ?   ?   F . n 
K 1 117 ASP 117 109 ?  ?   ?   F . n 
K 1 118 HIS 118 110 ?  ?   ?   F . n 
K 1 119 ALA 119 111 ?  ?   ?   F . n 
K 1 120 ILE 120 112 ?  ?   ?   F . n 
K 1 121 ILE 121 113 ?  ?   ?   F . n 
K 1 122 GLY 122 114 ?  ?   ?   F . n 
K 1 123 ARG 123 115 ?  ?   ?   F . n 
K 1 124 THR 124 116 ?  ?   ?   F . n 
K 1 125 LEU 125 117 ?  ?   ?   F . n 
K 1 126 VAL 126 118 ?  ?   ?   F . n 
K 1 127 VAL 127 119 ?  ?   ?   F . n 
K 1 128 HIS 128 120 ?  ?   ?   F . n 
K 1 129 GLU 129 121 ?  ?   ?   F . n 
K 1 130 LYS 130 122 ?  ?   ?   F . n 
K 1 131 ALA 131 123 ?  ?   ?   F . n 
K 1 132 ASP 132 124 ?  ?   ?   F . n 
K 1 133 ASP 133 125 ?  ?   ?   F . n 
K 1 134 LEU 134 126 ?  ?   ?   F . n 
K 1 135 GLY 135 127 ?  ?   ?   F . n 
K 1 136 LYS 136 128 ?  ?   ?   F . n 
K 1 137 GLY 137 129 ?  ?   ?   F . n 
K 1 138 GLY 138 130 ?  ?   ?   F . n 
K 1 139 ASN 139 131 ?  ?   ?   F . n 
K 1 140 GLU 140 132 ?  ?   ?   F . n 
K 1 141 GLU 141 133 ?  ?   ?   F . n 
K 1 142 SER 142 134 ?  ?   ?   F . n 
K 1 143 THR 143 135 ?  ?   ?   F . n 
K 1 144 LYS 144 136 ?  ?   ?   F . n 
K 1 145 THR 145 137 ?  ?   ?   F . n 
K 1 146 GLY 146 138 ?  ?   ?   F . n 
K 1 147 ASN 147 139 ?  ?   ?   F . n 
K 1 148 ALA 148 140 ?  ?   ?   F . n 
K 1 149 GLY 149 141 ?  ?   ?   F . n 
K 1 150 SER 150 142 ?  ?   ?   F . n 
K 1 151 ARG 151 143 ?  ?   ?   F . n 
K 1 152 LEU 152 144 ?  ?   ?   F . n 
K 1 153 ALA 153 145 ?  ?   ?   F . n 
K 1 154 CYS 154 146 ?  ?   ?   F . n 
K 1 155 GLY 155 147 ?  ?   ?   F . n 
K 1 156 VAL 156 148 ?  ?   ?   F . n 
K 1 157 ILE 157 149 ?  ?   ?   F . n 
K 1 158 GLY 158 150 ?  ?   ?   F . n 
K 1 159 ILE 159 151 ?  ?   ?   F . n 
K 1 160 ALA 160 152 ?  ?   ?   F . n 
K 1 161 GLN 161 153 ?  ?   ?   F . n 
L 2 1   UNK 1   1   1  UNK UNK L . n 
L 2 2   UNK 2   2   2  UNK UNK L . n 
L 2 3   UNK 3   3   3  UNK UNK L . n 
L 2 4   UNK 4   4   4  UNK UNK L . n 
L 2 5   UNK 5   5   5  UNK UNK L . n 
L 2 6   UNK 6   6   6  UNK UNK L . n 
L 2 7   UNK 7   7   7  UNK UNK L . n 
L 2 8   UNK 8   8   8  UNK UNK L . 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                     9JBP 
_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                         9JBP 
_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                   9JBP 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9JBP 
_struct.title                        'Cryo-EM structure of human SOD1 (C6A/C111A) 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        9JBP 
_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 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 1 ? 
F N N 2 ? 
G N N 1 ? 
H N N 2 ? 
I N N 1 ? 
J N N 2 ? 
K N N 1 ? 
L N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SODC_HUMAN P00441 ? 1 
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
1 
2 PDB 9JBP       9JBP   ? 2 ? 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 9JBP A 8 ? 161 ? P00441 1 ? 154 ? 0 153 
2  2 9JBP G 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
3  1 9JBP B 8 ? 161 ? P00441 1 ? 154 ? 0 153 
4  2 9JBP H 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
5  1 9JBP C 8 ? 161 ? P00441 1 ? 154 ? 0 153 
6  2 9JBP I 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
7  1 9JBP D 8 ? 161 ? P00441 1 ? 154 ? 0 153 
8  2 9JBP J 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
9  1 9JBP E 8 ? 161 ? P00441 1 ? 154 ? 0 153 
10 2 9JBP K 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
11 1 9JBP F 8 ? 161 ? P00441 1 ? 154 ? 0 153 
12 2 9JBP L 1 ? 8   ? 9JBP   1 ? 8   ? 1 8   
# 
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  9JBP GLY A 1   ? UNP P00441 ?   ?   'expression tag'      -7  1  
1  9JBP ALA A 2   ? UNP P00441 ?   ?   'expression tag'      -6  2  
1  9JBP MET A 3   ? UNP P00441 ?   ?   'expression tag'      -5  3  
1  9JBP ASP A 4   ? UNP P00441 ?   ?   'expression tag'      -4  4  
1  9JBP PRO A 5   ? UNP P00441 ?   ?   'expression tag'      -3  5  
1  9JBP GLU A 6   ? UNP P00441 ?   ?   'expression tag'      -2  6  
1  9JBP PHE A 7   ? UNP P00441 ?   ?   'expression tag'      -1  7  
1  9JBP ALA A 14  ? UNP P00441 CYS 7   'engineered mutation' 6   8  
1  9JBP ALA A 119 ? UNP P00441 CYS 112 'engineered mutation' 111 9  
3  9JBP GLY B 1   ? UNP P00441 ?   ?   'expression tag'      -7  10 
3  9JBP ALA B 2   ? UNP P00441 ?   ?   'expression tag'      -6  11 
3  9JBP MET B 3   ? UNP P00441 ?   ?   'expression tag'      -5  12 
3  9JBP ASP B 4   ? UNP P00441 ?   ?   'expression tag'      -4  13 
3  9JBP PRO B 5   ? UNP P00441 ?   ?   'expression tag'      -3  14 
3  9JBP GLU B 6   ? UNP P00441 ?   ?   'expression tag'      -2  15 
3  9JBP PHE B 7   ? UNP P00441 ?   ?   'expression tag'      -1  16 
3  9JBP ALA B 14  ? UNP P00441 CYS 7   'engineered mutation' 6   17 
3  9JBP ALA B 119 ? UNP P00441 CYS 112 'engineered mutation' 111 18 
5  9JBP GLY C 1   ? UNP P00441 ?   ?   'expression tag'      -7  19 
5  9JBP ALA C 2   ? UNP P00441 ?   ?   'expression tag'      -6  20 
5  9JBP MET C 3   ? UNP P00441 ?   ?   'expression tag'      -5  21 
5  9JBP ASP C 4   ? UNP P00441 ?   ?   'expression tag'      -4  22 
5  9JBP PRO C 5   ? UNP P00441 ?   ?   'expression tag'      -3  23 
5  9JBP GLU C 6   ? UNP P00441 ?   ?   'expression tag'      -2  24 
5  9JBP PHE C 7   ? UNP P00441 ?   ?   'expression tag'      -1  25 
5  9JBP ALA C 14  ? UNP P00441 CYS 7   'engineered mutation' 6   26 
5  9JBP ALA C 119 ? UNP P00441 CYS 112 'engineered mutation' 111 27 
7  9JBP GLY D 1   ? UNP P00441 ?   ?   'expression tag'      -7  28 
7  9JBP ALA D 2   ? UNP P00441 ?   ?   'expression tag'      -6  29 
7  9JBP MET D 3   ? UNP P00441 ?   ?   'expression tag'      -5  30 
7  9JBP ASP D 4   ? UNP P00441 ?   ?   'expression tag'      -4  31 
7  9JBP PRO D 5   ? UNP P00441 ?   ?   'expression tag'      -3  32 
7  9JBP GLU D 6   ? UNP P00441 ?   ?   'expression tag'      -2  33 
7  9JBP PHE D 7   ? UNP P00441 ?   ?   'expression tag'      -1  34 
7  9JBP ALA D 14  ? UNP P00441 CYS 7   'engineered mutation' 6   35 
7  9JBP ALA D 119 ? UNP P00441 CYS 112 'engineered mutation' 111 36 
9  9JBP GLY E 1   ? UNP P00441 ?   ?   'expression tag'      -7  37 
9  9JBP ALA E 2   ? UNP P00441 ?   ?   'expression tag'      -6  38 
9  9JBP MET E 3   ? UNP P00441 ?   ?   'expression tag'      -5  39 
9  9JBP ASP E 4   ? UNP P00441 ?   ?   'expression tag'      -4  40 
9  9JBP PRO E 5   ? UNP P00441 ?   ?   'expression tag'      -3  41 
9  9JBP GLU E 6   ? UNP P00441 ?   ?   'expression tag'      -2  42 
9  9JBP PHE E 7   ? UNP P00441 ?   ?   'expression tag'      -1  43 
9  9JBP ALA E 14  ? UNP P00441 CYS 7   'engineered mutation' 6   44 
9  9JBP ALA E 119 ? UNP P00441 CYS 112 'engineered mutation' 111 45 
11 9JBP GLY F 1   ? UNP P00441 ?   ?   'expression tag'      -7  46 
11 9JBP ALA F 2   ? UNP P00441 ?   ?   'expression tag'      -6  47 
11 9JBP MET F 3   ? UNP P00441 ?   ?   'expression tag'      -5  48 
11 9JBP ASP F 4   ? UNP P00441 ?   ?   'expression tag'      -4  49 
11 9JBP PRO F 5   ? UNP P00441 ?   ?   'expression tag'      -3  50 
11 9JBP GLU F 6   ? UNP P00441 ?   ?   'expression tag'      -2  51 
11 9JBP PHE F 7   ? UNP P00441 ?   ?   'expression tag'      -1  52 
11 9JBP ALA F 14  ? UNP P00441 CYS 7   'engineered mutation' 6   53 
11 9JBP ALA F 119 ? UNP P00441 CYS 112 'engineered mutation' 111 54 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dodecameric 
_pdbx_struct_assembly.oligomeric_count     12 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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                'amyloid filaments are shown 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 ? 
# 
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 
# 
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 13 ? LEU A 16 ? VAL A 5  LEU A 8  
AA1 2 VAL C 13 ? LEU C 16 ? VAL B 5  LEU B 8  
AA1 3 VAL E 13 ? LEU E 16 ? VAL C 5  LEU C 8  
AA2 1 VAL A 22 ? GLN A 23 ? VAL A 14 GLN A 15 
AA2 2 VAL C 22 ? ILE C 26 ? VAL B 14 ILE B 18 
AA2 3 VAL E 22 ? ILE E 26 ? VAL C 14 ILE C 18 
AA3 1 LYS A 38 ? ILE A 43 ? LYS A 30 ILE A 35 
AA3 2 LYS C 38 ? ILE C 43 ? LYS B 30 ILE B 35 
AA3 3 LYS E 38 ? ILE E 43 ? LYS C 30 ILE C 35 
AA4 1 UNK B 3  ? UNK B 6  ? UNK G 3  UNK G 6  
AA4 2 UNK D 3  ? UNK D 6  ? UNK H 3  UNK H 6  
AA4 3 UNK F 3  ? UNK F 6  ? UNK I 3  UNK I 6  
AA5 1 THR G 10 ? LEU G 16 ? THR D 2  LEU D 8  
AA5 2 THR I 10 ? LEU I 16 ? THR E 2  LEU E 8  
AA5 3 VAL K 13 ? LEU K 16 ? VAL F 5  LEU F 8  
AA6 1 VAL G 22 ? ILE G 26 ? VAL D 14 ILE D 18 
AA6 2 VAL I 22 ? ILE I 26 ? VAL E 14 ILE E 18 
AA6 3 VAL K 22 ? ILE K 26 ? VAL F 14 ILE F 18 
AA7 1 LYS G 38 ? ILE G 43 ? LYS D 30 ILE D 35 
AA7 2 LYS I 38 ? ILE I 43 ? LYS E 30 ILE E 35 
AA7 3 LYS K 38 ? ILE K 43 ? LYS F 30 ILE F 35 
AA8 1 UNK H 3  ? UNK H 6  ? UNK J 3  UNK J 6  
AA8 2 UNK J 3  ? UNK J 6  ? UNK K 3  UNK K 6  
AA8 3 UNK L 3  ? UNK L 6  ? UNK L 3  UNK L 6  
# 
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 VAL A 15 ? N VAL A 7  O ALA C 14 ? O ALA B 6  
AA1 2 3 N VAL C 15 ? N VAL B 7  O ALA E 14 ? O ALA C 6  
AA2 1 2 N GLN A 23 ? N GLN A 15 O GLY C 24 ? O GLY B 16 
AA2 2 3 N GLN C 23 ? N GLN B 15 O GLY E 24 ? O GLY C 16 
AA3 1 2 N VAL A 39 ? N VAL A 31 O LYS C 38 ? O LYS B 30 
AA3 2 3 N GLY C 41 ? N GLY B 33 O SER E 42 ? O SER C 34 
AA4 1 2 N UNK B 4  ? N UNK G 4  O UNK D 5  ? O UNK H 5  
AA4 2 3 N UNK D 4  ? N UNK H 4  O UNK F 5  ? O UNK I 5  
AA5 1 2 N VAL G 15 ? N VAL D 7  O ALA I 14 ? O ALA E 6  
AA5 2 3 N VAL I 15 ? N VAL E 7  O ALA K 14 ? O ALA F 6  
AA6 1 2 N GLN G 23 ? N GLN D 15 O GLY I 24 ? O GLY E 16 
AA6 2 3 N GLN I 23 ? N GLN E 15 O GLY K 24 ? O GLY F 16 
AA7 1 2 N GLY G 41 ? N GLY D 33 O SER I 42 ? O SER E 34 
AA7 2 3 N GLY I 41 ? N GLY E 33 O SER K 42 ? O SER F 34 
AA8 1 2 N UNK H 4  ? N UNK J 4  O UNK J 5  ? O UNK K 5  
AA8 2 3 N UNK J 4  ? N UNK K 4  O UNK L 5  ? O UNK L 5  
# 
_pdbx_entry_details.entry_id                   9JBP 
_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 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9JBP 
_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                    9JBP 
_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                  3.18 
_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               679265 
_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 C6A/C111A mutant SOD1 protein' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9JBP 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_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            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             2100 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           92000 
_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              9JBP 
_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                9JBP 
_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 A GLY -7  ? A GLY 1   
2   1 Y 1 A ALA -6  ? A ALA 2   
3   1 Y 1 A MET -5  ? A MET 3   
4   1 Y 1 A ASP -4  ? A ASP 4   
5   1 Y 1 A PRO -3  ? A PRO 5   
6   1 Y 1 A GLU -2  ? A GLU 6   
7   1 Y 1 A PHE -1  ? A PHE 7   
8   1 Y 1 A MET 0   ? A MET 8   
9   1 Y 1 A LEU 42  ? A LEU 50  
10  1 Y 1 A HIS 43  ? A HIS 51  
11  1 Y 1 A GLY 44  ? A GLY 52  
12  1 Y 1 A PHE 45  ? A PHE 53  
13  1 Y 1 A HIS 46  ? A HIS 54  
14  1 Y 1 A VAL 47  ? A VAL 55  
15  1 Y 1 A HIS 48  ? A HIS 56  
16  1 Y 1 A GLU 49  ? A GLU 57  
17  1 Y 1 A PHE 50  ? A PHE 58  
18  1 Y 1 A GLY 51  ? A GLY 59  
19  1 Y 1 A ASP 52  ? A ASP 60  
20  1 Y 1 A ASN 53  ? A ASN 61  
21  1 Y 1 A THR 54  ? A THR 62  
22  1 Y 1 A ALA 55  ? A ALA 63  
23  1 Y 1 A GLY 56  ? A GLY 64  
24  1 Y 1 A CYS 57  ? A CYS 65  
25  1 Y 1 A THR 58  ? A THR 66  
26  1 Y 1 A SER 59  ? A SER 67  
27  1 Y 1 A ALA 60  ? A ALA 68  
28  1 Y 1 A GLY 61  ? A GLY 69  
29  1 Y 1 A PRO 62  ? A PRO 70  
30  1 Y 1 A HIS 63  ? A HIS 71  
31  1 Y 1 A PHE 64  ? A PHE 72  
32  1 Y 1 A ASN 65  ? A ASN 73  
33  1 Y 1 A PRO 66  ? A PRO 74  
34  1 Y 1 A LEU 67  ? A LEU 75  
35  1 Y 1 A SER 68  ? A SER 76  
36  1 Y 1 A ARG 69  ? A ARG 77  
37  1 Y 1 A LYS 70  ? A LYS 78  
38  1 Y 1 A HIS 71  ? A HIS 79  
39  1 Y 1 A GLY 72  ? A GLY 80  
40  1 Y 1 A GLY 73  ? A GLY 81  
41  1 Y 1 A PRO 74  ? A PRO 82  
42  1 Y 1 A LYS 75  ? A LYS 83  
43  1 Y 1 A ASP 76  ? A ASP 84  
44  1 Y 1 A GLU 77  ? A GLU 85  
45  1 Y 1 A GLU 78  ? A GLU 86  
46  1 Y 1 A ARG 79  ? A ARG 87  
47  1 Y 1 A HIS 80  ? A HIS 88  
48  1 Y 1 A VAL 81  ? A VAL 89  
49  1 Y 1 A GLY 82  ? A GLY 90  
50  1 Y 1 A ASP 83  ? A ASP 91  
51  1 Y 1 A LEU 84  ? A LEU 92  
52  1 Y 1 A GLY 85  ? A GLY 93  
53  1 Y 1 A ASN 86  ? A ASN 94  
54  1 Y 1 A VAL 87  ? A VAL 95  
55  1 Y 1 A THR 88  ? A THR 96  
56  1 Y 1 A ALA 89  ? A ALA 97  
57  1 Y 1 A ASP 90  ? A ASP 98  
58  1 Y 1 A LYS 91  ? A LYS 99  
59  1 Y 1 A ASP 92  ? A ASP 100 
60  1 Y 1 A GLY 93  ? A GLY 101 
61  1 Y 1 A VAL 94  ? A VAL 102 
62  1 Y 1 A ALA 95  ? A ALA 103 
63  1 Y 1 A ASP 96  ? A ASP 104 
64  1 Y 1 A VAL 97  ? A VAL 105 
65  1 Y 1 A SER 98  ? A SER 106 
66  1 Y 1 A ILE 99  ? A ILE 107 
67  1 Y 1 A GLU 100 ? A GLU 108 
68  1 Y 1 A ASP 101 ? A ASP 109 
69  1 Y 1 A SER 102 ? A SER 110 
70  1 Y 1 A VAL 103 ? A VAL 111 
71  1 Y 1 A ILE 104 ? A ILE 112 
72  1 Y 1 A SER 105 ? A SER 113 
73  1 Y 1 A LEU 106 ? A LEU 114 
74  1 Y 1 A SER 107 ? A SER 115 
75  1 Y 1 A GLY 108 ? A GLY 116 
76  1 Y 1 A ASP 109 ? A ASP 117 
77  1 Y 1 A HIS 110 ? A HIS 118 
78  1 Y 1 A ALA 111 ? A ALA 119 
79  1 Y 1 A ILE 112 ? A ILE 120 
80  1 Y 1 A ILE 113 ? A ILE 121 
81  1 Y 1 A GLY 114 ? A GLY 122 
82  1 Y 1 A ARG 115 ? A ARG 123 
83  1 Y 1 A THR 116 ? A THR 124 
84  1 Y 1 A LEU 117 ? A LEU 125 
85  1 Y 1 A VAL 118 ? A VAL 126 
86  1 Y 1 A VAL 119 ? A VAL 127 
87  1 Y 1 A HIS 120 ? A HIS 128 
88  1 Y 1 A GLU 121 ? A GLU 129 
89  1 Y 1 A LYS 122 ? A LYS 130 
90  1 Y 1 A ALA 123 ? A ALA 131 
91  1 Y 1 A ASP 124 ? A ASP 132 
92  1 Y 1 A ASP 125 ? A ASP 133 
93  1 Y 1 A LEU 126 ? A LEU 134 
94  1 Y 1 A GLY 127 ? A GLY 135 
95  1 Y 1 A LYS 128 ? A LYS 136 
96  1 Y 1 A GLY 129 ? A GLY 137 
97  1 Y 1 A GLY 130 ? A GLY 138 
98  1 Y 1 A ASN 131 ? A ASN 139 
99  1 Y 1 A GLU 132 ? A GLU 140 
100 1 Y 1 A GLU 133 ? A GLU 141 
101 1 Y 1 A SER 134 ? A SER 142 
102 1 Y 1 A THR 135 ? A THR 143 
103 1 Y 1 A LYS 136 ? A LYS 144 
104 1 Y 1 A THR 137 ? A THR 145 
105 1 Y 1 A GLY 138 ? A GLY 146 
106 1 Y 1 A ASN 139 ? A ASN 147 
107 1 Y 1 A ALA 140 ? A ALA 148 
108 1 Y 1 A GLY 141 ? A GLY 149 
109 1 Y 1 A SER 142 ? A SER 150 
110 1 Y 1 A ARG 143 ? A ARG 151 
111 1 Y 1 A LEU 144 ? A LEU 152 
112 1 Y 1 A ALA 145 ? A ALA 153 
113 1 Y 1 A CYS 146 ? A CYS 154 
114 1 Y 1 A GLY 147 ? A GLY 155 
115 1 Y 1 A VAL 148 ? A VAL 156 
116 1 Y 1 A ILE 149 ? A ILE 157 
117 1 Y 1 A GLY 150 ? A GLY 158 
118 1 Y 1 A ILE 151 ? A ILE 159 
119 1 Y 1 A ALA 152 ? A ALA 160 
120 1 Y 1 A GLN 153 ? A GLN 161 
121 1 Y 1 B GLY -7  ? C GLY 1   
122 1 Y 1 B ALA -6  ? C ALA 2   
123 1 Y 1 B MET -5  ? C MET 3   
124 1 Y 1 B ASP -4  ? C ASP 4   
125 1 Y 1 B PRO -3  ? C PRO 5   
126 1 Y 1 B GLU -2  ? C GLU 6   
127 1 Y 1 B PHE -1  ? C PHE 7   
128 1 Y 1 B MET 0   ? C MET 8   
129 1 Y 1 B LEU 42  ? C LEU 50  
130 1 Y 1 B HIS 43  ? C HIS 51  
131 1 Y 1 B GLY 44  ? C GLY 52  
132 1 Y 1 B PHE 45  ? C PHE 53  
133 1 Y 1 B HIS 46  ? C HIS 54  
134 1 Y 1 B VAL 47  ? C VAL 55  
135 1 Y 1 B HIS 48  ? C HIS 56  
136 1 Y 1 B GLU 49  ? C GLU 57  
137 1 Y 1 B PHE 50  ? C PHE 58  
138 1 Y 1 B GLY 51  ? C GLY 59  
139 1 Y 1 B ASP 52  ? C ASP 60  
140 1 Y 1 B ASN 53  ? C ASN 61  
141 1 Y 1 B THR 54  ? C THR 62  
142 1 Y 1 B ALA 55  ? C ALA 63  
143 1 Y 1 B GLY 56  ? C GLY 64  
144 1 Y 1 B CYS 57  ? C CYS 65  
145 1 Y 1 B THR 58  ? C THR 66  
146 1 Y 1 B SER 59  ? C SER 67  
147 1 Y 1 B ALA 60  ? C ALA 68  
148 1 Y 1 B GLY 61  ? C GLY 69  
149 1 Y 1 B PRO 62  ? C PRO 70  
150 1 Y 1 B HIS 63  ? C HIS 71  
151 1 Y 1 B PHE 64  ? C PHE 72  
152 1 Y 1 B ASN 65  ? C ASN 73  
153 1 Y 1 B PRO 66  ? C PRO 74  
154 1 Y 1 B LEU 67  ? C LEU 75  
155 1 Y 1 B SER 68  ? C SER 76  
156 1 Y 1 B ARG 69  ? C ARG 77  
157 1 Y 1 B LYS 70  ? C LYS 78  
158 1 Y 1 B HIS 71  ? C HIS 79  
159 1 Y 1 B GLY 72  ? C GLY 80  
160 1 Y 1 B GLY 73  ? C GLY 81  
161 1 Y 1 B PRO 74  ? C PRO 82  
162 1 Y 1 B LYS 75  ? C LYS 83  
163 1 Y 1 B ASP 76  ? C ASP 84  
164 1 Y 1 B GLU 77  ? C GLU 85  
165 1 Y 1 B GLU 78  ? C GLU 86  
166 1 Y 1 B ARG 79  ? C ARG 87  
167 1 Y 1 B HIS 80  ? C HIS 88  
168 1 Y 1 B VAL 81  ? C VAL 89  
169 1 Y 1 B GLY 82  ? C GLY 90  
170 1 Y 1 B ASP 83  ? C ASP 91  
171 1 Y 1 B LEU 84  ? C LEU 92  
172 1 Y 1 B GLY 85  ? C GLY 93  
173 1 Y 1 B ASN 86  ? C ASN 94  
174 1 Y 1 B VAL 87  ? C VAL 95  
175 1 Y 1 B THR 88  ? C THR 96  
176 1 Y 1 B ALA 89  ? C ALA 97  
177 1 Y 1 B ASP 90  ? C ASP 98  
178 1 Y 1 B LYS 91  ? C LYS 99  
179 1 Y 1 B ASP 92  ? C ASP 100 
180 1 Y 1 B GLY 93  ? C GLY 101 
181 1 Y 1 B VAL 94  ? C VAL 102 
182 1 Y 1 B ALA 95  ? C ALA 103 
183 1 Y 1 B ASP 96  ? C ASP 104 
184 1 Y 1 B VAL 97  ? C VAL 105 
185 1 Y 1 B SER 98  ? C SER 106 
186 1 Y 1 B ILE 99  ? C ILE 107 
187 1 Y 1 B GLU 100 ? C GLU 108 
188 1 Y 1 B ASP 101 ? C ASP 109 
189 1 Y 1 B SER 102 ? C SER 110 
190 1 Y 1 B VAL 103 ? C VAL 111 
191 1 Y 1 B ILE 104 ? C ILE 112 
192 1 Y 1 B SER 105 ? C SER 113 
193 1 Y 1 B LEU 106 ? C LEU 114 
194 1 Y 1 B SER 107 ? C SER 115 
195 1 Y 1 B GLY 108 ? C GLY 116 
196 1 Y 1 B ASP 109 ? C ASP 117 
197 1 Y 1 B HIS 110 ? C HIS 118 
198 1 Y 1 B ALA 111 ? C ALA 119 
199 1 Y 1 B ILE 112 ? C ILE 120 
200 1 Y 1 B ILE 113 ? C ILE 121 
201 1 Y 1 B GLY 114 ? C GLY 122 
202 1 Y 1 B ARG 115 ? C ARG 123 
203 1 Y 1 B THR 116 ? C THR 124 
204 1 Y 1 B LEU 117 ? C LEU 125 
205 1 Y 1 B VAL 118 ? C VAL 126 
206 1 Y 1 B VAL 119 ? C VAL 127 
207 1 Y 1 B HIS 120 ? C HIS 128 
208 1 Y 1 B GLU 121 ? C GLU 129 
209 1 Y 1 B LYS 122 ? C LYS 130 
210 1 Y 1 B ALA 123 ? C ALA 131 
211 1 Y 1 B ASP 124 ? C ASP 132 
212 1 Y 1 B ASP 125 ? C ASP 133 
213 1 Y 1 B LEU 126 ? C LEU 134 
214 1 Y 1 B GLY 127 ? C GLY 135 
215 1 Y 1 B LYS 128 ? C LYS 136 
216 1 Y 1 B GLY 129 ? C GLY 137 
217 1 Y 1 B GLY 130 ? C GLY 138 
218 1 Y 1 B ASN 131 ? C ASN 139 
219 1 Y 1 B GLU 132 ? C GLU 140 
220 1 Y 1 B GLU 133 ? C GLU 141 
221 1 Y 1 B SER 134 ? C SER 142 
222 1 Y 1 B THR 135 ? C THR 143 
223 1 Y 1 B LYS 136 ? C LYS 144 
224 1 Y 1 B THR 137 ? C THR 145 
225 1 Y 1 B GLY 138 ? C GLY 146 
226 1 Y 1 B ASN 139 ? C ASN 147 
227 1 Y 1 B ALA 140 ? C ALA 148 
228 1 Y 1 B GLY 141 ? C GLY 149 
229 1 Y 1 B SER 142 ? C SER 150 
230 1 Y 1 B ARG 143 ? C ARG 151 
231 1 Y 1 B LEU 144 ? C LEU 152 
232 1 Y 1 B ALA 145 ? C ALA 153 
233 1 Y 1 B CYS 146 ? C CYS 154 
234 1 Y 1 B GLY 147 ? C GLY 155 
235 1 Y 1 B VAL 148 ? C VAL 156 
236 1 Y 1 B ILE 149 ? C ILE 157 
237 1 Y 1 B GLY 150 ? C GLY 158 
238 1 Y 1 B ILE 151 ? C ILE 159 
239 1 Y 1 B ALA 152 ? C ALA 160 
240 1 Y 1 B GLN 153 ? C GLN 161 
241 1 Y 1 C GLY -7  ? E GLY 1   
242 1 Y 1 C ALA -6  ? E ALA 2   
243 1 Y 1 C MET -5  ? E MET 3   
244 1 Y 1 C ASP -4  ? E ASP 4   
245 1 Y 1 C PRO -3  ? E PRO 5   
246 1 Y 1 C GLU -2  ? E GLU 6   
247 1 Y 1 C PHE -1  ? E PHE 7   
248 1 Y 1 C MET 0   ? E MET 8   
249 1 Y 1 C LEU 42  ? E LEU 50  
250 1 Y 1 C HIS 43  ? E HIS 51  
251 1 Y 1 C GLY 44  ? E GLY 52  
252 1 Y 1 C PHE 45  ? E PHE 53  
253 1 Y 1 C HIS 46  ? E HIS 54  
254 1 Y 1 C VAL 47  ? E VAL 55  
255 1 Y 1 C HIS 48  ? E HIS 56  
256 1 Y 1 C GLU 49  ? E GLU 57  
257 1 Y 1 C PHE 50  ? E PHE 58  
258 1 Y 1 C GLY 51  ? E GLY 59  
259 1 Y 1 C ASP 52  ? E ASP 60  
260 1 Y 1 C ASN 53  ? E ASN 61  
261 1 Y 1 C THR 54  ? E THR 62  
262 1 Y 1 C ALA 55  ? E ALA 63  
263 1 Y 1 C GLY 56  ? E GLY 64  
264 1 Y 1 C CYS 57  ? E CYS 65  
265 1 Y 1 C THR 58  ? E THR 66  
266 1 Y 1 C SER 59  ? E SER 67  
267 1 Y 1 C ALA 60  ? E ALA 68  
268 1 Y 1 C GLY 61  ? E GLY 69  
269 1 Y 1 C PRO 62  ? E PRO 70  
270 1 Y 1 C HIS 63  ? E HIS 71  
271 1 Y 1 C PHE 64  ? E PHE 72  
272 1 Y 1 C ASN 65  ? E ASN 73  
273 1 Y 1 C PRO 66  ? E PRO 74  
274 1 Y 1 C LEU 67  ? E LEU 75  
275 1 Y 1 C SER 68  ? E SER 76  
276 1 Y 1 C ARG 69  ? E ARG 77  
277 1 Y 1 C LYS 70  ? E LYS 78  
278 1 Y 1 C HIS 71  ? E HIS 79  
279 1 Y 1 C GLY 72  ? E GLY 80  
280 1 Y 1 C GLY 73  ? E GLY 81  
281 1 Y 1 C PRO 74  ? E PRO 82  
282 1 Y 1 C LYS 75  ? E LYS 83  
283 1 Y 1 C ASP 76  ? E ASP 84  
284 1 Y 1 C GLU 77  ? E GLU 85  
285 1 Y 1 C GLU 78  ? E GLU 86  
286 1 Y 1 C ARG 79  ? E ARG 87  
287 1 Y 1 C HIS 80  ? E HIS 88  
288 1 Y 1 C VAL 81  ? E VAL 89  
289 1 Y 1 C GLY 82  ? E GLY 90  
290 1 Y 1 C ASP 83  ? E ASP 91  
291 1 Y 1 C LEU 84  ? E LEU 92  
292 1 Y 1 C GLY 85  ? E GLY 93  
293 1 Y 1 C ASN 86  ? E ASN 94  
294 1 Y 1 C VAL 87  ? E VAL 95  
295 1 Y 1 C THR 88  ? E THR 96  
296 1 Y 1 C ALA 89  ? E ALA 97  
297 1 Y 1 C ASP 90  ? E ASP 98  
298 1 Y 1 C LYS 91  ? E LYS 99  
299 1 Y 1 C ASP 92  ? E ASP 100 
300 1 Y 1 C GLY 93  ? E GLY 101 
301 1 Y 1 C VAL 94  ? E VAL 102 
302 1 Y 1 C ALA 95  ? E ALA 103 
303 1 Y 1 C ASP 96  ? E ASP 104 
304 1 Y 1 C VAL 97  ? E VAL 105 
305 1 Y 1 C SER 98  ? E SER 106 
306 1 Y 1 C ILE 99  ? E ILE 107 
307 1 Y 1 C GLU 100 ? E GLU 108 
308 1 Y 1 C ASP 101 ? E ASP 109 
309 1 Y 1 C SER 102 ? E SER 110 
310 1 Y 1 C VAL 103 ? E VAL 111 
311 1 Y 1 C ILE 104 ? E ILE 112 
312 1 Y 1 C SER 105 ? E SER 113 
313 1 Y 1 C LEU 106 ? E LEU 114 
314 1 Y 1 C SER 107 ? E SER 115 
315 1 Y 1 C GLY 108 ? E GLY 116 
316 1 Y 1 C ASP 109 ? E ASP 117 
317 1 Y 1 C HIS 110 ? E HIS 118 
318 1 Y 1 C ALA 111 ? E ALA 119 
319 1 Y 1 C ILE 112 ? E ILE 120 
320 1 Y 1 C ILE 113 ? E ILE 121 
321 1 Y 1 C GLY 114 ? E GLY 122 
322 1 Y 1 C ARG 115 ? E ARG 123 
323 1 Y 1 C THR 116 ? E THR 124 
324 1 Y 1 C LEU 117 ? E LEU 125 
325 1 Y 1 C VAL 118 ? E VAL 126 
326 1 Y 1 C VAL 119 ? E VAL 127 
327 1 Y 1 C HIS 120 ? E HIS 128 
328 1 Y 1 C GLU 121 ? E GLU 129 
329 1 Y 1 C LYS 122 ? E LYS 130 
330 1 Y 1 C ALA 123 ? E ALA 131 
331 1 Y 1 C ASP 124 ? E ASP 132 
332 1 Y 1 C ASP 125 ? E ASP 133 
333 1 Y 1 C LEU 126 ? E LEU 134 
334 1 Y 1 C GLY 127 ? E GLY 135 
335 1 Y 1 C LYS 128 ? E LYS 136 
336 1 Y 1 C GLY 129 ? E GLY 137 
337 1 Y 1 C GLY 130 ? E GLY 138 
338 1 Y 1 C ASN 131 ? E ASN 139 
339 1 Y 1 C GLU 132 ? E GLU 140 
340 1 Y 1 C GLU 133 ? E GLU 141 
341 1 Y 1 C SER 134 ? E SER 142 
342 1 Y 1 C THR 135 ? E THR 143 
343 1 Y 1 C LYS 136 ? E LYS 144 
344 1 Y 1 C THR 137 ? E THR 145 
345 1 Y 1 C GLY 138 ? E GLY 146 
346 1 Y 1 C ASN 139 ? E ASN 147 
347 1 Y 1 C ALA 140 ? E ALA 148 
348 1 Y 1 C GLY 141 ? E GLY 149 
349 1 Y 1 C SER 142 ? E SER 150 
350 1 Y 1 C ARG 143 ? E ARG 151 
351 1 Y 1 C LEU 144 ? E LEU 152 
352 1 Y 1 C ALA 145 ? E ALA 153 
353 1 Y 1 C CYS 146 ? E CYS 154 
354 1 Y 1 C GLY 147 ? E GLY 155 
355 1 Y 1 C VAL 148 ? E VAL 156 
356 1 Y 1 C ILE 149 ? E ILE 157 
357 1 Y 1 C GLY 150 ? E GLY 158 
358 1 Y 1 C ILE 151 ? E ILE 159 
359 1 Y 1 C ALA 152 ? E ALA 160 
360 1 Y 1 C GLN 153 ? E GLN 161 
361 1 Y 1 D GLY -7  ? G GLY 1   
362 1 Y 1 D ALA -6  ? G ALA 2   
363 1 Y 1 D MET -5  ? G MET 3   
364 1 Y 1 D ASP -4  ? G ASP 4   
365 1 Y 1 D PRO -3  ? G PRO 5   
366 1 Y 1 D GLU -2  ? G GLU 6   
367 1 Y 1 D PHE -1  ? G PHE 7   
368 1 Y 1 D MET 0   ? G MET 8   
369 1 Y 1 D LEU 42  ? G LEU 50  
370 1 Y 1 D HIS 43  ? G HIS 51  
371 1 Y 1 D GLY 44  ? G GLY 52  
372 1 Y 1 D PHE 45  ? G PHE 53  
373 1 Y 1 D HIS 46  ? G HIS 54  
374 1 Y 1 D VAL 47  ? G VAL 55  
375 1 Y 1 D HIS 48  ? G HIS 56  
376 1 Y 1 D GLU 49  ? G GLU 57  
377 1 Y 1 D PHE 50  ? G PHE 58  
378 1 Y 1 D GLY 51  ? G GLY 59  
379 1 Y 1 D ASP 52  ? G ASP 60  
380 1 Y 1 D ASN 53  ? G ASN 61  
381 1 Y 1 D THR 54  ? G THR 62  
382 1 Y 1 D ALA 55  ? G ALA 63  
383 1 Y 1 D GLY 56  ? G GLY 64  
384 1 Y 1 D CYS 57  ? G CYS 65  
385 1 Y 1 D THR 58  ? G THR 66  
386 1 Y 1 D SER 59  ? G SER 67  
387 1 Y 1 D ALA 60  ? G ALA 68  
388 1 Y 1 D GLY 61  ? G GLY 69  
389 1 Y 1 D PRO 62  ? G PRO 70  
390 1 Y 1 D HIS 63  ? G HIS 71  
391 1 Y 1 D PHE 64  ? G PHE 72  
392 1 Y 1 D ASN 65  ? G ASN 73  
393 1 Y 1 D PRO 66  ? G PRO 74  
394 1 Y 1 D LEU 67  ? G LEU 75  
395 1 Y 1 D SER 68  ? G SER 76  
396 1 Y 1 D ARG 69  ? G ARG 77  
397 1 Y 1 D LYS 70  ? G LYS 78  
398 1 Y 1 D HIS 71  ? G HIS 79  
399 1 Y 1 D GLY 72  ? G GLY 80  
400 1 Y 1 D GLY 73  ? G GLY 81  
401 1 Y 1 D PRO 74  ? G PRO 82  
402 1 Y 1 D LYS 75  ? G LYS 83  
403 1 Y 1 D ASP 76  ? G ASP 84  
404 1 Y 1 D GLU 77  ? G GLU 85  
405 1 Y 1 D GLU 78  ? G GLU 86  
406 1 Y 1 D ARG 79  ? G ARG 87  
407 1 Y 1 D HIS 80  ? G HIS 88  
408 1 Y 1 D VAL 81  ? G VAL 89  
409 1 Y 1 D GLY 82  ? G GLY 90  
410 1 Y 1 D ASP 83  ? G ASP 91  
411 1 Y 1 D LEU 84  ? G LEU 92  
412 1 Y 1 D GLY 85  ? G GLY 93  
413 1 Y 1 D ASN 86  ? G ASN 94  
414 1 Y 1 D VAL 87  ? G VAL 95  
415 1 Y 1 D THR 88  ? G THR 96  
416 1 Y 1 D ALA 89  ? G ALA 97  
417 1 Y 1 D ASP 90  ? G ASP 98  
418 1 Y 1 D LYS 91  ? G LYS 99  
419 1 Y 1 D ASP 92  ? G ASP 100 
420 1 Y 1 D GLY 93  ? G GLY 101 
421 1 Y 1 D VAL 94  ? G VAL 102 
422 1 Y 1 D ALA 95  ? G ALA 103 
423 1 Y 1 D ASP 96  ? G ASP 104 
424 1 Y 1 D VAL 97  ? G VAL 105 
425 1 Y 1 D SER 98  ? G SER 106 
426 1 Y 1 D ILE 99  ? G ILE 107 
427 1 Y 1 D GLU 100 ? G GLU 108 
428 1 Y 1 D ASP 101 ? G ASP 109 
429 1 Y 1 D SER 102 ? G SER 110 
430 1 Y 1 D VAL 103 ? G VAL 111 
431 1 Y 1 D ILE 104 ? G ILE 112 
432 1 Y 1 D SER 105 ? G SER 113 
433 1 Y 1 D LEU 106 ? G LEU 114 
434 1 Y 1 D SER 107 ? G SER 115 
435 1 Y 1 D GLY 108 ? G GLY 116 
436 1 Y 1 D ASP 109 ? G ASP 117 
437 1 Y 1 D HIS 110 ? G HIS 118 
438 1 Y 1 D ALA 111 ? G ALA 119 
439 1 Y 1 D ILE 112 ? G ILE 120 
440 1 Y 1 D ILE 113 ? G ILE 121 
441 1 Y 1 D GLY 114 ? G GLY 122 
442 1 Y 1 D ARG 115 ? G ARG 123 
443 1 Y 1 D THR 116 ? G THR 124 
444 1 Y 1 D LEU 117 ? G LEU 125 
445 1 Y 1 D VAL 118 ? G VAL 126 
446 1 Y 1 D VAL 119 ? G VAL 127 
447 1 Y 1 D HIS 120 ? G HIS 128 
448 1 Y 1 D GLU 121 ? G GLU 129 
449 1 Y 1 D LYS 122 ? G LYS 130 
450 1 Y 1 D ALA 123 ? G ALA 131 
451 1 Y 1 D ASP 124 ? G ASP 132 
452 1 Y 1 D ASP 125 ? G ASP 133 
453 1 Y 1 D LEU 126 ? G LEU 134 
454 1 Y 1 D GLY 127 ? G GLY 135 
455 1 Y 1 D LYS 128 ? G LYS 136 
456 1 Y 1 D GLY 129 ? G GLY 137 
457 1 Y 1 D GLY 130 ? G GLY 138 
458 1 Y 1 D ASN 131 ? G ASN 139 
