data_9G58
# 
_entry.id   9G58 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9G58         pdb_00009g58 10.2210/pdb9g58/pdb 
WWPDB D_1292140292 ?            ?                   
# 
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 2025-04-09 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_CSD'          
4 2 'Structure model' '_citation.journal_id_ISSN'         
5 2 'Structure model' '_citation.pdbx_database_id_DOI'    
6 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 2 'Structure model' '_citation.title'                   
8 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G58 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-16 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              holger.sondermann@cssb-hamburg.de 
_pdbx_contact_author.name_first         Holger 
_pdbx_contact_author.name_last          Sondermann 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2211-6234 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lormand, J.D.'  1 0000-0002-7803-4716 
'Sondermann, H.' 2 0000-0003-2211-6234 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Secreted retropepsin-like enzymes are essential for stress tolerance and biofilm formation in Pseudomonas aeruginosa.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.03.18.643919 
_citation.pdbx_database_id_PubMed   40166241 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lormand, J.D.'       1 ?                   
primary 'Savelle, C.H.'       2 ?                   
primary 'Teschler, J.K.'      3 ?                   
primary 'Lopez, E.'           4 ?                   
primary 'Little, R.H.'        5 ?                   
primary 'Malone, J.'          6 ?                   
primary 'Yildiz, F.H.'        7 0000-0002-6384-7167 
primary 'Garcia-Garcia, M.J.' 8 ?                   
primary 'Sondermann, H.'      9 0000-0003-2211-6234 
# 
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 'Putative ATP-dependent zinc protease domain-containing protein' 17395.867 2  ? ? ? ? 
2 water   nat water                                                            18.015    27 ? ? ? ? 
# 
_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       
;AAGEKTVYGLNEYAALDGINLEVAAKLDTGAKTASLSARDIKRFKRNGESWVRFYLAIDAAHSHPIERPLARVSKIKRRA
GDYDPEEGKKYTARPVIELDICMGSAMRSIEVNLTDRSAFQYPLLIGSEALKRFDALVDPSLKYAAGKPACAIAAHTAE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AAGEKTVYGLNEYAALDGINLEVAAKLDTGAKTASLSARDIKRFKRNGESWVRFYLAIDAAHSHPIERPLARVSKIKRRA
GDYDPEEGKKYTARPVIELDICMGSAMRSIEVNLTDRSAFQYPLLIGSEALKRFDALVDPSLKYAAGKPACAIAAHTAE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ALA n 
1 3   GLY n 
1 4   GLU n 
1 5   LYS n 
1 6   THR n 
1 7   VAL n 
1 8   TYR n 
1 9   GLY n 
1 10  LEU n 
1 11  ASN n 
1 12  GLU n 
1 13  TYR n 
1 14  ALA n 
1 15  ALA n 
1 16  LEU n 
1 17  ASP n 
1 18  GLY n 
1 19  ILE n 
1 20  ASN n 
1 21  LEU n 
1 22  GLU n 
1 23  VAL n 
1 24  ALA n 
1 25  ALA n 
1 26  LYS n 
1 27  LEU n 
1 28  ASP n 
1 29  THR n 
1 30  GLY n 
1 31  ALA n 
1 32  LYS n 
1 33  THR n 
1 34  ALA n 
1 35  SER n 
1 36  LEU n 
1 37  SER n 
1 38  ALA n 
1 39  ARG n 
1 40  ASP n 
1 41  ILE n 
1 42  LYS n 
1 43  ARG n 
1 44  PHE n 
1 45  LYS n 
1 46  ARG n 
1 47  ASN n 
1 48  GLY n 
1 49  GLU n 
1 50  SER n 
1 51  TRP n 
1 52  VAL n 
1 53  ARG n 
1 54  PHE n 
1 55  TYR n 
1 56  LEU n 
1 57  ALA n 
1 58  ILE n 
1 59  ASP n 
1 60  ALA n 
1 61  ALA n 
1 62  HIS n 
1 63  SER n 
1 64  HIS n 
1 65  PRO n 
1 66  ILE n 
1 67  GLU n 
1 68  ARG n 
1 69  PRO n 
1 70  LEU n 
1 71  ALA n 
1 72  ARG n 
1 73  VAL n 
1 74  SER n 
1 75  LYS n 
1 76  ILE n 
1 77  LYS n 
1 78  ARG n 
1 79  ARG n 
1 80  ALA n 
1 81  GLY n 
1 82  ASP n 
1 83  TYR n 
1 84  ASP n 
1 85  PRO n 
1 86  GLU n 
1 87  GLU n 
1 88  GLY n 
1 89  LYS n 
1 90  LYS n 
1 91  TYR n 
1 92  THR n 
1 93  ALA n 
1 94  ARG n 
1 95  PRO n 
1 96  VAL n 
1 97  ILE n 
1 98  GLU n 
1 99  LEU n 
1 100 ASP n 
1 101 ILE n 
1 102 CYS n 
1 103 MET n 
1 104 GLY n 
1 105 SER n 
1 106 ALA n 
1 107 MET n 
1 108 ARG n 
1 109 SER n 
1 110 ILE n 
1 111 GLU n 
1 112 VAL n 
1 113 ASN n 
1 114 LEU n 
1 115 THR n 
1 116 ASP n 
1 117 ARG n 
1 118 SER n 
1 119 ALA n 
1 120 PHE n 
1 121 GLN n 
1 122 TYR n 
1 123 PRO n 
1 124 LEU n 
1 125 LEU n 
1 126 ILE n 
1 127 GLY n 
1 128 SER n 
1 129 GLU n 
1 130 ALA n 
1 131 LEU n 
1 132 LYS n 
1 133 ARG n 
1 134 PHE n 
1 135 ASP n 
1 136 ALA n 
1 137 LEU n 
1 138 VAL n 
1 139 ASP n 
1 140 PRO n 
1 141 SER n 
1 142 LEU n 
1 143 LYS n 
1 144 TYR n 
1 145 ALA n 
1 146 ALA n 
1 147 GLY n 
1 148 LYS n 
1 149 PRO n 
1 150 ALA n 
1 151 CYS n 
1 152 ALA n 
1 153 ILE n 
1 154 ALA n 
1 155 ALA n 
1 156 HIS n 
1 157 THR n 
1 158 ALA n 
1 159 GLU 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                   159 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Pfl01_1762 
_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      'Pseudomonas fluorescens Pf0-1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     205922 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   20  ?   ?   ?   A . n 
A 1 2   ALA 2   21  ?   ?   ?   A . n 
A 1 3   GLY 3   22  ?   ?   ?   A . n 
A 1 4   GLU 4   23  23  GLU GLU A . n 
A 1 5   LYS 5   24  24  LYS LYS A . n 
A 1 6   THR 6   25  25  THR THR A . n 
A 1 7   VAL 7   26  26  VAL VAL A . n 
A 1 8   TYR 8   27  27  TYR TYR A . n 
A 1 9   GLY 9   28  28  GLY GLY A . n 
A 1 10  LEU 10  29  29  LEU LEU A . n 
A 1 11  ASN 11  30  30  ASN ASN A . n 
A 1 12  GLU 12  31  31  GLU GLU A . n 
A 1 13  TYR 13  32  32  TYR TYR A . n 
A 1 14  ALA 14  33  33  ALA ALA A . n 
A 1 15  ALA 15  34  34  ALA ALA A . n 
A 1 16  LEU 16  35  35  LEU LEU A . n 
A 1 17  ASP 17  36  36  ASP ASP A . n 
A 1 18  GLY 18  37  37  GLY GLY A . n 
A 1 19  ILE 19  38  38  ILE ILE A . n 
A 1 20  ASN 20  39  39  ASN ASN A . n 
A 1 21  LEU 21  40  40  LEU LEU A . n 
A 1 22  GLU 22  41  41  GLU GLU A . n 
A 1 23  VAL 23  42  42  VAL VAL A . n 
A 1 24  ALA 24  43  43  ALA ALA A . n 
A 1 25  ALA 25  44  44  ALA ALA A . n 
A 1 26  LYS 26  45  45  LYS LYS A . n 
A 1 27  LEU 27  46  46  LEU LEU A . n 
A 1 28  ASP 28  47  47  ASP ASP A . n 
