data_9G1T
# 
_entry.id   9G1T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9G1T         pdb_00009g1t 10.2210/pdb9g1t/pdb 
WWPDB D_1292140134 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
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.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G1T 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              honnappa.srinivas@novartis.com 
_pdbx_contact_author.name_first         Honnappa 
_pdbx_contact_author.name_last          Srinivas 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5171-4236 
# 
_audit_author.name               'Srinivas, H.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                4721 
_citation.page_last                 4742 
_citation.title                     'Discovery of GJG057, a Potent and Highly Selective Inhibitor of Leukotriene C4 Synthase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02897 
_citation.pdbx_database_id_PubMed   39960261 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Thoma, G.'         1  0000-0003-0467-331X 
primary 'Miltz, W.'         2  ?                   
primary 'Waelchli, R.'      3  ?                   
primary 'Orain, D.'         4  ?                   
primary 'Spanka, C.'        5  0000-0003-0365-204X 
primary 'Decoret, O.'       6  ?                   
primary 'Wolf, R.M.'        7  ?                   
primary 'Hurley, B.'        8  0000-0002-2436-8390 
primary 'Cheung, A.K.'      9  0000-0002-2210-6362 
primary 'Sandham, D.A.'     10 0000-0003-4523-9931 
primary 'Honda, A.'         11 ?                   
primary 'Tichkule, R.'      12 ?                   
primary 'Chen, X.'          13 0000-0002-0930-0750 
primary 'Patel, T.'         14 ?                   
primary 'Labbe-Giguere, N.' 15 ?                   
primary 'Tan, K.L.'         16 0000-0001-8243-1223 
primary 'Springer, C.'      17 ?                   
primary 'Manchester, J.'    18 ?                   
primary 'Culshaw, A.J.'     19 ?                   
primary 'Hunt, P.'          20 ?                   
primary 'Srinivas, H.'      21 ?                   
primary 'Penno, C.A.'       22 ?                   
primary 'Ferrand, S.'       23 ?                   
primary 'Numao, S.'         24 0000-0002-6204-7117 
primary 'Schopfer, U.'      25 ?                   
primary 'Jager, P.'         26 ?                   
primary 'Wack, N.'          27 ?                   
primary 'Hasler, F.'        28 ?                   
primary 'Urban, B.'         29 ?                   
primary 'Sindelar, M.'      30 ?                   
primary 'Loetscher, P.'     31 ?                   
primary 'Kiffe, M.'         32 ?                   
primary 'Ren, X.'           33 ?                   
primary 'Nicklin, P.'       34 ?                   
primary 'White, K.'         35 ?                   
primary 'Subramanian, K.'   36 ?                   
primary 'Liu, H.'           37 ?                   
primary 'Growcott, E.J.'    38 ?                   
primary 'Rohn, T.A.'        39 ?                   
# 
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 'Leukotriene C4 synthase'                                                                             17468.596 
1 4.4.1.20,2.5.1.- ? ? ? 
2 non-polymer syn 'PALMITIC ACID'                                                                                       256.424   
1 ?                ? ? ? 
3 non-polymer syn 'PALMITOLEIC ACID'                                                                                    254.408   
1 ?                ? ? ? 
4 non-polymer syn '1-(4-chloranyl-3-fluoranyl-phenyl)-9-[(~{E})-3-phenylprop-2-enoyl]-1,9-diazaspiro[5.5]undecan-2-one' 426.911   
1 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'LTC4 synthase,Glutathione S-transferase LTC4,Leukotriene-C(4) synthase,Leukotriene-C4 synthase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHGKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIF
FHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIF
FHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PALMITIC ACID'                                                                                       PLM   
3 'PALMITOLEIC ACID'                                                                                    PAM   
4 '1-(4-chloranyl-3-fluoranyl-phenyl)-9-[(~{E})-3-phenylprop-2-enoyl]-1,9-diazaspiro[5.5]undecan-2-one' A1IH0 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   LYS n 
1 10  ASP n 
1 11  GLU n 
1 12  VAL n 
1 13  ALA n 
1 14  LEU n 
1 15  LEU n 
1 16  ALA n 
1 17  ALA n 
1 18  VAL n 
1 19  THR n 
1 20  LEU n 
1 21  LEU n 
1 22  GLY n 
1 23  VAL n 
1 24  LEU n 
1 25  LEU n 
1 26  GLN n 
1 27  ALA n 
1 28  TYR n 
1 29  PHE n 
1 30  SER n 
1 31  LEU n 
1 32  GLN n 
1 33  VAL n 
1 34  ILE n 
1 35  SER n 
1 36  ALA n 
1 37  ARG n 
1 38  ARG n 
1 39  ALA n 
1 40  PHE n 
1 41  ARG n 
1 42  VAL n 
1 43  SER n 
1 44  PRO n 
1 45  PRO n 
1 46  LEU n 
1 47  THR n 
1 48  THR n 
1 49  GLY n 
1 50  PRO n 
1 51  PRO n 
1 52  GLU n 
1 53  PHE n 
1 54  GLU n 
1 55  ARG n 
1 56  VAL n 
1 57  TYR n 
1 58  ARG n 
1 59  ALA n 
1 60  GLN n 
1 61  VAL n 
1 62  ASN n 
1 63  CYS n 
1 64  SER n 
1 65  GLU n 
1 66  TYR n 
1 67  PHE n 
1 68  PRO n 
1 69  LEU n 
1 70  PHE n 
1 71  LEU n 
1 72  ALA n 
1 73  THR n 
1 74  LEU n 
1 75  TRP n 
1 76  VAL n 
1 77  ALA n 
1 78  GLY n 
1 79  ILE n 
1 80  PHE n 
1 81  PHE n 
1 82  HIS n 
1 83  GLU n 
1 84  GLY n 
1 85  ALA n 
1 86  ALA n 
1 87  ALA n 
1 88  LEU n 
1 89  CYS n 
1 90  GLY n 
1 91  LEU n 
1 92  VAL n 
1 93  TYR n 
1 94  LEU n 
1 95  PHE n 
1 96  ALA n 
1 97  ARG n 
1 98  LEU n 
1 99  ARG n 
1 100 TYR n 
1 101 PHE n 
1 102 GLN n 
1 103 GLY n 
1 104 TYR n 
1 105 ALA n 
1 106 ARG n 
1 107 SER n 
1 108 ALA n 
1 109 GLN n 
1 110 LEU n 
1 111 ARG n 
1 112 LEU n 
1 113 ALA n 
1 114 PRO n 
1 115 LEU n 
1 116 TYR n 
1 117 ALA n 
1 118 SER n 
1 119 ALA n 
1 120 ARG n 
1 121 ALA n 
1 122 LEU n 
1 123 TRP n 
1 124 LEU n 
1 125 LEU n 
1 126 VAL n 
1 127 ALA n 
1 128 LEU n 
1 129 ALA n 
1 130 ALA n 
1 131 LEU n 
1 132 GLY n 
1 133 LEU n 
1 134 LEU n 
1 135 ALA n 
1 136 HIS n 
1 137 PHE n 
1 138 LEU n 
1 139 PRO n 
1 140 ALA n 
1 141 ALA n 
1 142 LEU n 
1 143 ARG n 
1 144 ALA n 
1 145 ALA n 
1 146 LEU n 
1 147 LEU n 
1 148 GLY n 
1 149 ARG n 
1 150 LEU n 
1 151 ARG n 
1 152 THR n 
1 153 LEU n 
1 154 LEU n 
1 155 PRO n 
1 156 TRP n 
1 157 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   157 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LTC4S 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      Pichia 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4919 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IH0 non-polymer         . '1-(4-chloranyl-3-fluoranyl-phenyl)-9-[(~{E})-3-phenylprop-2-enoyl]-1,9-diazaspiro[5.5]undecan-2-one' 
? 'C24 H24 Cl F N2 O2' 426.911 
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 
PAM   non-polymer         . 'PALMITOLEIC ACID'                                                                                    
? 'C16 H30 O2'         254.408 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                         
? 'C9 H11 N O2'        165.189 
PLM   non-polymer         . 'PALMITIC ACID'                                                                                       
? 'C16 H32 O2'         256.424 
PRO   'L-peptide linking' y PROLINE                                                                                               
? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE                                                                                                
? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE                                                                                             
? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                            
? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                              
? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE                                                                                                
? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -6  ?   ?   ?   A . n 
A 1 2   HIS 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   GLY 8   1   1   GLY GLY A . n 
A 1 9   LYS 9   2   2   LYS LYS A . n 
A 1 10  ASP 10  3   3   ASP ASP A . n 
A 1 11  GLU 11  4   4   GLU GLU A . n 
A 1 12  VAL 12  5   5   VAL VAL A . n 
A 1 13  ALA 13  6   6   ALA ALA A . n 
A 1 14  LEU 14  7   7   LEU LEU A . n 
A 1 15  LEU 15  8   8   LEU LEU A . n 
A 1 16  ALA 16  9   9   ALA ALA A . n 
A 1 17  ALA 17  10  10  ALA ALA A . n 
A 1 18  VAL 18  11  11  VAL VAL A . n 
A 1 19  THR 19  12  12  THR THR A . n 
A 1 20  LEU 20  13  13  LEU LEU A . n 
A 1 21  LEU 21  14  14  LEU LEU A . n 
A 1 22  GLY 22  15  15  GLY GLY A . n 
A 1 23  VAL 23  16  16  VAL VAL A . n 
A 1 24  LEU 24  17  17  LEU LEU A . n 
A 1 25  LEU 25  18  18  LEU LEU A . n 
A 1 26  GLN 26  19  19  GLN GLN A . n 
A 1 27  ALA 27  20  20  ALA ALA A . n 
A 1 28  TYR 28  21  21  TYR TYR A . n 
A 1 29  PHE 29  22  22  PHE PHE A . n 
A 1 30  SER 30  23  23  SER SER A . n 
A 1 31  LEU 31  24  24  LEU LEU A . n 
A 1 32  GLN 32  25  25  GLN GLN A . n 
A 1 33  VAL 33  26  26  VAL VAL A . n 
A 1 34  ILE 34  27  27  ILE ILE A . n 
A 1 35  SER 35  28  28  SER SER A . n 
A 1 36  ALA 36  29  29  ALA ALA A . n 
A 1 37  ARG 37  30  30  ARG ARG A . n 
A 1 38  ARG 38  31  31  ARG ARG A . n 
A 1 39  ALA 39  32  32  ALA ALA A . n 
A 1 40  PHE 40  33  33  PHE PHE A . n 
A 1 41  ARG 41  34  34  ARG ARG A . n 
A 1 42  VAL 42  35  35  VAL VAL A . n 
A 1 43  SER 43  36  36  SER SER A . n 
A 1 44  PRO 44  37  37  PRO PRO A . n 
A 1 45  PRO 45  38  38  PRO PRO A . n 
A 1 46  LEU 46  39  39  LEU LEU A . n 
A 1 47  THR 47  40  40  THR THR A . n 
A 1 48  THR 48  41  41  THR THR A . n 
A 1 49  GLY 49  42  42  GLY GLY A . n 
A 1 50  PRO 50  43  43  PRO PRO A . n 
A 1 51  PRO 51  44  44  PRO PRO A . n 
A 1 52  GLU 52  45  45  GLU GLU A . n 
A 1 53  PHE 53  46  46  PHE PHE A . n 
A 1 54  GLU 54  47  47  GLU GLU A . n 
A 1 55  ARG 55  48  48  ARG ARG A . n 
A 1 56  VAL 56  49  49  VAL VAL A . n 
A 1 57  TYR 57  50  50  TYR TYR A . n 
A 1 58  ARG 58  51  51  ARG ARG A . n 
A 1 59  ALA 59  52  52  ALA ALA A . n 
A 1 60  GLN 60  53  53  GLN GLN A . n 
A 1 61  VAL 61  54  54  VAL VAL A . n 
A 1 62  ASN 62  55  55  ASN ASN A . n 
A 1 63  CYS 63  56  56  CYS CYS A . n 
A 1 64  SER 64  57  57  SER SER A . n 
A 1 65  GLU 65  58  58  GLU GLU A . n 
A 1 66  TYR 66  59  59  TYR TYR A . n 
A 1 67  PHE 67  60  60  PHE PHE A . n 
A 1 68  PRO 68  61  61  PRO PRO A . n 
A 1 69  LEU 69  62  62  LEU LEU A . n 
A 1 70  PHE 70  63  63  PHE PHE A . n 
A 1 71  LEU 71  64  64  LEU LEU A . n 
A 1 72  ALA 72  65  65  ALA ALA A . n 
A 1 73  THR 73  66  66  THR THR A . n 
A 1 74  LEU 74  67  67  LEU LEU A . n 
A 1 75  TRP 75  68  68  TRP TRP A . n 
A 1 76  VAL 76  69  69  VAL VAL A . n 
A 1 77  ALA 77  70  70  ALA ALA A . n 
A 1 78  GLY 78  71  71  GLY GLY A . n 
A 1 79  ILE 79  72  72  ILE ILE A . n 
A 1 80  PHE 80  73  73  PHE PHE A . n 
A 1 81  PHE 81  74  74  PHE PHE A . n 
A 1 82  HIS 82  75  75  HIS HIS A . n 
A 1 83  GLU 83  76  76  GLU GLU A . n 
A 1 84  GLY 84  77  77  GLY GLY A . n 
A 1 85  ALA 85  78  78  ALA ALA A . n 
A 1 86  ALA 86  79  79  ALA ALA A . n 
A 1 87  ALA 87  80  80  ALA ALA A . n 
A 1 88  LEU 88  81  81  LEU LEU A . n 
A 1 89  CYS 89  82  82  CYS CYS A . n 
A 1 90  GLY 90  83  83  GLY GLY A . n 
A 1 91  LEU 91  84  84  LEU LEU A . n 
A 1 92  VAL 92  85  85  VAL VAL A . n 
A 1 93  TYR 93  86  86  TYR TYR A . n 
A 1 94  LEU 94  87  87  LEU LEU A . n 
A 1 95  PHE 95  88  88  PHE PHE A . n 
A 1 96  ALA 96  89  89  ALA ALA A . n 
A 1 97  ARG 97  90  90  ARG ARG A . n 
A 1 98  LEU 98  91  91  LEU LEU A . n 
A 1 99  ARG 99  92  92  ARG ARG A . n 
A 1 100 TYR 100 93  93  TYR TYR A . n 
A 1 101 PHE 101 94  94  PHE PHE A . n 
A 1 102 GLN 102 95  95  GLN GLN A . n 
A 1 103 GLY 103 96  96  GLY GLY A . n 
A 1 104 TYR 104 97  97  TYR TYR A . n 
A 1 105 ALA 105 98  98  ALA ALA A . n 
A 1 106 ARG 106 99  99  ARG ARG A . n 
A 1 107 SER 107 100 100 SER SER A . n 
A 1 108 ALA 108 101 101 ALA ALA A . n 
A 1 109 GLN 109 102 102 GLN GLN A . n 
A 1 110 LEU 110 103 103 LEU LEU A . n 
A 1 111 ARG 111 104 104 ARG ARG A . n 
A 1 112 LEU 112 105 105 LEU LEU A . n 
A 1 113 ALA 113 106 106 ALA ALA A . n 
A 1 114 PRO 114 107 107 PRO PRO A . n 
A 1 115 LEU 115 108 108 LEU LEU A . n 
A 1 116 TYR 116 109 109 TYR TYR A . n 
A 1 117 ALA 117 110 110 ALA ALA A . n 
A 1 118 SER 118 111 111 SER SER A . n 
A 1 119 ALA 119 112 112 ALA ALA A . n 
A 1 120 ARG 120 113 113 ARG ARG A . n 
A 1 121 ALA 121 114 114 ALA ALA A . n 
A 1 122 LEU 122 115 115 LEU LEU A . n 
A 1 123 TRP 123 116 116 TRP TRP A . n 
A 1 124 LEU 124 117 117 LEU LEU A . n 
A 1 125 LEU 125 118 118 LEU LEU A . n 
A 1 126 VAL 126 119 119 VAL VAL A . n 
A 1 127 ALA 127 120 120 ALA ALA A . n 
A 1 128 LEU 128 121 121 LEU LEU A . n 
A 1 129 ALA 129 122 122 ALA ALA A . n 
A 1 130 ALA 130 123 123 ALA ALA A . n 
A 1 131 LEU 131 124 124 LEU LEU A . n 
A 1 132 GLY 132 125 125 GLY GLY A . n 
A 1 133 LEU 133 126 126 LEU LEU A . n 
A 1 134 LEU 134 127 127 LEU LEU A . n 
A 1 135 ALA 135 128 128 ALA ALA A . n 
A 1 136 HIS 136 129 129 HIS HIS A . n 
A 1 137 PHE 137 130 130 PHE PHE A . n 
A 1 138 LEU 138 131 131 LEU LEU A . n 
A 1 139 PRO 139 132 132 PRO PRO A . n 
A 1 140 ALA 140 133 133 ALA ALA A . n 
A 1 141 ALA 141 134 134 ALA ALA A . n 
A 1 142 LEU 142 135 135 LEU LEU A . n 
A 1 143 ARG 143 136 136 ARG ARG A . n 
A 1 144 ALA 144 137 137 ALA ALA A . n 
A 1 145 ALA 145 138 138 ALA ALA A . n 
A 1 146 LEU 146 139 139 LEU LEU A . n 
A 1 147 LEU 147 140 140 LEU LEU A . n 
A 1 148 GLY 148 141 141 GLY GLY A . n 
A 1 149 ARG 149 142 142 ARG ARG A . n 
A 1 150 LEU 150 143 143 LEU LEU A . n 
A 1 151 ARG 151 144 ?   ?   ?   A . n 
A 1 152 THR 152 145 ?   ?   ?   A . n 
A 1 153 LEU 153 146 ?   ?   ?   A . n 
A 1 154 LEU 154 147 ?   ?   ?   A . n 
A 1 155 PRO 155 148 ?   ?   ?   A . n 
A 1 156 TRP 156 149 ?   ?   ?   A . n 
A 1 157 ALA 157 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IH0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IH0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PLM   1 201 909  PLM   PLM A . 
C 3 PAM   1 202 1002 PAM   PAM A . 
D 4 A1IH0 1 203 1    A1IH0 LI1 A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LEU 121 ? CD2 ? A LEU 128 CD2 
2  1 Y 1 A ARG 142 ? CG  ? A ARG 149 CG  
3  1 Y 1 A ARG 142 ? CD  ? A ARG 149 CD  
4  1 Y 1 A ARG 142 ? NE  ? A ARG 149 NE  
5  1 Y 1 A ARG 142 ? CZ  ? A ARG 149 CZ  
6  1 Y 1 A ARG 142 ? NH1 ? A ARG 149 NH1 
7  1 Y 1 A ARG 142 ? NH2 ? A ARG 149 NH2 
8  1 N 1 A PLM 201 ? C1  ? B PLM 1   C1  
9  1 N 1 A PLM 201 ? O1  ? B PLM 1   O1  
10 1 N 1 A PLM 201 ? O2  ? B PLM 1   O2  
11 1 N 1 A PLM 201 ? C2  ? B PLM 1   C2  
12 1 N 1 A PLM 201 ? C3  ? B PLM 1   C3  
13 1 N 1 A PLM 201 ? C4  ? B PLM 1   C4  
14 1 N 1 A PLM 201 ? C5  ? B PLM 1   C5  
15 1 N 1 A PAM 202 ? C1  ? C PAM 1   C1  
16 1 N 1 A PAM 202 ? O1  ? C PAM 1   O1  
17 1 N 1 A PAM 202 ? O2  ? C PAM 1   O2  
18 1 N 1 A PAM 202 ? C2  ? C PAM 1   C2  
19 1 N 1 A PAM 202 ? C3  ? C PAM 1   C3  
20 1 N 1 A PAM 202 ? C4  ? C PAM 1   C4  
21 1 N 1 A PAM 202 ? C5  ? C PAM 1   C5  
22 1 N 1 A PAM 202 ? C6  ? C PAM 1   C6  
23 1 N 1 A PAM 202 ? C7  ? C PAM 1   C7  
24 1 N 1 A PAM 202 ? C8  ? C PAM 1   C8  
25 1 N 1 A PAM 202 ? C9  ? C PAM 1   C9  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 2.11.5 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .      4 
# 
_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                     9G1T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     170.352 
_cell.length_a_esd                 ? 
_cell.length_b                     170.352 
_cell.length_b_esd                 ? 
_cell.length_c                     170.352 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9G1T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                196 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 2 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G1T 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             5.90 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          79.14 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10 % PEG8000, LITHIUM SULPHATE  0.5M' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-11-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G1T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.0 
_reflns.d_resolution_low                               28.8 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     8328 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          32.61 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.058 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.057 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
3.00  3.08  ? ? ? ? ? ? 611 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.727 ? ? 1  1 0.638 ? ? ? ? 2.662 ? ? ? ? ? ? ? ? ? 
3.08  3.16  ? ? ? ? ? ? 599 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.063 ? ? 2  1 0.68  ? ? ? ? 2.014 ? ? ? ? ? ? ? ? ? 
3.16  3.25  ? ? ? ? ? ? 578 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.538 ? ? 3  1 0.828 ? ? ? ? 1.501 ? ? ? ? ? ? ? ? ? 
3.25  3.35  ? ? ? ? ? ? 554 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.934 ? ? 4  1 0.906 ? ? ? ? 0.911 ? ? ? ? ? ? ? ? ? 
3.35  3.46  ? ? ? ? ? ? 555 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.709 ? ? 5  1 0.936 ? ? ? ? 0.69  ? ? ? ? ? ? ? ? ? 
3.46  3.59  ? ? ? ? ? ? 528 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.454 ? ? 6  1 0.965 ? ? ? ? 0.442 ? ? ? ? ? ? ? ? ? 
3.59  3.72  ? ? ? ? ? ? 505 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.276 ? ? 7  1 0.991 ? ? ? ? 0.269 ? ? ? ? ? ? ? ? ? 
3.72  3.87  ? ? ? ? ? ? 487 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.178 ? ? 8  1 0.996 ? ? ? ? 0.173 ? ? ? ? ? ? ? ? ? 
3.87  4.05  ? ? ? ? ? ? 465 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.117 ? ? 9  1 0.998 ? ? ? ? 0.114 ? ? ? ? ? ? ? ? ? 
4.05  4.24  ? ? ? ? ? ? 450 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.076 ? ? 10 1 0.999 ? ? ? ? 0.074 ? ? ? ? ? ? ? ? ? 
4.24  4.47  ? ? ? ? ? ? 446 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.052 ? ? 11 1 1.0   ? ? ? ? 0.051 ? ? ? ? ? ? ? ? ? 
4.47  4.74  ? ? ? ? ? ? 401 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.045 ? ? 12 1 1.0   ? ? ? ? 0.044 ? ? ? ? ? ? ? ? ? 
4.74  5.07  ? ? ? ? ? ? 381 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.046 ? ? 13 1 1.0   ? ? ? ? 0.045 ? ? ? ? ? ? ? ? ? 
5.07  5.48  ? ? ? ? ? ? 368 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.045 ? ? 14 1 1.0   ? ? ? ? 0.044 ? ? ? ? ? ? ? ? ? 
5.48  6.0   ? ? ? ? ? ? 321 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.047 ? ? 15 1 0.999 ? ? ? ? 0.046 ? ? ? ? ? ? ? ? ? 
6.00  6.71  ? ? ? ? ? ? 302 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.045 ? ? 16 1 0.999 ? ? ? ? 0.043 ? ? ? ? ? ? ? ? ? 
6.71  7.75  ? ? ? ? ? ? 270 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.035 ? ? 17 1 1.0   ? ? ? ? 0.034 ? ? ? ? ? ? ? ? ? 
7.75  9.49  ? ? ? ? ? ? 231 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03  ? ? 18 1 1.0   ? ? ? ? 0.03  ? ? ? ? ? ? ? ? ? 
9.49  13.42 ? ? ? ? ? ? 179 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.029 ? ? 19 1 1.0   ? ? ? ? 0.028 ? ? ? ? ? ? ? ? ? 
13.42 14    ? ? ? ? ? ? 97  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03  ? ? 20 1 1.0   ? ? ? ? 0.029 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.0000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               155.92 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.9426 
_refine.correlation_coeff_Fo_to_Fc_free          0.9422 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G1T 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.00 
_refine.ls_d_res_low                             19.89 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     8264 
_refine.ls_number_reflns_R_free                  414 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2115 
_refine.ls_R_factor_R_free                       0.2428 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2098 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.278 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.268 
_refine.pdbx_overall_SU_R_Blow_DPI               0.350 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.371 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9G1T 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.999 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        19.89 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               1169 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1121 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010 ? 1214 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.09  ? 1641 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 400  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 12   ? t_trig_c_planes           2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 183  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1214 ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.71  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 24.56 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 141  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1436 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.00 
_refine_ls_shell.d_res_low                        3.35 
_refine_ls_shell.number_reflns_all                2295 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             116 
_refine_ls_shell.number_reflns_R_work             2179 
_refine_ls_shell.percent_reflns_obs               99.49 
_refine_ls_shell.percent_reflns_R_free            5.05 
_refine_ls_shell.R_factor_all                     0.2887 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2881 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   5 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2996 
# 
_struct.entry_id                     9G1T 
_struct.title                        'Human LTC4 synthase in complex with compound 5' 
_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        9G1T 
_struct_keywords.text            'LTC4S, Inhibitor, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LTC4S_HUMAN 
_struct_ref.pdbx_db_accession          Q16873 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAAL
CGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9G1T 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 157 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q16873 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  150 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
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 9G1T MET A 1 ? UNP Q16873 ? ? 'initiating methionine' -6 1 
1 9G1T HIS A 2 ? UNP Q16873 ? ? 'expression tag'        -5 2 
1 9G1T HIS A 3 ? UNP Q16873 ? ? 'expression tag'        -4 3 
1 9G1T HIS A 4 ? UNP Q16873 ? ? 'expression tag'        -3 4 
1 9G1T HIS A 5 ? UNP Q16873 ? ? 'expression tag'        -2 5 
1 9G1T HIS A 6 ? UNP Q16873 ? ? 'expression tag'        -1 6 
1 9G1T HIS A 7 ? UNP Q16873 ? ? 'expression tag'        0  7 
1 9G1T GLY A 8 ? UNP Q16873 ? ? 'expression tag'        1  8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9070  ? 
1 MORE         -71   ? 
1 'SSA (A^2)'  19330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                
;NOTE: THERE IS 1 MOLECULES OF LTC4S-INHIBITOR COMPLEX IN ASYMMETRIC UNIT. BIOLOGICAL UNIT OF TRIMER CAN BE GENERATED BY DISPLAYING SYMMETRY EQUIVALENT MOLECULES.
;
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000 0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000 0.0000000000    
2 'crystal symmetry operation' 5_636 z+1,x-2,y+1 0.0000000000 0.0000000000 1.0000000000 170.3520000000 1.0000000000 0.0000000000 
0.0000000000 -340.7040000000 0.0000000000 1.0000000000 0.0000000000 170.3520000000  
3 'crystal symmetry operation' 9_744 y+2,z-1,x-1 0.0000000000 1.0000000000 0.0000000000 340.7040000000 0.0000000000 0.0000000000 
1.0000000000 -170.3520000000 1.0000000000 0.0000000000 0.0000000000 -170.3520000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 LYS A 9   ? GLU A 11  ? LYS A 2   GLU A 4   5 ? 3  
HELX_P HELX_P2 AA2 VAL A 12  ? ALA A 39  ? VAL A 5   ALA A 32  1 ? 28 
HELX_P HELX_P3 AA3 GLU A 52  ? PHE A 81  ? GLU A 45  PHE A 74  1 ? 30 
HELX_P HELX_P4 AA4 HIS A 82  ? ALA A 105 ? HIS A 75  ALA A 98  1 ? 24 
HELX_P HELX_P5 AA5 ARG A 111 ? LEU A 146 ? ARG A 104 LEU A 139 1 ? 36 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           44 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            37 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    45 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     38 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       9.63 
# 
_pdbx_entry_details.entry_id                   9G1T 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 38  ? ? -89.91  36.08  
2 1 PRO A 44  ? ? -65.79  6.18   
3 1 ARG A 99  ? ? -105.42 -91.50 
4 1 ARG A 142 ? ? -138.33 -43.95 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         355.7880 
_pdbx_refine_tls.origin_y         16.3504 
_pdbx_refine_tls.origin_z         199.1590 
_pdbx_refine_tls.T[1][1]          -0.3688 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.4560 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.1091 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.4261 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.2253 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.4443 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          4.9972 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          1.8102 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          2.0207 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          7.9393 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          3.4394 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          7.1118 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.5199 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.7450 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.5987 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          1.1797 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.7068 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.9302 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          1.5251 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -1.2911 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1869 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
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 MET -6  ? A MET 1   
2  1 Y 1 A HIS -5  ? A HIS 2   
3  1 Y 1 A HIS -4  ? A HIS 3   
4  1 Y 1 A HIS -3  ? A HIS 4   
5  1 Y 1 A HIS -2  ? A HIS 5   
6  1 Y 1 A HIS -1  ? A HIS 6   
7  1 Y 1 A HIS 0   ? A HIS 7   
8  1 Y 1 A ARG 144 ? A ARG 151 
9  1 Y 1 A THR 145 ? A THR 152 
10 1 Y 1 A LEU 146 ? A LEU 153 
11 1 Y 1 A LEU 147 ? A LEU 154 
12 1 Y 1 A PRO 148 ? A PRO 155 
13 1 Y 1 A TRP 149 ? A TRP 156 
14 1 Y 1 A ALA 150 ? A ALA 157 
# 
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 
A1IH0 C1   C  N N 1   
A1IH0 C2   C  N N 2   
A1IH0 C11  C  N N 3   
A1IH0 C13  C  Y N 4   
A1IH0 C14  C  N N 5   
A1IH0 C16  C  N N 6   
A1IH0 C17  C  N N 7   
A1IH0 C18  C  Y N 8   
A1IH0 C19  C  Y N 9   
A1IH0 C20  C  Y N 10  
A1IH0 C21  C  Y N 11  
A1IH0 C22  C  Y N 12  
A1IH0 C23  C  Y N 13  
A1IH0 C24  C  Y N 14  
A1IH0 C25  C  Y N 15  
A1IH0 C26  C  Y N 16  
A1IH0 C27  C  Y N 17  
A1IH0 C28  C  Y N 18  
A1IH0 N3   N  N N 19  
A1IH0 C4   C  N N 20  
A1IH0 C5   C  N N 21  
A1IH0 C6   C  N N 22  
A1IH0 N7   N  N N 23  
A1IH0 C8   C  N N 24  
A1IH0 C9   C  N N 25  
A1IH0 C10  C  N N 26  
A1IH0 O12  O  N N 27  
A1IH0 O15  O  N N 28  
A1IH0 CL29 CL N N 29  
A1IH0 F30  F  N N 30  
A1IH0 H1   H  N N 31  
A1IH0 H2   H  N N 32  
A1IH0 H3   H  N N 33  
A1IH0 H4   H  N N 34  
A1IH0 H5   H  N N 35  
A1IH0 H6   H  N N 36  
A1IH0 H7   H  N N 37  
A1IH0 H8   H  N N 38  
A1IH0 H9   H  N N 39  
A1IH0 H10  H  N N 40  
A1IH0 H11  H  N N 41  
A1IH0 H12  H  N N 42  
A1IH0 H13  H  N N 43  
A1IH0 H14  H  N N 44  
A1IH0 H15  H  N N 45  
A1IH0 H16  H  N N 46  
A1IH0 H17  H  N N 47  
A1IH0 H18  H  N N 48  
A1IH0 H19  H  N N 49  
A1IH0 H20  H  N N 50  
A1IH0 H21  H  N N 51  
A1IH0 H22  H  N N 52  
A1IH0 H23  H  N N 53  
A1IH0 H24  H  N N 54  
ALA   N    N  N N 55  
ALA   CA   C  N S 56  
ALA   C    C  N N 57  
ALA   O    O  N N 58  
ALA   CB   C  N N 59  
ALA   OXT  O  N N 60  
ALA   H    H  N N 61  
ALA   H2   H  N N 62  
ALA   HA   H  N N 63  
ALA   HB1  H  N N 64  
ALA   HB2  H  N N 65  
ALA   HB3  H  N N 66  
ALA   HXT  H  N N 67  
ARG   N    N  N N 68  
ARG   CA   C  N S 69  
ARG   C    C  N N 70  
ARG   O    O  N N 71  
ARG   CB   C  N N 72  
ARG   CG   C  N N 73  
ARG   CD   C  N N 74  
ARG   NE   N  N N 75  
ARG   CZ   C  N N 76  
ARG   NH1  N  N N 77  
ARG   NH2  N  N N 78  
ARG   OXT  O  N N 79  
ARG   H    H  N N 80  
ARG   H2   H  N N 81  
ARG   HA   H  N N 82  
ARG   HB2  H  N N 83  
ARG   HB3  H  N N 84  
ARG   HG2  H  N N 85  
ARG   HG3  H  N N 86  
ARG   HD2  H  N N 87  
ARG   HD3  H  N N 88  
ARG   HE   H  N N 89  
ARG   HH11 H  N N 90  
ARG   HH12 H  N N 91  
ARG   HH21 H  N N 92  
ARG   HH22 H  N N 93  
ARG   HXT  H  N N 94  
ASN   N    N  N N 95  
ASN   CA   C  N S 96  
ASN   C    C  N N 97  
ASN   O    O  N N 98  
ASN   CB   C  N N 99  
ASN   CG   C  N N 100 
ASN   OD1  O  N N 101 
ASN   ND2  N  N N 102 
ASN   OXT  O  N N 103 
ASN   H    H  N N 104 
ASN   H2   H  N N 105 
ASN   HA   H  N N 106 
ASN   HB2  H  N N 107 
ASN   HB3  H  N N 108 
ASN   HD21 H  N N 109 
ASN   HD22 H  N N 110 
ASN   HXT  H  N N 111 
ASP   N    N  N N 112 
ASP   CA   C  N S 113 
ASP   C    C  N N 114 
ASP   O    O  N N 115 
ASP   CB   C  N N 116 
ASP   CG   C  N N 117 
ASP   OD1  O  N N 118 
ASP   OD2  O  N N 119 
ASP   OXT  O  N N 120 
ASP   H    H  N N 121 
ASP   H2   H  N N 122 
ASP   HA   H  N N 123 
ASP   HB2  H  N N 124 
ASP   HB3  H  N N 125 
ASP   HD2  H  N N 126 
ASP   HXT  H  N N 127 
CYS   N    N  N N 128 
CYS   CA   C  N R 129 
CYS   C    C  N N 130 
CYS   O    O  N N 131 
CYS   CB   C  N N 132 
CYS   SG   S  N N 133 
CYS   OXT  O  N N 134 
CYS   H    H  N N 135 
CYS   H2   H  N N 136 
CYS   HA   H  N N 137 
CYS   HB2  H  N N 138 
CYS   HB3  H  N N 139 
CYS   HG   H  N N 140 
CYS   HXT  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PAM   C1   C  N N 301 
PAM   O1   O  N N 302 
PAM   O2   O  N N 303 
PAM   C2   C  N N 304 
PAM   C3   C  N N 305 
PAM   C4   C  N N 306 
PAM   C5   C  N N 307 
PAM   C6   C  N N 308 
PAM   C7   C  N N 309 
PAM   C8   C  N N 310 
PAM   C9   C  N N 311 
PAM   C10  C  N N 312 
PAM   C11  C  N N 313 
PAM   C12  C  N N 314 
PAM   C13  C  N N 315 
PAM   C14  C  N N 316 
PAM   C15  C  N N 317 
PAM   C16  C  N N 318 
PAM   HO1  H  N N 319 
PAM   H21  H  N N 320 
PAM   H22  H  N N 321 
PAM   H31  H  N N 322 
PAM   H32  H  N N 323 
PAM   H41  H  N N 324 
PAM   H42  H  N N 325 
PAM   H51  H  N N 326 
PAM   H52  H  N N 327 
PAM   H61  H  N N 328 
PAM   H62  H  N N 329 
PAM   H71  H  N N 330 
PAM   H72  H  N N 331 
PAM   H81  H  N N 332 
PAM   H82  H  N N 333 
PAM   H9   H  N N 334 
PAM   H10  H  N N 335 
PAM   H111 H  N N 336 
PAM   H112 H  N N 337 
PAM   H121 H  N N 338 
PAM   H122 H  N N 339 
PAM   H131 H  N N 340 
PAM   H132 H  N N 341 
PAM   H141 H  N N 342 
PAM   H142 H  N N 343 
PAM   H151 H  N N 344 
PAM   H152 H  N N 345 
PAM   H161 H  N N 346 
PAM   H162 H  N N 347 
PAM   H163 H  N N 348 
PHE   N    N  N N 349 
PHE   CA   C  N S 350 
PHE   C    C  N N 351 
PHE   O    O  N N 352 