459 1 Y 1 D GLU 132 ? G GLU 140 
460 1 Y 1 D GLU 133 ? G GLU 141 
461 1 Y 1 D SER 134 ? G SER 142 
462 1 Y 1 D THR 135 ? G THR 143 
463 1 Y 1 D LYS 136 ? G LYS 144 
464 1 Y 1 D THR 137 ? G THR 145 
465 1 Y 1 D GLY 138 ? G GLY 146 
466 1 Y 1 D ASN 139 ? G ASN 147 
467 1 Y 1 D ALA 140 ? G ALA 148 
468 1 Y 1 D GLY 141 ? G GLY 149 
469 1 Y 1 D SER 142 ? G SER 150 
470 1 Y 1 D ARG 143 ? G ARG 151 
471 1 Y 1 D LEU 144 ? G LEU 152 
472 1 Y 1 D ALA 145 ? G ALA 153 
473 1 Y 1 D CYS 146 ? G CYS 154 
474 1 Y 1 D GLY 147 ? G GLY 155 
475 1 Y 1 D VAL 148 ? G VAL 156 
476 1 Y 1 D ILE 149 ? G ILE 157 
477 1 Y 1 D GLY 150 ? G GLY 158 
478 1 Y 1 D ILE 151 ? G ILE 159 
479 1 Y 1 D ALA 152 ? G ALA 160 
480 1 Y 1 D GLN 153 ? G GLN 161 
481 1 Y 1 E GLY -7  ? I GLY 1   
482 1 Y 1 E ALA -6  ? I ALA 2   
483 1 Y 1 E MET -5  ? I MET 3   
484 1 Y 1 E ASP -4  ? I ASP 4   
485 1 Y 1 E PRO -3  ? I PRO 5   
486 1 Y 1 E GLU -2  ? I GLU 6   
487 1 Y 1 E PHE -1  ? I PHE 7   
488 1 Y 1 E MET 0   ? I MET 8   
489 1 Y 1 E LEU 42  ? I LEU 50  
490 1 Y 1 E HIS 43  ? I HIS 51  
491 1 Y 1 E GLY 44  ? I GLY 52  
492 1 Y 1 E PHE 45  ? I PHE 53  
493 1 Y 1 E HIS 46  ? I HIS 54  
494 1 Y 1 E VAL 47  ? I VAL 55  
495 1 Y 1 E HIS 48  ? I HIS 56  
496 1 Y 1 E GLU 49  ? I GLU 57  
497 1 Y 1 E PHE 50  ? I PHE 58  
498 1 Y 1 E GLY 51  ? I GLY 59  
499 1 Y 1 E ASP 52  ? I ASP 60  
500 1 Y 1 E ASN 53  ? I ASN 61  
501 1 Y 1 E THR 54  ? I THR 62  
502 1 Y 1 E ALA 55  ? I ALA 63  
503 1 Y 1 E GLY 56  ? I GLY 64  
504 1 Y 1 E CYS 57  ? I CYS 65  
505 1 Y 1 E THR 58  ? I THR 66  
506 1 Y 1 E SER 59  ? I SER 67  
507 1 Y 1 E ALA 60  ? I ALA 68  
508 1 Y 1 E GLY 61  ? I GLY 69  
509 1 Y 1 E PRO 62  ? I PRO 70  
510 1 Y 1 E HIS 63  ? I HIS 71  
511 1 Y 1 E PHE 64  ? I PHE 72  
512 1 Y 1 E ASN 65  ? I ASN 73  
513 1 Y 1 E PRO 66  ? I PRO 74  
514 1 Y 1 E LEU 67  ? I LEU 75  
515 1 Y 1 E SER 68  ? I SER 76  
516 1 Y 1 E ARG 69  ? I ARG 77  
517 1 Y 1 E LYS 70  ? I LYS 78  
518 1 Y 1 E HIS 71  ? I HIS 79  
519 1 Y 1 E GLY 72  ? I GLY 80  
520 1 Y 1 E GLY 73  ? I GLY 81  
521 1 Y 1 E PRO 74  ? I PRO 82  
522 1 Y 1 E LYS 75  ? I LYS 83  
523 1 Y 1 E ASP 76  ? I ASP 84  
524 1 Y 1 E GLU 77  ? I GLU 85  
525 1 Y 1 E GLU 78  ? I GLU 86  
526 1 Y 1 E ARG 79  ? I ARG 87  
527 1 Y 1 E HIS 80  ? I HIS 88  
528 1 Y 1 E VAL 81  ? I VAL 89  
529 1 Y 1 E GLY 82  ? I GLY 90  
530 1 Y 1 E ASP 83  ? I ASP 91  
531 1 Y 1 E LEU 84  ? I LEU 92  
532 1 Y 1 E GLY 85  ? I GLY 93  
533 1 Y 1 E ASN 86  ? I ASN 94  
534 1 Y 1 E VAL 87  ? I VAL 95  
535 1 Y 1 E THR 88  ? I THR 96  
536 1 Y 1 E ALA 89  ? I ALA 97  
537 1 Y 1 E ASP 90  ? I ASP 98  
538 1 Y 1 E LYS 91  ? I LYS 99  
539 1 Y 1 E ASP 92  ? I ASP 100 
540 1 Y 1 E GLY 93  ? I GLY 101 
541 1 Y 1 E VAL 94  ? I VAL 102 
542 1 Y 1 E ALA 95  ? I ALA 103 
543 1 Y 1 E ASP 96  ? I ASP 104 
544 1 Y 1 E VAL 97  ? I VAL 105 
545 1 Y 1 E SER 98  ? I SER 106 
546 1 Y 1 E ILE 99  ? I ILE 107 
547 1 Y 1 E GLU 100 ? I GLU 108 
548 1 Y 1 E ASP 101 ? I ASP 109 
549 1 Y 1 E SER 102 ? I SER 110 
550 1 Y 1 E VAL 103 ? I VAL 111 
551 1 Y 1 E ILE 104 ? I ILE 112 
552 1 Y 1 E SER 105 ? I SER 113 
553 1 Y 1 E LEU 106 ? I LEU 114 
554 1 Y 1 E SER 107 ? I SER 115 
555 1 Y 1 E GLY 108 ? I GLY 116 
556 1 Y 1 E ASP 109 ? I ASP 117 
557 1 Y 1 E HIS 110 ? I HIS 118 
558 1 Y 1 E ALA 111 ? I ALA 119 
559 1 Y 1 E ILE 112 ? I ILE 120 
560 1 Y 1 E ILE 113 ? I ILE 121 
561 1 Y 1 E GLY 114 ? I GLY 122 
562 1 Y 1 E ARG 115 ? I ARG 123 
563 1 Y 1 E THR 116 ? I THR 124 
564 1 Y 1 E LEU 117 ? I LEU 125 
565 1 Y 1 E VAL 118 ? I VAL 126 
566 1 Y 1 E VAL 119 ? I VAL 127 
567 1 Y 1 E HIS 120 ? I HIS 128 
568 1 Y 1 E GLU 121 ? I GLU 129 
569 1 Y 1 E LYS 122 ? I LYS 130 
570 1 Y 1 E ALA 123 ? I ALA 131 
571 1 Y 1 E ASP 124 ? I ASP 132 
572 1 Y 1 E ASP 125 ? I ASP 133 
573 1 Y 1 E LEU 126 ? I LEU 134 
574 1 Y 1 E GLY 127 ? I GLY 135 
575 1 Y 1 E LYS 128 ? I LYS 136 
576 1 Y 1 E GLY 129 ? I GLY 137 
577 1 Y 1 E GLY 130 ? I GLY 138 
578 1 Y 1 E ASN 131 ? I ASN 139 
579 1 Y 1 E GLU 132 ? I GLU 140 
580 1 Y 1 E GLU 133 ? I GLU 141 
581 1 Y 1 E SER 134 ? I SER 142 
582 1 Y 1 E THR 135 ? I THR 143 
583 1 Y 1 E LYS 136 ? I LYS 144 
584 1 Y 1 E THR 137 ? I THR 145 
585 1 Y 1 E GLY 138 ? I GLY 146 
586 1 Y 1 E ASN 139 ? I ASN 147 
587 1 Y 1 E ALA 140 ? I ALA 148 
588 1 Y 1 E GLY 141 ? I GLY 149 
589 1 Y 1 E SER 142 ? I SER 150 
590 1 Y 1 E ARG 143 ? I ARG 151 
591 1 Y 1 E LEU 144 ? I LEU 152 
592 1 Y 1 E ALA 145 ? I ALA 153 
593 1 Y 1 E CYS 146 ? I CYS 154 
594 1 Y 1 E GLY 147 ? I GLY 155 
595 1 Y 1 E VAL 148 ? I VAL 156 
596 1 Y 1 E ILE 149 ? I ILE 157 
597 1 Y 1 E GLY 150 ? I GLY 158 
598 1 Y 1 E ILE 151 ? I ILE 159 
599 1 Y 1 E ALA 152 ? I ALA 160 
600 1 Y 1 E GLN 153 ? I GLN 161 
601 1 Y 1 F GLY -7  ? K GLY 1   
602 1 Y 1 F ALA -6  ? K ALA 2   
603 1 Y 1 F MET -5  ? K MET 3   
604 1 Y 1 F ASP -4  ? K ASP 4   
605 1 Y 1 F PRO -3  ? K PRO 5   
606 1 Y 1 F GLU -2  ? K GLU 6   
607 1 Y 1 F PHE -1  ? K PHE 7   
608 1 Y 1 F MET 0   ? K MET 8   
609 1 Y 1 F LEU 42  ? K LEU 50  
610 1 Y 1 F HIS 43  ? K HIS 51  
611 1 Y 1 F GLY 44  ? K GLY 52  
612 1 Y 1 F PHE 45  ? K PHE 53  
613 1 Y 1 F HIS 46  ? K HIS 54  
614 1 Y 1 F VAL 47  ? K VAL 55  
615 1 Y 1 F HIS 48  ? K HIS 56  
616 1 Y 1 F GLU 49  ? K GLU 57  
617 1 Y 1 F PHE 50  ? K PHE 58  
618 1 Y 1 F GLY 51  ? K GLY 59  
619 1 Y 1 F ASP 52  ? K ASP 60  
620 1 Y 1 F ASN 53  ? K ASN 61  
621 1 Y 1 F THR 54  ? K THR 62  
622 1 Y 1 F ALA 55  ? K ALA 63  
623 1 Y 1 F GLY 56  ? K GLY 64  
624 1 Y 1 F CYS 57  ? K CYS 65  
625 1 Y 1 F THR 58  ? K THR 66  
626 1 Y 1 F SER 59  ? K SER 67  
627 1 Y 1 F ALA 60  ? K ALA 68  
628 1 Y 1 F GLY 61  ? K GLY 69  
629 1 Y 1 F PRO 62  ? K PRO 70  
630 1 Y 1 F HIS 63  ? K HIS 71  
631 1 Y 1 F PHE 64  ? K PHE 72  
632 1 Y 1 F ASN 65  ? K ASN 73  
633 1 Y 1 F PRO 66  ? K PRO 74  
634 1 Y 1 F LEU 67  ? K LEU 75  
635 1 Y 1 F SER 68  ? K SER 76  
636 1 Y 1 F ARG 69  ? K ARG 77  
637 1 Y 1 F LYS 70  ? K LYS 78  
638 1 Y 1 F HIS 71  ? K HIS 79  
639 1 Y 1 F GLY 72  ? K GLY 80  
640 1 Y 1 F GLY 73  ? K GLY 81  
641 1 Y 1 F PRO 74  ? K PRO 82  
642 1 Y 1 F LYS 75  ? K LYS 83  
643 1 Y 1 F ASP 76  ? K ASP 84  
644 1 Y 1 F GLU 77  ? K GLU 85  
645 1 Y 1 F GLU 78  ? K GLU 86  
646 1 Y 1 F ARG 79  ? K ARG 87  
647 1 Y 1 F HIS 80  ? K HIS 88  
648 1 Y 1 F VAL 81  ? K VAL 89  
649 1 Y 1 F GLY 82  ? K GLY 90  
650 1 Y 1 F ASP 83  ? K ASP 91  
651 1 Y 1 F LEU 84  ? K LEU 92  
652 1 Y 1 F GLY 85  ? K GLY 93  
653 1 Y 1 F ASN 86  ? K ASN 94  
654 1 Y 1 F VAL 87  ? K VAL 95  
655 1 Y 1 F THR 88  ? K THR 96  
656 1 Y 1 F ALA 89  ? K ALA 97  
657 1 Y 1 F ASP 90  ? K ASP 98  
658 1 Y 1 F LYS 91  ? K LYS 99  
659 1 Y 1 F ASP 92  ? K ASP 100 
660 1 Y 1 F GLY 93  ? K GLY 101 
661 1 Y 1 F VAL 94  ? K VAL 102 
662 1 Y 1 F ALA 95  ? K ALA 103 
663 1 Y 1 F ASP 96  ? K ASP 104 
664 1 Y 1 F VAL 97  ? K VAL 105 
665 1 Y 1 F SER 98  ? K SER 106 
666 1 Y 1 F ILE 99  ? K ILE 107 
667 1 Y 1 F GLU 100 ? K GLU 108 
668 1 Y 1 F ASP 101 ? K ASP 109 
669 1 Y 1 F SER 102 ? K SER 110 
670 1 Y 1 F VAL 103 ? K VAL 111 
671 1 Y 1 F ILE 104 ? K ILE 112 
672 1 Y 1 F SER 105 ? K SER 113 
673 1 Y 1 F LEU 106 ? K LEU 114 
674 1 Y 1 F SER 107 ? K SER 115 
675 1 Y 1 F GLY 108 ? K GLY 116 
676 1 Y 1 F ASP 109 ? K ASP 117 
677 1 Y 1 F HIS 110 ? K HIS 118 
678 1 Y 1 F ALA 111 ? K ALA 119 
679 1 Y 1 F ILE 112 ? K ILE 120 
680 1 Y 1 F ILE 113 ? K ILE 121 
681 1 Y 1 F GLY 114 ? K GLY 122 
682 1 Y 1 F ARG 115 ? K ARG 123 
683 1 Y 1 F THR 116 ? K THR 124 
684 1 Y 1 F LEU 117 ? K LEU 125 
685 1 Y 1 F VAL 118 ? K VAL 126 
686 1 Y 1 F VAL 119 ? K VAL 127 
687 1 Y 1 F HIS 120 ? K HIS 128 
688 1 Y 1 F GLU 121 ? K GLU 129 
689 1 Y 1 F LYS 122 ? K LYS 130 
690 1 Y 1 F ALA 123 ? K ALA 131 
691 1 Y 1 F ASP 124 ? K ASP 132 
692 1 Y 1 F ASP 125 ? K ASP 133 
693 1 Y 1 F LEU 126 ? K LEU 134 
694 1 Y 1 F GLY 127 ? K GLY 135 
695 1 Y 1 F LYS 128 ? K LYS 136 
696 1 Y 1 F GLY 129 ? K GLY 137 
697 1 Y 1 F GLY 130 ? K GLY 138 
698 1 Y 1 F ASN 131 ? K ASN 139 
699 1 Y 1 F GLU 132 ? K GLU 140 
700 1 Y 1 F GLU 133 ? K GLU 141 
701 1 Y 1 F SER 134 ? K SER 142 
702 1 Y 1 F THR 135 ? K THR 143 
703 1 Y 1 F LYS 136 ? K LYS 144 
704 1 Y 1 F THR 137 ? K THR 145 
705 1 Y 1 F GLY 138 ? K GLY 146 
706 1 Y 1 F ASN 139 ? K ASN 147 
707 1 Y 1 F ALA 140 ? K ALA 148 
708 1 Y 1 F GLY 141 ? K GLY 149 
709 1 Y 1 F SER 142 ? K SER 150 
710 1 Y 1 F ARG 143 ? K ARG 151 
711 1 Y 1 F LEU 144 ? K LEU 152 
712 1 Y 1 F ALA 145 ? K ALA 153 
713 1 Y 1 F CYS 146 ? K CYS 154 
714 1 Y 1 F GLY 147 ? K GLY 155 
715 1 Y 1 F VAL 148 ? K VAL 156 
716 1 Y 1 F ILE 149 ? K ILE 157 
717 1 Y 1 F GLY 150 ? K GLY 158 
718 1 Y 1 F ILE 151 ? K ILE 159 
719 1 Y 1 F ALA 152 ? K ALA 160 
720 1 Y 1 F GLN 153 ? K 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           9JBP 
_em_admin.last_update        2025-02-05 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'Cryo-EM structure of human SOD1 (C6A/C111A) 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                69.6 
# 
_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   179.602 
_em_helical_entity.axial_rise_per_subunit         2.397 
# 
_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         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (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                     1782 
# 
_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   973528 
_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'           CTFFIND-4.1                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           0.8 
_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 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9JBP 
_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 
# 
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  ? 185.328 149.737 117.490 1.00 28.61 ?  1  ALA A N   1 
ATOM 2    C CA  . ALA A 1 9  ? 184.746 150.432 118.631 1.00 25.85 ?  1  ALA A CA  1 
ATOM 3    C C   . ALA A 1 9  ? 183.574 149.647 119.207 1.00 26.65 ?  1  ALA A C   1 
ATOM 4    O O   . ALA A 1 9  ? 183.510 149.409 120.413 1.00 35.46 ?  1  ALA A O   1 
ATOM 5    C CB  . ALA A 1 9  ? 184.304 151.831 118.233 1.00 30.41 ?  1  ALA A CB  1 
ATOM 6    N N   . THR A 1 10 ? 182.645 149.247 118.342 1.00 21.88 ?  2  THR A N   1 
ATOM 7    C CA  . THR A 1 10 ? 181.470 148.493 118.752 1.00 20.68 ?  2  THR A CA  1 
ATOM 8    C C   . THR A 1 10 ? 181.329 147.242 117.899 1.00 16.28 ?  2  THR A C   1 
ATOM 9    O O   . THR A 1 10 ? 181.562 147.275 116.688 1.00 24.08 ?  2  THR A O   1 
ATOM 10   C CB  . THR A 1 10 ? 180.198 149.344 118.656 1.00 23.13 ?  2  THR A CB  1 
ATOM 11   O OG1 . THR A 1 10 ? 179.046 148.510 118.838 1.00 22.10 ?  2  THR A OG1 1 
ATOM 12   C CG2 . THR A 1 10 ? 180.115 150.049 117.316 1.00 25.90 ?  2  THR A CG2 1 
ATOM 13   N N   . LYS A 1 11 ? 180.958 146.137 118.540 1.00 12.40 ?  3  LYS A N   1 
ATOM 14   C CA  . LYS A 1 11 ? 180.751 144.866 117.864 1.00 11.07 ?  3  LYS A CA  1 
ATOM 15   C C   . LYS A 1 11 ? 179.407 144.291 118.282 1.00 8.74  ?  3  LYS A C   1 
ATOM 16   O O   . LYS A 1 11 ? 178.886 144.614 119.353 1.00 13.17 ?  3  LYS A O   1 
ATOM 17   C CB  . LYS A 1 11 ? 181.866 143.845 118.173 1.00 14.24 ?  3  LYS A CB  1 
ATOM 18   C CG  . LYS A 1 11 ? 183.260 144.196 117.648 1.00 15.39 ?  3  LYS A CG  1 
ATOM 19   C CD  . LYS A 1 11 ? 183.954 145.271 118.473 1.00 18.52 ?  3  LYS A CD  1 
ATOM 20   C CE  . LYS A 1 11 ? 185.269 145.691 117.841 1.00 22.30 ?  3  LYS A CE  1 
ATOM 21   N NZ  . LYS A 1 11 ? 185.870 146.859 118.541 1.00 19.90 1  3  LYS A NZ  1 
ATOM 22   N N   . ALA A 1 12 ? 178.848 143.440 117.428 1.00 4.49  ?  4  ALA A N   1 
ATOM 23   C CA  . ALA A 1 12 ? 177.568 142.802 117.711 1.00 4.08  ?  4  ALA A CA  1 
ATOM 24   C C   . ALA A 1 12 ? 177.537 141.443 117.035 1.00 3.13  ?  4  ALA A C   1 
ATOM 25   O O   . ALA A 1 12 ? 177.695 141.354 115.814 1.00 6.26  ?  4  ALA A O   1 
ATOM 26   C CB  . ALA A 1 12 ? 176.403 143.669 117.231 1.00 6.52  ?  4  ALA A CB  1 
ATOM 27   N N   . VAL A 1 13 ? 177.335 140.392 117.824 1.00 1.75  ?  5  VAL A N   1 
ATOM 28   C CA  . VAL A 1 13 ? 177.260 139.026 117.322 1.00 2.31  ?  5  VAL A CA  1 
ATOM 29   C C   . VAL A 1 13 ? 175.977 138.398 117.844 1.00 2.62  ?  5  VAL A C   1 
ATOM 30   O O   . VAL A 1 13 ? 175.687 138.477 119.043 1.00 5.53  ?  5  VAL A O   1 
ATOM 31   C CB  . VAL A 1 13 ? 178.484 138.190 117.745 1.00 2.59  ?  5  VAL A CB  1 
ATOM 32   C CG1 . VAL A 1 13 ? 178.326 136.746 117.296 1.00 2.08  ?  5  VAL A CG1 1 
ATOM 33   C CG2 . VAL A 1 13 ? 179.760 138.794 117.183 1.00 2.27  ?  5  VAL A CG2 1 
ATOM 34   N N   . ALA A 1 14 ? 175.211 137.780 116.950 1.00 2.76  ?  6  ALA A N   1 
ATOM 35   C CA  . ALA A 1 14 ? 173.970 137.108 117.308 1.00 4.23  ?  6  ALA A CA  1 
ATOM 36   C C   . ALA A 1 14 ? 174.009 135.683 116.780 1.00 4.41  ?  6  ALA A C   1 
ATOM 37   O O   . ALA A 1 14 ? 174.229 135.468 115.584 1.00 9.14  ?  6  ALA A O   1 
ATOM 38   C CB  . ALA A 1 14 ? 172.758 137.855 116.750 1.00 5.34  ?  6  ALA A CB  1 
ATOM 39   N N   . VAL A 1 15 ? 173.794 134.716 117.669 1.00 3.00  ?  7  VAL A N   1 
ATOM 40   C CA  . VAL A 1 15 ? 173.804 133.302 117.318 1.00 5.44  ?  7  VAL A CA  1 
ATOM 41   C C   . VAL A 1 15 ? 172.561 132.650 117.905 1.00 6.79  ?  7  VAL A C   1 
ATOM 42   O O   . VAL A 1 15 ? 172.263 132.829 119.091 1.00 12.06 ?  7  VAL A O   1 
ATOM 43   C CB  . VAL A 1 15 ? 175.077 132.596 117.824 1.00 7.38  ?  7  VAL A CB  1 
ATOM 44   C CG1 . VAL A 1 15 ? 174.915 131.085 117.758 1.00 6.30  ?  7  VAL A CG1 1 
ATOM 45   C CG2 . VAL A 1 15 ? 176.285 133.042 117.017 1.00 5.02  ?  7  VAL A CG2 1 
ATOM 46   N N   . LEU A 1 16 ? 171.836 131.902 117.078 1.00 7.33  ?  8  LEU A N   1 
ATOM 47   C CA  . LEU A 1 16 ? 170.674 131.149 117.526 1.00 9.02  ?  8  LEU A CA  1 
ATOM 48   C C   . LEU A 1 16 ? 170.686 129.788 116.850 1.00 13.78 ?  8  LEU A C   1 
ATOM 49   O O   . LEU A 1 16 ? 170.919 129.694 115.642 1.00 25.23 ?  8  LEU A O   1 
ATOM 50   C CB  . LEU A 1 16 ? 169.373 131.897 117.213 1.00 11.16 ?  8  LEU A CB  1 
ATOM 51   C CG  . LEU A 1 16 ? 168.059 131.113 117.270 1.00 14.67 ?  8  LEU A CG  1 
ATOM 52   C CD1 . LEU A 1 16 ? 167.858 130.448 118.617 1.00 20.42 ?  8  LEU A CD1 1 
ATOM 53   C CD2 . LEU A 1 16 ? 166.885 132.021 116.949 1.00 17.98 ?  8  LEU A CD2 1 
ATOM 54   N N   . LYS A 1 17 ? 170.436 128.738 117.630 1.00 11.41 ?  9  LYS A N   1 
ATOM 55   C CA  . LYS A 1 17 ? 170.433 127.374 117.117 1.00 13.56 ?  9  LYS A CA  1 
ATOM 56   C C   . LYS A 1 17 ? 169.102 126.718 117.473 1.00 15.29 ?  9  LYS A C   1 
ATOM 57   O O   . LYS A 1 17 ? 169.062 125.597 117.989 1.00 16.23 ?  9  LYS A O   1 
ATOM 58   C CB  . LYS A 1 17 ? 171.623 126.589 117.682 1.00 13.71 ?  9  LYS A CB  1 
ATOM 59   C CG  . LYS A 1 17 ? 171.878 125.232 117.035 1.00 14.94 ?  9  LYS A CG  1 
ATOM 60   C CD  . LYS A 1 17 ? 172.785 124.375 117.903 1.00 14.57 ?  9  LYS A CD  1 
ATOM 61   C CE  . LYS A 1 17 ? 174.189 124.952 117.973 1.00 16.26 ?  9  LYS A CE  1 
ATOM 62   N NZ  . LYS A 1 17 ? 175.196 123.922 118.348 1.00 15.38 1  9  LYS A NZ  1 
ATOM 63   N N   . GLY A 1 18 ? 168.008 127.419 117.214 1.00 16.28 ?  10 GLY A N   1 
ATOM 64   C CA  . GLY A 1 18 ? 166.693 126.947 117.606 1.00 20.25 ?  10 GLY A CA  1 
ATOM 65   C C   . GLY A 1 18 ? 165.719 126.948 116.451 1.00 26.23 ?  10 GLY A C   1 
ATOM 66   O O   . GLY A 1 18 ? 165.780 127.800 115.563 1.00 26.39 ?  10 GLY A O   1 
ATOM 67   N N   . ASP A 1 19 ? 164.801 125.978 116.479 1.00 32.75 ?  11 ASP A N   1 
ATOM 68   C CA  . ASP A 1 19 ? 163.778 125.850 115.449 1.00 34.06 ?  11 ASP A CA  1 
ATOM 69   C C   . ASP A 1 19 ? 162.783 127.005 115.486 1.00 34.38 ?  11 ASP A C   1 
ATOM 70   O O   . ASP A 1 19 ? 162.080 127.236 114.499 1.00 31.97 ?  11 ASP A O   1 
ATOM 71   C CB  . ASP A 1 19 ? 163.063 124.503 115.626 1.00 37.30 ?  11 ASP A CB  1 
ATOM 72   C CG  . ASP A 1 19 ? 162.312 124.044 114.378 1.00 41.59 ?  11 ASP A CG  1 
ATOM 73   O OD1 . ASP A 1 19 ? 161.710 124.867 113.665 1.00 43.60 -1 11 ASP A OD1 1 
ATOM 74   O OD2 . ASP A 1 19 ? 162.322 122.823 114.115 1.00 45.72 ?  11 ASP A OD2 1 
ATOM 75   N N   . GLY A 1 20 ? 162.717 127.742 116.591 1.00 35.94 ?  12 GLY A N   1 
ATOM 76   C CA  . GLY A 1 20 ? 161.784 128.835 116.727 1.00 34.39 ?  12 GLY A CA  1 
ATOM 77   C C   . GLY A 1 20 ? 161.990 129.943 115.716 1.00 29.47 ?  12 GLY A C   1 
ATOM 78   O O   . GLY A 1 20 ? 163.120 130.315 115.382 1.00 28.48 ?  12 GLY A O   1 
ATOM 79   N N   . PRO A 1 21 ? 160.890 130.486 115.202 1.00 26.81 ?  13 PRO A N   1 
ATOM 80   C CA  . PRO A 1 21 ? 160.989 131.611 114.267 1.00 26.71 ?  13 PRO A CA  1 
ATOM 81   C C   . PRO A 1 21 ? 161.557 132.851 114.938 1.00 25.45 ?  13 PRO A C   1 
ATOM 82   O O   . PRO A 1 21 ? 161.387 133.073 116.139 1.00 33.91 ?  13 PRO A O   1 
ATOM 83   C CB  . PRO A 1 21 ? 159.538 131.836 113.825 1.00 25.06 ?  13 PRO A CB  1 
ATOM 84   C CG  . PRO A 1 21 ? 158.829 130.558 114.148 1.00 25.84 ?  13 PRO A CG  1 
ATOM 85   C CD  . PRO A 1 21 ? 159.502 130.029 115.372 1.00 27.75 ?  13 PRO A CD  1 
ATOM 86   N N   . VAL A 1 22 ? 162.241 133.665 114.140 1.00 20.80 ?  14 VAL A N   1 
ATOM 87   C CA  . VAL A 1 22 ? 162.790 134.935 114.595 1.00 18.20 ?  14 VAL A CA  1 
ATOM 88   C C   . VAL A 1 22 ? 161.836 136.044 114.180 1.00 23.47 ?  14 VAL A C   1 
ATOM 89   O O   . VAL A 1 22 ? 161.447 136.133 113.009 1.00 33.83 ?  14 VAL A O   1 
ATOM 90   C CB  . VAL A 1 22 ? 164.196 135.172 114.018 1.00 17.86 ?  14 VAL A CB  1 
ATOM 91   C CG1 . VAL A 1 22 ? 164.541 136.650 114.049 1.00 15.32 ?  14 VAL A CG1 1 
ATOM 92   C CG2 . VAL A 1 22 ? 165.222 134.370 114.790 1.00 22.05 ?  14 VAL A CG2 1 
ATOM 93   N N   . GLN A 1 23 ? 161.455 136.888 115.136 1.00 22.36 ?  15 GLN A N   1 
ATOM 94   C CA  . GLN A 1 23 ? 160.507 137.971 114.895 1.00 20.30 ?  15 GLN A CA  1 
ATOM 95   C C   . GLN A 1 23 ? 161.073 139.252 115.492 1.00 19.11 ?  15 GLN A C   1 
ATOM 96   O O   . GLN A 1 23 ? 161.228 139.355 116.713 1.00 27.36 ?  15 GLN A O   1 
ATOM 97   C CB  . GLN A 1 23 ? 159.141 137.642 115.497 1.00 18.87 ?  15 GLN A CB  1 
ATOM 98   C CG  . GLN A 1 23 ? 157.984 138.360 114.840 1.00 17.91 ?  15 GLN A CG  1 
ATOM 99   C CD  . GLN A 1 23 ? 156.747 137.493 114.746 1.00 21.22 ?  15 GLN A CD  1 
ATOM 100  O OE1 . GLN A 1 23 ? 156.017 137.323 115.722 1.00 15.30 ?  15 GLN A OE1 1 
ATOM 101  N NE2 . GLN A 1 23 ? 156.507 136.934 113.566 1.00 24.15 ?  15 GLN A NE2 1 
ATOM 102  N N   . GLY A 1 24 ? 161.379 140.223 114.636 1.00 12.80 ?  16 GLY A N   1 
ATOM 103  C CA  . GLY A 1 24 ? 161.912 141.490 115.095 1.00 7.81  ?  16 GLY A CA  1 
ATOM 104  C C   . GLY A 1 24 ? 163.175 141.903 114.371 1.00 4.63  ?  16 GLY A C   1 
ATOM 105  O O   . GLY A 1 24 ? 163.414 141.477 113.238 1.00 5.60  ?  16 GLY A O   1 
ATOM 106  N N   . ILE A 1 25 ? 163.992 142.731 115.009 1.00 3.20  ?  17 ILE A N   1 
ATOM 107  C CA  . ILE A 1 25 ? 165.248 143.183 114.426 1.00 2.97  ?  17 ILE A CA  1 
ATOM 108  C C   . ILE A 1 25 ? 166.403 142.504 115.143 1.00 4.18  ?  17 ILE A C   1 
ATOM 109  O O   . ILE A 1 25 ? 166.338 142.217 116.343 1.00 20.36 ?  17 ILE A O   1 
ATOM 110  C CB  . ILE A 1 25 ? 165.381 144.717 114.495 1.00 2.76  ?  17 ILE A CB  1 
ATOM 111  C CG1 . ILE A 1 25 ? 164.013 145.379 114.358 1.00 3.84  ?  17 ILE A CG1 1 
ATOM 112  C CG2 . ILE A 1 25 ? 166.321 145.218 113.417 1.00 3.86  ?  17 ILE A CG2 1 
ATOM 113  C CD1 . ILE A 1 25 ? 164.040 146.862 114.624 1.00 2.74  ?  17 ILE A CD1 1 
ATOM 114  N N   . ILE A 1 26 ? 167.473 142.241 114.398 1.00 2.67  ?  18 ILE A N   1 
ATOM 115  C CA  . ILE A 1 26 ? 168.683 141.627 114.929 1.00 1.40  ?  18 ILE A CA  1 
ATOM 116  C C   . ILE A 1 26 ? 169.848 142.571 114.672 1.00 1.52  ?  18 ILE A C   1 
ATOM 117  O O   . ILE A 1 26 ? 170.027 143.048 113.547 1.00 2.00  ?  18 ILE A O   1 
ATOM 118  C CB  . ILE A 1 26 ? 168.947 140.249 114.297 1.00 1.45  ?  18 ILE A CB  1 
ATOM 119  C CG1 . ILE A 1 26 ? 167.633 139.501 114.075 1.00 1.29  ?  18 ILE A CG1 1 
ATOM 120  C CG2 . ILE A 1 26 ? 169.879 139.437 115.172 1.00 2.28  ?  18 ILE A CG2 1 
ATOM 121  C CD1 . ILE A 1 26 ? 166.975 139.032 115.342 1.00 1.32  ?  18 ILE A CD1 1 
ATOM 122  N N   . ASN A 1 27 ? 170.635 142.834 115.716 1.00 1.62  ?  19 ASN A N   1 
ATOM 123  C CA  . ASN A 1 27 ? 171.797 143.720 115.630 1.00 2.03  ?  19 ASN A CA  1 
ATOM 124  C C   . ASN A 1 27 ? 171.404 145.112 115.142 1.00 1.29  ?  19 ASN A C   1 
ATOM 125  O O   . ASN A 1 27 ? 172.080 145.713 114.307 1.00 2.24  ?  19 ASN A O   1 
ATOM 126  C CB  . ASN A 1 27 ? 172.887 143.119 114.740 1.00 2.07  ?  19 ASN A CB  1 
ATOM 127  C CG  . ASN A 1 27 ? 173.239 141.699 115.132 1.00 3.34  ?  19 ASN A CG  1 
ATOM 128  O OD1 . ASN A 1 27 ? 173.490 141.409 116.301 1.00 3.83  ?  19 ASN A OD1 1 
ATOM 129  N ND2 . ASN A 1 27 ? 173.258 140.804 114.153 1.00 4.34  ?  19 ASN A ND2 1 
ATOM 130  N N   . PHE A 1 28 ? 170.297 145.625 115.668 1.00 1.33  ?  20 PHE A N   1 
ATOM 131  C CA  . PHE A 1 28 ? 169.859 146.980 115.363 1.00 1.50  ?  20 PHE A CA  1 
ATOM 132  C C   . PHE A 1 28 ? 170.733 147.978 116.112 1.00 2.68  ?  20 PHE A C   1 
ATOM 133  O O   . PHE A 1 28 ? 170.873 147.897 117.336 1.00 9.02  ?  20 PHE A O   1 
ATOM 134  C CB  . PHE A 1 28 ? 168.389 147.145 115.745 1.00 2.39  ?  20 PHE A CB  1 
ATOM 135  C CG  . PHE A 1 28 ? 167.785 148.450 115.319 1.00 1.78  ?  20 PHE A CG  1 
ATOM 136  C CD1 . PHE A 1 28 ? 168.363 149.213 114.322 1.00 2.68  ?  20 PHE A CD1 1 
ATOM 137  C CD2 . PHE A 1 28 ? 166.626 148.908 115.914 1.00 2.10  ?  20 PHE A CD2 1 
ATOM 138  C CE1 . PHE A 1 28 ? 167.802 150.410 113.941 1.00 3.16  ?  20 PHE A CE1 1 
ATOM 139  C CE2 . PHE A 1 28 ? 166.063 150.101 115.534 1.00 2.00  ?  20 PHE A CE2 1 
ATOM 140  C CZ  . PHE A 1 28 ? 166.649 150.852 114.545 1.00 2.66  ?  20 PHE A CZ  1 
ATOM 141  N N   . GLU A 1 29 ? 171.322 148.920 115.379 1.00 1.15  ?  21 GLU A N   1 
ATOM 142  C CA  . GLU A 1 29 ? 172.305 149.850 115.927 1.00 1.57  ?  21 GLU A CA  1 
ATOM 143  C C   . GLU A 1 29 ? 171.954 151.286 115.566 1.00 1.73  ?  21 GLU A C   1 
ATOM 144  O O   . GLU A 1 29 ? 172.789 152.048 115.074 1.00 1.58  ?  21 GLU A O   1 
ATOM 145  C CB  . GLU A 1 29 ? 173.711 149.510 115.440 1.00 1.06  ?  21 GLU A CB  1 
ATOM 146  C CG  . GLU A 1 29 ? 174.008 148.021 115.383 1.00 1.10  ?  21 GLU A CG  1 
ATOM 147  C CD  . GLU A 1 29 ? 175.489 147.721 115.337 1.00 1.23  ?  21 GLU A CD  1 
ATOM 148  O OE1 . GLU A 1 29 ? 176.291 148.677 115.291 1.00 1.37  ?  21 GLU A OE1 1 
ATOM 149  O OE2 . GLU A 1 29 ? 175.851 146.527 115.346 1.00 1.43  -1 21 GLU A OE2 1 
ATOM 150  N N   . GLN A 1 30 ? 170.701 151.674 115.801 1.00 1.74  ?  22 GLN A N   1 
ATOM 151  C CA  . GLN A 1 30 ? 170.287 153.054 115.580 1.00 1.55  ?  22 GLN A CA  1 
ATOM 152  C C   . GLN A 1 30 ? 171.136 154.000 116.420 1.00 2.07  ?  22 GLN A C   1 
ATOM 153  O O   . GLN A 1 30 ? 171.343 153.771 117.613 1.00 7.82  ?  22 GLN A O   1 
ATOM 154  C CB  . GLN A 1 30 ? 168.807 153.221 115.921 1.00 1.81  ?  22 GLN A CB  1 
ATOM 155  C CG  . GLN A 1 30 ? 168.409 154.641 116.267 1.00 2.66  ?  22 GLN A CG  1 
ATOM 156  C CD  . GLN A 1 30 ? 166.907 154.849 116.279 1.00 2.57  ?  22 GLN A CD  1 
ATOM 157  O OE1 . GLN A 1 30 ? 166.236 154.667 115.265 1.00 2.36  ?  22 GLN A OE1 1 
ATOM 158  N NE2 . GLN A 1 30 ? 166.372 155.242 117.428 1.00 2.89  ?  22 GLN A NE2 1 
ATOM 159  N N   . LYS A 1 31 ? 171.634 155.065 115.795 1.00 1.87  ?  23 LYS A N   1 
ATOM 160  C CA  . LYS A 1 31 ? 172.601 155.930 116.455 1.00 1.92  ?  23 LYS A CA  1 
ATOM 161  C C   . LYS A 1 31 ? 172.460 157.361 115.962 1.00 3.06  ?  23 LYS A C   1 
ATOM 162  O O   . LYS A 1 31 ? 172.420 157.602 114.752 1.00 5.25  ?  23 LYS A O   1 
ATOM 163  C CB  . LYS A 1 31 ? 174.028 155.424 116.214 1.00 1.73  ?  23 LYS A CB  1 
ATOM 164  C CG  . LYS A 1 31 ? 175.106 156.483 116.357 1.00 1.66  ?  23 LYS A CG  1 
ATOM 165  C CD  . LYS A 1 31 ? 176.493 155.866 116.450 1.00 2.02  ?  23 LYS A CD  1 
ATOM 166  C CE  . LYS A 1 31 ? 176.591 154.573 115.657 1.00 2.93  ?  23 LYS A CE  1 
ATOM 167  N NZ  . LYS A 1 31 ? 177.885 153.876 115.892 1.00 4.12  1  23 LYS A NZ  1 
ATOM 168  N N   . GLU A 1 32 ? 172.396 158.300 116.908 1.00 4.10  ?  24 GLU A N   1 
ATOM 169  C CA  . GLU A 1 32 ? 172.370 159.735 116.616 1.00 5.39  ?  24 GLU A CA  1 
ATOM 170  C C   . GLU A 1 32 ? 171.247 160.092 115.648 1.00 7.25  ?  24 GLU A C   1 
ATOM 171  O O   . GLU A 1 32 ? 171.423 160.888 114.724 1.00 9.80  ?  24 GLU A O   1 
ATOM 172  C CB  . GLU A 1 32 ? 173.721 160.209 116.079 1.00 3.63  ?  24 GLU A CB  1 
ATOM 173  C CG  . GLU A 1 32 ? 174.873 160.004 117.044 1.00 4.42  ?  24 GLU A CG  1 
ATOM 174  C CD  . GLU A 1 32 ? 176.216 160.345 116.432 1.00 4.91  ?  24 GLU A CD  1 
ATOM 175  O OE1 . GLU A 1 32 ? 176.413 161.517 116.047 1.00 6.01  ?  24 GLU A OE1 1 
ATOM 176  O OE2 . GLU A 1 32 ? 177.074 159.443 116.337 1.00 3.74  -1 24 GLU A OE2 1 
ATOM 177  N N   . SER A 1 33 ? 170.078 159.505 115.866 1.00 6.77  ?  25 SER A N   1 
ATOM 178  C CA  . SER A 1 33 ? 168.937 159.702 114.987 1.00 10.76 ?  25 SER A CA  1 
ATOM 179  C C   . SER A 1 33 ? 167.752 160.237 115.789 1.00 15.28 ?  25 SER A C   1 
ATOM 180  O O   . SER A 1 33 ? 167.872 160.584 116.966 1.00 20.99 ?  25 SER A O   1 
ATOM 181  C CB  . SER A 1 33 ? 168.578 158.399 114.273 1.00 11.58 ?  25 SER A CB  1 
ATOM 182  O OG  . SER A 1 33 ? 167.977 157.493 115.176 1.00 6.84  ?  25 SER A OG  1 
ATOM 183  N N   . ASN A 1 34 ? 166.598 160.311 115.128 1.00 13.65 ?  26 ASN A N   1 
ATOM 184  C CA  . ASN A 1 34 ? 165.358 160.743 115.769 1.00 14.20 ?  26 ASN A CA  1 
ATOM 185  C C   . ASN A 1 34 ? 164.216 160.013 115.069 1.00 14.73 ?  26 ASN A C   1 
ATOM 186  O O   . ASN A 1 34 ? 163.803 160.406 113.974 1.00 20.09 ?  26 ASN A O   1 
ATOM 187  C CB  . ASN A 1 34 ? 165.190 162.253 115.690 1.00 20.75 ?  26 ASN A CB  1 
ATOM 188  C CG  . ASN A 1 34 ? 163.798 162.703 116.076 1.00 23.14 ?  26 ASN A CG  1 
ATOM 189  O OD1 . ASN A 1 34 ? 163.090 163.320 115.281 1.00 26.41 ?  26 ASN A OD1 1 
ATOM 190  N ND2 . ASN A 1 34 ? 163.396 162.395 117.303 1.00 21.92 ?  26 ASN A ND2 1 
ATOM 191  N N   . GLY A 1 35 ? 163.720 158.953 115.698 1.00 9.69  ?  27 GLY A N   1 