A 1 29  THR 29  48  48  THR THR A . n 
A 1 30  GLY 30  49  49  GLY GLY A . n 
A 1 31  ALA 31  50  50  ALA ALA A . n 
A 1 32  LYS 32  51  51  LYS LYS A . n 
A 1 33  THR 33  52  52  THR THR A . n 
A 1 34  ALA 34  53  53  ALA ALA A . n 
A 1 35  SER 35  54  54  SER SER A . n 
A 1 36  LEU 36  55  55  LEU LEU A . n 
A 1 37  SER 37  56  56  SER SER A . n 
A 1 38  ALA 38  57  57  ALA ALA A . n 
A 1 39  ARG 39  58  58  ARG ARG A . n 
A 1 40  ASP 40  59  59  ASP ASP A . n 
A 1 41  ILE 41  60  60  ILE ILE A . n 
A 1 42  LYS 42  61  61  LYS LYS A . n 
A 1 43  ARG 43  62  62  ARG ARG A . n 
A 1 44  PHE 44  63  63  PHE PHE A . n 
A 1 45  LYS 45  64  64  LYS LYS A . n 
A 1 46  ARG 46  65  65  ARG ARG A . n 
A 1 47  ASN 47  66  66  ASN ASN A . n 
A 1 48  GLY 48  67  67  GLY GLY A . n 
A 1 49  GLU 49  68  68  GLU GLU A . n 
A 1 50  SER 50  69  69  SER SER A . n 
A 1 51  TRP 51  70  70  TRP TRP A . n 
A 1 52  VAL 52  71  71  VAL VAL A . n 
A 1 53  ARG 53  72  72  ARG ARG A . n 
A 1 54  PHE 54  73  73  PHE PHE A . n 
A 1 55  TYR 55  74  74  TYR TYR A . n 
A 1 56  LEU 56  75  75  LEU LEU A . n 
A 1 57  ALA 57  76  76  ALA ALA A . n 
A 1 58  ILE 58  77  77  ILE ILE A . n 
A 1 59  ASP 59  78  78  ASP ASP A . n 
A 1 60  ALA 60  79  79  ALA ALA A . n 
A 1 61  ALA 61  80  80  ALA ALA A . n 
A 1 62  HIS 62  81  81  HIS HIS A . n 
A 1 63  SER 63  82  82  SER SER A . n 
A 1 64  HIS 64  83  83  HIS HIS A . n 
A 1 65  PRO 65  84  84  PRO PRO A . n 
A 1 66  ILE 66  85  85  ILE ILE A . n 
A 1 67  GLU 67  86  86  GLU GLU A . n 
A 1 68  ARG 68  87  87  ARG ARG A . n 
A 1 69  PRO 69  88  88  PRO PRO A . n 
A 1 70  LEU 70  89  89  LEU LEU A . n 
A 1 71  ALA 71  90  90  ALA ALA A . n 
A 1 72  ARG 72  91  91  ARG ARG A . n 
A 1 73  VAL 73  92  92  VAL VAL A . n 
A 1 74  SER 74  93  93  SER SER A . n 
A 1 75  LYS 75  94  94  LYS LYS A . n 
A 1 76  ILE 76  95  ?   ?   ?   A . n 
A 1 77  LYS 77  96  ?   ?   ?   A . n 
A 1 78  ARG 78  97  ?   ?   ?   A . n 
A 1 79  ARG 79  98  ?   ?   ?   A . n 
A 1 80  ALA 80  99  ?   ?   ?   A . n 
A 1 81  GLY 81  100 ?   ?   ?   A . n 
A 1 82  ASP 82  101 ?   ?   ?   A . n 
A 1 83  TYR 83  102 ?   ?   ?   A . n 
A 1 84  ASP 84  103 ?   ?   ?   A . n 
A 1 85  PRO 85  104 ?   ?   ?   A . n 
A 1 86  GLU 86  105 ?   ?   ?   A . n 
A 1 87  GLU 87  106 ?   ?   ?   A . n 
A 1 88  GLY 88  107 ?   ?   ?   A . n 
A 1 89  LYS 89  108 ?   ?   ?   A . n 
A 1 90  LYS 90  109 ?   ?   ?   A . n 
A 1 91  TYR 91  110 ?   ?   ?   A . n 
A 1 92  THR 92  111 ?   ?   ?   A . n 
A 1 93  ALA 93  112 112 ALA ALA A . n 
A 1 94  ARG 94  113 113 ARG ARG A . n 
A 1 95  PRO 95  114 114 PRO PRO A . n 
A 1 96  VAL 96  115 115 VAL VAL A . n 
A 1 97  ILE 97  116 116 ILE ILE A . n 
A 1 98  GLU 98  117 117 GLU GLU A . n 
A 1 99  LEU 99  118 118 LEU LEU A . n 
A 1 100 ASP 100 119 119 ASP ASP A . n 
A 1 101 ILE 101 120 120 ILE ILE A . n 
A 1 102 CYS 102 121 121 CYS CYS A . n 
A 1 103 MET 103 122 122 MET MET A . n 
A 1 104 GLY 104 123 123 GLY GLY A . n 
A 1 105 SER 105 124 124 SER SER A . n 
A 1 106 ALA 106 125 125 ALA ALA A . n 
A 1 107 MET 107 126 126 MET MET A . n 
A 1 108 ARG 108 127 127 ARG ARG A . n 
A 1 109 SER 109 128 128 SER SER A . n 
A 1 110 ILE 110 129 129 ILE ILE A . n 
A 1 111 GLU 111 130 130 GLU GLU A . n 
A 1 112 VAL 112 131 131 VAL VAL A . n 
A 1 113 ASN 113 132 132 ASN ASN A . n 
A 1 114 LEU 114 133 133 LEU LEU A . n 
A 1 115 THR 115 134 134 THR THR A . n 
A 1 116 ASP 116 135 135 ASP ASP A . n 
A 1 117 ARG 117 136 136 ARG ARG A . n 
A 1 118 SER 118 137 137 SER SER A . n 
A 1 119 ALA 119 138 138 ALA ALA A . n 
A 1 120 PHE 120 139 139 PHE PHE A . n 
A 1 121 GLN 121 140 140 GLN GLN A . n 
A 1 122 TYR 122 141 141 TYR TYR A . n 
A 1 123 PRO 123 142 142 PRO PRO A . n 
A 1 124 LEU 124 143 143 LEU LEU A . n 
A 1 125 LEU 125 144 144 LEU LEU A . n 
A 1 126 ILE 126 145 145 ILE ILE A . n 
A 1 127 GLY 127 146 146 GLY GLY A . n 
A 1 128 SER 128 147 147 SER SER A . n 
A 1 129 GLU 129 148 148 GLU GLU A . n 
A 1 130 ALA 130 149 149 ALA ALA A . n 
A 1 131 LEU 131 150 150 LEU LEU A . n 
A 1 132 LYS 132 151 151 LYS LYS A . n 
A 1 133 ARG 133 152 152 ARG ARG A . n 
A 1 134 PHE 134 153 153 PHE PHE A . n 
A 1 135 ASP 135 154 154 ASP ASP A . n 
A 1 136 ALA 136 155 155 ALA ALA A . n 
A 1 137 LEU 137 156 156 LEU LEU A . n 
A 1 138 VAL 138 157 157 VAL VAL A . n 
A 1 139 ASP 139 158 158 ASP ASP A . n 
A 1 140 PRO 140 159 159 PRO PRO A . n 
A 1 141 SER 141 160 160 SER SER A . n 
A 1 142 LEU 142 161 161 LEU LEU A . n 
A 1 143 LYS 143 162 162 LYS LYS A . n 
A 1 144 TYR 144 163 163 TYR TYR A . n 
A 1 145 ALA 145 164 164 ALA ALA A . n 
A 1 146 ALA 146 165 165 ALA ALA A . n 
A 1 147 GLY 147 166 166 GLY GLY A . n 
A 1 148 LYS 148 167 167 LYS LYS A . n 
A 1 149 PRO 149 168 168 PRO PRO A . n 
A 1 150 ALA 150 169 169 ALA ALA A . n 
A 1 151 CYS 151 170 170 CYS CYS A . n 
A 1 152 ALA 152 171 ?   ?   ?   A . n 
A 1 153 ILE 153 172 ?   ?   ?   A . n 
A 1 154 ALA 154 173 ?   ?   ?   A . n 
A 1 155 ALA 155 174 ?   ?   ?   A . n 
A 1 156 HIS 156 175 ?   ?   ?   A . n 
A 1 157 THR 157 176 ?   ?   ?   A . n 
A 1 158 ALA 158 177 ?   ?   ?   A . n 
A 1 159 GLU 159 178 ?   ?   ?   A . n 
B 1 1   ALA 1   20  ?   ?   ?   B . n 
B 1 2   ALA 2   21  ?   ?   ?   B . n 
B 1 3   GLY 3   22  ?   ?   ?   B . n 
B 1 4   GLU 4   23  23  GLU GLU B . n 
B 1 5   LYS 5   24  24  LYS LYS B . n 
B 1 6   THR 6   25  25  THR THR B . n 
B 1 7   VAL 7   26  26  VAL VAL B . n 
B 1 8   TYR 8   27  27  TYR TYR B . n 
B 1 9   GLY 9   28  28  GLY GLY B . n 
B 1 10  LEU 10  29  29  LEU LEU B . n 
B 1 11  ASN 11  30  30  ASN ASN B . n 
B 1 12  GLU 12  31  31  GLU GLU B . n 
B 1 13  TYR 13  32  32  TYR TYR B . n 
B 1 14  ALA 14  33  33  ALA ALA B . n 
B 1 15  ALA 15  34  34  ALA ALA B . n 
B 1 16  LEU 16  35  35  LEU LEU B . n 
B 1 17  ASP 17  36  36  ASP ASP B . n 
B 1 18  GLY 18  37  37  GLY GLY B . n 
B 1 19  ILE 19  38  38  ILE ILE B . n 
B 1 20  ASN 20  39  39  ASN ASN B . n 
B 1 21  LEU 21  40  40  LEU LEU B . n 
B 1 22  GLU 22  41  41  GLU GLU B . n 
B 1 23  VAL 23  42  42  VAL VAL B . n 
B 1 24  ALA 24  43  43  ALA ALA B . n 
B 1 25  ALA 25  44  44  ALA ALA B . n 