PHE   CB   C  N N 353 
PHE   CG   C  Y N 354 
PHE   CD1  C  Y N 355 
PHE   CD2  C  Y N 356 
PHE   CE1  C  Y N 357 
PHE   CE2  C  Y N 358 
PHE   CZ   C  Y N 359 
PHE   OXT  O  N N 360 
PHE   H    H  N N 361 
PHE   H2   H  N N 362 
PHE   HA   H  N N 363 
PHE   HB2  H  N N 364 
PHE   HB3  H  N N 365 
PHE   HD1  H  N N 366 
PHE   HD2  H  N N 367 
PHE   HE1  H  N N 368 
PHE   HE2  H  N N 369 
PHE   HZ   H  N N 370 
PHE   HXT  H  N N 371 
PLM   C1   C  N N 372 
PLM   O1   O  N N 373 
PLM   O2   O  N N 374 
PLM   C2   C  N N 375 
PLM   C3   C  N N 376 
PLM   C4   C  N N 377 
PLM   C5   C  N N 378 
PLM   C6   C  N N 379 
PLM   C7   C  N N 380 
PLM   C8   C  N N 381 
PLM   C9   C  N N 382 
PLM   CA   C  N N 383 
PLM   CB   C  N N 384 
PLM   CC   C  N N 385 
PLM   CD   C  N N 386 
PLM   CE   C  N N 387 
PLM   CF   C  N N 388 
PLM   CG   C  N N 389 
PLM   H    H  N N 390 
PLM   H21  H  N N 391 
PLM   H22  H  N N 392 
PLM   H31  H  N N 393 
PLM   H32  H  N N 394 
PLM   H41  H  N N 395 
PLM   H42  H  N N 396 
PLM   H51  H  N N 397 
PLM   H52  H  N N 398 
PLM   H61  H  N N 399 
PLM   H62  H  N N 400 
PLM   H71  H  N N 401 
PLM   H72  H  N N 402 
PLM   H81  H  N N 403 
PLM   H82  H  N N 404 
PLM   H91  H  N N 405 
PLM   H92  H  N N 406 
PLM   HA1  H  N N 407 
PLM   HA2  H  N N 408 
PLM   HB1  H  N N 409 
PLM   HB2  H  N N 410 
PLM   HC1  H  N N 411 
PLM   HC2  H  N N 412 
PLM   HD1  H  N N 413 
PLM   HD2  H  N N 414 
PLM   HE1  H  N N 415 
PLM   HE2  H  N N 416 
PLM   HF1  H  N N 417 
PLM   HF2  H  N N 418 
PLM   HG1  H  N N 419 
PLM   HG2  H  N N 420 
PLM   HG3  H  N N 421 
PRO   N    N  N N 422 
PRO   CA   C  N S 423 
PRO   C    C  N N 424 
PRO   O    O  N N 425 
PRO   CB   C  N N 426 
PRO   CG   C  N N 427 
PRO   CD   C  N N 428 
PRO   OXT  O  N N 429 
PRO   H    H  N N 430 
PRO   HA   H  N N 431 
PRO   HB2  H  N N 432 
PRO   HB3  H  N N 433 
PRO   HG2  H  N N 434 
PRO   HG3  H  N N 435 
PRO   HD2  H  N N 436 
PRO   HD3  H  N N 437 
PRO   HXT  H  N N 438 
SER   N    N  N N 439 
SER   CA   C  N S 440 
SER   C    C  N N 441 
SER   O    O  N N 442 
SER   CB   C  N N 443 
SER   OG   O  N N 444 
SER   OXT  O  N N 445 
SER   H    H  N N 446 
SER   H2   H  N N 447 
SER   HA   H  N N 448 
SER   HB2  H  N N 449 
SER   HB3  H  N N 450 
SER   HG   H  N N 451 
SER   HXT  H  N N 452 
THR   N    N  N N 453 
THR   CA   C  N S 454 
THR   C    C  N N 455 
THR   O    O  N N 456 
THR   CB   C  N R 457 
THR   OG1  O  N N 458 
THR   CG2  C  N N 459 
THR   OXT  O  N N 460 
THR   H    H  N N 461 
THR   H2   H  N N 462 
THR   HA   H  N N 463 
THR   HB   H  N N 464 
THR   HG1  H  N N 465 
THR   HG21 H  N N 466 
THR   HG22 H  N N 467 
THR   HG23 H  N N 468 
THR   HXT  H  N N 469 
TRP   N    N  N N 470 
TRP   CA   C  N S 471 
TRP   C    C  N N 472 
TRP   O    O  N N 473 
TRP   CB   C  N N 474 
TRP   CG   C  Y N 475 
TRP   CD1  C  Y N 476 
TRP   CD2  C  Y N 477 
TRP   NE1  N  Y N 478 
TRP   CE2  C  Y N 479 
TRP   CE3  C  Y N 480 
TRP   CZ2  C  Y N 481 
TRP   CZ3  C  Y N 482 
TRP   CH2  C  Y N 483 
TRP   OXT  O  N N 484 
TRP   H    H  N N 485 
TRP   H2   H  N N 486 
TRP   HA   H  N N 487 
TRP   HB2  H  N N 488 
TRP   HB3  H  N N 489 
TRP   HD1  H  N N 490 
TRP   HE1  H  N N 491 
TRP   HE3  H  N N 492 
TRP   HZ2  H  N N 493 
TRP   HZ3  H  N N 494 
TRP   HH2  H  N N 495 
TRP   HXT  H  N N 496 
TYR   N    N  N N 497 
TYR   CA   C  N S 498 
TYR   C    C  N N 499 
TYR   O    O  N N 500 
TYR   CB   C  N N 501 
TYR   CG   C  Y N 502 
TYR   CD1  C  Y N 503 
TYR   CD2  C  Y N 504 
TYR   CE1  C  Y N 505 
TYR   CE2  C  Y N 506 
TYR   CZ   C  Y N 507 
TYR   OH   O  N N 508 
TYR   OXT  O  N N 509 
TYR   H    H  N N 510 
TYR   H2   H  N N 511 
TYR   HA   H  N N 512 
TYR   HB2  H  N N 513 
TYR   HB3  H  N N 514 
TYR   HD1  H  N N 515 
TYR   HD2  H  N N 516 
TYR   HE1  H  N N 517 
TYR   HE2  H  N N 518 
TYR   HH   H  N N 519 
TYR   HXT  H  N N 520 
VAL   N    N  N N 521 
VAL   CA   C  N S 522 
VAL   C    C  N N 523 
VAL   O    O  N N 524 
VAL   CB   C  N N 525 
VAL   CG1  C  N N 526 
VAL   CG2  C  N N 527 
VAL   OXT  O  N N 528 
VAL   H    H  N N 529 
VAL   H2   H  N N 530 
VAL   HA   H  N N 531 
VAL   HB   H  N N 532 
VAL   HG11 H  N N 533 
VAL   HG12 H  N N 534 
VAL   HG13 H  N N 535 
VAL   HG21 H  N N 536 
VAL   HG22 H  N N 537 
VAL   HG23 H  N N 538 
VAL   HXT  H  N N 539 
# 
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 
A1IH0 C20 C21  doub Y N 1   
A1IH0 C20 C19  sing Y N 2   
A1IH0 C21 C22  sing Y N 3   
A1IH0 C19 C18  doub Y N 4   
A1IH0 C22 C23  doub Y N 5   
A1IH0 C18 C23  sing Y N 6   
A1IH0 C18 C17  sing N N 7   
A1IH0 C4  C5   sing N N 8   
A1IH0 C4  N3   sing N N 9   
A1IH0 C16 C17  doub N E 10  
A1IH0 C16 C14  sing N N 11  
A1IH0 C5  C6   sing N N 12  
A1IH0 F30 C27  sing N N 13  
A1IH0 C11 C10  sing N N 14  
A1IH0 C11 C6   sing N N 15  
A1IH0 C28 C27  doub Y N 16  
A1IH0 C28 C13  sing Y N 17  
A1IH0 N3  C14  sing N N 18  
A1IH0 N3  C2   sing N N 19  
A1IH0 C10 C9   sing N N 20  
A1IH0 C6  N7   sing N N 21  
A1IH0 C6  C1   sing N N 22  
A1IH0 C27 C26  sing Y N 23  
A1IH0 C14 O15  doub N N 24  
A1IH0 C9  C8   sing N N 25  
A1IH0 N7  C8   sing N N 26  
A1IH0 N7  C13  sing N N 27  
A1IH0 C8  O12  doub N N 28  
A1IH0 C13 C24  doub Y N 29  
A1IH0 C2  C1   sing N N 30  
A1IH0 C26 CL29 sing N N 31  
A1IH0 C26 C25  doub Y N 32  
A1IH0 C24 C25  sing Y N 33  
A1IH0 C1  H1   sing N N 34  
A1IH0 C1  H2   sing N N 35  
A1IH0 C2  H3   sing N N 36  
A1IH0 C2  H4   sing N N 37  
A1IH0 C11 H5   sing N N 38  
A1IH0 C11 H6   sing N N 39  
A1IH0 C16 H7   sing N N 40  
A1IH0 C17 H8   sing N N 41  
A1IH0 C19 H9   sing N N 42  
A1IH0 C20 H10  sing N N 43  
A1IH0 C21 H11  sing N N 44  
A1IH0 C22 H12  sing N N 45  
A1IH0 C23 H13  sing N N 46  
A1IH0 C24 H14  sing N N 47  
A1IH0 C25 H15  sing N N 48  
A1IH0 C28 H16  sing N N 49  
A1IH0 C4  H17  sing N N 50  
A1IH0 C4  H18  sing N N 51  
A1IH0 C5  H19  sing N N 52  
A1IH0 C5  H20  sing N N 53  
A1IH0 C9  H21  sing N N 54  
A1IH0 C9  H22  sing N N 55  
A1IH0 C10 H23  sing N N 56  
A1IH0 C10 H24  sing N N 57  
ALA   N   CA   sing N N 58  
ALA   N   H    sing N N 59  
ALA   N   H2   sing N N 60  
ALA   CA  C    sing N N 61  
ALA   CA  CB   sing N N 62  
ALA   CA  HA   sing N N 63  
ALA   C   O    doub N N 64  
ALA   C   OXT  sing N N 65  
ALA   CB  HB1  sing N N 66  
ALA   CB  HB2  sing N N 67  
ALA   CB  HB3  sing N N 68  
ALA   OXT HXT  sing N N 69  
ARG   N   CA   sing N N 70  
ARG   N   H    sing N N 71  
ARG   N   H2   sing N N 72  
ARG   CA  C    sing N N 73  
ARG   CA  CB   sing N N 74  
ARG   CA  HA   sing N N 75  
ARG   C   O    doub N N 76  
ARG   C   OXT  sing N N 77  
ARG   CB  CG   sing N N 78  
ARG   CB  HB2  sing N N 79  
ARG   CB  HB3  sing N N 80  
ARG   CG  CD   sing N N 81  
ARG   CG  HG2  sing N N 82  
ARG   CG  HG3  sing N N 83  
ARG   CD  NE   sing N N 84  
ARG   CD  HD2  sing N N 85  
ARG   CD  HD3  sing N N 86  
ARG   NE  CZ   sing N N 87  
ARG   NE  HE   sing N N 88  
ARG   CZ  NH1  sing N N 89  
ARG   CZ  NH2  doub N N 90  
ARG   NH1 HH11 sing N N 91  
ARG   NH1 HH12 sing N N 92  
ARG   NH2 HH21 sing N N 93  
ARG   NH2 HH22 sing N N 94  
ARG   OXT HXT  sing N N 95  
ASN   N   CA   sing N N 96  
ASN   N   H    sing N N 97  
ASN   N   H2   sing N N 98  
ASN   CA  C    sing N N 99  
ASN   CA  CB   sing N N 100 
ASN   CA  HA   sing N N 101 
ASN   C   O    doub N N 102 
ASN   C   OXT  sing N N 103 
ASN   CB  CG   sing N N 104 
ASN   CB  HB2  sing N N 105 
ASN   CB  HB3  sing N N 106 
ASN   CG  OD1  doub N N 107 
ASN   CG  ND2  sing N N 108 
ASN   ND2 HD21 sing N N 109 
ASN   ND2 HD22 sing N N 110 
ASN   OXT HXT  sing N N 111 
ASP   N   CA   sing N N 112 
ASP   N   H    sing N N 113 
ASP   N   H2   sing N N 114 
ASP   CA  C    sing N N 115 
ASP   CA  CB   sing N N 116 
ASP   CA  HA   sing N N 117 
ASP   C   O    doub N N 118 
ASP   C   OXT  sing N N 119 
ASP   CB  CG   sing N N 120 
ASP   CB  HB2  sing N N 121 
ASP   CB  HB3  sing N N 122 
ASP   CG  OD1  doub N N 123 
ASP   CG  OD2  sing N N 124 
ASP   OD2 HD2  sing N N 125 
ASP   OXT HXT  sing N N 126 
CYS   N   CA   sing N N 127 
CYS   N   H    sing N N 128 
CYS   N   H2   sing N N 129 
CYS   CA  C    sing N N 130 
CYS   CA  CB   sing N N 131 
CYS   CA  HA   sing N N 132 
CYS   C   O    doub N N 133 
CYS   C   OXT  sing N N 134 
CYS   CB  SG   sing N N 135 
CYS   CB  HB2  sing N N 136 
CYS   CB  HB3  sing N N 137 
CYS   SG  HG   sing N N 138 
CYS   OXT HXT  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PAM   C1  O1   sing N N 292 
PAM   C1  O2   doub N N 293 
PAM   C1  C2   sing N N 294 
PAM   O1  HO1  sing N N 295 
PAM   C2  C3   sing N N 296 
PAM   C2  H21  sing N N 297 
PAM   C2  H22  sing N N 298 
PAM   C3  C4   sing N N 299 
PAM   C3  H31  sing N N 300 
PAM   C3  H32  sing N N 301 
PAM   C4  C5   sing N N 302 
PAM   C4  H41  sing N N 303 
PAM   C4  H42  sing N N 304 
PAM   C5  C6   sing N N 305 
PAM   C5  H51  sing N N 306 
PAM   C5  H52  sing N N 307 
PAM   C6  C7   sing N N 308 
PAM   C6  H61  sing N N 309 
PAM   C6  H62  sing N N 310 
PAM   C7  C8   sing N N 311 
PAM   C7  H71  sing N N 312 
PAM   C7  H72  sing N N 313 
PAM   C8  C9   sing N N 314 
PAM   C8  H81  sing N N 315 
PAM   C8  H82  sing N N 316 
PAM   C9  C10  doub N Z 317 
PAM   C9  H9   sing N N 318 
PAM   C10 C11  sing N N 319 
PAM   C10 H10  sing N N 320 
PAM   C11 C12  sing N N 321 
PAM   C11 H111 sing N N 322 
PAM   C11 H112 sing N N 323 
PAM   C12 C13  sing N N 324 
PAM   C12 H121 sing N N 325 
PAM   C12 H122 sing N N 326 
PAM   C13 C14  sing N N 327 
PAM   C13 H131 sing N N 328 
PAM   C13 H132 sing N N 329 
PAM   C14 C15  sing N N 330 
PAM   C14 H141 sing N N 331 
PAM   C14 H142 sing N N 332 
PAM   C15 C16  sing N N 333 
PAM   C15 H151 sing N N 334 
PAM   C15 H152 sing N N 335 
PAM   C16 H161 sing N N 336 
PAM   C16 H162 sing N N 337 
PAM   C16 H163 sing N N 338 
PHE   N   CA   sing N N 339 
PHE   N   H    sing N N 340 
PHE   N   H2   sing N N 341 
PHE   CA  C    sing N N 342 
PHE   CA  CB   sing N N 343 
PHE   CA  HA   sing N N 344 
PHE   C   O    doub N N 345 
PHE   C   OXT  sing N N 346 
PHE   CB  CG   sing N N 347 
PHE   CB  HB2  sing N N 348 
PHE   CB  HB3  sing N N 349 
PHE   CG  CD1  doub Y N 350 
PHE   CG  CD2  sing Y N 351 
PHE   CD1 CE1  sing Y N 352 
PHE   CD1 HD1  sing N N 353 
PHE   CD2 CE2  doub Y N 354 
PHE   CD2 HD2  sing N N 355 
PHE   CE1 CZ   doub Y N 356 
PHE   CE1 HE1  sing N N 357 
PHE   CE2 CZ   sing Y N 358 
PHE   CE2 HE2  sing N N 359 
PHE   CZ  HZ   sing N N 360 
PHE   OXT HXT  sing N N 361 
PLM   C1  O1   sing N N 362 
PLM   C1  O2   doub N N 363 
PLM   C1  C2   sing N N 364 
PLM   O1  H    sing N N 365 
PLM   C2  C3   sing N N 366 
PLM   C2  H21  sing N N 367 
PLM   C2  H22  sing N N 368 
PLM   C3  C4   sing N N 369 
PLM   C3  H31  sing N N 370 
PLM   C3  H32  sing N N 371 
PLM   C4  C5   sing N N 372 
PLM   C4  H41  sing N N 373 
PLM   C4  H42  sing N N 374 
PLM   C5  C6   sing N N 375 
PLM   C5  H51  sing N N 376 
PLM   C5  H52  sing N N 377 
PLM   C6  C7   sing N N 378 
PLM   C6  H61  sing N N 379 
PLM   C6  H62  sing N N 380 
PLM   C7  C8   sing N N 381 
PLM   C7  H71  sing N N 382 
PLM   C7  H72  sing N N 383 
PLM   C8  C9   sing N N 384 
PLM   C8  H81  sing N N 385 
PLM   C8  H82  sing N N 386 
PLM   C9  CA   sing N N 387 
PLM   C9  H91  sing N N 388 
PLM   C9  H92  sing N N 389 
PLM   CA  CB   sing N N 390 
PLM   CA  HA1  sing N N 391 
PLM   CA  HA2  sing N N 392 
PLM   CB  CC   sing N N 393 
PLM   CB  HB1  sing N N 394 
PLM   CB  HB2  sing N N 395 
PLM   CC  CD   sing N N 396 
PLM   CC  HC1  sing N N 397 
PLM   CC  HC2  sing N N 398 
PLM   CD  CE   sing N N 399 
PLM   CD  HD1  sing N N 400 
PLM   CD  HD2  sing N N 401 
PLM   CE  CF   sing N N 402 
PLM   CE  HE1  sing N N 403 
PLM   CE  HE2  sing N N 404 
PLM   CF  CG   sing N N 405 
PLM   CF  HF1  sing N N 406 
PLM   CF  HF2  sing N N 407 
PLM   CG  HG1  sing N N 408 
PLM   CG  HG2  sing N N 409 
PLM   CG  HG3  sing N N 410 
PRO   N   CA   sing N N 411 
PRO   N   CD   sing N N 412 
PRO   N   H    sing N N 413 
PRO   CA  C    sing N N 414 
PRO   CA  CB   sing N N 415 
PRO   CA  HA   sing N N 416 
PRO   C   O    doub N N 417 
PRO   C   OXT  sing N N 418 
PRO   CB  CG   sing N N 419 
PRO   CB  HB2  sing N N 420 
PRO   CB  HB3  sing N N 421 
PRO   CG  CD   sing N N 422 
PRO   CG  HG2  sing N N 423 
PRO   CG  HG3  sing N N 424 
PRO   CD  HD2  sing N N 425 
PRO   CD  HD3  sing N N 426 
PRO   OXT HXT  sing N N 427 
SER   N   CA   sing N N 428 
SER   N   H    sing N N 429 
SER   N   H2   sing N N 430 
SER   CA  C    sing N N 431 
SER   CA  CB   sing N N 432 
SER   CA  HA   sing N N 433 
SER   C   O    doub N N 434 
SER   C   OXT  sing N N 435 
SER   CB  OG   sing N N 436 
SER   CB  HB2  sing N N 437 
SER   CB  HB3  sing N N 438 
SER   OG  HG   sing N N 439 
SER   OXT HXT  sing N N 440 
THR   N   CA   sing N N 441 
THR   N   H    sing N N 442 
THR   N   H2   sing N N 443 
THR   CA  C    sing N N 444 
THR   CA  CB   sing N N 445 
THR   CA  HA   sing N N 446 
THR   C   O    doub N N 447 
THR   C   OXT  sing N N 448 
THR   CB  OG1  sing N N 449 
THR   CB  CG2  sing N N 450 
THR   CB  HB   sing N N 451 
THR   OG1 HG1  sing N N 452 
THR   CG2 HG21 sing N N 453 
THR   CG2 HG22 sing N N 454 
THR   CG2 HG23 sing N N 455 
THR   OXT HXT  sing N N 456 
TRP   N   CA   sing N N 457 
TRP   N   H    sing N N 458 
TRP   N   H2   sing N N 459 
TRP   CA  C    sing N N 460 
TRP   CA  CB   sing N N 461 
TRP   CA  HA   sing N N 462 
TRP   C   O    doub N N 463 
TRP   C   OXT  sing N N 464 
TRP   CB  CG   sing N N 465 
TRP   CB  HB2  sing N N 466 
TRP   CB  HB3  sing N N 467 
TRP   CG  CD1  doub Y N 468 
TRP   CG  CD2  sing Y N 469 
TRP   CD1 NE1  sing Y N 470 
TRP   CD1 HD1  sing N N 471 
TRP   CD2 CE2  doub Y N 472 
TRP   CD2 CE3  sing Y N 473 
TRP   NE1 CE2  sing Y N 474 
TRP   NE1 HE1  sing N N 475 
TRP   CE2 CZ2  sing Y N 476 
TRP   CE3 CZ3  doub Y N 477 
TRP   CE3 HE3  sing N N 478 
TRP   CZ2 CH2  doub Y N 479 
TRP   CZ2 HZ2  sing N N 480 
TRP   CZ3 CH2  sing Y N 481 
TRP   CZ3 HZ3  sing N N 482 
TRP   CH2 HH2  sing N N 483 
TRP   OXT HXT  sing N N 484 
TYR   N   CA   sing N N 485 
TYR   N   H    sing N N 486 
TYR   N   H2   sing N N 487 
TYR   CA  C    sing N N 488 
TYR   CA  CB   sing N N 489 
TYR   CA  HA   sing N N 490 
TYR   C   O    doub N N 491 
TYR   C   OXT  sing N N 492 
TYR   CB  CG   sing N N 493 
TYR   CB  HB2  sing N N 494 
TYR   CB  HB3  sing N N 495 
TYR   CG  CD1  doub Y N 496 
TYR   CG  CD2  sing Y N 497 
TYR   CD1 CE1  sing Y N 498 
TYR   CD1 HD1  sing N N 499 
TYR   CD2 CE2  doub Y N 500 
TYR   CD2 HD2  sing N N 501 
TYR   CE1 CZ   doub Y N 502 
TYR   CE1 HE1  sing N N 503 
TYR   CE2 CZ   sing Y N 504 
TYR   CE2 HE2  sing N N 505 
TYR   CZ  OH   sing N N 506 
TYR   OH  HH   sing N N 507 
TYR   OXT HXT  sing N N 508 
VAL   N   CA   sing N N 509 
VAL   N   H    sing N N 510 
VAL   N   H2   sing N N 511 
VAL   CA  C    sing N N 512 
VAL   CA  CB   sing N N 513 
VAL   CA  HA   sing N N 514 
VAL   C   O    doub N N 515 
VAL   C   OXT  sing N N 516 
VAL   CB  CG1  sing N N 517 
VAL   CB  CG2  sing N N 518 
VAL   CB  HB   sing N N 519 
VAL   CG1 HG11 sing N N 520 
VAL   CG1 HG12 sing N N 521 
VAL   CG1 HG13 sing N N 522 
VAL   CG2 HG21 sing N N 523 
VAL   CG2 HG22 sing N N 524 
VAL   CG2 HG23 sing N N 525 
VAL   OXT HXT  sing N N 526 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2UUH 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G1T 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.005870 
_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]   0.005870 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005870 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLY   A 1 8   ? 375.490 29.940  209.203 1.00 158.35 ? 1   GLY   A N    1 
ATOM   2    C  CA   . GLY   A 1 8   ? 374.788 30.027  207.922 1.00 154.04 ? 1   GLY   A CA   1 
ATOM   3    C  C    . GLY   A 1 8   ? 374.204 28.715  207.416 1.00 155.20 ? 1   GLY   A C    1 
ATOM   4    O  O    . GLY   A 1 8   ? 373.113 28.703  206.846 1.00 151.97 ? 1   GLY   A O    1 
ATOM   5    N  N    . LYS   A 1 9   ? 374.950 27.605  207.619 1.00 152.61 ? 2   LYS   A N    1 
ATOM   6    C  CA   . LYS   A 1 9   ? 374.617 26.221  207.267 1.00 150.53 ? 2   LYS   A CA   1 
ATOM   7    C  C    . LYS   A 1 9   ? 373.929 25.525  208.448 1.00 156.04 ? 2   LYS   A C    1 
ATOM   8    O  O    . LYS   A 1 9   ? 373.237 24.523  208.263 1.00 155.50 ? 2   LYS   A O    1 
ATOM   9    C  CB   . LYS   A 1 9   ? 375.893 25.437  206.941 1.00 153.92 ? 2   LYS   A CB   1 
ATOM   10   C  CG   . LYS   A 1 9   ? 376.743 25.994  205.806 1.00 147.14 ? 2   LYS   A CG   1 
ATOM   11   C  CD   . LYS   A 1 9   ? 377.786 24.972  205.340 1.00 149.88 ? 2   LYS   A CD   1 
ATOM   12   C  CE   . LYS   A 1 9   ? 378.597 24.303  206.440 1.00 149.43 ? 2   LYS   A CE   1 
ATOM   13   N  NZ   . LYS   A 1 9   ? 379.159 22.993  206.014 1.00 147.82 ? 2   LYS   A NZ   1 
ATOM   14   N  N    . ASP   A 1 10  ? 374.126 26.038  209.658 1.00 155.11 ? 3   ASP   A N    1 
ATOM   15   C  CA   . ASP   A 1 10  ? 373.505 25.408  210.850 1.00 158.17 ? 3   ASP   A CA   1 
ATOM   16   C  C    . ASP   A 1 10  ? 372.015 25.735  210.845 1.00 156.59 ? 3   ASP   A C    1 
ATOM   17   O  O    . ASP   A 1 10  ? 371.208 24.835  211.130 1.00 157.82 ? 3   ASP   A O    1 
ATOM   18   C  CB   . ASP   A 1 10  ? 374.159 25.920  212.131 1.00 165.30 ? 3   ASP   A CB   1 
ATOM   19   C  CG   . ASP   A 1 10  ? 374.784 27.296  211.975 1.00 186.67 ? 3   ASP   A CG   1 
ATOM   20   O  OD1  . ASP   A 1 10  ? 374.223 28.114  211.218 1.00 192.57 ? 3   ASP   A OD1  1 
ATOM   21   O  OD2  . ASP   A 1 10  ? 375.827 27.538  212.612 1.00 193.64 ? 3   ASP   A OD2  1 
ATOM   22   N  N    . GLU   A 1 11  ? 371.679 26.979  210.527 1.00 147.32 ? 4   GLU   A N    1 
ATOM   23   C  CA   . GLU   A 1 11  ? 370.290 27.446  210.511 1.00 144.74 ? 4   GLU   A CA   1 
ATOM   24   C  C    . GLU   A 1 11  ? 369.391 26.832  209.388 1.00 142.23 ? 4   GLU   A C    1 
ATOM   25   O  O    . GLU   A 1 11  ? 368.196 27.162  209.299 1.00 141.72 ? 4   GLU   A O    1 
ATOM   26   C  CB   . GLU   A 1 11  ? 370.273 28.984  210.456 1.00 145.32 ? 4   GLU   A CB   1 
ATOM   27   C  CG   . GLU   A 1 11  ? 370.354 29.618  211.835 1.00 166.00 ? 4   GLU   A CG   1 
ATOM   28   C  CD   . GLU   A 1 11  ? 371.559 30.507  212.072 1.00 205.22 ? 4   GLU   A CD   1 
ATOM   29   O  OE1  . GLU   A 1 11  ? 371.555 31.651  211.563 1.00 209.46 ? 4   GLU   A OE1  1 
ATOM   30   O  OE2  . GLU   A 1 11  ? 372.485 30.080  212.801 1.00 207.89 ? 4   GLU   A OE2  1 
ATOM   31   N  N    . VAL   A 1 12  ? 369.970 25.947  208.536 1.00 132.29 ? 5   VAL   A N    1 
ATOM   32   C  CA   . VAL   A 1 12  ? 369.314 25.278  207.411 1.00 125.36 ? 5   VAL   A CA   1 
ATOM   33   C  C    . VAL   A 1 12  ? 369.558 23.741  207.425 1.00 127.58 ? 5   VAL   A C    1 
ATOM   34   O  O    . VAL   A 1 12  ? 368.979 23.034  206.607 1.00 126.81 ? 5   VAL   A O    1 
ATOM   35   C  CB   . VAL   A 1 12  ? 369.736 25.917  206.060 1.00 124.55 ? 5   VAL   A CB   1 
ATOM   36   C  CG1  . VAL   A 1 12  ? 369.495 27.424  206.039 1.00 122.61 ? 5   VAL   A CG1  1 
ATOM   37   C  CG2  . VAL   A 1 12  ? 371.186 25.600  205.714 1.00 125.34 ? 5   VAL   A CG2  1 
ATOM   38   N  N    . ALA   A 1 13  ? 370.409 23.232  208.342 1.00 125.08 ? 6   ALA   A N    1 
ATOM   39   C  CA   . ALA   A 1 13  ? 370.778 21.816  208.465 1.00 127.00 ? 6   ALA   A CA   1 
ATOM   40   C  C    . ALA   A 1 13  ? 369.603 20.840  208.675 1.00 131.92 ? 6   ALA   A C    1 
ATOM   41   O  O    . ALA   A 1 13  ? 369.689 19.708  208.188 1.00 134.83 ? 6   ALA   A O    1 
ATOM   42   C  CB   . ALA   A 1 13  ? 371.812 21.637  209.550 1.00 132.53 ? 6   ALA   A CB   1 
ATOM   43   N  N    . LEU   A 1 14  ? 368.500 21.262  209.345 1.00 125.36 ? 7   LEU   A N    1 
ATOM   44   C  CA   . LEU   A 1 14  ? 367.304 20.418  209.520 1.00 125.33 ? 7   LEU   A CA   1 
ATOM   45   C  C    . LEU   A 1 14  ? 366.548 20.334  208.195 1.00 125.17 ? 7   LEU   A C    1 
ATOM   46   O  O    . LEU   A 1 14  ? 366.092 19.251  207.823 1.00 126.61 ? 7   LEU   A O    1 
ATOM   47   C  CB   . LEU   A 1 14  ? 366.384 20.988  210.598 1.00 127.36 ? 7   LEU   A CB   1 
ATOM   48   C  CG   . LEU   A 1 14  ? 366.369 20.348  212.001 1.00 137.69 ? 7   LEU   A CG   1 
ATOM   49   C  CD1  . LEU   A 1 14  ? 367.747 19.839  212.460 1.00 140.51 ? 7   LEU   A CD1  1 
ATOM   50   C  CD2  . LEU   A 1 14  ? 365.807 21.319  213.007 1.00 140.00 ? 7   LEU   A CD2  1 
ATOM   51   N  N    . LEU   A 1 15  ? 366.443 21.479  207.462 1.00 115.91 ? 8   LEU   A N    1 
ATOM   52   C  CA   . LEU   A 1 15  ? 365.804 21.562  206.132 1.00 109.96 ? 8   LEU   A CA   1 
ATOM   53   C  C    . LEU   A 1 15  ? 366.621 20.730  205.130 1.00 113.69 ? 8   LEU   A C    1 
ATOM   54   O  O    . LEU   A 1 15  ? 366.034 20.035  204.295 1.00 111.95 ? 8   LEU   A O    1 
ATOM   55   C  CB   . LEU   A 1 15  ? 365.665 23.026  205.637 1.00 105.46 ? 8   LEU   A CB   1 
ATOM   56   C  CG   . LEU   A 1 15  ? 365.149 24.104  206.617 1.00 109.20 ? 8   LEU   A CG   1 
ATOM   57   C  CD1  . LEU   A 1 15  ? 365.228 25.472  205.996 1.00 104.70 ? 8   LEU   A CD1  1 
ATOM   58   C  CD2  . LEU   A 1 15  ? 363.731 23.814  207.114 1.00 113.39 ? 8   LEU   A CD2  1 
ATOM   59   N  N    . ALA   A 1 16  ? 367.978 20.769  205.235 1.00 111.86 ? 9   ALA   A N    1 
ATOM   60   C  CA   . ALA   A 1 16  ? 368.842 19.956  204.371 1.00 111.70 ? 9   ALA   A CA   1 
ATOM   61   C  C    . ALA   A 1 16  ? 368.599 18.470  204.663 1.00 119.85 ? 9   ALA   A C    1 
ATOM   62   O  O    . ALA   A 1 16  ? 368.404 17.700  203.718 1.00 118.93 ? 9   ALA   A O    1 
ATOM   63   C  CB   . ALA   A 1 16  ? 370.298 20.320  204.566 1.00 113.25 ? 9   ALA   A CB   1 
ATOM   64   N  N    . ALA   A 1 17  ? 368.495 18.088  205.968 1.00 120.50 ? 10  ALA   A N    1 
ATOM   65   C  CA   . ALA   A 1 17  ? 368.191 16.697  206.361 1.00 124.33 ? 10  ALA   A CA   1 
ATOM   66   C  C    . ALA   A 1 17  ? 366.845 16.225  205.762 1.00 125.36 ? 10  ALA   A C    1 
ATOM   67   O  O    . ALA   A 1 17  ? 366.849 15.286  204.978 1.00 125.27 ? 10  ALA   A O    1 
ATOM   68   C  CB   . ALA   A 1 17  ? 368.201 16.547  207.881 1.00 129.88 ? 10  ALA   A CB   1 
ATOM   69   N  N    . VAL   A 1 18  ? 365.732 16.948  206.041 1.00 120.09 ? 11  VAL   A N    1 
ATOM   70   C  CA   . VAL   A 1 18  ? 364.365 16.684  205.537 1.00 118.55 ? 11  VAL   A CA   1 
ATOM   71   C  C    . VAL   A 1 18  ? 364.313 16.645  203.973 1.00 118.29 ? 11  VAL   A C    1 
ATOM   72   O  O    . VAL   A 1 18  ? 363.580 15.829  203.417 1.00 118.08 ? 11  VAL   A O    1 
ATOM   73   C  CB   . VAL   A 1 18  ? 363.341 17.673  206.175 1.00 121.11 ? 11  VAL   A CB   1 
ATOM   74   C  CG1  . VAL   A 1 18  ? 361.981 17.623  205.487 1.00 119.63 ? 11  VAL   A CG1  1 
ATOM   75   C  CG2  . VAL   A 1 18  ? 363.186 17.403  207.665 1.00 125.73 ? 11  VAL   A CG2  1 
ATOM   76   N  N    . THR   A 1 19  ? 365.124 17.475  203.279 1.00 112.39 ? 12  THR   A N    1 
ATOM   77   C  CA   . THR   A 1 19  ? 365.234 17.475  201.808 1.00 109.10 ? 12  THR   A CA   1 
ATOM   78   C  C    . THR   A 1 19  ? 365.811 16.131  201.362 1.00 117.86 ? 12  THR   A C    1 
ATOM   79   O  O    . THR   A 1 19  ? 365.222 15.467  200.516 1.00 117.45 ? 12  THR   A O    1 
ATOM   80   C  CB   . THR   A 1 19  ? 366.134 18.615  201.351 1.00 113.02 ? 12  THR   A CB   1 
ATOM   81   O  OG1  . THR   A 1 19  ? 365.524 19.897  201.625 1.00 111.75 ? 12  THR   A OG1  1 
ATOM   82   C  CG2  . THR   A 1 19  ? 366.553 18.472  199.910 1.00 105.00 ? 12  THR   A CG2  1 
ATOM   83   N  N    . LEU   A 1 20  ? 366.935 15.702  201.985 1.00 120.02 ? 13  LEU   A N    1 
ATOM   84   C  CA   . LEU   A 1 20  ? 367.614 14.432  201.704 1.00 123.42 ? 13  LEU   A CA   1 
ATOM   85   C  C    . LEU   A 1 20  ? 366.736 13.216  201.923 1.00 130.11 ? 13  LEU   A C    1 
ATOM   86   O  O    . LEU   A 1 20  ? 366.870 12.234  201.189 1.00 131.91 ? 13  LEU   A O    1 
ATOM   87   C  CB   . LEU   A 1 20  ? 368.901 14.312  202.506 1.00 127.06 ? 13  LEU   A CB   1 
ATOM   88   C  CG   . LEU   A 1 20  ? 370.020 13.627  201.770 1.00 134.63 ? 13  LEU   A CG   1 
ATOM   89   C  CD1  . LEU   A 1 20  ? 370.281 14.322  200.407 1.00 131.31 ? 13  LEU   A CD1  1 
ATOM   90   C  CD2  . LEU   A 1 20  ? 371.281 13.552  202.644 1.00 140.74 ? 13  LEU   A CD2  1 
ATOM   91   N  N    . LEU   A 1 21  ? 365.827 13.293  202.919 1.00 127.02 ? 14  LEU   A N    1 
ATOM   92   C  CA   . LEU   A 1 21  ? 364.835 12.267  203.236 1.00 130.34 ? 14  LEU   A CA   1 
ATOM   93   C  C    . LEU   A 1 21  ? 363.857 12.167  202.065 1.00 131.52 ? 14  LEU   A C    1 
ATOM   94   O  O    . LEU   A 1 21  ? 363.617 11.069  201.576 1.00 133.93 ? 14  LEU   A O    1 
ATOM   95   C  CB   . LEU   A 1 21  ? 364.091 12.683  204.507 1.00 132.56 ? 14  LEU   A CB   1 
ATOM   96   C  CG   . LEU   A 1 21  ? 363.634 11.614  205.481 1.00 143.92 ? 14  LEU   A CG   1 
ATOM   97   C  CD1  . LEU   A 1 21  ? 364.515 10.371  205.429 1.00 148.69 ? 14  LEU   A CD1  1 
ATOM   98   C  CD2  . LEU   A 1 21  ? 363.635 12.173  206.888 1.00 147.38 ? 14  LEU   A CD2  1 
ATOM   99   N  N    . GLY   A 1 22  ? 363.377 13.327  201.586 1.00 122.97 ? 15  GLY   A N    1 
ATOM   100  C  CA   . GLY   A 1 22  ? 362.484 13.471  200.440 1.00 119.29 ? 15  GLY   A CA   1 
ATOM   101  C  C    . GLY   A 1 22  ? 363.084 12.903  199.176 1.00 121.19 ? 15  GLY   A C    1 
ATOM   102  O  O    . GLY   A 1 22  ? 362.421 12.139  198.480 1.00 122.59 ? 15  GLY   A O    1 
ATOM   103  N  N    . VAL   A 1 23  ? 364.367 13.220  198.898 1.00 115.03 ? 16  VAL   A N    1 
ATOM   104  C  CA   . VAL   A 1 23  ? 365.079 12.647  197.751 1.00 113.52 ? 16  VAL   A CA   1 
ATOM   105  C  C    . VAL   A 1 23  ? 365.051 11.121  197.833 1.00 124.21 ? 16  VAL   A C    1 
ATOM   106  O  O    . VAL   A 1 23  ? 364.589 10.502  196.885 1.00 125.57 ? 16  VAL   A O    1 
ATOM   107  C  CB   . VAL   A 1 23  ? 366.509 13.201  197.569 1.00 113.92 ? 16  VAL   A CB   1 
ATOM   108  C  CG1  . VAL   A 1 23  ? 367.253 12.447  196.475 1.00 114.37 ? 16  VAL   A CG1  1 
ATOM   109  C  CG2  . VAL   A 1 23  ? 366.476 14.687  197.258 1.00 108.86 ? 16  VAL   A CG2  1 
ATOM   110  N  N    . LEU   A 1 24  ? 365.469 10.522  198.980 1.00 125.85 ? 17  LEU   A N    1 
ATOM   111  C  CA   . LEU   A 1 24  ? 365.479 9.054   199.178 1.00 131.02 ? 17  LEU   A CA   1 
ATOM   112  C  C    . LEU   A 1 24  ? 364.093 8.450   199.089 1.00 137.36 ? 17  LEU   A C    1 
ATOM   113  O  O    . LEU   A 1 24  ? 363.959 7.355   198.546 1.00 141.75 ? 17  LEU   A O    1 
ATOM   114  C  CB   . LEU   A 1 24  ? 366.177 8.617   200.481 1.00 135.42 ? 17  LEU   A CB   1 
ATOM   115  C  CG   . LEU   A 1 24  ? 367.643 9.043   200.663 1.00 139.54 ? 17  LEU   A CG   1 
ATOM   116  C  CD1  . LEU   A 1 24  ? 368.030 9.041   202.121 1.00 142.82 ? 17  LEU   A CD1  1 
ATOM   117  C  CD2  . LEU   A 1 24  ? 368.593 8.171   199.847 1.00 144.26 ? 17  LEU   A CD2  1 
ATOM   118  N  N    . LEU   A 1 25  ? 363.053 9.171   199.567 1.00 131.09 ? 18  LEU   A N    1 
ATOM   119  C  CA   . LEU   A 1 25  ? 361.664 8.711   199.469 1.00 132.05 ? 18  LEU   A CA   1 
ATOM   120  C  C    . LEU   A 1 25  ? 361.283 8.571   197.986 1.00 135.52 ? 18  LEU   A C    1 
ATOM   121  O  O    . LEU   A 1 25  ? 360.596 7.612   197.627 1.00 139.12 ? 18  LEU   A O    1 
ATOM   122  C  CB   . LEU   A 1 25  ? 360.703 9.664   200.204 1.00 130.14 ? 18  LEU   A CB   1 
ATOM   123  C  CG   . LEU   A 1 25  ? 359.248 9.212   200.347 1.00 136.85 ? 18  LEU   A CG   1 
ATOM   124  C  CD1  . LEU   A 1 25  ? 359.089 8.171   201.419 1.00 143.36 ? 18  LEU   A CD1  1 
ATOM   125  C  CD2  . LEU   A 1 25  ? 358.347 10.374  200.643 1.00 135.90 ? 18  LEU   A CD2  1 
ATOM   126  N  N    . GLN   A 1 26  ? 361.772 9.495   197.123 1.00 127.27 ? 19  GLN   A N    1 
ATOM   127  C  CA   . GLN   A 1 26  ? 361.530 9.459   195.674 1.00 124.71 ? 19  GLN   A CA   1 
ATOM   128  C  C    . GLN   A 1 26  ? 362.284 8.309   195.005 1.00 132.10 ? 19  GLN   A C    1 
ATOM   129  O  O    . GLN   A 1 26  ? 361.757 7.727   194.052 1.00 134.30 ? 19  GLN   A O    1 
ATOM   130  C  CB   . GLN   A 1 26  ? 361.858 10.798  194.991 1.00 120.28 ? 19  GLN   A CB   1 
ATOM   131  C  CG   . GLN   A 1 26  ? 361.023 11.990  195.462 1.00 118.52 ? 19  GLN   A CG   1 
ATOM   132  C  CD   . GLN   A 1 26  ? 359.528 11.883  195.300 1.00 130.01 ? 19  GLN   A CD   1 
ATOM   133  O  OE1  . GLN   A 1 26  ? 358.770 12.245  196.208 1.00 122.44 ? 19  GLN   A OE1  1 
ATOM   134  N  NE2  . GLN   A 1 26  ? 359.065 11.455  194.127 1.00 129.51 ? 19  GLN   A NE2  1 
ATOM   135  N  N    . ALA   A 1 27  ? 363.498 7.973   195.502 1.00 129.56 ? 20  ALA   A N    1 
ATOM   136  C  CA   . ALA   A 1 27  ? 364.305 6.849   194.997 1.00 133.67 ? 20  ALA   A CA   1 
ATOM   137  C  C    . ALA   A 1 27  ? 363.586 5.497   195.276 1.00 142.34 ? 20  ALA   A C    1 
ATOM   138  O  O    . ALA   A 1 27  ? 363.649 4.567   194.460 1.00 144.12 ? 20  ALA   A O    1 
ATOM   139  C  CB   . ALA   A 1 27  ? 365.674 6.863   195.656 1.00 136.09 ? 20  ALA   A CB   1 
ATOM   140  N  N    . TYR   A 1 28  ? 362.890 5.422   196.438 1.00 140.15 ? 21  TYR   A N    1 
ATOM   141  C  CA   . TYR   A 1 28  ? 362.070 4.297   196.872 1.00 144.64 ? 21  TYR   A CA   1 
ATOM   142  C  C    . TYR   A 1 28  ? 360.874 4.128   195.926 1.00 147.38 ? 21  TYR   A C    1 
ATOM   143  O  O    . TYR   A 1 28  ? 360.599 3.012   195.510 1.00 151.94 ? 21  TYR   A O    1 
ATOM   144  C  CB   . TYR   A 1 28  ? 361.607 4.484   198.336 1.00 147.56 ? 21  TYR   A CB   1 
ATOM   145  C  CG   . TYR   A 1 28  ? 360.588 3.455   198.769 1.00 155.18 ? 21  TYR   A CG   1 
ATOM   146  C  CD1  . TYR   A 1 28  ? 360.946 2.120   198.944 1.00 163.95 ? 21  TYR   A CD1  1 
ATOM   147  C  CD2  . TYR   A 1 28  ? 359.256 3.803   198.957 1.00 155.69 ? 21  TYR   A CD2  1 
ATOM   148  C  CE1  . TYR   A 1 28  ? 360.000 1.155   199.288 1.00 171.50 ? 21  TYR   A CE1  1 
ATOM   149  C  CE2  . TYR   A 1 28  ? 358.304 2.852   199.321 1.00 163.18 ? 21  TYR   A CE2  1 
ATOM   150  C  CZ   . TYR   A 1 28  ? 358.678 1.525   199.479 1.00 178.16 ? 21  TYR   A CZ   1 
ATOM   151  O  OH   . TYR   A 1 28  ? 357.742 0.576   199.841 1.00 183.60 ? 21  TYR   A OH   1 
ATOM   152  N  N    . PHE   A 1 29  ? 360.187 5.236   195.569 1.00 138.85 ? 22  PHE   A N    1 
ATOM   153  C  CA   . PHE   A 1 29  ? 359.028 5.266   194.659 1.00 137.32 ? 22  PHE   A CA   1 
ATOM   154  C  C    . PHE   A 1 29  ? 359.405 4.822   193.254 1.00 141.43 ? 22  PHE   A C    1 
ATOM   155  O  O    . PHE   A 1 29  ? 358.591 4.184   192.591 1.00 144.19 ? 22  PHE   A O    1 
ATOM   156  C  CB   . PHE   A 1 29  ? 358.381 6.670   194.615 1.00 133.72 ? 22  PHE   A CB   1 
ATOM   157  C  CG   . PHE   A 1 29  ? 357.728 7.168   195.891 1.00 135.25 ? 22  PHE   A CG   1 
ATOM   158  C  CD1  . PHE   A 1 29  ? 357.365 6.285   196.904 1.00 143.79 ? 22  PHE   A CD1  1 
ATOM   159  C  CD2  . PHE   A 1 29  ? 357.412 8.508   196.049 1.00 131.73 ? 22  PHE   A CD2  1 
ATOM   160  C  CE1  . PHE   A 1 29  ? 356.753 6.748   198.072 1.00 145.27 ? 22  PHE   A CE1  1 
ATOM   161  C  CE2  . PHE   A 1 29  ? 356.781 8.962   197.208 1.00 135.05 ? 22  PHE   A CE2  1 
ATOM   162  C  CZ   . PHE   A 1 29  ? 356.449 8.080   198.207 1.00 138.71 ? 22  PHE   A CZ   1 
ATOM   163  N  N    . SER   A 1 30  ? 360.634 5.154   192.804 1.00 135.94 ? 23  SER   A N    1 
ATOM   164  C  CA   . SER   A 1 30  ? 361.170 4.779   191.491 1.00 136.54 ? 23  SER   A CA   1 
ATOM   165  C  C    . SER   A 1 30  ? 361.471 3.273   191.452 1.00 147.62 ? 23  SER   A C    1 
ATOM   166  O  O    . SER   A 1 30  ? 361.221 2.616   190.430 1.00 150.39 ? 23  SER   A O    1 
ATOM   167  C  CB   . SER   A 1 30  ? 362.419 5.592   191.171 1.00 138.06 ? 23  SER   A CB   1 
ATOM   168  O  OG   . SER   A 1 30  ? 362.151 6.987   191.195 1.00 145.43 ? 23  SER   A OG   1 