ATOM 192  C CA  . GLY A 1 35 ? 162.651 158.173 115.127 1.00 6.74  ?  27 GLY A CA  1 
ATOM 193  C C   . GLY A 1 35 ? 162.078 157.168 116.101 1.00 2.59  ?  27 GLY A C   1 
ATOM 194  O O   . GLY A 1 35 ? 162.803 156.411 116.752 1.00 2.30  ?  27 GLY A O   1 
ATOM 195  N N   . PRO A 1 36 ? 160.756 157.146 116.220 1.00 2.08  ?  28 PRO A N   1 
ATOM 196  C CA  . PRO A 1 36 ? 160.082 156.164 117.092 1.00 2.22  ?  28 PRO A CA  1 
ATOM 197  C C   . PRO A 1 36 ? 160.028 154.772 116.466 1.00 1.46  ?  28 PRO A C   1 
ATOM 198  O O   . PRO A 1 36 ? 159.045 154.347 115.860 1.00 1.56  ?  28 PRO A O   1 
ATOM 199  C CB  . PRO A 1 36 ? 158.688 156.770 117.267 1.00 3.18  ?  28 PRO A CB  1 
ATOM 200  C CG  . PRO A 1 36 ? 158.469 157.574 116.039 1.00 2.60  ?  28 PRO A CG  1 
ATOM 201  C CD  . PRO A 1 36 ? 159.810 158.102 115.620 1.00 3.15  ?  28 PRO A CD  1 
ATOM 202  N N   . VAL A 1 37 ? 161.131 154.035 116.612 1.00 1.09  ?  29 VAL A N   1 
ATOM 203  C CA  . VAL A 1 37 ? 161.187 152.673 116.098 1.00 1.31  ?  29 VAL A CA  1 
ATOM 204  C C   . VAL A 1 37 ? 160.173 151.800 116.822 1.00 1.06  ?  29 VAL A C   1 
ATOM 205  O O   . VAL A 1 37 ? 160.115 151.769 118.056 1.00 2.25  ?  29 VAL A O   1 
ATOM 206  C CB  . VAL A 1 37 ? 162.615 152.117 116.209 1.00 1.17  ?  29 VAL A CB  1 
ATOM 207  C CG1 . VAL A 1 37 ? 163.152 152.292 117.600 1.00 1.83  ?  29 VAL A CG1 1 
ATOM 208  C CG2 . VAL A 1 37 ? 162.625 150.641 115.847 1.00 1.49  ?  29 VAL A CG2 1 
ATOM 209  N N   . LYS A 1 38 ? 159.354 151.097 116.047 1.00 0.86  ?  30 LYS A N   1 
ATOM 210  C CA  . LYS A 1 38 ? 158.305 150.235 116.573 1.00 1.06  ?  30 LYS A CA  1 
ATOM 211  C C   . LYS A 1 38 ? 158.445 148.851 115.960 1.00 1.21  ?  30 LYS A C   1 
ATOM 212  O O   . LYS A 1 38 ? 158.578 148.719 114.740 1.00 3.08  ?  30 LYS A O   1 
ATOM 213  C CB  . LYS A 1 38 ? 156.920 150.816 116.274 1.00 1.14  ?  30 LYS A CB  1 
ATOM 214  C CG  . LYS A 1 38 ? 155.762 149.920 116.676 1.00 1.32  ?  30 LYS A CG  1 
ATOM 215  C CD  . LYS A 1 38 ? 154.431 150.553 116.308 1.00 1.00  ?  30 LYS A CD  1 
ATOM 216  C CE  . LYS A 1 38 ? 153.269 149.637 116.653 1.00 1.14  ?  30 LYS A CE  1 
ATOM 217  N NZ  . LYS A 1 38 ? 151.955 150.260 116.326 1.00 0.73  1  30 LYS A NZ  1 
ATOM 218  N N   . VAL A 1 39 ? 158.418 147.824 116.804 1.00 0.91  ?  31 VAL A N   1 
ATOM 219  C CA  . VAL A 1 39 ? 158.525 146.439 116.365 1.00 1.50  ?  31 VAL A CA  1 
ATOM 220  C C   . VAL A 1 39 ? 157.277 145.703 116.820 1.00 2.30  ?  31 VAL A C   1 
ATOM 221  O O   . VAL A 1 39 ? 156.948 145.706 118.012 1.00 4.40  ?  31 VAL A O   1 
ATOM 222  C CB  . VAL A 1 39 ? 159.790 145.760 116.914 1.00 2.29  ?  31 VAL A CB  1 
ATOM 223  C CG1 . VAL A 1 39 ? 159.889 144.333 116.399 1.00 2.31  ?  31 VAL A CG1 1 
ATOM 224  C CG2 . VAL A 1 39 ? 161.022 146.557 116.534 1.00 1.58  ?  31 VAL A CG2 1 
ATOM 225  N N   . TRP A 1 40 ? 156.588 145.070 115.877 1.00 2.21  ?  32 TRP A N   1 
ATOM 226  C CA  . TRP A 1 40 ? 155.373 144.316 116.155 1.00 2.99  ?  32 TRP A CA  1 
ATOM 227  C C   . TRP A 1 40 ? 155.606 142.866 115.762 1.00 3.21  ?  32 TRP A C   1 
ATOM 228  O O   . TRP A 1 40 ? 155.959 142.579 114.613 1.00 5.23  ?  32 TRP A O   1 
ATOM 229  C CB  . TRP A 1 40 ? 154.181 144.906 115.398 1.00 4.17  ?  32 TRP A CB  1 
ATOM 230  C CG  . TRP A 1 40 ? 152.844 144.402 115.853 1.00 3.61  ?  32 TRP A CG  1 
ATOM 231  C CD1 . TRP A 1 40 ? 152.445 143.102 115.952 1.00 4.41  ?  32 TRP A CD1 1 
ATOM 232  C CD2 . TRP A 1 40 ? 151.727 145.196 116.268 1.00 3.72  ?  32 TRP A CD2 1 
ATOM 233  N NE1 . TRP A 1 40 ? 151.150 143.036 116.404 1.00 3.94  ?  32 TRP A NE1 1 
ATOM 234  C CE2 . TRP A 1 40 ? 150.686 144.309 116.605 1.00 4.98  ?  32 TRP A CE2 1 
ATOM 235  C CE3 . TRP A 1 40 ? 151.506 146.571 116.387 1.00 3.71  ?  32 TRP A CE3 1 
ATOM 236  C CZ2 . TRP A 1 40 ? 149.444 144.752 117.054 1.00 6.31  ?  32 TRP A CZ2 1 
ATOM 237  C CZ3 . TRP A 1 40 ? 150.272 147.009 116.833 1.00 4.28  ?  32 TRP A CZ3 1 
ATOM 238  C CH2 . TRP A 1 40 ? 149.257 146.102 117.160 1.00 5.60  ?  32 TRP A CH2 1 
ATOM 239  N N   . GLY A 1 41 ? 155.411 141.958 116.712 1.00 3.12  ?  33 GLY A N   1 
ATOM 240  C CA  . GLY A 1 41 ? 155.596 140.547 116.447 1.00 7.91  ?  33 GLY A CA  1 
ATOM 241  C C   . GLY A 1 41 ? 154.429 139.699 116.902 1.00 9.98  ?  33 GLY A C   1 
ATOM 242  O O   . GLY A 1 41 ? 154.111 139.655 118.094 1.00 15.16 ?  33 GLY A O   1 
ATOM 243  N N   . SER A 1 42 ? 153.781 139.017 115.962 1.00 7.03  ?  34 SER A N   1 
ATOM 244  C CA  . SER A 1 42 ? 152.631 138.175 116.257 1.00 9.59  ?  34 SER A CA  1 
ATOM 245  C C   . SER A 1 42 ? 152.839 136.808 115.626 1.00 12.86 ?  34 SER A C   1 
ATOM 246  O O   . SER A 1 42 ? 153.340 136.711 114.502 1.00 22.86 ?  34 SER A O   1 
ATOM 247  C CB  . SER A 1 42 ? 151.334 138.807 115.741 1.00 10.24 ?  34 SER A CB  1 
ATOM 248  O OG  . SER A 1 42 ? 150.224 137.964 115.989 1.00 10.90 ?  34 SER A OG  1 
ATOM 249  N N   . ILE A 1 43 ? 152.461 135.758 116.352 1.00 8.73  ?  35 ILE A N   1 
ATOM 250  C CA  . ILE A 1 43 ? 152.527 134.389 115.853 1.00 12.07 ?  35 ILE A CA  1 
ATOM 251  C C   . ILE A 1 43 ? 151.391 133.598 116.485 1.00 13.05 ?  35 ILE A C   1 
ATOM 252  O O   . ILE A 1 43 ? 151.331 133.461 117.712 1.00 18.89 ?  35 ILE A O   1 
ATOM 253  C CB  . ILE A 1 43 ? 153.886 133.728 116.146 1.00 13.89 ?  35 ILE A CB  1 
ATOM 254  C CG1 . ILE A 1 43 ? 153.796 132.208 115.987 1.00 16.89 ?  35 ILE A CG1 1 
ATOM 255  C CG2 . ILE A 1 43 ? 154.404 134.128 117.517 1.00 19.63 ?  35 ILE A CG2 1 
ATOM 256  C CD1 . ILE A 1 43 ? 155.140 131.516 115.991 1.00 19.55 ?  35 ILE A CD1 1 
ATOM 257  N N   . LYS A 1 44 ? 150.484 133.085 115.654 1.00 13.71 ?  36 LYS A N   1 
ATOM 258  C CA  . LYS A 1 44 ? 149.333 132.324 116.129 1.00 19.51 ?  36 LYS A CA  1 
ATOM 259  C C   . LYS A 1 44 ? 149.340 130.937 115.497 1.00 24.14 ?  36 LYS A C   1 
ATOM 260  O O   . LYS A 1 44 ? 148.705 130.714 114.461 1.00 35.30 ?  36 LYS A O   1 
ATOM 261  C CB  . LYS A 1 44 ? 148.027 133.060 115.826 1.00 19.26 ?  36 LYS A CB  1 
ATOM 262  C CG  . LYS A 1 44 ? 147.977 134.475 116.384 1.00 15.07 ?  36 LYS A CG  1 
ATOM 263  C CD  . LYS A 1 44 ? 146.841 135.279 115.776 1.00 15.29 ?  36 LYS A CD  1 
ATOM 264  C CE  . LYS A 1 44 ? 145.496 134.851 116.339 1.00 19.88 ?  36 LYS A CE  1 
ATOM 265  N NZ  . LYS A 1 44 ? 144.473 135.924 116.193 1.00 20.42 1  36 LYS A NZ  1 
ATOM 266  N N   . GLY A 1 45 ? 150.053 130.006 116.128 1.00 22.39 ?  37 GLY A N   1 
ATOM 267  C CA  . GLY A 1 45 ? 150.099 128.634 115.673 1.00 34.53 ?  37 GLY A CA  1 
ATOM 268  C C   . GLY A 1 45 ? 150.842 127.766 116.668 1.00 50.93 ?  37 GLY A C   1 
ATOM 269  O O   . GLY A 1 45 ? 151.136 128.197 117.784 1.00 60.96 ?  37 GLY A O   1 
ATOM 270  N N   . LEU A 1 46 ? 151.167 126.542 116.260 1.00 55.90 ?  38 LEU A N   1 
ATOM 271  C CA  . LEU A 1 46 ? 151.819 125.601 117.160 1.00 62.17 ?  38 LEU A CA  1 
ATOM 272  C C   . LEU A 1 46 ? 153.099 125.060 116.540 1.00 63.02 ?  38 LEU A C   1 
ATOM 273  O O   . LEU A 1 46 ? 153.184 124.847 115.330 1.00 68.61 ?  38 LEU A O   1 
ATOM 274  C CB  . LEU A 1 46 ? 150.893 124.440 117.554 1.00 66.59 ?  38 LEU A CB  1 
ATOM 275  C CG  . LEU A 1 46 ? 150.453 123.344 116.582 1.00 64.08 ?  38 LEU A CG  1 
ATOM 276  C CD1 . LEU A 1 46 ? 149.703 122.267 117.329 1.00 67.23 ?  38 LEU A CD1 1 
ATOM 277  C CD2 . LEU A 1 46 ? 149.510 123.937 115.565 1.00 56.33 ?  38 LEU A CD2 1 
ATOM 278  N N   . THR A 1 47 ? 154.091 124.836 117.399 1.00 61.74 ?  39 THR A N   1 
ATOM 279  C CA  . THR A 1 47 ? 155.382 124.297 117.004 1.00 64.45 ?  39 THR A CA  1 
ATOM 280  C C   . THR A 1 47 ? 155.632 122.998 117.758 1.00 65.26 ?  39 THR A C   1 
ATOM 281  O O   . THR A 1 47 ? 155.035 122.753 118.812 1.00 68.25 ?  39 THR A O   1 
ATOM 282  C CB  . THR A 1 47 ? 156.505 125.303 117.278 1.00 67.76 ?  39 THR A CB  1 
ATOM 283  O OG1 . THR A 1 47 ? 156.673 125.462 118.691 1.00 67.28 ?  39 THR A OG1 1 
ATOM 284  C CG2 . THR A 1 47 ? 156.163 126.654 116.674 1.00 66.15 ?  39 THR A CG2 1 
ATOM 285  N N   . GLU A 1 48 ? 156.510 122.162 117.212 1.00 66.18 ?  40 GLU A N   1 
ATOM 286  C CA  . GLU A 1 48 ? 156.824 120.870 117.801 1.00 61.50 ?  40 GLU A CA  1 
ATOM 287  C C   . GLU A 1 48 ? 158.335 120.702 117.880 1.00 59.06 ?  40 GLU A C   1 
ATOM 288  O O   . GLU A 1 48 ? 159.097 121.461 117.276 1.00 60.79 ?  40 GLU A O   1 
ATOM 289  C CB  . GLU A 1 48 ? 156.206 119.725 116.991 1.00 62.11 ?  40 GLU A CB  1 
ATOM 290  C CG  . GLU A 1 48 ? 154.779 119.378 117.383 1.00 60.56 ?  40 GLU A CG  1 
ATOM 291  C CD  . GLU A 1 48 ? 153.783 120.439 116.956 1.00 65.93 ?  40 GLU A CD  1 
ATOM 292  O OE1 . GLU A 1 48 ? 153.785 120.815 115.767 1.00 71.63 ?  40 GLU A OE1 1 
ATOM 293  O OE2 . GLU A 1 48 ? 152.995 120.896 117.808 1.00 64.65 -1 40 GLU A OE2 1 
ATOM 294  N N   . GLY A 1 49 ? 158.757 119.698 118.640 1.00 60.96 ?  41 GLY A N   1 
ATOM 295  C CA  . GLY A 1 49 ? 160.168 119.404 118.801 1.00 63.08 ?  41 GLY A CA  1 
ATOM 296  C C   . GLY A 1 49 ? 160.568 118.068 118.207 1.00 60.55 ?  41 GLY A C   1 
ATOM 297  O O   . GLY A 1 49 ? 159.761 117.141 118.141 1.00 62.50 ?  41 GLY A O   1 
ATOM 298  N N   . UNK B 2 1  ? 179.367 116.868 119.159 1.00 26.05 ?  1  UNK G N   1 
ATOM 299  C CA  . UNK B 2 1  ? 180.346 117.718 119.827 1.00 26.04 ?  1  UNK G CA  1 
ATOM 300  C C   . UNK B 2 1  ? 180.189 119.172 119.396 1.00 26.58 ?  1  UNK G C   1 
ATOM 301  O O   . UNK B 2 1  ? 181.127 119.779 118.880 1.00 29.40 ?  1  UNK G O   1 
ATOM 302  C CB  . UNK B 2 1  ? 181.756 117.228 119.539 1.00 22.41 ?  1  UNK G CB  1 
ATOM 303  N N   . UNK B 2 2  ? 178.997 119.722 119.613 1.00 22.86 ?  2  UNK G N   1 
ATOM 304  C CA  . UNK B 2 2  ? 178.726 121.105 119.243 1.00 22.32 ?  2  UNK G CA  1 
ATOM 305  C C   . UNK B 2 2  ? 179.540 122.056 120.110 1.00 21.72 ?  2  UNK G C   1 
ATOM 306  O O   . UNK B 2 2  ? 179.579 121.912 121.336 1.00 26.76 ?  2  UNK G O   1 
ATOM 307  C CB  . UNK B 2 2  ? 177.234 121.401 119.378 1.00 21.86 ?  2  UNK G CB  1 
ATOM 308  N N   . UNK B 2 3  ? 180.192 123.026 119.474 1.00 21.09 ?  3  UNK G N   1 
ATOM 309  C CA  . UNK B 2 3  ? 181.012 123.998 120.180 1.00 25.47 ?  3  UNK G CA  1 
ATOM 310  C C   . UNK B 2 3  ? 180.881 125.356 119.510 1.00 29.06 ?  3  UNK G C   1 
ATOM 311  O O   . UNK B 2 3  ? 180.939 125.457 118.281 1.00 38.46 ?  3  UNK G O   1 
ATOM 312  C CB  . UNK B 2 3  ? 182.483 123.568 120.215 1.00 25.18 ?  3  UNK G CB  1 
ATOM 313  N N   . UNK B 2 4  ? 180.704 126.396 120.320 1.00 28.04 ?  4  UNK G N   1 
ATOM 314  C CA  . UNK B 2 4  ? 180.621 127.770 119.841 1.00 31.96 ?  4  UNK G CA  1 
ATOM 315  C C   . UNK B 2 4  ? 181.777 128.560 120.436 1.00 34.09 ?  4  UNK G C   1 
ATOM 316  O O   . UNK B 2 4  ? 181.924 128.623 121.661 1.00 39.06 ?  4  UNK G O   1 
ATOM 317  C CB  . UNK B 2 4  ? 179.281 128.406 120.214 1.00 32.03 ?  4  UNK G CB  1 
ATOM 318  N N   . UNK B 2 5  ? 182.593 129.159 119.572 1.00 29.75 ?  5  UNK G N   1 
ATOM 319  C CA  . UNK B 2 5  ? 183.770 129.906 119.996 1.00 30.80 ?  5  UNK G CA  1 
ATOM 320  C C   . UNK B 2 5  ? 183.740 131.294 119.377 1.00 29.10 ?  5  UNK G C   1 
ATOM 321  O O   . UNK B 2 5  ? 183.530 131.435 118.169 1.00 33.74 ?  5  UNK G O   1 
ATOM 322  C CB  . UNK B 2 5  ? 185.058 129.177 119.603 1.00 39.20 ?  5  UNK G CB  1 
ATOM 323  N N   . UNK B 2 6  ? 183.949 132.313 120.207 1.00 30.19 ?  6  UNK G N   1 
ATOM 324  C CA  . UNK B 2 6  ? 184.034 133.694 119.756 1.00 38.33 ?  6  UNK G CA  1 
ATOM 325  C C   . UNK B 2 6  ? 185.244 134.345 120.405 1.00 42.09 ?  6  UNK G C   1 
ATOM 326  O O   . UNK B 2 6  ? 185.408 134.274 121.627 1.00 49.64 ?  6  UNK G O   1 
ATOM 327  C CB  . UNK B 2 6  ? 182.759 134.472 120.096 1.00 37.15 ?  6  UNK G CB  1 
ATOM 328  N N   . UNK B 2 7  ? 186.085 134.976 119.591 1.00 39.87 ?  7  UNK G N   1 
ATOM 329  C CA  . UNK B 2 7  ? 187.306 135.604 120.068 1.00 42.13 ?  7  UNK G CA  1 
ATOM 330  C C   . UNK B 2 7  ? 187.384 137.032 119.550 1.00 45.23 ?  7  UNK G C   1 
ATOM 331  O O   . UNK B 2 7  ? 186.773 137.383 118.538 1.00 56.63 ?  7  UNK G O   1 
ATOM 332  C CB  . UNK B 2 7  ? 188.551 134.818 119.633 1.00 38.50 ?  7  UNK G CB  1 
ATOM 333  N N   . UNK B 2 8  ? 188.145 137.856 120.263 1.00 41.67 ?  8  UNK G N   1 
ATOM 334  C CA  . UNK B 2 8  ? 188.326 139.252 119.886 1.00 47.40 ?  8  UNK G CA  1 
ATOM 335  C C   . UNK B 2 8  ? 189.657 139.787 120.404 1.00 48.38 ?  8  UNK G C   1 
ATOM 336  O O   . UNK B 2 8  ? 189.908 140.991 120.370 1.00 49.71 ?  8  UNK G O   1 
ATOM 337  C CB  . UNK B 2 8  ? 187.175 140.097 120.408 1.00 45.22 ?  8  UNK G CB  1 
ATOM 338  N N   . ALA C 1 9  ? 185.110 149.406 122.286 1.00 28.61 ?  1  ALA B N   1 
ATOM 339  C CA  . ALA C 1 9  ? 184.532 150.103 123.427 1.00 25.85 ?  1  ALA B CA  1 
ATOM 340  C C   . ALA C 1 9  ? 183.354 149.325 124.002 1.00 26.65 ?  1  ALA B C   1 
ATOM 341  O O   . ALA C 1 9  ? 183.287 149.086 125.206 1.00 35.46 ?  1  ALA B O   1 
ATOM 342  C CB  . ALA C 1 9  ? 184.099 151.505 123.030 1.00 30.41 ?  1  ALA B CB  1 
ATOM 343  N N   . THR C 1 10 ? 182.424 148.932 123.135 1.00 21.88 ?  2  THR B N   1 
ATOM 344  C CA  . THR C 1 10 ? 181.243 148.185 123.543 1.00 20.68 ?  2  THR B CA  1 
ATOM 345  C C   . THR C 1 10 ? 181.095 146.935 122.688 1.00 16.28 ?  2  THR B C   1 
ATOM 346  O O   . THR C 1 10 ? 181.330 146.968 121.478 1.00 24.08 ?  2  THR B O   1 
ATOM 347  C CB  . THR C 1 10 ? 179.977 149.043 123.447 1.00 23.13 ?  2  THR B CB  1 
ATOM 348  O OG1 . THR C 1 10 ? 178.819 148.217 123.626 1.00 22.10 ?  2  THR B OG1 1 
ATOM 349  C CG2 . THR C 1 10 ? 179.900 149.750 122.107 1.00 25.90 ?  2  THR B CG2 1 
ATOM 350  N N   . LYS C 1 11 ? 180.717 145.832 123.328 1.00 12.40 ?  3  LYS B N   1 
ATOM 351  C CA  . LYS C 1 11 ? 180.503 144.563 122.651 1.00 11.07 ?  3  LYS B CA  1 
ATOM 352  C C   . LYS C 1 11 ? 179.155 143.996 123.067 1.00 8.74  ?  3  LYS B C   1 
ATOM 353  O O   . LYS C 1 11 ? 178.634 144.321 124.138 1.00 13.17 ?  3  LYS B O   1 
ATOM 354  C CB  . LYS C 1 11 ? 181.611 143.535 122.960 1.00 14.24 ?  3  LYS B CB  1 
ATOM 355  C CG  . LYS C 1 11 ? 183.008 143.878 122.437 1.00 15.39 ?  3  LYS B CG  1 
ATOM 356  C CD  . LYS C 1 11 ? 183.707 144.948 123.263 1.00 18.52 ?  3  LYS B CD  1 
ATOM 357  C CE  . LYS C 1 11 ? 185.026 145.360 122.633 1.00 22.30 ?  3  LYS B CE  1 
ATOM 358  N NZ  . LYS C 1 11 ? 185.633 146.524 123.335 1.00 19.90 1  3  LYS B NZ  1 
ATOM 359  N N   . ALA C 1 12 ? 178.591 143.149 122.212 1.00 4.49  ?  4  ALA B N   1 
ATOM 360  C CA  . ALA C 1 12 ? 177.307 142.519 122.493 1.00 4.08  ?  4  ALA B CA  1 
ATOM 361  C C   . ALA C 1 12 ? 177.269 141.160 121.815 1.00 3.13  ?  4  ALA B C   1 
ATOM 362  O O   . ALA C 1 12 ? 177.427 141.072 120.595 1.00 6.26  ?  4  ALA B O   1 
ATOM 363  C CB  . ALA C 1 12 ? 176.148 143.394 122.012 1.00 6.52  ?  4  ALA B CB  1 
ATOM 364  N N   . VAL C 1 13 ? 177.059 140.110 122.603 1.00 1.75  ?  5  VAL B N   1 
ATOM 365  C CA  . VAL C 1 13 ? 176.976 138.745 122.100 1.00 2.31  ?  5  VAL B CA  1 
ATOM 366  C C   . VAL C 1 13 ? 175.689 138.125 122.620 1.00 2.62  ?  5  VAL B C   1 
ATOM 367  O O   . VAL C 1 13 ? 175.398 138.204 123.819 1.00 5.53  ?  5  VAL B O   1 
ATOM 368  C CB  . VAL C 1 13 ? 178.194 137.902 122.523 1.00 2.59  ?  5  VAL B CB  1 
ATOM 369  C CG1 . VAL C 1 13 ? 178.028 136.458 122.073 1.00 2.08  ?  5  VAL B CG1 1 
ATOM 370  C CG2 . VAL C 1 13 ? 179.475 138.498 121.963 1.00 2.27  ?  5  VAL B CG2 1 
ATOM 371  N N   . ALA C 1 14 ? 174.920 137.512 121.725 1.00 2.76  ?  6  ALA B N   1 
ATOM 372  C CA  . ALA C 1 14 ? 173.674 136.848 122.081 1.00 4.23  ?  6  ALA B CA  1 
ATOM 373  C C   . ALA C 1 14 ? 173.704 135.423 121.552 1.00 4.41  ?  6  ALA B C   1 
ATOM 374  O O   . ALA C 1 14 ? 173.925 135.207 120.355 1.00 9.14  ?  6  ALA B O   1 
ATOM 375  C CB  . ALA C 1 14 ? 172.467 137.603 121.523 1.00 5.34  ?  6  ALA B CB  1 
ATOM 376  N N   . VAL C 1 15 ? 173.483 134.457 122.439 1.00 3.00  ?  7  VAL B N   1 
ATOM 377  C CA  . VAL C 1 15 ? 173.484 133.043 122.087 1.00 5.44  ?  7  VAL B CA  1 
ATOM 378  C C   . VAL C 1 15 ? 172.236 132.399 122.673 1.00 6.79  ?  7  VAL B C   1 
ATOM 379  O O   . VAL C 1 15 ? 171.938 132.578 123.858 1.00 12.06 ?  7  VAL B O   1 
ATOM 380  C CB  . VAL C 1 15 ? 174.752 132.329 122.594 1.00 7.38  ?  7  VAL B CB  1 
ATOM 381  C CG1 . VAL C 1 15 ? 174.581 130.819 122.526 1.00 6.30  ?  7  VAL B CG1 1 
ATOM 382  C CG2 . VAL C 1 15 ? 175.964 132.767 121.788 1.00 5.02  ?  7  VAL B CG2 1 
ATOM 383  N N   . LEU C 1 16 ? 171.508 131.655 121.844 1.00 7.33  ?  8  LEU B N   1 
ATOM 384  C CA  . LEU C 1 16 ? 170.341 130.909 122.290 1.00 9.02  ?  8  LEU B CA  1 
ATOM 385  C C   . LEU C 1 16 ? 170.345 129.548 121.613 1.00 13.78 ?  8  LEU B C   1 
ATOM 386  O O   . LEU C 1 16 ? 170.579 129.454 120.405 1.00 25.23 ?  8  LEU B O   1 
ATOM 387  C CB  . LEU C 1 16 ? 169.045 131.665 121.976 1.00 11.16 ?  8  LEU B CB  1 
ATOM 388  C CG  . LEU C 1 16 ? 167.725 130.890 122.032 1.00 14.67 ?  8  LEU B CG  1 
ATOM 389  C CD1 . LEU C 1 16 ? 167.519 130.225 123.377 1.00 20.42 ?  8  LEU B CD1 1 
ATOM 390  C CD2 . LEU C 1 16 ? 166.558 131.805 121.710 1.00 17.98 ?  8  LEU B CD2 1 
ATOM 391  N N   . LYS C 1 17 ? 170.087 128.499 122.392 1.00 11.41 ?  9  LYS B N   1 
ATOM 392  C CA  . LYS C 1 17 ? 170.076 127.136 121.877 1.00 13.56 ?  9  LYS B CA  1 
ATOM 393  C C   . LYS C 1 17 ? 168.741 126.488 122.232 1.00 15.29 ?  9  LYS B C   1 
ATOM 394  O O   . LYS C 1 17 ? 168.694 125.367 122.747 1.00 16.23 ?  9  LYS B O   1 
ATOM 395  C CB  . LYS C 1 17 ? 171.261 126.344 122.443 1.00 13.71 ?  9  LYS B CB  1 
ATOM 396  C CG  . LYS C 1 17 ? 171.509 124.986 121.795 1.00 14.94 ?  9  LYS B CG  1 
ATOM 397  C CD  . LYS C 1 17 ? 172.409 124.122 122.663 1.00 14.57 ?  9  LYS B CD  1 
ATOM 398  C CE  . LYS C 1 17 ? 173.817 124.690 122.735 1.00 16.26 ?  9  LYS B CE  1 
ATOM 399  N NZ  . LYS C 1 17 ? 174.816 123.653 123.110 1.00 15.38 1  9  LYS B NZ  1 
ATOM 400  N N   . GLY C 1 18 ? 167.652 127.197 121.972 1.00 16.28 ?  10 GLY B N   1 
ATOM 401  C CA  . GLY C 1 18 ? 166.333 126.732 122.362 1.00 20.25 ?  10 GLY B CA  1 
ATOM 402  C C   . GLY C 1 18 ? 165.360 126.740 121.206 1.00 26.23 ?  10 GLY B C   1 
ATOM 403  O O   . GLY C 1 18 ? 165.428 127.592 120.319 1.00 26.39 ?  10 GLY B O   1 
ATOM 404  N N   . ASP C 1 19 ? 164.437 125.776 121.232 1.00 32.75 ?  11 ASP B N   1 
ATOM 405  C CA  . ASP C 1 19 ? 163.414 125.655 120.201 1.00 34.06 ?  11 ASP B CA  1 
ATOM 406  C C   . ASP C 1 19 ? 162.426 126.816 120.238 1.00 34.38 ?  11 ASP B C   1 
ATOM 407  O O   . ASP C 1 19 ? 161.726 127.052 119.251 1.00 31.97 ?  11 ASP B O   1 
ATOM 408  C CB  . ASP C 1 19 ? 162.690 124.312 120.377 1.00 37.30 ?  11 ASP B CB  1 
ATOM 409  C CG  . ASP C 1 19 ? 161.938 123.859 119.128 1.00 41.59 ?  11 ASP B CG  1 
ATOM 410  O OD1 . ASP C 1 19 ? 161.341 124.687 118.415 1.00 43.60 -1 11 ASP B OD1 1 
ATOM 411  O OD2 . ASP C 1 19 ? 161.941 122.638 118.863 1.00 45.72 ?  11 ASP B OD2 1 
ATOM 412  N N   . GLY C 1 20 ? 162.363 127.553 121.344 1.00 35.94 ?  12 GLY B N   1 
ATOM 413  C CA  . GLY C 1 20 ? 161.437 128.651 121.480 1.00 34.39 ?  12 GLY B CA  1 
ATOM 414  C C   . GLY C 1 20 ? 161.652 129.759 120.470 1.00 29.47 ?  12 GLY B C   1 
ATOM 415  O O   . GLY C 1 20 ? 162.783 130.124 120.138 1.00 28.48 ?  12 GLY B O   1 
ATOM 416  N N   . PRO C 1 21 ? 160.555 130.310 119.956 1.00 26.81 ?  13 PRO B N   1 
ATOM 417  C CA  . PRO C 1 21 ? 160.662 131.434 119.022 1.00 26.71 ?  13 PRO B CA  1 
ATOM 418  C C   . PRO C 1 21 ? 161.237 132.670 119.695 1.00 25.45 ?  13 PRO B C   1 
ATOM 419  O O   . PRO C 1 21 ? 161.068 132.892 120.895 1.00 33.91 ?  13 PRO B O   1 
ATOM 420  C CB  . PRO C 1 21 ? 159.213 131.669 118.579 1.00 25.06 ?  13 PRO B CB  1 
ATOM 421  C CG  . PRO C 1 21 ? 158.496 130.395 118.899 1.00 25.84 ?  13 PRO B CG  1 
ATOM 422  C CD  . PRO C 1 21 ? 159.164 129.860 120.124 1.00 27.75 ?  13 PRO B CD  1 
ATOM 423  N N   . VAL C 1 22 ? 161.927 133.480 118.898 1.00 20.80 ?  14 VAL B N   1 
ATOM 424  C CA  . VAL C 1 22 ? 162.484 134.747 119.354 1.00 18.20 ?  14 VAL B CA  1 
ATOM 425  C C   . VAL C 1 22 ? 161.537 135.862 118.939 1.00 23.47 ?  14 VAL B C   1 
ATOM 426  O O   . VAL C 1 22 ? 161.149 135.954 117.768 1.00 33.83 ?  14 VAL B O   1 
ATOM 427  C CB  . VAL C 1 22 ? 163.891 134.975 118.779 1.00 17.86 ?  14 VAL B CB  1 
ATOM 428  C CG1 . VAL C 1 22 ? 164.245 136.452 118.812 1.00 15.32 ?  14 VAL B CG1 1 
ATOM 429  C CG2 . VAL C 1 22 ? 164.911 134.166 119.552 1.00 22.05 ?  14 VAL B CG2 1 
ATOM 430  N N   . GLN C 1 23 ? 161.160 136.708 119.896 1.00 22.36 ?  15 GLN B N   1 
ATOM 431  C CA  . GLN C 1 23 ? 160.219 137.797 119.655 1.00 20.30 ?  15 GLN B CA  1 
ATOM 432  C C   . GLN C 1 23 ? 160.793 139.073 120.253 1.00 19.11 ?  15 GLN B C   1 
ATOM 433  O O   . GLN C 1 23 ? 160.947 139.175 121.475 1.00 27.36 ?  15 GLN B O   1 
ATOM 434  C CB  . GLN C 1 23 ? 158.851 137.476 120.255 1.00 18.87 ?  15 GLN B CB  1 
ATOM 435  C CG  . GLN C 1 23 ? 157.698 138.202 119.598 1.00 17.91 ?  15 GLN B CG  1 
ATOM 436  C CD  . GLN C 1 23 ? 156.457 137.342 119.501 1.00 21.22 ?  15 GLN B CD  1 
ATOM 437  O OE1 . GLN C 1 23 ? 155.724 137.176 120.476 1.00 15.30 ?  15 GLN B OE1 1 
ATOM 438  N NE2 . GLN C 1 23 ? 156.214 136.786 118.320 1.00 24.15 ?  15 GLN B NE2 1 
ATOM 439  N N   . GLY C 1 24 ? 161.106 140.044 119.399 1.00 12.80 ?  16 GLY B N   1 
ATOM 440  C CA  . GLY C 1 24 ? 161.646 141.307 119.860 1.00 7.81  ?  16 GLY B CA  1 
ATOM 441  C C   . GLY C 1 24 ? 162.913 141.712 119.137 1.00 4.63  ?  16 GLY B C   1 
ATOM 442  O O   . GLY C 1 24 ? 163.149 141.286 118.004 1.00 5.60  ?  16 GLY B O   1 
ATOM 443  N N   . ILE C 1 25 ? 163.733 142.535 119.776 1.00 3.20  ?  17 ILE B N   1 
ATOM 444  C CA  . ILE C 1 25 ? 164.993 142.980 119.196 1.00 2.97  ?  17 ILE B CA  1 
ATOM 445  C C   . ILE C 1 25 ? 166.143 142.293 119.913 1.00 4.18  ?  17 ILE B C   1 
ATOM 446  O O   . ILE C 1 25 ? 166.075 142.005 121.113 1.00 20.36 ?  17 ILE B O   1 
ATOM 447  C CB  . ILE C 1 25 ? 165.136 144.513 119.266 1.00 2.76  ?  17 ILE B CB  1 
ATOM 448  C CG1 . ILE C 1 25 ? 163.772 145.184 119.128 1.00 3.84  ?  17 ILE B CG1 1 
ATOM 449  C CG2 . ILE C 1 25 ? 166.080 145.009 118.189 1.00 3.86  ?  17 ILE B CG2 1 
ATOM 450  C CD1 . ILE C 1 25 ? 163.808 146.666 119.395 1.00 2.74  ?  17 ILE B CD1 1 
ATOM 451  N N   . ILE C 1 26 ? 167.212 142.024 119.169 1.00 2.67  ?  18 ILE B N   1 
ATOM 452  C CA  . ILE C 1 26 ? 168.417 141.402 119.701 1.00 1.40  ?  18 ILE B CA  1 
ATOM 453  C C   . ILE C 1 26 ? 169.589 142.339 119.446 1.00 1.52  ?  18 ILE B C   1 
ATOM 454  O O   . ILE C 1 26 ? 169.772 142.816 118.321 1.00 2.00  ?  18 ILE B O   1 
ATOM 455  C CB  . ILE C 1 26 ? 168.674 140.023 119.068 1.00 1.45  ?  18 ILE B CB  1 
ATOM 456  C CG1 . ILE C 1 26 ? 167.355 139.283 118.844 1.00 1.29  ?  18 ILE B CG1 1 
ATOM 457  C CG2 . ILE C 1 26 ? 169.600 139.204 119.943 1.00 2.28  ?  18 ILE B CG2 1 
ATOM 458  C CD1 . ILE C 1 26 ? 166.693 138.817 120.110 1.00 1.32  ?  18 ILE B CD1 1 
ATOM 459  N N   . ASN C 1 27 ? 170.376 142.596 120.490 1.00 1.62  ?  19 ASN B N   1 
ATOM 460  C CA  . ASN C 1 27 ? 171.544 143.475 120.406 1.00 2.03  ?  19 ASN B CA  1 
ATOM 461  C C   . ASN C 1 27 ? 171.160 144.870 119.920 1.00 1.29  ?  19 ASN B C   1 
ATOM 462  O O   . ASN C 1 27 ? 171.841 145.467 119.085 1.00 2.24  ?  19 ASN B O   1 
ATOM 463  C CB  . ASN C 1 27 ? 172.631 142.867 119.518 1.00 2.07  ?  19 ASN B CB  1 
ATOM 464  C CG  . ASN C 1 27 ? 172.974 141.445 119.908 1.00 3.34  ?  19 ASN B CG  1 
ATOM 465  O OD1 . ASN C 1 27 ? 173.222 141.152 121.077 1.00 3.83  ?  19 ASN B OD1 1 
ATOM 466  N ND2 . ASN C 1 27 ? 172.988 140.551 118.928 1.00 4.34  ?  19 ASN B ND2 1 
ATOM 467  N N   . PHE C 1 28 ? 170.056 145.389 120.445 1.00 1.33  ?  20 PHE B N   1 
ATOM 468  C CA  . PHE C 1 28 ? 169.627 146.746 120.141 1.00 1.50  ?  20 PHE B CA  1 
ATOM 469  C C   . PHE C 1 28 ? 170.506 147.739 120.892 1.00 2.68  ?  20 PHE B C   1 
ATOM 470  O O   . PHE C 1 28 ? 170.644 147.656 122.116 1.00 9.02  ?  20 PHE B O   1 
ATOM 471  C CB  . PHE C 1 28 ? 168.157 146.921 120.522 1.00 2.39  ?  20 PHE B CB  1 
ATOM 472  C CG  . PHE C 1 28 ? 167.562 148.230 120.096 1.00 1.78  ?  20 PHE B CG  1 
ATOM 473  C CD1 . PHE C 1 28 ? 168.145 148.990 119.100 1.00 2.68  ?  20 PHE B CD1 1 
ATOM 474  C CD2 . PHE C 1 28 ? 166.406 148.694 120.690 1.00 2.10  ?  20 PHE B CD2 1 
ATOM 475  C CE1 . PHE C 1 28 ? 167.593 150.191 118.719 1.00 3.16  ?  20 PHE B CE1 1 
ATOM 476  C CE2 . PHE C 1 28 ? 165.850 149.892 120.311 1.00 2.00  ?  20 PHE B CE2 1 
ATOM 477  C CZ  . PHE C 1 28 ? 166.441 150.640 119.323 1.00 2.66  ?  20 PHE B CZ  1 
ATOM 478  N N   . GLU C 1 29 ? 171.102 148.677 120.160 1.00 1.15  ?  21 GLU B N   1 
ATOM 479  C CA  . GLU C 1 29 ? 172.090 149.601 120.709 1.00 1.57  ?  21 GLU B CA  1 
ATOM 480  C C   . GLU C 1 29 ? 171.748 151.040 120.349 1.00 1.73  ?  21 GLU B C   1 
ATOM 481  O O   . GLU C 1 29 ? 172.588 151.797 119.859 1.00 1.58  ?  21 GLU B O   1 
ATOM 482  C CB  . GLU C 1 29 ? 173.494 149.253 120.223 1.00 1.06  ?  21 GLU B CB  1 
ATOM 483  C CG  . GLU C 1 29 ? 173.782 147.762 120.166 1.00 1.10  ?  21 GLU B CG  1 
ATOM 484  C CD  . GLU C 1 29 ? 175.261 147.453 120.121 1.00 1.23  ?  21 GLU B CD  1 
ATOM 485  O OE1 . GLU C 1 29 ? 176.069 148.404 120.077 1.00 1.37  ?  21 GLU B OE1 1 
ATOM 486  O OE2 . GLU C 1 29 ? 175.616 146.256 120.130 1.00 1.43  -1 21 GLU B OE2 1 
ATOM 487  N N   . GLN C 1 30 ? 170.497 151.435 120.584 1.00 1.74  ?  22 GLN B N   1 
ATOM 488  C CA  . GLN C 1 30 ? 170.093 152.818 120.363 1.00 1.55  ?  22 GLN B CA  1 
ATOM 489  C C   . GLN C 1 30 ? 170.946 153.758 121.205 1.00 2.07  ?  22 GLN B C   1 
ATOM 490  O O   . GLN C 1 30 ? 171.150 153.526 122.398 1.00 7.82  ?  22 GLN B O   1 
ATOM 491  C CB  . GLN C 1 30 ? 168.613 152.994 120.703 1.00 1.81  ?  22 GLN B CB  1 
ATOM 492  C CG  . GLN C 1 30 ? 168.224 154.416 121.050 1.00 2.66  ?  22 GLN B CG  1 
ATOM 493  C CD  . GLN C 1 30 ? 166.723 154.634 121.060 1.00 2.57  ?  22 GLN B CD  1 
ATOM 494  O OE1 . GLN C 1 30 ? 166.052 154.456 120.045 1.00 2.36  ?  22 GLN B OE1 1 
ATOM 495  N NE2 . GLN C 1 30 ? 166.189 155.029 122.209 1.00 2.89  ?  22 GLN B NE2 1 
ATOM 496  N N   . LYS C 1 31 ? 171.451 154.820 120.581 1.00 1.87  ?  23 LYS B N   1 