B 1 26  LYS 26  45  45  LYS LYS B . n 
B 1 27  LEU 27  46  46  LEU LEU B . n 
B 1 28  ASP 28  47  47  ASP ASP B . n 
B 1 29  THR 29  48  48  THR THR B . n 
B 1 30  GLY 30  49  49  GLY GLY B . n 
B 1 31  ALA 31  50  50  ALA ALA B . n 
B 1 32  LYS 32  51  51  LYS LYS B . n 
B 1 33  THR 33  52  52  THR THR B . n 
B 1 34  ALA 34  53  53  ALA ALA B . n 
B 1 35  SER 35  54  54  SER SER B . n 
B 1 36  LEU 36  55  55  LEU LEU B . n 
B 1 37  SER 37  56  56  SER SER B . n 
B 1 38  ALA 38  57  57  ALA ALA B . n 
B 1 39  ARG 39  58  58  ARG ARG B . n 
B 1 40  ASP 40  59  59  ASP ASP B . n 
B 1 41  ILE 41  60  60  ILE ILE B . n 
B 1 42  LYS 42  61  61  LYS LYS B . n 
B 1 43  ARG 43  62  62  ARG ARG B . n 
B 1 44  PHE 44  63  63  PHE PHE B . n 
B 1 45  LYS 45  64  64  LYS LYS B . n 
B 1 46  ARG 46  65  65  ARG ARG B . n 
B 1 47  ASN 47  66  66  ASN ASN B . n 
B 1 48  GLY 48  67  67  GLY GLY B . n 
B 1 49  GLU 49  68  68  GLU GLU B . n 
B 1 50  SER 50  69  69  SER SER B . n 
B 1 51  TRP 51  70  70  TRP TRP B . n 
B 1 52  VAL 52  71  71  VAL VAL B . n 
B 1 53  ARG 53  72  72  ARG ARG B . n 
B 1 54  PHE 54  73  73  PHE PHE B . n 
B 1 55  TYR 55  74  74  TYR TYR B . n 
B 1 56  LEU 56  75  75  LEU LEU B . n 
B 1 57  ALA 57  76  76  ALA ALA B . n 
B 1 58  ILE 58  77  77  ILE ILE B . n 
B 1 59  ASP 59  78  78  ASP ASP B . n 
B 1 60  ALA 60  79  79  ALA ALA B . n 
B 1 61  ALA 61  80  80  ALA ALA B . n 
B 1 62  HIS 62  81  81  HIS HIS B . n 
B 1 63  SER 63  82  82  SER SER B . n 
B 1 64  HIS 64  83  83  HIS HIS B . n 
B 1 65  PRO 65  84  84  PRO PRO B . n 
B 1 66  ILE 66  85  85  ILE ILE B . n 
B 1 67  GLU 67  86  86  GLU GLU B . n 
B 1 68  ARG 68  87  87  ARG ARG B . n 
B 1 69  PRO 69  88  88  PRO PRO B . n 
B 1 70  LEU 70  89  89  LEU LEU B . n 
B 1 71  ALA 71  90  90  ALA ALA B . n 
B 1 72  ARG 72  91  ?   ?   ?   B . n 
B 1 73  VAL 73  92  ?   ?   ?   B . n 
B 1 74  SER 74  93  ?   ?   ?   B . n 
B 1 75  LYS 75  94  ?   ?   ?   B . n 
B 1 76  ILE 76  95  ?   ?   ?   B . n 
B 1 77  LYS 77  96  ?   ?   ?   B . n 
B 1 78  ARG 78  97  ?   ?   ?   B . n 
B 1 79  ARG 79  98  ?   ?   ?   B . n 
B 1 80  ALA 80  99  ?   ?   ?   B . n 
B 1 81  GLY 81  100 ?   ?   ?   B . n 
B 1 82  ASP 82  101 ?   ?   ?   B . n 
B 1 83  TYR 83  102 ?   ?   ?   B . n 
B 1 84  ASP 84  103 ?   ?   ?   B . n 
B 1 85  PRO 85  104 ?   ?   ?   B . n 
B 1 86  GLU 86  105 ?   ?   ?   B . n 
B 1 87  GLU 87  106 ?   ?   ?   B . n 
B 1 88  GLY 88  107 ?   ?   ?   B . n 
B 1 89  LYS 89  108 ?   ?   ?   B . n 
B 1 90  LYS 90  109 ?   ?   ?   B . n 
B 1 91  TYR 91  110 ?   ?   ?   B . n 
B 1 92  THR 92  111 111 THR THR B . n 
B 1 93  ALA 93  112 112 ALA ALA B . n 
B 1 94  ARG 94  113 113 ARG ARG B . n 
B 1 95  PRO 95  114 114 PRO PRO B . n 
B 1 96  VAL 96  115 115 VAL VAL B . n 
B 1 97  ILE 97  116 116 ILE ILE B . n 
B 1 98  GLU 98  117 117 GLU GLU B . n 
B 1 99  LEU 99  118 118 LEU LEU B . n 
B 1 100 ASP 100 119 119 ASP ASP B . n 
B 1 101 ILE 101 120 120 ILE ILE B . n 
B 1 102 CYS 102 121 121 CYS CYS B . n 
B 1 103 MET 103 122 122 MET MET B . n 
B 1 104 GLY 104 123 123 GLY GLY B . n 
B 1 105 SER 105 124 124 SER SER B . n 
B 1 106 ALA 106 125 125 ALA ALA B . n 
B 1 107 MET 107 126 126 MET MET B . n 
B 1 108 ARG 108 127 127 ARG ARG B . n 
B 1 109 SER 109 128 128 SER SER B . n 
B 1 110 ILE 110 129 129 ILE ILE B . n 
B 1 111 GLU 111 130 130 GLU GLU B . n 
B 1 112 VAL 112 131 131 VAL VAL B . n 
B 1 113 ASN 113 132 132 ASN ASN B . n 
B 1 114 LEU 114 133 133 LEU LEU B . n 
B 1 115 THR 115 134 134 THR THR B . n 
B 1 116 ASP 116 135 135 ASP ASP B . n 
B 1 117 ARG 117 136 136 ARG ARG B . n 
B 1 118 SER 118 137 137 SER SER B . n 
B 1 119 ALA 119 138 138 ALA ALA B . n 
B 1 120 PHE 120 139 139 PHE PHE B . n 
B 1 121 GLN 121 140 140 GLN GLN B . n 
B 1 122 TYR 122 141 141 TYR TYR B . n 
B 1 123 PRO 123 142 142 PRO PRO B . n 
B 1 124 LEU 124 143 143 LEU LEU B . n 
B 1 125 LEU 125 144 144 LEU LEU B . n 
B 1 126 ILE 126 145 145 ILE ILE B . n 
B 1 127 GLY 127 146 146 GLY GLY B . n 
B 1 128 SER 128 147 147 SER SER B . n 
B 1 129 GLU 129 148 148 GLU GLU B . n 
B 1 130 ALA 130 149 149 ALA ALA B . n 
B 1 131 LEU 131 150 150 LEU LEU B . n 
B 1 132 LYS 132 151 151 LYS LYS B . n 
B 1 133 ARG 133 152 152 ARG ARG B . n 
B 1 134 PHE 134 153 153 PHE PHE B . n 
B 1 135 ASP 135 154 154 ASP ASP B . n 
B 1 136 ALA 136 155 155 ALA ALA B . n 
B 1 137 LEU 137 156 156 LEU LEU B . n 
B 1 138 VAL 138 157 157 VAL VAL B . n 
B 1 139 ASP 139 158 158 ASP ASP B . n 
B 1 140 PRO 140 159 159 PRO PRO B . n 
B 1 141 SER 141 160 160 SER SER B . n 
B 1 142 LEU 142 161 161 LEU LEU B . n 
B 1 143 LYS 143 162 162 LYS LYS B . n 
B 1 144 TYR 144 163 163 TYR TYR B . n 
B 1 145 ALA 145 164 164 ALA ALA B . n 
B 1 146 ALA 146 165 165 ALA ALA B . n 
B 1 147 GLY 147 166 166 GLY GLY B . n 
B 1 148 LYS 148 167 167 LYS LYS B . n 
B 1 149 PRO 149 168 168 PRO PRO B . n 
B 1 150 ALA 150 169 169 ALA ALA B . n 
B 1 151 CYS 151 170 170 CYS CYS B . n 
B 1 152 ALA 152 171 ?   ?   ?   B . n 
B 1 153 ILE 153 172 ?   ?   ?   B . n 
B 1 154 ALA 154 173 ?   ?   ?   B . n 
B 1 155 ALA 155 174 ?   ?   ?   B . n 
B 1 156 HIS 156 175 ?   ?   ?   B . n 
B 1 157 THR 157 176 ?   ?   ?   B . n 
B 1 158 ALA 158 177 ?   ?   ?   B . n 
B 1 159 GLU 159 178 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  201 25 HOH HOH A . 
C 2 HOH 2  202 22 HOH HOH A . 
C 2 HOH 3  203 3  HOH HOH A . 
C 2 HOH 4  204 27 HOH HOH A . 
C 2 HOH 5  205 4  HOH HOH A . 
C 2 HOH 6  206 28 HOH HOH A . 
C 2 HOH 7  207 12 HOH HOH A . 
C 2 HOH 8  208 11 HOH HOH A . 
C 2 HOH 9  209 9  HOH HOH A . 
C 2 HOH 10 210 21 HOH HOH A . 
D 2 HOH 1  201 1  HOH HOH B . 
D 2 HOH 2  202 10 HOH HOH B . 
D 2 HOH 3  203 5  HOH HOH B . 
D 2 HOH 4  204 24 HOH HOH B . 
D 2 HOH 5  205 2  HOH HOH B . 
D 2 HOH 6  206 6  HOH HOH B . 
D 2 HOH 7  207 8  HOH HOH B . 
D 2 HOH 8  208 13 HOH HOH B . 
D 2 HOH 9  209 16 HOH HOH B . 
D 2 HOH 10 210 18 HOH HOH B . 
D 2 HOH 11 211 14 HOH HOH B . 
D 2 HOH 12 212 7  HOH HOH B . 
D 2 HOH 13 213 15 HOH HOH B . 
D 2 HOH 14 214 23 HOH HOH B . 
D 2 HOH 15 215 20 HOH HOH B . 
D 2 HOH 16 216 17 HOH HOH B . 
D 2 HOH 17 217 19 HOH HOH B . 