ATOM   169  N  N    . LEU   A 1 31  ? 361.973 2.724   192.590 1.00 146.28 ? 24  LEU   A N    1 
ATOM   170  C  CA   . LEU   A 1 31  ? 362.252 1.297   192.792 1.00 151.28 ? 24  LEU   A CA   1 
ATOM   171  C  C    . LEU   A 1 31  ? 360.933 0.548   192.748 1.00 158.31 ? 24  LEU   A C    1 
ATOM   172  O  O    . LEU   A 1 31  ? 360.870 -0.508  192.125 1.00 163.56 ? 24  LEU   A O    1 
ATOM   173  C  CB   . LEU   A 1 31  ? 362.935 1.079   194.155 1.00 153.44 ? 24  LEU   A CB   1 
ATOM   174  C  CG   . LEU   A 1 31  ? 363.285 -0.348  194.551 1.00 164.39 ? 24  LEU   A CG   1 
ATOM   175  C  CD1  . LEU   A 1 31  ? 364.572 -0.800  193.890 1.00 166.13 ? 24  LEU   A CD1  1 
ATOM   176  C  CD2  . LEU   A 1 31  ? 363.422 -0.463  196.048 1.00 169.07 ? 24  LEU   A CD2  1 
ATOM   177  N  N    . GLN   A 1 32  ? 359.878 1.107   193.388 1.00 152.12 ? 25  GLN   A N    1 
ATOM   178  C  CA   . GLN   A 1 32  ? 358.543 0.515   193.412 1.00 155.08 ? 25  GLN   A CA   1 
ATOM   179  C  C    . GLN   A 1 32  ? 357.941 0.424   192.015 1.00 160.15 ? 25  GLN   A C    1 
ATOM   180  O  O    . GLN   A 1 32  ? 357.373 -0.625  191.665 1.00 165.96 ? 25  GLN   A O    1 
ATOM   181  C  CB   . GLN   A 1 32  ? 357.610 1.244   194.384 1.00 154.16 ? 25  GLN   A CB   1 
ATOM   182  C  CG   . GLN   A 1 32  ? 357.981 1.098   195.861 1.00 165.61 ? 25  GLN   A CG   1 
ATOM   183  C  CD   . GLN   A 1 32  ? 358.031 -0.322  196.363 1.00 196.09 ? 25  GLN   A CD   1 
ATOM   184  O  OE1  . GLN   A 1 32  ? 357.008 -0.928  196.694 1.00 199.72 ? 25  GLN   A OE1  1 
ATOM   185  N  NE2  . GLN   A 1 32  ? 359.230 -0.874  196.460 1.00 189.63 ? 25  GLN   A NE2  1 
ATOM   186  N  N    . VAL   A 1 33  ? 358.115 1.481   191.196 1.00 150.54 ? 26  VAL   A N    1 
ATOM   187  C  CA   . VAL   A 1 33  ? 357.624 1.490   189.819 1.00 150.34 ? 26  VAL   A CA   1 
ATOM   188  C  C    . VAL   A 1 33  ? 358.466 0.526   188.959 1.00 159.68 ? 26  VAL   A C    1 
ATOM   189  O  O    . VAL   A 1 33  ? 357.886 -0.255  188.202 1.00 162.78 ? 26  VAL   A O    1 
ATOM   190  C  CB   . VAL   A 1 33  ? 357.479 2.920   189.255 1.00 148.23 ? 26  VAL   A CB   1 
ATOM   191  C  CG1  . VAL   A 1 33  ? 357.316 2.934   187.737 1.00 147.76 ? 26  VAL   A CG1  1 
ATOM   192  C  CG2  . VAL   A 1 33  ? 356.293 3.601   189.906 1.00 147.01 ? 26  VAL   A CG2  1 
ATOM   193  N  N    . ILE   A 1 34  ? 359.808 0.495   189.153 1.00 157.24 ? 27  ILE   A N    1 
ATOM   194  C  CA   . ILE   A 1 34  ? 360.689 -0.457  188.450 1.00 160.89 ? 27  ILE   A CA   1 
ATOM   195  C  C    . ILE   A 1 34  ? 360.256 -1.896  188.743 1.00 171.91 ? 27  ILE   A C    1 
ATOM   196  O  O    . ILE   A 1 34  ? 360.161 -2.688  187.809 1.00 176.33 ? 27  ILE   A O    1 
ATOM   197  C  CB   . ILE   A 1 34  ? 362.199 -0.188  188.724 1.00 162.85 ? 27  ILE   A CB   1 
ATOM   198  C  CG1  . ILE   A 1 34  ? 362.707 0.958   187.823 1.00 157.48 ? 27  ILE   A CG1  1 
ATOM   199  C  CG2  . ILE   A 1 34  ? 363.061 -1.456  188.544 1.00 169.89 ? 27  ILE   A CG2  1 
ATOM   200  C  CD1  . ILE   A 1 34  ? 363.855 1.757   188.375 1.00 158.29 ? 27  ILE   A CD1  1 
ATOM   201  N  N    . SER   A 1 35  ? 359.937 -2.209  190.018 1.00 170.58 ? 28  SER   A N    1 
ATOM   202  C  CA   . SER   A 1 35  ? 359.479 -3.534  190.454 1.00 178.12 ? 28  SER   A CA   1 
ATOM   203  C  C    . SER   A 1 35  ? 358.117 -3.915  189.860 1.00 184.52 ? 28  SER   A C    1 
ATOM   204  O  O    . SER   A 1 35  ? 357.922 -5.073  189.498 1.00 189.79 ? 28  SER   A O    1 
ATOM   205  C  CB   . SER   A 1 35  ? 359.467 -3.635  191.976 1.00 183.73 ? 28  SER   A CB   1 
ATOM   206  O  OG   . SER   A 1 35  ? 360.775 -3.468  192.501 1.00 191.50 ? 28  SER   A OG   1 
ATOM   207  N  N    . ALA   A 1 36  ? 357.200 -2.934  189.711 1.00 177.00 ? 29  ALA   A N    1 
ATOM   208  C  CA   . ALA   A 1 36  ? 355.876 -3.141  189.109 1.00 178.49 ? 29  ALA   A CA   1 
ATOM   209  C  C    . ALA   A 1 36  ? 355.970 -3.369  187.597 1.00 182.89 ? 29  ALA   A C    1 
ATOM   210  O  O    . ALA   A 1 36  ? 355.078 -3.986  187.028 1.00 187.21 ? 29  ALA   A O    1 
ATOM   211  C  CB   . ALA   A 1 36  ? 354.975 -1.952  189.400 1.00 174.38 ? 29  ALA   A CB   1 
ATOM   212  N  N    . ARG   A 1 37  ? 357.046 -2.881  186.952 1.00 175.96 ? 30  ARG   A N    1 
ATOM   213  C  CA   . ARG   A 1 37  ? 357.304 -3.036  185.515 1.00 176.59 ? 30  ARG   A CA   1 
ATOM   214  C  C    . ARG   A 1 37  ? 357.691 -4.474  185.164 1.00 190.23 ? 30  ARG   A C    1 
ATOM   215  O  O    . ARG   A 1 37  ? 357.454 -4.923  184.039 1.00 192.24 ? 30  ARG   A O    1 
ATOM   216  C  CB   . ARG   A 1 37  ? 358.393 -2.068  185.048 1.00 169.89 ? 30  ARG   A CB   1 
ATOM   217  C  CG   . ARG   A 1 37  ? 357.887 -0.663  184.850 1.00 168.81 ? 30  ARG   A CG   1 
ATOM   218  C  CD   . ARG   A 1 37  ? 358.704 0.043   183.813 1.00 172.04 ? 30  ARG   A CD   1 
ATOM   219  N  NE   . ARG   A 1 37  ? 358.129 1.343   183.475 1.00 174.76 ? 30  ARG   A NE   1 
ATOM   220  C  CZ   . ARG   A 1 37  ? 357.459 1.597   182.357 1.00 181.70 ? 30  ARG   A CZ   1 
ATOM   221  N  NH1  . ARG   A 1 37  ? 356.990 2.813   182.122 1.00 158.03 ? 30  ARG   A NH1  1 
ATOM   222  N  NH2  . ARG   A 1 37  ? 357.266 0.642   181.460 1.00 180.68 ? 30  ARG   A NH2  1 
ATOM   223  N  N    . ARG   A 1 38  ? 358.299 -5.181  186.128 1.00 192.30 ? 31  ARG   A N    1 
ATOM   224  C  CA   . ARG   A 1 38  ? 358.689 -6.585  186.005 1.00 198.79 ? 31  ARG   A CA   1 
ATOM   225  C  C    . ARG   A 1 38  ? 357.523 -7.478  186.462 1.00 204.30 ? 31  ARG   A C    1 
ATOM   226  O  O    . ARG   A 1 38  ? 357.253 -8.506  185.834 1.00 206.92 ? 31  ARG   A O    1 
ATOM   227  C  CB   . ARG   A 1 38  ? 360.013 -6.838  186.772 1.00 199.62 ? 31  ARG   A CB   1 
ATOM   228  C  CG   . ARG   A 1 38  ? 360.085 -8.024  187.755 1.00 208.41 ? 31  ARG   A CG   1 
ATOM   229  C  CD   . ARG   A 1 38  ? 360.547 -7.601  189.150 1.00 217.03 ? 31  ARG   A CD   1 
ATOM   230  N  NE   . ARG   A 1 38  ? 361.608 -6.583  189.120 1.00 224.20 ? 31  ARG   A NE   1 
ATOM   231  C  CZ   . ARG   A 1 38  ? 362.107 -5.977  190.194 1.00 233.48 ? 31  ARG   A CZ   1 
ATOM   232  N  NH1  . ARG   A 1 38  ? 361.661 -6.282  191.406 1.00 226.38 ? 31  ARG   A NH1  1 
ATOM   233  N  NH2  . ARG   A 1 38  ? 363.054 -5.055  190.063 1.00 222.03 ? 31  ARG   A NH2  1 
ATOM   234  N  N    . ALA   A 1 39  ? 356.802 -7.043  187.520 1.00 201.29 ? 32  ALA   A N    1 
ATOM   235  C  CA   . ALA   A 1 39  ? 355.652 -7.740  188.102 1.00 203.22 ? 32  ALA   A CA   1 
ATOM   236  C  C    . ALA   A 1 39  ? 354.394 -7.689  187.226 1.00 206.83 ? 32  ALA   A C    1 
ATOM   237  O  O    . ALA   A 1 39  ? 353.400 -8.333  187.564 1.00 208.99 ? 32  ALA   A O    1 
ATOM   238  C  CB   . ALA   A 1 39  ? 355.353 -7.192  189.489 1.00 202.74 ? 32  ALA   A CB   1 
ATOM   239  N  N    . PHE   A 1 40  ? 354.431 -6.937  186.110 1.00 202.86 ? 33  PHE   A N    1 
ATOM   240  C  CA   . PHE   A 1 40  ? 353.312 -6.834  185.168 1.00 203.67 ? 33  PHE   A CA   1 
ATOM   241  C  C    . PHE   A 1 40  ? 353.776 -6.860  183.687 1.00 206.74 ? 33  PHE   A C    1 
ATOM   242  O  O    . PHE   A 1 40  ? 352.944 -6.736  182.783 1.00 207.05 ? 33  PHE   A O    1 
ATOM   243  C  CB   . PHE   A 1 40  ? 352.442 -5.594  185.474 1.00 202.42 ? 33  PHE   A CB   1 
ATOM   244  C  CG   . PHE   A 1 40  ? 351.679 -5.600  186.784 1.00 204.24 ? 33  PHE   A CG   1 
ATOM   245  C  CD1  . PHE   A 1 40  ? 350.564 -6.410  186.956 1.00 208.55 ? 33  PHE   A CD1  1 
ATOM   246  C  CD2  . PHE   A 1 40  ? 352.027 -4.734  187.814 1.00 202.64 ? 33  PHE   A CD2  1 
ATOM   247  C  CE1  . PHE   A 1 40  ? 349.831 -6.380  188.147 1.00 209.67 ? 33  PHE   A CE1  1 
ATOM   248  C  CE2  . PHE   A 1 40  ? 351.298 -4.709  189.008 1.00 205.75 ? 33  PHE   A CE2  1 
ATOM   249  C  CZ   . PHE   A 1 40  ? 350.209 -5.539  189.169 1.00 207.00 ? 33  PHE   A CZ   1 
ATOM   250  N  N    . ARG   A 1 41  ? 355.103 -7.049  183.454 1.00 203.94 ? 34  ARG   A N    1 
ATOM   251  C  CA   . ARG   A 1 41  ? 355.778 -7.077  182.143 1.00 203.96 ? 34  ARG   A CA   1 
ATOM   252  C  C    . ARG   A 1 41  ? 355.487 -5.814  181.283 1.00 204.31 ? 34  ARG   A C    1 
ATOM   253  O  O    . ARG   A 1 41  ? 355.303 -5.920  180.057 1.00 205.07 ? 34  ARG   A O    1 
ATOM   254  C  CB   . ARG   A 1 41  ? 355.502 -8.380  181.373 1.00 207.54 ? 34  ARG   A CB   1 
ATOM   255  C  CG   . ARG   A 1 41  ? 356.436 -9.515  181.758 1.00 219.78 ? 34  ARG   A CG   1 
ATOM   256  C  CD   . ARG   A 1 41  ? 355.660 -10.805 181.968 1.00 238.31 ? 34  ARG   A CD   1 
ATOM   257  N  NE   . ARG   A 1 41  ? 356.009 -11.469 183.228 1.00 244.78 ? 34  ARG   A NE   1 
ATOM   258  C  CZ   . ARG   A 1 41  ? 355.477 -11.174 184.414 1.00 251.94 ? 34  ARG   A CZ   1 
ATOM   259  N  NH1  . ARG   A 1 41  ? 355.860 -11.831 185.501 1.00 251.98 ? 34  ARG   A NH1  1 
ATOM   260  N  NH2  . ARG   A 1 41  ? 354.566 -10.214 184.523 1.00 250.66 ? 34  ARG   A NH2  1 
ATOM   261  N  N    . VAL   A 1 42  ? 355.467 -4.618  181.942 1.00 192.80 ? 35  VAL   A N    1 
ATOM   262  C  CA   . VAL   A 1 42  ? 355.226 -3.327  181.280 1.00 186.51 ? 35  VAL   A CA   1 
ATOM   263  C  C    . VAL   A 1 42  ? 356.550 -2.741  180.771 1.00 188.32 ? 35  VAL   A C    1 
ATOM   264  O  O    . VAL   A 1 42  ? 357.367 -2.242  181.549 1.00 184.29 ? 35  VAL   A O    1 
ATOM   265  C  CB   . VAL   A 1 42  ? 354.381 -2.296  182.082 1.00 184.98 ? 35  VAL   A CB   1 
ATOM   266  C  CG1  . VAL   A 1 42  ? 354.011 -1.104  181.202 1.00 180.48 ? 35  VAL   A CG1  1 
ATOM   267  C  CG2  . VAL   A 1 42  ? 353.123 -2.931  182.668 1.00 189.10 ? 35  VAL   A CG2  1 
ATOM   268  N  N    . SER   A 1 43  ? 356.751 -2.838  179.452 1.00 187.52 ? 36  SER   A N    1 
ATOM   269  C  CA   . SER   A 1 43  ? 357.949 -2.386  178.755 1.00 185.52 ? 36  SER   A CA   1 
ATOM   270  C  C    . SER   A 1 43  ? 357.925 -0.869  178.563 1.00 181.65 ? 36  SER   A C    1 
ATOM   271  O  O    . SER   A 1 43  ? 356.918 -0.336  178.101 1.00 179.91 ? 36  SER   A O    1 
ATOM   272  C  CB   . SER   A 1 43  ? 358.066 -3.083  177.396 1.00 194.98 ? 36  SER   A CB   1 
ATOM   273  O  OG   . SER   A 1 43  ? 357.717 -4.461  177.429 1.00 212.18 ? 36  SER   A OG   1 
ATOM   274  N  N    . PRO   A 1 44  ? 359.016 -0.144  178.880 1.00 174.49 ? 37  PRO   A N    1 
ATOM   275  C  CA   . PRO   A 1 44  ? 359.020 1.309   178.630 1.00 169.10 ? 37  PRO   A CA   1 
ATOM   276  C  C    . PRO   A 1 44  ? 359.179 1.548   177.123 1.00 176.61 ? 37  PRO   A C    1 
ATOM   277  O  O    . PRO   A 1 44  ? 359.771 0.687   176.477 1.00 181.28 ? 37  PRO   A O    1 
ATOM   278  C  CB   . PRO   A 1 44  ? 360.227 1.813   179.442 1.00 167.14 ? 37  PRO   A CB   1 
ATOM   279  C  CG   . PRO   A 1 44  ? 360.701 0.621   180.260 1.00 174.88 ? 37  PRO   A CG   1 
ATOM   280  C  CD   . PRO   A 1 44  ? 360.300 -0.580  179.454 1.00 176.98 ? 37  PRO   A CD   1 
ATOM   281  N  N    . PRO   A 1 45  ? 358.593 2.594   176.492 1.00 172.04 ? 38  PRO   A N    1 
ATOM   282  C  CA   . PRO   A 1 45  ? 357.902 3.757   177.072 1.00 167.35 ? 38  PRO   A CA   1 
ATOM   283  C  C    . PRO   A 1 45  ? 356.385 3.621   177.313 1.00 171.95 ? 38  PRO   A C    1 
ATOM   284  O  O    . PRO   A 1 45  ? 355.665 4.616   177.187 1.00 169.82 ? 38  PRO   A O    1 
ATOM   285  C  CB   . PRO   A 1 45  ? 358.232 4.864   176.062 1.00 168.11 ? 38  PRO   A CB   1 
ATOM   286  C  CG   . PRO   A 1 45  ? 358.229 4.142   174.739 1.00 177.75 ? 38  PRO   A CG   1 
ATOM   287  C  CD   . PRO   A 1 45  ? 358.784 2.765   175.034 1.00 176.54 ? 38  PRO   A CD   1 
ATOM   288  N  N    . LEU   A 1 46  ? 355.899 2.432   177.706 1.00 171.63 ? 39  LEU   A N    1 
ATOM   289  C  CA   . LEU   A 1 46  ? 354.473 2.279   178.013 1.00 172.78 ? 39  LEU   A CA   1 
ATOM   290  C  C    . LEU   A 1 46  ? 354.192 2.567   179.480 1.00 174.88 ? 39  LEU   A C    1 
ATOM   291  O  O    . LEU   A 1 46  ? 354.995 2.212   180.339 1.00 175.76 ? 39  LEU   A O    1 
ATOM   292  C  CB   . LEU   A 1 46  ? 353.942 0.918   177.614 1.00 178.78 ? 39  LEU   A CB   1 
ATOM   293  C  CG   . LEU   A 1 46  ? 353.542 0.833   176.172 1.00 186.35 ? 39  LEU   A CG   1 
ATOM   294  C  CD1  . LEU   A 1 46  ? 354.443 -0.123  175.418 1.00 190.05 ? 39  LEU   A CD1  1 
ATOM   295  C  CD2  . LEU   A 1 46  ? 352.094 0.454   176.057 1.00 193.17 ? 39  LEU   A CD2  1 
ATOM   296  N  N    . THR   A 1 47  ? 353.072 3.249   179.761 1.00 168.24 ? 40  THR   A N    1 
ATOM   297  C  CA   . THR   A 1 47  ? 352.666 3.655   181.114 1.00 164.10 ? 40  THR   A CA   1 
ATOM   298  C  C    . THR   A 1 47  ? 351.333 2.981   181.492 1.00 169.95 ? 40  THR   A C    1 
ATOM   299  O  O    . THR   A 1 47  ? 350.837 3.148   182.616 1.00 168.44 ? 40  THR   A O    1 
ATOM   300  C  CB   . THR   A 1 47  ? 352.547 5.184   181.156 1.00 159.94 ? 40  THR   A CB   1 
ATOM   301  O  OG1  . THR   A 1 47  ? 351.339 5.581   180.499 1.00 161.06 ? 40  THR   A OG1  1 
ATOM   302  C  CG2  . THR   A 1 47  ? 353.750 5.890   180.531 1.00 150.61 ? 40  THR   A CG2  1 
ATOM   303  N  N    . THR   A 1 48  ? 350.759 2.242   180.521 1.00 169.50 ? 41  THR   A N    1 
ATOM   304  C  CA   . THR   A 1 48  ? 349.476 1.551   180.612 1.00 174.14 ? 41  THR   A CA   1 
ATOM   305  C  C    . THR   A 1 48  ? 349.619 0.041   180.806 1.00 182.21 ? 41  THR   A C    1 
ATOM   306  O  O    . THR   A 1 48  ? 350.412 -0.611  180.125 1.00 183.15 ? 41  THR   A O    1 
ATOM   307  C  CB   . THR   A 1 48  ? 348.580 1.895   179.403 1.00 183.01 ? 41  THR   A CB   1 
ATOM   308  O  OG1  . THR   A 1 48  ? 349.360 1.919   178.203 1.00 181.14 ? 41  THR   A OG1  1 
ATOM   309  C  CG2  . THR   A 1 48  ? 347.845 3.217   179.569 1.00 178.10 ? 41  THR   A CG2  1 
ATOM   310  N  N    . GLY   A 1 49  ? 348.825 -0.481  181.734 1.00 181.41 ? 42  GLY   A N    1 
ATOM   311  C  CA   . GLY   A 1 49  ? 348.759 -1.893  182.083 1.00 186.65 ? 42  GLY   A CA   1 
ATOM   312  C  C    . GLY   A 1 49  ? 347.509 -2.223  182.880 1.00 194.02 ? 42  GLY   A C    1 
ATOM   313  O  O    . GLY   A 1 49  ? 346.450 -1.629  182.640 1.00 193.33 ? 42  GLY   A O    1 
ATOM   314  N  N    . PRO   A 1 50  ? 347.606 -3.149  183.867 1.00 194.89 ? 43  PRO   A N    1 
ATOM   315  C  CA   . PRO   A 1 50  ? 346.421 -3.498  184.683 1.00 200.40 ? 43  PRO   A CA   1 
ATOM   316  C  C    . PRO   A 1 50  ? 345.972 -2.354  185.604 1.00 202.42 ? 43  PRO   A C    1 
ATOM   317  O  O    . PRO   A 1 50  ? 346.747 -1.397  185.760 1.00 195.78 ? 43  PRO   A O    1 
ATOM   318  C  CB   . PRO   A 1 50  ? 346.901 -4.711  185.504 1.00 205.43 ? 43  PRO   A CB   1 
ATOM   319  C  CG   . PRO   A 1 50  ? 348.160 -5.155  184.861 1.00 207.71 ? 43  PRO   A CG   1 
ATOM   320  C  CD   . PRO   A 1 50  ? 348.779 -3.943  184.275 1.00 196.95 ? 43  PRO   A CD   1 
ATOM   321  N  N    . PRO   A 1 51  ? 344.781 -2.418  186.275 1.00 204.20 ? 44  PRO   A N    1 
ATOM   322  C  CA   . PRO   A 1 51  ? 344.391 -1.312  187.182 1.00 201.52 ? 44  PRO   A CA   1 
ATOM   323  C  C    . PRO   A 1 51  ? 345.289 -1.152  188.420 1.00 202.61 ? 44  PRO   A C    1 
ATOM   324  O  O    . PRO   A 1 51  ? 344.993 -0.333  189.292 1.00 201.45 ? 44  PRO   A O    1 
ATOM   325  C  CB   . PRO   A 1 51  ? 342.943 -1.654  187.568 1.00 207.46 ? 44  PRO   A CB   1 
ATOM   326  C  CG   . PRO   A 1 51  ? 342.502 -2.714  186.608 1.00 212.01 ? 44  PRO   A CG   1 
ATOM   327  C  CD   . PRO   A 1 51  ? 343.738 -3.463  186.245 1.00 208.74 ? 44  PRO   A CD   1 
ATOM   328  N  N    . GLU   A 1 52  ? 346.392 -1.928  188.492 1.00 197.79 ? 45  GLU   A N    1 
ATOM   329  C  CA   . GLU   A 1 52  ? 347.347 -1.882  189.592 1.00 194.39 ? 45  GLU   A CA   1 
ATOM   330  C  C    . GLU   A 1 52  ? 348.686 -1.322  189.180 1.00 188.51 ? 45  GLU   A C    1 
ATOM   331  O  O    . GLU   A 1 52  ? 349.277 -0.595  189.974 1.00 183.75 ? 45  GLU   A O    1 
ATOM   332  C  CB   . GLU   A 1 52  ? 347.496 -3.242  190.295 1.00 201.56 ? 45  GLU   A CB   1 
ATOM   333  C  CG   . GLU   A 1 52  ? 347.936 -3.131  191.749 1.00 207.43 ? 45  GLU   A CG   1 
ATOM   334  C  CD   . GLU   A 1 52  ? 347.573 -1.829  192.440 1.00 217.87 ? 45  GLU   A CD   1 
ATOM   335  O  OE1  . GLU   A 1 52  ? 348.496 -1.023  192.699 1.00 218.57 ? 45  GLU   A OE1  1 
ATOM   336  O  OE2  . GLU   A 1 52  ? 346.363 -1.573  192.635 1.00 210.58 ? 45  GLU   A OE2  1 
ATOM   337  N  N    . PHE   A 1 53  ? 349.174 -1.635  187.958 1.00 182.97 ? 46  PHE   A N    1 
ATOM   338  C  CA   . PHE   A 1 53  ? 350.432 -1.045  187.504 1.00 176.07 ? 46  PHE   A CA   1 
ATOM   339  C  C    . PHE   A 1 53  ? 350.243 0.464   187.416 1.00 172.54 ? 46  PHE   A C    1 
ATOM   340  O  O    . PHE   A 1 53  ? 351.062 1.189   187.968 1.00 167.51 ? 46  PHE   A O    1 
ATOM   341  C  CB   . PHE   A 1 53  ? 350.947 -1.615  186.165 1.00 178.79 ? 46  PHE   A CB   1 
ATOM   342  C  CG   . PHE   A 1 53  ? 352.107 -0.808  185.616 1.00 174.07 ? 46  PHE   A CG   1 
ATOM   343  C  CD1  . PHE   A 1 53  ? 353.358 -0.849  186.229 1.00 174.90 ? 46  PHE   A CD1  1 
ATOM   344  C  CD2  . PHE   A 1 53  ? 351.929 0.055   184.539 1.00 172.71 ? 46  PHE   A CD2  1 
ATOM   345  C  CE1  . PHE   A 1 53  ? 354.413 -0.057  185.764 1.00 170.36 ? 46  PHE   A CE1  1 
ATOM   346  C  CE2  . PHE   A 1 53  ? 352.985 0.848   184.075 1.00 170.33 ? 46  PHE   A CE2  1 
ATOM   347  C  CZ   . PHE   A 1 53  ? 354.223 0.781   184.685 1.00 166.30 ? 46  PHE   A CZ   1 
ATOM   348  N  N    . GLU   A 1 54  ? 349.132 0.923   186.790 1.00 168.80 ? 47  GLU   A N    1 
ATOM   349  C  CA   . GLU   A 1 54  ? 348.781 2.340   186.645 1.00 163.71 ? 47  GLU   A CA   1 
ATOM   350  C  C    . GLU   A 1 54  ? 348.690 3.101   187.985 1.00 165.14 ? 47  GLU   A C    1 
ATOM   351  O  O    . GLU   A 1 54  ? 349.080 4.265   188.032 1.00 159.40 ? 47  GLU   A O    1 
ATOM   352  C  CB   . GLU   A 1 54  ? 347.488 2.511   185.843 1.00 168.30 ? 47  GLU   A CB   1 
ATOM   353  C  CG   . GLU   A 1 54  ? 347.625 2.116   184.382 1.00 182.67 ? 47  GLU   A CG   1 
ATOM   354  C  CD   . GLU   A 1 54  ? 346.341 1.979   183.578 1.00 209.72 ? 47  GLU   A CD   1 
ATOM   355  O  OE1  . GLU   A 1 54  ? 345.238 2.116   184.158 1.00 207.26 ? 47  GLU   A OE1  1 
ATOM   356  O  OE2  . GLU   A 1 54  ? 346.443 1.720   182.357 1.00 203.70 ? 47  GLU   A OE2  1 
ATOM   357  N  N    . ARG   A 1 55  ? 348.192 2.448   189.060 1.00 165.92 ? 48  ARG   A N    1 
ATOM   358  C  CA   . ARG   A 1 55  ? 348.049 3.041   190.398 1.00 164.62 ? 48  ARG   A CA   1 
ATOM   359  C  C    . ARG   A 1 55  ? 349.413 3.279   191.075 1.00 165.60 ? 48  ARG   A C    1 
ATOM   360  O  O    . ARG   A 1 55  ? 349.679 4.388   191.566 1.00 160.73 ? 48  ARG   A O    1 
ATOM   361  C  CB   . ARG   A 1 55  ? 347.096 2.210   191.280 1.00 170.16 ? 48  ARG   A CB   1 
ATOM   362  C  CG   . ARG   A 1 55  ? 345.635 2.298   190.839 1.00 177.82 ? 48  ARG   A CG   1 
ATOM   363  C  CD   . ARG   A 1 55  ? 344.661 2.194   191.993 1.00 186.25 ? 48  ARG   A CD   1 
ATOM   364  N  NE   . ARG   A 1 55  ? 344.186 0.825   192.226 1.00 196.49 ? 48  ARG   A NE   1 
ATOM   365  C  CZ   . ARG   A 1 55  ? 342.930 0.407   192.044 1.00 206.08 ? 48  ARG   A CZ   1 
ATOM   366  N  NH1  . ARG   A 1 55  ? 342.597 -0.850  192.315 1.00 206.63 ? 48  ARG   A NH1  1 
ATOM   367  N  NH2  . ARG   A 1 55  ? 341.996 1.245   191.598 1.00 179.67 ? 48  ARG   A NH2  1 
ATOM   368  N  N    . VAL   A 1 56  ? 350.288 2.251   191.059 1.00 164.27 ? 49  VAL   A N    1 
ATOM   369  C  CA   . VAL   A 1 56  ? 351.654 2.302   191.598 1.00 161.11 ? 49  VAL   A CA   1 
ATOM   370  C  C    . VAL   A 1 56  ? 352.422 3.389   190.831 1.00 158.89 ? 49  VAL   A C    1 
ATOM   371  O  O    . VAL   A 1 56  ? 353.058 4.243   191.439 1.00 156.30 ? 49  VAL   A O    1 
ATOM   372  C  CB   . VAL   A 1 56  ? 352.326 0.901   191.484 1.00 169.64 ? 49  VAL   A CB   1 
ATOM   373  C  CG1  . VAL   A 1 56  ? 353.847 0.979   191.567 1.00 166.29 ? 49  VAL   A CG1  1 
ATOM   374  C  CG2  . VAL   A 1 56  ? 351.778 -0.059  192.534 1.00 176.44 ? 49  VAL   A CG2  1 
ATOM   375  N  N    . TYR   A 1 57  ? 352.300 3.377   189.502 1.00 153.81 ? 50  TYR   A N    1 
ATOM   376  C  CA   . TYR   A 1 57  ? 352.918 4.314   188.580 1.00 147.93 ? 50  TYR   A CA   1 
ATOM   377  C  C    . TYR   A 1 57  ? 352.400 5.764   188.751 1.00 147.17 ? 50  TYR   A C    1 
ATOM   378  O  O    . TYR   A 1 57  ? 353.204 6.700   188.693 1.00 140.93 ? 50  TYR   A O    1 
ATOM   379  C  CB   . TYR   A 1 57  ? 352.756 3.794   187.135 1.00 151.13 ? 50  TYR   A CB   1 
ATOM   380  C  CG   . TYR   A 1 57  ? 353.030 4.830   186.078 1.00 149.24 ? 50  TYR   A CG   1 
ATOM   381  C  CD1  . TYR   A 1 57  ? 354.333 5.223   185.781 1.00 148.13 ? 50  TYR   A CD1  1 
ATOM   382  C  CD2  . TYR   A 1 57  ? 351.986 5.470   185.417 1.00 150.29 ? 50  TYR   A CD2  1 
ATOM   383  C  CE1  . TYR   A 1 57  ? 354.591 6.223   184.847 1.00 147.00 ? 50  TYR   A CE1  1 
ATOM   384  C  CE2  . TYR   A 1 57  ? 352.230 6.482   184.493 1.00 148.43 ? 50  TYR   A CE2  1 
ATOM   385  C  CZ   . TYR   A 1 57  ? 353.535 6.846   184.200 1.00 156.04 ? 50  TYR   A CZ   1 
ATOM   386  O  OH   . TYR   A 1 57  ? 353.776 7.840   183.284 1.00 159.12 ? 50  TYR   A OH   1 
ATOM   387  N  N    . ARG   A 1 58  ? 351.070 5.950   188.922 1.00 146.46 ? 51  ARG   A N    1 
ATOM   388  C  CA   . ARG   A 1 58  ? 350.472 7.284   189.069 1.00 143.76 ? 51  ARG   A CA   1 
ATOM   389  C  C    . ARG   A 1 58  ? 350.825 7.911   190.415 1.00 144.33 ? 51  ARG   A C    1 
ATOM   390  O  O    . ARG   A 1 58  ? 351.045 9.128   190.502 1.00 138.08 ? 51  ARG   A O    1 
ATOM   391  C  CB   . ARG   A 1 58  ? 348.954 7.261   188.828 1.00 149.49 ? 51  ARG   A CB   1 
ATOM   392  C  CG   . ARG   A 1 58  ? 348.367 8.658   188.628 1.00 161.62 ? 51  ARG   A CG   1 
ATOM   393  C  CD   . ARG   A 1 58  ? 347.638 8.839   187.309 1.00 177.71 ? 51  ARG   A CD   1 
ATOM   394  N  NE   . ARG   A 1 58  ? 348.470 8.596   186.127 1.00 183.14 ? 51  ARG   A NE   1 
ATOM   395  C  CZ   . ARG   A 1 58  ? 349.305 9.485   185.595 1.00 190.58 ? 51  ARG   A CZ   1 
ATOM   396  N  NH1  . ARG   A 1 58  ? 349.458 10.683  186.154 1.00 165.33 ? 51  ARG   A NH1  1 
ATOM   397  N  NH2  . ARG   A 1 58  ? 349.996 9.182   184.502 1.00 179.55 ? 51  ARG   A NH2  1 
ATOM   398  N  N    . ALA   A 1 59  ? 350.898 7.064   191.461 1.00 144.93 ? 52  ALA   A N    1 
ATOM   399  C  CA   . ALA   A 1 59  ? 351.282 7.477   192.809 1.00 143.59 ? 52  ALA   A CA   1 
ATOM   400  C  C    . ALA   A 1 59  ? 352.680 8.069   192.754 1.00 141.98 ? 52  ALA   A C    1 
ATOM   401  O  O    . ALA   A 1 59  ? 352.927 9.084   193.398 1.00 140.00 ? 52  ALA   A O    1 
ATOM   402  C  CB   . ALA   A 1 59  ? 351.250 6.286   193.753 1.00 149.55 ? 52  ALA   A CB   1 
ATOM   403  N  N    . GLN   A 1 60  ? 353.570 7.470   191.937 1.00 136.38 ? 53  GLN   A N    1 
ATOM   404  C  CA   . GLN   A 1 60  ? 354.948 7.916   191.700 1.00 131.55 ? 53  GLN   A CA   1 
ATOM   405  C  C    . GLN   A 1 60  ? 354.948 9.275   190.999 1.00 130.34 ? 53  GLN   A C    1 
ATOM   406  O  O    . GLN   A 1 60  ? 355.577 10.207  191.473 1.00 126.32 ? 53  GLN   A O    1 
ATOM   407  C  CB   . GLN   A 1 60  ? 355.675 6.857   190.850 1.00 134.38 ? 53  GLN   A CB   1 
ATOM   408  C  CG   . GLN   A 1 60  ? 357.117 7.160   190.465 1.00 147.69 ? 53  GLN   A CG   1 
ATOM   409  C  CD   . GLN   A 1 60  ? 357.247 7.865   189.141 1.00 166.83 ? 53  GLN   A CD   1 
ATOM   410  O  OE1  . GLN   A 1 60  ? 357.603 9.043   189.099 1.00 157.84 ? 53  GLN   A OE1  1 
ATOM   411  N  NE2  . GLN   A 1 60  ? 356.987 7.163   188.030 1.00 165.51 ? 53  GLN   A NE2  1 
ATOM   412  N  N    . VAL   A 1 61  ? 354.225 9.366   189.871 1.00 128.38 ? 54  VAL   A N    1 
ATOM   413  C  CA   . VAL   A 1 61  ? 354.056 10.528  188.987 1.00 124.43 ? 54  VAL   A CA   1 
ATOM   414  C  C    . VAL   A 1 61  ? 353.555 11.727  189.769 1.00 126.95 ? 54  VAL   A C    1 
ATOM   415  O  O    . VAL   A 1 61  ? 354.085 12.817  189.595 1.00 124.42 ? 54  VAL   A O    1 
ATOM   416  C  CB   . VAL   A 1 61  ? 353.163 10.163  187.758 1.00 129.54 ? 54  VAL   A CB   1 
ATOM   417  C  CG1  . VAL   A 1 61  ? 352.714 11.400  186.995 1.00 127.39 ? 54  VAL   A CG1  1 
ATOM   418  C  CG2  . VAL   A 1 61  ? 353.878 9.186   186.824 1.00 129.97 ? 54  VAL   A CG2  1 
ATOM   419  N  N    . ASN   A 1 62  ? 352.591 11.513  190.666 1.00 126.75 ? 55  ASN   A N    1 
ATOM   420  C  CA   . ASN   A 1 62  ? 352.019 12.557  191.514 1.00 126.57 ? 55  ASN   A CA   1 
ATOM   421  C  C    . ASN   A 1 62  ? 352.990 13.083  192.535 1.00 127.74 ? 55  ASN   A C    1 
ATOM   422  O  O    . ASN   A 1 62  ? 353.130 14.296  192.674 1.00 124.48 ? 55  ASN   A O    1 
ATOM   423  C  CB   . ASN   A 1 62  ? 350.773 12.055  192.202 1.00 135.53 ? 55  ASN   A CB   1 
ATOM   424  C  CG   . ASN   A 1 62  ? 349.548 12.667  191.615 1.00 165.10 ? 55  ASN   A CG   1 
ATOM   425  O  OD1  . ASN   A 1 62  ? 349.034 12.218  190.565 1.00 143.50 ? 55  ASN   A OD1  1 
ATOM   426  N  ND2  . ASN   A 1 62  ? 349.122 13.769  192.248 1.00 164.60 ? 55  ASN   A ND2  1 
ATOM   427  N  N    . CYS   A 1 63  ? 353.662 12.174  193.253 1.00 126.37 ? 56  CYS   A N    1 
ATOM   428  C  CA   . CYS   A 1 63  ? 354.661 12.523  194.254 1.00 124.73 ? 56  CYS   A CA   1 
ATOM   429  C  C    . CYS   A 1 63  ? 355.809 13.286  193.637 1.00 124.93 ? 56  CYS   A C    1 
ATOM   430  O  O    . CYS   A 1 63  ? 356.271 14.243  194.247 1.00 123.95 ? 56  CYS   A O    1 
ATOM   431  C  CB   . CYS   A 1 63  ? 355.144 11.286  194.994 1.00 128.32 ? 56  CYS   A CB   1 
ATOM   432  S  SG   . CYS   A 1 63  ? 353.855 10.475  195.959 1.00 138.61 ? 56  CYS   A SG   1 
ATOM   433  N  N    . SER   A 1 64  ? 356.242 12.882  192.425 1.00 120.47 ? 57  SER   A N    1 
ATOM   434  C  CA   . SER   A 1 64  ? 357.288 13.528  191.636 1.00 117.18 ? 57  SER   A CA   1 
ATOM   435  C  C    . SER   A 1 64  ? 356.924 14.973  191.341 1.00 119.41 ? 57  SER   A C    1 
ATOM   436  O  O    . SER   A 1 64  ? 357.771 15.846  191.547 1.00 117.13 ? 57  SER   A O    1 
ATOM   437  C  CB   . SER   A 1 64  ? 357.528 12.769  190.337 1.00 122.14 ? 57  SER   A CB   1 
ATOM   438  O  OG   . SER   A 1 64  ? 358.076 11.498  190.647 1.00 138.74 ? 57  SER   A OG   1 
ATOM   439  N  N    . GLU   A 1 65  ? 355.655 15.231  190.912 1.00 117.01 ? 58  GLU   A N    1 
ATOM   440  C  CA   . GLU   A 1 65  ? 355.103 16.559  190.612 1.00 115.19 ? 58  GLU   A CA   1 
ATOM   441  C  C    . GLU   A 1 65  ? 355.071 17.452  191.820 1.00 117.24 ? 58  GLU   A C    1 
ATOM   442  O  O    . GLU   A 1 65  ? 355.368 18.629  191.717 1.00 115.83 ? 58  GLU   A O    1 
ATOM   443  C  CB   . GLU   A 1 65  ? 353.666 16.436  190.150 1.00 120.15 ? 58  GLU   A CB   1 
ATOM   444  C  CG   . GLU   A 1 65  ? 353.470 15.997  188.716 1.00 141.11 ? 58  GLU   A CG   1 
ATOM   445  C  CD   . GLU   A 1 65  ? 352.054 16.252  188.233 1.00 170.30 ? 58  GLU   A CD   1 
ATOM   446  O  OE1  . GLU   A 1 65  ? 351.277 16.909  188.972 1.00 150.37 ? 58  GLU   A OE1  1 
ATOM   447  O  OE2  . GLU   A 1 65  ? 351.725 15.794  187.112 1.00 165.98 ? 58  GLU   A OE2  1 
ATOM   448  N  N    . TYR   A 1 66  ? 354.641 16.910  192.948 1.00 116.31 ? 59  TYR   A N    1 
ATOM   449  C  CA   . TYR   A 1 66  ? 354.456 17.633  194.194 1.00 116.76 ? 59  TYR   A CA   1 
ATOM   450  C  C    . TYR   A 1 66  ? 355.735 17.880  194.969 1.00 118.12 ? 59  TYR   A C    1 
ATOM   451  O  O    . TYR   A 1 66  ? 355.722 18.721  195.856 1.00 119.88 ? 59  TYR   A O    1 
ATOM   452  C  CB   . TYR   A 1 66  ? 353.407 16.904  195.047 1.00 123.14 ? 59  TYR   A CB   1 
ATOM   453  C  CG   . TYR   A 1 66  ? 352.007 17.408  194.784 1.00 129.02 ? 59  TYR   A CG   1 
ATOM   454  C  CD1  . TYR   A 1 66  ? 351.336 17.084  193.609 1.00 132.87 ? 59  TYR   A CD1  1 
ATOM   455  C  CD2  . TYR   A 1 66  ? 351.379 18.269  195.675 1.00 132.09 ? 59  TYR   A CD2  1 
ATOM   456  C  CE1  . TYR   A 1 66  ? 350.075 17.605  193.329 1.00 138.66 ? 59  TYR   A CE1  1 
ATOM   457  C  CE2  . TYR   A 1 66  ? 350.115 18.792  195.409 1.00 136.45 ? 59  TYR   A CE2  1 
ATOM   458  C  CZ   . TYR   A 1 66  ? 349.464 18.457  194.237 1.00 147.69 ? 59  TYR   A CZ   1 
ATOM   459  O  OH   . TYR   A 1 66  ? 348.197 18.944  194.008 1.00 154.36 ? 59  TYR   A OH   1 
ATOM   460  N  N    . PHE   A 1 67  ? 356.831 17.186  194.638 1.00 111.20 ? 60  PHE   A N    1 
ATOM   461  C  CA   . PHE   A 1 67  ? 358.116 17.320  195.300 1.00 109.10 ? 60  PHE   A CA   1 
ATOM   462  C  C    . PHE   A 1 67  ? 358.677 18.753  195.284 1.00 114.42 ? 60  PHE   A C    1 
ATOM   463  O  O    . PHE   A 1 67  ? 358.995 19.240  196.373 1.00 115.73 ? 60  PHE   A O    1 
ATOM   464  C  CB   . PHE   A 1 67  ? 359.122 16.319  194.750 1.00 110.55 ? 60  PHE   A CB   1 
ATOM   465  C  CG   . PHE   A 1 67  ? 360.342 16.147  195.613 1.00 112.33 ? 60  PHE   A CG   1 
ATOM   466  C  CD1  . PHE   A 1 67  ? 360.229 15.676  196.921 1.00 118.85 ? 60  PHE   A CD1  1 
ATOM   467  C  CD2  . PHE   A 1 67  ? 361.609 16.418  195.114 1.00 112.95 ? 60  PHE   A CD2  1 
ATOM   468  C  CE1  . PHE   A 1 67  ? 361.364 15.505  197.723 1.00 120.68 ? 60  PHE   A CE1  1 
ATOM   469  C  CE2  . PHE   A 1 67  ? 362.748 16.237  195.913 1.00 117.41 ? 60  PHE   A CE2  1 
ATOM   470  C  CZ   . PHE   A 1 67  ? 362.617 15.796  197.217 1.00 118.19 ? 60  PHE   A CZ   1 
ATOM   471  N  N    . PRO   A 1 68  ? 358.769 19.481  194.127 1.00 108.87 ? 61  PRO   A N    1 
ATOM   472  C  CA   . PRO   A 1 68  ? 359.283 20.868  194.153 1.00 105.69 ? 61  PRO   A CA   1 
ATOM   473  C  C    . PRO   A 1 68  ? 358.415 21.850  194.948 1.00 107.95 ? 61  PRO   A C    1 
ATOM   474  O  O    . PRO   A 1 68  ? 358.938 22.824  195.493 1.00 106.71 ? 61  PRO   A O    1 
ATOM   475  C  CB   . PRO   A 1 68  ? 359.301 21.241  192.677 1.00 106.74 ? 61  PRO   A CB   1 
ATOM   476  C  CG   . PRO   A 1 68  ? 359.372 19.956  191.986 1.00 112.14 ? 61  PRO   A CG   1 
ATOM   477  C  CD   . PRO   A 1 68  ? 358.460 19.096  192.741 1.00 110.22 ? 61  PRO   A CD   1 
ATOM   478  N  N    . LEU   A 1 69  ? 357.093 21.591  195.016 1.00 103.59 ? 62  LEU   A N    1 
ATOM   479  C  CA   . LEU   A 1 69  ? 356.152 22.364  195.809 1.00 103.69 ? 62  LEU   A CA   1 
ATOM   480  C  C    . LEU   A 1 69  ? 356.555 22.152  197.263 1.00 110.30 ? 62  LEU   A C    1 
ATOM   481  O  O    . LEU   A 1 69  ? 356.731 23.143  197.985 1.00 111.99 ? 62  LEU   A O    1 
ATOM   482  C  CB   . LEU   A 1 69  ? 354.714 21.875  195.566 1.00 106.38 ? 62  LEU   A CB   1 
ATOM   483  C  CG   . LEU   A 1 69  ? 353.817 22.756  194.719 1.00 110.49 ? 62  LEU   A CG   1 
ATOM   484  C  CD1  . LEU   A 1 69  ? 354.438 23.068  193.406 1.00 108.78 ? 62  LEU   A CD1  1 
ATOM   485  C  CD2  . LEU   A 1 69  ? 352.503 22.114  194.497 1.00 113.50 ? 62  LEU   A CD2  1 
ATOM   486  N  N    . PHE   A 1 70  ? 356.795 20.877  197.675 1.00 106.68 ? 63  PHE   A N    1 
ATOM   487  C  CA   . PHE   A 1 70  ? 357.277 20.561  199.025 1.00 107.71 ? 63  PHE   A CA   1 
ATOM   488  C  C    . PHE   A 1 70  ? 358.597 21.298  199.307 1.00 112.10 ? 63  PHE   A C    1 
ATOM   489  O  O    . PHE   A 1 70  ? 358.654 22.032  200.275 1.00 113.11 ? 63  PHE   A O    1 
ATOM   490  C  CB   . PHE   A 1 70  ? 357.446 19.049  199.209 1.00 110.99 ? 63  PHE   A CB   1 
ATOM   491  C  CG   . PHE   A 1 70  ? 358.410 18.612  200.292 1.00 113.02 ? 63  PHE   A CG   1 
ATOM   492  C  CD1  . PHE   A 1 70  ? 358.129 18.848  201.640 1.00 116.80 ? 63  PHE   A CD1  1 
ATOM   493  C  CD2  . PHE   A 1 70  ? 359.593 17.948  199.968 1.00 113.73 ? 63  PHE   A CD2  1 
ATOM   494  C  CE1  . PHE   A 1 70  ? 358.997 18.397  202.640 1.00 118.49 ? 63  PHE   A CE1  1 
ATOM   495  C  CE2  . PHE   A 1 70  ? 360.481 17.531  200.972 1.00 116.76 ? 63  PHE   A CE2  1 
ATOM   496  C  CZ   . PHE   A 1 70  ? 360.162 17.736  202.298 1.00 116.84 ? 63  PHE   A CZ   1 
ATOM   497  N  N    . LEU   A 1 71  ? 359.631 21.141  198.442 1.00 108.29 ? 64  LEU   A N    1 