ATOM 497  C CA  . LYS C 1 31 ? 172.423 155.679 121.244 1.00 1.92  ?  23 LYS B CA  1 
ATOM 498  C C   . LYS C 1 31 ? 172.292 157.111 120.751 1.00 3.06  ?  23 LYS B C   1 
ATOM 499  O O   . LYS C 1 31 ? 172.255 157.353 119.542 1.00 5.25  ?  23 LYS B O   1 
ATOM 500  C CB  . LYS C 1 31 ? 173.847 155.164 121.004 1.00 1.73  ?  23 LYS B CB  1 
ATOM 501  C CG  . LYS C 1 31 ? 174.931 156.217 121.149 1.00 1.66  ?  23 LYS B CG  1 
ATOM 502  C CD  . LYS C 1 31 ? 176.315 155.590 121.242 1.00 2.02  ?  23 LYS B CD  1 
ATOM 503  C CE  . LYS C 1 31 ? 176.406 154.297 120.448 1.00 2.93  ?  23 LYS B CE  1 
ATOM 504  N NZ  . LYS C 1 31 ? 177.695 153.592 120.685 1.00 4.12  1  23 LYS B NZ  1 
ATOM 505  N N   . GLU C 1 32 ? 172.232 158.050 121.699 1.00 4.10  ?  24 GLU B N   1 
ATOM 506  C CA  . GLU C 1 32 ? 172.216 159.485 121.408 1.00 5.39  ?  24 GLU B CA  1 
ATOM 507  C C   . GLU C 1 32 ? 171.097 159.850 120.438 1.00 7.25  ?  24 GLU B C   1 
ATOM 508  O O   . GLU C 1 32 ? 171.278 160.646 119.515 1.00 9.80  ?  24 GLU B O   1 
ATOM 509  C CB  . GLU C 1 32 ? 173.571 159.950 120.873 1.00 3.63  ?  24 GLU B CB  1 
ATOM 510  C CG  . GLU C 1 32 ? 174.720 159.738 121.839 1.00 4.42  ?  24 GLU B CG  1 
ATOM 511  C CD  . GLU C 1 32 ? 176.066 160.071 121.228 1.00 4.91  ?  24 GLU B CD  1 
ATOM 512  O OE1 . GLU C 1 32 ? 176.271 161.242 120.844 1.00 6.01  ?  24 GLU B OE1 1 
ATOM 513  O OE2 . GLU C 1 32 ? 176.918 159.163 121.133 1.00 3.74  -1 24 GLU B OE2 1 
ATOM 514  N N   . SER C 1 33 ? 169.924 159.269 120.655 1.00 6.77  ?  25 SER B N   1 
ATOM 515  C CA  . SER C 1 33 ? 168.784 159.475 119.775 1.00 10.76 ?  25 SER B CA  1 
ATOM 516  C C   . SER C 1 33 ? 167.602 160.016 120.576 1.00 15.28 ?  25 SER B C   1 
ATOM 517  O O   . SER C 1 33 ? 167.722 160.361 121.754 1.00 20.99 ?  25 SER B O   1 
ATOM 518  C CB  . SER C 1 33 ? 168.418 158.175 119.060 1.00 11.58 ?  25 SER B CB  1 
ATOM 519  O OG  . SER C 1 33 ? 167.810 157.272 119.961 1.00 6.84  ?  25 SER B OG  1 
ATOM 520  N N   . ASN C 1 34 ? 166.449 160.098 119.914 1.00 13.65 ?  26 ASN B N   1 
ATOM 521  C CA  . ASN C 1 34 ? 165.211 160.537 120.554 1.00 14.20 ?  26 ASN B CA  1 
ATOM 522  C C   . ASN C 1 34 ? 164.065 159.815 119.852 1.00 14.73 ?  26 ASN B C   1 
ATOM 523  O O   . ASN C 1 34 ? 163.656 160.212 118.758 1.00 20.09 ?  26 ASN B O   1 
ATOM 524  C CB  . ASN C 1 34 ? 165.053 162.049 120.476 1.00 20.75 ?  26 ASN B CB  1 
ATOM 525  C CG  . ASN C 1 34 ? 163.663 162.507 120.862 1.00 23.14 ?  26 ASN B CG  1 
ATOM 526  O OD1 . ASN C 1 34 ? 162.960 163.129 120.067 1.00 26.41 ?  26 ASN B OD1 1 
ATOM 527  N ND2 . ASN C 1 34 ? 163.257 162.200 122.088 1.00 21.92 ?  26 ASN B ND2 1 
ATOM 528  N N   . GLY C 1 35 ? 163.562 158.758 120.480 1.00 9.69  ?  27 GLY B N   1 
ATOM 529  C CA  . GLY C 1 35 ? 162.489 157.985 119.907 1.00 6.74  ?  27 GLY B CA  1 
ATOM 530  C C   . GLY C 1 35 ? 161.908 156.983 120.880 1.00 2.59  ?  27 GLY B C   1 
ATOM 531  O O   . GLY C 1 35 ? 162.628 156.220 121.531 1.00 2.30  ?  27 GLY B O   1 
ATOM 532  N N   . PRO C 1 36 ? 160.586 156.969 120.998 1.00 2.08  ?  28 PRO B N   1 
ATOM 533  C CA  . PRO C 1 36 ? 159.905 155.990 121.867 1.00 2.22  ?  28 PRO B CA  1 
ATOM 534  C C   . PRO C 1 36 ? 159.844 154.599 121.240 1.00 1.46  ?  28 PRO B C   1 
ATOM 535  O O   . PRO C 1 36 ? 158.858 154.181 120.633 1.00 1.56  ?  28 PRO B O   1 
ATOM 536  C CB  . PRO C 1 36 ? 158.515 156.605 122.041 1.00 3.18  ?  28 PRO B CB  1 
ATOM 537  C CG  . PRO C 1 36 ? 158.303 157.411 120.815 1.00 2.60  ?  28 PRO B CG  1 
ATOM 538  C CD  . PRO C 1 36 ? 159.646 157.931 120.397 1.00 3.15  ?  28 PRO B CD  1 
ATOM 539  N N   . VAL C 1 37 ? 160.942 153.855 121.387 1.00 1.09  ?  29 VAL B N   1 
ATOM 540  C CA  . VAL C 1 37 ? 160.990 152.493 120.871 1.00 1.31  ?  29 VAL B CA  1 
ATOM 541  C C   . VAL C 1 37 ? 159.970 151.626 121.594 1.00 1.06  ?  29 VAL B C   1 
ATOM 542  O O   . VAL C 1 37 ? 159.910 151.595 122.828 1.00 2.25  ?  29 VAL B O   1 
ATOM 543  C CB  . VAL C 1 37 ? 162.414 151.928 120.984 1.00 1.17  ?  29 VAL B CB  1 
ATOM 544  C CG1 . VAL C 1 37 ? 162.951 152.099 122.376 1.00 1.83  ?  29 VAL B CG1 1 
ATOM 545  C CG2 . VAL C 1 37 ? 162.415 150.452 120.621 1.00 1.49  ?  29 VAL B CG2 1 
ATOM 546  N N   . LYS C 1 38 ? 159.147 150.928 120.817 1.00 0.86  ?  30 LYS B N   1 
ATOM 547  C CA  . LYS C 1 38 ? 158.092 150.073 121.341 1.00 1.06  ?  30 LYS B CA  1 
ATOM 548  C C   . LYS C 1 38 ? 158.224 148.688 120.728 1.00 1.21  ?  30 LYS B C   1 
ATOM 549  O O   . LYS C 1 38 ? 158.357 148.557 119.508 1.00 3.08  ?  30 LYS B O   1 
ATOM 550  C CB  . LYS C 1 38 ? 156.711 150.663 121.041 1.00 1.14  ?  30 LYS B CB  1 
ATOM 551  C CG  . LYS C 1 38 ? 155.547 149.774 121.441 1.00 1.32  ?  30 LYS B CG  1 
ATOM 552  C CD  . LYS C 1 38 ? 154.220 150.415 121.073 1.00 1.00  ?  30 LYS B CD  1 
ATOM 553  C CE  . LYS C 1 38 ? 153.052 149.506 121.415 1.00 1.14  ?  30 LYS B CE  1 
ATOM 554  N NZ  . LYS C 1 38 ? 151.743 150.138 121.088 1.00 0.73  1  30 LYS B NZ  1 
ATOM 555  N N   . VAL C 1 39 ? 158.190 147.661 121.570 1.00 0.91  ?  31 VAL B N   1 
ATOM 556  C CA  . VAL C 1 39 ? 158.289 146.276 121.130 1.00 1.50  ?  31 VAL B CA  1 
ATOM 557  C C   . VAL C 1 39 ? 157.035 145.547 121.584 1.00 2.30  ?  31 VAL B C   1 
ATOM 558  O O   . VAL C 1 39 ? 156.705 145.551 122.776 1.00 4.40  ?  31 VAL B O   1 
ATOM 559  C CB  . VAL C 1 39 ? 159.549 145.589 121.680 1.00 2.29  ?  31 VAL B CB  1 
ATOM 560  C CG1 . VAL C 1 39 ? 159.639 144.162 121.164 1.00 2.31  ?  31 VAL B CG1 1 
ATOM 561  C CG2 . VAL C 1 39 ? 160.786 146.378 121.302 1.00 1.58  ?  31 VAL B CG2 1 
ATOM 562  N N   . TRP C 1 40 ? 156.343 144.919 120.639 1.00 2.21  ?  32 TRP B N   1 
ATOM 563  C CA  . TRP C 1 40 ? 155.123 144.173 120.915 1.00 2.99  ?  32 TRP B CA  1 
ATOM 564  C C   . TRP C 1 40 ? 155.348 142.721 120.521 1.00 3.21  ?  32 TRP B C   1 
ATOM 565  O O   . TRP C 1 40 ? 155.700 142.434 119.373 1.00 5.23  ?  32 TRP B O   1 
ATOM 566  C CB  . TRP C 1 40 ? 153.936 144.771 120.157 1.00 4.17  ?  32 TRP B CB  1 
ATOM 567  C CG  . TRP C 1 40 ? 152.595 144.275 120.611 1.00 3.61  ?  32 TRP B CG  1 
ATOM 568  C CD1 . TRP C 1 40 ? 152.188 142.977 120.709 1.00 4.41  ?  32 TRP B CD1 1 
ATOM 569  C CD2 . TRP C 1 40 ? 151.483 145.075 121.025 1.00 3.72  ?  32 TRP B CD2 1 
ATOM 570  N NE1 . TRP C 1 40 ? 150.892 142.919 121.158 1.00 3.94  ?  32 TRP B NE1 1 
ATOM 571  C CE2 . TRP C 1 40 ? 150.436 144.194 121.361 1.00 4.98  ?  32 TRP B CE2 1 
ATOM 572  C CE3 . TRP C 1 40 ? 151.271 146.452 121.146 1.00 3.71  ?  32 TRP B CE3 1 
ATOM 573  C CZ2 . TRP C 1 40 ? 149.196 144.644 121.808 1.00 6.31  ?  32 TRP B CZ2 1 
ATOM 574  C CZ3 . TRP C 1 40 ? 150.039 146.897 121.590 1.00 4.28  ?  32 TRP B CZ3 1 
ATOM 575  C CH2 . TRP C 1 40 ? 149.017 145.996 121.916 1.00 5.60  ?  32 TRP B CH2 1 
ATOM 576  N N   . GLY C 1 41 ? 155.146 141.814 121.470 1.00 3.12  ?  33 GLY B N   1 
ATOM 577  C CA  . GLY C 1 41 ? 155.323 140.402 121.204 1.00 7.91  ?  33 GLY B CA  1 
ATOM 578  C C   . GLY C 1 41 ? 154.150 139.561 121.658 1.00 9.98  ?  33 GLY B C   1 
ATOM 579  O O   . GLY C 1 41 ? 153.831 139.518 122.849 1.00 15.16 ?  33 GLY B O   1 
ATOM 580  N N   . SER C 1 42 ? 153.499 138.884 120.716 1.00 7.03  ?  34 SER B N   1 
ATOM 581  C CA  . SER C 1 42 ? 152.343 138.049 121.009 1.00 9.59  ?  34 SER B CA  1 
ATOM 582  C C   . SER C 1 42 ? 152.543 136.681 120.377 1.00 12.86 ?  34 SER B C   1 
ATOM 583  O O   . SER C 1 42 ? 153.045 136.582 119.253 1.00 22.86 ?  34 SER B O   1 
ATOM 584  C CB  . SER C 1 42 ? 151.051 138.690 120.492 1.00 10.24 ?  34 SER B CB  1 
ATOM 585  O OG  . SER C 1 42 ? 149.935 137.853 120.738 1.00 10.90 ?  34 SER B OG  1 
ATOM 586  N N   . ILE C 1 43 ? 152.158 135.633 121.101 1.00 8.73  ?  35 ILE B N   1 
ATOM 587  C CA  . ILE C 1 43 ? 152.216 134.264 120.601 1.00 12.07 ?  35 ILE B CA  1 
ATOM 588  C C   . ILE C 1 43 ? 151.074 133.479 121.231 1.00 13.05 ?  35 ILE B C   1 
ATOM 589  O O   . ILE C 1 43 ? 151.012 133.342 122.458 1.00 18.89 ?  35 ILE B O   1 
ATOM 590  C CB  . ILE C 1 43 ? 153.571 133.594 120.895 1.00 13.89 ?  35 ILE B CB  1 
ATOM 591  C CG1 . ILE C 1 43 ? 153.471 132.075 120.734 1.00 16.89 ?  35 ILE B CG1 1 
ATOM 592  C CG2 . ILE C 1 43 ? 154.089 133.990 122.267 1.00 19.63 ?  35 ILE B CG2 1 
ATOM 593  C CD1 . ILE C 1 43 ? 154.811 131.375 120.740 1.00 19.55 ?  35 ILE B CD1 1 
ATOM 594  N N   . LYS C 1 44 ? 150.165 132.973 120.399 1.00 13.71 ?  36 LYS B N   1 
ATOM 595  C CA  . LYS C 1 44 ? 149.009 132.218 120.872 1.00 19.51 ?  36 LYS B CA  1 
ATOM 596  C C   . LYS C 1 44 ? 149.008 130.832 120.239 1.00 24.14 ?  36 LYS B C   1 
ATOM 597  O O   . LYS C 1 44 ? 148.372 130.614 119.203 1.00 35.30 ?  36 LYS B O   1 
ATOM 598  C CB  . LYS C 1 44 ? 147.708 132.963 120.569 1.00 19.26 ?  36 LYS B CB  1 
ATOM 599  C CG  . LYS C 1 44 ? 147.666 134.378 121.127 1.00 15.07 ?  36 LYS B CG  1 
ATOM 600  C CD  . LYS C 1 44 ? 146.535 135.190 120.519 1.00 15.29 ?  36 LYS B CD  1 
ATOM 601  C CE  . LYS C 1 44 ? 145.187 134.770 121.081 1.00 19.88 ?  36 LYS B CE  1 
ATOM 602  N NZ  . LYS C 1 44 ? 144.172 135.849 120.934 1.00 20.42 1  36 LYS B NZ  1 
ATOM 603  N N   . GLY C 1 45 ? 149.714 129.897 120.870 1.00 22.39 ?  37 GLY B N   1 
ATOM 604  C CA  . GLY C 1 45 ? 149.753 128.524 120.413 1.00 34.53 ?  37 GLY B CA  1 
ATOM 605  C C   . GLY C 1 45 ? 150.489 127.651 121.408 1.00 50.93 ?  37 GLY B C   1 
ATOM 606  O O   . GLY C 1 45 ? 150.785 128.079 122.525 1.00 60.96 ?  37 GLY B O   1 
ATOM 607  N N   . LEU C 1 46 ? 150.806 126.425 121.000 1.00 55.90 ?  38 LEU B N   1 
ATOM 608  C CA  . LEU C 1 46 ? 151.452 125.479 121.900 1.00 62.17 ?  38 LEU B CA  1 
ATOM 609  C C   . LEU C 1 46 ? 152.729 124.931 121.281 1.00 63.02 ?  38 LEU B C   1 
ATOM 610  O O   . LEU C 1 46 ? 152.814 124.718 120.070 1.00 68.61 ?  38 LEU B O   1 
ATOM 611  C CB  . LEU C 1 46 ? 150.519 124.323 122.292 1.00 66.59 ?  38 LEU B CB  1 
ATOM 612  C CG  . LEU C 1 46 ? 150.072 123.232 121.318 1.00 64.08 ?  38 LEU B CG  1 
ATOM 613  C CD1 . LEU C 1 46 ? 149.315 122.158 122.063 1.00 67.23 ?  38 LEU B CD1 1 
ATOM 614  C CD2 . LEU C 1 46 ? 149.134 123.831 120.301 1.00 56.33 ?  38 LEU B CD2 1 
ATOM 615  N N   . THR C 1 47 ? 153.718 124.700 122.140 1.00 61.74 ?  39 THR B N   1 
ATOM 616  C CA  . THR C 1 47 ? 155.007 124.154 121.746 1.00 64.45 ?  39 THR B CA  1 
ATOM 617  C C   . THR C 1 47 ? 155.248 122.852 122.500 1.00 65.26 ?  39 THR B C   1 
ATOM 618  O O   . THR C 1 47 ? 154.648 122.609 123.552 1.00 68.25 ?  39 THR B O   1 
ATOM 619  C CB  . THR C 1 47 ? 156.136 125.152 122.022 1.00 67.76 ?  39 THR B CB  1 
ATOM 620  O OG1 . THR C 1 47 ? 156.304 125.308 123.436 1.00 67.28 ?  39 THR B OG1 1 
ATOM 621  C CG2 . THR C 1 47 ? 155.803 126.506 121.420 1.00 66.15 ?  39 THR B CG2 1 
ATOM 622  N N   . GLU C 1 48 ? 156.121 122.011 121.954 1.00 66.18 ?  40 GLU B N   1 
ATOM 623  C CA  . GLU C 1 48 ? 156.427 120.717 122.541 1.00 61.50 ?  40 GLU B CA  1 
ATOM 624  C C   . GLU C 1 48 ? 157.936 120.540 122.622 1.00 59.06 ?  40 GLU B C   1 
ATOM 625  O O   . GLU C 1 48 ? 158.704 121.294 122.019 1.00 60.79 ?  40 GLU B O   1 
ATOM 626  C CB  . GLU C 1 48 ? 155.802 119.576 121.730 1.00 62.11 ?  40 GLU B CB  1 
ATOM 627  C CG  . GLU C 1 48 ? 154.372 119.238 122.120 1.00 60.56 ?  40 GLU B CG  1 
ATOM 628  C CD  . GLU C 1 48 ? 153.384 120.305 121.693 1.00 65.93 ?  40 GLU B CD  1 
ATOM 629  O OE1 . GLU C 1 48 ? 153.390 120.682 120.505 1.00 71.63 ?  40 GLU B OE1 1 
ATOM 630  O OE2 . GLU C 1 48 ? 152.597 120.766 122.545 1.00 64.65 -1 40 GLU B OE2 1 
ATOM 631  N N   . GLY C 1 49 ? 158.351 119.532 123.382 1.00 60.96 ?  41 GLY B N   1 
ATOM 632  C CA  . GLY C 1 49 ? 159.761 119.229 123.544 1.00 63.08 ?  41 GLY B CA  1 
ATOM 633  C C   . GLY C 1 49 ? 160.153 117.891 122.949 1.00 60.55 ?  41 GLY B C   1 
ATOM 634  O O   . GLY C 1 49 ? 159.339 116.969 122.882 1.00 62.50 ?  41 GLY B O   1 
ATOM 635  N N   . UNK D 2 1  ? 178.942 116.573 123.920 1.00 26.05 ?  1  UNK H N   1 
ATOM 636  C CA  . UNK D 2 1  ? 179.926 117.416 124.589 1.00 26.04 ?  1  UNK H CA  1 
ATOM 637  C C   . UNK D 2 1  ? 179.779 118.871 124.160 1.00 26.58 ?  1  UNK H C   1 
ATOM 638  O O   . UNK D 2 1  ? 180.721 119.473 123.644 1.00 29.40 ?  1  UNK H O   1 
ATOM 639  C CB  . UNK D 2 1  ? 181.334 116.918 124.302 1.00 22.41 ?  1  UNK H CB  1 
ATOM 640  N N   . UNK D 2 2  ? 178.590 119.429 124.375 1.00 22.86 ?  2  UNK H N   1 
ATOM 641  C CA  . UNK D 2 2  ? 178.328 120.814 124.006 1.00 22.32 ?  2  UNK H CA  1 
ATOM 642  C C   . UNK D 2 2  ? 179.147 121.758 124.875 1.00 21.72 ?  2  UNK H C   1 
ATOM 643  O O   . UNK D 2 2  ? 179.184 121.614 126.101 1.00 26.76 ?  2  UNK H O   1 
ATOM 644  C CB  . UNK D 2 2  ? 176.838 121.119 124.140 1.00 21.86 ?  2  UNK H CB  1 
ATOM 645  N N   . UNK D 2 3  ? 179.806 122.725 124.241 1.00 21.09 ?  3  UNK H N   1 
ATOM 646  C CA  . UNK D 2 3  ? 180.631 123.692 124.948 1.00 25.47 ?  3  UNK H CA  1 
ATOM 647  C C   . UNK D 2 3  ? 180.509 125.051 124.279 1.00 29.06 ?  3  UNK H C   1 
ATOM 648  O O   . UNK D 2 3  ? 180.569 125.153 123.051 1.00 38.46 ?  3  UNK H O   1 
ATOM 649  C CB  . UNK D 2 3  ? 182.099 123.252 124.984 1.00 25.18 ?  3  UNK H CB  1 
ATOM 650  N N   . UNK D 2 4  ? 180.338 126.091 125.090 1.00 28.04 ?  4  UNK H N   1 
ATOM 651  C CA  . UNK D 2 4  ? 180.264 127.466 124.612 1.00 31.96 ?  4  UNK H CA  1 
ATOM 652  C C   . UNK D 2 4  ? 181.425 128.248 125.209 1.00 34.09 ?  4  UNK H C   1 
ATOM 653  O O   . UNK D 2 4  ? 181.570 128.310 126.434 1.00 39.06 ?  4  UNK H O   1 
ATOM 654  C CB  . UNK D 2 4  ? 178.928 128.110 124.985 1.00 32.03 ?  4  UNK H CB  1 
ATOM 655  N N   . UNK D 2 5  ? 182.245 128.843 124.346 1.00 29.75 ?  5  UNK H N   1 
ATOM 656  C CA  . UNK D 2 5  ? 183.426 129.582 124.772 1.00 30.80 ?  5  UNK H CA  1 
ATOM 657  C C   . UNK D 2 5  ? 183.405 130.971 124.155 1.00 29.10 ?  5  UNK H C   1 
ATOM 658  O O   . UNK D 2 5  ? 183.197 131.114 122.946 1.00 33.74 ?  5  UNK H O   1 
ATOM 659  C CB  . UNK D 2 5  ? 184.710 128.846 124.380 1.00 39.20 ?  5  UNK H CB  1 
ATOM 660  N N   . UNK D 2 6  ? 183.620 131.988 124.986 1.00 30.19 ?  6  UNK H N   1 
ATOM 661  C CA  . UNK D 2 6  ? 183.714 133.369 124.536 1.00 38.33 ?  6  UNK H CA  1 
ATOM 662  C C   . UNK D 2 6  ? 184.927 134.011 125.187 1.00 42.09 ?  6  UNK H C   1 
ATOM 663  O O   . UNK D 2 6  ? 185.089 133.939 126.409 1.00 49.64 ?  6  UNK H O   1 
ATOM 664  C CB  . UNK D 2 6  ? 182.443 134.155 124.875 1.00 37.15 ?  6  UNK H CB  1 
ATOM 665  N N   . UNK D 2 7  ? 185.773 134.638 124.375 1.00 39.87 ?  7  UNK H N   1 
ATOM 666  C CA  . UNK D 2 7  ? 186.998 135.258 124.853 1.00 42.13 ?  7  UNK H CA  1 
ATOM 667  C C   . UNK D 2 7  ? 187.085 136.686 124.337 1.00 45.23 ?  7  UNK H C   1 
ATOM 668  O O   . UNK D 2 7  ? 186.477 137.042 123.324 1.00 56.63 ?  7  UNK H O   1 
ATOM 669  C CB  . UNK D 2 7  ? 188.238 134.465 124.419 1.00 38.50 ?  7  UNK H CB  1 
ATOM 670  N N   . UNK D 2 8  ? 187.851 137.504 125.051 1.00 41.67 ?  8  UNK H N   1 
ATOM 671  C CA  . UNK D 2 8  ? 188.041 138.900 124.676 1.00 47.40 ?  8  UNK H CA  1 
ATOM 672  C C   . UNK D 2 8  ? 189.374 139.426 125.195 1.00 48.38 ?  8  UNK H C   1 
ATOM 673  O O   . UNK D 2 8  ? 189.633 140.629 125.163 1.00 49.71 ?  8  UNK H O   1 
ATOM 674  C CB  . UNK D 2 8  ? 186.894 139.751 125.197 1.00 45.22 ?  8  UNK H CB  1 
ATOM 675  N N   . ALA E 1 9  ? 184.982 149.011 127.131 1.00 28.61 ?  1  ALA C N   1 
ATOM 676  C CA  . ALA E 1 9  ? 184.416 149.721 128.271 1.00 25.85 ?  1  ALA C CA  1 
ATOM 677  C C   . ALA E 1 9  ? 183.218 148.971 128.840 1.00 26.65 ?  1  ALA C C   1 
ATOM 678  O O   . ALA E 1 9  ? 183.141 148.733 130.045 1.00 35.46 ?  1  ALA C O   1 
ATOM 679  C CB  . ALA E 1 9  ? 184.019 151.134 127.874 1.00 30.41 ?  1  ALA C CB  1 
ATOM 680  N N   . THR E 1 10 ? 182.282 148.602 127.970 1.00 21.88 ?  2  THR C N   1 
ATOM 681  C CA  . THR E 1 10 ? 181.082 147.883 128.373 1.00 20.68 ?  2  THR C CA  1 
ATOM 682  C C   . THR E 1 10 ? 180.906 146.639 127.517 1.00 16.28 ?  2  THR C C   1 
ATOM 683  O O   . THR E 1 10 ? 181.147 146.667 126.307 1.00 24.08 ?  2  THR C O   1 
ATOM 684  C CB  . THR E 1 10 ? 179.837 148.773 128.273 1.00 23.13 ?  2  THR C CB  1 
ATOM 685  O OG1 . THR E 1 10 ? 178.659 147.974 128.448 1.00 22.10 ?  2  THR C OG1 1 
ATOM 686  C CG2 . THR E 1 10 ? 179.782 149.482 126.934 1.00 25.90 ?  2  THR C CG2 1 
ATOM 687  N N   . LYS E 1 11 ? 180.499 145.544 128.154 1.00 12.40 ?  3  LYS C N   1 
ATOM 688  C CA  . LYS E 1 11 ? 180.257 144.281 127.474 1.00 11.07 ?  3  LYS C CA  1 
ATOM 689  C C   . LYS E 1 11 ? 178.894 143.747 127.885 1.00 8.74  ?  3  LYS C C   1 
ATOM 690  O O   . LYS E 1 11 ? 178.378 144.084 128.954 1.00 13.17 ?  3  LYS C O   1 
ATOM 691  C CB  . LYS E 1 11 ? 181.338 143.226 127.786 1.00 14.24 ?  3  LYS C CB  1 
ATOM 692  C CG  . LYS E 1 11 ? 182.745 143.536 127.268 1.00 15.39 ?  3  LYS C CG  1 
ATOM 693  C CD  . LYS E 1 11 ? 183.467 144.587 128.098 1.00 18.52 ?  3  LYS C CD  1 
ATOM 694  C CE  . LYS E 1 11 ? 184.798 144.968 127.474 1.00 22.30 ?  3  LYS C CE  1 
ATOM 695  N NZ  . LYS E 1 11 ? 185.431 146.116 128.178 1.00 19.90 1  3  LYS C NZ  1 
ATOM 696  N N   . ALA E 1 12 ? 178.313 142.915 127.027 1.00 4.49  ?  4  ALA C N   1 
ATOM 697  C CA  . ALA E 1 12 ? 177.012 142.316 127.302 1.00 4.08  ?  4  ALA C CA  1 
ATOM 698  C C   . ALA E 1 12 ? 176.944 140.960 126.624 1.00 3.13  ?  4  ALA C C   1 
ATOM 699  O O   . ALA E 1 12 ? 177.104 140.868 125.403 1.00 6.26  ?  4  ALA C O   1 
ATOM 700  C CB  . ALA E 1 12 ? 175.877 143.220 126.819 1.00 6.52  ?  4  ALA C CB  1 
ATOM 701  N N   . VAL E 1 13 ? 176.705 139.914 127.409 1.00 1.75  ?  5  VAL C N   1 
ATOM 702  C CA  . VAL E 1 13 ? 176.591 138.552 126.904 1.00 2.31  ?  5  VAL C CA  1 
ATOM 703  C C   . VAL E 1 13 ? 175.287 137.962 127.419 1.00 2.62  ?  5  VAL C C   1 
ATOM 704  O O   . VAL E 1 13 ? 174.994 138.048 128.617 1.00 5.53  ?  5  VAL C O   1 
ATOM 705  C CB  . VAL E 1 13 ? 177.787 137.679 127.331 1.00 2.59  ?  5  VAL C CB  1 
ATOM 706  C CG1 . VAL E 1 13 ? 177.587 136.240 126.878 1.00 2.08  ?  5  VAL C CG1 1 
ATOM 707  C CG2 . VAL E 1 13 ? 179.084 138.244 126.776 1.00 2.27  ?  5  VAL C CG2 1 
ATOM 708  N N   . ALA E 1 14 ? 174.507 137.370 126.521 1.00 2.76  ?  6  ALA C N   1 
ATOM 709  C CA  . ALA E 1 14 ? 173.244 136.735 126.872 1.00 4.23  ?  6  ALA C CA  1 
ATOM 710  C C   . ALA E 1 14 ? 173.242 135.311 126.341 1.00 4.41  ?  6  ALA C C   1 
ATOM 711  O O   . ALA E 1 14 ? 173.461 135.091 125.145 1.00 9.14  ?  6  ALA C O   1 
ATOM 712  C CB  . ALA E 1 14 ? 172.058 137.520 126.310 1.00 5.34  ?  6  ALA C CB  1 
ATOM 713  N N   . VAL E 1 15 ? 172.993 134.349 127.227 1.00 3.00  ?  7  VAL C N   1 
ATOM 714  C CA  . VAL E 1 15 ? 172.961 132.936 126.873 1.00 5.44  ?  7  VAL C CA  1 
ATOM 715  C C   . VAL E 1 15 ? 171.696 132.322 127.453 1.00 6.79  ?  7  VAL C C   1 
ATOM 716  O O   . VAL E 1 15 ? 171.399 132.508 128.638 1.00 12.06 ?  7  VAL C O   1 
ATOM 717  C CB  . VAL E 1 15 ? 174.210 132.191 127.383 1.00 7.38  ?  7  VAL C CB  1 
ATOM 718  C CG1 . VAL E 1 15 ? 174.003 130.686 127.313 1.00 6.30  ?  7  VAL C CG1 1 
ATOM 719  C CG2 . VAL E 1 15 ? 175.435 132.601 126.582 1.00 5.02  ?  7  VAL C CG2 1 
ATOM 720  N N   . LEU E 1 16 ? 170.953 131.597 126.621 1.00 7.33  ?  8  LEU C N   1 
ATOM 721  C CA  . LEU E 1 16 ? 169.767 130.880 127.062 1.00 9.02  ?  8  LEU C CA  1 
ATOM 722  C C   . LEU E 1 16 ? 169.740 129.520 126.383 1.00 13.78 ?  8  LEU C C   1 
ATOM 723  O O   . LEU E 1 16 ? 169.976 129.421 125.176 1.00 25.23 ?  8  LEU C O   1 
ATOM 724  C CB  . LEU E 1 16 ? 168.490 131.668 126.745 1.00 11.16 ?  8  LEU C CB  1 
ATOM 725  C CG  . LEU E 1 16 ? 167.152 130.924 126.795 1.00 14.67 ?  8  LEU C CG  1 
ATOM 726  C CD1 . LEU E 1 16 ? 166.925 130.263 128.139 1.00 20.42 ?  8  LEU C CD1 1 
ATOM 727  C CD2 . LEU E 1 16 ? 166.009 131.868 126.470 1.00 17.98 ?  8  LEU C CD2 1 
ATOM 728  N N   . LYS E 1 17 ? 169.454 128.477 127.161 1.00 11.41 ?  9  LYS C N   1 
ATOM 729  C CA  . LYS E 1 17 ? 169.412 127.115 126.644 1.00 13.56 ?  9  LYS C CA  1 
ATOM 730  C C   . LYS E 1 17 ? 168.060 126.499 126.994 1.00 15.29 ?  9  LYS C C   1 
ATOM 731  O O   . LYS E 1 17 ? 167.984 125.379 127.507 1.00 16.23 ?  9  LYS C O   1 
ATOM 732  C CB  . LYS E 1 17 ? 170.575 126.293 127.213 1.00 13.71 ?  9  LYS C CB  1 
ATOM 733  C CG  . LYS E 1 17 ? 170.792 124.930 126.564 1.00 14.94 ?  9  LYS C CG  1 
ATOM 734  C CD  . LYS E 1 17 ? 171.668 124.044 127.435 1.00 14.57 ?  9  LYS C CD  1 
ATOM 735  C CE  . LYS E 1 17 ? 173.089 124.577 127.512 1.00 16.26 ?  9  LYS C CE  1 
ATOM 736  N NZ  . LYS E 1 17 ? 174.061 123.516 127.890 1.00 15.38 1  9  LYS C NZ  1 
ATOM 737  N N   . GLY E 1 18 ? 166.989 127.234 126.731 1.00 16.28 ?  10 GLY C N   1 
ATOM 738  C CA  . GLY E 1 18 ? 165.658 126.801 127.115 1.00 20.25 ?  10 GLY C CA  1 
ATOM 739  C C   . GLY E 1 18 ? 164.690 126.834 125.956 1.00 26.23 ?  10 GLY C C   1 
ATOM 740  O O   . GLY E 1 18 ? 164.781 127.685 125.071 1.00 26.39 ?  10 GLY C O   1 
ATOM 741  N N   . ASP E 1 19 ? 163.743 125.893 125.978 1.00 32.75 ?  11 ASP C N   1 
ATOM 742  C CA  . ASP E 1 19 ? 162.721 125.798 124.943 1.00 34.06 ?  11 ASP C CA  1 
ATOM 743  C C   . ASP E 1 19 ? 161.762 126.983 124.978 1.00 34.38 ?  11 ASP C C   1 
ATOM 744  O O   . ASP E 1 19 ? 161.071 127.237 123.989 1.00 31.97 ?  11 ASP C O   1 
ATOM 745  C CB  . ASP E 1 19 ? 161.964 124.473 125.114 1.00 37.30 ?  11 ASP C CB  1 
ATOM 746  C CG  . ASP E 1 19 ? 161.206 124.040 123.862 1.00 41.59 ?  11 ASP C CG  1 
ATOM 747  O OD1 . ASP E 1 19 ? 160.632 124.883 123.148 1.00 43.60 -1 11 ASP C OD1 1 
ATOM 748  O OD2 . ASP E 1 19 ? 161.180 122.820 123.596 1.00 45.72 ?  11 ASP C OD2 1 
ATOM 749  N N   . GLY E 1 20 ? 161.713 127.720 126.084 1.00 35.94 ?  12 GLY C N   1 
ATOM 750  C CA  . GLY E 1 20 ? 160.813 128.840 126.218 1.00 34.39 ?  12 GLY C CA  1 
ATOM 751  C C   . GLY E 1 20 ? 161.058 129.943 125.211 1.00 29.47 ?  12 GLY C C   1 
ATOM 752  O O   . GLY E 1 20 ? 162.200 130.281 124.883 1.00 28.48 ?  12 GLY C O   1 
ATOM 753  N N   . PRO E 1 21 ? 159.977 130.521 124.693 1.00 26.81 ?  13 PRO C N   1 
ATOM 754  C CA  . PRO E 1 21 ? 160.115 131.644 123.761 1.00 26.71 ?  13 PRO C CA  1 
ATOM 755  C C   . PRO E 1 21 ? 160.718 132.865 124.437 1.00 25.45 ?  13 PRO C C   1 
ATOM 756  O O   . PRO E 1 21 ? 160.549 133.089 125.638 1.00 33.91 ?  13 PRO C O   1 
ATOM 757  C CB  . PRO E 1 21 ? 158.673 131.915 123.313 1.00 25.06 ?  13 PRO C CB  1 
ATOM 758  C CG  . PRO E 1 21 ? 157.925 130.658 123.630 1.00 25.84 ?  13 PRO C CG  1 
ATOM 759  C CD  . PRO E 1 21 ? 158.575 130.106 124.856 1.00 27.75 ?  13 PRO C CD  1 
ATOM 760  N N   . VAL E 1 22 ? 161.430 133.659 123.644 1.00 20.80 ?  14 VAL C N   1 
ATOM 761  C CA  . VAL E 1 22 ? 162.016 134.911 124.104 1.00 18.20 ?  14 VAL C CA  1 
ATOM 762  C C   . VAL E 1 22 ? 161.098 136.049 123.686 1.00 23.47 ?  14 VAL C C   1 
ATOM 763  O O   . VAL E 1 22 ? 160.717 136.152 122.514 1.00 33.83 ?  14 VAL C O   1 
ATOM 764  C CB  . VAL E 1 22 ? 163.430 135.105 123.534 1.00 17.86 ?  14 VAL C CB  1 
ATOM 765  C CG1 . VAL E 1 22 ? 163.820 136.573 123.569 1.00 15.32 ?  14 VAL C CG1 1 
ATOM 766  C CG2 . VAL E 1 22 ? 164.428 134.271 124.309 1.00 22.05 ?  14 VAL C CG2 1 
ATOM 767  N N   . GLN E 1 23 ? 160.739 136.903 124.642 1.00 22.36 ?  15 GLN C N   1 
ATOM 768  C CA  . GLN E 1 23 ? 159.825 138.014 124.400 1.00 20.30 ?  15 GLN C CA  1 
ATOM 769  C C   . GLN E 1 23 ? 160.428 139.276 125.002 1.00 19.11 ?  15 GLN C C   1 
ATOM 770  O O   . GLN E 1 23 ? 160.580 139.372 126.224 1.00 27.36 ?  15 GLN C O   1 
ATOM 771  C CB  . GLN E 1 23 ? 158.447 137.727 124.995 1.00 18.87 ?  15 GLN C CB  1 
ATOM 772  C CG  . GLN E 1 23 ? 157.315 138.481 124.334 1.00 17.91 ?  15 GLN C CG  1 
ATOM 773  C CD  . GLN E 1 23 ? 156.053 137.652 124.232 1.00 21.22 ?  15 GLN C CD  1 
ATOM 774  O OE1 . GLN E 1 23 ? 155.313 137.503 125.205 1.00 15.30 ?  15 GLN C OE1 1 
ATOM 775  N NE2 . GLN E 1 23 ? 155.802 137.103 123.050 1.00 24.15 ?  15 GLN C NE2 1 
ATOM 776  N N   . GLY E 1 24 ? 160.767 140.239 124.149 1.00 12.80 ?  16 GLY C N   1 
ATOM 777  C CA  . GLY E 1 24 ? 161.336 141.489 124.613 1.00 7.81  ?  16 GLY C CA  1 
ATOM 778  C C   . GLY E 1 24 ? 162.615 141.864 123.895 1.00 4.63  ?  16 GLY C C   1 
ATOM 779  O O   . GLY E 1 24 ? 162.845 141.433 122.763 1.00 5.60  ?  16 GLY C O   1 
ATOM 780  N N   . ILE E 1 25 ? 163.453 142.665 124.539 1.00 3.20  ?  17 ILE C N   1 
ATOM 781  C CA  . ILE E 1 25 ? 164.725 143.080 123.963 1.00 2.97  ?  17 ILE C CA  1 
ATOM 782  C C   . ILE E 1 25 ? 165.856 142.365 124.684 1.00 4.18  ?  17 ILE C C   1 
ATOM 783  O O   . ILE E 1 25 ? 165.777 142.077 125.883 1.00 20.36 ?  17 ILE C O   1 
ATOM 784  C CB  . ILE E 1 25 ? 164.905 144.609 124.036 1.00 2.76  ?  17 ILE C CB  1 
ATOM 785  C CG1 . ILE E 1 25 ? 163.558 145.313 123.894 1.00 3.84  ?  17 ILE C CG1 1 
ATOM 786  C CG2 . ILE E 1 25 ? 165.865 145.084 122.963 1.00 3.86  ?  17 ILE C CG2 1 
ATOM 787  C CD1 . ILE E 1 25 ? 163.630 146.794 124.163 1.00 2.74  ?  17 ILE C CD1 1 
ATOM 788  N N   . ILE E 1 26 ? 166.921 142.071 123.943 1.00 2.67  ?  18 ILE C N   1 
ATOM 789  C CA  . ILE E 1 26 ? 168.108 141.419 124.479 1.00 1.40  ?  18 ILE C CA  1 
ATOM 790  C C   . ILE E 1 26 ? 169.303 142.327 124.229 1.00 1.52  ?  18 ILE C C   1 
ATOM 791  O O   . ILE E 1 26 ? 169.502 142.801 123.105 1.00 2.00  ?  18 ILE C O   1 
ATOM 792  C CB  . ILE E 1 26 ? 168.334 140.035 123.844 1.00 1.45  ?  18 ILE C CB  1 
ATOM 793  C CG1 . ILE E 1 26 ? 166.998 139.327 123.615 1.00 1.29  ?  18 ILE C CG1 1 
ATOM 794  C CG2 . ILE E 1 26 ? 169.236 139.193 124.722 1.00 2.28  ?  18 ILE C CG2 1 
ATOM 795  C CD1 . ILE E 1 26 ? 166.321 138.876 124.878 1.00 1.32  ?  18 ILE C CD1 1 
ATOM 796  N N   . ASN E 1 27 ? 170.093 142.564 125.276 1.00 1.62  ?  19 ASN C N   1 
ATOM 797  C CA  . ASN E 1 27 ? 171.282 143.414 125.197 1.00 2.03  ?  19 ASN C CA  1 
ATOM 798  C C   . ASN E 1 27 ? 170.934 144.819 124.711 1.00 1.29  ?  19 ASN C C   1 
ATOM 799  O O   . ASN E 1 27 ? 171.632 145.400 123.880 1.00 2.24  ?  19 ASN C O   1 
ATOM 800  C CB  . ASN E 1 27 ? 172.357 142.782 124.312 1.00 2.07  ?  19 ASN C CB  1 
ATOM 801  C CG  . ASN E 1 27 ? 172.664 141.351 124.702 1.00 3.34  ?  19 ASN C CG  1 
ATOM 802  O OD1 . ASN E 1 27 ? 172.901 141.051 125.871 1.00 3.83  ?  19 ASN C OD1 1 