# 
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 GLU 23  ? CG  ? A GLU 4   CG  
2  1 Y 1 A GLU 23  ? CD  ? A GLU 4   CD  
3  1 Y 1 A GLU 23  ? OE1 ? A GLU 4   OE1 
4  1 Y 1 A GLU 23  ? OE2 ? A GLU 4   OE2 
5  1 Y 1 A LYS 61  ? CG  ? A LYS 42  CG  
6  1 Y 1 A LYS 61  ? CD  ? A LYS 42  CD  
7  1 Y 1 A LYS 61  ? CE  ? A LYS 42  CE  
8  1 Y 1 A LYS 61  ? NZ  ? A LYS 42  NZ  
9  1 Y 1 A LYS 94  ? CG  ? A LYS 75  CG  
10 1 Y 1 A LYS 94  ? CD  ? A LYS 75  CD  
11 1 Y 1 A LYS 94  ? CE  ? A LYS 75  CE  
12 1 Y 1 A LYS 94  ? NZ  ? A LYS 75  NZ  
13 1 Y 1 A ARG 113 ? NE  ? A ARG 94  NE  
14 1 Y 1 A ARG 113 ? CZ  ? A ARG 94  CZ  
15 1 Y 1 A ARG 113 ? NH1 ? A ARG 94  NH1 
16 1 Y 1 A ARG 113 ? NH2 ? A ARG 94  NH2 
17 1 Y 1 A LYS 167 ? CG  ? A LYS 148 CG  
18 1 Y 1 A LYS 167 ? CD  ? A LYS 148 CD  
19 1 Y 1 A LYS 167 ? CE  ? A LYS 148 CE  
20 1 Y 1 A LYS 167 ? NZ  ? A LYS 148 NZ  
21 1 Y 1 B GLU 23  ? CG  ? B GLU 4   CG  
22 1 Y 1 B GLU 23  ? CD  ? B GLU 4   CD  
23 1 Y 1 B GLU 23  ? OE1 ? B GLU 4   OE1 
24 1 Y 1 B GLU 23  ? OE2 ? B GLU 4   OE2 
25 1 Y 1 B ILE 38  ? CG1 ? B ILE 19  CG1 
26 1 Y 1 B ILE 38  ? CG2 ? B ILE 19  CG2 
27 1 Y 1 B ILE 38  ? CD1 ? B ILE 19  CD1 
28 1 Y 1 B ASN 39  ? CG  ? B ASN 20  CG  
29 1 Y 1 B ASN 39  ? OD1 ? B ASN 20  OD1 
30 1 Y 1 B ASN 39  ? ND2 ? B ASN 20  ND2 
31 1 Y 1 B LEU 40  ? CG  ? B LEU 21  CG  
32 1 Y 1 B LEU 40  ? CD1 ? B LEU 21  CD1 
33 1 Y 1 B LEU 40  ? CD2 ? B LEU 21  CD2 
34 1 Y 1 B THR 111 ? OG1 ? B THR 92  OG1 
35 1 Y 1 B THR 111 ? CG2 ? B THR 92  CG2 
36 1 Y 1 B ARG 113 ? CG  ? B ARG 94  CG  
37 1 Y 1 B ARG 113 ? CD  ? B ARG 94  CD  
38 1 Y 1 B ARG 113 ? NE  ? B ARG 94  NE  
39 1 Y 1 B ARG 113 ? CZ  ? B ARG 94  CZ  
40 1 Y 1 B ARG 113 ? NH1 ? B ARG 94  NH1 
41 1 Y 1 B ARG 113 ? NH2 ? B ARG 94  NH2 
42 1 Y 1 B ARG 136 ? CG  ? B ARG 117 CG  
43 1 Y 1 B ARG 136 ? CD  ? B ARG 117 CD  
44 1 Y 1 B ARG 136 ? NE  ? B ARG 117 NE  
45 1 Y 1 B ARG 136 ? CZ  ? B ARG 117 CZ  
46 1 Y 1 B ARG 136 ? NH1 ? B ARG 117 NH1 
47 1 Y 1 B ARG 136 ? NH2 ? B ARG 117 NH2 
48 1 Y 1 B PHE 139 ? CG  ? B PHE 120 CG  
49 1 Y 1 B PHE 139 ? CD1 ? B PHE 120 CD1 
50 1 Y 1 B PHE 139 ? CD2 ? B PHE 120 CD2 
51 1 Y 1 B PHE 139 ? CE1 ? B PHE 120 CE1 
52 1 Y 1 B PHE 139 ? CE2 ? B PHE 120 CE2 
53 1 Y 1 B PHE 139 ? CZ  ? B PHE 120 CZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G58 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.042 
_cell.length_a_esd                 ? 
_cell.length_b                     90.042 
_cell.length_b_esd                 ? 
_cell.length_c                     37.166 
_cell.length_c_esd                 ? 
_cell.volume                       301325.641 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9G58 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
_symmetry.space_group_name_Hall            'P 4w' 
_symmetry.space_group_name_H-M             'P 41' 
_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                   9G58 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.19 
_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, HANGING 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    
;0.2M ammonium acetate, 20% PEG 3350 and 0.1 M HEPES pH 8.0
(soak with condition incl. 20% xylitol)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-11-26 
_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   0.97918 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          57.22 
_reflns.entry_id                                       9G58 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.28 
_reflns.d_resolution_low                               45.02 
_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                                     26253 
_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                           98.91 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.91 
_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                                ? 
_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                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.09684 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.28 
_reflns_shell.d_res_low                                     2.36 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.42 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2402 
_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                               5.4 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.837 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          91.98 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.069 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               71.48 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G58 
_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                            2.40 
_refine.ls_d_res_low                             45.02 
_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                     13726 
_refine.ls_number_reflns_R_free                  1363 
_refine.ls_number_reflns_R_work                  10759 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.69 
_refine.ls_percent_reflns_R_free                 9.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2147 
_refine.ls_R_factor_R_free                       0.2447 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2113 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 30.9271 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3804 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        45.02 
_refine_hist.number_atoms_solvent             27 
_refine_hist.number_atoms_total               1972 
_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        1945 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.0026  ? 1985 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6093  ? 2689 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0431  ? 309  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0048  ? 347  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 20.1189 ? 724  ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    1.17553061568 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.51  . . 147 1331 99.53 . . . . 0.3312 . . . . . . . . . . . 0.4100 
'X-RAY DIFFRACTION' 2.51 2.64  . . 149 1338 99.60 . . . . 0.2735 . . . . . . . . . . . 0.3768 
'X-RAY DIFFRACTION' 2.64 2.81  . . 147 1320 99.53 . . . . 0.2731 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.81 3.02  . . 145 1326 99.59 . . . . 0.2902 . . . . . . . . . . . 0.3548 
'X-RAY DIFFRACTION' 3.02 3.33  . . 144 1344 99.87 . . . . 0.2379 . . . . . . . . . . . 0.3020 
'X-RAY DIFFRACTION' 3.33 3.81  . . 148 1333 99.87 . . . . 0.2252 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 3.81 4.80  . . 152 1359 99.80 . . . . 0.1685 . . . . . . . . . . . 0.1979 
'X-RAY DIFFRACTION' 4.80 45.02 . . 155 1408 99.74 . . . . 0.1787 . . . . . . . . . . . 0.1925 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   -0.936714235549 
_struct_ncs_oper.matrix[1][2]   -0.0673599407506 
_struct_ncs_oper.matrix[1][3]   0.343553604699 
_struct_ncs_oper.matrix[2][1]   -0.0283467356777 
_struct_ncs_oper.matrix[2][2]   -0.963500777858 
_struct_ncs_oper.matrix[2][3]   -0.266200513979 
_struct_ncs_oper.matrix[3][1]   0.348945416213 
_struct_ncs_oper.matrix[3][2]   -0.259092434178 
_struct_ncs_oper.matrix[3][3]   0.900615460147 
_struct_ncs_oper.vector[1]      -27.9655161285 
_struct_ncs_oper.vector[2]      56.7397287001 
_struct_ncs_oper.vector[3]      13.1013480297 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 23 through 37 or (resid 38 through 40 and (name N or name CA or name C or name O or name CB )) or resid 41 through 90 or (resid 112 through 113 and (name N or name CA or name C or name O or name CB )) or resid 114 through 135 or (resid 136 and (name N or name CA or name C or name O or name CB )) or resid 137 through 138 or (resid 139 and (name N or name CA or name C or name O or name CB )) or resid 140 through 147 or resid 149 through 170))
;
ens_1 d_2 
;(chain "B" and (resid 23 through 60 or (resid 61 and (name N or name CA or name C or name O or name CB )) or resid 62 through 90 or resid 112 through 147 or resid 149 through 166 or (resid 167 and (name N or name CA or name C or name O or name CB )) or resid 168 through 170))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A GLU 4   . A ALA 71  . A GLU 23  A ALA 90  ? ? 
ens_1 d_1 2 A ALA 93  . A SER 128 . A ALA 112 A SER 147 ? ? 
ens_1 d_1 3 A ALA 130 . A CYS 151 . A ALA 149 A CYS 170 ? ? 
ens_1 d_2 1 B GLU 4   . B ALA 71  . B GLU 23  B ALA 90  ? ? 
ens_1 d_2 2 B ALA 93  . B SER 128 . B ALA 112 B SER 147 ? ? 