ATOM   498  C  CA   . LEU   A 1 71  ? 360.942 21.794  198.567 1.00 106.44 ? 64  LEU   A CA   1 
ATOM   499  C  C    . LEU   A 1 71  ? 360.825 23.302  198.708 1.00 109.51 ? 64  LEU   A C    1 
ATOM   500  O  O    . LEU   A 1 71  ? 361.399 23.848  199.651 1.00 111.81 ? 64  LEU   A O    1 
ATOM   501  C  CB   . LEU   A 1 71  ? 361.854 21.470  197.377 1.00 105.27 ? 64  LEU   A CB   1 
ATOM   502  C  CG   . LEU   A 1 71  ? 362.454 20.080  197.320 1.00 112.78 ? 64  LEU   A CG   1 
ATOM   503  C  CD1  . LEU   A 1 71  ? 363.050 19.816  195.950 1.00 113.04 ? 64  LEU   A CD1  1 
ATOM   504  C  CD2  . LEU   A 1 71  ? 363.509 19.891  198.380 1.00 115.09 ? 64  LEU   A CD2  1 
ATOM   505  N  N    . ALA   A 1 72  ? 360.084 23.977  197.796 1.00 102.46 ? 65  ALA   A N    1 
ATOM   506  C  CA   . ALA   A 1 72  ? 359.892 25.423  197.844 1.00 101.41 ? 65  ALA   A CA   1 
ATOM   507  C  C    . ALA   A 1 72  ? 359.353 25.877  199.219 1.00 109.38 ? 65  ALA   A C    1 
ATOM   508  O  O    . ALA   A 1 72  ? 360.036 26.628  199.920 1.00 107.74 ? 65  ALA   A O    1 
ATOM   509  C  CB   . ALA   A 1 72  ? 358.958 25.855  196.737 1.00 102.21 ? 65  ALA   A CB   1 
ATOM   510  N  N    . THR   A 1 73  ? 358.190 25.323  199.646 1.00 110.98 ? 66  THR   A N    1 
ATOM   511  C  CA   . THR   A 1 73  ? 357.521 25.636  200.925 1.00 113.98 ? 66  THR   A CA   1 
ATOM   512  C  C    . THR   A 1 73  ? 358.400 25.327  202.157 1.00 118.16 ? 66  THR   A C    1 
ATOM   513  O  O    . THR   A 1 73  ? 358.533 26.202  203.013 1.00 120.09 ? 66  THR   A O    1 
ATOM   514  C  CB   . THR   A 1 73  ? 356.129 24.984  201.010 1.00 125.84 ? 66  THR   A CB   1 
ATOM   515  O  OG1  . THR   A 1 73  ? 356.216 23.626  200.601 1.00 129.66 ? 66  THR   A OG1  1 
ATOM   516  C  CG2  . THR   A 1 73  ? 355.121 25.669  200.124 1.00 124.34 ? 66  THR   A CG2  1 
ATOM   517  N  N    . LEU   A 1 74  ? 359.030 24.123  202.226 1.00 112.16 ? 67  LEU   A N    1 
ATOM   518  C  CA   . LEU   A 1 74  ? 359.911 23.679  203.324 1.00 112.04 ? 67  LEU   A CA   1 
ATOM   519  C  C    . LEU   A 1 74  ? 361.040 24.689  203.585 1.00 116.86 ? 67  LEU   A C    1 
ATOM   520  O  O    . LEU   A 1 74  ? 361.357 25.001  204.737 1.00 119.07 ? 67  LEU   A O    1 
ATOM   521  C  CB   . LEU   A 1 74  ? 360.518 22.303  202.975 1.00 110.95 ? 67  LEU   A CB   1 
ATOM   522  C  CG   . LEU   A 1 74  ? 361.606 21.749  203.893 1.00 115.97 ? 67  LEU   A CG   1 
ATOM   523  C  CD1  . LEU   A 1 74  ? 361.021 21.255  205.203 1.00 120.08 ? 67  LEU   A CD1  1 
ATOM   524  C  CD2  . LEU   A 1 74  ? 362.410 20.661  203.193 1.00 115.41 ? 67  LEU   A CD2  1 
ATOM   525  N  N    . TRP   A 1 75  ? 361.639 25.186  202.498 1.00 110.80 ? 68  TRP   A N    1 
ATOM   526  C  CA   . TRP   A 1 75  ? 362.738 26.120  202.531 1.00 109.01 ? 68  TRP   A CA   1 
ATOM   527  C  C    . TRP   A 1 75  ? 362.310 27.545  202.839 1.00 113.57 ? 68  TRP   A C    1 
ATOM   528  O  O    . TRP   A 1 75  ? 363.004 28.216  203.609 1.00 115.30 ? 68  TRP   A O    1 
ATOM   529  C  CB   . TRP   A 1 75  ? 363.517 26.010  201.240 1.00 105.60 ? 68  TRP   A CB   1 
ATOM   530  C  CG   . TRP   A 1 75  ? 364.412 24.810  201.247 1.00 107.13 ? 68  TRP   A CG   1 
ATOM   531  C  CD1  . TRP   A 1 75  ? 364.159 23.588  200.701 1.00 110.07 ? 68  TRP   A CD1  1 
ATOM   532  C  CD2  . TRP   A 1 75  ? 365.694 24.707  201.892 1.00 108.19 ? 68  TRP   A CD2  1 
ATOM   533  N  NE1  . TRP   A 1 75  ? 365.201 22.727  200.965 1.00 110.87 ? 68  TRP   A NE1  1 
ATOM   534  C  CE2  . TRP   A 1 75  ? 366.170 23.399  201.671 1.00 113.08 ? 68  TRP   A CE2  1 
ATOM   535  C  CE3  . TRP   A 1 75  ? 366.499 25.608  202.615 1.00 110.11 ? 68  TRP   A CE3  1 
ATOM   536  C  CZ2  . TRP   A 1 75  ? 367.409 22.960  202.167 1.00 114.41 ? 68  TRP   A CZ2  1 
ATOM   537  C  CZ3  . TRP   A 1 75  ? 367.715 25.167  203.113 1.00 113.30 ? 68  TRP   A CZ3  1 
ATOM   538  C  CH2  . TRP   A 1 75  ? 368.170 23.865  202.872 1.00 114.95 ? 68  TRP   A CH2  1 
ATOM   539  N  N    . VAL   A 1 76  ? 361.164 28.010  202.287 1.00 108.24 ? 69  VAL   A N    1 
ATOM   540  C  CA   . VAL   A 1 76  ? 360.689 29.372  202.560 1.00 108.25 ? 69  VAL   A CA   1 
ATOM   541  C  C    . VAL   A 1 76  ? 360.147 29.464  203.970 1.00 113.80 ? 69  VAL   A C    1 
ATOM   542  O  O    . VAL   A 1 76  ? 360.501 30.392  204.668 1.00 114.37 ? 69  VAL   A O    1 
ATOM   543  C  CB   . VAL   A 1 76  ? 359.718 29.936  201.500 1.00 112.48 ? 69  VAL   A CB   1 
ATOM   544  C  CG1  . VAL   A 1 76  ? 359.280 31.364  201.855 1.00 114.15 ? 69  VAL   A CG1  1 
ATOM   545  C  CG2  . VAL   A 1 76  ? 360.340 29.882  200.098 1.00 109.55 ? 69  VAL   A CG2  1 
ATOM   546  N  N    . ALA   A 1 77  ? 359.337 28.486  204.406 1.00 112.85 ? 70  ALA   A N    1 
ATOM   547  C  CA   . ALA   A 1 77  ? 358.816 28.424  205.777 1.00 116.43 ? 70  ALA   A CA   1 
ATOM   548  C  C    . ALA   A 1 77  ? 359.971 28.259  206.787 1.00 120.58 ? 70  ALA   A C    1 
ATOM   549  O  O    . ALA   A 1 77  ? 359.947 28.908  207.811 1.00 120.80 ? 70  ALA   A O    1 
ATOM   550  C  CB   . ALA   A 1 77  ? 357.828 27.277  205.920 1.00 119.49 ? 70  ALA   A CB   1 
ATOM   551  N  N    . GLY   A 1 78  ? 360.980 27.445  206.457 1.00 117.15 ? 71  GLY   A N    1 
ATOM   552  C  CA   . GLY   A 1 78  ? 362.145 27.187  207.299 1.00 118.38 ? 71  GLY   A CA   1 
ATOM   553  C  C    . GLY   A 1 78  ? 363.074 28.370  207.510 1.00 122.37 ? 71  GLY   A C    1 
ATOM   554  O  O    . GLY   A 1 78  ? 363.789 28.442  208.523 1.00 123.68 ? 71  GLY   A O    1 
ATOM   555  N  N    . ILE   A 1 79  ? 363.068 29.311  206.552 1.00 116.18 ? 72  ILE   A N    1 
ATOM   556  C  CA   . ILE   A 1 79  ? 363.916 30.494  206.610 1.00 114.50 ? 72  ILE   A CA   1 
ATOM   557  C  C    . ILE   A 1 79  ? 363.155 31.742  207.125 1.00 120.31 ? 72  ILE   A C    1 
ATOM   558  O  O    . ILE   A 1 79  ? 363.753 32.488  207.876 1.00 122.32 ? 72  ILE   A O    1 
ATOM   559  C  CB   . ILE   A 1 79  ? 364.626 30.683  205.252 1.00 113.74 ? 72  ILE   A CB   1 
ATOM   560  C  CG1  . ILE   A 1 79  ? 365.785 29.668  205.182 1.00 112.99 ? 72  ILE   A CG1  1 
ATOM   561  C  CG2  . ILE   A 1 79  ? 365.137 32.109  205.081 1.00 114.87 ? 72  ILE   A CG2  1 
ATOM   562  C  CD1  . ILE   A 1 79  ? 366.226 29.308  203.923 1.00 124.39 ? 72  ILE   A CD1  1 
ATOM   563  N  N    . PHE   A 1 80  ? 361.846 31.912  206.825 1.00 117.69 ? 73  PHE   A N    1 
ATOM   564  C  CA   . PHE   A 1 80  ? 361.065 33.078  207.244 1.00 120.21 ? 73  PHE   A CA   1 
ATOM   565  C  C    . PHE   A 1 80  ? 360.226 32.851  208.517 1.00 130.36 ? 73  PHE   A C    1 
ATOM   566  O  O    . PHE   A 1 80  ? 359.908 33.823  209.188 1.00 135.75 ? 73  PHE   A O    1 
ATOM   567  C  CB   . PHE   A 1 80  ? 360.245 33.630  206.078 1.00 121.30 ? 73  PHE   A CB   1 
ATOM   568  C  CG   . PHE   A 1 80  ? 361.183 34.188  205.019 1.00 121.21 ? 73  PHE   A CG   1 
ATOM   569  C  CD1  . PHE   A 1 80  ? 361.764 33.352  204.064 1.00 121.50 ? 73  PHE   A CD1  1 
ATOM   570  C  CD2  . PHE   A 1 80  ? 361.569 35.528  205.040 1.00 125.99 ? 73  PHE   A CD2  1 
ATOM   571  C  CE1  . PHE   A 1 80  ? 362.686 33.853  203.130 1.00 122.75 ? 73  PHE   A CE1  1 
ATOM   572  C  CE2  . PHE   A 1 80  ? 362.477 36.032  204.098 1.00 125.16 ? 73  PHE   A CE2  1 
ATOM   573  C  CZ   . PHE   A 1 80  ? 363.031 35.191  203.150 1.00 122.04 ? 73  PHE   A CZ   1 
ATOM   574  N  N    . PHE   A 1 81  ? 359.983 31.596  208.915 1.00 127.02 ? 74  PHE   A N    1 
ATOM   575  C  CA   . PHE   A 1 81  ? 359.334 31.168  210.176 1.00 130.76 ? 74  PHE   A CA   1 
ATOM   576  C  C    . PHE   A 1 81  ? 360.317 30.120  210.791 1.00 139.71 ? 74  PHE   A C    1 
ATOM   577  O  O    . PHE   A 1 81  ? 361.190 29.654  210.053 1.00 138.55 ? 74  PHE   A O    1 
ATOM   578  C  CB   . PHE   A 1 81  ? 357.961 30.523  209.886 1.00 132.53 ? 74  PHE   A CB   1 
ATOM   579  C  CG   . PHE   A 1 81  ? 357.057 30.459  211.086 1.00 138.54 ? 74  PHE   A CG   1 
ATOM   580  C  CD1  . PHE   A 1 81  ? 357.121 29.388  211.971 1.00 142.08 ? 74  PHE   A CD1  1 
ATOM   581  C  CD2  . PHE   A 1 81  ? 356.179 31.499  211.370 1.00 143.96 ? 74  PHE   A CD2  1 
ATOM   582  C  CE1  . PHE   A 1 81  ? 356.342 29.372  213.130 1.00 150.34 ? 74  PHE   A CE1  1 
ATOM   583  C  CE2  . PHE   A 1 81  ? 355.384 31.471  212.519 1.00 150.06 ? 74  PHE   A CE2  1 
ATOM   584  C  CZ   . PHE   A 1 81  ? 355.467 30.405  213.386 1.00 151.44 ? 74  PHE   A CZ   1 
ATOM   585  N  N    . HIS   A 1 82  ? 360.065 29.583  211.978 1.00 140.68 ? 75  HIS   A N    1 
ATOM   586  C  CA   . HIS   A 1 82  ? 360.966 28.557  212.579 1.00 141.71 ? 75  HIS   A CA   1 
ATOM   587  C  C    . HIS   A 1 82  ? 361.393 27.418  211.639 1.00 137.51 ? 75  HIS   A C    1 
ATOM   588  O  O    . HIS   A 1 82  ? 360.510 26.787  211.031 1.00 136.08 ? 75  HIS   A O    1 
ATOM   589  C  CB   . HIS   A 1 82  ? 360.327 27.952  213.833 1.00 150.51 ? 75  HIS   A CB   1 
ATOM   590  C  CG   . HIS   A 1 82  ? 361.265 27.117  214.636 1.00 159.63 ? 75  HIS   A CG   1 
ATOM   591  N  ND1  . HIS   A 1 82  ? 360.862 25.999  215.332 1.00 167.79 ? 75  HIS   A ND1  1 
ATOM   592  C  CD2  . HIS   A 1 82  ? 362.580 27.235  214.854 1.00 162.01 ? 75  HIS   A CD2  1 
ATOM   593  C  CE1  . HIS   A 1 82  ? 361.908 25.469  215.948 1.00 169.43 ? 75  HIS   A CE1  1 
ATOM   594  N  NE2  . HIS   A 1 82  ? 362.963 26.201  215.668 1.00 166.17 ? 75  HIS   A NE2  1 
ATOM   595  N  N    . GLU   A 1 83  ? 362.697 27.140  211.544 1.00 128.44 ? 76  GLU   A N    1 
ATOM   596  C  CA   . GLU   A 1 83  ? 363.290 26.024  210.797 1.00 124.53 ? 76  GLU   A CA   1 
ATOM   597  C  C    . GLU   A 1 83  ? 362.840 24.642  211.326 1.00 134.58 ? 76  GLU   A C    1 
ATOM   598  O  O    . GLU   A 1 83  ? 362.657 23.720  210.524 1.00 135.19 ? 76  GLU   A O    1 
ATOM   599  C  CB   . GLU   A 1 83  ? 364.835 26.142  210.845 1.00 124.15 ? 76  GLU   A CB   1 
ATOM   600  C  CG   . GLU   A 1 83  ? 365.641 25.065  210.133 1.00 129.55 ? 76  GLU   A CG   1 
ATOM   601  C  CD   . GLU   A 1 83  ? 366.972 24.608  210.715 1.00 158.34 ? 76  GLU   A CD   1 
ATOM   602  O  OE1  . GLU   A 1 83  ? 367.286 24.930  211.885 1.00 170.54 ? 76  GLU   A OE1  1 
ATOM   603  O  OE2  . GLU   A 1 83  ? 367.701 23.899  209.988 1.00 155.66 ? 76  GLU   A OE2  1 
ATOM   604  N  N    . GLY   A 1 84  ? 362.715 24.497  212.648 1.00 135.60 ? 77  GLY   A N    1 
ATOM   605  C  CA   . GLY   A 1 84  ? 362.295 23.260  213.301 1.00 139.81 ? 77  GLY   A CA   1 
ATOM   606  C  C    . GLY   A 1 84  ? 360.850 22.940  212.999 1.00 145.19 ? 77  GLY   A C    1 
ATOM   607  O  O    . GLY   A 1 84  ? 360.515 21.793  212.689 1.00 145.82 ? 77  GLY   A O    1 
ATOM   608  N  N    . ALA   A 1 85  ? 359.996 23.979  213.040 1.00 142.61 ? 78  ALA   A N    1 
ATOM   609  C  CA   . ALA   A 1 85  ? 358.570 23.907  212.726 1.00 144.55 ? 78  ALA   A CA   1 
ATOM   610  C  C    . ALA   A 1 85  ? 358.385 23.477  211.273 1.00 143.49 ? 78  ALA   A C    1 
ATOM   611  O  O    . ALA   A 1 85  ? 357.649 22.526  211.014 1.00 146.30 ? 78  ALA   A O    1 
ATOM   612  C  CB   . ALA   A 1 85  ? 357.925 25.260  212.958 1.00 146.45 ? 78  ALA   A CB   1 
ATOM   613  N  N    . ALA   A 1 86  ? 359.098 24.129  210.335 1.00 132.68 ? 79  ALA   A N    1 
ATOM   614  C  CA   . ALA   A 1 86  ? 359.074 23.778  208.921 1.00 127.17 ? 79  ALA   A CA   1 
ATOM   615  C  C    . ALA   A 1 86  ? 359.582 22.357  208.726 1.00 133.49 ? 79  ALA   A C    1 
ATOM   616  O  O    . ALA   A 1 86  ? 358.960 21.613  207.976 1.00 134.10 ? 79  ALA   A O    1 
ATOM   617  C  CB   . ALA   A 1 86  ? 359.907 24.750  208.115 1.00 122.27 ? 79  ALA   A CB   1 
ATOM   618  N  N    . ALA   A 1 87  ? 360.666 21.959  209.438 1.00 132.23 ? 80  ALA   A N    1 
ATOM   619  C  CA   . ALA   A 1 87  ? 361.242 20.604  209.373 1.00 133.50 ? 80  ALA   A CA   1 
ATOM   620  C  C    . ALA   A 1 87  ? 360.253 19.552  209.884 1.00 142.77 ? 80  ALA   A C    1 
ATOM   621  O  O    . ALA   A 1 87  ? 360.240 18.441  209.355 1.00 143.42 ? 80  ALA   A O    1 
ATOM   622  C  CB   . ALA   A 1 87  ? 362.557 20.529  210.148 1.00 135.69 ? 80  ALA   A CB   1 
ATOM   623  N  N    . LEU   A 1 88  ? 359.397 19.918  210.872 1.00 142.84 ? 81  LEU   A N    1 
ATOM   624  C  CA   . LEU   A 1 88  ? 358.358 19.044  211.421 1.00 147.94 ? 81  LEU   A CA   1 
ATOM   625  C  C    . LEU   A 1 88  ? 357.256 18.790  210.378 1.00 149.69 ? 81  LEU   A C    1 
ATOM   626  O  O    . LEU   A 1 88  ? 356.985 17.622  210.094 1.00 151.47 ? 81  LEU   A O    1 
ATOM   627  C  CB   . LEU   A 1 88  ? 357.760 19.620  212.722 1.00 153.73 ? 81  LEU   A CB   1 
ATOM   628  C  CG   . LEU   A 1 88  ? 358.004 18.887  214.073 1.00 165.73 ? 81  LEU   A CG   1 
ATOM   629  C  CD1  . LEU   A 1 88  ? 358.020 17.368  213.924 1.00 168.67 ? 81  LEU   A CD1  1 
ATOM   630  C  CD2  . LEU   A 1 88  ? 359.253 19.387  214.780 1.00 167.39 ? 81  LEU   A CD2  1 
ATOM   631  N  N    . CYS   A 1 89  ? 356.656 19.859  209.767 1.00 142.47 ? 82  CYS   A N    1 
ATOM   632  C  CA   . CYS   A 1 89  ? 355.620 19.692  208.719 1.00 141.37 ? 82  CYS   A CA   1 
ATOM   633  C  C    . CYS   A 1 89  ? 356.202 18.983  207.505 1.00 141.27 ? 82  CYS   A C    1 
ATOM   634  O  O    . CYS   A 1 89  ? 355.490 18.247  206.828 1.00 142.30 ? 82  CYS   A O    1 
ATOM   635  C  CB   . CYS   A 1 89  ? 354.961 21.009  208.311 1.00 139.71 ? 82  CYS   A CB   1 
ATOM   636  S  SG   . CYS   A 1 89  ? 354.629 22.148  209.672 1.00 147.93 ? 82  CYS   A SG   1 
ATOM   637  N  N    . GLY   A 1 90  ? 357.482 19.232  207.239 1.00 133.40 ? 83  GLY   A N    1 
ATOM   638  C  CA   . GLY   A 1 90  ? 358.235 18.598  206.167 1.00 129.75 ? 83  GLY   A CA   1 
ATOM   639  C  C    . GLY   A 1 90  ? 358.303 17.098  206.375 1.00 137.80 ? 83  GLY   A C    1 
ATOM   640  O  O    . GLY   A 1 90  ? 358.183 16.344  205.406 1.00 137.52 ? 83  GLY   A O    1 
ATOM   641  N  N    . LEU   A 1 91  ? 358.441 16.650  207.657 1.00 137.65 ? 84  LEU   A N    1 
ATOM   642  C  CA   . LEU   A 1 91  ? 358.452 15.225  208.027 1.00 141.32 ? 84  LEU   A CA   1 
ATOM   643  C  C    . LEU   A 1 91  ? 357.037 14.628  207.933 1.00 147.47 ? 84  LEU   A C    1 
ATOM   644  O  O    . LEU   A 1 91  ? 356.885 13.504  207.462 1.00 149.05 ? 84  LEU   A O    1 
ATOM   645  C  CB   . LEU   A 1 91  ? 359.032 15.008  209.432 1.00 145.78 ? 84  LEU   A CB   1 
ATOM   646  C  CG   . LEU   A 1 91  ? 360.545 15.033  209.554 1.00 148.00 ? 84  LEU   A CG   1 
ATOM   647  C  CD1  . LEU   A 1 91  ? 360.953 15.456  210.927 1.00 152.03 ? 84  LEU   A CD1  1 
ATOM   648  C  CD2  . LEU   A 1 91  ? 361.147 13.688  209.235 1.00 150.91 ? 84  LEU   A CD2  1 
ATOM   649  N  N    . VAL   A 1 92  ? 356.013 15.394  208.374 1.00 143.81 ? 85  VAL   A N    1 
ATOM   650  C  CA   . VAL   A 1 92  ? 354.587 15.047  208.325 1.00 146.52 ? 85  VAL   A CA   1 
ATOM   651  C  C    . VAL   A 1 92  ? 354.168 14.811  206.863 1.00 145.96 ? 85  VAL   A C    1 
ATOM   652  O  O    . VAL   A 1 92  ? 353.602 13.758  206.558 1.00 149.02 ? 85  VAL   A O    1 
ATOM   653  C  CB   . VAL   A 1 92  ? 353.740 16.152  209.005 1.00 151.59 ? 85  VAL   A CB   1 
ATOM   654  C  CG1  . VAL   A 1 92  ? 352.267 16.049  208.636 1.00 154.18 ? 85  VAL   A CG1  1 
ATOM   655  C  CG2  . VAL   A 1 92  ? 353.923 16.130  210.515 1.00 157.15 ? 85  VAL   A CG2  1 
ATOM   656  N  N    . TYR   A 1 93  ? 354.476 15.783  205.969 1.00 135.39 ? 86  TYR   A N    1 
ATOM   657  C  CA   . TYR   A 1 93  ? 354.174 15.716  204.539 1.00 131.05 ? 86  TYR   A CA   1 
ATOM   658  C  C    . TYR   A 1 93  ? 354.788 14.464  203.942 1.00 134.62 ? 86  TYR   A C    1 
ATOM   659  O  O    . TYR   A 1 93  ? 354.048 13.628  203.431 1.00 137.70 ? 86  TYR   A O    1 
ATOM   660  C  CB   . TYR   A 1 93  ? 354.633 16.984  203.796 1.00 125.54 ? 86  TYR   A CB   1 
ATOM   661  C  CG   . TYR   A 1 93  ? 354.600 16.835  202.296 1.00 124.10 ? 86  TYR   A CG   1 
ATOM   662  C  CD1  . TYR   A 1 93  ? 355.707 16.357  201.598 1.00 122.07 ? 86  TYR   A CD1  1 
ATOM   663  C  CD2  . TYR   A 1 93  ? 353.460 17.165  201.565 1.00 126.99 ? 86  TYR   A CD2  1 
ATOM   664  C  CE1  . TYR   A 1 93  ? 355.674 16.188  200.213 1.00 120.70 ? 86  TYR   A CE1  1 
ATOM   665  C  CE2  . TYR   A 1 93  ? 353.408 16.981  200.178 1.00 125.72 ? 86  TYR   A CE2  1 
ATOM   666  C  CZ   . TYR   A 1 93  ? 354.520 16.493  199.507 1.00 126.79 ? 86  TYR   A CZ   1 
ATOM   667  O  OH   . TYR   A 1 93  ? 354.496 16.291  198.147 1.00 122.26 ? 86  TYR   A OH   1 
ATOM   668  N  N    . LEU   A 1 94  ? 356.121 14.311  204.046 1.00 127.95 ? 87  LEU   A N    1 
ATOM   669  C  CA   . LEU   A 1 94  ? 356.830 13.137  203.541 1.00 127.52 ? 87  LEU   A CA   1 
ATOM   670  C  C    . LEU   A 1 94  ? 356.254 11.820  204.053 1.00 140.38 ? 87  LEU   A C    1 
ATOM   671  O  O    . LEU   A 1 94  ? 356.045 10.921  203.236 1.00 142.64 ? 87  LEU   A O    1 
ATOM   672  C  CB   . LEU   A 1 94  ? 358.319 13.203  203.844 1.00 125.01 ? 87  LEU   A CB   1 
ATOM   673  C  CG   . LEU   A 1 94  ? 359.114 14.216  203.073 1.00 122.24 ? 87  LEU   A CG   1 
ATOM   674  C  CD1  . LEU   A 1 94  ? 360.553 14.196  203.520 1.00 121.23 ? 87  LEU   A CD1  1 
ATOM   675  C  CD2  . LEU   A 1 94  ? 358.971 14.019  201.585 1.00 120.10 ? 87  LEU   A CD2  1 
ATOM   676  N  N    . PHE   A 1 95  ? 355.963 11.706  205.381 1.00 141.56 ? 88  PHE   A N    1 
ATOM   677  C  CA   . PHE   A 1 95  ? 355.370 10.489  205.953 1.00 147.88 ? 88  PHE   A CA   1 
ATOM   678  C  C    . PHE   A 1 95  ? 353.985 10.209  205.367 1.00 151.07 ? 88  PHE   A C    1 
ATOM   679  O  O    . PHE   A 1 95  ? 353.724 9.075   204.976 1.00 152.49 ? 88  PHE   A O    1 
ATOM   680  C  CB   . PHE   A 1 95  ? 355.361 10.482  207.494 1.00 155.59 ? 88  PHE   A CB   1 
ATOM   681  C  CG   . PHE   A 1 95  ? 354.761 9.214   208.073 1.00 166.38 ? 88  PHE   A CG   1 
ATOM   682  C  CD1  . PHE   A 1 95  ? 355.242 7.956   207.700 1.00 171.56 ? 88  PHE   A CD1  1 
ATOM   683  C  CD2  . PHE   A 1 95  ? 353.705 9.273   208.977 1.00 175.02 ? 88  PHE   A CD2  1 
ATOM   684  C  CE1  . PHE   A 1 95  ? 354.672 6.788   208.218 1.00 179.93 ? 88  PHE   A CE1  1 
ATOM   685  C  CE2  . PHE   A 1 95  ? 353.143 8.098   209.501 1.00 183.31 ? 88  PHE   A CE2  1 
ATOM   686  C  CZ   . PHE   A 1 95  ? 353.636 6.869   209.121 1.00 182.35 ? 88  PHE   A CZ   1 
ATOM   687  N  N    . ALA   A 1 96  ? 353.141 11.258  205.234 1.00 145.83 ? 89  ALA   A N    1 
ATOM   688  C  CA   . ALA   A 1 96  ? 351.815 11.182  204.614 1.00 147.41 ? 89  ALA   A CA   1 
ATOM   689  C  C    . ALA   A 1 96  ? 351.936 10.691  203.168 1.00 149.51 ? 89  ALA   A C    1 
ATOM   690  O  O    . ALA   A 1 96  ? 351.068 9.951   202.704 1.00 153.20 ? 89  ALA   A O    1 
ATOM   691  C  CB   . ALA   A 1 96  ? 351.139 12.544  204.642 1.00 145.97 ? 89  ALA   A CB   1 
ATOM   692  N  N    . ARG   A 1 97  ? 353.023 11.078  202.465 1.00 140.09 ? 90  ARG   A N    1 
ATOM   693  C  CA   . ARG   A 1 97  ? 353.273 10.645  201.091 1.00 136.71 ? 90  ARG   A CA   1 
ATOM   694  C  C    . ARG   A 1 97  ? 353.574 9.155   200.968 1.00 144.34 ? 90  ARG   A C    1 
ATOM   695  O  O    . ARG   A 1 97  ? 353.145 8.546   199.991 1.00 145.02 ? 90  ARG   A O    1 
ATOM   696  C  CB   . ARG   A 1 97  ? 354.362 11.484  200.428 1.00 129.40 ? 90  ARG   A CB   1 
ATOM   697  C  CG   . ARG   A 1 97  ? 353.845 12.799  199.881 1.00 132.36 ? 90  ARG   A CG   1 
ATOM   698  C  CD   . ARG   A 1 97  ? 352.994 12.601  198.638 1.00 132.38 ? 90  ARG   A CD   1 
ATOM   699  N  NE   . ARG   A 1 97  ? 352.162 13.772  198.417 1.00 134.84 ? 90  ARG   A NE   1 
ATOM   700  C  CZ   . ARG   A 1 97  ? 351.400 13.971  197.356 1.00 140.15 ? 90  ARG   A CZ   1 
ATOM   701  N  NH1  . ARG   A 1 97  ? 351.352 13.071  196.389 1.00 122.57 ? 90  ARG   A NH1  1 
ATOM   702  N  NH2  . ARG   A 1 97  ? 350.679 15.078  197.251 1.00 137.86 ? 90  ARG   A NH2  1 
ATOM   703  N  N    . LEU   A 1 98  ? 354.288 8.562   201.954 1.00 143.14 ? 91  LEU   A N    1 
ATOM   704  C  CA   . LEU   A 1 98  ? 354.591 7.131   201.966 1.00 146.72 ? 91  LEU   A CA   1 
ATOM   705  C  C    . LEU   A 1 98  ? 353.265 6.409   202.065 1.00 156.85 ? 91  LEU   A C    1 
ATOM   706  O  O    . LEU   A 1 98  ? 353.012 5.509   201.263 1.00 160.32 ? 91  LEU   A O    1 
ATOM   707  C  CB   . LEU   A 1 98  ? 355.467 6.758   203.168 1.00 149.93 ? 91  LEU   A CB   1 
ATOM   708  C  CG   . LEU   A 1 98  ? 356.651 5.811   202.931 1.00 155.27 ? 91  LEU   A CG   1 
ATOM   709  C  CD1  . LEU   A 1 98  ? 357.269 5.387   204.257 1.00 160.36 ? 91  LEU   A CD1  1 
ATOM   710  C  CD2  . LEU   A 1 98  ? 356.270 4.573   202.111 1.00 158.98 ? 91  LEU   A CD2  1 
ATOM   711  N  N    . ARG   A 1 99  ? 352.387 6.851   203.005 1.00 154.45 ? 92  ARG   A N    1 
ATOM   712  C  CA   . ARG   A 1 99  ? 351.037 6.308   203.194 1.00 159.53 ? 92  ARG   A CA   1 
ATOM   713  C  C    . ARG   A 1 99  ? 350.204 6.491   201.913 1.00 159.50 ? 92  ARG   A C    1 
ATOM   714  O  O    . ARG   A 1 99  ? 349.560 5.539   201.497 1.00 163.22 ? 92  ARG   A O    1 
ATOM   715  C  CB   . ARG   A 1 99  ? 350.330 6.953   204.390 1.00 161.50 ? 92  ARG   A CB   1 
ATOM   716  C  CG   . ARG   A 1 99  ? 350.855 6.555   205.759 1.00 177.28 ? 92  ARG   A CG   1 
ATOM   717  C  CD   . ARG   A 1 99  ? 351.035 7.789   206.636 1.00 192.70 ? 92  ARG   A CD   1 
ATOM   718  N  NE   . ARG   A 1 99  ? 349.787 8.531   206.847 1.00 205.01 ? 92  ARG   A NE   1 
ATOM   719  C  CZ   . ARG   A 1 99  ? 349.702 9.732   207.416 1.00 218.03 ? 92  ARG   A CZ   1 
ATOM   720  N  NH1  . ARG   A 1 99  ? 350.796 10.353  207.843 1.00 209.20 ? 92  ARG   A NH1  1 
ATOM   721  N  NH2  . ARG   A 1 99  ? 348.523 10.322  207.562 1.00 212.38 ? 92  ARG   A NH2  1 
ATOM   722  N  N    . TYR   A 1 100 ? 350.270 7.686   201.265 1.00 148.90 ? 93  TYR   A N    1 
ATOM   723  C  CA   . TYR   A 1 100 ? 349.585 8.005   200.004 1.00 145.71 ? 93  TYR   A CA   1 
ATOM   724  C  C    . TYR   A 1 100 ? 349.933 6.953   198.976 1.00 149.87 ? 93  TYR   A C    1 
ATOM   725  O  O    . TYR   A 1 100 ? 349.033 6.395   198.356 1.00 152.36 ? 93  TYR   A O    1 
ATOM   726  C  CB   . TYR   A 1 100 ? 350.009 9.399   199.463 1.00 138.90 ? 93  TYR   A CB   1 
ATOM   727  C  CG   . TYR   A 1 100 ? 349.544 9.664   198.040 1.00 136.25 ? 93  TYR   A CG   1 
ATOM   728  C  CD1  . TYR   A 1 100 ? 348.281 10.182  197.787 1.00 140.69 ? 93  TYR   A CD1  1 
ATOM   729  C  CD2  . TYR   A 1 100 ? 350.369 9.388   196.946 1.00 131.81 ? 93  TYR   A CD2  1 
ATOM   730  C  CE1  . TYR   A 1 100 ? 347.834 10.398  196.485 1.00 140.89 ? 93  TYR   A CE1  1 
ATOM   731  C  CE2  . TYR   A 1 100 ? 349.924 9.586   195.635 1.00 130.90 ? 93  TYR   A CE2  1 
ATOM   732  C  CZ   . TYR   A 1 100 ? 348.645 10.079  195.410 1.00 140.39 ? 93  TYR   A CZ   1 
ATOM   733  O  OH   . TYR   A 1 100 ? 348.139 10.285  194.141 1.00 135.60 ? 93  TYR   A OH   1 
ATOM   734  N  N    . PHE   A 1 101 ? 351.249 6.730   198.763 1.00 144.08 ? 94  PHE   A N    1 
ATOM   735  C  CA   . PHE   A 1 101 ? 351.784 5.778   197.798 1.00 144.29 ? 94  PHE   A CA   1 
ATOM   736  C  C    . PHE   A 1 101 ? 351.278 4.378   198.125 1.00 157.65 ? 94  PHE   A C    1 
ATOM   737  O  O    . PHE   A 1 101 ? 350.634 3.759   197.275 1.00 160.25 ? 94  PHE   A O    1 
ATOM   738  C  CB   . PHE   A 1 101 ? 353.319 5.834   197.774 1.00 141.96 ? 94  PHE   A CB   1 
ATOM   739  C  CG   . PHE   A 1 101 ? 353.942 5.043   196.654 1.00 143.19 ? 94  PHE   A CG   1 
ATOM   740  C  CD1  . PHE   A 1 101 ? 354.163 5.622   195.414 1.00 140.91 ? 94  PHE   A CD1  1 
ATOM   741  C  CD2  . PHE   A 1 101 ? 354.303 3.715   196.835 1.00 152.06 ? 94  PHE   A CD2  1 
ATOM   742  C  CE1  . PHE   A 1 101 ? 354.719 4.885   194.367 1.00 144.17 ? 94  PHE   A CE1  1 
ATOM   743  C  CE2  . PHE   A 1 101 ? 354.847 2.971   195.785 1.00 153.34 ? 94  PHE   A CE2  1 
ATOM   744  C  CZ   . PHE   A 1 101 ? 355.063 3.564   194.561 1.00 147.56 ? 94  PHE   A CZ   1 
ATOM   745  N  N    . GLN   A 1 102 ? 351.498 3.920   199.379 1.00 158.74 ? 95  GLN   A N    1 
ATOM   746  C  CA   . GLN   A 1 102 ? 351.078 2.604   199.889 1.00 166.54 ? 95  GLN   A CA   1 
ATOM   747  C  C    . GLN   A 1 102 ? 349.544 2.324   199.772 1.00 175.18 ? 95  GLN   A C    1 
ATOM   748  O  O    . GLN   A 1 102 ? 349.149 1.173   199.573 1.00 180.01 ? 95  GLN   A O    1 
ATOM   749  C  CB   . GLN   A 1 102 ? 351.574 2.419   201.339 1.00 171.26 ? 95  GLN   A CB   1 
ATOM   750  C  CG   . GLN   A 1 102 ? 353.086 2.173   201.451 1.00 169.82 ? 95  GLN   A CG   1 
ATOM   751  C  CD   . GLN   A 1 102 ? 353.625 2.151   202.868 1.00 185.17 ? 95  GLN   A CD   1 
ATOM   752  O  OE1  . GLN   A 1 102 ? 354.718 1.636   203.127 1.00 179.10 ? 95  GLN   A OE1  1 
ATOM   753  N  NE2  . GLN   A 1 102 ? 352.909 2.739   203.817 1.00 180.23 ? 95  GLN   A NE2  1 
ATOM   754  N  N    . GLY   A 1 103 ? 348.730 3.379   199.902 1.00 170.67 ? 96  GLY   A N    1 
ATOM   755  C  CA   . GLY   A 1 103 ? 347.273 3.356   199.804 1.00 175.79 ? 96  GLY   A CA   1 
ATOM   756  C  C    . GLY   A 1 103 ? 346.806 3.208   198.371 1.00 179.95 ? 96  GLY   A C    1 
ATOM   757  O  O    . GLY   A 1 103 ? 345.964 2.355   198.085 1.00 186.04 ? 96  GLY   A O    1 
ATOM   758  N  N    . TYR   A 1 104 ? 347.381 4.020   197.458 1.00 169.90 ? 97  TYR   A N    1 
ATOM   759  C  CA   . TYR   A 1 104 ? 347.136 4.006   196.009 1.00 167.88 ? 97  TYR   A CA   1 
ATOM   760  C  C    . TYR   A 1 104 ? 347.587 2.653   195.428 1.00 175.25 ? 97  TYR   A C    1 
ATOM   761  O  O    . TYR   A 1 104 ? 346.898 2.099   194.568 1.00 177.73 ? 97  TYR   A O    1 
ATOM   762  C  CB   . TYR   A 1 104 ? 347.937 5.141   195.333 1.00 160.44 ? 97  TYR   A CB   1 
ATOM   763  C  CG   . TYR   A 1 104 ? 347.290 5.824   194.140 1.00 159.91 ? 97  TYR   A CG   1 
ATOM   764  C  CD1  . TYR   A 1 104 ? 346.341 5.170   193.360 1.00 166.54 ? 97  TYR   A CD1  1 
ATOM   765  C  CD2  . TYR   A 1 104 ? 347.683 7.095   193.748 1.00 154.65 ? 97  TYR   A CD2  1 
ATOM   766  C  CE1  . TYR   A 1 104 ? 345.761 5.792   192.252 1.00 165.62 ? 97  TYR   A CE1  1 
ATOM   767  C  CE2  . TYR   A 1 104 ? 347.116 7.722   192.639 1.00 153.95 ? 97  TYR   A CE2  1 
ATOM   768  C  CZ   . TYR   A 1 104 ? 346.150 7.073   191.900 1.00 161.46 ? 97  TYR   A CZ   1 
ATOM   769  O  OH   . TYR   A 1 104 ? 345.612 7.724   190.817 1.00 157.96 ? 97  TYR   A OH   1 
ATOM   770  N  N    . ALA   A 1 105 ? 348.736 2.120   195.925 1.00 172.13 ? 98  ALA   A N    1 
ATOM   771  C  CA   . ALA   A 1 105 ? 349.305 0.826   195.546 1.00 175.97 ? 98  ALA   A CA   1 
ATOM   772  C  C    . ALA   A 1 105 ? 348.341 -0.332  195.901 1.00 191.90 ? 98  ALA   A C    1 
ATOM   773  O  O    . ALA   A 1 105 ? 348.550 -1.470  195.474 1.00 193.94 ? 98  ALA   A O    1 
ATOM   774  C  CB   . ALA   A 1 105 ? 350.661 0.632   196.210 1.00 175.03 ? 98  ALA   A CB   1 
ATOM   775  N  N    . ARG   A 1 106 ? 347.280 -0.026  196.679 1.00 192.58 ? 99  ARG   A N    1 
ATOM   776  C  CA   . ARG   A 1 106 ? 346.188 -0.936  197.011 1.00 196.03 ? 99  ARG   A CA   1 
ATOM   777  C  C    . ARG   A 1 106 ? 345.009 -0.448  196.156 1.00 200.29 ? 99  ARG   A C    1 
ATOM   778  O  O    . ARG   A 1 106 ? 344.951 -0.831  194.990 1.00 201.38 ? 99  ARG   A O    1 
ATOM   779  C  CB   . ARG   A 1 106 ? 345.888 -0.962  198.520 1.00 197.39 ? 99  ARG   A CB   1 
ATOM   780  C  CG   . ARG   A 1 106 ? 346.282 -2.281  199.165 1.00 207.55 ? 99  ARG   A CG   1 
ATOM   781  C  CD   . ARG   A 1 106 ? 346.852 -2.055  200.545 1.00 215.81 ? 99  ARG   A CD   1 
ATOM   782  N  NE   . ARG   A 1 106 ? 345.908 -2.439  201.594 1.00 225.43 ? 99  ARG   A NE   1 
ATOM   783  C  CZ   . ARG   A 1 106 ? 345.816 -1.839  202.777 1.00 237.82 ? 99  ARG   A CZ   1 
ATOM   784  N  NH1  . ARG   A 1 106 ? 346.600 -0.805  203.069 1.00 230.69 ? 99  ARG   A NH1  1 
ATOM   785  N  NH2  . ARG   A 1 106 ? 344.933 -2.260  203.673 1.00 229.41 ? 99  ARG   A NH2  1 
ATOM   786  N  N    . SER   A 1 107 ? 344.144 0.460   196.665 1.00 197.05 ? 100 SER   A N    1 
ATOM   787  C  CA   . SER   A 1 107 ? 343.051 1.019   195.855 1.00 197.01 ? 100 SER   A CA   1 
ATOM   788  C  C    . SER   A 1 107 ? 343.177 2.544   195.680 1.00 195.80 ? 100 SER   A C    1 
ATOM   789  O  O    . SER   A 1 107 ? 343.842 3.200   196.482 1.00 194.31 ? 100 SER   A O    1 
ATOM   790  C  CB   . SER   A 1 107 ? 341.673 0.605   196.382 1.00 201.96 ? 100 SER   A CB   1 
ATOM   791  O  OG   . SER   A 1 107 ? 341.465 0.886   197.757 1.00 206.70 ? 100 SER   A OG   1 
ATOM   792  N  N    . ALA   A 1 108 ? 342.561 3.106   194.623 1.00 191.49 ? 101 ALA   A N    1 
ATOM   793  C  CA   . ALA   A 1 108 ? 342.572 4.550   194.385 1.00 185.20 ? 101 ALA   A CA   1 
ATOM   794  C  C    . ALA   A 1 108 ? 341.669 5.305   195.400 1.00 191.66 ? 101 ALA   A C    1 
ATOM   795  O  O    . ALA   A 1 108 ? 341.544 6.523   195.310 1.00 190.24 ? 101 ALA   A O    1 
ATOM   796  C  CB   . ALA   A 1 108 ? 342.178 4.868   192.948 1.00 183.44 ? 101 ALA   A CB   1 
ATOM   797  N  N    . GLN   A 1 109 ? 341.071 4.583   196.381 1.00 191.22 ? 102 GLN   A N    1 
ATOM   798  C  CA   . GLN   A 1 109 ? 340.260 5.154   197.467 1.00 191.65 ? 102 GLN   A CA   1 
ATOM   799  C  C    . GLN   A 1 109 ? 341.131 5.322   198.745 1.00 192.94 ? 102 GLN   A C    1 
ATOM   800  O  O    . GLN   A 1 109 ? 341.114 6.393   199.365 1.00 191.05 ? 102 GLN   A O    1 
ATOM   801  C  CB   . GLN   A 1 109 ? 339.033 4.272   197.755 1.00 195.76 ? 102 GLN   A CB   1 
ATOM   802  C  CG   . GLN   A 1 109 ? 338.045 4.854   198.784 1.00 204.42 ? 102 GLN   A CG   1 
ATOM   803  C  CD   . GLN   A 1 109 ? 338.235 4.368   200.213 1.00 212.04 ? 102 GLN   A CD   1 
ATOM   804  O  OE1  . GLN   A 1 109 ? 338.956 3.399   200.499 1.00 207.74 ? 102 GLN   A OE1  1 
ATOM   805  N  NE2  . GLN   A 1 109 ? 337.569 5.035   201.148 1.00 204.02 ? 102 GLN   A NE2  1 
ATOM   806  N  N    . LEU   A 1 110 ? 341.891 4.254   199.119 1.00 190.70 ? 103 LEU   A N    1 
ATOM   807  C  CA   . LEU   A 1 110 ? 342.767 4.189   200.297 1.00 189.35 ? 103 LEU   A CA   1 
ATOM   808  C  C    . LEU   A 1 110 ? 343.920 5.198   200.260 1.00 189.51 ? 103 LEU   A C    1 
ATOM   809  O  O    . LEU   A 1 110 ? 344.690 5.271   201.223 1.00 188.50 ? 103 LEU   A O    1 
ATOM   810  C  CB   . LEU   A 1 110 ? 343.295 2.751   200.548 1.00 190.54 ? 103 LEU   A CB   1 
ATOM   811  C  CG   . LEU   A 1 110 ? 342.295 1.640   200.985 1.00 196.46 ? 103 LEU   A CG   1 
ATOM   812  C  CD1  . LEU   A 1 110 ? 343.017 0.320   201.162 1.00 197.46 ? 103 LEU   A CD1  1 
ATOM   813  C  CD2  . LEU   A 1 110 ? 341.550 1.982   202.290 1.00 197.65 ? 103 LEU   A CD2  1 
ATOM   814  N  N    . ARG   A 1 111 ? 344.022 5.988   199.163 1.00 184.98 ? 104 ARG   A N    1 
ATOM   815  C  CA   . ARG   A 1 111 ? 345.020 7.049   198.998 1.00 176.07 ? 104 ARG   A CA   1 
ATOM   816  C  C    . ARG   A 1 111 ? 344.498 8.435   199.449 1.00 178.84 ? 104 ARG   A C    1 
ATOM   817  O  O    . ARG   A 1 111 ? 345.308 9.263   199.826 1.00 173.33 ? 104 ARG   A O    1 
ATOM   818  C  CB   . ARG   A 1 111 ? 345.590 7.073   197.556 1.00 168.76 ? 104 ARG   A CB   1 
ATOM   819  C  CG   . ARG   A 1 111 ? 345.154 8.231   196.654 1.00 167.41 ? 104 ARG   A CG   1 
ATOM   820  C  CD   . ARG   A 1 111 ? 344.515 7.696   195.396 1.00 178.01 ? 104 ARG   A CD   1 
ATOM   821  N  NE   . ARG   A 1 111 ? 344.106 8.741   194.456 1.00 179.93 ? 104 ARG   A NE   1 
ATOM   822  C  CZ   . ARG   A 1 111 ? 342.961 9.416   194.522 1.00 195.55 ? 104 ARG   A CZ   1 
ATOM   823  N  NH1  . ARG   A 1 111 ? 342.668 10.325  193.606 1.00 180.78 ? 104 ARG   A NH1  1 
ATOM   824  N  NH2  . ARG   A 1 111 ? 342.112 9.201   195.515 1.00 190.61 ? 104 ARG   A NH2  1 
ATOM   825  N  N    . LEU   A 1 112 ? 343.167 8.666   199.428 1.00 181.68 ? 105 LEU   A N    1 
ATOM   826  C  CA   . LEU   A 1 112 ? 342.484 9.918   199.793 1.00 182.55 ? 105 LEU   A CA   1 
ATOM   827  C  C    . LEU   A 1 112 ? 342.855 10.483  201.167 1.00 186.62 ? 105 LEU   A C    1 