ATOM 803  N ND2 . ASN E 1 27 ? 172.660 140.458 123.721 1.00 4.34  ?  19 ASN C ND2 1 
ATOM 804  N N   . PHE E 1 28 ? 169.841 145.364 125.233 1.00 1.33  ?  20 PHE C N   1 
ATOM 805  C CA  . PHE E 1 28 ? 169.446 146.732 124.928 1.00 1.50  ?  20 PHE C CA  1 
ATOM 806  C C   . PHE E 1 28 ? 170.347 147.702 125.684 1.00 2.68  ?  20 PHE C C   1 
ATOM 807  O O   . PHE E 1 28 ? 170.479 147.614 126.908 1.00 9.02  ?  20 PHE C O   1 
ATOM 808  C CB  . PHE E 1 28 ? 167.980 146.942 125.304 1.00 2.39  ?  20 PHE C CB  1 
ATOM 809  C CG  . PHE E 1 28 ? 167.418 148.265 124.878 1.00 1.78  ?  20 PHE C CG  1 
ATOM 810  C CD1 . PHE E 1 28 ? 168.023 149.012 123.885 1.00 2.68  ?  20 PHE C CD1 1 
ATOM 811  C CD2 . PHE E 1 28 ? 166.271 148.757 125.469 1.00 2.10  ?  20 PHE C CD2 1 
ATOM 812  C CE1 . PHE E 1 28 ? 167.502 150.227 123.504 1.00 3.16  ?  20 PHE C CE1 1 
ATOM 813  C CE2 . PHE E 1 28 ? 165.746 149.968 125.089 1.00 2.00  ?  20 PHE C CE2 1 
ATOM 814  C CZ  . PHE E 1 28 ? 166.359 150.703 124.104 1.00 2.66  ?  20 PHE C CZ  1 
ATOM 815  N N   . GLU E 1 29 ? 170.967 148.626 124.955 1.00 1.15  ?  21 GLU C N   1 
ATOM 816  C CA  . GLU E 1 29 ? 171.976 149.525 125.509 1.00 1.57  ?  21 GLU C CA  1 
ATOM 817  C C   . GLU E 1 29 ? 171.670 150.972 125.149 1.00 1.73  ?  21 GLU C C   1 
ATOM 818  O O   . GLU E 1 29 ? 172.530 151.709 124.663 1.00 1.58  ?  21 GLU C O   1 
ATOM 819  C CB  . GLU E 1 29 ? 173.373 149.143 125.028 1.00 1.06  ?  21 GLU C CB  1 
ATOM 820  C CG  . GLU E 1 29 ? 173.624 147.646 124.969 1.00 1.10  ?  21 GLU C CG  1 
ATOM 821  C CD  . GLU E 1 29 ? 175.096 147.301 124.930 1.00 1.23  ?  21 GLU C CD  1 
ATOM 822  O OE1 . GLU E 1 29 ? 175.927 148.232 124.889 1.00 1.37  ?  21 GLU C OE1 1 
ATOM 823  O OE2 . GLU E 1 29 ? 175.422 146.096 124.938 1.00 1.43  -1 21 GLU C OE2 1 
ATOM 824  N N   . GLN E 1 30 ? 170.428 151.397 125.380 1.00 1.74  ?  22 GLN C N   1 
ATOM 825  C CA  . GLN E 1 30 ? 170.059 152.790 125.159 1.00 1.55  ?  22 GLN C CA  1 
ATOM 826  C C   . GLN E 1 30 ? 170.932 153.708 126.005 1.00 2.07  ?  22 GLN C C   1 
ATOM 827  O O   . GLN E 1 30 ? 171.126 153.470 127.199 1.00 7.82  ?  22 GLN C O   1 
ATOM 828  C CB  . GLN E 1 30 ? 168.582 153.001 125.494 1.00 1.81  ?  22 GLN C CB  1 
ATOM 829  C CG  . GLN E 1 30 ? 168.227 154.433 125.842 1.00 2.66  ?  22 GLN C CG  1 
ATOM 830  C CD  . GLN E 1 30 ? 166.731 154.687 125.847 1.00 2.57  ?  22 GLN C CD  1 
ATOM 831  O OE1 . GLN E 1 30 ? 166.060 154.527 124.830 1.00 2.36  ?  22 GLN C OE1 1 
ATOM 832  N NE2 . GLN E 1 30 ? 166.204 155.093 126.995 1.00 2.89  ?  22 GLN C NE2 1 
ATOM 833  N N   . LYS E 1 31 ? 171.465 154.759 125.385 1.00 1.87  ?  23 LYS C N   1 
ATOM 834  C CA  . LYS E 1 31 ? 172.455 155.593 126.052 1.00 1.92  ?  23 LYS C CA  1 
ATOM 835  C C   . LYS E 1 31 ? 172.361 157.028 125.560 1.00 3.06  ?  23 LYS C C   1 
ATOM 836  O O   . LYS E 1 31 ? 172.334 157.272 124.351 1.00 5.25  ?  23 LYS C O   1 
ATOM 837  C CB  . LYS E 1 31 ? 173.867 155.043 125.816 1.00 1.73  ?  23 LYS C CB  1 
ATOM 838  C CG  . LYS E 1 31 ? 174.976 156.069 125.966 1.00 1.66  ?  23 LYS C CG  1 
ATOM 839  C CD  . LYS E 1 31 ? 176.343 155.409 126.064 1.00 2.02  ?  23 LYS C CD  1 
ATOM 840  C CE  . LYS E 1 31 ? 176.406 154.115 125.268 1.00 2.93  ?  23 LYS C CE  1 
ATOM 841  N NZ  . LYS E 1 31 ? 177.676 153.378 125.508 1.00 4.12  1  23 LYS C NZ  1 
ATOM 842  N N   . GLU E 1 32 ? 172.320 157.967 126.508 1.00 4.10  ?  24 GLU C N   1 
ATOM 843  C CA  . GLU E 1 32 ? 172.340 159.402 126.219 1.00 5.39  ?  24 GLU C CA  1 
ATOM 844  C C   . GLU E 1 32 ? 171.233 159.795 125.246 1.00 7.25  ?  24 GLU C C   1 
ATOM 845  O O   . GLU E 1 32 ? 171.437 160.588 124.325 1.00 9.80  ?  24 GLU C O   1 
ATOM 846  C CB  . GLU E 1 32 ? 173.708 159.835 125.690 1.00 3.63  ?  24 GLU C CB  1 
ATOM 847  C CG  . GLU E 1 32 ? 174.848 159.593 126.659 1.00 4.42  ?  24 GLU C CG  1 
ATOM 848  C CD  . GLU E 1 32 ? 176.203 159.895 126.054 1.00 4.91  ?  24 GLU C CD  1 
ATOM 849  O OE1 . GLU E 1 32 ? 176.438 161.061 125.672 1.00 6.01  ?  24 GLU C OE1 1 
ATOM 850  O OE2 . GLU E 1 32 ? 177.034 158.967 125.960 1.00 3.74  -1 24 GLU C OE2 1 
ATOM 851  N N   . SER E 1 33 ? 170.046 159.243 125.459 1.00 6.77  ?  25 SER C N   1 
ATOM 852  C CA  . SER E 1 33 ? 168.915 159.477 124.575 1.00 10.76 ?  25 SER C CA  1 
ATOM 853  C C   . SER E 1 33 ? 167.743 160.047 125.372 1.00 15.28 ?  25 SER C C   1 
ATOM 854  O O   . SER E 1 33 ? 167.868 160.387 126.551 1.00 20.99 ?  25 SER C O   1 
ATOM 855  C CB  . SER E 1 33 ? 168.519 158.188 123.856 1.00 11.58 ?  25 SER C CB  1 
ATOM 856  O OG  . SER E 1 33 ? 167.887 157.299 124.755 1.00 6.84  ?  25 SER C OG  1 
ATOM 857  N N   . ASN E 1 34 ? 166.595 160.157 124.706 1.00 13.65 ?  26 ASN C N   1 
ATOM 858  C CA  . ASN E 1 34 ? 165.366 160.626 125.342 1.00 14.20 ?  26 ASN C CA  1 
ATOM 859  C C   . ASN E 1 34 ? 164.205 159.933 124.636 1.00 14.73 ?  26 ASN C C   1 
ATOM 860  O O   . ASN E 1 34 ? 163.810 160.340 123.540 1.00 20.09 ?  26 ASN C O   1 
ATOM 861  C CB  . ASN E 1 34 ? 165.245 162.141 125.266 1.00 20.75 ?  26 ASN C CB  1 
ATOM 862  C CG  . ASN E 1 34 ? 163.865 162.632 125.647 1.00 23.14 ?  26 ASN C CG  1 
ATOM 863  O OD1 . ASN E 1 34 ? 163.180 163.272 124.850 1.00 26.41 ?  26 ASN C OD1 1 
ATOM 864  N ND2 . ASN E 1 34 ? 163.448 162.334 126.871 1.00 21.92 ?  26 ASN C ND2 1 
ATOM 865  N N   . GLY E 1 35 ? 163.674 158.887 125.261 1.00 9.69  ?  27 GLY C N   1 
ATOM 866  C CA  . GLY E 1 35 ? 162.585 158.141 124.683 1.00 6.74  ?  27 GLY C CA  1 
ATOM 867  C C   . GLY E 1 35 ? 161.977 157.152 125.653 1.00 2.59  ?  27 GLY C C   1 
ATOM 868  O O   . GLY E 1 35 ? 162.675 156.372 126.305 1.00 2.30  ?  27 GLY C O   1 
ATOM 869  N N   . PRO E 1 36 ? 160.654 157.171 125.766 1.00 2.08  ?  28 PRO C N   1 
ATOM 870  C CA  . PRO E 1 36 ? 159.946 156.207 126.632 1.00 2.22  ?  28 PRO C CA  1 
ATOM 871  C C   . PRO E 1 36 ? 159.853 154.819 126.003 1.00 1.46  ?  28 PRO C C   1 
ATOM 872  O O   . PRO E 1 36 ? 158.860 154.426 125.392 1.00 1.56  ?  28 PRO C O   1 
ATOM 873  C CB  . PRO E 1 36 ? 158.571 156.856 126.802 1.00 3.18  ?  28 PRO C CB  1 
ATOM 874  C CG  . PRO E 1 36 ? 158.382 157.668 125.575 1.00 2.60  ?  28 PRO C CG  1 
ATOM 875  C CD  . PRO E 1 36 ? 159.740 158.156 125.163 1.00 3.15  ?  28 PRO C CD  1 
ATOM 876  N N   . VAL E 1 37 ? 160.932 154.049 126.152 1.00 1.09  ?  29 VAL C N   1 
ATOM 877  C CA  . VAL E 1 37 ? 160.949 152.687 125.636 1.00 1.31  ?  29 VAL C CA  1 
ATOM 878  C C   . VAL E 1 37 ? 159.905 151.844 126.353 1.00 1.06  ?  29 VAL C C   1 
ATOM 879  O O   . VAL E 1 37 ? 159.840 151.812 127.588 1.00 2.25  ?  29 VAL C O   1 
ATOM 880  C CB  . VAL E 1 37 ? 162.358 152.087 125.752 1.00 1.17  ?  29 VAL C CB  1 
ATOM 881  C CG1 . VAL E 1 37 ? 162.894 152.243 127.146 1.00 1.83  ?  29 VAL C CG1 1 
ATOM 882  C CG2 . VAL E 1 37 ? 162.325 150.612 125.388 1.00 1.49  ?  29 VAL C CG2 1 
ATOM 883  N N   . LYS E 1 38 ? 159.068 151.167 125.573 1.00 0.86  ?  30 LYS C N   1 
ATOM 884  C CA  . LYS E 1 38 ? 157.992 150.337 126.093 1.00 1.06  ?  30 LYS C CA  1 
ATOM 885  C C   . LYS E 1 38 ? 158.092 148.950 125.478 1.00 1.21  ?  30 LYS C C   1 
ATOM 886  O O   . LYS E 1 38 ? 158.226 148.817 124.258 1.00 3.08  ?  30 LYS C O   1 
ATOM 887  C CB  . LYS E 1 38 ? 156.627 150.961 125.789 1.00 1.14  ?  30 LYS C CB  1 
ATOM 888  C CG  . LYS E 1 38 ? 155.440 150.100 126.183 1.00 1.32  ?  30 LYS C CG  1 
ATOM 889  C CD  . LYS E 1 38 ? 154.130 150.773 125.812 1.00 1.00  ?  30 LYS C CD  1 
ATOM 890  C CE  . LYS E 1 38 ? 152.939 149.893 126.149 1.00 1.14  ?  30 LYS C CE  1 
ATOM 891  N NZ  . LYS E 1 38 ? 151.646 150.556 125.818 1.00 0.73  1  30 LYS C NZ  1 
ATOM 892  N N   . VAL E 1 39 ? 158.030 147.923 126.319 1.00 0.91  ?  31 VAL C N   1 
ATOM 893  C CA  . VAL E 1 39 ? 158.096 146.537 125.878 1.00 1.50  ?  31 VAL C CA  1 
ATOM 894  C C   . VAL E 1 39 ? 156.824 145.838 126.326 1.00 2.30  ?  31 VAL C C   1 
ATOM 895  O O   . VAL E 1 39 ? 156.490 145.849 127.517 1.00 4.40  ?  31 VAL C O   1 
ATOM 896  C CB  . VAL E 1 39 ? 159.337 145.818 126.431 1.00 2.29  ?  31 VAL C CB  1 
ATOM 897  C CG1 . VAL E 1 39 ? 159.394 144.390 125.914 1.00 2.31  ?  31 VAL C CG1 1 
ATOM 898  C CG2 . VAL E 1 39 ? 160.595 146.577 126.059 1.00 1.58  ?  31 VAL C CG2 1 
ATOM 899  N N   . TRP E 1 40 ? 156.120 145.228 125.378 1.00 2.21  ?  32 TRP C N   1 
ATOM 900  C CA  . TRP E 1 40 ? 154.882 144.511 125.650 1.00 2.99  ?  32 TRP C CA  1 
ATOM 901  C C   . TRP E 1 40 ? 155.072 143.055 125.255 1.00 3.21  ?  32 TRP C C   1 
ATOM 902  O O   . TRP E 1 40 ? 155.421 142.760 124.107 1.00 5.23  ?  32 TRP C O   1 
ATOM 903  C CB  . TRP E 1 40 ? 153.712 145.139 124.888 1.00 4.17  ?  32 TRP C CB  1 
ATOM 904  C CG  . TRP E 1 40 ? 152.358 144.675 125.337 1.00 3.61  ?  32 TRP C CG  1 
ATOM 905  C CD1 . TRP E 1 40 ? 151.919 143.387 125.431 1.00 4.41  ?  32 TRP C CD1 1 
ATOM 906  C CD2 . TRP E 1 40 ? 151.264 145.502 125.748 1.00 3.72  ?  32 TRP C CD2 1 
ATOM 907  N NE1 . TRP E 1 40 ? 150.620 143.360 125.876 1.00 3.94  ?  32 TRP C NE1 1 
ATOM 908  C CE2 . TRP E 1 40 ? 150.195 144.646 126.078 1.00 4.98  ?  32 TRP C CE2 1 
ATOM 909  C CE3 . TRP E 1 40 ? 151.085 146.883 125.869 1.00 3.71  ?  32 TRP C CE3 1 
ATOM 910  C CZ2 . TRP E 1 40 ? 148.964 145.126 126.522 1.00 6.31  ?  32 TRP C CZ2 1 
ATOM 911  C CZ3 . TRP E 1 40 ? 149.863 147.358 126.310 1.00 4.28  ?  32 TRP C CZ3 1 
ATOM 912  C CH2 . TRP E 1 40 ? 148.818 146.481 126.631 1.00 5.60  ?  32 TRP C CH2 1 
ATOM 913  N N   . GLY E 1 41 ? 154.845 142.152 126.202 1.00 3.12  ?  33 GLY C N   1 
ATOM 914  C CA  . GLY E 1 41 ? 154.988 140.736 125.934 1.00 7.91  ?  33 GLY C CA  1 
ATOM 915  C C   . GLY E 1 41 ? 153.793 139.923 126.383 1.00 9.98  ?  33 GLY C C   1 
ATOM 916  O O   . GLY E 1 41 ? 153.469 139.887 127.574 1.00 15.16 ?  33 GLY C O   1 
ATOM 917  N N   . SER E 1 42 ? 153.129 139.264 125.438 1.00 7.03  ?  34 SER C N   1 
ATOM 918  C CA  . SER E 1 42 ? 151.953 138.457 125.726 1.00 9.59  ?  34 SER C CA  1 
ATOM 919  C C   . SER E 1 42 ? 152.121 137.086 125.093 1.00 12.86 ?  34 SER C C   1 
ATOM 920  O O   . SER E 1 42 ? 152.625 136.975 123.972 1.00 22.86 ?  34 SER C O   1 
ATOM 921  C CB  . SER E 1 42 ? 150.678 139.129 125.206 1.00 10.24 ?  34 SER C CB  1 
ATOM 922  O OG  . SER E 1 42 ? 149.542 138.320 125.447 1.00 10.90 ?  34 SER C OG  1 
ATOM 923  N N   . ILE E 1 43 ? 151.708 136.046 125.815 1.00 8.73  ?  35 ILE C N   1 
ATOM 924  C CA  . ILE E 1 43 ? 151.735 134.677 125.314 1.00 12.07 ?  35 ILE C CA  1 
ATOM 925  C C   . ILE E 1 43 ? 150.572 133.919 125.939 1.00 13.05 ?  35 ILE C C   1 
ATOM 926  O O   . ILE E 1 43 ? 150.503 133.782 127.166 1.00 18.89 ?  35 ILE C O   1 
ATOM 927  C CB  . ILE E 1 43 ? 153.072 133.973 125.612 1.00 13.89 ?  35 ILE C CB  1 
ATOM 928  C CG1 . ILE E 1 43 ? 152.936 132.458 125.449 1.00 16.89 ?  35 ILE C CG1 1 
ATOM 929  C CG2 . ILE E 1 43 ? 153.595 134.355 126.986 1.00 19.63 ?  35 ILE C CG2 1 
ATOM 930  C CD1 . ILE E 1 43 ? 154.258 131.725 125.458 1.00 19.55 ?  35 ILE C CD1 1 
ATOM 931  N N   . LYS E 1 44 ? 149.654 133.436 125.103 1.00 13.71 ?  36 LYS C N   1 
ATOM 932  C CA  . LYS E 1 44 ? 148.478 132.709 125.572 1.00 19.51 ?  36 LYS C CA  1 
ATOM 933  C C   . LYS E 1 44 ? 148.446 131.324 124.936 1.00 24.14 ?  36 LYS C C   1 
ATOM 934  O O   . LYS E 1 44 ? 147.808 131.123 123.898 1.00 35.30 ?  36 LYS C O   1 
ATOM 935  C CB  . LYS E 1 44 ? 147.196 133.486 125.264 1.00 19.26 ?  36 LYS C CB  1 
ATOM 936  C CG  . LYS E 1 44 ? 147.187 134.900 125.824 1.00 15.07 ?  36 LYS C CG  1 
ATOM 937  C CD  . LYS E 1 44 ? 146.079 135.740 125.213 1.00 15.29 ?  36 LYS C CD  1 
ATOM 938  C CE  . LYS E 1 44 ? 144.719 135.353 125.769 1.00 19.88 ?  36 LYS C CE  1 
ATOM 939  N NZ  . LYS E 1 44 ? 143.730 136.456 125.621 1.00 20.42 1  36 LYS C NZ  1 
ATOM 940  N N   . GLY E 1 45 ? 149.127 130.371 125.569 1.00 22.39 ?  37 GLY C N   1 
ATOM 941  C CA  . GLY E 1 45 ? 149.133 128.998 125.111 1.00 34.53 ?  37 GLY C CA  1 
ATOM 942  C C   . GLY E 1 45 ? 149.845 128.107 126.107 1.00 50.93 ?  37 GLY C C   1 
ATOM 943  O O   . GLY E 1 45 ? 150.147 128.526 127.226 1.00 60.96 ?  37 GLY C O   1 
ATOM 944  N N   . LEU E 1 46 ? 150.134 126.874 125.699 1.00 55.90 ?  38 LEU C N   1 
ATOM 945  C CA  . LEU E 1 46 ? 150.752 125.911 126.600 1.00 62.17 ?  38 LEU C CA  1 
ATOM 946  C C   . LEU E 1 46 ? 152.018 125.333 125.985 1.00 63.02 ?  38 LEU C C   1 
ATOM 947  O O   . LEU E 1 46 ? 152.102 125.120 124.774 1.00 68.61 ?  38 LEU C O   1 
ATOM 948  C CB  . LEU E 1 46 ? 149.790 124.778 126.987 1.00 66.59 ?  38 LEU C CB  1 
ATOM 949  C CG  . LEU E 1 46 ? 149.321 123.699 126.011 1.00 64.08 ?  38 LEU C CG  1 
ATOM 950  C CD1 . LEU E 1 46 ? 148.535 122.644 126.752 1.00 67.23 ?  38 LEU C CD1 1 
ATOM 951  C CD2 . LEU E 1 46 ? 148.401 124.322 124.991 1.00 56.33 ?  38 LEU C CD2 1 
ATOM 952  N N   . THR E 1 47 ? 152.999 125.077 126.847 1.00 61.74 ?  39 THR C N   1 
ATOM 953  C CA  . THR E 1 47 ? 154.275 124.500 126.457 1.00 64.45 ?  39 THR C CA  1 
ATOM 954  C C   . THR E 1 47 ? 154.481 123.192 127.210 1.00 65.26 ?  39 THR C C   1 
ATOM 955  O O   . THR E 1 47 ? 153.872 122.963 128.260 1.00 68.25 ?  39 THR C O   1 
ATOM 956  C CB  . THR E 1 47 ? 155.427 125.470 126.738 1.00 67.76 ?  39 THR C CB  1 
ATOM 957  O OG1 . THR E 1 47 ? 155.593 125.621 128.152 1.00 67.28 ?  39 THR C OG1 1 
ATOM 958  C CG2 . THR E 1 47 ? 155.129 126.833 126.136 1.00 66.15 ?  39 THR C CG2 1 
ATOM 959  N N   . GLU E 1 48 ? 155.336 122.331 126.666 1.00 66.18 ?  40 GLU C N   1 
ATOM 960  C CA  . GLU E 1 48 ? 155.608 121.029 127.253 1.00 61.50 ?  40 GLU C CA  1 
ATOM 961  C C   . GLU E 1 48 ? 157.112 120.815 127.339 1.00 59.06 ?  40 GLU C C   1 
ATOM 962  O O   . GLU E 1 48 ? 157.900 121.551 126.740 1.00 60.79 ?  40 GLU C O   1 
ATOM 963  C CB  . GLU E 1 48 ? 154.958 119.904 126.439 1.00 62.11 ?  40 GLU C CB  1 
ATOM 964  C CG  . GLU E 1 48 ? 153.519 119.600 126.823 1.00 60.56 ?  40 GLU C CG  1 
ATOM 965  C CD  . GLU E 1 48 ? 152.558 120.692 126.394 1.00 65.93 ?  40 GLU C CD  1 
ATOM 966  O OE1 . GLU E 1 48 ? 152.578 121.071 125.206 1.00 71.63 ?  40 GLU C OE1 1 
ATOM 967  O OE2 . GLU E 1 48 ? 151.781 121.172 127.243 1.00 64.65 -1 40 GLU C OE2 1 
ATOM 968  N N   . GLY E 1 49 ? 157.500 119.797 128.099 1.00 60.96 ?  41 GLY C N   1 
ATOM 969  C CA  . GLY E 1 49 ? 158.901 119.459 128.265 1.00 63.08 ?  41 GLY C CA  1 
ATOM 970  C C   . GLY E 1 49 ? 159.262 118.112 127.671 1.00 60.55 ?  41 GLY C C   1 
ATOM 971  O O   . GLY E 1 49 ? 158.427 117.211 127.599 1.00 62.50 ?  41 GLY C O   1 
ATOM 972  N N   . UNK F 2 1  ? 178.011 116.337 128.706 1.00 26.05 ?  1  UNK I N   1 
ATOM 973  C CA  . UNK F 2 1  ? 179.012 117.155 129.379 1.00 26.04 ?  1  UNK I CA  1 
ATOM 974  C C   . UNK F 2 1  ? 178.902 118.613 128.951 1.00 26.58 ?  1  UNK I C   1 
ATOM 975  O O   . UNK F 2 1  ? 179.860 119.193 128.440 1.00 29.40 ?  1  UNK I O   1 
ATOM 976  C CB  . UNK F 2 1  ? 180.409 116.623 129.097 1.00 22.41 ?  1  UNK I CB  1 
ATOM 977  N N   . UNK F 2 2  ? 177.727 119.200 129.163 1.00 22.86 ?  2  UNK I N   1 
ATOM 978  C CA  . UNK F 2 2  ? 177.500 120.591 128.795 1.00 22.32 ?  2  UNK I CA  1 
ATOM 979  C C   . UNK F 2 2  ? 178.338 121.514 129.668 1.00 21.72 ?  2  UNK I C   1 
ATOM 980  O O   . UNK F 2 2  ? 178.368 121.368 130.893 1.00 26.76 ?  2  UNK I O   1 
ATOM 981  C CB  . UNK F 2 2  ? 176.017 120.932 128.924 1.00 21.86 ?  2  UNK I CB  1 
ATOM 982  N N   . UNK F 2 3  ? 179.023 122.465 129.037 1.00 21.09 ?  3  UNK I N   1 
ATOM 983  C CA  . UNK F 2 3  ? 179.869 123.411 129.748 1.00 25.47 ?  3  UNK I CA  1 
ATOM 984  C C   . UNK F 2 3  ? 179.782 124.774 129.080 1.00 29.06 ?  3  UNK I C   1 
ATOM 985  O O   . UNK F 2 3  ? 179.849 124.875 127.852 1.00 38.46 ?  3  UNK I O   1 
ATOM 986  C CB  . UNK F 2 3  ? 181.326 122.936 129.789 1.00 25.18 ?  3  UNK I CB  1 
ATOM 987  N N   . UNK F 2 4  ? 179.634 125.817 129.892 1.00 28.04 ?  4  UNK I N   1 
ATOM 988  C CA  . UNK F 2 4  ? 179.595 127.194 129.415 1.00 31.96 ?  4  UNK I CA  1 
ATOM 989  C C   . UNK F 2 4  ? 180.772 127.947 130.017 1.00 34.09 ?  4  UNK I C   1 
ATOM 990  O O   . UNK F 2 4  ? 180.915 128.003 131.243 1.00 39.06 ?  4  UNK I O   1 
ATOM 991  C CB  . UNK F 2 4  ? 178.273 127.869 129.784 1.00 32.03 ?  4  UNK I CB  1 
ATOM 992  N N   . UNK F 2 5  ? 181.610 128.522 129.158 1.00 29.75 ?  5  UNK I N   1 
ATOM 993  C CA  . UNK F 2 5  ? 182.806 129.232 129.588 1.00 30.80 ?  5  UNK I CA  1 
ATOM 994  C C   . UNK F 2 5  ? 182.822 130.621 128.973 1.00 29.10 ?  5  UNK I C   1 
ATOM 995  O O   . UNK F 2 5  ? 182.622 130.771 127.764 1.00 33.74 ?  5  UNK I O   1 
ATOM 996  C CB  . UNK F 2 5  ? 184.074 128.465 129.200 1.00 39.20 ?  5  UNK I CB  1 
ATOM 997  N N   . UNK F 2 6  ? 183.058 131.632 129.806 1.00 30.19 ?  6  UNK I N   1 
ATOM 998  C CA  . UNK F 2 6  ? 183.187 133.011 129.358 1.00 38.33 ?  6  UNK I CA  1 
ATOM 999  C C   . UNK F 2 6  ? 184.414 133.623 130.014 1.00 42.09 ?  6  UNK I C   1 
ATOM 1000 O O   . UNK F 2 6  ? 184.570 133.545 131.237 1.00 49.64 ?  6  UNK I O   1 
ATOM 1001 C CB  . UNK F 2 6  ? 181.935 133.827 129.693 1.00 37.15 ?  6  UNK I CB  1 
ATOM 1002 N N   . UNK F 2 7  ? 185.278 134.230 129.205 1.00 39.87 ?  7  UNK I N   1 
ATOM 1003 C CA  . UNK F 2 7  ? 186.515 134.819 129.688 1.00 42.13 ?  7  UNK I CA  1 
ATOM 1004 C C   . UNK F 2 7  ? 186.639 136.245 129.174 1.00 45.23 ?  7  UNK I C   1 
ATOM 1005 O O   . UNK F 2 7  ? 186.043 136.617 128.160 1.00 56.63 ?  7  UNK I O   1 
ATOM 1006 C CB  . UNK F 2 7  ? 187.738 133.996 129.258 1.00 38.50 ?  7  UNK I CB  1 
ATOM 1007 N N   . UNK F 2 8  ? 187.422 137.044 129.892 1.00 41.67 ?  8  UNK I N   1 
ATOM 1008 C CA  . UNK F 2 8  ? 187.647 138.434 129.519 1.00 47.40 ?  8  UNK I CA  1 
ATOM 1009 C C   . UNK F 2 8  ? 188.992 138.927 130.044 1.00 48.38 ?  8  UNK I C   1 
ATOM 1010 O O   . UNK F 2 8  ? 189.280 140.124 130.014 1.00 49.71 ?  8  UNK I O   1 
ATOM 1011 C CB  . UNK F 2 8  ? 186.520 139.313 130.038 1.00 45.22 ?  8  UNK I CB  1 
ATOM 1012 N N   . ALA G 1 9  ? 138.766 174.506 119.894 1.00 28.61 ?  1  ALA D N   1 
ATOM 1013 C CA  . ALA G 1 9  ? 139.342 173.806 121.035 1.00 25.85 ?  1  ALA D CA  1 
ATOM 1014 C C   . ALA G 1 9  ? 140.523 174.579 121.609 1.00 26.65 ?  1  ALA D C   1 
ATOM 1015 O O   . ALA G 1 9  ? 140.591 174.818 122.814 1.00 35.46 ?  1  ALA D O   1 
ATOM 1016 C CB  . ALA G 1 9  ? 139.769 172.402 120.638 1.00 30.41 ?  1  ALA D CB  1 
ATOM 1017 N N   . THR G 1 10 ? 141.455 174.969 120.743 1.00 21.88 ?  2  THR D N   1 
ATOM 1018 C CA  . THR G 1 10 ? 142.638 175.711 121.151 1.00 20.68 ?  2  THR D CA  1 
ATOM 1019 C C   . THR G 1 10 ? 142.791 176.960 120.296 1.00 16.28 ?  2  THR D C   1 
ATOM 1020 O O   . THR G 1 10 ? 142.556 176.928 119.085 1.00 24.08 ?  2  THR D O   1 
ATOM 1021 C CB  . THR G 1 10 ? 143.901 174.847 121.054 1.00 23.13 ?  2  THR D CB  1 
ATOM 1022 O OG1 . THR G 1 10 ? 145.062 175.669 121.233 1.00 22.10 ?  2  THR D OG1 1 
ATOM 1023 C CG2 . THR G 1 10 ? 143.975 174.140 119.714 1.00 25.90 ?  2  THR D CG2 1 
ATOM 1024 N N   . LYS G 1 11 ? 143.174 178.062 120.936 1.00 12.40 ?  3  LYS D N   1 
ATOM 1025 C CA  . LYS G 1 11 ? 143.393 179.330 120.258 1.00 11.07 ?  3  LYS D CA  1 
ATOM 1026 C C   . LYS G 1 11 ? 144.744 179.891 120.674 1.00 8.74  ?  3  LYS D C   1 
ATOM 1027 O O   . LYS G 1 11 ? 145.263 179.564 121.745 1.00 13.17 ?  3  LYS D O   1 
ATOM 1028 C CB  . LYS G 1 11 ? 142.289 180.362 120.567 1.00 14.24 ?  3  LYS D CB  1 
ATOM 1029 C CG  . LYS G 1 11 ? 140.891 180.025 120.045 1.00 15.39 ?  3  LYS D CG  1 
ATOM 1030 C CD  . LYS G 1 11 ? 140.188 178.958 120.871 1.00 18.52 ?  3  LYS D CD  1 
ATOM 1031 C CE  . LYS G 1 11 ? 138.867 178.551 120.241 1.00 22.30 ?  3  LYS D CE  1 
ATOM 1032 N NZ  . LYS G 1 11 ? 138.255 177.390 120.943 1.00 19.90 1  3  LYS D NZ  1 
ATOM 1033 N N   . ALA G 1 12 ? 145.311 180.736 119.819 1.00 4.49  ?  4  ALA D N   1 
ATOM 1034 C CA  . ALA G 1 12 ? 146.598 181.360 120.100 1.00 4.08  ?  4  ALA D CA  1 
ATOM 1035 C C   . ALA G 1 12 ? 146.641 182.719 119.422 1.00 3.13  ?  4  ALA D C   1 
ATOM 1036 O O   . ALA G 1 12 ? 146.483 182.808 118.202 1.00 6.26  ?  4  ALA D O   1 
ATOM 1037 C CB  . ALA G 1 12 ? 147.753 180.481 119.619 1.00 6.52  ?  4  ALA D CB  1 
ATOM 1038 N N   . VAL G 1 13 ? 146.856 183.769 120.210 1.00 1.75  ?  5  VAL D N   1 
ATOM 1039 C CA  . VAL G 1 13 ? 146.944 185.133 119.707 1.00 2.31  ?  5  VAL D CA  1 
ATOM 1040 C C   . VAL G 1 13 ? 148.234 185.748 120.227 1.00 2.62  ?  5  VAL D C   1 
ATOM 1041 O O   . VAL G 1 13 ? 148.525 185.667 121.425 1.00 5.53  ?  5  VAL D O   1 
ATOM 1042 C CB  . VAL G 1 13 ? 145.729 185.982 120.131 1.00 2.59  ?  5  VAL D CB  1 
ATOM 1043 C CG1 . VAL G 1 13 ? 145.901 187.424 119.680 1.00 2.08  ?  5  VAL D CG1 1 
ATOM 1044 C CG2 . VAL G 1 13 ? 144.446 185.390 119.570 1.00 2.27  ?  5  VAL D CG2 1 
ATOM 1045 N N   . ALA G 1 14 ? 149.005 186.358 119.332 1.00 2.76  ?  6  ALA D N   1 
ATOM 1046 C CA  . ALA G 1 14 ? 150.254 187.017 119.688 1.00 4.23  ?  6  ALA D CA  1 
ATOM 1047 C C   . ALA G 1 14 ? 150.229 188.442 119.159 1.00 4.41  ?  6  ALA D C   1 
ATOM 1048 O O   . ALA G 1 14 ? 150.010 188.658 117.962 1.00 9.14  ?  6  ALA D O   1 
ATOM 1049 C CB  . ALA G 1 14 ? 151.457 186.257 119.129 1.00 5.34  ?  6  ALA D CB  1 
ATOM 1050 N N   . VAL G 1 15 ? 150.455 189.407 120.046 1.00 3.00  ?  7  VAL D N   1 
ATOM 1051 C CA  . VAL G 1 15 ? 150.459 190.821 119.694 1.00 5.44  ?  7  VAL D CA  1 
ATOM 1052 C C   . VAL G 1 15 ? 151.710 191.460 120.280 1.00 6.79  ?  7  VAL D C   1 
ATOM 1053 O O   . VAL G 1 15 ? 152.007 191.279 121.465 1.00 12.06 ?  7  VAL D O   1 
ATOM 1054 C CB  . VAL G 1 15 ? 149.194 191.540 120.201 1.00 7.38  ?  7  VAL D CB  1 
ATOM 1055 C CG1 . VAL G 1 15 ? 149.371 193.050 120.133 1.00 6.30  ?  7  VAL D CG1 1 
ATOM 1056 C CG2 . VAL G 1 15 ? 147.981 191.107 119.395 1.00 5.02  ?  7  VAL D CG2 1 
ATOM 1057 N N   . LEU G 1 16 ? 152.441 192.201 119.450 1.00 7.33  ?  8  LEU D N   1 
ATOM 1058 C CA  . LEU G 1 16 ? 153.611 192.942 119.897 1.00 9.02  ?  8  LEU D CA  1 
ATOM 1059 C C   . LEU G 1 16 ? 153.613 194.303 119.219 1.00 13.78 ?  8  LEU D C   1 
ATOM 1060 O O   . LEU G 1 16 ? 153.379 194.398 118.011 1.00 25.23 ?  8  LEU D O   1 
ATOM 1061 C CB  . LEU G 1 16 ? 154.904 192.180 119.582 1.00 11.16 ?  8  LEU D CB  1 
ATOM 1062 C CG  . LEU G 1 16 ? 156.227 192.951 119.638 1.00 14.67 ?  8  LEU D CG  1 
ATOM 1063 C CD1 . LEU G 1 16 ? 156.436 193.614 120.983 1.00 20.42 ?  8  LEU D CD1 1 
ATOM 1064 C CD2 . LEU G 1 16 ? 157.390 192.030 119.316 1.00 17.98 ?  8  LEU D CD2 1 
ATOM 1065 N N   . LYS G 1 17 ? 153.875 195.350 119.999 1.00 11.41 ?  9  LYS D N   1 
ATOM 1066 C CA  . LYS G 1 17 ? 153.891 196.714 119.484 1.00 13.56 ?  9  LYS D CA  1 
ATOM 1067 C C   . LYS G 1 17 ? 155.229 197.356 119.838 1.00 15.29 ?  9  LYS D C   1 
ATOM 1068 O O   . LYS G 1 17 ? 155.281 198.477 120.353 1.00 16.23 ?  9  LYS D O   1 
ATOM 1069 C CB  . LYS G 1 17 ? 152.710 197.511 120.050 1.00 13.71 ?  9  LYS D CB  1 
ATOM 1070 C CG  . LYS G 1 17 ? 152.468 198.870 119.401 1.00 14.94 ?  9  LYS D CG  1 
ATOM 1071 C CD  . LYS G 1 17 ? 151.571 199.737 120.270 1.00 14.57 ?  9  LYS D CD  1 
ATOM 1072 C CE  . LYS G 1 17 ? 150.161 199.175 120.342 1.00 16.26 ?  9  LYS D CE  1 
ATOM 1073 N NZ  . LYS G 1 17 ? 149.166 200.216 120.717 1.00 15.38 1  9  LYS D NZ  1 
ATOM 1074 N N   . GLY G 1 18 ? 156.315 196.643 119.579 1.00 16.28 ?  10 GLY D N   1 
ATOM 1075 C CA  . GLY G 1 18 ? 157.636 197.103 119.968 1.00 20.25 ?  10 GLY D CA  1 
ATOM 1076 C C   . GLY G 1 18 ? 158.609 197.090 118.812 1.00 26.23 ?  10 GLY D C   1 
ATOM 1077 O O   . GLY G 1 18 ? 158.538 196.238 117.925 1.00 26.39 ?  10 GLY D O   1 
ATOM 1078 N N   . ASP G 1 19 ? 159.536 198.050 118.838 1.00 32.75 ?  11 ASP D N   1 
ATOM 1079 C CA  . ASP G 1 19 ? 160.559 198.168 117.807 1.00 34.06 ?  11 ASP D CA  1 
ATOM 1080 C C   . ASP G 1 19 ? 161.542 197.002 117.844 1.00 34.38 ?  11 ASP D C   1 
ATOM 1081 O O   . ASP G 1 19 ? 162.242 196.763 116.856 1.00 31.97 ?  11 ASP D O   1 
ATOM 1082 C CB  . ASP G 1 19 ? 161.289 199.507 117.982 1.00 37.30 ?  11 ASP D CB  1 
ATOM 1083 C CG  . ASP G 1 19 ? 162.042 199.957 116.733 1.00 41.59 ?  11 ASP D CG  1 
ATOM 1084 O OD1 . ASP G 1 19 ? 162.636 199.127 116.020 1.00 43.60 -1 11 ASP D OD1 1 
ATOM 1085 O OD2 . ASP G 1 19 ? 162.045 201.178 116.468 1.00 45.72 ?  11 ASP D OD2 1 
ATOM 1086 N N   . GLY G 1 20 ? 161.602 196.265 118.949 1.00 35.94 ?  12 GLY D N   1 
ATOM 1087 C CA  . GLY G 1 20 ? 162.524 195.163 119.086 1.00 34.39 ?  12 GLY D CA  1 
ATOM 1088 C C   . GLY G 1 20 ? 162.305 194.056 118.076 1.00 29.47 ?  12 GLY D C   1 
ATOM 1089 O O   . GLY G 1 20 ? 161.171 193.696 117.743 1.00 28.48 ?  12 GLY D O   1 
ATOM 1090 N N   . PRO G 1 21 ? 163.399 193.501 117.561 1.00 26.81 ?  13 PRO D N   1 
ATOM 1091 C CA  . PRO G 1 21 ? 163.287 192.377 116.627 1.00 26.71 ?  13 PRO D CA  1 
ATOM 1092 C C   . PRO G 1 21 ? 162.707 191.143 117.300 1.00 25.45 ?  13 PRO D C   1 
ATOM 1093 O O   . PRO G 1 21 ? 162.876 190.921 118.501 1.00 33.91 ?  13 PRO D O   1 
ATOM 1094 C CB  . PRO G 1 21 ? 164.736 192.136 116.184 1.00 25.06 ?  13 PRO D CB  1 
ATOM 1095 C CG  . PRO G 1 21 ? 165.458 193.407 116.505 1.00 25.84 ?  13 PRO D CG  1 
ATOM 1096 C CD  . PRO G 1 21 ? 164.792 193.945 117.729 1.00 27.75 ?  13 PRO D CD  1 
ATOM 1097 N N   . VAL G 1 22 ? 162.014 190.336 116.504 1.00 20.80 ?  14 VAL D N   1 
ATOM 1098 C CA  . VAL G 1 22 ? 161.452 189.071 116.960 1.00 18.20 ?  14 VAL D CA  1 
ATOM 1099 C C   . VAL G 1 22 ? 162.394 187.953 116.544 1.00 23.47 ?  14 VAL D C   1 
ATOM 1100 O O   . VAL G 1 22 ? 162.781 187.859 115.373 1.00 33.83 ?  14 VAL D O   1 
ATOM 1101 C CB  . VAL G 1 22 ? 160.044 188.849 116.385 1.00 17.86 ?  14 VAL D CB  1 
ATOM 1102 C CG1 . VAL G 1 22 ? 159.684 187.374 116.418 1.00 15.32 ?  14 VAL D CG1 1 
ATOM 1103 C CG2 . VAL G 1 22 ? 159.027 189.662 117.158 1.00 22.05 ?  14 VAL D CG2 1 
ATOM 1104 N N   . GLN G 1 23 ? 162.767 187.106 117.501 1.00 22.36 ?  15 GLN D N   1 
ATOM 1105 C CA  . GLN G 1 23 ? 163.704 186.013 117.260 1.00 20.30 ?  15 GLN D CA  1 
ATOM 1106 C C   . GLN G 1 23 ? 163.125 184.738 117.859 1.00 19.11 ?  15 GLN D C   1 
ATOM 1107 O O   . GLN G 1 23 ? 162.971 184.638 119.080 1.00 27.36 ?  15 GLN D O   1 