ens_1 d_2 3 B ALA 130 . B CYS 151 . B ALA 149 B CYS 170 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     9G58 
_struct.title                        'Pseudomonas fluorescens periplasmic aspartic peptidase Pfl01_1762 (RloA)' 
_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        9G58 
_struct_keywords.text            'retropepsin-like, periplasm, bacteria, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q3KFF1_PSEPF 
_struct_ref.pdbx_db_accession          Q3KFF1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AAGEKTVYGLNEYAALDGINLEVAAKLDTGAKTASLSARDIKRFKRNGESWVRFYLAIDAAHSHPIERPLARVSKIKRRA
GDYDPEEGKKYTARPVIELDICMGSAMRSIEVNLTDRSAFQYPLLIGSEALKRFDALVDPSLKYAAGKPACAIAAHTAE
;
_struct_ref.pdbx_align_begin           20 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G58 A 1 ? 159 ? Q3KFF1 20 ? 178 ? 20 178 
2 1 9G58 B 1 ? 159 ? Q3KFF1 20 ? 178 ? 20 178 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 1350  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  12250 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_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 GLY A 127 ? PHE A 134 ? GLY A 146 PHE A 153 1 ? 8 
HELX_P HELX_P2 AA2 GLY B 127 ? PHE B 134 ? GLY B 146 PHE B 153 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 102 SG ? ? ? 1_555 A CYS 151 SG ? ? A CYS 121 A CYS 170 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2 disulf ? ? B CYS 102 SG ? ? ? 1_555 B CYS 151 SG ? ? B CYS 121 B CYS 170 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 102 ? CYS A 151 ? CYS A 121 ? 1_555 CYS A 170 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 102 ? CYS B 151 ? CYS B 121 ? 1_555 CYS B 170 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
AA5 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA5 8 9 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 6   ? GLY A 9   ? THR A 25  GLY A 28  
AA1 2 ALA A 136 ? ASP A 139 ? ALA A 155 ASP A 158 
AA2 1 ILE A 66  ? PRO A 69  ? ILE A 85  PRO A 88  
AA2 2 GLU A 49  ? LEU A 56  ? GLU A 68  LEU A 75  
AA2 3 ALA A 34  ? ARG A 46  ? ALA A 53  ARG A 65  
AA2 4 ALA A 106 ? THR A 115 ? ALA A 125 THR A 134 
AA2 5 PRO A 95  ? MET A 103 ? PRO A 114 MET A 122 
AA2 6 ARG A 72  ? VAL A 73  ? ARG A 91  VAL A 92  
AA3 1 ILE A 66  ? PRO A 69  ? ILE A 85  PRO A 88  
AA3 2 GLU A 49  ? LEU A 56  ? GLU A 68  LEU A 75  
AA3 3 ALA A 34  ? ARG A 46  ? ALA A 53  ARG A 65  
AA3 4 LEU A 124 ? ILE A 126 ? LEU A 143 ILE A 145 
AA3 5 VAL A 23  ? LEU A 27  ? VAL A 42  LEU A 46  
AA3 6 ASN A 11  ? LEU A 16  ? ASN A 30  LEU A 35  
AA3 7 PRO A 95  ? MET A 103 ? PRO A 114 MET A 122 
AA3 8 ARG A 72  ? VAL A 73  ? ARG A 91  VAL A 92  
AA4 1 THR B 6   ? GLY B 9   ? THR B 25  GLY B 28  
AA4 2 ALA B 136 ? ASP B 139 ? ALA B 155 ASP B 158 
AA5 1 ILE B 66  ? PRO B 69  ? ILE B 85  PRO B 88  
AA5 2 GLU B 49  ? LEU B 56  ? GLU B 68  LEU B 75  
AA5 3 ALA B 34  ? ARG B 46  ? ALA B 53  ARG B 65  
AA5 4 LEU B 124 ? ILE B 126 ? LEU B 143 ILE B 145 
AA5 5 GLU B 22  ? LEU B 27  ? GLU B 41  LEU B 46  
AA5 6 ASN B 11  ? LEU B 16  ? ASN B 30  LEU B 35  
AA5 7 VAL B 96  ? MET B 103 ? VAL B 115 MET B 122 
AA5 8 ALA B 106 ? THR B 115 ? ALA B 125 THR B 134 
AA5 9 ALA B 34  ? ARG B 46  ? ALA B 53  ARG B 65  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 8   ? N TYR A 27  O ASP A 139 ? O ASP A 158 
AA2 1 2 O ARG A 68  ? O ARG A 87  N VAL A 52  ? N VAL A 71  
AA2 2 3 O TRP A 51  ? O TRP A 70  N PHE A 44  ? N PHE A 63  
AA2 3 4 N ALA A 38  ? N ALA A 57  O THR A 115 ? O THR A 134 
AA2 4 5 O ILE A 110 ? O ILE A 129 N LEU A 99  ? N LEU A 118 
AA2 5 6 O VAL A 96  ? O VAL A 115 N ARG A 72  ? N ARG A 91  
AA3 1 2 O ARG A 68  ? O ARG A 87  N VAL A 52  ? N VAL A 71  
AA3 2 3 O TRP A 51  ? O TRP A 70  N PHE A 44  ? N PHE A 63  
AA3 3 4 N SER A 35  ? N SER A 54  O LEU A 125 ? O LEU A 144 
AA3 4 5 O ILE A 126 ? O ILE A 145 N LYS A 26  ? N LYS A 45  
AA3 5 6 O ALA A 25  ? O ALA A 44  N GLU A 12  ? N GLU A 31  
AA3 6 7 N ALA A 15  ? N ALA A 34  O CYS A 102 ? O CYS A 121 
AA3 7 8 O VAL A 96  ? O VAL A 115 N ARG A 72  ? N ARG A 91  
AA4 1 2 N TYR B 8   ? N TYR B 27  O ASP B 139 ? O ASP B 158 
AA5 1 2 O ILE B 66  ? O ILE B 85  N PHE B 54  ? N PHE B 73  
AA5 2 3 O TRP B 51  ? O TRP B 70  N PHE B 44  ? N PHE B 63  
AA5 3 4 N SER B 35  ? N SER B 54  O LEU B 125 ? O LEU B 144 
AA5 4 5 O ILE B 126 ? O ILE B 145 N LYS B 26  ? N LYS B 45  
AA5 5 6 O ALA B 25  ? O ALA B 44  N GLU B 12  ? N GLU B 31  
AA5 6 7 N ALA B 15  ? N ALA B 34  O CYS B 102 ? O CYS B 121 
AA5 7 8 N LEU B 99  ? N LEU B 118 O ILE B 110 ? O ILE B 129 
AA5 8 9 O THR B 115 ? O THR B 134 N ALA B 38  ? N ALA B 57  
# 
_pdbx_entry_details.entry_id                   9G58 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASP A 135 ? ? -89.67  36.52  
2 1 GLN A 140 ? ? -59.19  179.64 
3 1 ALA A 169 ? ? -145.34 56.96  
4 1 ALA B 112 ? ? -152.83 82.75  
5 1 ALA B 169 ? ? -145.21 57.88  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -y,x,z+1/4  
3 y,-x,z+3/4  
4 -x,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -33.671404961  28.0919881157 2.91574738868 0.532193975616 ? 0.0424646630675   ? -0.118737759618  ? 
0.592155405386 ? -0.0482140343692  ? 0.42097392415  ? 8.34683308987 ? -0.0789611978175 ? 2.79367658679  ? 5.74118427613 ? 
0.249466057579 ? 5.44209219743 ? -0.120315313888   ? -0.135471975932 ? 0.0811489611754 ? -0.622911449851 ? -0.152368386459  ? 
0.658646212731  ? -0.236717107087  ? -1.06180137863  ? 0.220808856878  ? 
2 'X-RAY DIFFRACTION' ? refined -22.6065858882 24.5768362295 6.96202795211 0.489151402027 ? -0.0792147851344  ? -0.0815429938082 ? 
0.407090984449 ? 0.0767175715817   ? 0.469632221742 ? 7.68923404255 ? -1.79529990086   ? 0.310652190498 ? 9.34987878006 ? 
1.22581185284  ? 3.5505175583  ? 0.169895186033    ? 0.0637580152136 ? -0.553309138258 ? -0.539720496599 ? 0.081476302307   ? 
0.391266393963  ? -0.0755492059165 ? -0.437393998615 ? -0.255586207508 ? 
3 'X-RAY DIFFRACTION' ? refined -3.7883750445  31.9338240097 5.14232113989 0.478704601123 ? 0.023978521593    ? -0.0664762143238 ? 
0.36451423974  ? -0.00490950602397 ? 0.502268784169 ? 4.19288599507 ? 1.19202293661    ? -4.09312064901 ? 4.82973256436 ? 
0.710511720543 ? 4.77070587297 ? 0.171194474105    ? -0.147513731898 ? 0.0650162259914 ? 0.0987021453333 ? 0.102316494103   ? 
-0.54180164756  ? -0.429692162251  ? 0.485704944637  ? -0.391269291979 ? 
4 'X-RAY DIFFRACTION' ? refined 6.00622817167  29.240298871  -6.8825776285 0.49374756749  ? 0.113479721403    ? -0.0894601492452 ? 
0.510453080597 ? -0.0119077651495  ? 0.516079860035 ? 5.79185518745 ? 0.443856866344   ? -4.45592799589 ? 2.59438156854 ? 
0.802141998751 ? 6.86570933468 ? -0.00976172506423 ? 0.231389827793  ? 0.189704789632  ? -0.400308116711 ? -0.0586159589658 ? 
0.0048195020514 ? 0.145774465098   ? 0.334739622865  ? 0.0326017826654 ? 
5 'X-RAY DIFFRACTION' ? refined -5.82342011826 32.0510477839 5.31673378994 0.484286453228 ? -0.00150891291219 ? -0.144006583665  ? 
0.39576121812  ? -0.00504973128128 ? 0.471985865166 ? 9.19521650983 ? 0.82066895593    ? -4.47224815206 ? 5.48178522835 ? 
3.10606520287  ? 6.37392766676 ? -0.10055421916    ? 0.199561150189  ? 0.318350956173  ? -0.424779045136 ? 0.292349858492   ? 