ATOM   828  O  O    . LEU   A 1 112 ? 343.223 11.653  201.244 1.00 182.92 ? 105 LEU   A O    1 
ATOM   829  C  CB   . LEU   A 1 112 ? 340.954 9.761   199.703 1.00 186.69 ? 105 LEU   A CB   1 
ATOM   830  C  CG   . LEU   A 1 112 ? 340.327 9.645   198.318 1.00 190.40 ? 105 LEU   A CG   1 
ATOM   831  C  CD1  . LEU   A 1 112 ? 339.009 8.902   198.392 1.00 193.35 ? 105 LEU   A CD1  1 
ATOM   832  C  CD2  . LEU   A 1 112 ? 340.136 11.021  197.676 1.00 190.58 ? 105 LEU   A CD2  1 
ATOM   833  N  N    . ALA   A 1 113 ? 342.720 9.671   202.247 1.00 185.90 ? 106 ALA   A N    1 
ATOM   834  C  CA   . ALA   A 1 113 ? 343.034 10.050  203.634 1.00 185.59 ? 106 ALA   A CA   1 
ATOM   835  C  C    . ALA   A 1 113 ? 344.519 10.461  203.794 1.00 186.02 ? 106 ALA   A C    1 
ATOM   836  O  O    . ALA   A 1 113 ? 344.750 11.614  204.189 1.00 185.04 ? 106 ALA   A O    1 
ATOM   837  C  CB   . ALA   A 1 113 ? 342.651 8.935   204.602 1.00 188.59 ? 106 ALA   A CB   1 
ATOM   838  N  N    . PRO   A 1 114 ? 345.541 9.647   203.387 1.00 179.53 ? 107 PRO   A N    1 
ATOM   839  C  CA   . PRO   A 1 114 ? 346.919 10.151  203.462 1.00 171.43 ? 107 PRO   A CA   1 
ATOM   840  C  C    . PRO   A 1 114 ? 347.204 11.245  202.430 1.00 167.12 ? 107 PRO   A C    1 
ATOM   841  O  O    . PRO   A 1 114 ? 348.203 11.938  202.585 1.00 162.06 ? 107 PRO   A O    1 
ATOM   842  C  CB   . PRO   A 1 114 ? 347.773 8.908   203.242 1.00 172.90 ? 107 PRO   A CB   1 
ATOM   843  C  CG   . PRO   A 1 114 ? 346.936 7.991   202.501 1.00 181.75 ? 107 PRO   A CG   1 
ATOM   844  C  CD   . PRO   A 1 114 ? 345.516 8.259   202.878 1.00 183.89 ? 107 PRO   A CD   1 
ATOM   845  N  N    . LEU   A 1 115 ? 346.340 11.418  201.394 1.00 162.98 ? 108 LEU   A N    1 
ATOM   846  C  CA   . LEU   A 1 115 ? 346.498 12.491  200.401 1.00 156.44 ? 108 LEU   A CA   1 
ATOM   847  C  C    . LEU   A 1 115 ? 346.085 13.801  201.055 1.00 161.69 ? 108 LEU   A C    1 
ATOM   848  O  O    . LEU   A 1 115 ? 346.782 14.811  200.871 1.00 155.70 ? 108 LEU   A O    1 
ATOM   849  C  CB   . LEU   A 1 115 ? 345.691 12.261  199.099 1.00 156.96 ? 108 LEU   A CB   1 
ATOM   850  C  CG   . LEU   A 1 115 ? 345.574 13.454  198.134 1.00 157.04 ? 108 LEU   A CG   1 
ATOM   851  C  CD1  . LEU   A 1 115 ? 346.871 13.706  197.383 1.00 149.94 ? 108 LEU   A CD1  1 
ATOM   852  C  CD2  . LEU   A 1 115 ? 344.405 13.306  197.192 1.00 161.65 ? 108 LEU   A CD2  1 
ATOM   853  N  N    . TYR   A 1 116 ? 344.961 13.780  201.826 1.00 165.22 ? 109 TYR   A N    1 
ATOM   854  C  CA   . TYR   A 1 116 ? 344.474 14.960  202.537 1.00 167.41 ? 109 TYR   A CA   1 
ATOM   855  C  C    . TYR   A 1 116 ? 345.388 15.330  203.712 1.00 169.98 ? 109 TYR   A C    1 
ATOM   856  O  O    . TYR   A 1 116 ? 345.516 16.519  204.034 1.00 167.70 ? 109 TYR   A O    1 
ATOM   857  C  CB   . TYR   A 1 116 ? 343.019 14.818  202.970 1.00 178.18 ? 109 TYR   A CB   1 
ATOM   858  C  CG   . TYR   A 1 116 ? 342.019 14.620  201.848 1.00 183.81 ? 109 TYR   A CG   1 
ATOM   859  C  CD1  . TYR   A 1 116 ? 342.254 15.133  200.570 1.00 180.88 ? 109 TYR   A CD1  1 
ATOM   860  C  CD2  . TYR   A 1 116 ? 340.807 13.970  202.079 1.00 187.21 ? 109 TYR   A CD2  1 
ATOM   861  C  CE1  . TYR   A 1 116 ? 341.325 14.961  199.540 1.00 185.63 ? 109 TYR   A CE1  1 
ATOM   862  C  CE2  . TYR   A 1 116 ? 339.866 13.803  201.063 1.00 189.08 ? 109 TYR   A CE2  1 
ATOM   863  C  CZ   . TYR   A 1 116 ? 340.126 14.298  199.795 1.00 194.13 ? 109 TYR   A CZ   1 
ATOM   864  O  OH   . TYR   A 1 116 ? 339.170 14.114  198.819 1.00 196.10 ? 109 TYR   A OH   1 
ATOM   865  N  N    . ALA   A 1 117 ? 346.055 14.320  204.321 1.00 166.81 ? 110 ALA   A N    1 
ATOM   866  C  CA   . ALA   A 1 117 ? 347.034 14.532  205.388 1.00 164.89 ? 110 ALA   A CA   1 
ATOM   867  C  C    . ALA   A 1 117 ? 348.234 15.300  204.796 1.00 160.60 ? 110 ALA   A C    1 
ATOM   868  O  O    . ALA   A 1 117 ? 348.697 16.265  205.407 1.00 158.96 ? 110 ALA   A O    1 
ATOM   869  C  CB   . ALA   A 1 117 ? 347.483 13.199  205.965 1.00 168.88 ? 110 ALA   A CB   1 
ATOM   870  N  N    . SER   A 1 118 ? 348.683 14.909  203.575 1.00 152.20 ? 111 SER   A N    1 
ATOM   871  C  CA   . SER   A 1 118 ? 349.762 15.556  202.825 1.00 144.10 ? 111 SER   A CA   1 
ATOM   872  C  C    . SER   A 1 118 ? 349.366 17.009  202.509 1.00 146.21 ? 111 SER   A C    1 
ATOM   873  O  O    . SER   A 1 118 ? 350.182 17.913  202.710 1.00 141.72 ? 111 SER   A O    1 
ATOM   874  C  CB   . SER   A 1 118 ? 350.094 14.766  201.555 1.00 143.60 ? 111 SER   A CB   1 
ATOM   875  O  OG   . SER   A 1 118 ? 349.880 15.487  200.350 1.00 147.50 ? 111 SER   A OG   1 
ATOM   876  N  N    . ALA   A 1 119 ? 348.100 17.234  202.069 1.00 146.14 ? 112 ALA   A N    1 
ATOM   877  C  CA   . ALA   A 1 119 ? 347.586 18.573  201.760 1.00 145.32 ? 112 ALA   A CA   1 
ATOM   878  C  C    . ALA   A 1 119 ? 347.680 19.516  202.981 1.00 151.83 ? 112 ALA   A C    1 
ATOM   879  O  O    . ALA   A 1 119 ? 348.202 20.627  202.849 1.00 147.86 ? 112 ALA   A O    1 
ATOM   880  C  CB   . ALA   A 1 119 ? 346.154 18.484  201.270 1.00 150.99 ? 112 ALA   A CB   1 
ATOM   881  N  N    . ARG   A 1 120 ? 347.216 19.039  204.171 1.00 153.81 ? 113 ARG   A N    1 
ATOM   882  C  CA   . ARG   A 1 120 ? 347.233 19.751  205.450 1.00 155.45 ? 113 ARG   A CA   1 
ATOM   883  C  C    . ARG   A 1 120 ? 348.618 20.257  205.752 1.00 153.70 ? 113 ARG   A C    1 
ATOM   884  O  O    . ARG   A 1 120 ? 348.762 21.445  206.022 1.00 153.11 ? 113 ARG   A O    1 
ATOM   885  C  CB   . ARG   A 1 120 ? 346.729 18.858  206.599 1.00 161.82 ? 113 ARG   A CB   1 
ATOM   886  C  CG   . ARG   A 1 120 ? 345.218 18.874  206.733 1.00 181.27 ? 113 ARG   A CG   1 
ATOM   887  C  CD   . ARG   A 1 120 ? 344.689 17.840  207.714 1.00 194.39 ? 113 ARG   A CD   1 
ATOM   888  N  NE   . ARG   A 1 120 ? 343.235 17.693  207.592 1.00 200.42 ? 113 ARG   A NE   1 
ATOM   889  C  CZ   . ARG   A 1 120 ? 342.626 16.771  206.851 1.00 205.29 ? 113 ARG   A CZ   1 
ATOM   890  N  NH1  . ARG   A 1 120 ? 341.302 16.731  206.787 1.00 196.88 ? 113 ARG   A NH1  1 
ATOM   891  N  NH2  . ARG   A 1 120 ? 343.337 15.875  206.178 1.00 190.27 ? 113 ARG   A NH2  1 
ATOM   892  N  N    . ALA   A 1 121 ? 349.642 19.377  205.654 1.00 146.28 ? 114 ALA   A N    1 
ATOM   893  C  CA   . ALA   A 1 121 ? 351.050 19.716  205.895 1.00 140.92 ? 114 ALA   A CA   1 
ATOM   894  C  C    . ALA   A 1 121 ? 351.593 20.734  204.878 1.00 139.43 ? 114 ALA   A C    1 
ATOM   895  O  O    . ALA   A 1 121 ? 352.423 21.570  205.231 1.00 136.06 ? 114 ALA   A O    1 
ATOM   896  C  CB   . ALA   A 1 121 ? 351.898 18.459  205.885 1.00 140.64 ? 114 ALA   A CB   1 
ATOM   897  N  N    . LEU   A 1 122 ? 351.097 20.678  203.629 1.00 136.04 ? 115 LEU   A N    1 
ATOM   898  C  CA   . LEU   A 1 122 ? 351.496 21.581  202.553 1.00 131.11 ? 115 LEU   A CA   1 
ATOM   899  C  C    . LEU   A 1 122 ? 350.943 22.993  202.764 1.00 137.50 ? 115 LEU   A C    1 
ATOM   900  O  O    . LEU   A 1 122 ? 351.683 23.961  202.612 1.00 134.99 ? 115 LEU   A O    1 
ATOM   901  C  CB   . LEU   A 1 122 ? 351.135 20.996  201.172 1.00 129.59 ? 115 LEU   A CB   1 
ATOM   902  C  CG   . LEU   A 1 122 ? 352.119 21.322  200.035 1.00 127.92 ? 115 LEU   A CG   1 
ATOM   903  C  CD1  . LEU   A 1 122 ? 353.584 21.139  200.473 1.00 125.13 ? 115 LEU   A CD1  1 
ATOM   904  C  CD2  . LEU   A 1 122 ? 351.816 20.521  198.765 1.00 125.55 ? 115 LEU   A CD2  1 
ATOM   905  N  N    . TRP   A 1 123 ? 349.671 23.104  203.178 1.00 139.39 ? 116 TRP   A N    1 
ATOM   906  C  CA   . TRP   A 1 123 ? 349.005 24.369  203.505 1.00 141.73 ? 116 TRP   A CA   1 
ATOM   907  C  C    . TRP   A 1 123 ? 349.591 24.976  204.780 1.00 146.87 ? 116 TRP   A C    1 
ATOM   908  O  O    . TRP   A 1 123 ? 349.631 26.202  204.909 1.00 146.94 ? 116 TRP   A O    1 
ATOM   909  C  CB   . TRP   A 1 123 ? 347.511 24.138  203.725 1.00 147.16 ? 116 TRP   A CB   1 
ATOM   910  C  CG   . TRP   A 1 123 ? 346.700 23.933  202.482 1.00 148.54 ? 116 TRP   A CG   1 
ATOM   911  C  CD1  . TRP   A 1 123 ? 345.865 22.888  202.216 1.00 154.94 ? 116 TRP   A CD1  1 
ATOM   912  C  CD2  . TRP   A 1 123 ? 346.563 24.848  201.384 1.00 146.30 ? 116 TRP   A CD2  1 
ATOM   913  N  NE1  . TRP   A 1 123 ? 345.235 23.080  201.010 1.00 154.18 ? 116 TRP   A NE1  1 
ATOM   914  C  CE2  . TRP   A 1 123 ? 345.637 24.278  200.480 1.00 152.21 ? 116 TRP   A CE2  1 
ATOM   915  C  CE3  . TRP   A 1 123 ? 347.155 26.087  201.061 1.00 144.14 ? 116 TRP   A CE3  1 
ATOM   916  C  CZ2  . TRP   A 1 123 ? 345.291 24.897  199.273 1.00 150.74 ? 116 TRP   A CZ2  1 
ATOM   917  C  CZ3  . TRP   A 1 123 ? 346.805 26.701  199.866 1.00 145.06 ? 116 TRP   A CZ3  1 
ATOM   918  C  CH2  . TRP   A 1 123 ? 345.873 26.114  198.993 1.00 148.31 ? 116 TRP   A CH2  1 
ATOM   919  N  N    . LEU   A 1 124 ? 350.010 24.111  205.734 1.00 144.35 ? 117 LEU   A N    1 
ATOM   920  C  CA   . LEU   A 1 124 ? 350.635 24.492  207.000 1.00 144.92 ? 117 LEU   A CA   1 
ATOM   921  C  C    . LEU   A 1 124 ? 351.959 25.177  206.726 1.00 143.10 ? 117 LEU   A C    1 
ATOM   922  O  O    . LEU   A 1 124 ? 352.208 26.226  207.304 1.00 143.47 ? 117 LEU   A O    1 
ATOM   923  C  CB   . LEU   A 1 124 ? 350.830 23.268  207.904 1.00 148.15 ? 117 LEU   A CB   1 
ATOM   924  C  CG   . LEU   A 1 124 ? 351.223 23.490  209.371 1.00 155.86 ? 117 LEU   A CG   1 
ATOM   925  C  CD1  . LEU   A 1 124 ? 350.475 24.660  210.012 1.00 159.48 ? 117 LEU   A CD1  1 
ATOM   926  C  CD2  . LEU   A 1 124 ? 350.968 22.234  210.172 1.00 163.88 ? 117 LEU   A CD2  1 
ATOM   927  N  N    . LEU   A 1 125 ? 352.779 24.620  205.805 1.00 134.82 ? 118 LEU   A N    1 
ATOM   928  C  CA   . LEU   A 1 125 ? 354.060 25.205  205.390 1.00 128.88 ? 118 LEU   A CA   1 
ATOM   929  C  C    . LEU   A 1 125 ? 353.819 26.529  204.660 1.00 132.57 ? 118 LEU   A C    1 
ATOM   930  O  O    . LEU   A 1 125 ? 354.526 27.502  204.924 1.00 130.22 ? 118 LEU   A O    1 
ATOM   931  C  CB   . LEU   A 1 125 ? 354.857 24.240  204.500 1.00 124.45 ? 118 LEU   A CB   1 
ATOM   932  C  CG   . LEU   A 1 125 ? 355.513 23.048  205.194 1.00 129.01 ? 118 LEU   A CG   1 
ATOM   933  C  CD1  . LEU   A 1 125 ? 355.906 21.974  204.177 1.00 126.21 ? 118 LEU   A CD1  1 
ATOM   934  C  CD2  . LEU   A 1 125 ? 356.713 23.482  206.037 1.00 128.13 ? 118 LEU   A CD2  1 
ATOM   935  N  N    . VAL   A 1 126 ? 352.792 26.574  203.778 1.00 131.09 ? 119 VAL   A N    1 
ATOM   936  C  CA   . VAL   A 1 126 ? 352.414 27.782  203.044 1.00 130.52 ? 119 VAL   A CA   1 
ATOM   937  C  C    . VAL   A 1 126 ? 352.055 28.903  204.016 1.00 137.86 ? 119 VAL   A C    1 
ATOM   938  O  O    . VAL   A 1 126 ? 352.584 30.001  203.873 1.00 137.23 ? 119 VAL   A O    1 
ATOM   939  C  CB   . VAL   A 1 126 ? 351.333 27.503  201.971 1.00 135.83 ? 119 VAL   A CB   1 
ATOM   940  C  CG1  . VAL   A 1 126 ? 350.342 28.657  201.822 1.00 139.11 ? 119 VAL   A CG1  1 
ATOM   941  C  CG2  . VAL   A 1 126 ? 351.987 27.194  200.639 1.00 130.89 ? 119 VAL   A CG2  1 
ATOM   942  N  N    . ALA   A 1 127 ? 351.239 28.603  205.043 1.00 138.16 ? 120 ALA   A N    1 
ATOM   943  C  CA   . ALA   A 1 127 ? 350.821 29.581  206.052 1.00 142.11 ? 120 ALA   A CA   1 
ATOM   944  C  C    . ALA   A 1 127 ? 352.012 30.139  206.851 1.00 143.58 ? 120 ALA   A C    1 
ATOM   945  O  O    . ALA   A 1 127 ? 352.105 31.349  207.032 1.00 144.13 ? 120 ALA   A O    1 
ATOM   946  C  CB   . ALA   A 1 127 ? 349.786 28.966  206.989 1.00 149.14 ? 120 ALA   A CB   1 
ATOM   947  N  N    . LEU   A 1 128 ? 352.924 29.257  207.299 1.00 136.50 ? 121 LEU   A N    1 
ATOM   948  C  CA   . LEU   A 1 128 ? 354.114 29.611  208.057 1.00 133.55 ? 121 LEU   A CA   1 
ATOM   949  C  C    . LEU   A 1 128 ? 355.088 30.454  207.206 1.00 134.88 ? 121 LEU   A C    1 
ATOM   950  O  O    . LEU   A 1 128 ? 355.674 31.403  207.719 1.00 136.22 ? 121 LEU   A O    1 
ATOM   951  C  CB   . LEU   A 1 128 ? 354.782 28.348  208.573 1.00 132.03 ? 121 LEU   A CB   1 
ATOM   952  C  CG   . LEU   A 1 128 ? 354.103 27.683  209.742 1.00 140.94 ? 121 LEU   A CG   1 
ATOM   953  C  CD1  . LEU   A 1 128 ? 354.871 26.461  210.136 1.00 140.11 ? 121 LEU   A CD1  1 
ATOM   954  N  N    . ALA   A 1 129 ? 355.218 30.148  205.907 1.00 127.97 ? 122 ALA   A N    1 
ATOM   955  C  CA   . ALA   A 1 129 ? 356.042 30.919  204.974 1.00 123.31 ? 122 ALA   A CA   1 
ATOM   956  C  C    . ALA   A 1 129 ? 355.380 32.272  204.803 1.00 128.30 ? 122 ALA   A C    1 
ATOM   957  O  O    . ALA   A 1 129 ? 356.070 33.277  204.882 1.00 126.02 ? 122 ALA   A O    1 
ATOM   958  C  CB   . ALA   A 1 129 ? 356.111 30.213  203.629 1.00 120.76 ? 122 ALA   A CB   1 
ATOM   959  N  N    . ALA   A 1 130 ? 354.031 32.297  204.609 1.00 128.86 ? 123 ALA   A N    1 
ATOM   960  C  CA   . ALA   A 1 130 ? 353.233 33.521  204.462 1.00 131.75 ? 123 ALA   A CA   1 
ATOM   961  C  C    . ALA   A 1 130 ? 353.351 34.413  205.706 1.00 138.08 ? 123 ALA   A C    1 
ATOM   962  O  O    . ALA   A 1 130 ? 353.678 35.587  205.561 1.00 138.22 ? 123 ALA   A O    1 
ATOM   963  C  CB   . ALA   A 1 130 ? 351.781 33.184  204.174 1.00 136.34 ? 123 ALA   A CB   1 
ATOM   964  N  N    . LEU   A 1 131 ? 353.181 33.841  206.916 1.00 136.13 ? 124 LEU   A N    1 
ATOM   965  C  CA   . LEU   A 1 131 ? 353.317 34.557  208.186 1.00 139.23 ? 124 LEU   A CA   1 
ATOM   966  C  C    . LEU   A 1 131 ? 354.730 35.108  208.406 1.00 140.07 ? 124 LEU   A C    1 
ATOM   967  O  O    . LEU   A 1 131 ? 354.859 36.206  208.928 1.00 142.55 ? 124 LEU   A O    1 
ATOM   968  C  CB   . LEU   A 1 131 ? 352.882 33.701  209.383 1.00 142.95 ? 124 LEU   A CB   1 
ATOM   969  C  CG   . LEU   A 1 131 ? 351.387 33.465  209.558 1.00 152.61 ? 124 LEU   A CG   1 
ATOM   970  C  CD1  . LEU   A 1 131 ? 351.144 32.501  210.664 1.00 156.12 ? 124 LEU   A CD1  1 
ATOM   971  C  CD2  . LEU   A 1 131 ? 350.647 34.745  209.856 1.00 159.53 ? 124 LEU   A CD2  1 
ATOM   972  N  N    . GLY   A 1 132 ? 355.753 34.367  207.980 1.00 131.35 ? 125 GLY   A N    1 
ATOM   973  C  CA   . GLY   A 1 132 ? 357.152 34.782  208.053 1.00 128.26 ? 125 GLY   A CA   1 
ATOM   974  C  C    . GLY   A 1 132 ? 357.502 35.959  207.151 1.00 132.20 ? 125 GLY   A C    1 
ATOM   975  O  O    . GLY   A 1 132 ? 358.286 36.834  207.531 1.00 133.86 ? 125 GLY   A O    1 
ATOM   976  N  N    . LEU   A 1 133 ? 356.901 36.008  205.959 1.00 127.59 ? 126 LEU   A N    1 
ATOM   977  C  CA   . LEU   A 1 133 ? 357.103 37.078  204.976 1.00 126.44 ? 126 LEU   A CA   1 
ATOM   978  C  C    . LEU   A 1 133 ? 356.241 38.275  205.339 1.00 136.74 ? 126 LEU   A C    1 
ATOM   979  O  O    . LEU   A 1 133 ? 356.673 39.411  205.141 1.00 138.02 ? 126 LEU   A O    1 
ATOM   980  C  CB   . LEU   A 1 133 ? 356.774 36.596  203.535 1.00 123.43 ? 126 LEU   A CB   1 
ATOM   981  C  CG   . LEU   A 1 133 ? 357.674 35.505  202.946 1.00 120.92 ? 126 LEU   A CG   1 
ATOM   982  C  CD1  . LEU   A 1 133 ? 356.995 34.839  201.843 1.00 120.21 ? 126 LEU   A CD1  1 
ATOM   983  C  CD2  . LEU   A 1 133 ? 358.975 36.058  202.452 1.00 118.42 ? 126 LEU   A CD2  1 
ATOM   984  N  N    . LEU   A 1 134 ? 355.015 38.023  205.861 1.00 136.92 ? 127 LEU   A N    1 
ATOM   985  C  CA   . LEU   A 1 134 ? 354.087 39.058  206.318 1.00 142.55 ? 127 LEU   A CA   1 
ATOM   986  C  C    . LEU   A 1 134 ? 354.797 39.859  207.381 1.00 147.95 ? 127 LEU   A C    1 
ATOM   987  O  O    . LEU   A 1 134 ? 355.015 41.044  207.186 1.00 149.22 ? 127 LEU   A O    1 
ATOM   988  C  CB   . LEU   A 1 134 ? 352.830 38.423  206.913 1.00 146.95 ? 127 LEU   A CB   1 
ATOM   989  C  CG   . LEU   A 1 134 ? 351.595 38.499  206.054 1.00 154.64 ? 127 LEU   A CG   1 
ATOM   990  C  CD1  . LEU   A 1 134 ? 350.914 37.156  205.997 1.00 154.96 ? 127 LEU   A CD1  1 
ATOM   991  C  CD2  . LEU   A 1 134 ? 350.643 39.560  206.576 1.00 163.92 ? 127 LEU   A CD2  1 
ATOM   992  N  N    . ALA   A 1 135 ? 355.287 39.169  208.434 1.00 144.45 ? 128 ALA   A N    1 
ATOM   993  C  CA   . ALA   A 1 135 ? 356.050 39.726  209.548 1.00 145.97 ? 128 ALA   A CA   1 
ATOM   994  C  C    . ALA   A 1 135 ? 357.357 40.401  209.079 1.00 148.80 ? 128 ALA   A C    1 
ATOM   995  O  O    . ALA   A 1 135 ? 357.900 41.242  209.803 1.00 151.24 ? 128 ALA   A O    1 
ATOM   996  C  CB   . ALA   A 1 135 ? 356.340 38.641  210.574 1.00 146.19 ? 128 ALA   A CB   1 
ATOM   997  N  N    . HIS   A 1 136 ? 357.842 40.061  207.870 1.00 141.26 ? 129 HIS   A N    1 
ATOM   998  C  CA   . HIS   A 1 136 ? 359.038 40.682  207.306 1.00 139.33 ? 129 HIS   A CA   1 
ATOM   999  C  C    . HIS   A 1 136 ? 358.721 42.044  206.660 1.00 143.80 ? 129 HIS   A C    1 
ATOM   1000 O  O    . HIS   A 1 136 ? 359.328 43.038  207.042 1.00 145.12 ? 129 HIS   A O    1 
ATOM   1001 C  CB   . HIS   A 1 136 ? 359.757 39.729  206.317 1.00 136.04 ? 129 HIS   A CB   1 
ATOM   1002 C  CG   . HIS   A 1 136 ? 360.972 40.333  205.673 1.00 138.29 ? 129 HIS   A CG   1 
ATOM   1003 N  ND1  . HIS   A 1 136 ? 360.870 41.141  204.544 1.00 141.01 ? 129 HIS   A ND1  1 
ATOM   1004 C  CD2  . HIS   A 1 136 ? 362.271 40.260  206.040 1.00 138.86 ? 129 HIS   A CD2  1 
ATOM   1005 C  CE1  . HIS   A 1 136 ? 362.104 41.522  204.259 1.00 139.19 ? 129 HIS   A CE1  1 
ATOM   1006 N  NE2  . HIS   A 1 136 ? 362.982 41.025  205.136 1.00 138.32 ? 129 HIS   A NE2  1 
ATOM   1007 N  N    . PHE   A 1 137 ? 357.774 42.082  205.694 1.00 140.66 ? 130 PHE   A N    1 
ATOM   1008 C  CA   . PHE   A 1 137 ? 357.372 43.267  204.926 1.00 143.48 ? 130 PHE   A CA   1 
ATOM   1009 C  C    . PHE   A 1 137 ? 356.399 44.227  205.604 1.00 154.38 ? 130 PHE   A C    1 
ATOM   1010 O  O    . PHE   A 1 137 ? 356.525 45.431  205.390 1.00 158.72 ? 130 PHE   A O    1 
ATOM   1011 C  CB   . PHE   A 1 137 ? 356.768 42.857  203.582 1.00 144.05 ? 130 PHE   A CB   1 
ATOM   1012 C  CG   . PHE   A 1 137 ? 357.667 42.103  202.629 1.00 140.14 ? 130 PHE   A CG   1 
ATOM   1013 C  CD1  . PHE   A 1 137 ? 358.704 42.749  201.967 1.00 142.14 ? 130 PHE   A CD1  1 
ATOM   1014 C  CD2  . PHE   A 1 137 ? 357.417 40.776  202.319 1.00 138.11 ? 130 PHE   A CD2  1 
ATOM   1015 C  CE1  . PHE   A 1 137 ? 359.498 42.067  201.043 1.00 138.13 ? 130 PHE   A CE1  1 
ATOM   1016 C  CE2  . PHE   A 1 137 ? 358.233 40.090  201.423 1.00 136.28 ? 130 PHE   A CE2  1 
ATOM   1017 C  CZ   . PHE   A 1 137 ? 359.254 40.746  200.777 1.00 133.10 ? 130 PHE   A CZ   1 
ATOM   1018 N  N    . LEU   A 1 138 ? 355.402 43.710  206.352 1.00 152.37 ? 131 LEU   A N    1 
ATOM   1019 C  CA   . LEU   A 1 138 ? 354.345 44.492  207.013 1.00 158.79 ? 131 LEU   A CA   1 
ATOM   1020 C  C    . LEU   A 1 138 ? 354.837 45.617  207.945 1.00 167.26 ? 131 LEU   A C    1 
ATOM   1021 O  O    . LEU   A 1 138 ? 354.328 46.725  207.797 1.00 172.36 ? 131 LEU   A O    1 
ATOM   1022 C  CB   . LEU   A 1 138 ? 353.377 43.576  207.762 1.00 160.88 ? 131 LEU   A CB   1 
ATOM   1023 C  CG   . LEU   A 1 138 ? 351.934 44.010  207.804 1.00 172.28 ? 131 LEU   A CG   1 
ATOM   1024 C  CD1  . LEU   A 1 138 ? 351.126 43.301  206.738 1.00 170.74 ? 131 LEU   A CD1  1 
ATOM   1025 C  CD2  . LEU   A 1 138 ? 351.345 43.752  209.172 1.00 179.88 ? 131 LEU   A CD2  1 
ATOM   1026 N  N    . PRO   A 1 139 ? 355.785 45.403  208.899 1.00 162.59 ? 132 PRO   A N    1 
ATOM   1027 C  CA   . PRO   A 1 139 ? 356.213 46.513  209.766 1.00 166.17 ? 132 PRO   A CA   1 
ATOM   1028 C  C    . PRO   A 1 139 ? 356.789 47.709  209.012 1.00 170.42 ? 132 PRO   A C    1 
ATOM   1029 O  O    . PRO   A 1 139 ? 356.557 48.842  209.426 1.00 176.51 ? 132 PRO   A O    1 
ATOM   1030 C  CB   . PRO   A 1 139 ? 357.277 45.870  210.664 1.00 164.96 ? 132 PRO   A CB   1 
ATOM   1031 C  CG   . PRO   A 1 139 ? 356.970 44.435  210.656 1.00 166.31 ? 132 PRO   A CG   1 
ATOM   1032 C  CD   . PRO   A 1 139 ? 356.515 44.168  209.252 1.00 159.30 ? 132 PRO   A CD   1 
ATOM   1033 N  N    . ALA   A 1 140 ? 357.529 47.464  207.914 1.00 160.65 ? 133 ALA   A N    1 
ATOM   1034 C  CA   . ALA   A 1 140 ? 358.132 48.516  207.095 1.00 160.58 ? 133 ALA   A CA   1 
ATOM   1035 C  C    . ALA   A 1 140 ? 357.059 49.274  206.328 1.00 166.91 ? 133 ALA   A C    1 
ATOM   1036 O  O    . ALA   A 1 140 ? 357.176 50.488  206.144 1.00 170.30 ? 133 ALA   A O    1 
ATOM   1037 C  CB   . ALA   A 1 140 ? 359.129 47.907  206.128 1.00 155.40 ? 133 ALA   A CB   1 
ATOM   1038 N  N    . ALA   A 1 141 ? 356.003 48.549  205.896 1.00 162.27 ? 134 ALA   A N    1 
ATOM   1039 C  CA   . ALA   A 1 141 ? 354.864 49.100  205.168 1.00 166.59 ? 134 ALA   A CA   1 
ATOM   1040 C  C    . ALA   A 1 141 ? 354.046 49.992  206.103 1.00 177.82 ? 134 ALA   A C    1 
ATOM   1041 O  O    . ALA   A 1 141 ? 353.906 51.177  205.827 1.00 181.18 ? 134 ALA   A O    1 
ATOM   1042 C  CB   . ALA   A 1 141 ? 354.011 47.975  204.616 1.00 164.85 ? 134 ALA   A CB   1 
ATOM   1043 N  N    . LEU   A 1 142 ? 353.582 49.428  207.244 1.00 176.84 ? 135 LEU   A N    1 
ATOM   1044 C  CA   . LEU   A 1 142 ? 352.851 50.096  208.316 1.00 183.99 ? 135 LEU   A CA   1 
ATOM   1045 C  C    . LEU   A 1 142 ? 353.605 51.379  208.728 1.00 189.04 ? 135 LEU   A C    1 
ATOM   1046 O  O    . LEU   A 1 142 ? 352.963 52.409  208.909 1.00 191.40 ? 135 LEU   A O    1 
ATOM   1047 C  CB   . LEU   A 1 142 ? 352.628 49.079  209.490 1.00 184.31 ? 135 LEU   A CB   1 
ATOM   1048 C  CG   . LEU   A 1 142 ? 352.647 49.452  211.043 1.00 190.47 ? 135 LEU   A CG   1 
ATOM   1049 C  CD1  . LEU   A 1 142 ? 354.068 49.566  211.661 1.00 190.28 ? 135 LEU   A CD1  1 
ATOM   1050 C  CD2  . LEU   A 1 142 ? 351.648 50.543  211.455 1.00 195.39 ? 135 LEU   A CD2  1 
ATOM   1051 N  N    . ARG   A 1 143 ? 354.959 51.329  208.808 1.00 184.36 ? 136 ARG   A N    1 
ATOM   1052 C  CA   . ARG   A 1 143 ? 355.805 52.471  209.166 1.00 186.54 ? 136 ARG   A CA   1 
ATOM   1053 C  C    . ARG   A 1 143 ? 355.793 53.576  208.110 1.00 189.51 ? 136 ARG   A C    1 
ATOM   1054 O  O    . ARG   A 1 143 ? 355.594 54.738  208.458 1.00 190.76 ? 136 ARG   A O    1 
ATOM   1055 C  CB   . ARG   A 1 143 ? 357.244 52.022  209.460 1.00 181.79 ? 136 ARG   A CB   1 
ATOM   1056 C  CG   . ARG   A 1 143 ? 357.700 52.310  210.886 1.00 198.09 ? 136 ARG   A CG   1 
ATOM   1057 C  CD   . ARG   A 1 143 ? 357.546 51.107  211.802 1.00 207.69 ? 136 ARG   A CD   1 
ATOM   1058 N  NE   . ARG   A 1 143 ? 358.843 50.561  212.206 1.00 213.07 ? 136 ARG   A NE   1 
ATOM   1059 C  CZ   . ARG   A 1 143 ? 359.002 49.595  213.103 1.00 220.48 ? 136 ARG   A CZ   1 
ATOM   1060 N  NH1  . ARG   A 1 143 ? 360.218 49.160  213.410 1.00 210.53 ? 136 ARG   A NH1  1 
ATOM   1061 N  NH2  . ARG   A 1 143 ? 357.947 49.058  213.705 1.00 208.90 ? 136 ARG   A NH2  1 
ATOM   1062 N  N    . ALA   A 1 144 ? 356.009 53.214  206.826 1.00 185.86 ? 137 ALA   A N    1 
ATOM   1063 C  CA   . ALA   A 1 144 ? 356.026 54.157  205.702 1.00 186.60 ? 137 ALA   A CA   1 
ATOM   1064 C  C    . ALA   A 1 144 ? 354.629 54.710  205.385 1.00 191.08 ? 137 ALA   A C    1 
ATOM   1065 O  O    . ALA   A 1 144 ? 354.511 55.876  204.995 1.00 192.30 ? 137 ALA   A O    1 
ATOM   1066 C  CB   . ALA   A 1 144 ? 356.629 53.500  204.476 1.00 184.26 ? 137 ALA   A CB   1 
ATOM   1067 N  N    . ALA   A 1 145 ? 353.578 53.870  205.557 1.00 188.44 ? 138 ALA   A N    1 
ATOM   1068 C  CA   . ALA   A 1 145 ? 352.168 54.223  205.360 1.00 189.73 ? 138 ALA   A CA   1 
ATOM   1069 C  C    . ALA   A 1 145 ? 351.768 55.306  206.379 1.00 195.79 ? 138 ALA   A C    1 
ATOM   1070 O  O    . ALA   A 1 145 ? 351.267 56.363  205.985 1.00 197.85 ? 138 ALA   A O    1 
ATOM   1071 C  CB   . ALA   A 1 145 ? 351.288 52.988  205.521 1.00 188.97 ? 138 ALA   A CB   1 
ATOM   1072 N  N    . LEU   A 1 146 ? 352.076 55.071  207.679 1.00 193.47 ? 139 LEU   A N    1 
ATOM   1073 C  CA   . LEU   A 1 146 ? 351.839 56.000  208.786 1.00 195.42 ? 139 LEU   A CA   1 
ATOM   1074 C  C    . LEU   A 1 146 ? 352.741 57.208  208.687 1.00 199.23 ? 139 LEU   A C    1 
ATOM   1075 O  O    . LEU   A 1 146 ? 352.511 58.191  209.382 1.00 201.34 ? 139 LEU   A O    1 
ATOM   1076 C  CB   . LEU   A 1 146 ? 352.052 55.301  210.129 1.00 195.19 ? 139 LEU   A CB   1 
ATOM   1077 C  CG   . LEU   A 1 146 ? 350.790 55.010  210.909 1.00 199.70 ? 139 LEU   A CG   1 
ATOM   1078 C  CD1  . LEU   A 1 146 ? 350.190 53.662  210.522 1.00 197.68 ? 139 LEU   A CD1  1 
ATOM   1079 C  CD2  . LEU   A 1 146 ? 351.062 55.069  212.381 1.00 203.21 ? 139 LEU   A CD2  1 
ATOM   1080 N  N    . LEU   A 1 147 ? 353.753 57.147  207.810 1.00 196.12 ? 140 LEU   A N    1 
ATOM   1081 C  CA   . LEU   A 1 147 ? 354.671 58.248  207.557 1.00 197.83 ? 140 LEU   A CA   1 
ATOM   1082 C  C    . LEU   A 1 147 ? 354.027 59.309  206.635 1.00 203.41 ? 140 LEU   A C    1 
ATOM   1083 O  O    . LEU   A 1 147 ? 354.686 60.282  206.252 1.00 204.40 ? 140 LEU   A O    1 
ATOM   1084 C  CB   . LEU   A 1 147 ? 356.029 57.731  207.018 1.00 195.99 ? 140 LEU   A CB   1 
ATOM   1085 C  CG   . LEU   A 1 147 ? 357.297 57.947  207.876 1.00 199.89 ? 140 LEU   A CG   1 
ATOM   1086 C  CD1  . LEU   A 1 147 ? 357.702 59.409  207.922 1.00 202.79 ? 140 LEU   A CD1  1 
ATOM   1087 C  CD2  . LEU   A 1 147 ? 357.150 57.398  209.284 1.00 202.22 ? 140 LEU   A CD2  1 
ATOM   1088 N  N    . GLY   A 1 148 ? 352.734 59.129  206.341 1.00 202.23 ? 141 GLY   A N    1 
ATOM   1089 C  CA   . GLY   A 1 148 ? 351.917 60.060  205.571 1.00 204.33 ? 141 GLY   A CA   1 
ATOM   1090 C  C    . GLY   A 1 148 ? 351.010 60.868  206.485 1.00 210.85 ? 141 GLY   A C    1 
ATOM   1091 O  O    . GLY   A 1 148 ? 349.892 60.432  206.778 1.00 211.21 ? 141 GLY   A O    1 
ATOM   1092 N  N    . ARG   A 1 149 ? 351.503 62.027  206.989 1.00 210.91 ? 142 ARG   A N    1 
ATOM   1093 C  CA   . ARG   A 1 149 ? 350.766 62.922  207.896 1.00 214.02 ? 142 ARG   A CA   1 
ATOM   1094 C  C    . ARG   A 1 149 ? 350.983 64.394  207.515 1.00 218.86 ? 142 ARG   A C    1 
ATOM   1095 O  O    . ARG   A 1 149 ? 350.052 65.205  207.588 1.00 221.23 ? 142 ARG   A O    1 
ATOM   1096 C  CB   . ARG   A 1 149 ? 351.231 62.730  209.343 1.00 215.14 ? 142 ARG   A CB   1 
ATOM   1097 N  N    . LEU   A 1 150 ? 352.264 64.716  207.224 1.00 215.95 ? 143 LEU   A N    1 
ATOM   1098 C  CA   . LEU   A 1 150 ? 352.947 65.937  206.759 1.00 216.67 ? 143 LEU   A CA   1 
ATOM   1099 C  C    . LEU   A 1 150 ? 352.228 67.308  206.969 1.00 220.65 ? 143 LEU   A C    1 
ATOM   1100 O  O    . LEU   A 1 150 ? 351.052 67.473  206.641 1.00 221.42 ? 143 LEU   A O    1 
ATOM   1101 C  CB   . LEU   A 1 150 ? 353.316 65.764  205.270 1.00 215.64 ? 143 LEU   A CB   1 
ATOM   1102 C  CG   . LEU   A 1 150 ? 354.234 64.560  204.943 1.00 216.25 ? 143 LEU   A CG   1 
ATOM   1103 C  CD1  . LEU   A 1 150 ? 353.439 63.364  204.458 1.00 214.21 ? 143 LEU   A CD1  1 
ATOM   1104 C  CD2  . LEU   A 1 150 ? 355.247 64.918  203.890 1.00 218.64 ? 143 LEU   A CD2  1 
HETATM 1105 C  C6   . PLM   B 2 .   ? 370.034 33.253  203.211 1.00 132.11 ? 201 PLM   A C6   1 
HETATM 1106 C  C7   . PLM   B 2 .   ? 369.360 32.915  201.843 1.00 126.97 ? 201 PLM   A C7   1 
HETATM 1107 C  C8   . PLM   B 2 .   ? 369.088 31.387  201.749 1.00 123.58 ? 201 PLM   A C8   1 
HETATM 1108 C  C9   . PLM   B 2 .   ? 368.599 30.947  200.339 1.00 119.90 ? 201 PLM   A C9   1 
HETATM 1109 C  CA   . PLM   B 2 .   ? 367.292 30.120  200.438 1.00 115.26 ? 201 PLM   A CA   1 
HETATM 1110 C  CB   . PLM   B 2 .   ? 366.760 29.710  199.048 1.00 112.68 ? 201 PLM   A CB   1 
HETATM 1111 C  CC   . PLM   B 2 .   ? 366.006 28.366  199.181 1.00 111.19 ? 201 PLM   A CC   1 
HETATM 1112 C  CD   . PLM   B 2 .   ? 365.630 27.767  197.806 1.00 106.30 ? 201 PLM   A CD   1 
HETATM 1113 C  CE   . PLM   B 2 .   ? 364.088 27.686  197.653 1.00 104.73 ? 201 PLM   A CE   1 
HETATM 1114 C  CF   . PLM   B 2 .   ? 363.627 26.357  196.997 1.00 107.02 ? 201 PLM   A CF   1 
HETATM 1115 C  CG   . PLM   B 2 .   ? 363.893 26.281  195.466 1.00 105.41 ? 201 PLM   A CG   1 
HETATM 1116 C  C10  . PAM   C 3 .   ? 359.590 44.573  192.650 1.00 157.13 ? 202 PAM   A C10  1 
HETATM 1117 C  C11  . PAM   C 3 .   ? 359.103 43.160  192.389 1.00 154.53 ? 202 PAM   A C11  1 
HETATM 1118 C  C12  . PAM   C 3 .   ? 357.743 42.894  193.094 1.00 156.09 ? 202 PAM   A C12  1 
HETATM 1119 C  C13  . PAM   C 3 .   ? 357.745 41.561  193.899 1.00 150.51 ? 202 PAM   A C13  1 
HETATM 1120 C  C14  . PAM   C 3 .   ? 356.419 41.350  194.689 1.00 152.12 ? 202 PAM   A C14  1 
HETATM 1121 C  C15  . PAM   C 3 .   ? 356.164 39.841  194.978 1.00 148.08 ? 202 PAM   A C15  1 
HETATM 1122 C  C16  . PAM   C 3 .   ? 354.660 39.504  195.177 1.00 150.37 ? 202 PAM   A C16  1 
HETATM 1123 C  C1   . A1IH0 D 4 .   ? 345.050 20.620  198.617 1.00 135.91 ? 203 A1IH0 A C1   1 
HETATM 1124 C  C2   . A1IH0 D 4 .   ? 343.597 21.045  198.296 1.00 133.57 ? 203 A1IH0 A C2   1 
HETATM 1125 C  C11  . A1IH0 D 4 .   ? 345.704 19.248  196.537 1.00 142.01 ? 203 A1IH0 A C11  1 
HETATM 1126 C  C13  . A1IH0 D 4 .   ? 348.205 21.446  198.163 1.00 144.06 ? 203 A1IH0 A C13  1 
HETATM 1127 C  C14  . A1IH0 D 4 .   ? 342.685 23.162  197.449 1.00 134.56 ? 203 A1IH0 A C14  1 
HETATM 1128 C  C16  . A1IH0 D 4 .   ? 342.599 24.238  196.440 1.00 136.71 ? 203 A1IH0 A C16  1 
HETATM 1129 C  C17  . A1IH0 D 4 .   ? 343.120 25.452  196.655 1.00 140.84 ? 203 A1IH0 A C17  1 
HETATM 1130 C  C18  . A1IH0 D 4 .   ? 343.076 26.593  195.665 1.00 145.21 ? 203 A1IH0 A C18  1 
HETATM 1131 C  C19  . A1IH0 D 4 .   ? 343.633 26.375  194.400 1.00 147.62 ? 203 A1IH0 A C19  1 
HETATM 1132 C  C20  . A1IH0 D 4 .   ? 343.628 27.384  193.435 1.00 148.78 ? 203 A1IH0 A C20  1 
HETATM 1133 C  C21  . A1IH0 D 4 .   ? 343.062 28.627  193.729 1.00 149.59 ? 203 A1IH0 A C21  1 
HETATM 1134 C  C22  . A1IH0 D 4 .   ? 342.504 28.853  194.990 1.00 149.20 ? 203 A1IH0 A C22  1 
HETATM 1135 C  C23  . A1IH0 D 4 .   ? 342.511 27.841  195.953 1.00 146.95 ? 203 A1IH0 A C23  1 
HETATM 1136 C  C24  . A1IH0 D 4 .   ? 348.143 22.067  199.414 1.00 145.60 ? 203 A1IH0 A C24  1 
HETATM 1137 C  C25  . A1IH0 D 4 .   ? 348.906 23.205  199.673 1.00 147.77 ? 203 A1IH0 A C25  1 
HETATM 1138 C  C26  . A1IH0 D 4 .   ? 349.738 23.734  198.689 1.00 149.25 ? 203 A1IH0 A C26  1 
HETATM 1139 C  C27  . A1IH0 D 4 .   ? 349.804 23.122  197.437 1.00 147.55 ? 203 A1IH0 A C27  1 
HETATM 1140 C  C28  . A1IH0 D 4 .   ? 349.042 21.983  197.176 1.00 145.74 ? 203 A1IH0 A C28  1 
HETATM 1141 N  N3   . A1IH0 D 4 .   ? 343.512 22.095  197.293 1.00 132.68 ? 203 A1IH0 A N3   1 
HETATM 1142 C  C4   . A1IH0 D 4 .   ? 344.340 22.030  196.100 1.00 132.64 ? 203 A1IH0 A C4   1 
HETATM 1143 C  C5   . A1IH0 D 4 .   ? 345.808 21.729  196.478 1.00 135.32 ? 203 A1IH0 A C5   1 
HETATM 1144 C  C6   . A1IH0 D 4 .   ? 346.034 20.494  197.412 1.00 139.09 ? 203 A1IH0 A C6   1 
HETATM 1145 N  N7   . A1IH0 D 4 .   ? 347.416 20.293  197.897 1.00 142.81 ? 203 A1IH0 A N7   1 
HETATM 1146 C  C8   . A1IH0 D 4 .   ? 347.961 19.061  198.117 1.00 144.82 ? 203 A1IH0 A C8   1 
HETATM 1147 C  C9   . A1IH0 D 4 .   ? 347.246 17.753  197.882 1.00 146.57 ? 203 A1IH0 A C9   1 
HETATM 1148 C  C10  . A1IH0 D 4 .   ? 345.810 17.923  197.326 1.00 144.72 ? 203 A1IH0 A C10  1 
HETATM 1149 O  O12  . A1IH0 D 4 .   ? 349.101 18.945  198.528 1.00 143.29 ? 203 A1IH0 A O12  1 
HETATM 1150 O  O15  . A1IH0 D 4 .   ? 341.971 23.284  198.430 1.00 134.32 ? 203 A1IH0 A O15  1 
HETATM 1151 CL CL29 . A1IH0 D 4 .   ? 350.700 25.160  199.019 1.00 151.35 ? 203 A1IH0 A CL29 1 
HETATM 1152 F  F30  . A1IH0 D 4 .   ? 350.599 23.623  196.494 1.00 146.83 ? 203 A1IH0 A F30  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 8   ? 2.0363 2.0590 1.9213 -0.1832 -0.5122 -0.3311 1   GLY A N   
2    C CA  . GLY A 8   ? 1.9630 2.0015 1.8884 -0.1859 -0.4600 -0.3248 1   GLY A CA  
3    C C   . GLY A 8   ? 1.9894 2.0070 1.9007 -0.1718 -0.4508 -0.3000 1   GLY A C   
4    O O   . GLY A 8   ? 1.9546 1.9638 1.8560 -0.1782 -0.4095 -0.2904 1   GLY A O   
5    N N   . LYS A 9   ? 1.9591 1.9662 1.8732 -0.1508 -0.4941 -0.2919 2   LYS A N   