ATOM 1108 C CB  . GLN G 1 23 ? 165.074 186.328 117.860 1.00 18.87 ?  15 GLN D CB  1 
ATOM 1109 C CG  . GLN G 1 23 ? 166.223 185.597 117.202 1.00 17.91 ?  15 GLN D CG  1 
ATOM 1110 C CD  . GLN G 1 23 ? 167.468 186.452 117.106 1.00 21.22 ?  15 GLN D CD  1 
ATOM 1111 O OE1 . GLN G 1 23 ? 168.202 186.615 118.081 1.00 15.30 ?  15 GLN D OE1 1 
ATOM 1112 N NE2 . GLN G 1 23 ? 167.713 187.007 115.925 1.00 24.15 ?  15 GLN D NE2 1 
ATOM 1113 N N   . GLY G 1 24 ? 162.808 183.769 117.004 1.00 12.80 ?  16 GLY D N   1 
ATOM 1114 C CA  . GLY G 1 24 ? 162.263 182.508 117.465 1.00 7.81  ?  16 GLY D CA  1 
ATOM 1115 C C   . GLY G 1 24 ? 160.995 182.108 116.742 1.00 4.63  ?  16 GLY D C   1 
ATOM 1116 O O   . GLY G 1 24 ? 160.760 182.536 115.610 1.00 5.60  ?  16 GLY D O   1 
ATOM 1117 N N   . ILE G 1 25 ? 160.171 181.289 117.382 1.00 3.20  ?  17 ILE D N   1 
ATOM 1118 C CA  . ILE G 1 25 ? 158.909 180.849 116.801 1.00 2.97  ?  17 ILE D CA  1 
ATOM 1119 C C   . ILE G 1 25 ? 157.761 181.541 117.519 1.00 4.18  ?  17 ILE D C   1 
ATOM 1120 O O   . ILE G 1 25 ? 157.831 181.829 118.719 1.00 20.36 ?  17 ILE D O   1 
ATOM 1121 C CB  . ILE G 1 25 ? 158.760 179.317 116.872 1.00 2.76  ?  17 ILE D CB  1 
ATOM 1122 C CG1 . ILE G 1 25 ? 160.121 178.640 116.734 1.00 3.84  ?  17 ILE D CG1 1 
ATOM 1123 C CG2 . ILE G 1 25 ? 157.814 178.824 115.795 1.00 3.86  ?  17 ILE D CG2 1 
ATOM 1124 C CD1 . ILE G 1 25 ? 160.079 177.158 117.001 1.00 2.74  ?  17 ILE D CD1 1 
ATOM 1125 N N   . ILE G 1 26 ? 156.694 181.814 116.775 1.00 2.67  ?  18 ILE D N   1 
ATOM 1126 C CA  . ILE G 1 26 ? 155.491 182.441 117.307 1.00 1.40  ?  18 ILE D CA  1 
ATOM 1127 C C   . ILE G 1 26 ? 154.316 181.509 117.052 1.00 1.52  ?  18 ILE D C   1 
ATOM 1128 O O   . ILE G 1 26 ? 154.130 181.033 115.927 1.00 2.00  ?  18 ILE D O   1 
ATOM 1129 C CB  . ILE G 1 26 ? 155.240 183.821 116.674 1.00 1.45  ?  18 ILE D CB  1 
ATOM 1130 C CG1 . ILE G 1 26 ? 156.562 184.556 116.449 1.00 1.29  ?  18 ILE D CG1 1 
ATOM 1131 C CG2 . ILE G 1 26 ? 154.318 184.644 117.549 1.00 2.28  ?  18 ILE D CG2 1 
ATOM 1132 C CD1 . ILE G 1 26 ? 157.226 185.019 117.716 1.00 1.32  ?  18 ILE D CD1 1 
ATOM 1133 N N   . ASN G 1 27 ? 153.528 181.255 118.097 1.00 1.62  ?  19 ASN D N   1 
ATOM 1134 C CA  . ASN G 1 27 ? 152.356 180.381 118.013 1.00 2.03  ?  19 ASN D CA  1 
ATOM 1135 C C   . ASN G 1 27 ? 152.734 178.985 117.526 1.00 1.29  ?  19 ASN D C   1 
ATOM 1136 O O   . ASN G 1 27 ? 152.051 178.390 116.692 1.00 2.24  ?  19 ASN D O   1 
ATOM 1137 C CB  . ASN G 1 27 ? 151.272 180.993 117.124 1.00 2.07  ?  19 ASN D CB  1 
ATOM 1138 C CG  . ASN G 1 27 ? 150.935 182.417 117.515 1.00 3.34  ?  19 ASN D CG  1 
ATOM 1139 O OD1 . ASN G 1 27 ? 150.688 182.710 118.684 1.00 3.83  ?  19 ASN D OD1 1 
ATOM 1140 N ND2 . ASN G 1 27 ? 150.924 183.311 116.535 1.00 4.34  ?  19 ASN D ND2 1 
ATOM 1141 N N   . PHE G 1 28 ? 153.837 178.461 118.051 1.00 1.33  ?  20 PHE D N   1 
ATOM 1142 C CA  . PHE G 1 28 ? 154.260 177.102 117.747 1.00 1.50  ?  20 PHE D CA  1 
ATOM 1143 C C   . PHE G 1 28 ? 153.376 176.113 118.498 1.00 2.68  ?  20 PHE D C   1 
ATOM 1144 O O   . PHE G 1 28 ? 153.239 176.197 119.722 1.00 9.02  ?  20 PHE D O   1 
ATOM 1145 C CB  . PHE G 1 28 ? 155.729 176.921 118.127 1.00 2.39  ?  20 PHE D CB  1 
ATOM 1146 C CG  . PHE G 1 28 ? 156.318 175.610 117.701 1.00 1.78  ?  20 PHE D CG  1 
ATOM 1147 C CD1 . PHE G 1 28 ? 155.732 174.852 116.706 1.00 2.68  ?  20 PHE D CD1 1 
ATOM 1148 C CD2 . PHE G 1 28 ? 157.473 175.141 118.296 1.00 2.10  ?  20 PHE D CD2 1 
ATOM 1149 C CE1 . PHE G 1 28 ? 156.279 173.649 116.325 1.00 3.16  ?  20 PHE D CE1 1 
ATOM 1150 C CE2 . PHE G 1 28 ? 158.024 173.941 117.916 1.00 2.00  ?  20 PHE D CE2 1 
ATOM 1151 C CZ  . PHE G 1 28 ? 157.429 173.195 116.928 1.00 2.66  ?  20 PHE D CZ  1 
ATOM 1152 N N   . GLU G 1 29 ? 152.777 175.177 117.766 1.00 1.15  ?  21 GLU D N   1 
ATOM 1153 C CA  . GLU G 1 29 ? 151.785 174.257 118.316 1.00 1.57  ?  21 GLU D CA  1 
ATOM 1154 C C   . GLU G 1 29 ? 152.121 172.817 117.955 1.00 1.73  ?  21 GLU D C   1 
ATOM 1155 O O   . GLU G 1 29 ? 151.278 172.063 117.465 1.00 1.58  ?  21 GLU D O   1 
ATOM 1156 C CB  . GLU G 1 29 ? 150.383 174.611 117.830 1.00 1.06  ?  21 GLU D CB  1 
ATOM 1157 C CG  . GLU G 1 29 ? 150.101 176.103 117.772 1.00 1.10  ?  21 GLU D CG  1 
ATOM 1158 C CD  . GLU G 1 29 ? 148.622 176.418 117.728 1.00 1.23  ?  21 GLU D CD  1 
ATOM 1159 O OE1 . GLU G 1 29 ? 147.811 175.471 117.684 1.00 1.37  ?  21 GLU D OE1 1 
ATOM 1160 O OE2 . GLU G 1 29 ? 148.273 177.616 117.736 1.00 1.43  -1 21 GLU D OE2 1 
ATOM 1161 N N   . GLN G 1 30 ? 153.371 172.417 118.189 1.00 1.74  ?  22 GLN D N   1 
ATOM 1162 C CA  . GLN G 1 30 ? 153.769 171.032 117.969 1.00 1.55  ?  22 GLN D CA  1 
ATOM 1163 C C   . GLN G 1 30 ? 152.912 170.096 118.811 1.00 2.07  ?  22 GLN D C   1 
ATOM 1164 O O   . GLN G 1 30 ? 152.709 170.328 120.004 1.00 7.82  ?  22 GLN D O   1 
ATOM 1165 C CB  . GLN G 1 30 ? 155.248 170.850 118.308 1.00 1.81  ?  22 GLN D CB  1 
ATOM 1166 C CG  . GLN G 1 30 ? 155.632 169.426 118.655 1.00 2.66  ?  22 GLN D CG  1 
ATOM 1167 C CD  . GLN G 1 30 ? 157.132 169.202 118.666 1.00 2.57  ?  22 GLN D CD  1 
ATOM 1168 O OE1 . GLN G 1 30 ? 157.803 169.377 117.651 1.00 2.36  ?  22 GLN D OE1 1 
ATOM 1169 N NE2 . GLN G 1 30 ? 157.664 168.805 119.815 1.00 2.89  ?  22 GLN D NE2 1 
ATOM 1170 N N   . LYS G 1 31 ? 152.402 169.035 118.187 1.00 1.87  ?  23 LYS D N   1 
ATOM 1171 C CA  . LYS G 1 31 ? 151.427 168.180 118.850 1.00 1.92  ?  23 LYS D CA  1 
ATOM 1172 C C   . LYS G 1 31 ? 151.552 166.748 118.357 1.00 3.06  ?  23 LYS D C   1 
ATOM 1173 O O   . LYS G 1 31 ? 151.588 166.506 117.148 1.00 5.25  ?  23 LYS D O   1 
ATOM 1174 C CB  . LYS G 1 31 ? 150.005 168.701 118.610 1.00 1.73  ?  23 LYS D CB  1 
ATOM 1175 C CG  . LYS G 1 31 ? 148.917 167.653 118.755 1.00 1.66  ?  23 LYS D CG  1 
ATOM 1176 C CD  . LYS G 1 31 ? 147.536 168.285 118.849 1.00 2.02  ?  23 LYS D CD  1 
ATOM 1177 C CE  . LYS G 1 31 ? 147.450 169.579 118.055 1.00 2.93  ?  23 LYS D CE  1 
ATOM 1178 N NZ  . LYS G 1 31 ? 146.164 170.289 118.291 1.00 4.12  1  23 LYS D NZ  1 
ATOM 1179 N N   . GLU G 1 32 ? 151.608 165.809 119.305 1.00 4.10  ?  24 GLU D N   1 
ATOM 1180 C CA  . GLU G 1 32 ? 151.618 164.374 119.014 1.00 5.39  ?  24 GLU D CA  1 
ATOM 1181 C C   . GLU G 1 32 ? 152.736 164.005 118.044 1.00 7.25  ?  24 GLU D C   1 
ATOM 1182 O O   . GLU G 1 32 ? 152.552 163.209 117.121 1.00 9.80  ?  24 GLU D O   1 
ATOM 1183 C CB  . GLU G 1 32 ? 150.262 163.914 118.479 1.00 3.63  ?  24 GLU D CB  1 
ATOM 1184 C CG  . GLU G 1 32 ? 149.113 164.131 119.445 1.00 4.42  ?  24 GLU D CG  1 
ATOM 1185 C CD  . GLU G 1 32 ? 147.767 163.803 118.835 1.00 4.91  ?  24 GLU D CD  1 
ATOM 1186 O OE1 . GLU G 1 32 ? 147.557 162.634 118.451 1.00 6.01  ?  24 GLU D OE1 1 
ATOM 1187 O OE2 . GLU G 1 32 ? 146.918 164.715 118.739 1.00 3.74  -1 24 GLU D OE2 1 
ATOM 1188 N N   . SER G 1 33 ? 153.912 164.580 118.261 1.00 6.77  ?  25 SER D N   1 
ATOM 1189 C CA  . SER G 1 33 ? 155.050 164.370 117.381 1.00 10.76 ?  25 SER D CA  1 
ATOM 1190 C C   . SER G 1 33 ? 156.230 163.823 118.182 1.00 15.28 ?  25 SER D C   1 
ATOM 1191 O O   . SER G 1 33 ? 156.109 163.479 119.359 1.00 20.99 ?  25 SER D O   1 
ATOM 1192 C CB  . SER G 1 33 ? 155.422 165.668 116.665 1.00 11.58 ?  25 SER D CB  1 
ATOM 1193 O OG  . SER G 1 33 ? 156.033 166.569 117.567 1.00 6.84  ?  25 SER D OG  1 
ATOM 1194 N N   . ASN G 1 34 ? 157.383 163.737 117.519 1.00 13.65 ?  26 ASN D N   1 
ATOM 1195 C CA  . ASN G 1 34 ? 158.619 163.293 118.159 1.00 14.20 ?  26 ASN D CA  1 
ATOM 1196 C C   . ASN G 1 34 ? 159.768 164.010 117.457 1.00 14.73 ?  26 ASN D C   1 
ATOM 1197 O O   . ASN G 1 34 ? 160.175 163.612 116.363 1.00 20.09 ?  26 ASN D O   1 
ATOM 1198 C CB  . ASN G 1 34 ? 158.771 161.781 118.081 1.00 20.75 ?  26 ASN D CB  1 
ATOM 1199 C CG  . ASN G 1 34 ? 160.159 161.317 118.467 1.00 23.14 ?  26 ASN D CG  1 
ATOM 1200 O OD1 . ASN G 1 34 ? 160.860 160.692 117.671 1.00 26.41 ?  26 ASN D OD1 1 
ATOM 1201 N ND2 . ASN G 1 34 ? 160.566 161.622 119.693 1.00 21.92 ?  26 ASN D ND2 1 
ATOM 1202 N N   . GLY G 1 35 ? 160.275 165.065 118.085 1.00 9.69  ?  27 GLY D N   1 
ATOM 1203 C CA  . GLY G 1 35 ? 161.351 165.834 117.512 1.00 6.74  ?  27 GLY D CA  1 
ATOM 1204 C C   . GLY G 1 35 ? 161.936 166.834 118.485 1.00 2.59  ?  27 GLY D C   1 
ATOM 1205 O O   . GLY G 1 35 ? 161.220 167.599 119.136 1.00 2.30  ?  27 GLY D O   1 
ATOM 1206 N N   . PRO G 1 36 ? 163.259 166.842 118.602 1.00 2.08  ?  28 PRO D N   1 
ATOM 1207 C CA  . PRO G 1 36 ? 163.944 167.818 119.472 1.00 2.22  ?  28 PRO D CA  1 
ATOM 1208 C C   . PRO G 1 36 ? 164.011 169.209 118.845 1.00 1.46  ?  28 PRO D C   1 
ATOM 1209 O O   . PRO G 1 36 ? 164.998 169.623 118.237 1.00 1.56  ?  28 PRO D O   1 
ATOM 1210 C CB  . PRO G 1 36 ? 165.331 167.198 119.646 1.00 3.18  ?  28 PRO D CB  1 
ATOM 1211 C CG  . PRO G 1 36 ? 165.540 166.391 118.419 1.00 2.60  ?  28 PRO D CG  1 
ATOM 1212 C CD  . PRO G 1 36 ? 164.194 165.876 118.002 1.00 3.15  ?  28 PRO D CD  1 
ATOM 1213 N N   . VAL G 1 37 ? 162.916 169.957 118.992 1.00 1.09  ?  29 VAL D N   1 
ATOM 1214 C CA  . VAL G 1 37 ? 162.873 171.319 118.476 1.00 1.31  ?  29 VAL D CA  1 
ATOM 1215 C C   . VAL G 1 37 ? 163.897 172.182 119.198 1.00 1.06  ?  29 VAL D C   1 
ATOM 1216 O O   . VAL G 1 37 ? 163.957 172.214 120.433 1.00 2.25  ?  29 VAL D O   1 
ATOM 1217 C CB  . VAL G 1 37 ? 161.452 171.890 118.589 1.00 1.17  ?  29 VAL D CB  1 
ATOM 1218 C CG1 . VAL G 1 37 ? 160.914 171.722 119.981 1.00 1.83  ?  29 VAL D CG1 1 
ATOM 1219 C CG2 . VAL G 1 37 ? 161.457 173.366 118.226 1.00 1.49  ?  29 VAL D CG2 1 
ATOM 1220 N N   . LYS G 1 38 ? 164.723 172.877 118.422 1.00 0.86  ?  30 LYS D N   1 
ATOM 1221 C CA  . LYS G 1 38 ? 165.781 173.728 118.946 1.00 1.06  ?  30 LYS D CA  1 
ATOM 1222 C C   . LYS G 1 38 ? 165.654 175.113 118.332 1.00 1.21  ?  30 LYS D C   1 
ATOM 1223 O O   . LYS G 1 38 ? 165.522 175.245 117.112 1.00 3.08  ?  30 LYS D O   1 
ATOM 1224 C CB  . LYS G 1 38 ? 167.159 173.132 118.646 1.00 1.14  ?  30 LYS D CB  1 
ATOM 1225 C CG  . LYS G 1 38 ? 168.327 174.016 119.046 1.00 1.32  ?  30 LYS D CG  1 
ATOM 1226 C CD  . LYS G 1 38 ? 169.651 173.370 118.677 1.00 1.00  ?  30 LYS D CD  1 
ATOM 1227 C CE  . LYS G 1 38 ? 170.824 174.274 119.019 1.00 1.14  ?  30 LYS D CE  1 
ATOM 1228 N NZ  . LYS G 1 38 ? 172.130 173.637 118.692 1.00 0.73  1  30 LYS D NZ  1 
ATOM 1229 N N   . VAL G 1 39 ? 165.693 176.140 119.175 1.00 0.91  ?  31 VAL D N   1 
ATOM 1230 C CA  . VAL G 1 39 ? 165.600 177.525 118.735 1.00 1.50  ?  31 VAL D CA  1 
ATOM 1231 C C   . VAL G 1 39 ? 166.857 178.250 119.188 1.00 2.30  ?  31 VAL D C   1 
ATOM 1232 O O   . VAL G 1 39 ? 167.187 178.244 120.380 1.00 4.40  ?  31 VAL D O   1 
ATOM 1233 C CB  . VAL G 1 39 ? 164.343 178.218 119.285 1.00 2.29  ?  31 VAL D CB  1 
ATOM 1234 C CG1 . VAL G 1 39 ? 164.259 179.645 118.769 1.00 2.31  ?  31 VAL D CG1 1 
ATOM 1235 C CG2 . VAL G 1 39 ? 163.102 177.434 118.907 1.00 1.58  ?  31 VAL D CG2 1 
ATOM 1236 N N   . TRP G 1 40 ? 167.551 178.874 118.243 1.00 2.21  ?  32 TRP D N   1 
ATOM 1237 C CA  . TRP G 1 40 ? 168.774 179.616 118.520 1.00 2.99  ?  32 TRP D CA  1 
ATOM 1238 C C   . TRP G 1 40 ? 168.555 181.068 118.126 1.00 3.21  ?  32 TRP D C   1 
ATOM 1239 O O   . TRP G 1 40 ? 168.204 181.357 116.977 1.00 5.23  ?  32 TRP D O   1 
ATOM 1240 C CB  . TRP G 1 40 ? 169.959 179.013 117.761 1.00 4.17  ?  32 TRP D CB  1 
ATOM 1241 C CG  . TRP G 1 40 ? 171.302 179.503 118.215 1.00 3.61  ?  32 TRP D CG  1 
ATOM 1242 C CD1 . TRP G 1 40 ? 171.714 180.800 118.313 1.00 4.41  ?  32 TRP D CD1 1 
ATOM 1243 C CD2 . TRP G 1 40 ? 172.411 178.698 118.629 1.00 3.72  ?  32 TRP D CD2 1 
ATOM 1244 N NE1 . TRP G 1 40 ? 173.010 180.852 118.762 1.00 3.94  ?  32 TRP D NE1 1 
ATOM 1245 C CE2 . TRP G 1 40 ? 173.461 179.575 118.964 1.00 4.98  ?  32 TRP D CE2 1 
ATOM 1246 C CE3 . TRP G 1 40 ? 172.617 177.321 118.749 1.00 3.71  ?  32 TRP D CE3 1 
ATOM 1247 C CZ2 . TRP G 1 40 ? 174.699 179.120 119.412 1.00 6.31  ?  32 TRP D CZ2 1 
ATOM 1248 C CZ3 . TRP G 1 40 ? 173.847 176.871 119.194 1.00 4.28  ?  32 TRP D CZ3 1 
ATOM 1249 C CH2 . TRP G 1 40 ? 174.872 177.768 119.520 1.00 5.60  ?  32 TRP D CH2 1 
ATOM 1250 N N   . GLY G 1 41 ? 168.761 181.975 119.075 1.00 3.12  ?  33 GLY D N   1 
ATOM 1251 C CA  . GLY G 1 41 ? 168.590 183.388 118.808 1.00 7.91  ?  33 GLY D CA  1 
ATOM 1252 C C   . GLY G 1 41 ? 169.767 184.224 119.262 1.00 9.98  ?  33 GLY D C   1 
ATOM 1253 O O   . GLY G 1 41 ? 170.086 184.265 120.453 1.00 15.16 ?  33 GLY D O   1 
ATOM 1254 N N   . SER G 1 42 ? 170.420 184.898 118.320 1.00 7.03  ?  34 SER D N   1 
ATOM 1255 C CA  . SER G 1 42 ? 171.579 185.728 118.613 1.00 9.59  ?  34 SER D CA  1 
ATOM 1256 C C   . SER G 1 42 ? 171.385 187.096 117.981 1.00 12.86 ?  34 SER D C   1 
ATOM 1257 O O   . SER G 1 42 ? 170.883 187.198 116.858 1.00 22.86 ?  34 SER D O   1 
ATOM 1258 C CB  . SER G 1 42 ? 172.869 185.082 118.096 1.00 10.24 ?  34 SER D CB  1 
ATOM 1259 O OG  . SER G 1 42 ? 173.988 185.914 118.342 1.00 10.90 ?  34 SER D OG  1 
ATOM 1260 N N   . ILE G 1 43 ? 171.775 188.143 118.705 1.00 8.73  ?  35 ILE D N   1 
ATOM 1261 C CA  . ILE G 1 43 ? 171.722 189.512 118.206 1.00 12.07 ?  35 ILE D CA  1 
ATOM 1262 C C   . ILE G 1 43 ? 172.867 190.293 118.835 1.00 13.05 ?  35 ILE D C   1 
ATOM 1263 O O   . ILE G 1 43 ? 172.930 190.429 120.062 1.00 18.89 ?  35 ILE D O   1 
ATOM 1264 C CB  . ILE G 1 43 ? 170.370 190.188 118.500 1.00 13.89 ?  35 ILE D CB  1 
ATOM 1265 C CG1 . ILE G 1 43 ? 170.476 191.706 118.339 1.00 16.89 ?  35 ILE D CG1 1 
ATOM 1266 C CG2 . ILE G 1 43 ? 169.850 189.795 119.871 1.00 19.63 ?  35 ILE D CG2 1 
ATOM 1267 C CD1 . ILE G 1 43 ? 169.139 192.412 118.344 1.00 19.55 ?  35 ILE D CD1 1 
ATOM 1268 N N   . LYS G 1 44 ? 173.778 190.795 118.003 1.00 13.71 ?  36 LYS D N   1 
ATOM 1269 C CA  . LYS G 1 44 ? 174.937 191.545 118.476 1.00 19.51 ?  36 LYS D CA  1 
ATOM 1270 C C   . LYS G 1 44 ? 174.944 192.931 117.843 1.00 24.14 ?  36 LYS D C   1 
ATOM 1271 O O   . LYS G 1 44 ? 175.580 193.146 116.807 1.00 35.30 ?  36 LYS D O   1 
ATOM 1272 C CB  . LYS G 1 44 ? 176.236 190.795 118.173 1.00 19.26 ?  36 LYS D CB  1 
ATOM 1273 C CG  . LYS G 1 44 ? 176.272 189.380 118.731 1.00 15.07 ?  36 LYS D CG  1 
ATOM 1274 C CD  . LYS G 1 44 ? 177.399 188.563 118.123 1.00 15.29 ?  36 LYS D CD  1 
ATOM 1275 C CE  . LYS G 1 44 ? 178.748 188.978 118.684 1.00 19.88 ?  36 LYS D CE  1 
ATOM 1276 N NZ  . LYS G 1 44 ? 179.760 187.895 118.538 1.00 20.42 1  36 LYS D NZ  1 
ATOM 1277 N N   . GLY G 1 45 ? 174.242 193.870 118.474 1.00 22.39 ?  37 GLY D N   1 
ATOM 1278 C CA  . GLY G 1 45 ? 174.209 195.242 118.018 1.00 34.53 ?  37 GLY D CA  1 
ATOM 1279 C C   . GLY G 1 45 ? 173.476 196.118 119.013 1.00 50.93 ?  37 GLY D C   1 
ATOM 1280 O O   . GLY G 1 45 ? 173.179 195.691 120.130 1.00 60.96 ?  37 GLY D O   1 
ATOM 1281 N N   . LEU G 1 46 ? 173.164 197.345 118.605 1.00 55.90 ?  38 LEU D N   1 
ATOM 1282 C CA  . LEU G 1 46 ? 172.523 198.294 119.504 1.00 62.17 ?  38 LEU D CA  1 
ATOM 1283 C C   . LEU G 1 46 ? 171.248 198.847 118.886 1.00 63.02 ?  38 LEU D C   1 
ATOM 1284 O O   . LEU G 1 46 ? 171.163 199.060 117.675 1.00 68.61 ?  38 LEU D O   1 
ATOM 1285 C CB  . LEU G 1 46 ? 173.460 199.446 119.896 1.00 66.59 ?  38 LEU D CB  1 
ATOM 1286 C CG  . LEU G 1 46 ? 173.911 200.536 118.923 1.00 64.08 ?  38 LEU D CG  1 
ATOM 1287 C CD1 . LEU G 1 46 ? 174.673 201.606 119.668 1.00 67.23 ?  38 LEU D CD1 1 
ATOM 1288 C CD2 . LEU G 1 46 ? 174.847 199.933 117.905 1.00 56.33 ?  38 LEU D CD2 1 
ATOM 1289 N N   . THR G 1 47 ? 170.259 199.083 119.745 1.00 61.74 ?  39 THR D N   1 
ATOM 1290 C CA  . THR G 1 47 ? 168.973 199.634 119.351 1.00 64.45 ?  39 THR D CA  1 
ATOM 1291 C C   . THR G 1 47 ? 168.737 200.937 120.105 1.00 65.26 ?  39 THR D C   1 
ATOM 1292 O O   . THR G 1 47 ? 169.338 201.177 121.157 1.00 68.25 ?  39 THR D O   1 
ATOM 1293 C CB  . THR G 1 47 ? 167.840 198.640 119.628 1.00 67.76 ?  39 THR D CB  1 
ATOM 1294 O OG1 . THR G 1 47 ? 167.671 198.485 121.041 1.00 67.28 ?  39 THR D OG1 1 
ATOM 1295 C CG2 . THR G 1 47 ? 168.167 197.285 119.025 1.00 66.15 ?  39 THR D CG2 1 
ATOM 1296 N N   . GLU G 1 48 ? 167.867 201.781 119.559 1.00 66.18 ?  40 GLU D N   1 
ATOM 1297 C CA  . GLU G 1 48 ? 167.567 203.077 120.147 1.00 61.50 ?  40 GLU D CA  1 
ATOM 1298 C C   . GLU G 1 48 ? 166.059 203.260 120.227 1.00 59.06 ?  40 GLU D C   1 
ATOM 1299 O O   . GLU G 1 48 ? 165.287 202.509 119.625 1.00 60.79 ?  40 GLU D O   1 
ATOM 1300 C CB  . GLU G 1 48 ? 168.196 204.215 119.336 1.00 62.11 ?  40 GLU D CB  1 
ATOM 1301 C CG  . GLU G 1 48 ? 169.627 204.548 119.725 1.00 60.56 ?  40 GLU D CG  1 
ATOM 1302 C CD  . GLU G 1 48 ? 170.612 203.476 119.298 1.00 65.93 ?  40 GLU D CD  1 
ATOM 1303 O OE1 . GLU G 1 48 ? 170.604 203.099 118.110 1.00 71.63 ?  40 GLU D OE1 1 
ATOM 1304 O OE2 . GLU G 1 48 ? 171.396 203.012 120.150 1.00 64.65 -1 40 GLU D OE2 1 
ATOM 1305 N N   . GLY G 1 49 ? 165.647 204.269 120.988 1.00 60.96 ?  41 GLY D N   1 
ATOM 1306 C CA  . GLY G 1 49 ? 164.239 204.578 121.149 1.00 63.08 ?  41 GLY D CA  1 
ATOM 1307 C C   . GLY G 1 49 ? 163.853 205.918 120.555 1.00 60.55 ?  41 GLY D C   1 
ATOM 1308 O O   . GLY G 1 49 ? 164.670 206.836 120.487 1.00 62.50 ?  41 GLY D O   1 
ATOM 1309 N N   . UNK H 2 1  ? 145.069 207.313 121.528 1.00 26.05 ?  1  UNK J N   1 
ATOM 1310 C CA  . UNK H 2 1  ? 144.082 206.474 122.197 1.00 26.04 ?  1  UNK J CA  1 
ATOM 1311 C C   . UNK H 2 1  ? 144.223 205.018 121.768 1.00 26.58 ?  1  UNK J C   1 
ATOM 1312 O O   . UNK H 2 1  ? 143.278 204.420 121.252 1.00 29.40 ?  1  UNK J O   1 
ATOM 1313 C CB  . UNK H 2 1  ? 142.676 206.978 121.910 1.00 22.41 ?  1  UNK J CB  1 
ATOM 1314 N N   . UNK H 2 2  ? 145.409 204.456 121.983 1.00 22.86 ?  2  UNK J N   1 
ATOM 1315 C CA  . UNK H 2 2  ? 145.666 203.070 121.614 1.00 22.32 ?  2  UNK J CA  1 
ATOM 1316 C C   . UNK H 2 2  ? 144.843 202.129 122.483 1.00 21.72 ?  2  UNK J C   1 
ATOM 1317 O O   . UNK H 2 2  ? 144.806 202.273 123.709 1.00 26.76 ?  2  UNK J O   1 
ATOM 1318 C CB  . UNK H 2 2  ? 147.155 202.758 121.748 1.00 21.86 ?  2  UNK J CB  1 
ATOM 1319 N N   . UNK H 2 3  ? 144.180 201.165 121.849 1.00 21.09 ?  3  UNK J N   1 
ATOM 1320 C CA  . UNK H 2 3  ? 143.351 200.201 122.556 1.00 25.47 ?  3  UNK J CA  1 
ATOM 1321 C C   . UNK H 2 3  ? 143.467 198.841 121.887 1.00 29.06 ?  3  UNK J C   1 
ATOM 1322 O O   . UNK H 2 3  ? 143.406 198.740 120.659 1.00 38.46 ?  3  UNK J O   1 
ATOM 1323 C CB  . UNK H 2 3  ? 141.884 200.647 122.592 1.00 25.18 ?  3  UNK J CB  1 
ATOM 1324 N N   . UNK H 2 4  ? 143.634 197.800 122.698 1.00 28.04 ?  4  UNK J N   1 
ATOM 1325 C CA  . UNK H 2 4  ? 143.702 196.425 122.220 1.00 31.96 ?  4  UNK J CA  1 
ATOM 1326 C C   . UNK H 2 4  ? 142.539 195.648 122.817 1.00 34.09 ?  4  UNK J C   1 
ATOM 1327 O O   . UNK H 2 4  ? 142.393 195.587 124.042 1.00 39.06 ?  4  UNK J O   1 
ATOM 1328 C CB  . UNK H 2 4  ? 145.036 195.776 122.592 1.00 32.03 ?  4  UNK J CB  1 
ATOM 1329 N N   . UNK H 2 5  ? 141.716 195.056 121.954 1.00 29.75 ?  5  UNK J N   1 
ATOM 1330 C CA  . UNK H 2 5  ? 140.532 194.322 122.380 1.00 30.80 ?  5  UNK J CA  1 
ATOM 1331 C C   . UNK H 2 5  ? 140.547 192.933 121.763 1.00 29.10 ?  5  UNK J C   1 
ATOM 1332 O O   . UNK H 2 5  ? 140.754 192.789 120.554 1.00 33.74 ?  5  UNK J O   1 
ATOM 1333 C CB  . UNK H 2 5  ? 139.250 195.064 121.988 1.00 39.20 ?  5  UNK J CB  1 
ATOM 1334 N N   . UNK H 2 6  ? 140.328 191.918 122.594 1.00 30.19 ?  6  UNK J N   1 
ATOM 1335 C CA  . UNK H 2 6  ? 140.229 190.537 122.144 1.00 38.33 ?  6  UNK J CA  1 
ATOM 1336 C C   . UNK H 2 6  ? 139.012 189.899 122.795 1.00 42.09 ?  6  UNK J C   1 
ATOM 1337 O O   . UNK H 2 6  ? 138.851 189.972 124.018 1.00 49.64 ?  6  UNK J O   1 
ATOM 1338 C CB  . UNK H 2 6  ? 141.496 189.746 122.483 1.00 37.15 ?  6  UNK J CB  1 
ATOM 1339 N N   . UNK H 2 7  ? 138.164 189.276 121.983 1.00 39.87 ?  7  UNK J N   1 
ATOM 1340 C CA  . UNK H 2 7  ? 136.937 188.661 122.461 1.00 42.13 ?  7  UNK J CA  1 
ATOM 1341 C C   . UNK H 2 7  ? 136.844 187.233 121.945 1.00 45.23 ?  7  UNK J C   1 
ATOM 1342 O O   . UNK H 2 7  ? 137.450 186.875 120.932 1.00 56.63 ?  7  UNK J O   1 
ATOM 1343 C CB  . UNK H 2 7  ? 135.700 189.460 122.028 1.00 38.50 ?  7  UNK J CB  1 
ATOM 1344 N N   . UNK H 2 8  ? 136.075 186.418 122.660 1.00 41.67 ?  8  UNK J N   1 
ATOM 1345 C CA  . UNK H 2 8  ? 135.879 185.024 122.284 1.00 47.40 ?  8  UNK J CA  1 
ATOM 1346 C C   . UNK H 2 8  ? 134.543 184.503 122.804 1.00 48.38 ?  8  UNK J C   1 
ATOM 1347 O O   . UNK H 2 8  ? 134.280 183.301 122.772 1.00 49.71 ?  8  UNK J O   1 
ATOM 1348 C CB  . UNK H 2 8  ? 137.022 184.167 122.806 1.00 45.22 ?  8  UNK J CB  1 
ATOM 1349 N N   . ALA I 1 9  ? 138.966 174.710 124.687 1.00 28.61 ?  1  ALA E N   1 
ATOM 1350 C CA  . ALA I 1 9  ? 139.535 174.007 125.829 1.00 25.85 ?  1  ALA E CA  1 
ATOM 1351 C C   . ALA I 1 9  ? 140.723 174.772 126.402 1.00 26.65 ?  1  ALA E C   1 
ATOM 1352 O O   . ALA I 1 9  ? 140.793 175.012 127.606 1.00 35.46 ?  1  ALA E O   1 
ATOM 1353 C CB  . ALA I 1 9  ? 139.951 172.600 125.434 1.00 30.41 ?  1  ALA E CB  1 
ATOM 1354 N N   . THR I 1 10 ? 141.657 175.152 125.535 1.00 21.88 ?  2  THR E N   1 
ATOM 1355 C CA  . THR I 1 10 ? 142.847 175.885 125.941 1.00 20.68 ?  2  THR E CA  1 
ATOM 1356 C C   . THR I 1 10 ? 143.011 177.132 125.085 1.00 16.28 ?  2  THR E C   1 
ATOM 1357 O O   . THR I 1 10 ? 142.775 177.100 123.874 1.00 24.08 ?  2  THR E O   1 
ATOM 1358 C CB  . THR I 1 10 ? 144.103 175.011 125.846 1.00 23.13 ?  2  THR E CB  1 
ATOM 1359 O OG1 . THR I 1 10 ? 145.270 175.823 126.024 1.00 22.10 ?  2  THR E OG1 1 
ATOM 1360 C CG2 . THR I 1 10 ? 144.171 174.302 124.507 1.00 25.90 ?  2  THR E CG2 1 
ATOM 1361 N N   . LYS I 1 11 ? 143.403 178.231 125.723 1.00 12.40 ?  3  LYS E N   1 
ATOM 1362 C CA  . LYS I 1 11 ? 143.632 179.497 125.043 1.00 11.07 ?  3  LYS E CA  1 
ATOM 1363 C C   . LYS I 1 11 ? 144.987 180.047 125.459 1.00 8.74  ?  3  LYS E C   1 
ATOM 1364 O O   . LYS I 1 11 ? 145.504 179.717 126.529 1.00 13.17 ?  3  LYS E O   1 
ATOM 1365 C CB  . LYS I 1 11 ? 142.537 180.538 125.351 1.00 14.24 ?  3  LYS E CB  1 
ATOM 1366 C CG  . LYS I 1 11 ? 141.136 180.212 124.829 1.00 15.39 ?  3  LYS E CG  1 
ATOM 1367 C CD  . LYS I 1 11 ? 140.423 179.152 125.657 1.00 18.52 ?  3  LYS E CD  1 
ATOM 1368 C CE  . LYS I 1 11 ? 139.099 178.755 125.028 1.00 22.30 ?  3  LYS E CE  1 
ATOM 1369 N NZ  . LYS I 1 11 ? 138.478 177.600 125.731 1.00 19.90 1  3  LYS E NZ  1 
ATOM 1370 N N   . ALA I 1 12 ? 145.561 180.886 124.602 1.00 4.49  ?  4  ALA E N   1 
ATOM 1371 C CA  . ALA I 1 12 ? 146.853 181.500 124.882 1.00 4.08  ?  4  ALA E CA  1 
ATOM 1372 C C   . ALA I 1 12 ? 146.908 182.858 124.202 1.00 3.13  ?  4  ALA E C   1 
ATOM 1373 O O   . ALA I 1 12 ? 146.750 182.946 122.981 1.00 6.26  ?  4  ALA E O   1 
ATOM 1374 C CB  . ALA I 1 12 ? 148.001 180.611 124.402 1.00 6.52  ?  4  ALA E CB  1 
ATOM 1375 N N   . VAL I 1 13 ? 147.131 183.907 124.988 1.00 1.75  ?  5  VAL E N   1 
ATOM 1376 C CA  . VAL I 1 13 ? 147.230 185.269 124.483 1.00 2.31  ?  5  VAL E CA  1 
ATOM 1377 C C   . VAL I 1 13 ? 148.525 185.875 125.002 1.00 2.62  ?  5  VAL E C   1 
ATOM 1378 O O   . VAL I 1 13 ? 148.815 185.793 126.201 1.00 5.53  ?  5  VAL E O   1 
ATOM 1379 C CB  . VAL I 1 13 ? 146.023 186.128 124.905 1.00 2.59  ?  5  VAL E CB  1 
ATOM 1380 C CG1 . VAL I 1 13 ? 146.206 187.569 124.453 1.00 2.08  ?  5  VAL E CG1 1 
ATOM 1381 C CG2 . VAL I 1 13 ? 144.735 185.547 124.346 1.00 2.27  ?  5  VAL E CG2 1 
ATOM 1382 N N   . ALA I 1 14 ? 149.301 186.476 124.106 1.00 2.76  ?  6  ALA E N   1 
ATOM 1383 C CA  . ALA I 1 14 ? 150.556 187.126 124.461 1.00 4.23  ?  6  ALA E CA  1 
ATOM 1384 C C   . ALA I 1 14 ? 150.542 188.550 123.930 1.00 4.41  ?  6  ALA E C   1 
ATOM 1385 O O   . ALA I 1 14 ? 150.325 188.767 122.733 1.00 9.14  ?  6  ALA E O   1 
ATOM 1386 C CB  . ALA I 1 14 ? 151.752 186.355 123.903 1.00 5.34  ?  6  ALA E CB  1 
ATOM 1387 N N   . VAL I 1 15 ? 150.776 189.515 124.816 1.00 3.00  ?  7  VAL E N   1 
ATOM 1388 C CA  . VAL I 1 15 ? 150.792 190.928 124.461 1.00 5.44  ?  7  VAL E CA  1 
ATOM 1389 C C   . VAL I 1 15 ? 152.048 191.558 125.046 1.00 6.79  ?  7  VAL E C   1 
ATOM 1390 O O   . VAL I 1 15 ? 152.344 191.376 126.232 1.00 12.06 ?  7  VAL E O   1 
ATOM 1391 C CB  . VAL I 1 15 ? 149.533 191.659 124.967 1.00 7.38  ?  7  VAL E CB  1 
ATOM 1392 C CG1 . VAL I 1 15 ? 149.723 193.166 124.897 1.00 6.30  ?  7  VAL E CG1 1 
ATOM 1393 C CG2 . VAL I 1 15 ? 148.316 191.234 124.162 1.00 5.02  ?  7  VAL E CG2 1 
ATOM 1394 N N   . LEU I 1 16 ? 152.785 192.291 124.215 1.00 7.33  ?  8  LEU E N   1 
ATOM 1395 C CA  . LEU I 1 16 ? 153.961 193.023 124.660 1.00 9.02  ?  8  LEU E CA  1 
ATOM 1396 C C   . LEU I 1 16 ? 153.974 194.383 123.981 1.00 13.78 ?  8  LEU E C   1 
ATOM 1397 O O   . LEU I 1 16 ? 153.741 194.478 122.773 1.00 25.23 ?  8  LEU E O   1 
ATOM 1398 C CB  . LEU I 1 16 ? 155.248 192.250 124.347 1.00 11.16 ?  8  LEU E CB  1 
ATOM 1399 C CG  . LEU I 1 16 ? 156.577 193.010 124.402 1.00 14.67 ?  8  LEU E CG  1 
ATOM 1400 C CD1 . LEU I 1 16 ? 156.792 193.674 125.746 1.00 20.42 ?  8  LEU E CD1 1 
ATOM 1401 C CD2 . LEU I 1 16 ? 157.733 192.080 124.081 1.00 17.98 ?  8  LEU E CD2 1 
ATOM 1402 N N   . LYS I 1 17 ? 154.245 195.430 124.759 1.00 11.41 ?  9  LYS E N   1 
ATOM 1403 C CA  . LYS I 1 17 ? 154.272 196.792 124.242 1.00 13.56 ?  9  LYS E CA  1 
ATOM 1404 C C   . LYS I 1 17 ? 155.616 197.424 124.595 1.00 15.29 ?  9  LYS E C   1 
ATOM 1405 O O   . LYS I 1 17 ? 155.677 198.545 125.108 1.00 16.23 ?  9  LYS E O   1 
ATOM 1406 C CB  . LYS I 1 17 ? 153.098 197.600 124.807 1.00 13.71 ?  9  LYS E CB  1 
ATOM 1407 C CG  . LYS I 1 17 ? 152.867 198.960 124.156 1.00 14.94 ?  9  LYS E CG  1 
ATOM 1408 C CD  . LYS I 1 17 ? 151.977 199.836 125.023 1.00 14.57 ?  9  LYS E CD  1 
ATOM 1409 C CE  . LYS I 1 17 ? 150.563 199.285 125.096 1.00 16.26 ?  9  LYS E CE  1 
ATOM 1410 N NZ  . LYS I 1 17 ? 149.576 200.335 125.470 1.00 15.38 1  9  LYS E NZ  1 
ATOM 1411 N N   . GLY I 1 18 ? 156.696 196.702 124.337 1.00 16.28 ?  10 GLY E N   1 
ATOM 1412 C CA  . GLY I 1 18 ? 158.020 197.151 124.725 1.00 20.25 ?  10 GLY E CA  1 