-0.133357276569 ? -0.27189005066   ? -0.201280453436 ? -0.160710370758 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 A 1  A 23  ? A 96  A 135 ? ? '(chain A and resid 23:135)'  
2 'X-RAY DIFFRACTION' 2 A 97 A 136 ? A 131 A 170 ? ? '(chain A and resid 136:170)' 
3 'X-RAY DIFFRACTION' 3 B 1  B 23  ? B 32  B 54  ? ? '(chain B and resid 23:54)'   
4 'X-RAY DIFFRACTION' 4 B 33 B 55  ? B 92  B 134 ? ? '(chain B and resid 55:134)'  
5 'X-RAY DIFFRACTION' 5 B 93 B 135 ? B 128 B 170 ? ? '(chain B and resid 135:170)' 
# 
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 ALA 20  ? A ALA 1   
2  1 Y 1 A ALA 21  ? A ALA 2   
3  1 Y 1 A GLY 22  ? A GLY 3   
4  1 Y 1 A ILE 95  ? A ILE 76  
5  1 Y 1 A LYS 96  ? A LYS 77  
6  1 Y 1 A ARG 97  ? A ARG 78  
7  1 Y 1 A ARG 98  ? A ARG 79  
8  1 Y 1 A ALA 99  ? A ALA 80  
9  1 Y 1 A GLY 100 ? A GLY 81  
10 1 Y 1 A ASP 101 ? A ASP 82  
11 1 Y 1 A TYR 102 ? A TYR 83  
12 1 Y 1 A ASP 103 ? A ASP 84  
13 1 Y 1 A PRO 104 ? A PRO 85  
14 1 Y 1 A GLU 105 ? A GLU 86  
15 1 Y 1 A GLU 106 ? A GLU 87  
16 1 Y 1 A GLY 107 ? A GLY 88  
17 1 Y 1 A LYS 108 ? A LYS 89  
18 1 Y 1 A LYS 109 ? A LYS 90  
19 1 Y 1 A TYR 110 ? A TYR 91  
20 1 Y 1 A THR 111 ? A THR 92  
21 1 Y 1 A ALA 171 ? A ALA 152 
22 1 Y 1 A ILE 172 ? A ILE 153 
23 1 Y 1 A ALA 173 ? A ALA 154 
24 1 Y 1 A ALA 174 ? A ALA 155 
25 1 Y 1 A HIS 175 ? A HIS 156 
26 1 Y 1 A THR 176 ? A THR 157 
27 1 Y 1 A ALA 177 ? A ALA 158 
28 1 Y 1 A GLU 178 ? A GLU 159 
29 1 Y 1 B ALA 20  ? B ALA 1   
30 1 Y 1 B ALA 21  ? B ALA 2   
31 1 Y 1 B GLY 22  ? B GLY 3   
32 1 Y 1 B ARG 91  ? B ARG 72  
33 1 Y 1 B VAL 92  ? B VAL 73  
34 1 Y 1 B SER 93  ? B SER 74  
35 1 Y 1 B LYS 94  ? B LYS 75  
36 1 Y 1 B ILE 95  ? B ILE 76  
37 1 Y 1 B LYS 96  ? B LYS 77  
38 1 Y 1 B ARG 97  ? B ARG 78  
39 1 Y 1 B ARG 98  ? B ARG 79  
40 1 Y 1 B ALA 99  ? B ALA 80  
41 1 Y 1 B GLY 100 ? B GLY 81  
42 1 Y 1 B ASP 101 ? B ASP 82  
43 1 Y 1 B TYR 102 ? B TYR 83  
44 1 Y 1 B ASP 103 ? B ASP 84  
45 1 Y 1 B PRO 104 ? B PRO 85  
46 1 Y 1 B GLU 105 ? B GLU 86  
47 1 Y 1 B GLU 106 ? B GLU 87  
48 1 Y 1 B GLY 107 ? B GLY 88  
49 1 Y 1 B LYS 108 ? B LYS 89  
50 1 Y 1 B LYS 109 ? B LYS 90  
51 1 Y 1 B TYR 110 ? B TYR 91  
52 1 Y 1 B ALA 171 ? B ALA 152 
53 1 Y 1 B ILE 172 ? B ILE 153 
54 1 Y 1 B ALA 173 ? B ALA 154 
55 1 Y 1 B ALA 174 ? B ALA 155 
56 1 Y 1 B HIS 175 ? B HIS 156 
57 1 Y 1 B THR 176 ? B THR 157 
58 1 Y 1 B ALA 177 ? B ALA 158 
59 1 Y 1 B GLU 178 ? B GLU 159 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' R01AI114261 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' R01AI168017 2 
# 
_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   2pma 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41' 
_space_group.name_Hall        'P 4w' 
_space_group.IT_number        76 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9G58 
_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]   0.011106 
_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]   0.011106 
_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]   0.026906 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU A 1 4   ? -20.10120 31.21126 23.31384  1.000 100.60929 ? 23  GLU A N   1 
ATOM   2    C CA  . GLU A 1 4   ? -21.05353 30.34937 22.62041  1.000 103.15776 ? 23  GLU A CA  1 
ATOM   3    C C   . GLU A 1 4   ? -20.47954 29.84577 21.29818  1.000 92.24124  ? 23  GLU A C   1 
ATOM   4    O O   . GLU A 1 4   ? -21.22028 29.43454 20.40528  1.000 87.01292  ? 23  GLU A O   1 
ATOM   5    C CB  . GLU A 1 4   ? -22.36911 31.09375 22.37399  1.000 94.79122  ? 23  GLU A CB  1 
ATOM   6    N N   . LYS A 1 5   ? -19.15327 29.87192 21.18672  1.000 89.06817  ? 24  LYS A N   1 
ATOM   7    C CA  . LYS A 1 5   ? -18.46275 29.45320 19.96994  1.000 85.11597  ? 24  LYS A CA  1 
ATOM   8    C C   . LYS A 1 5   ? -18.47030 27.93151 19.86284  1.000 78.19700  ? 24  LYS A C   1 
ATOM   9    O O   . LYS A 1 5   ? -17.76858 27.24263 20.61078  1.000 81.94301  ? 24  LYS A O   1 
ATOM   10   C CB  . LYS A 1 5   ? -17.03884 30.00221 19.94838  1.000 80.20948  ? 24  LYS A CB  1 
ATOM   11   C CG  . LYS A 1 5   ? -16.96268 31.49080 19.64448  1.000 78.76588  ? 24  LYS A CG  1 
ATOM   12   C CD  . LYS A 1 5   ? -17.56380 31.80124 18.27999  1.000 79.63357  ? 24  LYS A CD  1 
ATOM   13   C CE  . LYS A 1 5   ? -17.77435 33.29716 18.08520  1.000 82.27770  ? 24  LYS A CE  1 
ATOM   14   N NZ  . LYS A 1 5   ? -16.50823 34.07066 18.21199  1.000 77.31377  ? 24  LYS A NZ  1 
ATOM   15   N N   . THR A 1 6   ? -19.26882 27.40869 18.93715  1.000 71.44582  ? 25  THR A N   1 
ATOM   16   C CA  . THR A 1 6   ? -19.42304 25.97513 18.73500  1.000 72.43045  ? 25  THR A CA  1 
ATOM   17   C C   . THR A 1 6   ? -18.63495 25.56005 17.49818  1.000 64.38290  ? 25  THR A C   1 
ATOM   18   O O   . THR A 1 6   ? -18.60472 26.28522 16.50057  1.000 61.07353  ? 25  THR A O   1 
ATOM   19   C CB  . THR A 1 6   ? -20.90197 25.60760 18.56902  1.000 69.52451  ? 25  THR A CB  1 
ATOM   20   O OG1 . THR A 1 6   ? -21.65604 26.15123 19.65982  1.000 83.14182  ? 25  THR A OG1 1 
ATOM   21   C CG2 . THR A 1 6   ? -21.09374 24.09756 18.52881  1.000 61.74098  ? 25  THR A CG2 1 
ATOM   22   N N   . VAL A 1 7   ? -18.00174 24.39181 17.56328  1.000 59.23223  ? 26  VAL A N   1 
ATOM   23   C CA  . VAL A 1 7   ? -17.18220 23.89174 16.46417  1.000 55.60562  ? 26  VAL A CA  1 
ATOM   24   C C   . VAL A 1 7   ? -18.03408 23.01353 15.55580  1.000 58.99908  ? 26  VAL A C   1 
ATOM   25   O O   . VAL A 1 7   ? -18.68085 22.06582 16.01791  1.000 68.68253  ? 26  VAL A O   1 
ATOM   26   C CB  . VAL A 1 7   ? -15.96462 23.11297 16.99465  1.000 61.32281  ? 26  VAL A CB  1 
ATOM   27   C CG1 . VAL A 1 7   ? -15.20015 22.46389 15.84622  1.000 56.38810  ? 26  VAL A CG1 1 
ATOM   28   C CG2 . VAL A 1 7   ? -15.04739 24.02268 17.80210  1.000 54.41241  ? 26  VAL A CG2 1 
ATOM   29   N N   . TYR A 1 8   ? -18.04708 23.33811 14.26592  1.000 54.84462  ? 27  TYR A N   1 
ATOM   30   C CA  . TYR A 1 8   ? -18.64710 22.51144 13.22915  1.000 53.75023  ? 27  TYR A CA  1 
ATOM   31   C C   . TYR A 1 8   ? -17.56873 22.16829 12.20854  1.000 55.91441  ? 27  TYR A C   1 
ATOM   32   O O   . TYR A 1 8   ? -16.45568 22.68892 12.26705  1.000 51.13172  ? 27  TYR A O   1 