6    C CA  . LYS A 9   ? 1.9491 1.9236 1.8468 -0.1350 -0.4990 -0.2699 2   LYS A CA  
7    C C   . LYS A 9   ? 2.0845 1.9815 1.8628 -0.1440 -0.5170 -0.2436 2   LYS A C   
8    O O   . LYS A 9   ? 2.1048 1.9590 1.8445 -0.1442 -0.5086 -0.2211 2   LYS A O   
9    C CB  . LYS A 9   ? 1.9597 1.9592 1.9295 -0.1036 -0.5437 -0.2805 2   LYS A CB  
10   C CG  . LYS A 9   ? 1.8059 1.8892 1.8955 -0.0986 -0.5256 -0.3107 2   LYS A CG  
11   C CD  . LYS A 9   ? 1.8050 1.9175 1.9722 -0.0634 -0.5610 -0.3260 2   LYS A CD  
12   C CE  . LYS A 9   ? 1.8154 1.8982 1.9640 -0.0363 -0.6359 -0.3256 2   LYS A CE  
13   N NZ  . LYS A 9   ? 1.7781 1.8590 1.9795 0.0047  -0.6703 -0.3331 2   LYS A NZ  
14   N N   . ASP A 10  ? 2.1008 1.9765 1.8162 -0.1547 -0.5430 -0.2473 3   ASP A N   
15   C CA  . ASP A 10  ? 2.2088 2.0079 1.7932 -0.1707 -0.5595 -0.2240 3   ASP A CA  
16   C C   . ASP A 10  ? 2.2118 1.9979 1.7402 -0.2015 -0.4959 -0.2173 3   ASP A C   
17   O O   . ASP A 10  ? 2.2727 2.0032 1.7205 -0.2171 -0.4872 -0.1918 3   ASP A O   
18   C CB  . ASP A 10  ? 2.3199 2.1076 1.8531 -0.1759 -0.6021 -0.2367 3   ASP A CB  
19   C CG  . ASP A 10  ? 2.5525 2.3759 2.1640 -0.1469 -0.6651 -0.2549 3   ASP A CG  
20   O OD1 . ASP A 10  ? 2.5615 2.4612 2.2939 -0.1377 -0.6499 -0.2806 3   ASP A OD1 
21   O OD2 . ASP A 10  ? 2.6774 2.4540 2.2260 -0.1368 -0.7297 -0.2459 3   ASP A OD2 
22   N N   . GLU A 11  ? 2.0604 1.8984 1.6388 -0.2100 -0.4526 -0.2418 4   GLU A N   
23   C CA  . GLU A 11  ? 2.0355 1.8781 1.5860 -0.2323 -0.3948 -0.2468 4   GLU A CA  
24   C C   . GLU A 11  ? 1.9850 1.8405 1.5785 -0.2311 -0.3578 -0.2351 4   GLU A C   
25   O O   . GLU A 11  ? 1.9764 1.8455 1.5628 -0.2466 -0.3124 -0.2426 4   GLU A O   
26   C CB  . GLU A 11  ? 2.0160 1.8989 1.6068 -0.2351 -0.3740 -0.2795 4   GLU A CB  
27   C CG  . GLU A 11  ? 2.3136 2.1725 1.8214 -0.2511 -0.3856 -0.2950 4   GLU A CG  
28   C CD  . GLU A 11  ? 2.7907 2.6698 2.3369 -0.2443 -0.4177 -0.3194 4   GLU A CD  
29   O OE1 . GLU A 11  ? 2.8160 2.7243 2.4183 -0.2447 -0.3936 -0.3435 4   GLU A OE1 
30   O OE2 . GLU A 11  ? 2.8399 2.7013 2.3575 -0.2398 -0.4700 -0.3151 4   GLU A OE2 
31   N N   . VAL A 12  ? 1.8431 1.6978 1.4855 -0.2112 -0.3794 -0.2214 5   VAL A N   
32   C CA  . VAL A 12  ? 1.7389 1.6020 1.4223 -0.2077 -0.3541 -0.2120 5   VAL A CA  
33   C C   . VAL A 12  ? 1.7962 1.6050 1.4462 -0.2010 -0.3844 -0.1862 5   VAL A C   
34   O O   . VAL A 12  ? 1.7816 1.5855 1.4512 -0.2019 -0.3664 -0.1779 5   VAL A O   
35   C CB  . VAL A 12  ? 1.6757 1.5949 1.4618 -0.1899 -0.3427 -0.2290 5   VAL A CB  
36   C CG1 . VAL A 12  ? 1.6319 1.5851 1.4417 -0.1974 -0.3185 -0.2507 5   VAL A CG1 
37   C CG2 . VAL A 12  ? 1.6630 1.5972 1.5021 -0.1664 -0.3818 -0.2343 5   VAL A CG2 
38   N N   . ALA A 13  ? 1.7973 1.5597 1.3955 -0.1930 -0.4350 -0.1748 6   ALA A N   
39   C CA  . ALA A 13  ? 1.8564 1.5515 1.4174 -0.1810 -0.4771 -0.1504 6   ALA A CA  
40   C C   . ALA A 13  ? 1.9683 1.5980 1.4459 -0.2117 -0.4548 -0.1226 6   ALA A C   
41   O O   . ALA A 13  ? 2.0188 1.6044 1.4996 -0.2006 -0.4742 -0.1075 6   ALA A O   
42   C CB  . ALA A 13  ? 1.9578 1.6102 1.4674 -0.1677 -0.5408 -0.1439 6   ALA A CB  
43   N N   . LEU A 14  ? 1.9086 1.5355 1.3190 -0.2514 -0.4117 -0.1201 7   LEU A N   
44   C CA  . LEU A 14  ? 1.9470 1.5267 1.2883 -0.2899 -0.3804 -0.0988 7   LEU A CA  
45   C C   . LEU A 14  ? 1.8975 1.5296 1.3287 -0.2876 -0.3406 -0.1111 7   LEU A C   
46   O O   . LEU A 14  ? 1.9355 1.5248 1.3503 -0.3000 -0.3386 -0.0939 7   LEU A O   
47   C CB  . LEU A 14  ? 2.0008 1.5809 1.2573 -0.3336 -0.3400 -0.1023 7   LEU A CB  
48   C CG  . LEU A 14  ? 2.2149 1.6990 1.3178 -0.3687 -0.3601 -0.0725 7   LEU A CG  
49   C CD1 . LEU A 14  ? 2.2882 1.7022 1.3485 -0.3378 -0.4408 -0.0523 7   LEU A CD1 
50   C CD2 . LEU A 14  ? 2.2567 1.7668 1.2960 -0.4018 -0.3201 -0.0912 7   LEU A CD2 
51   N N   . LEU A 15  ? 1.7216 1.4389 1.2437 -0.2718 -0.3137 -0.1406 8   LEU A N   
52   C CA  . LEU A 15  ? 1.6009 1.3694 1.2078 -0.2653 -0.2831 -0.1540 8   LEU A CA  
53   C C   . LEU A 15  ? 1.6364 1.3902 1.2930 -0.2352 -0.3139 -0.1491 8   LEU A C   
54   O O   . LEU A 15  ? 1.6072 1.3583 1.2881 -0.2393 -0.3003 -0.1471 8   LEU A O   
55   C CB  . LEU A 15  ? 1.4955 1.3395 1.1721 -0.2534 -0.2581 -0.1827 8   LEU A CB  
56   C CG  . LEU A 15  ? 1.5465 1.4122 1.1905 -0.2708 -0.2337 -0.1991 8   LEU A CG  
57   C CD1 . LEU A 15  ? 1.4466 1.3686 1.1631 -0.2521 -0.2213 -0.2253 8   LEU A CD1 
58   C CD2 . LEU A 15  ? 1.6138 1.4797 1.2147 -0.3076 -0.1930 -0.2000 8   LEU A CD2 
59   N N   . ALA A 16  ? 1.6090 1.3569 1.2842 -0.2050 -0.3559 -0.1517 9   ALA A N   
60   C CA  . ALA A 16  ? 1.5922 1.3320 1.3200 -0.1730 -0.3852 -0.1548 9   ALA A CA  
61   C C   . ALA A 16  ? 1.7460 1.3970 1.4109 -0.1797 -0.4098 -0.1296 9   ALA A C   
62   O O   . ALA A 16  ? 1.7268 1.3677 1.4243 -0.1717 -0.4064 -0.1322 9   ALA A O   
63   C CB  . ALA A 16  ? 1.5910 1.3531 1.3590 -0.1417 -0.4245 -0.1686 9   ALA A CB  
64   N N   . ALA A 17  ? 1.8118 1.3910 1.3755 -0.1998 -0.4321 -0.1044 10  ALA A N   
65   C CA  . ALA A 17  ? 1.9227 1.3969 1.4045 -0.2149 -0.4567 -0.0739 10  ALA A CA  
66   C C   . ALA A 17  ? 1.9383 1.4086 1.4162 -0.2505 -0.4101 -0.0692 10  ALA A C   
67   O O   . ALA A 17  ? 1.9401 1.3772 1.4424 -0.2390 -0.4226 -0.0680 10  ALA A O   
68   C CB  . ALA A 17  ? 2.0604 1.4578 1.4168 -0.2408 -0.4807 -0.0459 10  ALA A CB  
69   N N   . VAL A 18  ? 1.8610 1.3774 1.3244 -0.2893 -0.3570 -0.0743 11  VAL A N   
70   C CA  . VAL A 18  ? 1.8315 1.3671 1.3056 -0.3260 -0.3097 -0.0773 11  VAL A CA  
71   C C   . VAL A 18  ? 1.7763 1.3643 1.3539 -0.2994 -0.3019 -0.0995 11  VAL A C   
72   O O   . VAL A 18  ? 1.7805 1.3458 1.3603 -0.3189 -0.2908 -0.0961 11  VAL A O   
73   C CB  . VAL A 18  ? 1.8490 1.4444 1.3083 -0.3619 -0.2579 -0.0897 11  VAL A CB  
74   C CG1 . VAL A 18  ? 1.7965 1.4443 1.3047 -0.3894 -0.2108 -0.1052 11  VAL A CG1 
75   C CG2 . VAL A 18  ? 1.9713 1.4996 1.3061 -0.4023 -0.2577 -0.0660 11  VAL A CG2 
76   N N   . THR A 19  ? 1.6547 1.3063 1.3094 -0.2590 -0.3088 -0.1217 12  THR A N   
77   C CA  . THR A 19  ? 1.5707 1.2665 1.3081 -0.2346 -0.3030 -0.1425 12  THR A CA  
78   C C   . THR A 19  ? 1.7043 1.3351 1.4386 -0.2160 -0.3373 -0.1369 12  THR A C   
79   O O   . THR A 19  ? 1.6956 1.3184 1.4485 -0.2230 -0.3274 -0.1427 12  THR A O   
80   C CB  . THR A 19  ? 1.5771 1.3399 1.3772 -0.2031 -0.3041 -0.1632 12  THR A CB  
81   O OG1 . THR A 19  ? 1.5403 1.3571 1.3485 -0.2176 -0.2734 -0.1719 12  THR A OG1 
82   C CG2 . THR A 19  ? 1.4432 1.2365 1.3099 -0.1780 -0.3038 -0.1824 12  THR A CG2 
83   N N   . LEU A 20  ? 1.7572 1.3369 1.4662 -0.1917 -0.3819 -0.1275 13  LEU A N   
84   C CA  . LEU A 20  ? 1.8244 1.3332 1.5317 -0.1653 -0.4242 -0.1253 13  LEU A CA  
85   C C   . LEU A 20  ? 1.9642 1.3787 1.6009 -0.1988 -0.4278 -0.1011 13  LEU A C   
86   O O   . LEU A 20  ? 1.9953 1.3666 1.6500 -0.1835 -0.4454 -0.1085 13  LEU A O   
87   C CB  . LEU A 20  ? 1.8859 1.3611 1.5806 -0.1315 -0.4774 -0.1207 13  LEU A CB  
88   C CG  . LEU A 20  ? 1.9597 1.4325 1.7231 -0.0797 -0.5144 -0.1454 13  LEU A CG  
89   C CD1 . LEU A 20  ? 1.8471 1.4290 1.7131 -0.0626 -0.4770 -0.1842 13  LEU A CD1 
90   C CD2 . LEU A 20  ? 2.0474 1.4934 1.8067 -0.0439 -0.5743 -0.1438 13  LEU A CD2 
91   N N   . LEU A 21  ? 1.9625 1.3454 1.5184 -0.2478 -0.4083 -0.0751 14  LEU A N   
92   C CA  . LEU A 21  ? 2.0570 1.3568 1.5385 -0.2964 -0.4001 -0.0506 14  LEU A CA  
93   C C   . LEU A 21  ? 2.0331 1.3867 1.5773 -0.3133 -0.3612 -0.0720 14  LEU A C   
94   O O   . LEU A 21  ? 2.0873 1.3782 1.6233 -0.3205 -0.3741 -0.0694 14  LEU A O   
95   C CB  . LEU A 21  ? 2.1175 1.4065 1.5126 -0.3486 -0.3729 -0.0281 14  LEU A CB  
96   C CG  . LEU A 21  ? 2.3460 1.5084 1.6139 -0.3972 -0.3865 0.0116  14  LEU A CG  
97   C CD1 . LEU A 21  ? 2.4594 1.4990 1.6911 -0.3657 -0.4539 0.0304  14  LEU A CD1 
98   C CD2 . LEU A 21  ? 2.4257 1.5732 1.6009 -0.4242 -0.3807 0.0308  14  LEU A CD2 
99   N N   . GLY A 22  ? 1.8667 1.3312 1.4744 -0.3142 -0.3210 -0.0948 15  GLY A N   
100  C CA  . GLY A 22  ? 1.7767 1.3060 1.4498 -0.3235 -0.2899 -0.1183 15  GLY A CA  
101  C C   . GLY A 22  ? 1.7864 1.3081 1.5101 -0.2862 -0.3119 -0.1373 15  GLY A C   
102  O O   . GLY A 22  ? 1.8084 1.3093 1.5402 -0.3032 -0.3076 -0.1442 15  GLY A O   
103  N N   . VAL A 23  ? 1.6916 1.2298 1.4491 -0.2374 -0.3353 -0.1491 16  VAL A N   
104  C CA  . VAL A 23  ? 1.6585 1.1918 1.4630 -0.2003 -0.3534 -0.1731 16  VAL A CA  
105  C C   . VAL A 23  ? 1.8441 1.2688 1.6064 -0.2052 -0.3841 -0.1631 16  VAL A C   
106  O O   . VAL A 23  ? 1.8591 1.2733 1.6388 -0.2117 -0.3782 -0.1788 16  VAL A O   
107  C CB  . VAL A 23  ? 1.6337 1.2086 1.4862 -0.1519 -0.3702 -0.1913 16  VAL A CB  
108  C CG1 . VAL A 23  ? 1.6272 1.1934 1.5250 -0.1155 -0.3863 -0.2211 16  VAL A CG1 
109  C CG2 . VAL A 23  ? 1.5234 1.1964 1.4165 -0.1524 -0.3380 -0.2028 16  VAL A CG2 
110  N N   . LEU A 24  ? 1.9159 1.2515 1.6142 -0.2057 -0.4191 -0.1356 17  LEU A N   
111  C CA  . LEU A 24  ? 2.0418 1.2503 1.6860 -0.2104 -0.4565 -0.1206 17  LEU A CA  
112  C C   . LEU A 24  ? 2.1490 1.3174 1.7526 -0.2700 -0.4313 -0.1079 17  LEU A C   
113  O O   . LEU A 24  ? 2.2307 1.3272 1.8279 -0.2706 -0.4498 -0.1145 17  LEU A O   
114  C CB  . LEU A 24  ? 2.1554 1.2659 1.7241 -0.2016 -0.5048 -0.0883 17  LEU A CB  
115  C CG  . LEU A 24  ? 2.1824 1.3219 1.7976 -0.1386 -0.5437 -0.1043 17  LEU A CG  
116  C CD1 . LEU A 24  ? 2.2751 1.3450 1.8065 -0.1432 -0.5821 -0.0685 17  LEU A CD1 
117  C CD2 . LEU A 24  ? 2.2347 1.3403 1.9064 -0.0828 -0.5836 -0.1351 17  LEU A CD2 
118  N N   . LEU A 25  ? 2.0576 1.2798 1.6435 -0.3196 -0.3878 -0.0959 18  LEU A N   
119  C CA  . LEU A 25  ? 2.0807 1.2906 1.6458 -0.3811 -0.3572 -0.0906 18  LEU A CA  
120  C C   . LEU A 25  ? 2.0820 1.3439 1.7231 -0.3697 -0.3468 -0.1264 18  LEU A C   
121  O O   . LEU A 25  ? 2.1509 1.3584 1.7768 -0.4027 -0.3481 -0.1276 18  LEU A O   
122  C CB  . LEU A 25  ? 2.0355 1.3194 1.5897 -0.4272 -0.3098 -0.0828 18  LEU A CB  
123  C CG  . LEU A 25  ? 2.1285 1.4086 1.6627 -0.4988 -0.2742 -0.0785 18  LEU A CG  
124  C CD1 . LEU A 25  ? 2.2919 1.4424 1.7129 -0.5488 -0.2855 -0.0393 18  LEU A CD1 
125  C CD2 . LEU A 25  ? 2.0636 1.4625 1.6374 -0.5243 -0.2242 -0.0932 18  LEU A CD2 
126  N N   . GLN A 26  ? 1.9210 1.2793 1.6353 -0.3255 -0.3389 -0.1551 19  GLN A N   
127  C CA  . GLN A 26  ? 1.8530 1.2588 1.6267 -0.3111 -0.3321 -0.1893 19  GLN A CA  
128  C C   . GLN A 26  ? 1.9741 1.2999 1.7452 -0.2807 -0.3669 -0.2048 19  GLN A C   
129  O O   . GLN A 26  ? 2.0007 1.3158 1.7861 -0.2924 -0.3657 -0.2254 19  GLN A O   
130  C CB  . GLN A 26  ? 1.7403 1.2560 1.5738 -0.2779 -0.3143 -0.2109 19  GLN A CB  
131  C CG  . GLN A 26  ? 1.6856 1.2836 1.5341 -0.3020 -0.2821 -0.2048 19  GLN A CG  
132  C CD  . GLN A 26  ? 1.8194 1.4430 1.6773 -0.3494 -0.2604 -0.2087 19  GLN A CD  
133  O OE1 . GLN A 26  ? 1.7228 1.3640 1.5654 -0.3852 -0.2388 -0.1956 19  GLN A OE1 
134  N NE2 . GLN A 26  ? 1.7994 1.4345 1.6868 -0.3514 -0.2643 -0.2313 19  GLN A NE2 
135  N N   . ALA A 27  ? 1.9652 1.2360 1.7215 -0.2402 -0.4006 -0.1988 20  ALA A N   
136  C CA  . ALA A 27  ? 2.0432 1.2329 1.8027 -0.2026 -0.4392 -0.2178 20  ALA A CA  
137  C C   . ALA A 27  ? 2.2169 1.2785 1.9129 -0.2418 -0.4598 -0.1993 20  ALA A C   
138  O O   . ALA A 27  ? 2.2543 1.2616 1.9599 -0.2292 -0.4778 -0.2243 20  ALA A O   
139  C CB  . ALA A 27  ? 2.0807 1.2458 1.8441 -0.1518 -0.4752 -0.2145 20  ALA A CB  
140  N N   . TYR A 28  ? 2.2286 1.2411 1.8555 -0.2936 -0.4543 -0.1568 21  TYR A N   
141  C CA  . TYR A 28  ? 2.3494 1.2426 1.9037 -0.3485 -0.4647 -0.1316 21  TYR A CA  
142  C C   . TYR A 28  ? 2.3586 1.2942 1.9472 -0.3903 -0.4338 -0.1550 21  TYR A C   
143  O O   . TYR A 28  ? 2.4524 1.2981 2.0224 -0.4036 -0.4543 -0.1634 21  TYR A O   
144  C CB  . TYR A 28  ? 2.4271 1.2818 1.8979 -0.4014 -0.4532 -0.0837 21  TYR A CB  
145  C CG  . TYR A 28  ? 2.5843 1.3333 1.9784 -0.4766 -0.4482 -0.0573 21  TYR A CG  
146  C CD1 . TYR A 28  ? 2.7727 1.3569 2.1000 -0.4771 -0.4972 -0.0405 21  TYR A CD1 
147  C CD2 . TYR A 28  ? 2.5691 1.3833 1.9630 -0.5482 -0.3950 -0.0528 21  TYR A CD2 
148  C CE1 . TYR A 28  ? 2.9284 1.4071 2.1809 -0.5537 -0.4914 -0.0156 21  TYR A CE1 
149  C CE2 . TYR A 28  ? 2.7151 1.4405 2.0444 -0.6257 -0.3848 -0.0319 21  TYR A CE2 
150  C CZ  . TYR A 28  ? 2.9875 1.5406 2.2413 -0.6317 -0.4322 -0.0111 21  TYR A CZ  
151  O OH  . TYR A 28  ? 3.1125 1.5679 2.2955 -0.7158 -0.4212 0.0117  21  TYR A OH  
152  N N   . PHE A 29  ? 2.1884 1.2579 1.8296 -0.4070 -0.3900 -0.1683 22  PHE A N   
153  C CA  . PHE A 29  ? 2.1331 1.2657 1.8187 -0.4421 -0.3642 -0.1938 22  PHE A CA  
154  C C   . PHE A 29  ? 2.1717 1.3035 1.8984 -0.4028 -0.3830 -0.2349 22  PHE A C   
155  O O   . PHE A 29  ? 2.2093 1.3252 1.9440 -0.4352 -0.3824 -0.2528 22  PHE A O   
156  C CB  . PHE A 29  ? 2.0222 1.2983 1.7601 -0.4515 -0.3239 -0.2012 22  PHE A CB  
157  C CG  . PHE A 29  ? 2.0435 1.3436 1.7517 -0.4977 -0.2942 -0.1726 22  PHE A CG  
158  C CD1 . PHE A 29  ? 2.2101 1.4115 1.8419 -0.5521 -0.2942 -0.1410 22  PHE A CD1 
159  C CD2 . PHE A 29  ? 1.9449 1.3628 1.6974 -0.4913 -0.2643 -0.1799 22  PHE A CD2 
160  C CE1 . PHE A 29  ? 2.2316 1.4592 1.8288 -0.5997 -0.2602 -0.1188 22  PHE A CE1 
161  C CE2 . PHE A 29  ? 1.9860 1.4314 1.7138 -0.5338 -0.2329 -0.1617 22  PHE A CE2 
162  C CZ  . PHE A 29  ? 2.0885 1.4435 1.7385 -0.5893 -0.2280 -0.1326 22  PHE A CZ  
163  N N   . SER A 30  ? 2.0865 1.2391 1.8395 -0.3366 -0.3979 -0.2532 23  SER A N   
164  C CA  . SER A 30  ? 2.0812 1.2381 1.8685 -0.2952 -0.4107 -0.2971 23  SER A CA  
165  C C   . SER A 30  ? 2.2788 1.2988 2.0314 -0.2899 -0.4486 -0.3048 23  SER A C   
166  O O   . SER A 30  ? 2.3171 1.3165 2.0806 -0.2913 -0.4548 -0.3390 23  SER A O   
167  C CB  . SER A 30  ? 2.0656 1.2887 1.8912 -0.2336 -0.4090 -0.3146 23  SER A CB  
168  O OG  . SER A 30  ? 2.1127 1.4482 1.9648 -0.2391 -0.3774 -0.3067 23  SER A OG  
169  N N   . LEU A 31  ? 2.3120 1.2299 2.0160 -0.2849 -0.4778 -0.2724 24  LEU A N   
170  C CA  . LEU A 31  ? 2.4429 1.2047 2.1002 -0.2805 -0.5226 -0.2697 24  LEU A CA  
171  C C   . LEU A 31  ? 2.5668 1.2648 2.1836 -0.3553 -0.5150 -0.2577 24  LEU A C   
172  O O   . LEU A 31  ? 2.6673 1.2745 2.2728 -0.3558 -0.5400 -0.2803 24  LEU A O   
173  C CB  . LEU A 31  ? 2.5188 1.1904 2.1207 -0.2662 -0.5568 -0.2276 24  LEU A CB  
174  C CG  . LEU A 31  ? 2.7390 1.2284 2.2787 -0.2586 -0.6135 -0.2152 24  LEU A CG  
175  C CD1 . LEU A 31  ? 2.7515 1.2179 2.3428 -0.1720 -0.6543 -0.2597 24  LEU A CD1 
176  C CD2 . LEU A 31  ? 2.8593 1.2542 2.3104 -0.2833 -0.6371 -0.1558 24  LEU A CD2 
177  N N   . GLN A 32  ? 2.4764 1.2267 2.0768 -0.4193 -0.4791 -0.2271 25  GLN A N   
178  C CA  . GLN A 32  ? 2.5341 1.2495 2.1090 -0.4997 -0.4633 -0.2182 25  GLN A CA  
179  C C   . GLN A 32  ? 2.5585 1.3345 2.1918 -0.5044 -0.4547 -0.2664 25  GLN A C   
180  O O   . GLN A 32  ? 2.6681 1.3576 2.2800 -0.5420 -0.4697 -0.2768 25  GLN A O   
181  C CB  . GLN A 32  ? 2.5039 1.2882 2.0653 -0.5612 -0.4207 -0.1854 25  GLN A CB  
182  C CG  . GLN A 32  ? 2.7073 1.4031 2.1822 -0.5786 -0.4295 -0.1335 25  GLN A CG  
183  C CD  . GLN A 32  ? 3.1874 1.6937 2.5694 -0.6100 -0.4675 -0.1055 25  GLN A CD  
184  O OE1 . GLN A 32  ? 3.2669 1.7170 2.6044 -0.6909 -0.4509 -0.0885 25  GLN A OE1 
185  N NE2 . GLN A 32  ? 3.1508 1.5521 2.5021 -0.5477 -0.5207 -0.1006 25  GLN A NE2 
186  N N   . VAL A 33  ? 2.3695 1.2820 2.0683 -0.4659 -0.4351 -0.2957 26  VAL A N   
187  C CA  . VAL A 33  ? 2.3320 1.3041 2.0762 -0.4644 -0.4314 -0.3414 26  VAL A CA  
188  C C   . VAL A 33  ? 2.4817 1.3685 2.2171 -0.4178 -0.4651 -0.3784 26  VAL A C   
189  O O   . VAL A 33  ? 2.5344 1.3821 2.2685 -0.4419 -0.4765 -0.4072 26  VAL A O   
190  C CB  . VAL A 33  ? 2.2348 1.3627 2.0346 -0.4437 -0.4035 -0.3554 26  VAL A CB  
191  C CG1 . VAL A 33  ? 2.2032 1.3782 2.0329 -0.4291 -0.4087 -0.4028 26  VAL A CG1 
192  C CG2 . VAL A 33  ? 2.1881 1.3917 2.0058 -0.4983 -0.3737 -0.3319 26  VAL A CG2 
193  N N   . ILE A 34  ? 2.4638 1.3159 2.1947 -0.3539 -0.4831 -0.3803 27  ILE A N   
194  C CA  . ILE A 34  ? 2.5374 1.3081 2.2676 -0.3036 -0.5151 -0.4209 27  ILE A CA  
195  C C   . ILE A 34  ? 2.7475 1.3578 2.4264 -0.3389 -0.5491 -0.4140 27  ILE A C   
196  O O   . ILE A 34  ? 2.8188 1.3802 2.5005 -0.3321 -0.5652 -0.4571 27  ILE A O   
197  C CB  . ILE A 34  ? 2.5538 1.3302 2.3037 -0.2288 -0.5287 -0.4266 27  ILE A CB  
198  C CG1 . ILE A 34  ? 2.4185 1.3420 2.2230 -0.1913 -0.4959 -0.4582 27  ILE A CG1 
199  C CG2 . ILE A 34  ? 2.6877 1.3382 2.4290 -0.1817 -0.5735 -0.4572 27  ILE A CG2 
200  C CD1 . ILE A 34  ? 2.4017 1.3792 2.2333 -0.1447 -0.4924 -0.4468 27  ILE A CD1 
201  N N   . SER A 35  ? 2.7767 1.3028 2.4018 -0.3823 -0.5581 -0.3604 28  SER A N   
202  C CA  . SER A 35  ? 2.9497 1.3080 2.5100 -0.4282 -0.5893 -0.3426 28  SER A CA  
203  C C   . SER A 35  ? 3.0263 1.3932 2.5912 -0.5014 -0.5724 -0.3590 28  SER A C   
204  O O   . SER A 35  ? 3.1418 1.3891 2.6802 -0.5166 -0.6017 -0.3790 28  SER A O   
205  C CB  . SER A 35  ? 3.0727 1.3471 2.5613 -0.4639 -0.5970 -0.2772 28  SER A CB  
206  O OG  . SER A 35  ? 3.1807 1.4318 2.6635 -0.3936 -0.6247 -0.2653 28  SER A OG  
207  N N   . ALA A 36  ? 2.8696 1.3805 2.4750 -0.5426 -0.5290 -0.3559 29  ALA A N   
208  C CA  . ALA A 36  ? 2.8669 1.4187 2.4962 -0.6096 -0.5132 -0.3765 29  ALA A CA  
209  C C   . ALA A 36  ? 2.9022 1.4794 2.5674 -0.5759 -0.5281 -0.4387 29  ALA A C   
210  O O   . ALA A 36  ? 2.9648 1.5154 2.6330 -0.6253 -0.5352 -0.4621 29  ALA A O   
211  C CB  . ALA A 36  ? 2.7469 1.4562 2.4224 -0.6458 -0.4689 -0.3624 29  ALA A CB  
212  N N   . ARG A 37  ? 2.7895 1.4176 2.4786 -0.4963 -0.5314 -0.4671 30  ARG A N   
213  C CA  . ARG A 37  ? 2.7820 1.4351 2.4924 -0.4589 -0.5410 -0.5283 30  ARG A CA  
214  C C   . ARG A 37  ? 3.0183 1.5153 2.6943 -0.4468 -0.5801 -0.5593 30  ARG A C   
215  O O   . ARG A 37  ? 3.0447 1.5345 2.7251 -0.4486 -0.5902 -0.6100 30  ARG A O   
216  C CB  . ARG A 37  ? 2.6553 1.4051 2.3946 -0.3845 -0.5261 -0.5470 30  ARG A CB  
217  C CG  . ARG A 37  ? 2.5784 1.4834 2.3523 -0.3948 -0.4927 -0.5361 30  ARG A CG  
218  C CD  . ARG A 37  ? 2.5866 1.5731 2.3772 -0.3383 -0.4809 -0.5741 30  ARG A CD  
219  N NE  . ARG A 37  ? 2.5694 1.6873 2.3834 -0.3507 -0.4567 -0.5652 30  ARG A NE  
220  C CZ  . ARG A 37  ? 2.6387 1.8112 2.4540 -0.3653 -0.4580 -0.5952 30  ARG A CZ  
221  N NH1 . ARG A 37  ? 2.2965 1.5774 2.1305 -0.3706 -0.4432 -0.5835 30  ARG A NH1 
222  N NH2 . ARG A 37  ? 2.6526 1.7655 2.4468 -0.3730 -0.4787 -0.6384 30  ARG A NH2 
223  N N   . ARG A 38  ? 3.1008 1.4673 2.7385 -0.4323 -0.6061 -0.5302 31  ARG A N   
224  C CA  . ARG A 38  ? 3.2303 1.4709 2.8518 -0.4185 -0.6167 -0.5532 31  ARG A CA  
225  C C   . ARG A 38  ? 3.2885 1.5406 2.9334 -0.4997 -0.5478 -0.5328 31  ARG A C   
226  O O   . ARG A 38  ? 3.3124 1.5598 2.9899 -0.5131 -0.5085 -0.5714 31  ARG A O   
227  C CB  . ARG A 38  ? 3.2476 1.4593 2.8776 -0.3518 -0.6029 -0.5361 31  ARG A CB  
228  C CG  . ARG A 38  ? 3.3344 1.5745 3.0097 -0.3702 -0.4885 -0.4978 31  ARG A CG  
229  C CD  . ARG A 38  ? 3.3947 1.7412 3.1105 -0.3560 -0.4165 -0.4390 31  ARG A CD  
230  N NE  . ARG A 38  ? 3.4260 1.9118 3.1806 -0.2955 -0.3728 -0.4393 31  ARG A NE  
231  C CZ  . ARG A 38  ? 3.4878 2.0975 3.2860 -0.2750 -0.3019 -0.3957 31  ARG A CZ  
232  N NH1 . ARG A 38  ? 3.4455 1.9522 3.2037 -0.3033 -0.3441 -0.3493 31  ARG A NH1 
233  N NH2 . ARG A 38  ? 3.3883 1.9174 3.1305 -0.2212 -0.4171 -0.4039 31  ARG A NH2 
234  N N   . ALA A 39  ? 3.2706 1.4990 2.8784 -0.5590 -0.5639 -0.4751 32  ALA A N   
235  C CA  . ALA A 39  ? 3.2804 1.5203 2.9206 -0.6352 -0.5122 -0.4557 32  ALA A CA  
236  C C   . ALA A 39  ? 3.2708 1.6146 2.9733 -0.6878 -0.4865 -0.4954 32  ALA A C   
237  O O   . ALA A 39  ? 3.2654 1.6435 3.0320 -0.7420 -0.4417 -0.4939 32  ALA A O   
238  C CB  . ALA A 39  ? 3.2799 1.5295 2.8939 -0.6715 -0.4991 -0.3907 32  ALA A CB  
239  N N   . PHE A 40  ? 3.2348 1.5787 2.8943 -0.6763 -0.5511 -0.5274 33  PHE A N   
240  C CA  . PHE A 40  ? 3.2091 1.6260 2.9034 -0.7250 -0.5526 -0.5652 33  PHE A CA  
241  C C   . PHE A 40  ? 3.2249 1.6899 2.9403 -0.6684 -0.5550 -0.6316 33  PHE A C   
242  O O   . PHE A 40  ? 3.2028 1.7246 2.9394 -0.7000 -0.5646 -0.6677 33  PHE A O   
243  C CB  . PHE A 40  ? 3.1567 1.6773 2.8569 -0.7736 -0.5553 -0.5356 33  PHE A CB  
244  C CG  . PHE A 40  ? 3.1689 1.7080 2.8832 -0.8421 -0.5145 -0.4880 33  PHE A CG  
245  C CD1 . PHE A 40  ? 3.1633 1.7712 2.9895 -0.8859 -0.4596 -0.5093 33  PHE A CD1 
246  C CD2 . PHE A 40  ? 3.1533 1.7116 2.8346 -0.8377 -0.5019 -0.4364 33  PHE A CD2 
247  C CE1 . PHE A 40  ? 3.1445 1.7988 3.0232 -0.9304 -0.4160 -0.4725 33  PHE A CE1 
248  C CE2 . PHE A 40  ? 3.1689 1.7691 2.8795 -0.8928 -0.4521 -0.4000 33  PHE A CE2 
249  C CZ  . PHE A 40  ? 3.1413 1.7797 2.9441 -0.9405 -0.4144 -0.4163 33  PHE A CZ  
250  N N   . ARG A 41  ? 3.2213 1.6223 2.9051 -0.5922 -0.5731 -0.6460 34  ARG A N   
251  C CA  . ARG A 41  ? 3.2157 1.6366 2.8971 -0.5343 -0.5816 -0.7071 34  ARG A CA  
252  C C   . ARG A 41  ? 3.1829 1.7086 2.8714 -0.5221 -0.6114 -0.7257 34  ARG A C   
253  O O   . ARG A 41  ? 3.1785 1.7452 2.8680 -0.5164 -0.6095 -0.7786 34  ARG A O   
254  C CB  . ARG A 41  ? 3.2534 1.6750 2.9573 -0.5556 -0.5206 -0.7571 34  ARG A CB  
255  C CG  . ARG A 41  ? 3.3589 1.8616 3.1300 -0.5305 -0.3530 -0.7533 34  ARG A CG  
256  C CD  . ARG A 41  ? 3.5339 2.1306 3.3903 -0.5565 -0.2558 -0.7343 34  ARG A CD  
257  N NE  . ARG A 41  ? 3.5621 2.2757 3.4625 -0.4812 -0.2039 -0.6129 34  ARG A NE  
258  C CZ  . ARG A 41  ? 3.5762 2.4711 3.5254 -0.4349 -0.1742 -0.5030 34  ARG A CZ  
259  N NH1 . ARG A 41  ? 3.6222 2.3681 3.5836 -0.4641 -0.1713 -0.5193 34  ARG A NH1 
260  N NH2 . ARG A 41  ? 3.5854 2.3881 3.5505 -0.5264 -0.2153 -0.5708 34  ARG A NH2 
261  N N   . VAL A 42  ? 2.9909 1.6280 2.7067 -0.5189 -0.5814 -0.6804 35  VAL A N   
262  C CA  . VAL A 42  ? 2.8483 1.6434 2.5950 -0.5053 -0.5588 -0.6883 35  VAL A CA  
263  C C   . VAL A 42  ? 2.8601 1.6944 2.6010 -0.4264 -0.5459 -0.7073 35  VAL A C   
264  O O   . VAL A 42  ? 2.8032 1.6469 2.5520 -0.3921 -0.5318 -0.6754 35  VAL A O   
265  C CB  . VAL A 42  ? 2.7804 1.6826 2.5656 -0.5458 -0.5347 -0.6407 35  VAL A CB  
266  C CG1 . VAL A 42  ? 2.6673 1.7104 2.4797 -0.5334 -0.5254 -0.6580 35  VAL A CG1 
267  C CG2 . VAL A 42  ? 2.8413 1.7059 2.6377 -0.6289 -0.5402 -0.6242 35  VAL A CG2 
268  N N   . SER A 43  ? 2.8484 1.7037 2.5728 -0.4020 -0.5505 -0.7625 36  SER A N   
269  C CA  . SER A 43  ? 2.8136 1.7074 2.5279 -0.3362 -0.5335 -0.7943 36  SER A CA  
270  C C   . SER A 43  ? 2.7154 1.7462 2.4403 -0.3272 -0.5055 -0.7737 36  SER A C   
271  O O   . SER A 43  ? 2.6728 1.7669 2.3960 -0.3616 -0.5101 -0.7720 36  SER A O   
272  C CB  . SER A 43  ? 2.9588 1.8117 2.6378 -0.3228 -0.5470 -0.8654 36  SER A CB  
273  O OG  . SER A 43  ? 3.2201 1.9558 2.8860 -0.3566 -0.5801 -0.8852 36  SER A OG  
274  N N   . PRO A 44  ? 2.6053 1.6819 2.3425 -0.2809 -0.4801 -0.7599 37  PRO A N   
275  C CA  . PRO A 44  ? 2.4970 1.6916 2.2367 -0.2745 -0.4546 -0.7408 37  PRO A CA  
276  C C   . PRO A 44  ? 2.5957 1.8246 2.2900 -0.2629 -0.4486 -0.7907 37  PRO A C   
277  O O   . PRO A 44  ? 2.6808 1.8539 2.3533 -0.2404 -0.4512 -0.8418 37  PRO A O   
278  C CB  . PRO A 44  ? 2.4565 1.6724 2.2219 -0.2313 -0.4318 -0.7184 37  PRO A CB  
279  C CG  . PRO A 44  ? 2.5857 1.6941 2.3646 -0.2192 -0.4523 -0.7157 37  PRO A CG  
280  C CD  . PRO A 44  ? 2.6494 1.6732 2.4017 -0.2322 -0.4771 -0.7628 37  PRO A CD  
281  N N   . PRO A 45  ? 2.5191 1.8265 2.1911 -0.2798 -0.4455 -0.7813 38  PRO A N   
282  C CA  . PRO A 45  ? 2.4259 1.8080 2.1246 -0.2995 -0.4435 -0.7297 38  PRO A CA  
283  C C   . PRO A 45  ? 2.4724 1.8620 2.1989 -0.3482 -0.4728 -0.7144 38  PRO A C   
284  O O   . PRO A 45  ? 2.4175 1.8796 2.1553 -0.3613 -0.4788 -0.6936 38  PRO A O   
285  C CB  . PRO A 45  ? 2.4303 1.8769 2.0803 -0.2853 -0.4298 -0.7380 38  PRO A CB  
286  C CG  . PRO A 45  ? 2.5858 1.9927 2.1750 -0.2875 -0.4422 -0.7952 38  PRO A CG  
287  C CD  . PRO A 45  ? 2.5917 1.9169 2.1993 -0.2725 -0.4419 -0.8273 38  PRO A CD  
288  N N   . LEU A 46  ? 2.4872 1.8041 2.2298 -0.3757 -0.4911 -0.7248 39  LEU A N   
289  C CA  . LEU A 46  ? 2.4837 1.8177 2.2636 -0.4291 -0.5130 -0.7131 39  LEU A CA  
290  C C   . LEU A 46  ? 2.4878 1.8386 2.3184 -0.4488 -0.4966 -0.6627 39  LEU A C   
291  O O   . LEU A 46  ? 2.5201 1.8104 2.3477 -0.4355 -0.4835 -0.6439 39  LEU A O   
292  C CB  . LEU A 46  ? 2.5910 1.8429 2.3591 -0.4621 -0.5407 -0.7507 39  LEU A CB  
293  C CG  . LEU A 46  ? 2.6945 1.9616 2.4243 -0.4667 -0.5667 -0.7979 39  LEU A CG  
294  C CD1 . LEU A 46  ? 2.7890 1.9705 2.4614 -0.4392 -0.5688 -0.8477 39  LEU A CD1 
295  C CD2 . LEU A 46  ? 2.7642 2.0451 2.5304 -0.5246 -0.5988 -0.8081 39  LEU A CD2 
296  N N   . THR A 47  ? 2.3607 1.7952 2.2366 -0.4784 -0.4991 -0.6436 40  THR A N   
297  C CA  . THR A 47  ? 2.2805 1.7496 2.2050 -0.5019 -0.4788 -0.6010 40  THR A CA  
298  C C   . THR A 47  ? 2.3396 1.8096 2.3081 -0.5686 -0.4897 -0.6061 40  THR A C   
299  O O   . THR A 47  ? 2.3001 1.7939 2.3060 -0.6014 -0.4691 -0.5765 40  THR A O   
300  C CB  . THR A 47  ? 2.1837 1.7595 2.1338 -0.4788 -0.4680 -0.5811 40  THR A CB  
301  O OG1 . THR A 47  ? 2.1629 1.8098 2.1467 -0.5000 -0.4939 -0.6014 40  THR A OG1 
302  C CG2 . THR A 47  ? 2.0800 1.6596 1.9830 -0.4231 -0.4583 -0.5818 40  THR A CG2 
303  N N   . THR A 48  ? 2.3430 1.7914 2.3057 -0.5917 -0.5202 -0.6469 41  THR A N   
304  C CA  . THR A 48  ? 2.3843 1.8392 2.3929 -0.6588 -0.5350 -0.6626 41  THR A CA  
305  C C   . THR A 48  ? 2.5416 1.8650 2.5165 -0.6942 -0.5416 -0.6719 41  THR A C   
306  O O   . THR A 48  ? 2.6023 1.8367 2.5200 -0.6638 -0.5560 -0.6952 41  THR A O   
307  C CB  . THR A 48  ? 2.4638 1.9927 2.4971 -0.6654 -0.5719 -0.7029 41  THR A CB  
308  O OG1 . THR A 48  ? 2.4759 1.9682 2.4385 -0.6187 -0.5910 -0.7297 41  THR A OG1 
309  C CG2 . THR A 48  ? 2.3345 1.9980 2.4345 -0.6595 -0.5719 -0.6915 41  THR A CG2 
310  N N   . GLY A 49  ? 2.5234 1.8354 2.5338 -0.7603 -0.5299 -0.6557 42  GLY A N   
311  C CA  . GLY A 49  ? 2.6446 1.8246 2.6227 -0.8088 -0.5366 -0.6571 42  GLY A CA  
312  C C   . GLY A 49  ? 2.7118 1.9185 2.7416 -0.8973 -0.5210 -0.6456 42  GLY A C   
313  O O   . GLY A 49  ? 2.6346 1.9694 2.7415 -0.9256 -0.5208 -0.6636 42  GLY A O   
314  N N   . PRO A 50  ? 2.7763 1.8636 2.7649 -0.9437 -0.5075 -0.6159 43  PRO A N   
315  C CA  . PRO A 50  ? 2.8256 1.9341 2.8547 -1.0399 -0.4841 -0.6040 43  PRO A CA  
316  C C   . PRO A 50  ? 2.7870 2.0313 2.8727 -1.0508 -0.4409 -0.5763 43  PRO A C   
317  O O   . PRO A 50  ? 2.6911 1.9804 2.7672 -0.9820 -0.4311 -0.5567 43  PRO A O   
318  C CB  . PRO A 50  ? 2.9629 1.9070 2.9355 -1.0582 -0.4757 -0.5756 43  PRO A CB  
319  C CG  . PRO A 50  ? 3.0431 1.8882 2.9605 -0.9783 -0.5023 -0.5923 43  PRO A CG  
320  C CD  . PRO A 50  ? 2.8860 1.8094 2.7877 -0.9136 -0.5156 -0.5935 43  PRO A CD  
321  N N   . PRO A 51  ? 2.7671 2.0790 2.9126 -1.1367 -0.4114 -0.5764 44  PRO A N   
322  C CA  . PRO A 51  ? 2.6698 2.1152 2.8717 -1.1433 -0.3668 -0.5572 44  PRO A CA  
323  C C   . PRO A 51  ? 2.7339 2.1073 2.8570 -1.1288 -0.3339 -0.4999 44  PRO A C   
324  O O   . PRO A 51  ? 2.6763 2.1442 2.8336 -1.1432 -0.2927 -0.4837 44  PRO A O   
325  C CB  . PRO A 51  ? 2.6661 2.2006 3.0159 -1.1809 -0.3584 -0.5631 44  PRO A CB  
326  C CG  . PRO A 51  ? 2.7002 2.1970 3.1580 -1.1232 -0.4203 -0.5824 44  PRO A CG  
327  C CD  . PRO A 51  ? 2.7677 2.0976 3.0658 -1.1343 -0.4221 -0.5923 44  PRO A CD  
328  N N   . GLU A 52  ? 2.7627 1.9700 2.7826 -1.0980 -0.3550 -0.4731 45  GLU A N   
329  C CA  . GLU A 52  ? 2.7759 1.8971 2.7129 -1.0772 -0.3377 -0.4200 45  GLU A CA  
330  C C   . GLU A 52  ? 2.7170 1.8213 2.6241 -0.9723 -0.3612 -0.4147 45  GLU A C   
331  O O   . GLU A 52  ? 2.6554 1.7837 2.5427 -0.9399 -0.3411 -0.3828 45  GLU A O   
332  C CB  . GLU A 52  ? 2.9428 1.8989 2.8166 -1.1177 -0.3379 -0.3894 45  GLU A CB  
333  C CG  . GLU A 52  ? 3.0083 1.9654 2.9076 -1.0615 -0.2989 -0.3391 45  GLU A CG  
334  C CD  . GLU A 52  ? 3.0402 2.1815 3.0565 -1.0162 -0.2543 -0.3270 45  GLU A CD  
335  O OE1 . GLU A 52  ? 3.1019 2.2101 2.9927 -1.0177 -0.2605 -0.3072 45  GLU A OE1 
336  O OE2 . GLU A 52  ? 2.9418 2.1256 2.9338 -1.1406 -0.2303 -0.3340 45  GLU A OE2 
337  N N   . PHE A 53  ? 2.6605 1.7275 2.5639 -0.9220 -0.4008 -0.4486 46  PHE A N   
338  C CA  . PHE A 53  ? 2.5797 1.6474 2.4628 -0.8267 -0.4163 -0.4500 46  PHE A CA  
339  C C   . PHE A 53  ? 2.4595 1.6914 2.4049 -0.7922 -0.3952 -0.4529 46  PHE A C   
340  O O   . PHE A 53  ? 2.3970 1.6437 2.3240 -0.7468 -0.3818 -0.4259 46  PHE A O   
341  C CB  . PHE A 53  ? 2.6378 1.6492 2.5060 -0.7833 -0.4553 -0.4932 46  PHE A CB  
342  C CG  . PHE A 53  ? 2.5668 1.6178 2.4294 -0.6932 -0.4604 -0.5020 46  PHE A CG  
343  C CD1 . PHE A 53  ? 2.6155 1.5963 2.4337 -0.6436 -0.4606 -0.4757 46  PHE A CD1 
344  C CD2 . PHE A 53  ? 2.4990 1.6624 2.4008 -0.6615 -0.4645 -0.5345 46  PHE A CD2 
345  C CE1 . PHE A 53  ? 2.5396 1.5711 2.3623 -0.5680 -0.4592 -0.4857 46  PHE A CE1 
346  C CE2 . PHE A 53  ? 2.4601 1.6608 2.3507 -0.5884 -0.4625 -0.5394 46  PHE A CE2 
347  C CZ  . PHE A 53  ? 2.4413 1.5804 2.2971 -0.5441 -0.4569 -0.5169 46  PHE A CZ  
348  N N   . GLU A 54  ? 2.3476 1.6982 2.3679 -0.8164 -0.3952 -0.4852 47  GLU A N   
349  C CA  . GLU A 54  ? 2.2108 1.7130 2.2963 -0.7865 -0.3831 -0.4923 47  GLU A CA  
350  C C   . GLU A 54  ? 2.2059 1.7632 2.3054 -0.7992 -0.3417 -0.4570 47  GLU A C   
351  O O   . GLU A 54  ? 2.1017 1.7350 2.2200 -0.7486 -0.3339 -0.4504 47  GLU A O   
352  C CB  . GLU A 54  ? 2.2074 1.8132 2.3739 -0.8181 -0.3985 -0.5345 47  GLU A CB  
353  C CG  . GLU A 54  ? 2.4072 1.9774 2.5560 -0.7952 -0.4426 -0.5734 47  GLU A CG  
354  C CD  . GLU A 54  ? 2.6997 2.3496 2.9194 -0.8336 -0.4685 -0.6176 47  GLU A CD  
355  O OE1 . GLU A 54  ? 2.6136 2.3502 2.9112 -0.8877 -0.4507 -0.6228 47  GLU A OE1 
356  O OE2 . GLU A 54  ? 2.6379 2.2659 2.8360 -0.8106 -0.5071 -0.6508 47  GLU A OE2 
357  N N   . ARG A 55  ? 2.2364 1.7491 2.3186 -0.8691 -0.3146 -0.4349 48  ARG A N   
358  C CA  . ARG A 55  ? 2.2061 1.7611 2.2876 -0.8922 -0.2710 -0.4036 48  ARG A CA  
359  C C   . ARG A 55  ? 2.2715 1.7476 2.2730 -0.8398 -0.2701 -0.3629 48  ARG A C   
360  O O   . ARG A 55  ? 2.1796 1.7305 2.1970 -0.8057 -0.2509 -0.3513 48  ARG A O   
361  C CB  . ARG A 55  ? 2.2886 1.8138 2.3629 -0.9923 -0.2398 -0.3940 48  ARG A CB  
362  C CG  . ARG A 55  ? 2.3081 1.9582 2.4900 -1.0467 -0.2303 -0.4385 48  ARG A CG  
363  C CD  . ARG A 55  ? 2.3918 2.0888 2.5959 -1.1363 -0.1757 -0.4314 48  ARG A CD  
364  N NE  . ARG A 55  ? 2.5736 2.1608 2.7311 -1.2255 -0.1705 -0.4235 48  ARG A NE  
365  C CZ  . ARG A 55  ? 2.6075 2.2732 2.9495 -1.1926 -0.1919 -0.4264 48  ARG A CZ  
366  N NH1 . ARG A 55  ? 2.6259 2.2056 3.0196 -1.1835 -0.2073 -0.3969 48  ARG A NH1 
367  N NH2 . ARG A 55  ? 2.2085 2.0419 2.5762 -1.2993 -0.1527 -0.5075 48  ARG A NH2 
368  N N   . VAL A 56  ? 2.3318 1.6570 2.2528 -0.8301 -0.2956 -0.3454 49  VAL A N   
369  C CA  . VAL A 56  ? 2.3442 1.5828 2.1943 -0.7766 -0.3067 -0.3126 49  VAL A CA  
370  C C   . VAL A 56  ? 2.2770 1.5968 2.1632 -0.6926 -0.3173 -0.3301 49  VAL A C   
371  O O   . VAL A 56  ? 2.2385 1.5864 2.1139 -0.6558 -0.3059 -0.3090 49  VAL A O   
372  C CB  . VAL A 56  ? 2.5348 1.6000 2.3107 -0.7778 -0.3423 -0.3043 49  VAL A CB  
373  C CG1 . VAL A 56  ? 2.5297 1.5264 2.2622 -0.6990 -0.3683 -0.2911 49  VAL A CG1 
374  C CG2 . VAL A 56  ? 2.6774 1.6373 2.3892 -0.8607 -0.3303 -0.2705 49  VAL A CG2 
375  N N   . TYR A 57  ? 2.1872 1.5448 2.1121 -0.6694 -0.3381 -0.3692 50  TYR A N   
376  C CA  . TYR A 57  ? 2.0813 1.5084 2.0308 -0.6018 -0.3482 -0.3891 50  TYR A CA  
377  C C   . TYR A 57  ? 2.0073 1.5713 2.0134 -0.5929 -0.3259 -0.3877 50  TYR A C   
378  O O   . TYR A 57  ? 1.9174 1.5167 1.9207 -0.5403 -0.3230 -0.3803 50  TYR A O   