ATOM 1413 C C   . GLY I 1 18 ? 158.993 197.129 123.569 1.00 26.23 ?  10 GLY E C   1 
ATOM 1414 O O   . GLY I 1 18 ? 158.915 196.276 122.684 1.00 26.39 ?  10 GLY E O   1 
ATOM 1415 N N   . ASP I 1 19 ? 159.928 198.081 123.594 1.00 32.75 ?  11 ASP E N   1 
ATOM 1416 C CA  . ASP I 1 19 ? 160.952 198.189 122.563 1.00 34.06 ?  11 ASP E CA  1 
ATOM 1417 C C   . ASP I 1 19 ? 161.926 197.015 122.601 1.00 34.38 ?  11 ASP E C   1 
ATOM 1418 O O   . ASP I 1 19 ? 162.623 196.769 121.614 1.00 31.97 ?  11 ASP E O   1 
ATOM 1419 C CB  . ASP I 1 19 ? 161.693 199.522 122.736 1.00 37.30 ?  11 ASP E CB  1 
ATOM 1420 C CG  . ASP I 1 19 ? 162.450 199.964 121.486 1.00 41.59 ?  11 ASP E CG  1 
ATOM 1421 O OD1 . ASP I 1 19 ? 163.036 199.128 120.774 1.00 43.60 -1 11 ASP E OD1 1 
ATOM 1422 O OD2 . ASP I 1 19 ? 162.462 201.185 121.219 1.00 45.72 ?  11 ASP E OD2 1 
ATOM 1423 N N   . GLY I 1 20 ? 161.980 196.279 123.708 1.00 35.94 ?  12 GLY E N   1 
ATOM 1424 C CA  . GLY I 1 20 ? 162.892 195.170 123.846 1.00 34.39 ?  12 GLY E CA  1 
ATOM 1425 C C   . GLY I 1 20 ? 162.664 194.063 122.838 1.00 29.47 ?  12 GLY E C   1 
ATOM 1426 O O   . GLY I 1 20 ? 161.528 193.712 122.506 1.00 28.48 ?  12 GLY E O   1 
ATOM 1427 N N   . PRO I 1 21 ? 163.754 193.498 122.324 1.00 26.81 ?  13 PRO E N   1 
ATOM 1428 C CA  . PRO I 1 21 ? 163.632 192.374 121.391 1.00 26.71 ?  13 PRO E CA  1 
ATOM 1429 C C   . PRO I 1 21 ? 163.042 191.146 122.066 1.00 25.45 ?  13 PRO E C   1 
ATOM 1430 O O   . PRO I 1 21 ? 163.209 190.924 123.267 1.00 33.91 ?  13 PRO E O   1 
ATOM 1431 C CB  . PRO I 1 21 ? 165.079 192.120 120.948 1.00 25.06 ?  13 PRO E CB  1 
ATOM 1432 C CG  . PRO I 1 21 ? 165.811 193.386 121.267 1.00 25.84 ?  13 PRO E CG  1 
ATOM 1433 C CD  . PRO I 1 21 ? 165.150 193.931 122.491 1.00 27.75 ?  13 PRO E CD  1 
ATOM 1434 N N   . VAL I 1 22 ? 162.342 190.343 121.271 1.00 20.80 ?  14 VAL E N   1 
ATOM 1435 C CA  . VAL I 1 22 ? 161.770 189.084 121.729 1.00 18.20 ?  14 VAL E CA  1 
ATOM 1436 C C   . VAL I 1 22 ? 162.703 187.957 121.316 1.00 23.47 ?  14 VAL E C   1 
ATOM 1437 O O   . VAL I 1 22 ? 163.089 187.858 120.144 1.00 33.83 ?  14 VAL E O   1 
ATOM 1438 C CB  . VAL I 1 22 ? 160.360 188.872 121.155 1.00 17.86 ?  14 VAL E CB  1 
ATOM 1439 C CG1 . VAL I 1 22 ? 159.988 187.401 121.190 1.00 15.32 ?  14 VAL E CG1 1 
ATOM 1440 C CG2 . VAL I 1 22 ? 159.350 189.695 121.926 1.00 22.05 ?  14 VAL E CG2 1 
ATOM 1441 N N   . GLN I 1 23 ? 163.069 187.108 122.273 1.00 22.36 ?  15 GLN E N   1 
ATOM 1442 C CA  . GLN I 1 23 ? 163.997 186.007 122.034 1.00 20.30 ?  15 GLN E CA  1 
ATOM 1443 C C   . GLN I 1 23 ? 163.408 184.739 122.635 1.00 19.11 ?  15 GLN E C   1 
ATOM 1444 O O   . GLN I 1 23 ? 163.253 184.641 123.856 1.00 27.36 ?  15 GLN E O   1 
ATOM 1445 C CB  . GLN I 1 23 ? 165.369 186.312 122.634 1.00 18.87 ?  15 GLN E CB  1 
ATOM 1446 C CG  . GLN I 1 23 ? 166.513 185.571 121.977 1.00 17.91 ?  15 GLN E CG  1 
ATOM 1447 C CD  . GLN I 1 23 ? 167.765 186.415 121.879 1.00 21.22 ?  15 GLN E CD  1 
ATOM 1448 O OE1 . GLN I 1 23 ? 168.499 186.574 122.854 1.00 15.30 ?  15 GLN E OE1 1 
ATOM 1449 N NE2 . GLN I 1 23 ? 168.014 186.967 120.698 1.00 24.15 ?  15 GLN E NE2 1 
ATOM 1450 N N   . GLY I 1 24 ? 163.083 183.771 121.782 1.00 12.80 ?  16 GLY E N   1 
ATOM 1451 C CA  . GLY I 1 24 ? 162.527 182.515 122.244 1.00 7.81  ?  16 GLY E CA  1 
ATOM 1452 C C   . GLY I 1 24 ? 161.255 182.124 121.522 1.00 4.63  ?  16 GLY E C   1 
ATOM 1453 O O   . GLY I 1 24 ? 161.024 182.552 120.389 1.00 5.60  ?  16 GLY E O   1 
ATOM 1454 N N   . ILE I 1 25 ? 160.425 181.313 122.163 1.00 3.20  ?  17 ILE E N   1 
ATOM 1455 C CA  . ILE I 1 25 ? 159.160 180.883 121.583 1.00 2.97  ?  17 ILE E CA  1 
ATOM 1456 C C   . ILE I 1 25 ? 158.018 181.585 122.300 1.00 4.18  ?  17 ILE E C   1 
ATOM 1457 O O   . ILE I 1 25 ? 158.090 181.874 123.499 1.00 20.36 ?  17 ILE E O   1 
ATOM 1458 C CB  . ILE I 1 25 ? 158.998 179.352 121.657 1.00 2.76  ?  17 ILE E CB  1 
ATOM 1459 C CG1 . ILE I 1 25 ? 160.353 178.664 121.519 1.00 3.84  ?  17 ILE E CG1 1 
ATOM 1460 C CG2 . ILE I 1 25 ? 158.048 178.866 120.580 1.00 3.86  ?  17 ILE E CG2 1 
ATOM 1461 C CD1 . ILE I 1 25 ? 160.299 177.183 121.788 1.00 2.74  ?  17 ILE E CD1 1 
ATOM 1462 N N   . ILE I 1 26 ? 156.952 181.866 121.556 1.00 2.67  ?  18 ILE E N   1 
ATOM 1463 C CA  . ILE I 1 26 ? 155.755 182.504 122.087 1.00 1.40  ?  18 ILE E CA  1 
ATOM 1464 C C   . ILE I 1 26 ? 154.572 181.581 121.834 1.00 1.52  ?  18 ILE E C   1 
ATOM 1465 O O   . ILE I 1 26 ? 154.382 181.105 120.709 1.00 2.00  ?  18 ILE E O   1 
ATOM 1466 C CB  . ILE I 1 26 ? 155.515 183.885 121.452 1.00 1.45  ?  18 ILE E CB  1 
ATOM 1467 C CG1 . ILE I 1 26 ? 156.843 184.608 121.226 1.00 1.29  ?  18 ILE E CG1 1 
ATOM 1468 C CG2 . ILE I 1 26 ? 154.600 184.716 122.326 1.00 2.28  ?  18 ILE E CG2 1 
ATOM 1469 C CD1 . ILE I 1 26 ? 157.511 185.068 122.491 1.00 1.32  ?  18 ILE E CD1 1 
ATOM 1470 N N   . ASN I 1 27 ? 153.782 181.335 122.878 1.00 1.62  ?  19 ASN E N   1 
ATOM 1471 C CA  . ASN I 1 27 ? 152.603 180.471 122.796 1.00 2.03  ?  19 ASN E CA  1 
ATOM 1472 C C   . ASN I 1 27 ? 152.970 179.070 122.311 1.00 1.29  ?  19 ASN E C   1 
ATOM 1473 O O   . ASN I 1 27 ? 152.282 178.480 121.478 1.00 2.24  ?  19 ASN E O   1 
ATOM 1474 C CB  . ASN I 1 27 ? 151.524 181.090 121.906 1.00 2.07  ?  19 ASN E CB  1 
ATOM 1475 C CG  . ASN I 1 27 ? 151.198 182.517 122.295 1.00 3.34  ?  19 ASN E CG  1 
ATOM 1476 O OD1 . ASN I 1 27 ? 150.954 182.814 123.464 1.00 3.83  ?  19 ASN E OD1 1 
ATOM 1477 N ND2 . ASN I 1 27 ? 151.195 183.410 121.313 1.00 4.34  ?  19 ASN E ND2 1 
ATOM 1478 N N   . PHE I 1 28 ? 154.068 178.538 122.837 1.00 1.33  ?  20 PHE E N   1 
ATOM 1479 C CA  . PHE I 1 28 ? 154.480 177.175 122.535 1.00 1.50  ?  20 PHE E CA  1 
ATOM 1480 C C   . PHE I 1 28 ? 153.588 176.195 123.288 1.00 2.68  ?  20 PHE E C   1 
ATOM 1481 O O   . PHE I 1 28 ? 153.451 176.282 124.511 1.00 9.02  ?  20 PHE E O   1 
ATOM 1482 C CB  . PHE I 1 28 ? 155.947 176.983 122.916 1.00 2.39  ?  20 PHE E CB  1 
ATOM 1483 C CG  . PHE I 1 28 ? 156.526 175.666 122.492 1.00 1.78  ?  20 PHE E CG  1 
ATOM 1484 C CD1 . PHE I 1 28 ? 155.933 174.912 121.497 1.00 2.68  ?  20 PHE E CD1 1 
ATOM 1485 C CD2 . PHE I 1 28 ? 157.677 175.189 123.087 1.00 2.10  ?  20 PHE E CD2 1 
ATOM 1486 C CE1 . PHE I 1 28 ? 156.471 173.703 121.118 1.00 3.16  ?  20 PHE E CE1 1 
ATOM 1487 C CE2 . PHE I 1 28 ? 158.218 173.984 122.709 1.00 2.00  ?  20 PHE E CE2 1 
ATOM 1488 C CZ  . PHE I 1 28 ? 157.617 173.242 121.722 1.00 2.66  ?  20 PHE E CZ  1 
ATOM 1489 N N   . GLU I 1 29 ? 152.981 175.262 122.557 1.00 1.15  ?  21 GLU E N   1 
ATOM 1490 C CA  . GLU I 1 29 ? 151.982 174.352 123.108 1.00 1.57  ?  21 GLU E CA  1 
ATOM 1491 C C   . GLU I 1 29 ? 152.306 172.908 122.750 1.00 1.73  ?  21 GLU E C   1 
ATOM 1492 O O   . GLU I 1 29 ? 151.456 172.161 122.261 1.00 1.58  ?  21 GLU E O   1 
ATOM 1493 C CB  . GLU I 1 29 ? 150.582 174.717 122.622 1.00 1.06  ?  21 GLU E CB  1 
ATOM 1494 C CG  . GLU I 1 29 ? 150.313 176.211 122.562 1.00 1.10  ?  21 GLU E CG  1 
ATOM 1495 C CD  . GLU I 1 29 ? 148.837 176.538 122.517 1.00 1.23  ?  21 GLU E CD  1 
ATOM 1496 O OE1 . GLU I 1 29 ? 148.018 175.597 122.475 1.00 1.37  ?  21 GLU E OE1 1 
ATOM 1497 O OE2 . GLU I 1 29 ? 148.497 177.739 122.524 1.00 1.43  -1 21 GLU E OE2 1 
ATOM 1498 N N   . GLN I 1 30 ? 153.552 172.499 122.985 1.00 1.74  ?  22 GLN E N   1 
ATOM 1499 C CA  . GLN I 1 30 ? 153.939 171.110 122.766 1.00 1.55  ?  22 GLN E CA  1 
ATOM 1500 C C   . GLN I 1 30 ? 153.074 170.182 123.610 1.00 2.07  ?  22 GLN E C   1 
ATOM 1501 O O   . GLN I 1 30 ? 152.873 170.418 124.803 1.00 7.82  ?  22 GLN E O   1 
ATOM 1502 C CB  . GLN I 1 30 ? 155.417 170.917 123.106 1.00 1.81  ?  22 GLN E CB  1 
ATOM 1503 C CG  . GLN I 1 30 ? 155.788 169.490 123.455 1.00 2.66  ?  22 GLN E CG  1 
ATOM 1504 C CD  . GLN I 1 30 ? 157.287 169.254 123.466 1.00 2.57  ?  22 GLN E CD  1 
ATOM 1505 O OE1 . GLN I 1 30 ? 157.959 169.422 122.451 1.00 2.36  ?  22 GLN E OE1 1 
ATOM 1506 N NE2 . GLN I 1 30 ? 157.815 168.854 124.616 1.00 2.89  ?  22 GLN E NE2 1 
ATOM 1507 N N   . LYS I 1 31 ? 152.556 169.125 122.988 1.00 1.87  ?  23 LYS E N   1 
ATOM 1508 C CA  . LYS I 1 31 ? 151.574 168.279 123.652 1.00 1.92  ?  23 LYS E CA  1 
ATOM 1509 C C   . LYS I 1 31 ? 151.687 166.845 123.162 1.00 3.06  ?  23 LYS E C   1 
ATOM 1510 O O   . LYS I 1 31 ? 151.721 166.601 121.952 1.00 5.25  ?  23 LYS E O   1 
ATOM 1511 C CB  . LYS I 1 31 ? 150.156 168.811 123.411 1.00 1.73  ?  23 LYS E CB  1 
ATOM 1512 C CG  . LYS I 1 31 ? 149.059 167.773 123.558 1.00 1.66  ?  23 LYS E CG  1 
ATOM 1513 C CD  . LYS I 1 31 ? 147.683 168.416 123.651 1.00 2.02  ?  23 LYS E CD  1 
ATOM 1514 C CE  . LYS I 1 31 ? 147.608 169.709 122.855 1.00 2.93  ?  23 LYS E CE  1 
ATOM 1515 N NZ  . LYS I 1 31 ? 146.328 170.431 123.090 1.00 4.12  1  23 LYS E NZ  1 
ATOM 1516 N N   . GLU I 1 32 ? 151.735 165.907 124.110 1.00 4.10  ?  24 GLU E N   1 
ATOM 1517 C CA  . GLU I 1 32 ? 151.734 164.472 123.822 1.00 5.39  ?  24 GLU E CA  1 
ATOM 1518 C C   . GLU I 1 32 ? 152.849 164.091 122.853 1.00 7.25  ?  24 GLU E C   1 
ATOM 1519 O O   . GLU I 1 32 ? 152.658 163.296 121.931 1.00 9.80  ?  24 GLU E O   1 
ATOM 1520 C CB  . GLU I 1 32 ? 150.374 164.022 123.288 1.00 3.63  ?  24 GLU E CB  1 
ATOM 1521 C CG  . GLU I 1 32 ? 149.227 164.250 124.253 1.00 4.42  ?  24 GLU E CG  1 
ATOM 1522 C CD  . GLU I 1 32 ? 147.877 163.932 123.644 1.00 4.91  ?  24 GLU E CD  1 
ATOM 1523 O OE1 . GLU I 1 32 ? 147.658 162.764 123.262 1.00 6.01  ?  24 GLU E OE1 1 
ATOM 1524 O OE2 . GLU I 1 32 ? 147.036 164.850 123.547 1.00 3.74  -1 24 GLU E OE2 1 
ATOM 1525 N N   . SER I 1 33 ? 154.029 164.658 123.069 1.00 6.77  ?  25 SER E N   1 
ATOM 1526 C CA  . SER I 1 33 ? 155.165 164.437 122.189 1.00 10.76 ?  25 SER E CA  1 
ATOM 1527 C C   . SER I 1 33 ? 156.341 163.882 122.990 1.00 15.28 ?  25 SER E C   1 
ATOM 1528 O O   . SER I 1 33 ? 156.216 163.540 124.169 1.00 20.99 ?  25 SER E O   1 
ATOM 1529 C CB  . SER I 1 33 ? 155.548 165.731 121.471 1.00 11.58 ?  25 SER E CB  1 
ATOM 1530 O OG  . SER I 1 33 ? 156.167 166.628 122.371 1.00 6.84  ?  25 SER E OG  1 
ATOM 1531 N N   . ASN I 1 34 ? 157.492 163.785 122.328 1.00 13.65 ?  26 ASN E N   1 
ATOM 1532 C CA  . ASN I 1 34 ? 158.725 163.331 122.968 1.00 14.20 ?  26 ASN E CA  1 
ATOM 1533 C C   . ASN I 1 34 ? 159.880 164.038 122.266 1.00 14.73 ?  26 ASN E C   1 
ATOM 1534 O O   . ASN I 1 34 ? 160.284 163.635 121.172 1.00 20.09 ?  26 ASN E O   1 
ATOM 1535 C CB  . ASN I 1 34 ? 158.865 161.818 122.893 1.00 20.75 ?  26 ASN E CB  1 
ATOM 1536 C CG  . ASN I 1 34 ? 160.249 161.343 123.279 1.00 23.14 ?  26 ASN E CG  1 
ATOM 1537 O OD1 . ASN I 1 34 ? 160.944 160.712 122.485 1.00 26.41 ?  26 ASN E OD1 1 
ATOM 1538 N ND2 . ASN I 1 34 ? 160.658 161.647 124.505 1.00 21.92 ?  26 ASN E ND2 1 
ATOM 1539 N N   . GLY I 1 35 ? 160.396 165.090 122.892 1.00 9.69  ?  27 GLY E N   1 
ATOM 1540 C CA  . GLY I 1 35 ? 161.478 165.849 122.317 1.00 6.74  ?  27 GLY E CA  1 
ATOM 1541 C C   . GLY I 1 35 ? 162.071 166.845 123.289 1.00 2.59  ?  27 GLY E C   1 
ATOM 1542 O O   . GLY I 1 35 ? 161.362 167.618 123.939 1.00 2.30  ?  27 GLY E O   1 
ATOM 1543 N N   . PRO I 1 36 ? 163.394 166.843 123.406 1.00 2.08  ?  28 PRO E N   1 
ATOM 1544 C CA  . PRO I 1 36 ? 164.087 167.815 124.274 1.00 2.22  ?  28 PRO E CA  1 
ATOM 1545 C C   . PRO I 1 36 ? 164.166 169.204 123.645 1.00 1.46  ?  28 PRO E C   1 
ATOM 1546 O O   . PRO I 1 36 ? 165.156 169.609 123.037 1.00 1.56  ?  28 PRO E O   1 
ATOM 1547 C CB  . PRO I 1 36 ? 165.469 167.184 124.449 1.00 3.18  ?  28 PRO E CB  1 
ATOM 1548 C CG  . PRO I 1 36 ? 165.672 166.373 123.223 1.00 2.60  ?  28 PRO E CG  1 
ATOM 1549 C CD  . PRO I 1 36 ? 164.322 165.869 122.807 1.00 3.15  ?  28 PRO E CD  1 
ATOM 1550 N N   . VAL I 1 37 ? 163.077 169.962 123.791 1.00 1.09  ?  29 VAL E N   1 
ATOM 1551 C CA  . VAL I 1 37 ? 163.045 171.323 123.273 1.00 1.31  ?  29 VAL E CA  1 
ATOM 1552 C C   . VAL I 1 37 ? 164.076 172.179 123.994 1.00 1.06  ?  29 VAL E C   1 
ATOM 1553 O O   . VAL I 1 37 ? 164.137 172.211 125.228 1.00 2.25  ?  29 VAL E O   1 
ATOM 1554 C CB  . VAL I 1 37 ? 161.628 171.906 123.385 1.00 1.17  ?  29 VAL E CB  1 
ATOM 1555 C CG1 . VAL I 1 37 ? 161.090 171.744 124.777 1.00 1.83  ?  29 VAL E CG1 1 
ATOM 1556 C CG2 . VAL I 1 37 ? 161.646 173.381 123.019 1.00 1.49  ?  29 VAL E CG2 1 
ATOM 1557 N N   . LYS I 1 38 ? 164.908 172.865 123.216 1.00 0.86  ?  30 LYS E N   1 
ATOM 1558 C CA  . LYS I 1 38 ? 165.973 173.708 123.739 1.00 1.06  ?  30 LYS E CA  1 
ATOM 1559 C C   . LYS I 1 38 ? 165.858 175.094 123.123 1.00 1.21  ?  30 LYS E C   1 
ATOM 1560 O O   . LYS I 1 38 ? 165.726 175.225 121.903 1.00 3.08  ?  30 LYS E O   1 
ATOM 1561 C CB  . LYS I 1 38 ? 167.346 173.101 123.440 1.00 1.14  ?  30 LYS E CB  1 
ATOM 1562 C CG  . LYS I 1 38 ? 168.521 173.976 123.838 1.00 1.32  ?  30 LYS E CG  1 
ATOM 1563 C CD  . LYS I 1 38 ? 169.840 173.318 123.471 1.00 1.00  ?  30 LYS E CD  1 
ATOM 1564 C CE  . LYS I 1 38 ? 171.020 174.213 123.811 1.00 1.14  ?  30 LYS E CE  1 
ATOM 1565 N NZ  . LYS I 1 38 ? 172.321 173.565 123.485 1.00 0.73  1  30 LYS E NZ  1 
ATOM 1566 N N   . VAL I 1 39 ? 165.905 176.121 123.964 1.00 0.91  ?  31 VAL E N   1 
ATOM 1567 C CA  . VAL I 1 39 ? 165.823 177.507 123.522 1.00 1.50  ?  31 VAL E CA  1 
ATOM 1568 C C   . VAL I 1 39 ? 167.086 178.222 123.974 1.00 2.30  ?  31 VAL E C   1 
ATOM 1569 O O   . VAL I 1 39 ? 167.416 178.215 125.166 1.00 4.40  ?  31 VAL E O   1 
ATOM 1570 C CB  . VAL I 1 39 ? 164.572 178.211 124.071 1.00 2.29  ?  31 VAL E CB  1 
ATOM 1571 C CG1 . VAL I 1 39 ? 164.499 179.638 123.553 1.00 2.31  ?  31 VAL E CG1 1 
ATOM 1572 C CG2 . VAL I 1 39 ? 163.325 177.437 123.695 1.00 1.58  ?  31 VAL E CG2 1 
ATOM 1573 N N   . TRP I 1 40 ? 167.785 178.839 123.028 1.00 2.21  ?  32 TRP E N   1 
ATOM 1574 C CA  . TRP I 1 40 ? 169.014 179.571 123.303 1.00 2.99  ?  32 TRP E CA  1 
ATOM 1575 C C   . TRP I 1 40 ? 168.807 181.024 122.907 1.00 3.21  ?  32 TRP E C   1 
ATOM 1576 O O   . TRP I 1 40 ? 168.459 181.314 121.758 1.00 5.23  ?  32 TRP E O   1 
ATOM 1577 C CB  . TRP I 1 40 ? 170.194 178.957 122.546 1.00 4.17  ?  32 TRP E CB  1 
ATOM 1578 C CG  . TRP I 1 40 ? 171.541 179.437 122.999 1.00 3.61  ?  32 TRP E CG  1 
ATOM 1579 C CD1 . TRP I 1 40 ? 171.964 180.730 123.094 1.00 4.41  ?  32 TRP E CD1 1 
ATOM 1580 C CD2 . TRP I 1 40 ? 172.643 178.624 123.414 1.00 3.72  ?  32 TRP E CD2 1 
ATOM 1581 N NE1 . TRP I 1 40 ? 173.260 180.773 123.544 1.00 3.94  ?  32 TRP E NE1 1 
ATOM 1582 C CE2 . TRP I 1 40 ? 173.701 179.492 123.748 1.00 4.98  ?  32 TRP E CE2 1 
ATOM 1583 C CE3 . TRP I 1 40 ? 172.839 177.245 123.537 1.00 3.71  ?  32 TRP E CE3 1 
ATOM 1584 C CZ2 . TRP I 1 40 ? 174.935 179.028 124.196 1.00 6.31  ?  32 TRP E CZ2 1 
ATOM 1585 C CZ3 . TRP I 1 40 ? 174.065 176.785 123.982 1.00 4.28  ?  32 TRP E CZ3 1 
ATOM 1586 C CH2 . TRP I 1 40 ? 175.097 177.674 124.306 1.00 5.60  ?  32 TRP E CH2 1 
ATOM 1587 N N   . GLY I 1 41 ? 169.020 181.931 123.855 1.00 3.12  ?  33 GLY E N   1 
ATOM 1588 C CA  . GLY I 1 41 ? 168.861 183.345 123.586 1.00 7.91  ?  33 GLY E CA  1 
ATOM 1589 C C   . GLY I 1 41 ? 170.045 184.172 124.039 1.00 9.98  ?  33 GLY E C   1 
ATOM 1590 O O   . GLY I 1 41 ? 170.364 184.212 125.230 1.00 15.16 ?  33 GLY E O   1 
ATOM 1591 N N   . SER I 1 42 ? 170.704 184.839 123.096 1.00 7.03  ?  34 SER E N   1 
ATOM 1592 C CA  . SER I 1 42 ? 171.869 185.660 123.387 1.00 9.59  ?  34 SER E CA  1 
ATOM 1593 C C   . SER I 1 42 ? 171.687 187.029 122.753 1.00 12.86 ?  34 SER E C   1 
ATOM 1594 O O   . SER I 1 42 ? 171.185 187.133 121.630 1.00 22.86 ?  34 SER E O   1 
ATOM 1595 C CB  . SER I 1 42 ? 173.154 185.003 122.871 1.00 10.24 ?  34 SER E CB  1 
ATOM 1596 O OG  . SER I 1 42 ? 174.280 185.826 123.116 1.00 10.90 ?  34 SER E OG  1 
ATOM 1597 N N   . ILE I 1 43 ? 172.085 188.073 123.476 1.00 8.73  ?  35 ILE E N   1 
ATOM 1598 C CA  . ILE I 1 43 ? 172.044 189.442 122.974 1.00 12.07 ?  35 ILE E CA  1 
ATOM 1599 C C   . ILE I 1 43 ? 173.195 190.214 123.603 1.00 13.05 ?  35 ILE E C   1 
ATOM 1600 O O   . ILE I 1 43 ? 173.259 190.352 124.829 1.00 18.89 ?  35 ILE E O   1 
ATOM 1601 C CB  . ILE I 1 43 ? 170.697 190.130 123.267 1.00 13.89 ?  35 ILE E CB  1 
ATOM 1602 C CG1 . ILE I 1 43 ? 170.815 191.647 123.104 1.00 16.89 ?  35 ILE E CG1 1 
ATOM 1603 C CG2 . ILE I 1 43 ? 170.174 189.743 124.639 1.00 19.63 ?  35 ILE E CG2 1 
ATOM 1604 C CD1 . ILE I 1 43 ? 169.484 192.364 123.108 1.00 19.55 ?  35 ILE E CD1 1 
ATOM 1605 N N   . LYS I 1 44 ? 174.110 190.708 122.769 1.00 13.71 ?  36 LYS E N   1 
ATOM 1606 C CA  . LYS I 1 44 ? 175.275 191.449 123.241 1.00 19.51 ?  36 LYS E CA  1 
ATOM 1607 C C   . LYS I 1 44 ? 175.293 192.834 122.606 1.00 24.14 ?  36 LYS E C   1 
ATOM 1608 O O   . LYS I 1 44 ? 175.931 193.043 121.569 1.00 35.30 ?  36 LYS E O   1 
ATOM 1609 C CB  . LYS I 1 44 ? 176.567 190.688 122.939 1.00 19.26 ?  36 LYS E CB  1 
ATOM 1610 C CG  . LYS I 1 44 ? 176.592 189.274 123.500 1.00 15.07 ?  36 LYS E CG  1 
ATOM 1611 C CD  . LYS I 1 44 ? 177.712 188.447 122.892 1.00 15.29 ?  36 LYS E CD  1 
ATOM 1612 C CE  . LYS I 1 44 ? 179.065 188.851 123.453 1.00 19.88 ?  36 LYS E CE  1 
ATOM 1613 N NZ  . LYS I 1 44 ? 180.068 187.759 123.308 1.00 20.42 1  36 LYS E NZ  1 
ATOM 1614 N N   . GLY I 1 45 ? 174.599 193.779 123.236 1.00 22.39 ?  37 GLY E N   1 
ATOM 1615 C CA  . GLY I 1 45 ? 174.577 195.152 122.777 1.00 34.53 ?  37 GLY E CA  1 
ATOM 1616 C C   . GLY I 1 45 ? 173.852 196.035 123.771 1.00 50.93 ?  37 GLY E C   1 
ATOM 1617 O O   . GLY I 1 45 ? 173.551 195.612 124.889 1.00 60.96 ?  37 GLY E O   1 
ATOM 1618 N N   . LEU I 1 46 ? 173.550 197.264 123.361 1.00 55.90 ?  38 LEU E N   1 
ATOM 1619 C CA  . LEU I 1 46 ? 172.916 198.219 124.259 1.00 62.17 ?  38 LEU E CA  1 
ATOM 1620 C C   . LEU I 1 46 ? 171.646 198.782 123.640 1.00 63.02 ?  38 LEU E C   1 
ATOM 1621 O O   . LEU I 1 46 ? 171.563 198.994 122.429 1.00 68.61 ?  38 LEU E O   1 
ATOM 1622 C CB  . LEU I 1 46 ? 173.864 199.364 124.649 1.00 66.59 ?  38 LEU E CB  1 
ATOM 1623 C CG  . LEU I 1 46 ? 174.323 200.449 123.674 1.00 64.08 ?  38 LEU E CG  1 
ATOM 1624 C CD1 . LEU I 1 46 ? 175.093 201.514 124.417 1.00 67.23 ?  38 LEU E CD1 1 
ATOM 1625 C CD2 . LEU I 1 46 ? 175.254 199.836 122.657 1.00 56.33 ?  38 LEU E CD2 1 
ATOM 1626 N N   . THR I 1 47 ? 170.659 199.027 124.498 1.00 61.74 ?  39 THR E N   1 
ATOM 1627 C CA  . THR I 1 47 ? 169.377 199.588 124.104 1.00 64.45 ?  39 THR E CA  1 
ATOM 1628 C C   . THR I 1 47 ? 169.153 200.894 124.856 1.00 65.26 ?  39 THR E C   1 
ATOM 1629 O O   . THR I 1 47 ? 169.755 201.131 125.908 1.00 68.25 ?  39 THR E O   1 
ATOM 1630 C CB  . THR I 1 47 ? 168.237 198.604 124.382 1.00 67.76 ?  39 THR E CB  1 
ATOM 1631 O OG1 . THR I 1 47 ? 168.067 198.452 125.795 1.00 67.28 ?  39 THR E OG1 1 
ATOM 1632 C CG2 . THR I 1 47 ? 168.553 197.245 123.781 1.00 66.15 ?  39 THR E CG2 1 
ATOM 1633 N N   . GLU I 1 48 ? 168.290 201.744 124.308 1.00 66.18 ?  40 GLU E N   1 
ATOM 1634 C CA  . GLU I 1 48 ? 168.000 203.044 124.894 1.00 61.50 ?  40 GLU E CA  1 
ATOM 1635 C C   . GLU I 1 48 ? 166.493 203.240 124.975 1.00 59.06 ?  40 GLU E C   1 
ATOM 1636 O O   . GLU I 1 48 ? 165.716 202.494 124.373 1.00 60.79 ?  40 GLU E O   1 
ATOM 1637 C CB  . GLU I 1 48 ? 168.639 204.175 124.081 1.00 62.11 ?  40 GLU E CB  1 
ATOM 1638 C CG  . GLU I 1 48 ? 170.073 204.497 124.471 1.00 60.56 ?  40 GLU E CG  1 
ATOM 1639 C CD  . GLU I 1 48 ? 171.048 203.417 124.045 1.00 65.93 ?  40 GLU E CD  1 
ATOM 1640 O OE1 . GLU I 1 48 ? 171.037 203.037 122.857 1.00 71.63 ?  40 GLU E OE1 1 
ATOM 1641 O OE2 . GLU I 1 48 ? 171.829 202.947 124.897 1.00 64.65 -1 40 GLU E OE2 1 
ATOM 1642 N N   . GLY I 1 49 ? 166.091 204.253 125.733 1.00 60.96 ?  41 GLY E N   1 
ATOM 1643 C CA  . GLY I 1 49 ? 164.685 204.574 125.895 1.00 63.08 ?  41 GLY E CA  1 
ATOM 1644 C C   . GLY I 1 49 ? 164.309 205.916 125.298 1.00 60.55 ?  41 GLY E C   1 
ATOM 1645 O O   . GLY I 1 49 ? 165.134 206.827 125.229 1.00 62.50 ?  41 GLY E O   1 
ATOM 1646 N N   . UNK J 2 1  ? 145.538 207.466 126.270 1.00 26.05 ?  1  UNK K N   1 
ATOM 1647 C CA  . UNK J 2 1  ? 144.544 206.637 126.940 1.00 26.04 ?  1  UNK K CA  1 
ATOM 1648 C C   . UNK J 2 1  ? 144.673 205.179 126.513 1.00 26.58 ?  1  UNK K C   1 
ATOM 1649 O O   . UNK J 2 1  ? 143.724 204.588 125.999 1.00 29.40 ?  1  UNK K O   1 
ATOM 1650 C CB  . UNK J 2 1  ? 143.142 207.152 126.653 1.00 22.41 ?  1  UNK K CB  1 
ATOM 1651 N N   . UNK J 2 2  ? 145.855 204.607 126.729 1.00 22.86 ?  2  UNK K N   1 
ATOM 1652 C CA  . UNK J 2 2  ? 146.100 203.219 126.362 1.00 22.32 ?  2  UNK K CA  1 
ATOM 1653 C C   . UNK J 2 2  ? 145.269 202.286 127.233 1.00 21.72 ?  2  UNK K C   1 
ATOM 1654 O O   . UNK J 2 2  ? 145.234 202.433 128.458 1.00 26.76 ?  2  UNK K O   1 
ATOM 1655 C CB  . UNK J 2 2  ? 147.586 202.895 126.497 1.00 21.86 ?  2  UNK K CB  1 
ATOM 1656 N N   . UNK J 2 3  ? 144.599 201.326 126.600 1.00 21.09 ?  3  UNK K N   1 
ATOM 1657 C CA  . UNK J 2 3  ? 143.761 200.371 127.309 1.00 25.47 ?  3  UNK K CA  1 
ATOM 1658 C C   . UNK J 2 3  ? 143.866 199.009 126.642 1.00 29.06 ?  3  UNK K C   1 
ATOM 1659 O O   . UNK J 2 3  ? 143.805 198.906 125.414 1.00 38.46 ?  3  UNK K O   1 
ATOM 1660 C CB  . UNK J 2 3  ? 142.299 200.829 127.345 1.00 25.18 ?  3  UNK K CB  1 
ATOM 1661 N N   . UNK J 2 4  ? 144.025 197.968 127.455 1.00 28.04 ?  4  UNK K N   1 
ATOM 1662 C CA  . UNK J 2 4  ? 144.082 196.592 126.979 1.00 31.96 ?  4  UNK K CA  1 
ATOM 1663 C C   . UNK J 2 4  ? 142.912 195.825 127.577 1.00 34.09 ?  4  UNK K C   1 
ATOM 1664 O O   . UNK J 2 4  ? 142.766 195.767 128.802 1.00 39.06 ?  4  UNK K O   1 
ATOM 1665 C CB  . UNK J 2 4  ? 145.410 195.932 127.352 1.00 32.03 ?  4  UNK K CB  1 
ATOM 1666 N N   . UNK J 2 5  ? 142.084 195.239 126.715 1.00 29.75 ?  5  UNK K N   1 
ATOM 1667 C CA  . UNK J 2 5  ? 140.894 194.515 127.142 1.00 30.80 ?  5  UNK K CA  1 
ATOM 1668 C C   . UNK J 2 5  ? 140.898 193.125 126.528 1.00 29.10 ?  5  UNK K C   1 
ATOM 1669 O O   . UNK J 2 5  ? 141.104 192.977 125.319 1.00 33.74 ?  5  UNK K O   1 
ATOM 1670 C CB  . UNK J 2 5  ? 139.619 195.267 126.749 1.00 39.20 ?  5  UNK K CB  1 
ATOM 1671 N N   . UNK J 2 6  ? 140.671 192.113 127.360 1.00 30.19 ?  6  UNK K N   1 
ATOM 1672 C CA  . UNK J 2 6  ? 140.560 190.732 126.912 1.00 38.33 ?  6  UNK K CA  1 
ATOM 1673 C C   . UNK J 2 6  ? 139.338 190.106 127.565 1.00 42.09 ?  6  UNK K C   1 
ATOM 1674 O O   . UNK J 2 6  ? 139.177 190.182 128.787 1.00 49.64 ?  6  UNK K O   1 
ATOM 1675 C CB  . UNK J 2 6  ? 141.820 189.931 127.252 1.00 37.15 ?  6  UNK K CB  1 
ATOM 1676 N N   . UNK J 2 7  ? 138.485 189.488 126.753 1.00 39.87 ?  7  UNK K N   1 
ATOM 1677 C CA  . UNK J 2 7  ? 137.253 188.884 127.232 1.00 42.13 ?  7  UNK K CA  1 
ATOM 1678 C C   . UNK J 2 7  ? 137.148 187.456 126.718 1.00 45.23 ?  7  UNK K C   1 
ATOM 1679 O O   . UNK J 2 7  ? 137.751 187.092 125.706 1.00 56.63 ?  7  UNK K O   1 
ATOM 1680 C CB  . UNK J 2 7  ? 136.022 189.692 126.798 1.00 38.50 ?  7  UNK K CB  1 
ATOM 1681 N N   . UNK J 2 8  ? 136.372 186.649 127.434 1.00 41.67 ?  8  UNK K N   1 
ATOM 1682 C CA  . UNK J 2 8  ? 136.165 185.255 127.061 1.00 47.40 ?  8  UNK K CA  1 
ATOM 1683 C C   . UNK J 2 8  ? 134.825 184.746 127.581 1.00 48.38 ?  8  UNK K C   1 
ATOM 1684 O O   . UNK J 2 8  ? 134.551 183.546 127.551 1.00 49.71 ?  8  UNK K O   1 
ATOM 1685 C CB  . UNK J 2 8  ? 137.301 184.390 127.584 1.00 45.22 ?  8  UNK K CB  1 
ATOM 1686 N N   . ALA K 1 9  ? 139.122 175.141 129.544 1.00 28.61 ?  1  ALA F N   1 
ATOM 1687 C CA  . ALA K 1 9  ? 139.684 174.427 130.683 1.00 25.85 ?  1  ALA F CA  1 
ATOM 1688 C C   . ALA K 1 9  ? 140.888 175.168 131.251 1.00 26.65 ?  1  ALA F C   1 
ATOM 1689 O O   . ALA K 1 9  ? 140.967 175.405 132.455 1.00 35.46 ?  1  ALA F O   1 
ATOM 1690 C CB  . ALA K 1 9  ? 140.071 173.012 130.284 1.00 30.41 ?  1  ALA F CB  1 
ATOM 1691 N N   . THR K 1 10 ? 141.826 175.532 130.380 1.00 21.88 ?  2  THR F N   1 
ATOM 1692 C CA  . THR K 1 10 ? 143.030 176.242 130.783 1.00 20.68 ?  2  THR F CA  1 
ATOM 1693 C C   . THR K 1 10 ? 143.214 177.486 129.926 1.00 16.28 ?  2  THR F C   1 
ATOM 1694 O O   . THR K 1 10 ? 142.972 177.460 128.717 1.00 24.08 ?  2  THR F O   1 
ATOM 1695 C CB  . THR K 1 10 ? 144.269 175.344 130.681 1.00 23.13 ?  2  THR F CB  1 
ATOM 1696 O OG1 . THR K 1 10 ? 145.452 176.135 130.855 1.00 22.10 ?  2  THR F OG1 1 
ATOM 1697 C CG2 . THR K 1 10 ? 144.319 174.635 129.342 1.00 25.90 ?  2  THR F CG2 1 
ATOM 1698 N N   . LYS K 1 11 ? 143.629 178.577 130.564 1.00 12.40 ?  3  LYS F N   1 
ATOM 1699 C CA  . LYS K 1 11 ? 143.879 179.839 129.885 1.00 11.07 ?  3  LYS F CA  1 
ATOM 1700 C C   . LYS K 1 11 ? 145.246 180.364 130.295 1.00 8.74  ?  3  LYS F C   1 
ATOM 1701 O O   . LYS K 1 11 ? 145.761 180.023 131.363 1.00 13.17 ?  3  LYS F O   1 
ATOM 1702 C CB  . LYS K 1 11 ? 142.805 180.901 130.198 1.00 14.24 ?  3  LYS F CB  1 
ATOM 1703 C CG  . LYS K 1 11 ? 141.396 180.601 129.681 1.00 15.39 ?  3  LYS F CG  1 
ATOM 1704 C CD  . LYS K 1 11 ? 140.667 179.554 130.511 1.00 18.52 ?  3  LYS F CD  1 
ATOM 1705 C CE  . LYS K 1 11 ? 139.333 179.183 129.888 1.00 22.30 ?  3  LYS F CE  1 
ATOM 1706 N NZ  . LYS K 1 11 ? 138.693 178.039 130.593 1.00 19.90 1  3  LYS F NZ  1 
ATOM 1707 N N   . ALA K 1 12 ? 145.832 181.193 129.436 1.00 4.49  ?  4  ALA F N   1 
ATOM 1708 C CA  . ALA K 1 12 ? 147.136 181.782 129.711 1.00 4.08  ?  4  ALA F CA  1 
ATOM 1709 C C   . ALA K 1 12 ? 147.213 183.139 129.033 1.00 3.13  ?  4  ALA F C   1 
ATOM 1710 O O   . ALA K 1 12 ? 147.053 183.232 127.813 1.00 6.26  ?  4  ALA F O   1 
ATOM 1711 C CB  . ALA K 1 12 ? 148.265 180.872 129.226 1.00 6.52  ?  4  ALA F CB  1 
ATOM 1712 N N   . VAL K 1 13 ? 147.459 184.183 129.819 1.00 1.75  ?  5  VAL F N   1 
ATOM 1713 C CA  . VAL K 1 13 ? 147.582 185.544 129.314 1.00 2.31  ?  5  VAL F CA  1 
ATOM 1714 C C   . VAL K 1 13 ? 148.890 186.125 129.829 1.00 2.62  ?  5  VAL F C   1 
ATOM 1715 O O   . VAL K 1 13 ? 149.184 186.037 131.026 1.00 5.53  ?  5  VAL F O   1 
ATOM 1716 C CB  . VAL K 1 13 ? 146.393 186.425 129.743 1.00 2.59  ?  5  VAL F CB  1 
ATOM 1717 C CG1 . VAL K 1 13 ? 146.601 187.862 129.290 1.00 2.08  ?  5  VAL F CG1 1 