ATOM   33   C CB  . TYR A 1 8   ? -19.81974 23.22879 12.54663  1.000 51.21853  ? 27  TYR A CB  1 
ATOM   34   C CG  . TYR A 1 8   ? -20.93438 23.66770 13.47034  1.000 55.00585  ? 27  TYR A CG  1 
ATOM   35   C CD1 . TYR A 1 8   ? -21.94308 22.79035 13.84490  1.000 60.30864  ? 27  TYR A CD1 1 
ATOM   36   C CD2 . TYR A 1 8   ? -20.98132 24.96626 13.95995  1.000 58.28019  ? 27  TYR A CD2 1 
ATOM   37   C CE1 . TYR A 1 8   ? -22.96586 23.19600 14.68635  1.000 63.55250  ? 27  TYR A CE1 1 
ATOM   38   C CE2 . TYR A 1 8   ? -21.99522 25.38029 14.79974  1.000 56.16153  ? 27  TYR A CE2 1 
ATOM   39   C CZ  . TYR A 1 8   ? -22.98558 24.49325 15.15920  1.000 69.83363  ? 27  TYR A CZ  1 
ATOM   40   O OH  . TYR A 1 8   ? -23.99453 24.90981 15.99654  1.000 62.08451  ? 27  TYR A OH  1 
ATOM   41   N N   . GLY A 1 9   ? -17.91036 21.30616 11.24722  1.000 61.72235  ? 28  GLY A N   1 
ATOM   42   C CA  . GLY A 1 9   ? -16.98238 20.85445 10.23899  1.000 46.21628  ? 28  GLY A CA  1 
ATOM   43   C C   . GLY A 1 9   ? -17.25134 21.46033 8.87192   1.000 44.57756  ? 28  GLY A C   1 
ATOM   44   O O   . GLY A 1 9   ? -18.07877 22.35742 8.70749   1.000 47.38992  ? 28  GLY A O   1 
ATOM   45   N N   . LEU A 1 10  ? -16.51602 20.95295 7.87514   1.000 46.36135  ? 29  LEU A N   1 
ATOM   46   C CA  . LEU A 1 10  ? -16.73042 21.40233 6.50011   1.000 46.94055  ? 29  LEU A CA  1 
ATOM   47   C C   . LEU A 1 10  ? -18.14662 21.11708 6.02792   1.000 54.57865  ? 29  LEU A C   1 
ATOM   48   O O   . LEU A 1 10  ? -18.70468 21.88715 5.23775   1.000 51.06846  ? 29  LEU A O   1 
ATOM   49   C CB  . LEU A 1 10  ? -15.73918 20.73836 5.54531   1.000 44.22793  ? 29  LEU A CB  1 
ATOM   50   C CG  . LEU A 1 10  ? -14.27722 21.16983 5.60377   1.000 65.30313  ? 29  LEU A CG  1 
ATOM   51   C CD1 . LEU A 1 10  ? -13.44073 20.37540 4.61097   1.000 47.60373  ? 29  LEU A CD1 1 
ATOM   52   C CD2 . LEU A 1 10  ? -14.16005 22.66624 5.34037   1.000 56.27759  ? 29  LEU A CD2 1 
ATOM   53   N N   . ASN A 1 11  ? -18.73325 20.01141 6.47718   1.000 56.46762  ? 30  ASN A N   1 
ATOM   54   C CA  . ASN A 1 11  ? -20.08769 19.64153 6.10501   1.000 53.61239  ? 30  ASN A CA  1 
ATOM   55   C C   . ASN A 1 11  ? -20.86646 19.25332 7.35008   1.000 55.00046  ? 30  ASN A C   1 
ATOM   56   O O   . ASN A 1 11  ? -20.32866 18.60933 8.25457   1.000 57.37589  ? 30  ASN A O   1 
ATOM   57   C CB  . ASN A 1 11  ? -20.08755 18.48005 5.10587   1.000 53.36950  ? 30  ASN A CB  1 
ATOM   58   C CG  . ASN A 1 11  ? -19.40674 18.83574 3.80152   1.000 55.72807  ? 30  ASN A CG  1 
ATOM   59   O OD1 . ASN A 1 11  ? -18.28873 18.39896 3.53271   1.000 62.37838  ? 30  ASN A OD1 1 
ATOM   60   N ND2 . ASN A 1 11  ? -20.07843 19.63409 2.98262   1.000 59.08953  ? 30  ASN A ND2 1 
ATOM   61   N N   . GLU A 1 12  ? -22.13120 19.65903 7.39593   1.000 53.74708  ? 31  GLU A N   1 
ATOM   62   C CA  . GLU A 1 12  ? -23.01376 19.30146 8.49685   1.000 55.08734  ? 31  GLU A CA  1 
ATOM   63   C C   . GLU A 1 12  ? -24.38738 18.97796 7.93108   1.000 64.43160  ? 31  GLU A C   1 
ATOM   64   O O   . GLU A 1 12  ? -24.66794 19.20435 6.75290   1.000 57.90138  ? 31  GLU A O   1 
ATOM   65   C CB  . GLU A 1 12  ? -23.11399 20.41666 9.54797   1.000 52.93682  ? 31  GLU A CB  1 
ATOM   66   C CG  . GLU A 1 12  ? -21.81613 20.74756 10.26323  1.000 55.44175  ? 31  GLU A CG  1 
ATOM   67   C CD  . GLU A 1 12  ? -21.36244 19.65733 11.21550  1.000 59.15352  ? 31  GLU A CD  1 
ATOM   68   O OE1 . GLU A 1 12  ? -22.19094 18.81054 11.60602  1.000 60.96645  ? 31  GLU A OE1 1 
ATOM   69   O OE2 . GLU A 1 12  ? -20.16856 19.64900 11.57857  1.000 63.57240  ? 31  GLU A OE2 1 
ATOM   70   N N   . TYR A 1 13  ? -25.24441 18.41678 8.77334   1.000 56.83625  ? 32  TYR A N   1 
ATOM   71   C CA  . TYR A 1 13  ? -26.64487 18.23510 8.42853   1.000 61.25462  ? 32  TYR A CA  1 
ATOM   72   C C   . TYR A 1 13  ? -27.45361 19.35871 9.05608   1.000 61.99905  ? 32  TYR A C   1 
ATOM   73   O O   . TYR A 1 13  ? -27.29598 19.65330 10.24514  1.000 71.47422  ? 32  TYR A O   1 
ATOM   74   C CB  . TYR A 1 13  ? -27.14932 16.86367 8.87753   1.000 64.98686  ? 32  TYR A CB  1 
ATOM   75   C CG  . TYR A 1 13  ? -26.64577 15.76849 7.96815   1.000 58.85724  ? 32  TYR A CG  1 
ATOM   76   C CD1 . TYR A 1 13  ? -26.96899 15.76010 6.61802   1.000 61.46820  ? 32  TYR A CD1 1 
ATOM   77   C CD2 . TYR A 1 13  ? -25.81739 14.76571 8.44831   1.000 62.86509  ? 32  TYR A CD2 1 
ATOM   78   C CE1 . TYR A 1 13  ? -26.49352 14.77402 5.77488   1.000 61.07396  ? 32  TYR A CE1 1 
ATOM   79   C CE2 . TYR A 1 13  ? -25.33847 13.77802 7.61256   1.000 60.84496  ? 32  TYR A CE2 1 
ATOM   80   C CZ  . TYR A 1 13  ? -25.67901 13.78885 6.27730   1.000 59.93191  ? 32  TYR A CZ  1 
ATOM   81   O OH  . TYR A 1 13  ? -25.20431 12.80485 5.44164   1.000 79.93332  ? 32  TYR A OH  1 
ATOM   82   N N   . ALA A 1 14  ? -28.28277 20.00683 8.24636   1.000 57.77946  ? 33  ALA A N   1 
ATOM   83   C CA  . ALA A 1 14  ? -29.14568 21.08371 8.69735   1.000 65.11347  ? 33  ALA A CA  1 
ATOM   84   C C   . ALA A 1 14  ? -30.60144 20.75241 8.39928   1.000 70.96716  ? 33  ALA A C   1 
ATOM   85   O O   . ALA A 1 14  ? -30.91322 19.98424 7.47953   1.000 61.65647  ? 33  ALA A O   1 
ATOM   86   C CB  . ALA A 1 14  ? -28.76912 22.41148 8.03324   1.000 60.02388  ? 33  ALA A CB  1 
ATOM   87   N N   . ALA A 1 15  ? -31.48566 21.32647 9.21028   1.000 62.85607  ? 34  ALA A N   1 
ATOM   88   C CA  . ALA A 1 15  ? -32.92465 21.18065 9.05010   1.000 65.98433  ? 34  ALA A CA  1 
ATOM   89   C C   . ALA A 1 15  ? -33.59253 22.54732 9.00228   1.000 73.07741  ? 34  ALA A C   1 
ATOM   90   O O   . ALA A 1 15  ? -33.26413 23.43911 9.78688   1.000 67.66448  ? 34  ALA A O   1 
ATOM   91   C CB  . ALA A 1 15  ? -33.53542 20.34556 10.18208  1.000 65.75901  ? 34  ALA A CB  1 
ATOM   92   N N   . LEU A 1 16  ? -34.52204 22.71248 8.07091   1.000 70.77731  ? 35  LEU A N   1 
ATOM   93   C CA  . LEU A 1 16  ? -35.37698 23.89392 8.04044   1.000 67.58804  ? 35  LEU A CA  1 
ATOM   94   C C   . LEU A 1 16  ? -36.49355 23.67669 9.05271   1.000 67.69842  ? 35  LEU A C   1 
ATOM   95   O O   . LEU A 1 16  ? -37.29110 22.74516 8.90711   1.000 81.58403  ? 35  LEU A O   1 