379  C CB  . TYR A 57  ? 2.1221 1.5389 2.0811 -0.5932 -0.3770 -0.4316 50  TYR A CB  
380  C CG  . TYR A 57  ? 2.0631 1.5637 2.0436 -0.5410 -0.3846 -0.4538 50  TYR A CG  
381  C CD1 . TYR A 57  ? 2.0654 1.5480 2.0147 -0.4804 -0.3857 -0.4519 50  TYR A CD1 
382  C CD2 . TYR A 57  ? 2.0258 1.6263 2.0580 -0.5537 -0.3908 -0.4755 50  TYR A CD2 
383  C CE1 . TYR A 57  ? 2.0249 1.5787 1.9818 -0.4409 -0.3879 -0.4675 50  TYR A CE1 
384  C CE2 . TYR A 57  ? 1.9795 1.6440 2.0163 -0.5082 -0.4008 -0.4888 50  TYR A CE2 
385  C CZ  . TYR A 57  ? 2.0999 1.7364 2.0926 -0.4554 -0.3971 -0.4831 50  TYR A CZ  
386  O OH  . TYR A 57  ? 2.1237 1.8138 2.1084 -0.4192 -0.4040 -0.4934 50  TYR A OH  
387  N N   . ARG A 58  ? 1.9535 1.5952 2.0160 -0.6434 -0.3115 -0.3986 51  ARG A N   
388  C CA  . ARG A 58  ? 1.8547 1.6258 1.9817 -0.6332 -0.2949 -0.4046 51  ARG A CA  
389  C C   . ARG A 58  ? 1.8641 1.6461 1.9737 -0.6323 -0.2615 -0.3720 51  ARG A C   
390  O O   . ARG A 58  ? 1.7524 1.6067 1.8874 -0.5937 -0.2543 -0.3705 51  ARG A O   
391  C CB  . ARG A 58  ? 1.8710 1.7308 2.0782 -0.6835 -0.2926 -0.4353 51  ARG A CB  
392  C CG  . ARG A 58  ? 1.9543 1.9477 2.2387 -0.6559 -0.2913 -0.4531 51  ARG A CG  
393  C CD  . ARG A 58  ? 2.1188 2.1745 2.4589 -0.6448 -0.3303 -0.4923 51  ARG A CD  
394  N NE  . ARG A 58  ? 2.2304 2.2174 2.5109 -0.6051 -0.3662 -0.4975 51  ARG A NE  
395  C CZ  . ARG A 58  ? 2.3375 2.3213 2.5822 -0.5451 -0.3786 -0.4890 51  ARG A CZ  
396  N NH1 . ARG A 58  ? 1.9946 2.0312 2.2561 -0.5152 -0.3626 -0.4722 51  ARG A NH1 
397  N NH2 . ARG A 58  ? 2.2355 2.1618 2.4246 -0.5178 -0.4048 -0.4995 51  ARG A NH2 
398  N N   . ALA A 59  ? 1.9160 1.6169 1.9737 -0.6770 -0.2440 -0.3455 52  ALA A N   
399  C CA  . ALA A 59  ? 1.9157 1.6054 1.9348 -0.6832 -0.2152 -0.3123 52  ALA A CA  
400  C C   . ALA A 59  ? 1.9171 1.5776 1.8998 -0.6122 -0.2311 -0.2961 52  ALA A C   
401  O O   . ALA A 59  ? 1.8735 1.5849 1.8612 -0.5917 -0.2133 -0.2848 52  ALA A O   
402  C CB  . ALA A 59  ? 2.0533 1.6300 1.9990 -0.7430 -0.2052 -0.2837 52  ALA A CB  
403  N N   . GLN A 60  ? 1.8806 1.4673 1.8341 -0.5751 -0.2634 -0.3010 53  GLN A N   
404  C CA  . GLN A 60  ? 1.8339 1.3996 1.7649 -0.5088 -0.2789 -0.2951 53  GLN A CA  
405  C C   . GLN A 60  ? 1.7657 1.4393 1.7473 -0.4698 -0.2746 -0.3125 53  GLN A C   
406  O O   . GLN A 60  ? 1.7055 1.4095 1.6848 -0.4400 -0.2648 -0.2989 53  GLN A O   
407  C CB  . GLN A 60  ? 1.9086 1.3854 1.8118 -0.4855 -0.3101 -0.3099 53  GLN A CB  
408  C CG  . GLN A 60  ? 2.0856 1.5485 1.9773 -0.4192 -0.3239 -0.3145 53  GLN A CG  
409  C CD  . GLN A 60  ? 2.2913 1.8305 2.2170 -0.3853 -0.3251 -0.3443 53  GLN A CD  
410  O OE1 . GLN A 60  ? 2.1495 1.7560 2.0918 -0.3576 -0.3132 -0.3395 53  GLN A OE1 
411  N NE2 . GLN A 60  ? 2.2797 1.8017 2.2072 -0.3889 -0.3409 -0.3751 53  GLN A NE2 
412  N N   . VAL A 61  ? 1.7114 1.4337 1.7327 -0.4721 -0.2862 -0.3422 54  VAL A N   
413  C CA  . VAL A 61  ? 1.6201 1.4280 1.6796 -0.4396 -0.2925 -0.3600 54  VAL A CA  
414  C C   . VAL A 61  ? 1.6119 1.5017 1.7101 -0.4404 -0.2713 -0.3510 54  VAL A C   
415  O O   . VAL A 61  ? 1.5693 1.4903 1.6678 -0.4010 -0.2714 -0.3462 54  VAL A O   
416  C CB  . VAL A 61  ? 1.6675 1.4997 1.7549 -0.4534 -0.3158 -0.3927 54  VAL A CB  
417  C CG1 . VAL A 61  ? 1.5986 1.5178 1.7239 -0.4279 -0.3275 -0.4070 54  VAL A CG1 
418  C CG2 . VAL A 61  ? 1.7144 1.4680 1.7560 -0.4380 -0.3371 -0.4078 54  VAL A CG2 
419  N N   . ASN A 62  ? 1.5895 1.5097 1.7168 -0.4870 -0.2505 -0.3501 55  ASN A N   
420  C CA  . ASN A 62  ? 1.5464 1.5476 1.7152 -0.4921 -0.2252 -0.3491 55  ASN A CA  
421  C C   . ASN A 62  ? 1.5853 1.5588 1.7093 -0.4724 -0.2080 -0.3210 55  ASN A C   
422  O O   . ASN A 62  ? 1.5185 1.5465 1.6648 -0.4427 -0.2021 -0.3224 55  ASN A O   
423  C CB  . ASN A 62  ? 1.6351 1.6734 1.8413 -0.5545 -0.2000 -0.3595 55  ASN A CB  
424  C CG  . ASN A 62  ? 1.9409 2.0909 2.2413 -0.5568 -0.2058 -0.3961 55  ASN A CG  
425  O OD1 . ASN A 62  ? 1.6524 1.8153 1.9848 -0.5631 -0.2335 -0.4196 55  ASN A OD1 
426  N ND2 . ASN A 62  ? 1.8923 2.1233 2.2385 -0.5450 -0.1852 -0.4041 55  ASN A ND2 
427  N N   . CYS A 63  ? 1.6198 1.5027 1.6790 -0.4884 -0.2046 -0.2960 56  CYS A N   
428  C CA  . CYS A 63  ? 1.6288 1.4730 1.6376 -0.4706 -0.1967 -0.2687 56  CYS A CA  
429  C C   . CYS A 63  ? 1.6300 1.4790 1.6378 -0.4112 -0.2144 -0.2691 56  CYS A C   
430  O O   . CYS A 63  ? 1.6081 1.4865 1.6150 -0.3914 -0.2044 -0.2607 56  CYS A O   
431  C CB  . CYS A 63  ? 1.7353 1.4687 1.6718 -0.4965 -0.2023 -0.2427 56  CYS A CB  
432  S SG  . CYS A 63  ? 1.8775 1.5960 1.7932 -0.5804 -0.1707 -0.2336 56  CYS A SG  
433  N N   . SER A 64  ? 1.5820 1.4058 1.5896 -0.3868 -0.2378 -0.2821 57  SER A N   
434  C CA  . SER A 64  ? 1.5376 1.3707 1.5439 -0.3380 -0.2496 -0.2876 57  SER A CA  
435  C C   . SER A 64  ? 1.5270 1.4403 1.5698 -0.3217 -0.2432 -0.2950 57  SER A C   
436  O O   . SER A 64  ? 1.4967 1.4214 1.5323 -0.2949 -0.2388 -0.2860 57  SER A O   
437  C CB  . SER A 64  ? 1.6133 1.4150 1.6124 -0.3258 -0.2694 -0.3079 57  SER A CB  
438  O OG  . SER A 64  ? 1.8633 1.5804 1.8278 -0.3278 -0.2796 -0.3023 57  SER A OG  
439  N N   . GLU A 65  ? 1.4647 1.4315 1.5498 -0.3388 -0.2455 -0.3124 58  GLU A N   
440  C CA  . GLU A 65  ? 1.4043 1.4420 1.5303 -0.3222 -0.2482 -0.3229 58  GLU A CA  
441  C C   . GLU A 65  ? 1.4145 1.4858 1.5543 -0.3208 -0.2264 -0.3136 58  GLU A C   
442  O O   . GLU A 65  ? 1.3855 1.4819 1.5334 -0.2923 -0.2300 -0.3132 58  GLU A O   
443  C CB  . GLU A 65  ? 1.4323 1.5212 1.6116 -0.3441 -0.2583 -0.3470 58  GLU A CB  
444  C CG  . GLU A 65  ? 1.7047 1.7802 1.8767 -0.3360 -0.2893 -0.3632 58  GLU A CG  
445  C CD  . GLU A 65  ? 2.0312 2.1737 2.2658 -0.3443 -0.3102 -0.3896 58  GLU A CD  
446  O OE1 . GLU A 65  ? 1.7369 1.9454 2.0312 -0.3513 -0.2985 -0.3985 58  GLU A OE1 
447  O OE2 . GLU A 65  ? 1.9831 2.1147 2.2088 -0.3422 -0.3399 -0.4051 58  GLU A OE2 
448  N N   . TYR A 66  ? 1.4046 1.4727 1.5420 -0.3552 -0.2035 -0.3075 59  TYR A N   
449  C CA  . TYR A 66  ? 1.3967 1.4981 1.5414 -0.3625 -0.1777 -0.3038 59  TYR A CA  
450  C C   . TYR A 66  ? 1.4480 1.5021 1.5380 -0.3458 -0.1733 -0.2796 59  TYR A C   
451  O O   . TYR A 66  ? 1.4606 1.5420 1.5521 -0.3439 -0.1563 -0.2791 59  TYR A O   
452  C CB  . TYR A 66  ? 1.4673 1.5872 1.6245 -0.4157 -0.1507 -0.3100 59  TYR A CB  
453  C CG  . TYR A 66  ? 1.4814 1.6968 1.7239 -0.4260 -0.1440 -0.3444 59  TYR A CG  
454  C CD1 . TYR A 66  ? 1.5068 1.7468 1.7948 -0.4262 -0.1689 -0.3647 59  TYR A CD1 
455  C CD2 . TYR A 66  ? 1.4839 1.7687 1.7661 -0.4311 -0.1163 -0.3616 59  TYR A CD2 
456  C CE1 . TYR A 66  ? 1.5190 1.8531 1.8964 -0.4290 -0.1714 -0.4002 59  TYR A CE1 
457  C CE2 . TYR A 66  ? 1.4755 1.8574 1.8517 -0.4325 -0.1140 -0.4004 59  TYR A CE2 
458  C CZ  . TYR A 66  ? 1.5922 2.0000 2.0192 -0.4305 -0.1439 -0.4191 59  TYR A CZ  
459  O OH  . TYR A 66  ? 1.6085 2.1182 2.1382 -0.4299 -0.1471 -0.4611 59  TYR A OH  
460  N N   . PHE A 67  ? 1.3966 1.3848 1.4439 -0.3315 -0.1902 -0.2645 60  PHE A N   
461  C CA  . PHE A 67  ? 1.3979 1.3443 1.4029 -0.3130 -0.1935 -0.2454 60  PHE A CA  
462  C C   . PHE A 67  ? 1.4473 1.4322 1.4681 -0.2819 -0.1924 -0.2484 60  PHE A C   
463  O O   . PHE A 67  ? 1.4699 1.4552 1.4722 -0.2840 -0.1822 -0.2397 60  PHE A O   
464  C CB  . PHE A 67  ? 1.4471 1.3290 1.4241 -0.2976 -0.2149 -0.2392 60  PHE A CB  
465  C CG  . PHE A 67  ? 1.4979 1.3332 1.4370 -0.2827 -0.2241 -0.2214 60  PHE A CG  
466  C CD1 . PHE A 67  ? 1.6101 1.4024 1.5033 -0.3081 -0.2209 -0.2013 60  PHE A CD1 
467  C CD2 . PHE A 67  ? 1.5036 1.3373 1.4506 -0.2456 -0.2375 -0.2262 60  PHE A CD2 
468  C CE1 . PHE A 67  ? 1.6621 1.4065 1.5167 -0.2913 -0.2391 -0.1848 60  PHE A CE1 
469  C CE2 . PHE A 67  ? 1.5795 1.3780 1.5036 -0.2290 -0.2521 -0.2145 60  PHE A CE2 
470  C CZ  . PHE A 67  ? 1.6204 1.3723 1.4978 -0.2493 -0.2569 -0.1931 60  PHE A CZ  
471  N N   . PRO A 68  ? 1.3593 1.3713 1.4061 -0.2574 -0.2030 -0.2600 61  PRO A N   
472  C CA  . PRO A 68  ? 1.3083 1.3444 1.3630 -0.2340 -0.2024 -0.2603 61  PRO A CA  
473  C C   . PRO A 68  ? 1.3138 1.3936 1.3943 -0.2390 -0.1890 -0.2690 61  PRO A C   
474  O O   . PRO A 68  ? 1.2984 1.3827 1.3734 -0.2260 -0.1855 -0.2668 61  PRO A O   
475  C CB  . PRO A 68  ? 1.3162 1.3593 1.3801 -0.2172 -0.2176 -0.2688 61  PRO A CB  
476  C CG  . PRO A 68  ? 1.3988 1.4128 1.4493 -0.2247 -0.2252 -0.2719 61  PRO A CG  
477  C CD  . PRO A 68  ? 1.3725 1.3843 1.4309 -0.2525 -0.2179 -0.2720 61  PRO A CD  
478  N N   . LEU A 69  ? 1.2356 1.3511 1.3492 -0.2585 -0.1808 -0.2837 62  LEU A N   
479  C CA  . LEU A 69  ? 1.2076 1.3755 1.3567 -0.2645 -0.1633 -0.3013 62  LEU A CA  
480  C C   . LEU A 69  ? 1.3121 1.4605 1.4184 -0.2853 -0.1398 -0.2899 62  LEU A C   
481  O O   . LEU A 69  ? 1.3288 1.4926 1.4335 -0.2750 -0.1304 -0.2960 62  LEU A O   
482  C CB  . LEU A 69  ? 1.2069 1.4256 1.4095 -0.2860 -0.1576 -0.3240 62  LEU A CB  
483  C CG  . LEU A 69  ? 1.2203 1.4905 1.4873 -0.2604 -0.1789 -0.3489 62  LEU A CG  
484  C CD1 . LEU A 69  ? 1.2190 1.4508 1.4634 -0.2332 -0.2132 -0.3372 62  LEU A CD1 
485  C CD2 . LEU A 69  ? 1.2194 1.5463 1.5468 -0.2844 -0.1749 -0.3744 62  LEU A CD2 
486  N N   . PHE A 70  ? 1.2963 1.3988 1.3582 -0.3130 -0.1353 -0.2720 63  PHE A N   
487  C CA  . PHE A 70  ? 1.3425 1.4068 1.3434 -0.3336 -0.1219 -0.2548 63  PHE A CA  
488  C C   . PHE A 70  ? 1.4150 1.4546 1.3895 -0.3025 -0.1375 -0.2438 63  PHE A C   
489  O O   . PHE A 70  ? 1.4301 1.4808 1.3865 -0.3053 -0.1248 -0.2474 63  PHE A O   
490  C CB  . PHE A 70  ? 1.4230 1.4204 1.3736 -0.3617 -0.1277 -0.2330 63  PHE A CB  
491  C CG  . PHE A 70  ? 1.4979 1.4264 1.3701 -0.3686 -0.1352 -0.2066 63  PHE A CG  
492  C CD1 . PHE A 70  ? 1.5609 1.4898 1.3871 -0.3965 -0.1116 -0.2029 63  PHE A CD1 
493  C CD2 . PHE A 70  ? 1.5376 1.4020 1.3817 -0.3457 -0.1680 -0.1888 63  PHE A CD2 
494  C CE1 . PHE A 70  ? 1.6345 1.4908 1.3767 -0.4035 -0.1261 -0.1764 63  PHE A CE1 
495  C CE2 . PHE A 70  ? 1.6206 1.4198 1.3961 -0.3469 -0.1848 -0.1657 63  PHE A CE2 
496  C CZ  . PHE A 70  ? 1.6432 1.4337 1.3625 -0.3770 -0.1664 -0.1569 63  PHE A CZ  
497  N N   . LEU A 71  ? 1.3752 1.3879 1.3515 -0.2753 -0.1625 -0.2354 64  LEU A N   
498  C CA  . LEU A 71  ? 1.3604 1.3593 1.3244 -0.2496 -0.1766 -0.2291 64  LEU A CA  
499  C C   . LEU A 71  ? 1.3779 1.4166 1.3664 -0.2362 -0.1690 -0.2432 64  LEU A C   
500  O O   . LEU A 71  ? 1.4172 1.4491 1.3818 -0.2350 -0.1679 -0.2412 64  LEU A O   
501  C CB  . LEU A 71  ? 1.3467 1.3294 1.3237 -0.2267 -0.1959 -0.2272 64  LEU A CB  
502  C CG  . LEU A 71  ? 1.4660 1.3992 1.4198 -0.2282 -0.2109 -0.2170 64  LEU A CG  
503  C CD1 . LEU A 71  ? 1.4609 1.3955 1.4388 -0.2069 -0.2211 -0.2267 64  LEU A CD1 
504  C CD2 . LEU A 71  ? 1.5204 1.4151 1.4374 -0.2239 -0.2260 -0.2031 64  LEU A CD2 
505  N N   . ALA A 72  ? 1.2626 1.3357 1.2948 -0.2252 -0.1685 -0.2581 65  ALA A N   
506  C CA  . ALA A 72  ? 1.2328 1.3314 1.2887 -0.2089 -0.1674 -0.2724 65  ALA A CA  
507  C C   . ALA A 72  ? 1.3286 1.4486 1.3787 -0.2209 -0.1466 -0.2860 65  ALA A C   
508  O O   . ALA A 72  ? 1.3178 1.4274 1.3486 -0.2141 -0.1472 -0.2873 65  ALA A O   
509  C CB  . ALA A 72  ? 1.2203 1.3443 1.3189 -0.1963 -0.1768 -0.2856 65  ALA A CB  
510  N N   . THR A 73  ? 1.3350 1.4844 1.3973 -0.2438 -0.1258 -0.2977 66  THR A N   
511  C CA  . THR A 73  ? 1.3655 1.5444 1.4210 -0.2623 -0.0967 -0.3165 66  THR A CA  
512  C C   . THR A 73  ? 1.4583 1.5940 1.4373 -0.2798 -0.0911 -0.2990 66  THR A C   
513  O O   . THR A 73  ? 1.4848 1.6293 1.4489 -0.2766 -0.0813 -0.3135 66  THR A O   
514  C CB  . THR A 73  ? 1.4890 1.7146 1.5776 -0.2907 -0.0714 -0.3342 66  THR A CB  
515  O OG1 . THR A 73  ? 1.5591 1.7487 1.6187 -0.3147 -0.0763 -0.3100 66  THR A OG1 
516  C CG2 . THR A 73  ? 1.4227 1.7051 1.5965 -0.2681 -0.0801 -0.3625 66  THR A CG2 
517  N N   . LEU A 74  ? 1.4160 1.5001 1.3454 -0.2947 -0.1030 -0.2696 67  LEU A N   
518  C CA  . LEU A 74  ? 1.4585 1.4893 1.3093 -0.3082 -0.1104 -0.2487 67  LEU A CA  
519  C C   . LEU A 74  ? 1.5240 1.5468 1.3695 -0.2810 -0.1304 -0.2507 67  LEU A C   
520  O O   . LEU A 74  ? 1.5740 1.5818 1.3685 -0.2905 -0.1278 -0.2518 67  LEU A O   
521  C CB  . LEU A 74  ? 1.4751 1.4471 1.2935 -0.3134 -0.1339 -0.2196 67  LEU A CB  
522  C CG  . LEU A 74  ? 1.5866 1.4917 1.3281 -0.3173 -0.1580 -0.1949 67  LEU A CG  
523  C CD1 . LEU A 74  ? 1.6760 1.5503 1.3363 -0.3613 -0.1371 -0.1849 67  LEU A CD1 
524  C CD2 . LEU A 74  ? 1.5965 1.4516 1.3369 -0.3017 -0.1915 -0.1756 67  LEU A CD2 
525  N N   . TRP A 75  ? 1.4284 1.4596 1.3220 -0.2517 -0.1494 -0.2520 68  TRP A N   
526  C CA  . TRP A 75  ? 1.4058 1.4318 1.3043 -0.2312 -0.1673 -0.2544 68  TRP A CA  
527  C C   . TRP A 75  ? 1.4477 1.5015 1.3662 -0.2239 -0.1549 -0.2794 68  TRP A C   
528  O O   . TRP A 75  ? 1.4819 1.5244 1.3747 -0.2228 -0.1617 -0.2847 68  TRP A O   
529  C CB  . TRP A 75  ? 1.3517 1.3743 1.2863 -0.2117 -0.1858 -0.2468 68  TRP A CB  
530  C CG  . TRP A 75  ? 1.3895 1.3791 1.3020 -0.2108 -0.2055 -0.2288 68  TRP A CG  
531  C CD1 . TRP A 75  ? 1.4339 1.4045 1.3438 -0.2149 -0.2088 -0.2185 68  TRP A CD1 
532  C CD2 . TRP A 75  ? 1.4167 1.3856 1.3085 -0.2033 -0.2296 -0.2226 68  TRP A CD2 
533  N NE1 . TRP A 75  ? 1.4634 1.3975 1.3518 -0.2071 -0.2341 -0.2064 68  TRP A NE1 
534  C CE2 . TRP A 75  ? 1.4928 1.4297 1.3742 -0.1982 -0.2488 -0.2092 68  TRP A CE2 
535  C CE3 . TRP A 75  ? 1.4412 1.4156 1.3267 -0.1990 -0.2406 -0.2301 68  TRP A CE3 
536  C CZ2 . TRP A 75  ? 1.5214 1.4347 1.3910 -0.1847 -0.2816 -0.2036 68  TRP A CZ2 
537  C CZ3 . TRP A 75  ? 1.4921 1.4478 1.3651 -0.1900 -0.2717 -0.2242 68  TRP A CZ3 
538  C CH2 . TRP A 75  ? 1.5239 1.4513 1.3923 -0.1806 -0.2934 -0.2115 68  TRP A CH2 
539  N N   . VAL A 76  ? 1.3532 1.4412 1.3181 -0.2176 -0.1407 -0.2977 69  VAL A N   
540  C CA  . VAL A 76  ? 1.3375 1.4470 1.3284 -0.2042 -0.1335 -0.3260 69  VAL A CA  
541  C C   . VAL A 76  ? 1.4136 1.5383 1.3720 -0.2223 -0.1077 -0.3460 69  VAL A C   
542  O O   . VAL A 76  ? 1.4285 1.5456 1.3714 -0.2161 -0.1088 -0.3620 69  VAL A O   
543  C CB  . VAL A 76  ? 1.3610 1.4981 1.4147 -0.1846 -0.1361 -0.3421 69  VAL A CB  
544  C CG1 . VAL A 76  ? 1.3692 1.5180 1.4501 -0.1650 -0.1348 -0.3741 69  VAL A CG1 
545  C CG2 . VAL A 76  ? 1.3280 1.4407 1.3936 -0.1714 -0.1609 -0.3207 69  VAL A CG2 
546  N N   . ALA A 77  ? 1.4014 1.5437 1.3426 -0.2492 -0.0831 -0.3458 70  ALA A N   
547  C CA  . ALA A 77  ? 1.4578 1.6133 1.3527 -0.2765 -0.0510 -0.3637 70  ALA A CA  
548  C C   . ALA A 77  ? 1.5575 1.6595 1.3643 -0.2890 -0.0652 -0.3440 70  ALA A C   
549  O O   . ALA A 77  ? 1.5716 1.6765 1.3419 -0.2962 -0.0515 -0.3654 70  ALA A O   
550  C CB  . ALA A 77  ? 1.4913 1.6694 1.3795 -0.3120 -0.0211 -0.3617 70  ALA A CB  
551  N N   . GLY A 78  ? 1.5390 1.5948 1.3172 -0.2879 -0.0959 -0.3078 71  GLY A N   
552  C CA  . GLY A 78  ? 1.5963 1.6010 1.3004 -0.2940 -0.1215 -0.2880 71  GLY A CA  
553  C C   . GLY A 78  ? 1.6447 1.6473 1.3574 -0.2727 -0.1425 -0.3020 71  GLY A C   
554  O O   . GLY A 78  ? 1.6928 1.6658 1.3409 -0.2814 -0.1575 -0.2997 71  GLY A O   
555  N N   . ILE A 79  ? 1.5330 1.5611 1.3202 -0.2474 -0.1464 -0.3161 72  ILE A N   
556  C CA  . ILE A 79  ? 1.5087 1.5308 1.3111 -0.2315 -0.1652 -0.3295 72  ILE A CA  
557  C C   . ILE A 79  ? 1.5724 1.6134 1.3853 -0.2270 -0.1440 -0.3680 72  ILE A C   
558  O O   . ILE A 79  ? 1.6127 1.6376 1.3972 -0.2278 -0.1541 -0.3826 72  ILE A O   
559  C CB  . ILE A 79  ? 1.4795 1.5017 1.3403 -0.2127 -0.1855 -0.3167 72  ILE A CB  
560  C CG1 . ILE A 79  ? 1.4818 1.4852 1.3261 -0.2145 -0.2114 -0.2906 72  ILE A CG1 
561  C CG2 . ILE A 79  ? 1.4868 1.5041 1.3737 -0.2018 -0.1959 -0.3341 72  ILE A CG2 
562  C CD1 . ILE A 79  ? 1.6084 1.6183 1.4994 -0.2029 -0.2210 -0.2789 72  ILE A CD1 
563  N N   . PHE A 80  ? 1.5142 1.5904 1.3670 -0.2224 -0.1167 -0.3884 73  PHE A N   
564  C CA  . PHE A 80  ? 1.5306 1.6291 1.4076 -0.2108 -0.0986 -0.4319 73  PHE A CA  
565  C C   . PHE A 80  ? 1.6646 1.7904 1.4980 -0.2344 -0.0595 -0.4594 73  PHE A C   
566  O O   . PHE A 80  ? 1.7269 1.8663 1.5648 -0.2264 -0.0449 -0.5007 73  PHE A O   
567  C CB  . PHE A 80  ? 1.5093 1.6306 1.4690 -0.1831 -0.1012 -0.4449 73  PHE A CB  
568  C CG  . PHE A 80  ? 1.5143 1.5962 1.4947 -0.1656 -0.1364 -0.4237 73  PHE A CG  
569  C CD1 . PHE A 80  ? 1.5208 1.5913 1.5041 -0.1697 -0.1515 -0.3866 73  PHE A CD1 
570  C CD2 . PHE A 80  ? 1.5818 1.6339 1.5713 -0.1499 -0.1522 -0.4423 73  PHE A CD2 
571  C CE1 . PHE A 80  ? 1.5433 1.5820 1.5385 -0.1615 -0.1761 -0.3695 73  PHE A CE1 
572  C CE2 . PHE A 80  ? 1.5817 1.5934 1.5804 -0.1442 -0.1797 -0.4209 73  PHE A CE2 
573  C CZ  . PHE A 80  ? 1.5421 1.5515 1.5432 -0.1517 -0.1888 -0.3850 73  PHE A CZ  
574  N N   . PHE A 81  ? 1.6401 1.7653 1.4210 -0.2664 -0.0433 -0.4372 74  PHE A N   
575  C CA  . PHE A 81  ? 1.7058 1.8447 1.4180 -0.3029 -0.0033 -0.4537 74  PHE A CA  
576  C C   . PHE A 81  ? 1.8744 1.9509 1.4831 -0.3306 -0.0249 -0.4085 74  PHE A C   
577  O O   . PHE A 81  ? 1.8657 1.9109 1.4876 -0.3173 -0.0624 -0.3725 74  PHE A O   
578  C CB  . PHE A 81  ? 1.6938 1.8902 1.4514 -0.3202 0.0375  -0.4672 74  PHE A CB  
579  C CG  . PHE A 81  ? 1.7736 2.0058 1.4846 -0.3573 0.0915  -0.5014 74  PHE A CG  
580  C CD1 . PHE A 81  ? 1.8666 2.0635 1.4683 -0.4082 0.1098  -0.4744 74  PHE A CD1 
581  C CD2 . PHE A 81  ? 1.8014 2.0973 1.5713 -0.3423 0.1238  -0.5626 74  PHE A CD2 
582  C CE1 . PHE A 81  ? 1.9816 2.2072 1.5235 -0.4502 0.1649  -0.5063 74  PHE A CE1 
583  C CE2 . PHE A 81  ? 1.8800 2.2163 1.6053 -0.3795 0.1808  -0.6011 74  PHE A CE2 
584  C CZ  . PHE A 81  ? 1.9481 2.2501 1.5557 -0.4368 0.2039  -0.5718 74  PHE A CZ  
585  N N   . HIS A 82  ? 1.9284 1.9834 1.4333 -0.3674 -0.0047 -0.4103 75  HIS A N   
586  C CA  . HIS A 82  ? 2.0005 1.9831 1.4006 -0.3894 -0.0360 -0.3652 75  HIS A CA  
587  C C   . HIS A 82  ? 1.9498 1.9046 1.3702 -0.3885 -0.0600 -0.3189 75  HIS A C   
588  O O   . HIS A 82  ? 1.9085 1.8923 1.3697 -0.4012 -0.0318 -0.3179 75  HIS A O   
589  C CB  . HIS A 82  ? 2.1629 2.1204 1.4353 -0.4380 -0.0047 -0.3695 75  HIS A CB  
590  C CG  . HIS A 82  ? 2.2864 2.2552 1.5237 -0.4352 0.0061  -0.4125 75  HIS A CG  
591  N ND1 . HIS A 82  ? 2.3812 2.3967 1.5973 -0.4609 0.0673  -0.4593 75  HIS A ND1 
592  C CD2 . HIS A 82  ? 2.3272 2.2715 1.5570 -0.4095 -0.0356 -0.4206 75  HIS A CD2 
593  C CE1 . HIS A 82  ? 2.4139 2.4231 1.6006 -0.4485 0.0590  -0.4929 75  HIS A CE1 
594  N NE2 . HIS A 82  ? 2.3849 2.3502 1.5786 -0.4189 -0.0034 -0.4703 75  HIS A NE2 
595  N N   . GLU A 83  ? 1.8563 1.7619 1.2620 -0.3688 -0.1143 -0.2881 76  GLU A N   
596  C CA  . GLU A 83  ? 1.8149 1.6835 1.2331 -0.3590 -0.1490 -0.2494 76  GLU A CA  
597  C C   . GLU A 83  ? 1.9915 1.8037 1.3184 -0.3983 -0.1423 -0.2174 76  GLU A C   
598  O O   . GLU A 83  ? 1.9935 1.7923 1.3509 -0.3973 -0.1482 -0.1966 76  GLU A O   
599  C CB  . GLU A 83  ? 1.8222 1.6580 1.2370 -0.3308 -0.2073 -0.2363 76  GLU A CB  
600  C CG  . GLU A 83  ? 1.8955 1.6965 1.3305 -0.3125 -0.2489 -0.2048 76  GLU A CG  
601  C CD  . GLU A 83  ? 2.2944 2.0415 1.6802 -0.2993 -0.3089 -0.1856 76  GLU A CD  
602  O OE1 . GLU A 83  ? 2.4862 2.2040 1.7896 -0.3123 -0.3244 -0.1875 76  GLU A OE1 
603  O OE2 . GLU A 83  ? 2.2496 1.9844 1.6804 -0.2744 -0.3429 -0.1713 76  GLU A OE2 
604  N N   . GLY A 84  ? 2.0576 1.8286 1.2661 -0.4343 -0.1325 -0.2127 77  GLY A N   
605  C CA  . GLY A 84  ? 2.1711 1.8726 1.2684 -0.4811 -0.1251 -0.1793 77  GLY A CA  
606  C C   . GLY A 84  ? 2.2143 1.9619 1.3406 -0.5183 -0.0618 -0.1925 77  GLY A C   
607  O O   . GLY A 84  ? 2.2423 1.9497 1.3483 -0.5424 -0.0610 -0.1640 77  GLY A O   
608  N N   . ALA A 85  ? 2.1329 1.9681 1.3174 -0.5204 -0.0112 -0.2401 78  ALA A N   
609  C CA  . ALA A 85  ? 2.1145 2.0212 1.3565 -0.5491 0.0503  -0.2672 78  ALA A CA  
610  C C   . ALA A 85  ? 2.0540 1.9880 1.4099 -0.5229 0.0359  -0.2596 78  ALA A C   
611  O O   . ALA A 85  ? 2.0909 2.0214 1.4465 -0.5576 0.0572  -0.2475 78  ALA A O   
612  C CB  . ALA A 85  ? 2.0881 2.0846 1.3917 -0.5368 0.0912  -0.3259 78  ALA A CB  
613  N N   . ALA A 86  ? 1.8817 1.8351 1.3246 -0.4662 -0.0017 -0.2649 79  ALA A N   
614  C CA  . ALA A 86  ? 1.7740 1.7457 1.3122 -0.4382 -0.0208 -0.2574 79  ALA A CA  
615  C C   . ALA A 86  ? 1.8981 1.7904 1.3836 -0.4511 -0.0516 -0.2126 79  ALA A C   
616  O O   . ALA A 86  ? 1.8899 1.7904 1.4147 -0.4628 -0.0426 -0.2075 79  ALA A O   
617  C CB  . ALA A 86  ? 1.6809 1.6726 1.2921 -0.3839 -0.0542 -0.2675 79  ALA A CB  
618  N N   . ALA A 87  ? 1.9389 1.7511 1.3340 -0.4493 -0.0908 -0.1826 80  ALA A N   
619  C CA  . ALA A 87  ? 2.0044 1.7263 1.3417 -0.4558 -0.1292 -0.1409 80  ALA A CA  
620  C C   . ALA A 87  ? 2.1610 1.8408 1.4227 -0.5170 -0.0972 -0.1230 80  ALA A C   
621  O O   . ALA A 87  ? 2.1865 1.8165 1.4463 -0.5243 -0.1140 -0.0997 80  ALA A O   
622  C CB  . ALA A 87  ? 2.0826 1.7327 1.3404 -0.4388 -0.1819 -0.1184 80  ALA A CB  
623  N N   . LEU A 88  ? 2.1736 1.8767 1.3770 -0.5636 -0.0473 -0.1381 81  LEU A N   
624  C CA  . LEU A 88  ? 2.2715 1.9472 1.4025 -0.6336 -0.0041 -0.1264 81  LEU A CA  
625  C C   . LEU A 88  ? 2.2319 1.9819 1.4736 -0.6456 0.0317  -0.1487 81  LEU A C   
626  O O   . LEU A 88  ? 2.2821 1.9766 1.4964 -0.6779 0.0283  -0.1229 81  LEU A O   
627  C CB  . LEU A 88  ? 2.3671 2.0622 1.4118 -0.6809 0.0466  -0.1450 81  LEU A CB  
628  C CG  . LEU A 88  ? 2.6214 2.1970 1.4785 -0.7347 0.0383  -0.1036 81  LEU A CG  
629  C CD1 . LEU A 88  ? 2.7193 2.1803 1.5091 -0.7616 0.0062  -0.0514 81  LEU A CD1 
630  C CD2 . LEU A 88  ? 2.6837 2.2095 1.4669 -0.7009 -0.0115 -0.0937 81  LEU A CD2 
631  N N   . CYS A 89  ? 2.0596 1.9274 1.4262 -0.6173 0.0588  -0.1961 82  CYS A N   
632  C CA  . CYS A 89  ? 1.9822 1.9264 1.4630 -0.6217 0.0830  -0.2208 82  CYS A CA  
633  C C   . CYS A 89  ? 1.9815 1.8822 1.5039 -0.5885 0.0337  -0.1964 82  CYS A C   
634  O O   . CYS A 89  ? 1.9763 1.8892 1.5411 -0.6104 0.0435  -0.1981 82  CYS A O   
635  C CB  . CYS A 89  ? 1.8808 1.9460 1.4816 -0.5888 0.1077  -0.2746 82  CYS A CB  
636  S SG  . CYS A 89  ? 1.9803 2.0970 1.5432 -0.6046 0.1554  -0.3136 82  CYS A SG  
637  N N   . GLY A 90  ? 1.8986 1.7560 1.4138 -0.5372 -0.0165 -0.1793 83  GLY A N   
638  C CA  . GLY A 90  ? 1.8560 1.6708 1.4033 -0.5018 -0.0629 -0.1602 83  GLY A CA  
639  C C   . GLY A 90  ? 2.0184 1.7322 1.4853 -0.5374 -0.0787 -0.1238 83  GLY A C   
640  O O   . GLY A 90  ? 2.0063 1.7051 1.5138 -0.5335 -0.0921 -0.1203 83  GLY A O   
641  N N   . LEU A 91  ? 2.0834 1.7199 1.4267 -0.5761 -0.0775 -0.0968 84  LEU A N   
642  C CA  . LEU A 91  ? 2.2027 1.7214 1.4455 -0.6179 -0.0941 -0.0569 84  LEU A CA  
643  C C   . LEU A 91  ? 2.2697 1.8127 1.5207 -0.6844 -0.0421 -0.0651 84  LEU A C   
644  O O   . LEU A 91  ? 2.3160 1.7933 1.5539 -0.7043 -0.0573 -0.0462 84  LEU A O   
645  C CB  . LEU A 91  ? 2.3402 1.7628 1.4360 -0.6414 -0.1117 -0.0239 84  LEU A CB  
646  C CG  . LEU A 91  ? 2.3999 1.7566 1.4667 -0.5840 -0.1820 -0.0040 84  LEU A CG  
647  C CD1 . LEU A 91  ? 2.5055 1.8170 1.4540 -0.6006 -0.1901 0.0110  84  LEU A CD1 
648  C CD2 . LEU A 91  ? 2.4890 1.7279 1.5170 -0.5737 -0.2367 0.0302  84  LEU A CD2 
649  N N   . VAL A 92  ? 2.1812 1.8223 1.4608 -0.7180 0.0190  -0.0981 85  VAL A N   
650  C CA  . VAL A 92  ? 2.1850 1.8842 1.4977 -0.7818 0.0771  -0.1191 85  VAL A CA  
651  C C   . VAL A 92  ? 2.1183 1.8701 1.5576 -0.7576 0.0649  -0.1390 85  VAL A C   
652  O O   . VAL A 92  ? 2.1729 1.8866 1.6025 -0.8032 0.0713  -0.1282 85  VAL A O   
653  C CB  . VAL A 92  ? 2.1981 2.0153 1.5461 -0.8016 0.1395  -0.1638 85  VAL A CB  
654  C CG1 . VAL A 92  ? 2.1634 2.0868 1.6079 -0.8456 0.1948  -0.2039 85  VAL A CG1 
655  C CG2 . VAL A 92  ? 2.3385 2.0945 1.5380 -0.8498 0.1634  -0.1445 85  VAL A CG2 
656  N N   . TYR A 93  ? 1.9224 1.7518 1.4699 -0.6885 0.0445  -0.1664 86  TYR A N   
657  C CA  . TYR A 93  ? 1.8138 1.6928 1.4727 -0.6582 0.0272  -0.1864 86  TYR A CA  
658  C C   . TYR A 93  ? 1.9074 1.6800 1.5274 -0.6550 -0.0161 -0.1541 86  TYR A C   
659  O O   . TYR A 93  ? 1.9391 1.7081 1.5847 -0.6893 -0.0088 -0.1587 86  TYR A O   
660  C CB  . TYR A 93  ? 1.6905 1.6422 1.4374 -0.5864 0.0072  -0.2116 86  TYR A CB  
661  C CG  . TYR A 93  ? 1.6365 1.6113 1.4674 -0.5513 -0.0216 -0.2231 86  TYR A CG  
662  C CD1 . TYR A 93  ? 1.6417 1.5445 1.4520 -0.5149 -0.0671 -0.2006 86  TYR A CD1 
663  C CD2 . TYR A 93  ? 1.6077 1.6784 1.5389 -0.5538 -0.0050 -0.2599 86  TYR A CD2 
664  C CE1 . TYR A 93  ? 1.5966 1.5176 1.4717 -0.4869 -0.0901 -0.2133 86  TYR A CE1 
665  C CE2 . TYR A 93  ? 1.5664 1.6502 1.5602 -0.5250 -0.0353 -0.2692 86  TYR A CE2 
666  C CZ  . TYR A 93  ? 1.6172 1.6238 1.5765 -0.4937 -0.0753 -0.2453 86  TYR A CZ  
667  O OH  . TYR A 93  ? 1.5409 1.5559 1.5484 -0.4689 -0.1020 -0.2563 86  TYR A OH  
668  N N   . LEU A 94  ? 1.8707 1.5581 1.4327 -0.6148 -0.0619 -0.1255 87  LEU A N   
669  C CA  . LEU A 94  ? 1.9122 1.4939 1.4389 -0.6025 -0.1076 -0.0995 87  LEU A CA  
670  C C   . LEU A 94  ? 2.1342 1.6215 1.5779 -0.6708 -0.0993 -0.0733 87  LEU A C   
671  O O   . LEU A 94  ? 2.1684 1.6173 1.6340 -0.6773 -0.1157 -0.0734 87  LEU A O   
672  C CB  . LEU A 94  ? 1.9195 1.4325 1.3978 -0.5520 -0.1557 -0.0774 87  LEU A CB  
673  C CG  . LEU A 94  ? 1.8327 1.4180 1.3937 -0.4853 -0.1723 -0.1003 87  LEU A CG  
674  C CD1 . LEU A 94  ? 1.8546 1.3800 1.3717 -0.4442 -0.2169 -0.0818 87  LEU A CD1 
675  C CD2 . LEU A 94  ? 1.7646 1.3864 1.4122 -0.4595 -0.1810 -0.1220 87  LEU A CD2 
676  N N   . PHE A 95  ? 2.1960 1.6430 1.5395 -0.7264 -0.0718 -0.0523 88  PHE A N   
677  C CA  . PHE A 95  ? 2.3411 1.6892 1.5886 -0.8040 -0.0583 -0.0235 88  PHE A CA  
678  C C   . PHE A 95  ? 2.3299 1.7544 1.6556 -0.8566 -0.0131 -0.0527 88  PHE A C   
679  O O   . PHE A 95  ? 2.3805 1.7280 1.6853 -0.8898 -0.0264 -0.0389 88  PHE A O   
680  C CB  . PHE A 95  ? 2.5044 1.7926 1.6147 -0.8568 -0.0355 0.0053  88  PHE A CB  
681  C CG  . PHE A 95  ? 2.7178 1.8902 1.7137 -0.9447 -0.0207 0.0399  88  PHE A CG  
682  C CD1 . PHE A 95  ? 2.8496 1.8777 1.7911 -0.9432 -0.0742 0.0739  88  PHE A CD1 
683  C CD2 . PHE A 95  ? 2.8345 2.0393 1.7762 -1.0315 0.0485  0.0359  88  PHE A CD2 
684  C CE1 . PHE A 95  ? 3.0334 1.9408 1.8624 -1.0289 -0.0624 0.1083  88  PHE A CE1 
685  C CE2 . PHE A 95  ? 2.9874 2.1087 1.8688 -1.0863 0.0655  0.0703  88  PHE A CE2 
686  C CZ  . PHE A 95  ? 3.0355 2.0166 1.8765 -1.0751 0.0106  0.1071  88  PHE A CZ  
687  N N   . ALA A 96  ? 2.1797 1.7563 1.6049 -0.8579 0.0340  -0.0969 89  ALA A N   
688  C CA  . ALA A 96  ? 2.1313 1.8105 1.6593 -0.8969 0.0730  -0.1355 89  ALA A CA  
689  C C   . ALA A 96  ? 2.1334 1.8073 1.7399 -0.8585 0.0305  -0.1460 89  ALA A C   
690  O O   . ALA A 96  ? 2.1625 1.8501 1.8083 -0.9047 0.0435  -0.1598 89  ALA A O   
691  C CB  . ALA A 96  ? 2.0249 1.8650 1.6563 -0.8782 0.1131  -0.1843 89  ALA A CB  
692  N N   . ARG A 97  ? 2.0140 1.6685 1.6404 -0.7781 -0.0187 -0.1419 90  ARG A N   
693  C CA  . ARG A 97  ? 1.9542 1.5988 1.6414 -0.7382 -0.0584 -0.1534 90  ARG A CA  
694  C C   . ARG A 97  ? 2.1218 1.6259 1.7364 -0.7636 -0.0893 -0.1248 90  ARG A C   
695  O O   . ARG A 97  ? 2.1138 1.6191 1.7773 -0.7708 -0.1010 -0.1423 90  ARG A O   
696  C CB  . ARG A 97  ? 1.8398 1.5110 1.5659 -0.6529 -0.0928 -0.1605 90  ARG A CB  
697  C CG  . ARG A 97  ? 1.7962 1.6060 1.6270 -0.6241 -0.0746 -0.1992 90  ARG A CG  
698  C CD  . ARG A 97  ? 1.7500 1.6136 1.6662 -0.6260 -0.0816 -0.2292 90  ARG A CD  
699  N NE  . ARG A 97  ? 1.7062 1.6996 1.7174 -0.6131 -0.0621 -0.2662 90  ARG A NE  
700  C CZ  . ARG A 97  ? 1.7226 1.7835 1.8188 -0.6017 -0.0744 -0.2971 90  ARG A CZ  
701  N NH1 . ARG A 97  ? 1.5157 1.5300 1.6116 -0.6047 -0.1022 -0.2973 90  ARG A NH1 
702  N NH2 . ARG A 97  ? 1.6285 1.8003 1.8091 -0.5848 -0.0631 -0.3302 90  ARG A NH2 
703  N N   . LEU A 98  ? 2.1889 1.5661 1.6835 -0.7778 -0.1061 -0.0822 91  LEU A N   
704  C CA  . LEU A 98  ? 2.3131 1.5359 1.7257 -0.8022 -0.1407 -0.0517 91  LEU A CA  
705  C C   . LEU A 98  ? 2.4437 1.6646 1.8513 -0.8928 -0.1019 -0.0559 91  LEU A C   
706  O O   . LEU A 98  ? 2.4970 1.6699 1.9246 -0.9062 -0.1215 -0.0632 91  LEU A O   
707  C CB  . LEU A 98  ? 2.4431 1.5330 1.7204 -0.8055 -0.1666 -0.0037 91  LEU A CB  
708  C CG  . LEU A 98  ? 2.5779 1.5208 1.8007 -0.7587 -0.2367 0.0208  91  LEU A CG  
709  C CD1 . LEU A 98  ? 2.7366 1.5422 1.8143 -0.7762 -0.2632 0.0709  91  LEU A CD1 
710  C CD2 . LEU A 98  ? 2.6485 1.5127 1.8792 -0.7823 -0.2554 0.0160  91  LEU A CD2 
711  N N   . ARG A 99  ? 2.3975 1.6827 1.7881 -0.9562 -0.0435 -0.0580 92  ARG A N   
712  C CA  . ARG A 99  ? 2.4495 1.7624 1.8494 -1.0514 0.0064  -0.0693 92  ARG A CA  
713  C C   . ARG A 99  ? 2.3575 1.7955 1.9071 -1.0411 0.0124  -0.1209 92  ARG A C   
714  O O   . ARG A 99  ? 2.4141 1.8153 1.9724 -1.0938 0.0128  -0.1258 92  ARG A O   
715  C CB  . ARG A 99  ? 2.4606 1.8459 1.8300 -1.1106 0.0732  -0.0729 92  ARG A CB  
716  C CG  . ARG A 99  ? 2.7639 2.0116 1.9604 -1.1505 0.0746  -0.0197 92  ARG A CG  
717  C CD  . ARG A 99  ? 2.9035 2.2639 2.1542 -1.0802 0.1009  -0.0249 92  ARG A CD  
718  N NE  . ARG A 99  ? 2.9043 2.4823 2.4028 -0.9909 0.1482  -0.0514 92  ARG A NE  
719  C CZ  . ARG A 99  ? 2.9877 2.6899 2.6064 -0.8810 0.1576  -0.0559 92  ARG A CZ  
720  N NH1 . ARG A 99  ? 2.9688 2.5917 2.3883 -0.9472 0.1558  -0.0627 92  ARG A NH1 
721  N NH2 . ARG A 99  ? 2.8616 2.6773 2.5306 -0.9343 0.2119  -0.0931 92  ARG A NH2 
722  N N   . TYR A 100 ? 2.1417 1.7145 1.8015 -0.9723 0.0100  -0.1575 93  TYR A N   
723  C CA  . TYR A 100 ? 2.0175 1.7059 1.8130 -0.9495 0.0040  -0.2051 93  TYR A CA  
724  C C   . TYR A 100 ? 2.1039 1.6989 1.8915 -0.9364 -0.0445 -0.2006 93  TYR A C   
725  O O   . TYR A 100 ? 2.1064 1.7318 1.9509 -0.9773 -0.0403 -0.2258 93  TYR A O   
726  C CB  . TYR A 100 ? 1.8695 1.6634 1.7448 -0.8631 -0.0100 -0.2298 93  TYR A CB  
727  C CG  . TYR A 100 ? 1.7702 1.6480 1.7587 -0.8277 -0.0344 -0.2698 93  TYR A CG  
728  C CD1 . TYR A 100 ? 1.7442 1.7587 1.8425 -0.8512 -0.0083 -0.3139 93  TYR A CD1 
729  C CD2 . TYR A 100 ? 1.7347 1.5550 1.7185 -0.7714 -0.0850 -0.2662 93  TYR A CD2 
730  C CE1 . TYR A 100 ? 1.6924 1.7755 1.8853 -0.8192 -0.0389 -0.3490 93  TYR A CE1 
731  C CE2 . TYR A 100 ? 1.6725 1.5595 1.7418 -0.7444 -0.1088 -0.3013 93  TYR A CE2 
732  C CZ  . TYR A 100 ? 1.7169 1.7306 1.8868 -0.7688 -0.0891 -0.3405 93  TYR A CZ  
733  O OH  . TYR A 100 ? 1.6079 1.6860 1.8581 -0.7432 -0.1193 -0.3751 93  TYR A OH  
734  N N   . PHE A 101 ? 2.0855 1.5764 1.8123 -0.8754 -0.0915 -0.1746 94  PHE A N   
735  C CA  . PHE A 101 ? 2.1237 1.5197 1.8387 -0.8494 -0.1400 -0.1743 94  PHE A CA  
736  C C   . PHE A 101 ? 2.3549 1.6326 2.0026 -0.9280 -0.1390 -0.1553 94  PHE A C   
737  O O   . PHE A 101 ? 2.3706 1.6531 2.0651 -0.9538 -0.1469 -0.1805 94  PHE A O   
738  C CB  . PHE A 101 ? 2.1390 1.4529 1.8018 -0.7735 -0.1830 -0.1523 94  PHE A CB  
739  C CG  . PHE A 101 ? 2.1763 1.4181 1.8462 -0.7320 -0.2299 -0.1648 94  PHE A CG  
740  C CD1 . PHE A 101 ? 2.0933 1.4179 1.8427 -0.6751 -0.2436 -0.2006 94  PHE A CD1 
741  C CD2 . PHE A 101 ? 2.3673 1.4520 1.9582 -0.7504 -0.2609 -0.1422 94  PHE A CD2 
742  C CE1 . PHE A 101 ? 2.1545 1.4169 1.9064 -0.6400 -0.2812 -0.2181 94  PHE A CE1 
743  C CE2 . PHE A 101 ? 2.4010 1.4217 2.0037 -0.7104 -0.3024 -0.1619 94  PHE A CE2 
744  C CZ  . PHE A 101 ? 2.2694 1.3842 1.9530 -0.6556 -0.3095 -0.2015 94  PHE A CZ  
745  N N   . GLN A 102 ? 2.4420 1.6136 1.9756 -0.9719 -0.1285 -0.1112 95  GLN A N   
746  C CA  . GLN A 102 ? 2.6176 1.6509 2.0591 -1.0552 -0.1268 -0.0825 95  GLN A CA  
747  C C   . GLN A 102 ? 2.6807 1.7933 2.1820 -1.1482 -0.0782 -0.1101 95  GLN A C   
748  O O   . GLN A 102 ? 2.7842 1.8009 2.2546 -1.2042 -0.0891 -0.1049 95  GLN A O   
749  C CB  . GLN A 102 ? 2.7626 1.6820 2.0625 -1.0848 -0.1214 -0.0286 95  GLN A CB  
750  C CG  . GLN A 102 ? 2.8126 1.6018 2.0380 -1.0070 -0.1865 0.0026  95  GLN A CG  