ATOM 1718 C CG2 . VAL K 1 13 ? 145.092 185.868 129.188 1.00 2.27  ?  5  VAL F CG2 1 
ATOM 1719 N N   . ALA K 1 14 ? 149.674 186.712 128.929 1.00 2.76  ?  6  ALA F N   1 
ATOM 1720 C CA  . ALA K 1 14 ? 150.942 187.338 129.280 1.00 4.23  ?  6  ALA F CA  1 
ATOM 1721 C C   . ALA K 1 14 ? 150.953 188.763 128.750 1.00 4.41  ?  6  ALA F C   1 
ATOM 1722 O O   . ALA K 1 14 ? 150.734 188.985 127.554 1.00 9.14  ?  6  ALA F O   1 
ATOM 1723 C CB  . ALA K 1 14 ? 152.121 186.546 128.717 1.00 5.34  ?  6  ALA F CB  1 
ATOM 1724 N N   . VAL K 1 15 ? 151.208 189.722 129.636 1.00 3.00  ?  7  VAL F N   1 
ATOM 1725 C CA  . VAL K 1 15 ? 151.249 191.135 129.283 1.00 5.44  ?  7  VAL F CA  1 
ATOM 1726 C C   . VAL K 1 15 ? 152.519 191.741 129.862 1.00 6.79  ?  7  VAL F C   1 
ATOM 1727 O O   . VAL K 1 15 ? 152.816 191.553 131.047 1.00 12.06 ?  7  VAL F O   1 
ATOM 1728 C CB  . VAL K 1 15 ? 150.006 191.889 129.794 1.00 7.38  ?  7  VAL F CB  1 
ATOM 1729 C CG1 . VAL K 1 15 ? 150.223 193.393 129.725 1.00 6.30  ?  7  VAL F CG1 1 
ATOM 1730 C CG2 . VAL K 1 15 ? 148.778 191.488 128.994 1.00 5.02  ?  7  VAL F CG2 1 
ATOM 1731 N N   . LEU K 1 16 ? 153.266 192.461 129.030 1.00 7.33  ?  8  LEU F N   1 
ATOM 1732 C CA  . LEU K 1 16 ? 154.458 193.171 129.470 1.00 9.02  ?  8  LEU F CA  1 
ATOM 1733 C C   . LEU K 1 16 ? 154.493 194.531 128.792 1.00 13.78 ?  8  LEU F C   1 
ATOM 1734 O O   . LEU K 1 16 ? 154.257 194.631 127.585 1.00 25.23 ?  8  LEU F O   1 
ATOM 1735 C CB  . LEU K 1 16 ? 155.729 192.374 129.151 1.00 11.16 ?  8  LEU F CB  1 
ATOM 1736 C CG  . LEU K 1 16 ? 157.072 193.109 129.200 1.00 14.67 ?  8  LEU F CG  1 
ATOM 1737 C CD1 . LEU K 1 16 ? 157.304 193.767 130.545 1.00 20.42 ?  8  LEU F CD1 1 
ATOM 1738 C CD2 . LEU K 1 16 ? 158.208 192.157 128.874 1.00 17.98 ?  8  LEU F CD2 1 
ATOM 1739 N N   . LYS K 1 17 ? 154.787 195.571 129.570 1.00 11.41 ?  9  LYS F N   1 
ATOM 1740 C CA  . LYS K 1 17 ? 154.837 196.933 129.054 1.00 13.56 ?  9  LYS F CA  1 
ATOM 1741 C C   . LYS K 1 17 ? 156.194 197.540 129.402 1.00 15.29 ?  9  LYS F C   1 
ATOM 1742 O O   . LYS K 1 17 ? 156.278 198.659 129.916 1.00 16.23 ?  9  LYS F O   1 
ATOM 1743 C CB  . LYS K 1 17 ? 153.681 197.762 129.624 1.00 13.71 ?  9  LYS F CB  1 
ATOM 1744 C CG  . LYS K 1 17 ? 153.472 199.127 128.976 1.00 14.94 ?  9  LYS F CG  1 
ATOM 1745 C CD  . LYS K 1 17 ? 152.603 200.019 129.848 1.00 14.57 ?  9  LYS F CD  1 
ATOM 1746 C CE  . LYS K 1 17 ? 151.179 199.495 129.926 1.00 16.26 ?  9  LYS F CE  1 
ATOM 1747 N NZ  . LYS K 1 17 ? 150.213 200.562 130.305 1.00 15.38 1  9  LYS F NZ  1 
ATOM 1748 N N   . GLY K 1 18 ? 157.259 196.798 129.138 1.00 16.28 ?  10 GLY F N   1 
ATOM 1749 C CA  . GLY K 1 18 ? 158.594 197.222 129.522 1.00 20.25 ?  10 GLY F CA  1 
ATOM 1750 C C   . GLY K 1 18 ? 159.561 197.183 128.362 1.00 26.23 ?  10 GLY F C   1 
ATOM 1751 O O   . GLY K 1 18 ? 159.463 196.332 127.476 1.00 26.39 ?  10 GLY F O   1 
ATOM 1752 N N   . ASP K 1 19 ? 160.513 198.117 128.383 1.00 32.75 ?  11 ASP F N   1 
ATOM 1753 C CA  . ASP K 1 19 ? 161.535 198.206 127.348 1.00 34.06 ?  11 ASP F CA  1 
ATOM 1754 C C   . ASP K 1 19 ? 162.487 197.015 127.381 1.00 34.38 ?  11 ASP F C   1 
ATOM 1755 O O   . ASP K 1 19 ? 163.175 196.757 126.391 1.00 31.97 ?  11 ASP F O   1 
ATOM 1756 C CB  . ASP K 1 19 ? 162.301 199.526 127.519 1.00 37.30 ?  11 ASP F CB  1 
ATOM 1757 C CG  . ASP K 1 19 ? 163.061 199.955 126.266 1.00 41.59 ?  11 ASP F CG  1 
ATOM 1758 O OD1 . ASP K 1 19 ? 163.629 199.108 125.551 1.00 43.60 -1 11 ASP F OD1 1 
ATOM 1759 O OD2 . ASP K 1 19 ? 163.095 201.175 126.001 1.00 45.72 ?  11 ASP F OD2 1 
ATOM 1760 N N   . GLY K 1 20 ? 162.531 196.277 128.487 1.00 35.94 ?  12 GLY F N   1 
ATOM 1761 C CA  . GLY K 1 20 ? 163.424 195.151 128.620 1.00 34.39 ?  12 GLY F CA  1 
ATOM 1762 C C   . GLY K 1 20 ? 163.171 194.049 127.612 1.00 29.47 ?  12 GLY F C   1 
ATOM 1763 O O   . GLY K 1 20 ? 162.026 193.720 127.284 1.00 28.48 ?  12 GLY F O   1 
ATOM 1764 N N   . PRO K 1 21 ? 164.247 193.465 127.093 1.00 26.81 ?  13 PRO F N   1 
ATOM 1765 C CA  . PRO K 1 21 ? 164.101 192.344 126.160 1.00 26.71 ?  13 PRO F CA  1 
ATOM 1766 C C   . PRO K 1 21 ? 163.491 191.126 126.836 1.00 25.45 ?  13 PRO F C   1 
ATOM 1767 O O   . PRO K 1 21 ? 163.659 190.900 128.036 1.00 33.91 ?  13 PRO F O   1 
ATOM 1768 C CB  . PRO K 1 21 ? 165.541 192.063 125.711 1.00 25.06 ?  13 PRO F CB  1 
ATOM 1769 C CG  . PRO K 1 21 ? 166.298 193.315 126.027 1.00 25.84 ?  13 PRO F CG  1 
ATOM 1770 C CD  . PRO K 1 21 ? 165.652 193.871 127.254 1.00 27.75 ?  13 PRO F CD  1 
ATOM 1771 N N   . VAL K 1 22 ? 162.773 190.338 126.043 1.00 20.80 ?  14 VAL F N   1 
ATOM 1772 C CA  . VAL K 1 22 ? 162.179 189.089 126.503 1.00 18.20 ?  14 VAL F CA  1 
ATOM 1773 C C   . VAL K 1 22 ? 163.089 187.945 126.084 1.00 23.47 ?  14 VAL F C   1 
ATOM 1774 O O   . VAL K 1 22 ? 163.469 187.840 124.911 1.00 33.83 ?  14 VAL F O   1 
ATOM 1775 C CB  . VAL K 1 22 ? 160.763 188.904 125.934 1.00 17.86 ?  14 VAL F CB  1 
ATOM 1776 C CG1 . VAL K 1 22 ? 160.363 187.440 125.969 1.00 15.32 ?  14 VAL F CG1 1 
ATOM 1777 C CG2 . VAL K 1 22 ? 159.772 189.745 126.710 1.00 22.05 ?  14 VAL F CG2 1 
ATOM 1778 N N   . GLN K 1 23 ? 163.443 187.089 127.039 1.00 22.36 ?  15 GLN F N   1 
ATOM 1779 C CA  . GLN K 1 23 ? 164.349 185.971 126.795 1.00 20.30 ?  15 GLN F CA  1 
ATOM 1780 C C   . GLN K 1 23 ? 163.739 184.713 127.397 1.00 19.11 ?  15 GLN F C   1 
ATOM 1781 O O   . GLN K 1 23 ? 163.587 184.617 128.619 1.00 27.36 ?  15 GLN F O   1 
ATOM 1782 C CB  . GLN K 1 23 ? 165.730 186.249 127.390 1.00 18.87 ?  15 GLN F CB  1 
ATOM 1783 C CG  . GLN K 1 23 ? 166.856 185.488 126.727 1.00 17.91 ?  15 GLN F CG  1 
ATOM 1784 C CD  . GLN K 1 23 ? 168.123 186.309 126.625 1.00 21.22 ?  15 GLN F CD  1 
ATOM 1785 O OE1 . GLN K 1 23 ? 168.865 186.452 127.597 1.00 15.30 ?  15 GLN F OE1 1 
ATOM 1786 N NE2 . GLN K 1 23 ? 168.378 186.856 125.443 1.00 24.15 ?  15 GLN F NE2 1 
ATOM 1787 N N   . GLY K 1 24 ? 163.392 183.752 126.545 1.00 12.80 ?  16 GLY F N   1 
ATOM 1788 C CA  . GLY K 1 24 ? 162.815 182.507 127.009 1.00 7.81  ?  16 GLY F CA  1 
ATOM 1789 C C   . GLY K 1 24 ? 161.534 182.141 126.292 1.00 4.63  ?  16 GLY F C   1 
ATOM 1790 O O   . GLY K 1 24 ? 161.305 182.574 125.160 1.00 5.60  ?  16 GLY F O   1 
ATOM 1791 N N   . ILE K 1 25 ? 160.691 181.344 126.935 1.00 3.20  ?  17 ILE F N   1 
ATOM 1792 C CA  . ILE K 1 25 ? 159.415 180.938 126.360 1.00 2.97  ?  17 ILE F CA  1 
ATOM 1793 C C   . ILE K 1 25 ? 158.290 181.661 127.082 1.00 4.18  ?  17 ILE F C   1 
ATOM 1794 O O   . ILE K 1 25 ? 158.372 181.947 128.282 1.00 20.36 ?  17 ILE F O   1 
ATOM 1795 C CB  . ILE K 1 25 ? 159.225 179.410 126.433 1.00 2.76  ?  17 ILE F CB  1 
ATOM 1796 C CG1 . ILE K 1 25 ? 160.567 178.697 126.289 1.00 3.84  ?  17 ILE F CG1 1 
ATOM 1797 C CG2 . ILE K 1 25 ? 158.261 178.943 125.360 1.00 3.86  ?  17 ILE F CG2 1 
ATOM 1798 C CD1 . ILE K 1 25 ? 160.486 177.217 126.557 1.00 2.74  ?  17 ILE F CD1 1 
ATOM 1799 N N   . ILE K 1 26 ? 157.226 181.962 126.343 1.00 2.67  ?  18 ILE F N   1 
ATOM 1800 C CA  . ILE K 1 26 ? 156.043 182.622 126.880 1.00 1.40  ?  18 ILE F CA  1 
ATOM 1801 C C   . ILE K 1 26 ? 154.843 181.722 126.631 1.00 1.52  ?  18 ILE F C   1 
ATOM 1802 O O   . ILE K 1 26 ? 154.639 181.250 125.506 1.00 2.00  ?  18 ILE F O   1 
ATOM 1803 C CB  . ILE K 1 26 ? 155.827 184.008 126.247 1.00 1.45  ?  18 ILE F CB  1 
ATOM 1804 C CG1 . ILE K 1 26 ? 157.167 184.706 126.016 1.00 1.29  ?  18 ILE F CG1 1 
ATOM 1805 C CG2 . ILE K 1 26 ? 154.931 184.855 127.125 1.00 2.28  ?  18 ILE F CG2 1 
ATOM 1806 C CD1 . ILE K 1 26 ? 157.849 185.152 127.279 1.00 1.32  ?  18 ILE F CD1 1 
ATOM 1807 N N   . ASN K 1 27 ? 154.052 181.489 127.679 1.00 1.62  ?  19 ASN F N   1 
ATOM 1808 C CA  . ASN K 1 27 ? 152.857 180.647 127.600 1.00 2.03  ?  19 ASN F CA  1 
ATOM 1809 C C   . ASN K 1 27 ? 153.196 179.241 127.113 1.00 1.29  ?  19 ASN F C   1 
ATOM 1810 O O   . ASN K 1 27 ? 152.493 178.664 126.282 1.00 2.24  ?  19 ASN F O   1 
ATOM 1811 C CB  . ASN K 1 27 ? 151.786 181.288 126.716 1.00 2.07  ?  19 ASN F CB  1 
ATOM 1812 C CG  . ASN K 1 27 ? 151.489 182.720 127.107 1.00 3.34  ?  19 ASN F CG  1 
ATOM 1813 O OD1 . ASN K 1 27 ? 151.255 183.021 128.277 1.00 3.83  ?  19 ASN F OD1 1 
ATOM 1814 N ND2 . ASN K 1 27 ? 151.498 183.614 126.126 1.00 4.34  ?  19 ASN F ND2 1 
ATOM 1815 N N   . PHE K 1 28 ? 154.286 178.688 127.634 1.00 1.33  ?  20 PHE F N   1 
ATOM 1816 C CA  . PHE K 1 28 ? 154.671 177.318 127.328 1.00 1.50  ?  20 PHE F CA  1 
ATOM 1817 C C   . PHE K 1 28 ? 153.764 176.354 128.084 1.00 2.68  ?  20 PHE F C   1 
ATOM 1818 O O   . PHE K 1 28 ? 153.634 176.442 129.308 1.00 9.02  ?  20 PHE F O   1 
ATOM 1819 C CB  . PHE K 1 28 ? 156.136 177.098 127.703 1.00 2.39  ?  20 PHE F CB  1 
ATOM 1820 C CG  . PHE K 1 28 ? 156.688 175.771 127.275 1.00 1.78  ?  20 PHE F CG  1 
ATOM 1821 C CD1 . PHE K 1 28 ? 156.077 175.029 126.283 1.00 2.68  ?  20 PHE F CD1 1 
ATOM 1822 C CD2 . PHE K 1 28 ? 157.832 175.271 127.865 1.00 2.10  ?  20 PHE F CD2 1 
ATOM 1823 C CE1 . PHE K 1 28 ? 156.591 173.811 125.900 1.00 3.16  ?  20 PHE F CE1 1 
ATOM 1824 C CE2 . PHE K 1 28 ? 158.349 174.057 127.484 1.00 2.00  ?  20 PHE F CE2 1 
ATOM 1825 C CZ  . PHE K 1 28 ? 157.730 173.327 126.499 1.00 2.66  ?  20 PHE F CZ  1 
ATOM 1826 N N   . GLU K 1 29 ? 153.137 175.433 127.355 1.00 1.15  ?  21 GLU F N   1 
ATOM 1827 C CA  . GLU K 1 29 ? 152.123 174.541 127.910 1.00 1.57  ?  21 GLU F CA  1 
ATOM 1828 C C   . GLU K 1 29 ? 152.419 173.092 127.549 1.00 1.73  ?  21 GLU F C   1 
ATOM 1829 O O   . GLU K 1 29 ? 151.553 172.361 127.063 1.00 1.58  ?  21 GLU F O   1 
ATOM 1830 C CB  . GLU K 1 29 ? 150.728 174.933 127.430 1.00 1.06  ?  21 GLU F CB  1 
ATOM 1831 C CG  . GLU K 1 29 ? 150.487 176.431 127.372 1.00 1.10  ?  21 GLU F CG  1 
ATOM 1832 C CD  . GLU K 1 29 ? 149.017 176.786 127.334 1.00 1.23  ?  21 GLU F CD  1 
ATOM 1833 O OE1 . GLU K 1 29 ? 148.180 175.861 127.294 1.00 1.37  ?  21 GLU F OE1 1 
ATOM 1834 O OE2 . GLU K 1 29 ? 148.700 177.993 127.343 1.00 1.43  -1 21 GLU F OE2 1 
ATOM 1835 N N   . GLN K 1 30 ? 153.658 172.659 127.778 1.00 1.74  ?  22 GLN F N   1 
ATOM 1836 C CA  . GLN K 1 30 ? 154.018 171.263 127.557 1.00 1.55  ?  22 GLN F CA  1 
ATOM 1837 C C   . GLN K 1 30 ? 153.139 170.351 128.403 1.00 2.07  ?  22 GLN F C   1 
ATOM 1838 O O   . GLN K 1 30 ? 152.948 170.589 129.597 1.00 7.82  ?  22 GLN F O   1 
ATOM 1839 C CB  . GLN K 1 30 ? 155.493 171.042 127.890 1.00 1.81  ?  22 GLN F CB  1 
ATOM 1840 C CG  . GLN K 1 30 ? 155.839 169.608 128.236 1.00 2.66  ?  22 GLN F CG  1 
ATOM 1841 C CD  . GLN K 1 30 ? 157.333 169.344 128.240 1.00 2.57  ?  22 GLN F CD  1 
ATOM 1842 O OE1 . GLN K 1 30 ? 158.004 169.501 127.223 1.00 2.36  ?  22 GLN F OE1 1 
ATOM 1843 N NE2 . GLN K 1 30 ? 157.859 168.934 129.387 1.00 2.89  ?  22 GLN F NE2 1 
ATOM 1844 N N   . LYS K 1 31 ? 152.599 169.304 127.782 1.00 1.87  ?  23 LYS F N   1 
ATOM 1845 C CA  . LYS K 1 31 ? 151.603 168.477 128.450 1.00 1.92  ?  23 LYS F CA  1 
ATOM 1846 C C   . LYS K 1 31 ? 151.688 167.041 127.957 1.00 3.06  ?  23 LYS F C   1 
ATOM 1847 O O   . LYS K 1 31 ? 151.712 166.797 126.748 1.00 5.25  ?  23 LYS F O   1 
ATOM 1848 C CB  . LYS K 1 31 ? 150.195 169.035 128.216 1.00 1.73  ?  23 LYS F CB  1 
ATOM 1849 C CG  . LYS K 1 31 ? 149.080 168.017 128.366 1.00 1.66  ?  23 LYS F CG  1 
ATOM 1850 C CD  . LYS K 1 31 ? 147.717 168.686 128.465 1.00 2.02  ?  23 LYS F CD  1 
ATOM 1851 C CE  . LYS K 1 31 ? 147.662 169.981 127.670 1.00 2.93  ?  23 LYS F CE  1 
ATOM 1852 N NZ  . LYS K 1 31 ? 146.397 170.726 127.912 1.00 4.12  1  23 LYS F NZ  1 
ATOM 1853 N N   . GLU K 1 32 ? 151.723 166.102 128.905 1.00 4.10  ?  24 GLU F N   1 
ATOM 1854 C CA  . GLU K 1 32 ? 151.693 164.667 128.615 1.00 5.39  ?  24 GLU F CA  1 
ATOM 1855 C C   . GLU K 1 32 ? 152.797 164.266 127.641 1.00 7.25  ?  24 GLU F C   1 
ATOM 1856 O O   . GLU K 1 32 ? 152.587 163.476 126.719 1.00 9.80  ?  24 GLU F O   1 
ATOM 1857 C CB  . GLU K 1 32 ? 150.322 164.243 128.087 1.00 3.63  ?  24 GLU F CB  1 
ATOM 1858 C CG  . GLU K 1 32 ? 149.184 164.492 129.057 1.00 4.42  ?  24 GLU F CG  1 
ATOM 1859 C CD  . GLU K 1 32 ? 147.827 164.199 128.453 1.00 4.91  ?  24 GLU F CD  1 
ATOM 1860 O OE1 . GLU K 1 32 ? 147.584 163.036 128.071 1.00 6.01  ?  24 GLU F OE1 1 
ATOM 1861 O OE2 . GLU K 1 32 ? 147.002 165.133 128.361 1.00 3.74  -1 24 GLU F OE2 1 
ATOM 1862 N N   . SER K 1 33 ? 153.988 164.810 127.853 1.00 6.77  ?  25 SER F N   1 
ATOM 1863 C CA  . SER K 1 33 ? 155.117 164.569 126.968 1.00 10.76 ?  25 SER F CA  1 
ATOM 1864 C C   . SER K 1 33 ? 156.285 163.991 127.764 1.00 15.28 ?  25 SER F C   1 
ATOM 1865 O O   . SER K 1 33 ? 156.159 163.651 128.942 1.00 20.99 ?  25 SER F O   1 
ATOM 1866 C CB  . SER K 1 33 ? 155.520 165.856 126.250 1.00 11.58 ?  25 SER F CB  1 
ATOM 1867 O OG  . SER K 1 33 ? 156.159 166.741 127.148 1.00 6.84  ?  25 SER F OG  1 
ATOM 1868 N N   . ASN K 1 34 ? 157.432 163.874 127.096 1.00 13.65 ?  26 ASN F N   1 
ATOM 1869 C CA  . ASN K 1 34 ? 158.659 163.397 127.731 1.00 14.20 ?  26 ASN F CA  1 
ATOM 1870 C C   . ASN K 1 34 ? 159.823 164.082 127.024 1.00 14.73 ?  26 ASN F C   1 
ATOM 1871 O O   . ASN K 1 34 ? 160.215 163.673 125.928 1.00 20.09 ?  26 ASN F O   1 
ATOM 1872 C CB  . ASN K 1 34 ? 158.769 161.881 127.654 1.00 20.75 ?  26 ASN F CB  1 
ATOM 1873 C CG  . ASN K 1 34 ? 160.146 161.380 128.034 1.00 23.14 ?  26 ASN F CG  1 
ATOM 1874 O OD1 . ASN K 1 34 ? 160.826 160.736 127.236 1.00 26.41 ?  26 ASN F OD1 1 
ATOM 1875 N ND2 . ASN K 1 34 ? 160.566 161.675 129.258 1.00 21.92 ?  26 ASN F ND2 1 
ATOM 1876 N N   . GLY K 1 35 ? 160.361 165.124 127.649 1.00 9.69  ?  27 GLY F N   1 
ATOM 1877 C CA  . GLY K 1 35 ? 161.455 165.863 127.071 1.00 6.74  ?  27 GLY F CA  1 
ATOM 1878 C C   . GLY K 1 35 ? 162.071 166.847 128.040 1.00 2.59  ?  27 GLY F C   1 
ATOM 1879 O O   . GLY K 1 35 ? 161.379 167.632 128.694 1.00 2.30  ?  27 GLY F O   1 
ATOM 1880 N N   . PRO K 1 36 ? 163.394 166.820 128.152 1.00 2.08  ?  28 PRO F N   1 
ATOM 1881 C CA  . PRO K 1 36 ? 164.109 167.778 129.019 1.00 2.22  ?  28 PRO F CA  1 
ATOM 1882 C C   . PRO K 1 36 ? 164.211 169.166 128.390 1.00 1.46  ?  28 PRO F C   1 
ATOM 1883 O O   . PRO K 1 36 ? 165.205 169.553 127.778 1.00 1.56  ?  28 PRO F O   1 
ATOM 1884 C CB  . PRO K 1 36 ? 165.480 167.121 129.187 1.00 3.18  ?  28 PRO F CB  1 
ATOM 1885 C CG  . PRO K 1 36 ? 165.662 166.307 127.960 1.00 2.60  ?  28 PRO F CG  1 
ATOM 1886 C CD  . PRO K 1 36 ? 164.300 165.829 127.549 1.00 3.15  ?  28 PRO F CD  1 
ATOM 1887 N N   . VAL K 1 37 ? 163.137 169.944 128.541 1.00 1.09  ?  29 VAL F N   1 
ATOM 1888 C CA  . VAL K 1 37 ? 163.128 171.306 128.025 1.00 1.31  ?  29 VAL F CA  1 
ATOM 1889 C C   . VAL K 1 37 ? 164.178 172.141 128.742 1.00 1.06  ?  29 VAL F C   1 
ATOM 1890 O O   . VAL K 1 37 ? 164.245 172.172 129.976 1.00 2.25  ?  29 VAL F O   1 
ATOM 1891 C CB  . VAL K 1 37 ? 161.723 171.915 128.143 1.00 1.17  ?  29 VAL F CB  1 
ATOM 1892 C CG1 . VAL K 1 37 ? 161.188 171.762 129.538 1.00 1.83  ?  29 VAL F CG1 1 
ATOM 1893 C CG2 . VAL K 1 37 ? 161.766 173.390 127.779 1.00 1.49  ?  29 VAL F CG2 1 
ATOM 1894 N N   . LYS K 1 38 ? 165.019 172.813 127.962 1.00 0.86  ?  30 LYS F N   1 
ATOM 1895 C CA  . LYS K 1 38 ? 166.102 173.635 128.480 1.00 1.06  ?  30 LYS F CA  1 
ATOM 1896 C C   . LYS K 1 38 ? 166.010 175.023 127.867 1.00 1.21  ?  30 LYS F C   1 
ATOM 1897 O O   . LYS K 1 38 ? 165.876 175.158 126.647 1.00 3.08  ?  30 LYS F O   1 
ATOM 1898 C CB  . LYS K 1 38 ? 167.462 173.003 128.175 1.00 1.14  ?  30 LYS F CB  1 
ATOM 1899 C CG  . LYS K 1 38 ? 168.656 173.856 128.569 1.00 1.32  ?  30 LYS F CG  1 
ATOM 1900 C CD  . LYS K 1 38 ? 169.960 173.174 128.196 1.00 1.00  ?  30 LYS F CD  1 
ATOM 1901 C CE  . LYS K 1 38 ? 171.158 174.045 128.532 1.00 1.14  ?  30 LYS F CE  1 
ATOM 1902 N NZ  . LYS K 1 38 ? 172.445 173.374 128.200 1.00 0.73  1  30 LYS F NZ  1 
ATOM 1903 N N   . VAL K 1 39 ? 166.080 176.049 128.708 1.00 0.91  ?  31 VAL F N   1 
ATOM 1904 C CA  . VAL K 1 39 ? 166.022 177.437 128.268 1.00 1.50  ?  31 VAL F CA  1 
ATOM 1905 C C   . VAL K 1 39 ? 167.300 178.127 128.715 1.00 2.30  ?  31 VAL F C   1 
ATOM 1906 O O   . VAL K 1 39 ? 167.635 178.113 129.906 1.00 4.40  ?  31 VAL F O   1 
ATOM 1907 C CB  . VAL K 1 39 ? 164.787 178.163 128.822 1.00 2.29  ?  31 VAL F CB  1 
ATOM 1908 C CG1 . VAL K 1 39 ? 164.739 179.592 128.306 1.00 2.31  ?  31 VAL F CG1 1 
ATOM 1909 C CG2 . VAL K 1 39 ? 163.524 177.413 128.451 1.00 1.58  ?  31 VAL F CG2 1 
ATOM 1910 N N   . TRP K 1 40 ? 168.007 178.732 127.767 1.00 2.21  ?  32 TRP F N   1 
ATOM 1911 C CA  . TRP K 1 40 ? 169.250 179.440 128.038 1.00 2.99  ?  32 TRP F CA  1 
ATOM 1912 C C   . TRP K 1 40 ? 169.069 180.898 127.644 1.00 3.21  ?  32 TRP F C   1 
ATOM 1913 O O   . TRP K 1 40 ? 168.721 181.196 126.496 1.00 5.23  ?  32 TRP F O   1 
ATOM 1914 C CB  . TRP K 1 40 ? 170.416 178.806 127.275 1.00 4.17  ?  32 TRP F CB  1 
ATOM 1915 C CG  . TRP K 1 40 ? 171.773 179.260 127.722 1.00 3.61  ?  32 TRP F CG  1 
ATOM 1916 C CD1 . TRP K 1 40 ? 172.221 180.545 127.817 1.00 4.41  ?  32 TRP F CD1 1 
ATOM 1917 C CD2 . TRP K 1 40 ? 172.861 178.426 128.132 1.00 3.72  ?  32 TRP F CD2 1 
ATOM 1918 N NE1 . TRP K 1 40 ? 173.519 180.563 128.261 1.00 3.94  ?  32 TRP F NE1 1 
ATOM 1919 C CE2 . TRP K 1 40 ? 173.936 179.274 128.462 1.00 4.98  ?  32 TRP F CE2 1 
ATOM 1920 C CE3 . TRP K 1 40 ? 173.032 177.043 128.252 1.00 3.71  ?  32 TRP F CE3 1 
ATOM 1921 C CZ2 . TRP K 1 40 ? 175.164 178.786 128.905 1.00 6.31  ?  32 TRP F CZ2 1 
ATOM 1922 C CZ3 . TRP K 1 40 ? 174.251 176.560 128.692 1.00 4.28  ?  32 TRP F CZ3 1 
ATOM 1923 C CH2 . TRP K 1 40 ? 175.301 177.429 129.013 1.00 5.60  ?  32 TRP F CH2 1 
ATOM 1924 N N   . GLY K 1 41 ? 169.303 181.800 128.591 1.00 3.12  ?  33 GLY F N   1 
ATOM 1925 C CA  . GLY K 1 41 ? 169.169 183.216 128.324 1.00 7.91  ?  33 GLY F CA  1 
ATOM 1926 C C   . GLY K 1 41 ? 170.370 184.021 128.772 1.00 9.98  ?  33 GLY F C   1 
ATOM 1927 O O   . GLY K 1 41 ? 170.695 184.054 129.963 1.00 15.16 ?  33 GLY F O   1 
ATOM 1928 N N   . SER K 1 42 ? 171.037 184.676 127.828 1.00 7.03  ?  34 SER F N   1 
ATOM 1929 C CA  . SER K 1 42 ? 172.219 185.475 128.115 1.00 9.59  ?  34 SER F CA  1 
ATOM 1930 C C   . SER K 1 42 ? 172.060 186.848 127.483 1.00 12.86 ?  34 SER F C   1 
ATOM 1931 O O   . SER K 1 42 ? 171.556 186.962 126.362 1.00 22.86 ?  34 SER F O   1 
ATOM 1932 C CB  . SER K 1 42 ? 173.489 184.794 127.593 1.00 10.24 ?  34 SER F CB  1 
ATOM 1933 O OG  . SER K 1 42 ? 174.631 185.596 127.833 1.00 10.90 ?  34 SER F OG  1 
ATOM 1934 N N   . ILE K 1 43 ? 172.480 187.884 128.205 1.00 8.73  ?  35 ILE F N   1 
ATOM 1935 C CA  . ILE K 1 43 ? 172.463 189.254 127.704 1.00 12.07 ?  35 ILE F CA  1 
ATOM 1936 C C   . ILE K 1 43 ? 173.631 190.004 128.329 1.00 13.05 ?  35 ILE F C   1 
ATOM 1937 O O   . ILE K 1 43 ? 173.702 190.139 129.555 1.00 18.89 ?  35 ILE F O   1 
ATOM 1938 C CB  . ILE K 1 43 ? 171.130 189.966 128.004 1.00 13.89 ?  35 ILE F CB  1 
ATOM 1939 C CG1 . ILE K 1 43 ? 171.276 191.481 127.841 1.00 16.89 ?  35 ILE F CG1 1 
ATOM 1940 C CG2 . ILE K 1 43 ? 170.606 189.588 129.378 1.00 19.63 ?  35 ILE F CG2 1 
ATOM 1941 C CD1 . ILE K 1 43 ? 169.959 192.223 127.852 1.00 19.55 ?  35 ILE F CD1 1 
ATOM 1942 N N   . LYS K 1 44 ? 174.552 190.481 127.492 1.00 13.71 ?  36 LYS F N   1 
ATOM 1943 C CA  . LYS K 1 44 ? 175.732 191.200 127.960 1.00 19.51 ?  36 LYS F CA  1 
ATOM 1944 C C   . LYS K 1 44 ? 175.773 192.585 127.325 1.00 24.14 ?  36 LYS F C   1 
ATOM 1945 O O   . LYS K 1 44 ? 176.411 192.782 126.286 1.00 35.30 ?  36 LYS F O   1 
ATOM 1946 C CB  . LYS K 1 44 ? 177.009 190.415 127.651 1.00 19.26 ?  36 LYS F CB  1 
ATOM 1947 C CG  . LYS K 1 44 ? 177.009 189.000 128.211 1.00 15.07 ?  36 LYS F CG  1 
ATOM 1948 C CD  . LYS K 1 44 ? 178.111 188.153 127.598 1.00 15.29 ?  36 LYS F CD  1 
ATOM 1949 C CE  . LYS K 1 44 ? 179.474 188.531 128.153 1.00 19.88 ?  36 LYS F CE  1 
ATOM 1950 N NZ  . LYS K 1 44 ? 180.455 187.421 128.003 1.00 20.42 1  36 LYS F NZ  1 
ATOM 1951 N N   . GLY K 1 45 ? 175.100 193.542 127.959 1.00 22.39 ?  37 GLY F N   1 
ATOM 1952 C CA  . GLY K 1 45 ? 175.102 194.915 127.502 1.00 34.53 ?  37 GLY F CA  1 
ATOM 1953 C C   . GLY K 1 45 ? 174.397 195.811 128.499 1.00 50.93 ?  37 GLY F C   1 
ATOM 1954 O O   . GLY K 1 45 ? 174.093 195.393 129.618 1.00 60.96 ?  37 GLY F O   1 
ATOM 1955 N N   . LEU K 1 46 ? 174.116 197.046 128.092 1.00 55.90 ?  38 LEU F N   1 
ATOM 1956 C CA  . LEU K 1 46 ? 173.505 198.012 128.994 1.00 62.17 ?  38 LEU F CA  1 
ATOM 1957 C C   . LEU K 1 46 ? 172.242 198.599 128.380 1.00 63.02 ?  38 LEU F C   1 
ATOM 1958 O O   . LEU K 1 46 ? 172.158 198.813 127.170 1.00 68.61 ?  38 LEU F O   1 
ATOM 1959 C CB  . LEU K 1 46 ? 174.475 199.138 129.381 1.00 66.59 ?  38 LEU F CB  1 
ATOM 1960 C CG  . LEU K 1 46 ? 174.950 200.215 128.405 1.00 64.08 ?  38 LEU F CG  1 
ATOM 1961 C CD1 . LEU K 1 46 ? 175.744 201.265 129.146 1.00 67.23 ?  38 LEU F CD1 1 
ATOM 1962 C CD2 . LEU K 1 46 ? 175.865 199.587 127.383 1.00 56.33 ?  38 LEU F CD2 1 
ATOM 1963 N N   . THR K 1 47 ? 171.264 198.861 129.243 1.00 61.74 ?  39 THR F N   1 
ATOM 1964 C CA  . THR K 1 47 ? 169.991 199.447 128.855 1.00 64.45 ?  39 THR F CA  1 
ATOM 1965 C C   . THR K 1 47 ? 169.794 200.756 129.608 1.00 65.26 ?  39 THR F C   1 
ATOM 1966 O O   . THR K 1 47 ? 170.406 200.980 130.658 1.00 68.25 ?  39 THR F O   1 
ATOM 1967 C CB  . THR K 1 47 ? 168.834 198.484 129.137 1.00 67.76 ?  39 THR F CB  1 
ATOM 1968 O OG1 . THR K 1 47 ? 168.667 198.334 130.551 1.00 67.28 ?  39 THR F OG1 1 
ATOM 1969 C CG2 . THR K 1 47 ? 169.122 197.120 128.533 1.00 66.15 ?  39 THR F CG2 1 
ATOM 1970 N N   . GLU K 1 48 ? 168.945 201.623 129.065 1.00 66.18 ?  40 GLU F N   1 
ATOM 1971 C CA  . GLU K 1 48 ? 168.683 202.926 129.654 1.00 61.50 ?  40 GLU F CA  1 
ATOM 1972 C C   . GLU K 1 48 ? 167.180 203.151 129.741 1.00 59.06 ?  40 GLU F C   1 
ATOM 1973 O O   . GLU K 1 48 ? 166.386 202.420 129.142 1.00 60.79 ?  40 GLU F O   1 
ATOM 1974 C CB  . GLU K 1 48 ? 169.339 204.047 128.839 1.00 62.11 ?  40 GLU F CB  1 
ATOM 1975 C CG  . GLU K 1 48 ? 170.780 204.341 129.223 1.00 60.56 ?  40 GLU F CG  1 
ATOM 1976 C CD  . GLU K 1 48 ? 171.733 203.243 128.792 1.00 65.93 ?  40 GLU F CD  1 
ATOM 1977 O OE1 . GLU K 1 48 ? 171.710 202.866 127.604 1.00 71.63 ?  40 GLU F OE1 1 
ATOM 1978 O OE2 . GLU K 1 48 ? 172.508 202.758 129.641 1.00 64.65 -1 40 GLU F OE2 1 
ATOM 1979 N N   . GLY K 1 49 ? 166.799 204.171 130.502 1.00 60.96 ?  41 GLY F N   1 
ATOM 1980 C CA  . GLY K 1 49 ? 165.401 204.518 130.670 1.00 63.08 ?  41 GLY F CA  1 
ATOM 1981 C C   . GLY K 1 49 ? 165.048 205.867 130.076 1.00 60.55 ?  41 GLY F C   1 
ATOM 1982 O O   . GLY K 1 49 ? 165.889 206.763 130.004 1.00 62.50 ?  41 GLY F O   1 
ATOM 1983 N N   . UNK L 2 1  ? 146.313 207.767 131.128 1.00 26.05 ?  1  UNK L N   1 
ATOM 1984 C CA  . UNK L 2 1  ? 145.306 206.956 131.802 1.00 26.04 ?  1  UNK L CA  1 
ATOM 1985 C C   . UNK L 2 1  ? 145.406 205.497 131.373 1.00 26.58 ?  1  UNK L C   1 
ATOM 1986 O O   . UNK L 2 1  ? 144.444 204.924 130.862 1.00 29.40 ?  1  UNK L O   1 
ATOM 1987 C CB  . UNK L 2 1  ? 143.913 207.497 131.521 1.00 22.41 ?  1  UNK L CB  1 
ATOM 1988 N N   . UNK L 2 2  ? 146.578 204.902 131.584 1.00 22.86 ?  2  UNK L N   1 
ATOM 1989 C CA  . UNK L 2 2  ? 146.795 203.510 131.215 1.00 22.32 ?  2  UNK L CA  1 
ATOM 1990 C C   . UNK L 2 2  ? 145.951 202.592 132.088 1.00 21.72 ?  2  UNK L C   1 
ATOM 1991 O O   . UNK L 2 2  ? 145.924 202.738 133.314 1.00 26.76 ?  2  UNK L O   1 
ATOM 1992 C CB  . UNK L 2 2  ? 148.276 203.158 131.343 1.00 21.86 ?  2  UNK L CB  1 
ATOM 1993 N N   . UNK L 2 3  ? 145.260 201.645 131.457 1.00 21.09 ?  3  UNK L N   1 
ATOM 1994 C CA  . UNK L 2 3  ? 144.408 200.705 132.169 1.00 25.47 ?  3  UNK L CA  1 
ATOM 1995 C C   . UNK L 2 3  ? 144.485 199.342 131.500 1.00 29.06 ?  3  UNK L C   1 
ATOM 1996 O O   . UNK L 2 3  ? 144.416 199.242 130.272 1.00 38.46 ?  3  UNK L O   1 
ATOM 1997 C CB  . UNK L 2 3  ? 142.954 201.190 132.211 1.00 25.18 ?  3  UNK L CB  1 
ATOM 1998 N N   . UNK L 2 4  ? 144.627 198.298 132.311 1.00 28.04 ?  4  UNK L N   1 
ATOM 1999 C CA  . UNK L 2 4  ? 144.656 196.921 131.834 1.00 31.96 ?  4  UNK L CA  1 
ATOM 2000 C C   . UNK L 2 4  ? 143.475 196.175 132.436 1.00 34.09 ?  4  UNK L C   1 
ATOM 2001 O O   . UNK L 2 4  ? 143.333 196.119 133.662 1.00 39.06 ?  4  UNK L O   1 
ATOM 2002 C CB  . UNK L 2 4  ? 145.974 196.236 132.201 1.00 32.03 ?  4  UNK L CB  1 
ATOM 2003 N N   . UNK L 2 5  ? 142.633 195.606 131.577 1.00 29.75 ?  5  UNK L N   1 
ATOM 2004 C CA  . UNK L 2 5  ? 141.432 194.904 132.009 1.00 30.80 ?  5  UNK L CA  1 
ATOM 2005 C C   . UNK L 2 5  ? 141.406 193.515 131.393 1.00 29.10 ?  5  UNK L C   1 
ATOM 2006 O O   . UNK L 2 5  ? 141.604 193.365 130.183 1.00 33.74 ?  5  UNK L O   1 
ATOM 2007 C CB  . UNK L 2 5  ? 140.169 195.680 131.622 1.00 39.20 ?  5  UNK L CB  1 
ATOM 2008 N N   . UNK L 2 6  ? 141.164 192.506 132.225 1.00 30.19 ?  6  UNK L N   1 
ATOM 2009 C CA  . UNK L 2 6  ? 141.025 191.128 131.776 1.00 38.33 ?  6  UNK L CA  1 
ATOM 2010 C C   . UNK L 2 6  ? 139.795 190.524 132.434 1.00 42.09 ?  6  UNK L C   1 
ATOM 2011 O O   . UNK L 2 6  ? 139.641 190.602 133.656 1.00 49.64 ?  6  UNK L O   1 
ATOM 2012 C CB  . UNK L 2 6  ? 142.272 190.303 132.111 1.00 37.15 ?  6  UNK L CB  1 
ATOM 2013 N N   . UNK L 2 7  ? 138.927 189.923 131.625 1.00 39.87 ?  7  UNK L N   1 
ATOM 2014 C CA  . UNK L 2 7  ? 137.686 189.342 132.109 1.00 42.13 ?  7  UNK L CA  1 
ATOM 2015 C C   . UNK L 2 7  ? 137.552 187.917 131.594 1.00 45.23 ?  7  UNK L C   1 
ATOM 2016 O O   . UNK L 2 7  ? 138.144 187.542 130.579 1.00 56.63 ?  7  UNK L O   1 
ATOM 2017 C CB  . UNK L 2 7  ? 136.468 190.173 131.680 1.00 38.50 ?  7  UNK L CB  1 
ATOM 2018 N N   . UNK L 2 8  ? 136.764 187.123 132.313 1.00 41.67 ?  8  UNK L N   1 
ATOM 2019 C CA  . UNK L 2 8  ? 136.529 185.734 131.939 1.00 47.40 ?  8  UNK L CA  1 
ATOM 2020 C C   . UNK L 2 8  ? 135.182 185.250 132.465 1.00 48.38 ?  8  UNK L C   1 
ATOM 2021 O O   . UNK L 2 8  ? 134.886 184.056 132.435 1.00 49.71 ?  8  UNK L O   1 
ATOM 2022 C CB  . UNK L 2 8  ? 137.651 184.848 132.456 1.00 45.22 ?  8  UNK L CB  1 
# 