751  C CD  . GLN A 102 ? 3.0873 1.7737 2.1746 -1.0258 -0.1903 0.0540  95  GLN A CD  
752  O OE1 . GLN A 102 ? 3.0823 1.6322 2.0906 -0.9803 -0.2489 0.0850  95  GLN A OE1 
753  N NE2 . GLN A 102 ? 3.0134 1.7652 2.0692 -1.0891 -0.1308 0.0610  95  GLN A NE2 
754  N N   . GLY A 103 ? 2.5358 1.8219 2.1271 -1.1611 -0.0280 -0.1422 96  GLY A N   
755  C CA  . GLY A 103 ? 2.5326 1.9355 2.2110 -1.2389 0.0211  -0.1797 96  GLY A CA  
756  C C   . GLY A 103 ? 2.5231 1.9949 2.3193 -1.2145 -0.0081 -0.2258 96  GLY A C   
757  O O   . GLY A 103 ? 2.5964 2.0561 2.4162 -1.2852 -0.0001 -0.2412 96  GLY A O   
758  N N   . TYR A 104 ? 2.3524 1.8885 2.2144 -1.1173 -0.0440 -0.2470 97  TYR A N   
759  C CA  . TYR A 104 ? 2.2767 1.8689 2.2329 -1.0794 -0.0808 -0.2884 97  TYR A CA  
760  C C   . TYR A 104 ? 2.4448 1.8784 2.3354 -1.0890 -0.1245 -0.2753 97  TYR A C   
761  O O   . TYR A 104 ? 2.4524 1.9031 2.3976 -1.1192 -0.1378 -0.3071 97  TYR A O   
762  C CB  . TYR A 104 ? 2.1467 1.8043 2.1450 -0.9746 -0.1092 -0.3002 97  TYR A CB  
763  C CG  . TYR A 104 ? 2.0549 1.8468 2.1743 -0.9410 -0.1255 -0.3500 97  TYR A CG  
764  C CD1 . TYR A 104 ? 2.1094 1.9293 2.2890 -0.9842 -0.1368 -0.3838 97  TYR A CD1 
765  C CD2 . TYR A 104 ? 1.9445 1.8221 2.1095 -0.8651 -0.1367 -0.3620 97  TYR A CD2 
766  C CE1 . TYR A 104 ? 2.0247 1.9605 2.3075 -0.9504 -0.1611 -0.4285 97  TYR A CE1 
767  C CE2 . TYR A 104 ? 1.8683 1.8519 2.1291 -0.8325 -0.1599 -0.4031 97  TYR A CE2 
768  C CZ  . TYR A 104 ? 1.9340 1.9479 2.2529 -0.8737 -0.1738 -0.4363 97  TYR A CZ  
769  O OH  . TYR A 104 ? 1.8272 1.9410 2.2335 -0.8382 -0.2045 -0.4757 97  TYR A OH  
770  N N   . ALA A 105 ? 2.4955 1.7738 2.2710 -1.0628 -0.1497 -0.2313 98  ALA A N   
771  C CA  . ALA A 105 ? 2.6259 1.7329 2.3274 -1.0635 -0.1946 -0.2161 98  ALA A CA  
772  C C   . ALA A 105 ? 2.8662 1.8945 2.5308 -1.1725 -0.1771 -0.2085 98  ALA A C   
773  O O   . ALA A 105 ? 2.9341 1.8462 2.5885 -1.1601 -0.2106 -0.2049 98  ALA A O   
774  C CB  . ALA A 105 ? 2.6943 1.6671 2.2890 -1.0145 -0.2229 -0.1713 98  ALA A CB  
775  N N   . ARG A 106 ? 2.8116 1.9559 2.5498 -1.2201 -0.1202 -0.2109 99  ARG A N   
776  C CA  . ARG A 106 ? 2.7911 1.9795 2.6778 -1.2190 -0.0980 -0.2053 99  ARG A CA  
777  C C   . ARG A 106 ? 2.7335 2.0961 2.7804 -1.2190 -0.0939 -0.2565 99  ARG A C   
778  O O   . ARG A 106 ? 2.7451 2.0961 2.8103 -1.2167 -0.1309 -0.2930 99  ARG A O   
779  C CB  . ARG A 106 ? 2.7881 2.0018 2.7099 -1.2061 -0.0530 -0.1569 99  ARG A CB  
780  C CG  . ARG A 106 ? 2.9054 2.0490 2.9317 -1.1030 -0.0609 -0.1099 99  ARG A CG  
781  C CD  . ARG A 106 ? 2.9911 2.1585 3.0500 -1.0164 -0.0340 -0.0583 99  ARG A CD  
782  N NE  . ARG A 106 ? 3.0131 2.2805 3.2717 -0.9500 0.0005  -0.0183 99  ARG A NE  
783  C CZ  . ARG A 106 ? 3.0986 2.4700 3.4673 -0.8514 0.0278  0.0246  99  ARG A CZ  
784  N NH1 . ARG A 106 ? 3.0830 2.4160 3.2660 -0.8953 0.0344  0.0227  99  ARG A NH1 
785  N NH2 . ARG A 106 ? 3.0257 2.3568 3.3342 -0.9579 0.0657  0.0579  99  ARG A NH2 
786  N N   . SER A 107 ? 2.6233 2.1293 2.7344 -1.2524 -0.0491 -0.2674 100 SER A N   
787  C CA  . SER A 107 ? 2.5247 2.1923 2.7683 -1.2638 -0.0500 -0.3202 100 SER A CA  
788  C C   . SER A 107 ? 2.4645 2.2661 2.7089 -1.2544 -0.0280 -0.3602 100 SER A C   
789  O O   . SER A 107 ? 2.4794 2.2672 2.6362 -1.2528 0.0015  -0.3421 100 SER A O   
790  C CB  . SER A 107 ? 2.5000 2.2504 2.9230 -1.2444 -0.0446 -0.2934 100 SER A CB  
791  O OG  . SER A 107 ? 2.5379 2.3146 3.0010 -1.2040 -0.0119 -0.2368 100 SER A OG  
792  N N   . ALA A 108 ? 2.3401 2.2753 2.6604 -1.2793 -0.0309 -0.4322 101 ALA A N   
793  C CA  . ALA A 108 ? 2.1881 2.2686 2.5799 -1.2190 -0.0264 -0.4653 101 ALA A CA  
794  C C   . ALA A 108 ? 2.1930 2.4108 2.6783 -1.2311 0.0237  -0.4703 101 ALA A C   
795  O O   . ALA A 108 ? 2.1054 2.4632 2.6598 -1.2042 0.0391  -0.5172 101 ALA A O   
796  C CB  . ALA A 108 ? 2.1045 2.2671 2.5984 -1.1671 -0.0797 -0.5111 101 ALA A CB  
797  N N   . GLN A 109 ? 2.1986 2.3729 2.6939 -1.2588 0.0456  -0.4194 102 GLN A N   
798  C CA  . GLN A 109 ? 2.1435 2.4167 2.7217 -1.2469 0.0840  -0.3979 102 GLN A CA  
799  C C   . GLN A 109 ? 2.2283 2.4163 2.6864 -1.2380 0.1195  -0.3485 102 GLN A C   
800  O O   . GLN A 109 ? 2.1722 2.4488 2.6380 -1.2269 0.1578  -0.3632 102 GLN A O   
801  C CB  . GLN A 109 ? 2.1534 2.4322 2.8524 -1.2418 0.0656  -0.3490 102 GLN A CB  
802  C CG  . GLN A 109 ? 2.1957 2.5549 3.0166 -1.1636 0.0689  -0.2796 102 GLN A CG  
803  C CD  . GLN A 109 ? 2.3293 2.5969 3.1302 -1.1160 0.0831  -0.1873 102 GLN A CD  
804  O OE1 . GLN A 109 ? 2.3497 2.4934 3.0502 -1.1600 0.0965  -0.1784 102 GLN A OE1 
805  N NE2 . GLN A 109 ? 2.1882 2.5637 3.0001 -1.1736 0.1562  -0.2054 102 GLN A NE2 
806  N N   . LEU A 110 ? 2.3016 2.3204 2.6239 -1.2763 0.1182  -0.3093 103 LEU A N   
807  C CA  . LEU A 110 ? 2.3668 2.2782 2.5494 -1.2817 0.1437  -0.2610 103 LEU A CA  
808  C C   . LEU A 110 ? 2.4082 2.3097 2.4826 -1.2630 0.1442  -0.2788 103 LEU A C   
809  O O   . LEU A 110 ? 2.4629 2.2807 2.4186 -1.2628 0.1582  -0.2396 103 LEU A O   
810  C CB  . LEU A 110 ? 2.4699 2.1975 2.5723 -1.2850 0.1164  -0.2044 103 LEU A CB  
811  C CG  . LEU A 110 ? 2.5006 2.2222 2.7417 -1.2567 0.1105  -0.1572 103 LEU A CG  
812  C CD1 . LEU A 110 ? 2.5952 2.1439 2.7636 -1.2473 0.0855  -0.1154 103 LEU A CD1 
813  C CD2 . LEU A 110 ? 2.4686 2.2680 2.7731 -1.2435 0.1568  -0.1186 103 LEU A CD2 
814  N N   . ARG A 111 ? 2.3107 2.3022 2.4154 -1.2643 0.1342  -0.3447 104 ARG A N   
815  C CA  . ARG A 111 ? 2.1955 2.1989 2.2955 -1.1602 0.1036  -0.3359 104 ARG A CA  
816  C C   . ARG A 111 ? 2.1459 2.3138 2.3356 -1.1374 0.1433  -0.3730 104 ARG A C   
817  O O   . ARG A 111 ? 2.0932 2.2501 2.2423 -1.0798 0.1381  -0.3559 104 ARG A O   
818  C CB  . ARG A 111 ? 2.0957 2.0798 2.2367 -1.0786 0.0350  -0.3456 104 ARG A CB  
819  C CG  . ARG A 111 ? 1.9816 2.1201 2.2590 -1.0158 0.0179  -0.3946 104 ARG A CG  
820  C CD  . ARG A 111 ? 2.0812 2.2476 2.4349 -1.0237 -0.0175 -0.4281 104 ARG A CD  
821  N NE  . ARG A 111 ? 2.0237 2.3188 2.4940 -0.9618 -0.0462 -0.4712 104 ARG A NE  
822  C CZ  . ARG A 111 ? 2.1280 2.5789 2.7230 -0.9756 -0.0251 -0.5187 104 ARG A CZ  
823  N NH1 . ARG A 111 ? 1.8784 2.4238 2.5667 -0.9125 -0.0640 -0.5533 104 ARG A NH1 
824  N NH2 . ARG A 111 ? 2.0348 2.5472 2.6602 -1.0521 0.0347  -0.5331 104 ARG A NH2 
825  N N   . LEU A 112 ? 2.0900 2.4085 2.4044 -1.1820 0.1810  -0.4265 105 LEU A N   
826  C CA  . LEU A 112 ? 2.0082 2.4962 2.4317 -1.1610 0.2177  -0.4746 105 LEU A CA  
827  C C   . LEU A 112 ? 2.0905 2.5616 2.4385 -1.1577 0.2607  -0.4466 105 LEU A C   
828  O O   . LEU A 112 ? 2.0145 2.5487 2.3867 -1.1010 0.2607  -0.4689 105 LEU A O   
829  C CB  . LEU A 112 ? 1.9693 2.5702 2.5538 -1.1619 0.2196  -0.4866 105 LEU A CB  
830  C CG  . LEU A 112 ? 1.9577 2.6130 2.6635 -1.1236 0.1584  -0.5112 105 LEU A CG  
831  C CD1 . LEU A 112 ? 1.9570 2.6247 2.7647 -1.1260 0.1367  -0.4673 105 LEU A CD1 
832  C CD2 . LEU A 112 ? 1.8769 2.6730 2.6912 -1.0579 0.1406  -0.5712 105 LEU A CD2 
833  N N   . ALA A 113 ? 2.1376 2.5142 2.4116 -1.1894 0.2823  -0.3838 106 ALA A N   
834  C CA  . ALA A 113 ? 2.1709 2.5170 2.3639 -1.1829 0.3190  -0.3487 106 ALA A CA  
835  C C   . ALA A 113 ? 2.2603 2.5092 2.2984 -1.1768 0.3062  -0.3400 106 ALA A C   
836  O O   . ALA A 113 ? 2.2220 2.5447 2.2639 -1.1532 0.3284  -0.3710 106 ALA A O   
837  C CB  . ALA A 113 ? 2.2468 2.5006 2.4181 -1.1838 0.3238  -0.2685 106 ALA A CB  
838  N N   . PRO A 114 ? 2.2723 2.3634 2.1857 -1.1893 0.2636  -0.3020 107 PRO A N   
839  C CA  . PRO A 114 ? 2.2232 2.2296 2.0607 -1.1078 0.2175  -0.2662 107 PRO A CA  
840  C C   . PRO A 114 ? 2.0997 2.1975 2.0525 -1.0081 0.1782  -0.2975 107 PRO A C   
841  O O   . PRO A 114 ? 2.0590 2.1260 1.9727 -0.9447 0.1537  -0.2802 107 PRO A O   
842  C CB  . PRO A 114 ? 2.3400 2.1645 2.0647 -1.1148 0.1687  -0.2126 107 PRO A CB  
843  C CG  . PRO A 114 ? 2.4317 2.2622 2.2118 -1.1663 0.1692  -0.2296 107 PRO A CG  
844  C CD  . PRO A 114 ? 2.3814 2.3573 2.2484 -1.2369 0.2381  -0.2756 107 PRO A CD  
845  N N   . LEU A 115 ? 1.9651 2.1721 2.0553 -0.9968 0.1702  -0.3433 108 LEU A N   
846  C CA  . LEU A 115 ? 1.8199 2.1111 2.0131 -0.9087 0.1324  -0.3731 108 LEU A CA  
847  C C   . LEU A 115 ? 1.8250 2.2381 2.0803 -0.8891 0.1697  -0.4093 108 LEU A C   
848  O O   . LEU A 115 ? 1.7429 2.1657 2.0074 -0.8153 0.1435  -0.4091 108 LEU A O   
849  C CB  . LEU A 115 ? 1.7655 2.1246 2.0737 -0.9035 0.1044  -0.4094 108 LEU A CB  
850  C CG  . LEU A 115 ? 1.6971 2.1547 2.1149 -0.8231 0.0681  -0.4452 108 LEU A CG  
851  C CD1 . LEU A 115 ? 1.6560 2.0253 2.0157 -0.7472 0.0145  -0.4133 108 LEU A CD1 
852  C CD2 . LEU A 115 ? 1.6848 2.2343 2.2226 -0.8363 0.0516  -0.4900 108 LEU A CD2 
853  N N   . TYR A 116 ? 1.8253 2.3299 2.1226 -0.9575 0.2327  -0.4428 109 TYR A N   
854  C CA  . TYR A 116 ? 1.7923 2.4173 2.1512 -0.9445 0.2756  -0.4858 109 TYR A CA  
855  C C   . TYR A 116 ? 1.8939 2.4420 2.1225 -0.9409 0.2957  -0.4517 109 TYR A C   
856  O O   . TYR A 116 ? 1.8332 2.4433 2.0951 -0.8926 0.3032  -0.4768 109 TYR A O   
857  C CB  . TYR A 116 ? 1.8531 2.6110 2.3058 -1.0184 0.3405  -0.5399 109 TYR A CB  
858  C CG  . TYR A 116 ? 1.8413 2.6963 2.4463 -1.0110 0.3144  -0.5792 109 TYR A CG  
859  C CD1 . TYR A 116 ? 1.7700 2.6502 2.4525 -0.9319 0.2484  -0.5962 109 TYR A CD1 
860  C CD2 . TYR A 116 ? 1.8594 2.7181 2.5356 -1.0090 0.3079  -0.5286 109 TYR A CD2 
861  C CE1 . TYR A 116 ? 1.7553 2.7270 2.5707 -0.9301 0.2211  -0.6387 109 TYR A CE1 
862  C CE2 . TYR A 116 ? 1.8162 2.7425 2.6254 -0.9862 0.2658  -0.5410 109 TYR A CE2 
863  C CZ  . TYR A 116 ? 1.8545 2.8018 2.7199 -0.9209 0.2025  -0.5631 109 TYR A CZ  
864  O OH  . TYR A 116 ? 1.8243 2.8237 2.8028 -0.8980 0.1531  -0.5644 109 TYR A OH  
865  N N   . ALA A 117 ? 1.9516 2.3568 2.0295 -0.9887 0.2975  -0.3947 110 ALA A N   
866  C CA  . ALA A 117 ? 2.0046 2.3168 1.9435 -0.9848 0.3030  -0.3560 110 ALA A CA  
867  C C   . ALA A 117 ? 1.9627 2.2364 1.9029 -0.8861 0.2406  -0.3396 110 ALA A C   
868  O O   . ALA A 117 ? 1.9430 2.2345 1.8622 -0.8516 0.2471  -0.3459 110 ALA A O   
869  C CB  . ALA A 117 ? 2.1591 2.3144 1.9430 -1.0495 0.3008  -0.2968 110 ALA A CB  
870  N N   . SER A 118 ? 1.8610 2.0901 1.8320 -0.8439 0.1836  -0.3243 111 SER A N   
871  C CA  . SER A 118 ? 1.7645 1.9641 1.7465 -0.7576 0.1276  -0.3122 111 SER A CA  
872  C C   . SER A 118 ? 1.7130 2.0357 1.8065 -0.7037 0.1308  -0.3588 111 SER A C   
873  O O   . SER A 118 ? 1.6681 1.9772 1.7395 -0.6532 0.1145  -0.3524 111 SER A O   
874  C CB  . SER A 118 ? 1.7721 1.9141 1.7698 -0.7360 0.0776  -0.2966 111 SER A CB  
875  O OG  . SER A 118 ? 1.7591 1.9792 1.8661 -0.6816 0.0497  -0.3280 111 SER A OG  
876  N N   . ALA A 119 ? 1.6327 2.0735 1.8463 -0.7162 0.1502  -0.4074 112 ALA A N   
877  C CA  . ALA A 119 ? 1.5462 2.1016 1.8737 -0.6637 0.1476  -0.4558 112 ALA A CA  
878  C C   . ALA A 119 ? 1.6259 2.2144 1.9287 -0.6592 0.1862  -0.4726 112 ALA A C   
879  O O   . ALA A 119 ? 1.5671 2.1629 1.8879 -0.5964 0.1619  -0.4800 112 ALA A O   
880  C CB  . ALA A 119 ? 1.5339 2.2102 1.9927 -0.6863 0.1627  -0.5076 112 ALA A CB  
881  N N   . ARG A 120 ? 1.6650 2.2639 1.9152 -0.7303 0.2467  -0.4773 113 ARG A N   
882  C CA  . ARG A 120 ? 1.6912 2.3167 1.8986 -0.7414 0.2926  -0.4953 113 ARG A CA  
883  C C   . ARG A 120 ? 1.7347 2.2618 1.8434 -0.6952 0.2576  -0.4563 113 ARG A C   
884  O O   . ARG A 120 ? 1.7039 2.2727 1.8411 -0.6515 0.2591  -0.4838 113 ARG A O   
885  C CB  . ARG A 120 ? 1.8038 2.4172 1.9272 -0.8375 0.3584  -0.4895 113 ARG A CB  
886  C CG  . ARG A 120 ? 1.9627 2.7217 2.2031 -0.8854 0.4178  -0.5530 113 ARG A CG  
887  C CD  . ARG A 120 ? 2.1796 2.8474 2.3591 -0.8888 0.4274  -0.4615 113 ARG A CD  
888  N NE  . ARG A 120 ? 2.1888 2.9152 2.5111 -0.8375 0.4171  -0.4286 113 ARG A NE  
889  C CZ  . ARG A 120 ? 2.2369 2.9409 2.6222 -0.8323 0.3824  -0.3878 113 ARG A CZ  
890  N NH1 . ARG A 120 ? 2.0541 2.8745 2.5520 -0.8655 0.4168  -0.4218 113 ARG A NH1 
891  N NH2 . ARG A 120 ? 2.0835 2.7760 2.3699 -0.9824 0.4189  -0.4629 113 ARG A NH2 
892  N N   . ALA A 121 ? 1.7192 2.1176 1.7212 -0.7014 0.2222  -0.3964 114 ALA A N   
893  C CA  . ALA A 121 ? 1.7124 2.0164 1.6257 -0.6594 0.1829  -0.3583 114 ALA A CA  
894  C C   . ALA A 121 ? 1.6597 1.9872 1.6508 -0.5782 0.1358  -0.3691 114 ALA A C   
895  O O   . ALA A 121 ? 1.6347 1.9401 1.5947 -0.5414 0.1210  -0.3651 114 ALA A O   
896  C CB  . ALA A 121 ? 1.7876 1.9614 1.5946 -0.6811 0.1519  -0.3004 114 ALA A CB  
897  N N   . LEU A 122 ? 1.5705 1.9406 1.6577 -0.5550 0.1125  -0.3837 115 LEU A N   
898  C CA  . LEU A 122 ? 1.4803 1.8674 1.6337 -0.4861 0.0685  -0.3923 115 LEU A CA  
899  C C   . LEU A 122 ? 1.5062 1.9813 1.7368 -0.4536 0.0824  -0.4399 115 LEU A C   
900  O O   . LEU A 122 ? 1.4828 1.9373 1.7089 -0.4057 0.0570  -0.4376 115 LEU A O   
901  C CB  . LEU A 122 ? 1.4379 1.8337 1.6523 -0.4771 0.0377  -0.3922 115 LEU A CB  
902  C CG  . LEU A 122 ? 1.4351 1.7799 1.6454 -0.4223 -0.0152 -0.3705 115 LEU A CG  
903  C CD1 . LEU A 122 ? 1.4642 1.7140 1.5760 -0.4129 -0.0299 -0.3295 115 LEU A CD1 
904  C CD2 . LEU A 122 ? 1.3955 1.7346 1.6403 -0.4237 -0.0424 -0.3683 115 LEU A CD2 
905  N N   . TRP A 123 ? 1.4751 2.0462 1.7749 -0.4822 0.1245  -0.4854 116 TRP A N   
906  C CA  . TRP A 123 ? 1.4469 2.1095 1.8288 -0.4531 0.1427  -0.5407 116 TRP A CA  
907  C C   . TRP A 123 ? 1.5475 2.1827 1.8501 -0.4571 0.1702  -0.5416 116 TRP A C   
908  O O   . TRP A 123 ? 1.5256 2.1896 1.8680 -0.4119 0.1631  -0.5726 116 TRP A O   
909  C CB  . TRP A 123 ? 1.4444 2.2247 1.9223 -0.4913 0.1880  -0.5936 116 TRP A CB  
910  C CG  . TRP A 123 ? 1.4030 2.2441 1.9967 -0.4726 0.1559  -0.6150 116 TRP A CG  
911  C CD1 . TRP A 123 ? 1.4544 2.3404 2.0920 -0.5226 0.1726  -0.6245 116 TRP A CD1 
912  C CD2 . TRP A 123 ? 1.3379 2.2030 2.0178 -0.4012 0.1002  -0.6336 116 TRP A CD2 
913  N NE1 . TRP A 123 ? 1.3895 2.3305 2.1382 -0.4844 0.1280  -0.6493 116 TRP A NE1 
914  C CE2 . TRP A 123 ? 1.3617 2.2878 2.1337 -0.4090 0.0818  -0.6539 116 TRP A CE2 
915  C CE3 . TRP A 123 ? 1.3219 2.1529 2.0017 -0.3341 0.0606  -0.6326 116 TRP A CE3 
916  C CZ2 . TRP A 123 ? 1.3065 2.2579 2.1632 -0.3495 0.0219  -0.6714 116 TRP A CZ2 
917  C CZ3 . TRP A 123 ? 1.3007 2.1505 2.0606 -0.2784 0.0043  -0.6475 116 TRP A CZ3 
918  C CH2 . TRP A 123 ? 1.2934 2.2031 2.1388 -0.2848 -0.0161 -0.6668 116 TRP A CH2 
919  N N   . LEU A 124 ? 1.5754 2.1486 1.7608 -0.5122 0.1984  -0.5086 117 LEU A N   
920  C CA  . LEU A 124 ? 1.6287 2.1623 1.7153 -0.5239 0.2205  -0.5037 117 LEU A CA  
921  C C   . LEU A 124 ? 1.6438 2.1025 1.6910 -0.4693 0.1682  -0.4750 117 LEU A C   
922  O O   . LEU A 124 ? 1.6483 2.1159 1.6871 -0.4453 0.1729  -0.4981 117 LEU A O   
923  C CB  . LEU A 124 ? 1.7344 2.2019 1.6927 -0.5966 0.2512  -0.4669 117 LEU A CB  
924  C CG  . LEU A 124 ? 1.8846 2.3138 1.7237 -0.6242 0.2811  -0.4646 117 LEU A CG  
925  C CD1 . LEU A 124 ? 1.8767 2.4067 1.7761 -0.6129 0.3255  -0.5324 117 LEU A CD1 
926  C CD2 . LEU A 124 ? 2.0419 2.4195 1.7653 -0.7070 0.3188  -0.4354 117 LEU A CD2 
927  N N   . LEU A 125 ? 1.5669 1.9579 1.5978 -0.4501 0.1200  -0.4305 118 LEU A N   
928  C CA  . LEU A 125 ? 1.5206 1.8496 1.5267 -0.4022 0.0719  -0.4050 118 LEU A CA  
929  C C   . LEU A 125 ? 1.5198 1.8973 1.6198 -0.3474 0.0523  -0.4383 118 LEU A C   
930  O O   . LEU A 125 ? 1.5045 1.8568 1.5863 -0.3177 0.0361  -0.4407 118 LEU A O   
931  C CB  . LEU A 125 ? 1.4966 1.7564 1.4754 -0.3977 0.0327  -0.3589 118 LEU A CB  
932  C CG  . LEU A 125 ? 1.6186 1.7951 1.4882 -0.4352 0.0306  -0.3171 118 LEU A CG  
933  C CD1 . LEU A 125 ? 1.6003 1.7257 1.4696 -0.4311 -0.0024 -0.2854 118 LEU A CD1 
934  C CD2 . LEU A 125 ? 1.6516 1.7732 1.4435 -0.4215 0.0130  -0.3006 118 LEU A CD2 
935  N N   . VAL A 126 ? 1.4465 1.8894 1.6447 -0.3356 0.0508  -0.4651 119 VAL A N   
936  C CA  . VAL A 126 ? 1.3970 1.8789 1.6832 -0.2827 0.0255  -0.4966 119 VAL A CA  
937  C C   . VAL A 126 ? 1.4692 1.9930 1.7758 -0.2696 0.0512  -0.5425 119 VAL A C   
938  O O   . VAL A 126 ? 1.4699 1.9644 1.7796 -0.2286 0.0245  -0.5475 119 VAL A O   
939  C CB  . VAL A 126 ? 1.4119 1.9537 1.7952 -0.2738 0.0117  -0.5162 119 VAL A CB  
940  C CG1 . VAL A 126 ? 1.3938 2.0096 1.8823 -0.2323 0.0046  -0.5710 119 VAL A CG1 
941  C CG2 . VAL A 126 ? 1.3744 1.8568 1.7422 -0.2543 -0.0363 -0.4767 119 VAL A CG2 
942  N N   . ALA A 127 ? 1.4520 2.0363 1.7612 -0.3089 0.1053  -0.5752 120 ALA A N   
943  C CA  . ALA A 127 ? 1.4806 2.1125 1.8065 -0.3011 0.1387  -0.6273 120 ALA A CA  
944  C C   . ALA A 127 ? 1.5585 2.1130 1.7838 -0.2952 0.1309  -0.6080 120 ALA A C   
945  O O   . ALA A 127 ? 1.5555 2.1135 1.8073 -0.2567 0.1209  -0.6401 120 ALA A O   
946  C CB  . ALA A 127 ? 1.5416 2.2514 1.8738 -0.3571 0.2061  -0.6624 120 ALA A CB  
947  N N   . LEU A 128 ? 1.5304 2.0121 1.6437 -0.3314 0.1298  -0.5570 121 LEU A N   
948  C CA  . LEU A 128 ? 1.5504 1.9586 1.5654 -0.3304 0.1159  -0.5349 121 LEU A CA  
949  C C   . LEU A 128 ? 1.5764 1.9355 1.6129 -0.2793 0.0610  -0.5177 121 LEU A C   
950  O O   . LEU A 128 ? 1.6117 1.9438 1.6204 -0.2620 0.0513  -0.5299 121 LEU A O   
951  C CB  . LEU A 128 ? 1.5902 1.9327 1.4937 -0.3765 0.1172  -0.4836 121 LEU A CB  
952  C CG  . LEU A 128 ? 1.7196 2.0804 1.5550 -0.4369 0.1723  -0.4943 121 LEU A CG  
953  C CD1 . LEU A 128 ? 1.7785 2.0497 1.4952 -0.4751 0.1579  -0.4362 121 LEU A CD1 
954  N N   . ALA A 129 ? 1.4769 1.8249 1.5606 -0.2590 0.0274  -0.4925 122 ALA A N   
955  C CA  . ALA A 129 ? 1.4257 1.7302 1.5293 -0.2180 -0.0190 -0.4763 122 ALA A CA  
956  C C   . ALA A 129 ? 1.4539 1.7907 1.6302 -0.1790 -0.0245 -0.5222 122 ALA A C   
957  O O   . ALA A 129 ? 1.4436 1.7388 1.6057 -0.1561 -0.0460 -0.5251 122 ALA A O   
958  C CB  . ALA A 129 ? 1.3882 1.6806 1.5197 -0.2115 -0.0456 -0.4449 122 ALA A CB  
959  N N   . ALA A 130 ? 1.4089 1.8201 1.6671 -0.1719 -0.0068 -0.5615 123 ALA A N   
960  C CA  . ALA A 130 ? 1.4047 1.8541 1.7469 -0.1287 -0.0153 -0.6133 123 ALA A CA  
961  C C   . ALA A 130 ? 1.4934 1.9435 1.8094 -0.1256 0.0089  -0.6525 123 ALA A C   
962  O O   . ALA A 130 ? 1.5045 1.9148 1.8324 -0.0883 -0.0200 -0.6663 123 ALA A O   
963  C CB  . ALA A 130 ? 1.3989 1.9426 1.8388 -0.1273 0.0026  -0.6525 123 ALA A CB  
964  N N   . LEU A 131 ? 1.4752 1.9567 1.7403 -0.1688 0.0598  -0.6660 124 LEU A N   
965  C CA  . LEU A 131 ? 1.5291 2.0103 1.7506 -0.1738 0.0876  -0.7039 124 LEU A CA  
966  C C   . LEU A 131 ? 1.5978 1.9865 1.7378 -0.1669 0.0542  -0.6729 124 LEU A C   
967  O O   . LEU A 131 ? 1.6347 2.0090 1.7727 -0.1457 0.0520  -0.7095 124 LEU A O   
968  C CB  . LEU A 131 ? 1.5811 2.1062 1.7440 -0.2308 0.1496  -0.7175 124 LEU A CB  
969  C CG  . LEU A 131 ? 1.6369 2.2740 1.8874 -0.2427 0.1994  -0.7737 124 LEU A CG  
970  C CD1 . LEU A 131 ? 1.7011 2.3617 1.8691 -0.3123 0.2601  -0.7715 124 LEU A CD1 
971  C CD2 . LEU A 131 ? 1.6780 2.3717 2.0116 -0.2000 0.2114  -0.8515 124 LEU A CD2 
972  N N   . GLY A 132 ? 1.5256 1.8565 1.6088 -0.1831 0.0275  -0.6114 125 GLY A N   
973  C CA  . GLY A 132 ? 1.5325 1.7866 1.5542 -0.1786 -0.0072 -0.5810 125 GLY A CA  
974  C C   . GLY A 132 ? 1.5782 1.7948 1.6500 -0.1362 -0.0487 -0.5844 125 GLY A C   
975  O O   . GLY A 132 ? 1.6247 1.7950 1.6664 -0.1282 -0.0657 -0.5918 125 GLY A O   
976  N N   . LEU A 133 ? 1.4913 1.7221 1.6344 -0.1113 -0.0673 -0.5796 126 LEU A N   
977  C CA  . LEU A 133 ? 1.4795 1.6639 1.6609 -0.0736 -0.1096 -0.5778 126 LEU A CA  
978  C C   . LEU A 133 ? 1.5865 1.7868 1.8223 -0.0382 -0.1087 -0.6374 126 LEU A C   
979  O O   . LEU A 133 ? 1.6235 1.7625 1.8580 -0.0141 -0.1394 -0.6439 126 LEU A O   
980  C CB  . LEU A 133 ? 1.4264 1.6134 1.6498 -0.0616 -0.1340 -0.5488 126 LEU A CB  
981  C CG  . LEU A 133 ? 1.4181 1.5810 1.5952 -0.0888 -0.1408 -0.4934 126 LEU A CG  
982  C CD1 . LEU A 133 ? 1.3870 1.5753 1.6053 -0.0830 -0.1504 -0.4805 126 LEU A CD1 
983  C CD2 . LEU A 133 ? 1.4230 1.5148 1.5618 -0.0879 -0.1703 -0.4626 126 LEU A CD2 
984  N N   . LEU A 134 ? 1.5442 1.8272 1.8309 -0.0362 -0.0727 -0.6839 127 LEU A N   
985  C CA  . LEU A 134 ? 1.5823 1.9001 1.9340 -0.0007 -0.0643 -0.7532 127 LEU A CA  
986  C C   . LEU A 134 ? 1.6864 1.9588 1.9762 -0.0056 -0.0566 -0.7745 127 LEU A C   
987  O O   . LEU A 134 ? 1.7159 1.9319 2.0217 0.0290  -0.0897 -0.7930 127 LEU A O   
988  C CB  . LEU A 134 ? 1.5832 2.0121 1.9879 -0.0149 -0.0118 -0.7994 127 LEU A CB  
989  C CG  . LEU A 134 ? 1.6187 2.1132 2.1438 0.0221  -0.0258 -0.8322 127 LEU A CG  
990  C CD1 . LEU A 134 ? 1.5868 2.1650 2.1362 -0.0165 0.0110  -0.8251 127 LEU A CD1 
991  C CD2 . LEU A 134 ? 1.6916 2.2372 2.2995 0.0638  -0.0143 -0.9159 127 LEU A CD2 
992  N N   . ALA A 135 ? 1.6664 1.9483 1.8736 -0.0516 -0.0204 -0.7641 128 ALA A N   
993  C CA  . ALA A 135 ? 1.7250 1.9658 1.8556 -0.0658 -0.0130 -0.7803 128 ALA A CA  
994  C C   . ALA A 135 ? 1.8049 1.9497 1.8990 -0.0580 -0.0635 -0.7438 128 ALA A C   
995  O O   . ALA A 135 ? 1.8633 1.9663 1.9168 -0.0579 -0.0695 -0.7676 128 ALA A O   
996  C CB  . ALA A 135 ? 1.7512 2.0129 1.7906 -0.1193 0.0257  -0.7627 128 ALA A CB  
997  N N   . HIS A 136 ? 1.7156 1.8276 1.8241 -0.0547 -0.0973 -0.6900 129 HIS A N   
998  C CA  . HIS A 136 ? 1.7277 1.7571 1.8091 -0.0536 -0.1395 -0.6557 129 HIS A CA  
999  C C   . HIS A 136 ? 1.7852 1.7626 1.9159 -0.0121 -0.1734 -0.6793 129 HIS A C   
1000 O O   . HIS A 136 ? 1.8307 1.7473 1.9360 -0.0092 -0.1910 -0.6943 129 HIS A O   
1001 C CB  . HIS A 136 ? 1.6945 1.7126 1.7619 -0.0728 -0.1551 -0.5914 129 HIS A CB  
1002 C CG  . HIS A 136 ? 1.7543 1.6995 1.8005 -0.0776 -0.1909 -0.5592 129 HIS A CG  
1003 N ND1 . HIS A 136 ? 1.7952 1.6899 1.8727 -0.0545 -0.2219 -0.5504 129 HIS A ND1 
1004 C CD2 . HIS A 136 ? 1.7870 1.7044 1.7845 -0.1055 -0.1996 -0.5367 129 HIS A CD2 
1005 C CE1 . HIS A 136 ? 1.8021 1.6408 1.8455 -0.0750 -0.2416 -0.5223 129 HIS A CE1 
1006 N NE2 . HIS A 136 ? 1.7982 1.6553 1.8019 -0.1044 -0.2292 -0.5162 129 HIS A NE2 
1007 N N   . PHE A 137 ? 1.7172 1.7122 1.9151 0.0195  -0.1872 -0.6822 130 PHE A N   
1008 C CA  . PHE A 137 ? 1.7571 1.6941 2.0005 0.0637  -0.2295 -0.6978 130 PHE A CA  
1009 C C   . PHE A 137 ? 1.8711 1.8245 2.1702 0.1057  -0.2262 -0.7722 130 PHE A C   
1010 O O   . PHE A 137 ? 1.9505 1.8230 2.2570 0.1358  -0.2645 -0.7875 130 PHE A O   
1011 C CB  . PHE A 137 ? 1.7461 1.6939 2.0333 0.0815  -0.2535 -0.6691 130 PHE A CB  
1012 C CG  . PHE A 137 ? 1.7233 1.6391 1.9624 0.0500  -0.2657 -0.6004 130 PHE A CG  
1013 C CD1 . PHE A 137 ? 1.7963 1.6163 1.9883 0.0406  -0.2983 -0.5639 130 PHE A CD1 
1014 C CD2 . PHE A 137 ? 1.6742 1.6545 1.9189 0.0298  -0.2446 -0.5758 130 PHE A CD2 
1015 C CE1 . PHE A 137 ? 1.7649 1.5648 1.9185 0.0116  -0.3044 -0.5079 130 PHE A CE1 
1016 C CE2 . PHE A 137 ? 1.6736 1.6262 1.8783 0.0048  -0.2550 -0.5199 130 PHE A CE2 
1017 C CZ  . PHE A 137 ? 1.6759 1.5433 1.8379 -0.0029 -0.2833 -0.4883 130 PHE A CZ  
1018 N N   . LEU A 138 ? 1.7980 1.8532 2.1383 0.1077  -0.1811 -0.8199 131 LEU A N   
1019 C CA  . LEU A 138 ? 1.8425 1.9395 2.2514 0.1484  -0.1680 -0.9015 131 LEU A CA  
1020 C C   . LEU A 138 ? 1.9824 2.0195 2.3532 0.1559  -0.1699 -0.9432 131 LEU A C   
1021 O O   . LEU A 138 ? 2.0399 2.0426 2.4665 0.2066  -0.1985 -0.9907 131 LEU A O   
1022 C CB  . LEU A 138 ? 1.8133 2.0396 2.2598 0.1316  -0.1063 -0.9413 131 LEU A CB  
1023 C CG  . LEU A 138 ? 1.8904 2.1980 2.4574 0.1801  -0.0984 -1.0163 131 LEU A CG  
1024 C CD1 . LEU A 138 ? 1.8298 2.1849 2.4726 0.1948  -0.1197 -0.9936 131 LEU A CD1 
1025 C CD2 . LEU A 138 ? 1.9484 2.3623 2.5238 0.1559  -0.0245 -1.0791 131 LEU A CD2 
1026 N N   . PRO A 139 ? 1.9592 1.9793 2.2392 0.1107  -0.1452 -0.9316 132 PRO A N   
1027 C CA  . PRO A 139 ? 2.0353 1.9976 2.2809 0.1186  -0.1503 -0.9774 132 PRO A CA  
1028 C C   . PRO A 139 ? 2.1313 1.9692 2.3749 0.1432  -0.2119 -0.9613 132 PRO A C   
1029 O O   . PRO A 139 ? 2.2196 2.0095 2.4774 0.1740  -0.2263 -1.0165 132 PRO A O   
1030 C CB  . PRO A 139 ? 2.0538 2.0180 2.1959 0.0603  -0.1235 -0.9509 132 PRO A CB  
1031 C CG  . PRO A 139 ? 2.0463 2.0925 2.1804 0.0290  -0.0884 -0.9164 132 PRO A CG  
1032 C CD  . PRO A 139 ? 1.9342 1.9808 2.1377 0.0533  -0.1178 -0.8796 132 PRO A CD  
1033 N N   . ALA A 140 ? 2.0336 1.8153 2.2550 0.1270  -0.2465 -0.8880 133 ALA A N   
1034 C CA  . ALA A 140 ? 2.0797 1.7360 2.2857 0.1384  -0.3022 -0.8625 133 ALA A CA  
1035 C C   . ALA A 140 ? 2.1458 1.7698 2.4264 0.2002  -0.3410 -0.8886 133 ALA A C   
1036 O O   . ALA A 140 ? 2.2257 1.7422 2.5029 0.2260  -0.3845 -0.9032 133 ALA A O   
1037 C CB  . ALA A 140 ? 2.0408 1.6635 2.2002 0.0975  -0.3173 -0.7805 133 ALA A CB  
1038 N N   . ALA A 141 ? 2.0340 1.7487 2.3828 0.2239  -0.3291 -0.8957 134 ALA A N   
1039 C CA  . ALA A 141 ? 2.0628 1.7697 2.4971 0.2872  -0.3689 -0.9247 134 ALA A CA  
1040 C C   . ALA A 141 ? 2.1771 1.9041 2.6752 0.3368  -0.3625 -1.0189 134 ALA A C   
1041 O O   . ALA A 141 ? 2.2460 1.8744 2.7635 0.3826  -0.4147 -1.0421 134 ALA A O   
1042 C CB  . ALA A 141 ? 1.9846 1.8014 2.4774 0.2903  -0.3515 -0.9129 134 ALA A CB  
1043 N N   . LEU A 142 ? 2.1172 1.9642 2.6376 0.3235  -0.2970 -1.0726 135 LEU A N   
1044 C CA  . LEU A 142 ? 2.1842 2.0665 2.7400 0.3536  -0.2641 -1.1544 135 LEU A CA  
1045 C C   . LEU A 142 ? 2.3398 2.0618 2.7812 0.3430  -0.2691 -1.1204 135 LEU A C   
1046 O O   . LEU A 142 ? 2.4099 2.0523 2.8101 0.3654  -0.2452 -1.0974 135 LEU A O   
1047 C CB  . LEU A 142 ? 2.1445 2.1655 2.6930 0.3118  -0.1844 -1.1937 135 LEU A CB  
1048 C CG  . LEU A 142 ? 2.2775 2.2625 2.6967 0.2794  -0.1090 -1.1848 135 LEU A CG  
1049 C CD1 . LEU A 142 ? 2.3079 2.2569 2.6651 0.2415  -0.1272 -1.2087 135 LEU A CD1 
1050 C CD2 . LEU A 142 ? 2.3904 2.2846 2.7489 0.3118  -0.0711 -1.1499 135 LEU A CD2 
1051 N N   . ARG A 143 ? 2.3030 1.9867 2.7150 0.3135  -0.3076 -1.1313 136 ARG A N   
1052 C CA  . ARG A 143 ? 2.3947 1.9498 2.7430 0.3076  -0.3357 -1.1378 136 ARG A CA  
1053 C C   . ARG A 143 ? 2.5010 1.8971 2.8024 0.3209  -0.3702 -1.0631 136 ARG A C   
1054 O O   . ARG A 143 ? 2.5664 1.8678 2.8136 0.3275  -0.3485 -1.0558 136 ARG A O   
1055 C CB  . ARG A 143 ? 2.3774 1.9053 2.6245 0.2361  -0.3245 -1.0826 136 ARG A CB  
1056 C CG  . ARG A 143 ? 2.6122 2.1339 2.7804 0.2037  -0.2824 -1.1130 136 ARG A CG  
1057 C CD  . ARG A 143 ? 2.7329 2.3444 2.8140 0.1522  -0.1980 -1.0693 136 ARG A CD  
1058 N NE  . ARG A 143 ? 2.8259 2.4354 2.8343 0.0946  -0.2008 -1.0286 136 ARG A NE  
1059 C CZ  . ARG A 143 ? 2.9440 2.5870 2.8462 0.0471  -0.1479 -0.9789 136 ARG A CZ  
1060 N NH1 . ARG A 143 ? 2.7836 2.4914 2.7241 0.0218  -0.1843 -1.0319 136 ARG A NH1 
1061 N NH2 . ARG A 143 ? 2.7275 2.5037 2.7061 0.0716  -0.1143 -1.0816 136 ARG A NH2 
1062 N N   . ALA A 144 ? 2.4479 1.8210 2.7929 0.3342  -0.4391 -1.0348 137 ALA A N   
1063 C CA  . ALA A 144 ? 2.5191 1.7477 2.8231 0.3444  -0.4801 -0.9709 137 ALA A CA  
1064 C C   . ALA A 144 ? 2.5775 1.8045 2.8783 0.3726  -0.4264 -0.9295 137 ALA A C   
1065 O O   . ALA A 144 ? 2.6470 1.7581 2.9013 0.3786  -0.4251 -0.8916 137 ALA A O   
1066 C CB  . ALA A 144 ? 2.5009 1.6998 2.8002 0.3285  -0.5395 -0.9189 137 ALA A CB  
1067 N N   . ALA A 145 ? 2.4709 1.8330 2.8559 0.4034  -0.4054 -0.9653 138 ALA A N   
1068 C CA  . ALA A 145 ? 2.4717 1.8553 2.8820 0.4399  -0.3669 -0.9436 138 ALA A CA  
1069 C C   . ALA A 145 ? 2.5915 1.9229 2.9249 0.4337  -0.2838 -0.9311 138 ALA A C   
1070 O O   . ALA A 145 ? 2.6524 1.9034 2.9617 0.4550  -0.2677 -0.8940 138 ALA A O   
1071 C CB  . ALA A 145 ? 2.3823 1.9250 2.8726 0.4497  -0.3409 -0.9647 138 ALA A CB  
1072 N N   . LEU A 146 ? 2.5506 1.9277 2.8728 0.4185  -0.2562 -0.9929 139 LEU A N   
1073 C CA  . LEU A 146 ? 2.6159 1.9393 2.8700 0.4183  -0.1966 -1.0065 139 LEU A CA  
1074 C C   . LEU A 146 ? 2.7490 1.9149 2.9058 0.3894  -0.1994 -0.9682 139 LEU A C   
1075 O O   . LEU A 146 ? 2.8197 1.9153 2.9148 0.3902  -0.1544 -0.9738 139 LEU A O   
1076 C CB  . LEU A 146 ? 2.5930 1.9997 2.8236 0.3920  -0.1563 -1.0567 139 LEU A CB  
1077 C CG  . LEU A 146 ? 2.6388 2.1059 2.8429 0.4014  -0.0732 -1.0414 139 LEU A CG  
1078 C CD1 . LEU A 146 ? 2.5336 2.1489 2.8285 0.4066  -0.0714 -1.0479 139 LEU A CD1 
1079 C CD2 . LEU A 146 ? 2.7243 2.1730 2.8238 0.3705  -0.0207 -1.0579 139 LEU A CD2 
1080 N N   . LEU A 147 ? 2.7231 1.8371 2.8916 0.3748  -0.2692 -0.9539 140 LEU A N   
1081 C CA  . LEU A 147 ? 2.8165 1.7882 2.9121 0.3446  -0.2811 -0.9235 140 LEU A CA  
1082 C C   . LEU A 147 ? 2.9289 1.8143 2.9854 0.3490  -0.2364 -0.8409 140 LEU A C   
1083 O O   . LEU A 147 ? 2.9915 1.7678 3.0069 0.3253  -0.2474 -0.8121 140 LEU A O   
1084 C CB  . LEU A 147 ? 2.8012 1.7513 2.8943 0.3086  -0.3496 -0.9159 140 LEU A CB  
1085 C CG  . LEU A 147 ? 2.8903 1.7981 2.9064 0.2486  -0.3355 -0.9225 140 LEU A CG  
1086 C CD1 . LEU A 147 ? 2.9967 1.7682 2.9404 0.2231  -0.3085 -0.8996 140 LEU A CD1 
1087 C CD2 . LEU A 147 ? 2.8958 1.8948 2.8928 0.2370  -0.2876 -0.9668 140 LEU A CD2 
1088 N N   . GLY A 148 ? 2.8796 1.8205 2.9838 0.3956  -0.2115 -0.8355 141 GLY A N   
1089 C CA  . GLY A 148 ? 2.9261 1.8081 3.0294 0.4224  -0.1847 -0.7857 141 GLY A CA  
1090 C C   . GLY A 148 ? 3.0351 1.8957 3.0804 0.4272  -0.0833 -0.7685 141 GLY A C   
1091 O O   . GLY A 148 ? 3.0017 1.9423 3.0811 0.4604  -0.0540 -0.7734 141 GLY A O   
1092 N N   . ARG A 149 ? 3.0927 1.8413 3.0795 0.4115  -0.0614 -0.7812 142 ARG A N   
1093 C CA  . ARG A 149 ? 3.1669 1.8682 3.0967 0.4226  0.0199  -0.7794 142 ARG A CA  
1094 C C   . ARG A 149 ? 3.2943 1.8715 3.1499 0.3907  0.0898  -0.7143 142 ARG A C   
1095 O O   . ARG A 149 ? 3.3407 1.8797 3.1855 0.4211  0.1458  -0.6932 142 ARG A O   
1096 C CB  . ARG A 149 ? 3.2075 1.9070 3.0600 0.3887  0.0511  -0.8169 142 ARG A CB  
1097 N N   . LEU A 150 ? 3.2805 1.7935 3.1311 0.3555  0.0409  -0.7322 143 LEU A N   
1098 C CA  . LEU A 150 ? 3.3367 1.7398 3.1561 0.3233  0.0642  -0.7057 143 LEU A CA  
1099 C C   . LEU A 150 ? 3.4144 1.7574 3.2119 0.3394  0.1342  -0.6814 143 LEU A C   
1100 O O   . LEU A 150 ? 3.4048 1.7679 3.2403 0.3925  0.1505  -0.6619 143 LEU A O   
1101 C CB  . LEU A 150 ? 3.3056 1.7092 3.1783 0.3241  0.0079  -0.6676 143 LEU A CB  
1102 C CG  . LEU A 150 ? 3.2891 1.7531 3.1743 0.2937  -0.0579 -0.6724 143 LEU A CG  
1103 C CD1 . LEU A 150 ? 3.2078 1.7755 3.1558 0.3370  -0.1027 -0.6683 143 LEU A CD1 
1104 C CD2 . LEU A 150 ? 3.3407 1.7486 3.2179 0.2508  -0.0753 -0.6329 143 LEU A CD2 
1105 C C6  . PLM B .   ? 1.6714 1.6903 1.6579 -0.2106 -0.2652 -0.3168 201 PLM A C6  
1106 C C7  . PLM B .   ? 1.6002 1.6194 1.6045 -0.2042 -0.2462 -0.3031 201 PLM A C7  
1107 C C8  . PLM B .   ? 1.5559 1.5865 1.5530 -0.1952 -0.2450 -0.2887 201 PLM A C8  
1108 C C9  . PLM B .   ? 1.5012 1.5359 1.5187 -0.1907 -0.2315 -0.2777 201 PLM A C9  
1109 C CA  . PLM B .   ? 1.4494 1.4808 1.4492 -0.1846 -0.2220 -0.2710 201 PLM A CA  
1110 C CB  . PLM B .   ? 1.4102 1.4442 1.4269 -0.1803 -0.2137 -0.2630 201 PLM A CB  
1111 C CC  . PLM B .   ? 1.3947 1.4299 1.4000 -0.1792 -0.2100 -0.2559 201 PLM A CC  
1112 C CD  . PLM B .   ? 1.3274 1.3647 1.3469 -0.1757 -0.2061 -0.2505 201 PLM A CD  
1113 C CE  . PLM B .   ? 1.3043 1.3479 1.3271 -0.1759 -0.1982 -0.2544 201 PLM A CE  
1114 C CF  . PLM B .   ? 1.3332 1.3763 1.3570 -0.1793 -0.1975 -0.2486 201 PLM A CF  
1115 C CG  . PLM B .   ? 1.3117 1.3504 1.3429 -0.1735 -0.2024 -0.2465 201 PLM A CG  
1116 C C10 . PAM C .   ? 2.2596 1.5517 2.1587 0.0247  -0.5462 -0.2837 202 PAM A C10 
1117 C C11 . PAM C .   ? 2.1755 1.5799 2.1160 0.0277  -0.5237 -0.2867 202 PAM A C11 
1118 C C12 . PAM C .   ? 2.1318 1.6234 2.1756 0.0795  -0.5308 -0.3380 202 PAM A C12 
1119 C C13 . PAM C .   ? 1.9992 1.6228 2.0967 0.0628  -0.4742 -0.3571 202 PAM A C13 
1120 C C14 . PAM C .   ? 1.9552 1.6706 2.1539 0.1045  -0.4731 -0.4105 202 PAM A C14 
1121 C C15 . PAM C .   ? 1.8540 1.6831 2.0891 0.0834  -0.4297 -0.4159 202 PAM A C15 
1122 C C16 . PAM C .   ? 1.8197 1.7398 2.1538 0.1182  -0.4348 -0.4628 202 PAM A C16 
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