ATOM   96   C CB  . LEU A 1 16  ? -35.93097 24.15809 6.64278   1.000 68.89886  ? 35  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 16  ? -34.98690 24.52605 5.49092   1.000 80.48997  ? 35  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 16  ? -34.06567 23.39057 5.05655   1.000 74.06974  ? 35  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 16  ? -35.81801 25.02687 4.31948   1.000 70.79234  ? 35  LEU A CD2 1 
ATOM   100  N N   . ASP A 1 17  ? -36.50425 24.48984 10.11184  1.000 65.07186  ? 36  ASP A N   1 
ATOM   101  C CA  . ASP A 1 17  ? -37.45571 24.32448 11.20668  1.000 73.35015  ? 36  ASP A CA  1 
ATOM   102  C C   . ASP A 1 17  ? -38.87599 24.15122 10.68727  1.000 72.42034  ? 36  ASP A C   1 
ATOM   103  O O   . ASP A 1 17  ? -39.34605 24.92170 9.84575   1.000 69.78272  ? 36  ASP A O   1 
ATOM   104  C CB  . ASP A 1 17  ? -37.39133 25.54358 12.12887  1.000 74.66800  ? 36  ASP A CB  1 
ATOM   105  C CG  . ASP A 1 17  ? -38.44341 25.50599 13.22137  1.000 88.80301  ? 36  ASP A CG  1 
ATOM   106  O OD1 . ASP A 1 17  ? -38.53795 24.47850 13.92718  1.000 93.62773  ? 36  ASP A OD1 1 
ATOM   107  O OD2 . ASP A 1 17  ? -39.18466 26.50334 13.36723  1.000 77.81823  ? 36  ASP A OD2 1 
ATOM   108  N N   . GLY A 1 18  ? -39.56094 23.13043 11.20466  1.000 65.19022  ? 37  GLY A N   1 
ATOM   109  C CA  . GLY A 1 18  ? -40.87577 22.77024 10.75253  1.000 77.15569  ? 37  GLY A CA  1 
ATOM   110  C C   . GLY A 1 18  ? -40.86819 21.67306 9.70765   1.000 78.65906  ? 37  GLY A C   1 
ATOM   111  O O   . GLY A 1 18  ? -41.84394 20.92052 9.59777   1.000 73.01080  ? 37  GLY A O   1 
ATOM   112  N N   . ILE A 1 19  ? -39.79694 21.58775 8.92242   1.000 70.25182  ? 38  ILE A N   1 
ATOM   113  C CA  . ILE A 1 19  ? -39.66116 20.60642 7.85314   1.000 79.82664  ? 38  ILE A CA  1 
ATOM   114  C C   . ILE A 1 19  ? -38.77991 19.46155 8.33259   1.000 67.76114  ? 38  ILE A C   1 
ATOM   115  O O   . ILE A 1 19  ? -37.68415 19.68704 8.86077   1.000 77.16949  ? 38  ILE A O   1 
ATOM   116  C CB  . ILE A 1 19  ? -39.08492 21.25984 6.58667   1.000 69.66271  ? 38  ILE A CB  1 
ATOM   117  C CG1 . ILE A 1 19  ? -39.92492 22.48095 6.21194   1.000 83.49559  ? 38  ILE A CG1 1 
ATOM   118  C CG2 . ILE A 1 19  ? -39.04606 20.27078 5.44334   1.000 71.96368  ? 38  ILE A CG2 1 
ATOM   119  C CD1 . ILE A 1 19  ? -39.26478 23.38601 5.21396   1.000 77.88642  ? 38  ILE A CD1 1 
ATOM   120  N N   . ASN A 1 20  ? -39.25779 18.23165 8.14325   1.000 80.17081  ? 39  ASN A N   1 
ATOM   121  C CA  . ASN A 1 20  ? -38.53114 17.02758 8.55109   1.000 79.81561  ? 39  ASN A CA  1 
ATOM   122  C C   . ASN A 1 20  ? -37.74660 16.48175 7.35673   1.000 81.31487  ? 39  ASN A C   1 
ATOM   123  O O   . ASN A 1 20  ? -38.03696 15.42319 6.79480   1.000 91.61119  ? 39  ASN A O   1 
ATOM   124  C CB  . ASN A 1 20  ? -39.49093 15.99103 9.12026   1.000 92.84209  ? 39  ASN A CB  1 
ATOM   125  C CG  . ASN A 1 20  ? -38.77262 14.77935 9.68290   1.000 96.39419  ? 39  ASN A CG  1 
ATOM   126  O OD1 . ASN A 1 20  ? -37.59048 14.84464 10.01921  1.000 92.89118  ? 39  ASN A OD1 1 
ATOM   127  N ND2 . ASN A 1 20  ? -39.48660 13.66453 9.78845   1.000 104.06341 ? 39  ASN A ND2 1 
ATOM   128  N N   . LEU A 1 21  ? -36.73572 17.25145 6.96436   1.000 74.09121  ? 40  LEU A N   1 
ATOM   129  C CA  . LEU A 1 21  ? -35.88845 16.92251 5.82681   1.000 72.36325  ? 40  LEU A CA  1 
ATOM   130  C C   . LEU A 1 21  ? -34.43453 17.14908 6.20304   1.000 74.31493  ? 40  LEU A C   1 
ATOM   131  O O   . LEU A 1 21  ? -34.09905 18.17189 6.80658   1.000 68.24127  ? 40  LEU A O   1 
ATOM   132  C CB  . LEU A 1 21  ? -36.24489 17.76202 4.59394   1.000 65.77576  ? 40  LEU A CB  1 
ATOM   133  C CG  . LEU A 1 21  ? -37.53676 17.39716 3.86403   1.000 79.75007  ? 40  LEU A CG  1 
ATOM   134  C CD1 . LEU A 1 21  ? -37.66156 18.19246 2.57611   1.000 71.78564  ? 40  LEU A CD1 1 
ATOM   135  C CD2 . LEU A 1 21  ? -37.58973 15.90610 3.58475   1.000 82.91602  ? 40  LEU A CD2 1 
ATOM   136  N N   . GLU A 1 22  ? -33.58017 16.19144 5.85773   1.000 78.52937  ? 41  GLU A N   1 
ATOM   137  C CA  . GLU A 1 22  ? -32.14838 16.31618 6.08909   1.000 75.21491  ? 41  GLU A CA  1 
ATOM   138  C C   . GLU A 1 22  ? -31.54271 17.06316 4.91384   1.000 73.98370  ? 41  GLU A C   1 
ATOM   139  O O   . GLU A 1 22  ? -31.71965 16.65761 3.75993   1.000 84.73237  ? 41  GLU A O   1 
ATOM   140  C CB  . GLU A 1 22  ? -31.46894 14.95588 6.20862   1.000 83.01372  ? 41  GLU A CB  1 
ATOM   141  C CG  . GLU A 1 22  ? -32.05320 13.99919 7.20160   1.000 95.58453  ? 41  GLU A CG  1 
ATOM   142  C CD  . GLU A 1 22  ? -31.45441 12.62368 7.03111   1.000 105.59535 ? 41  GLU A CD  1 
ATOM   143  O OE1 . GLU A 1 22  ? -30.89305 12.36592 5.94542   1.000 107.32329 ? 41  GLU A OE1 1 
ATOM   144  O OE2 . GLU A 1 22  ? -31.52791 11.80667 7.97023   1.000 116.17392 ? 41  GLU A OE2 1 
ATOM   145  N N   . VAL A 1 23  ? -30.83517 18.14978 5.19643   1.000 61.60305  ? 42  VAL A N   1 
ATOM   146  C CA  . VAL A 1 23  ? -30.15267 18.89970 4.15545   1.000 66.57761  ? 42  VAL A CA  1 
ATOM   147  C C   . VAL A 1 23  ? -28.65832 18.82236 4.42477   1.000 69.45125  ? 42  VAL A C   1 
ATOM   148  O O   . VAL A 1 23  ? -28.21196 19.03618 5.55692   1.000 61.66083  ? 42  VAL A O   1 
ATOM   149  C CB  . VAL A 1 23  ? -30.63436 20.35999 4.10993   1.000 65.12188  ? 42  VAL A CB  1 
ATOM   150  C CG1 . VAL A 1 23  ? -29.94775 21.10719 2.98716   1.000 64.48862  ? 42  VAL A CG1 1 
ATOM   151  C CG2 . VAL A 1 23  ? -32.14529 20.40444 3.94330   1.000 73.64907  ? 42  VAL A CG2 1 
ATOM   152  N N   . ALA A 1 24  ? -27.88728 18.54176 3.38178   1.000 62.64233  ? 43  ALA A N   1 
ATOM   153  C CA  . ALA A 1 24  ? -26.43840 18.56185 3.49171   1.000 58.57021  ? 43  ALA A CA  1 
ATOM   154  C C   . ALA A 1 24  ? -25.95808 19.99197 3.31088   1.000 55.73664  ? 43  ALA A C   1 
ATOM   155  O O   . ALA A 1 24  ? -26.24842 20.62505 2.29044   1.000 64.62237  ? 43  ALA A O   1 
ATOM   156  C CB  . ALA A 1 24  ? -25.80844 17.63551 2.45440   1.000 59.36789  ? 43  ALA A CB  1 
ATOM   157  N N   . ALA A 1 25  ? -25.22107 20.50045 4.28881   1.000 60.93676  ? 44  ALA A N   1 
ATOM   158  C CA  . ALA A 1 25  ? -24.74878 21.87134 4.28019   1.000 55.86613  ? 44  ALA A CA  1 
ATOM   159  C C   . ALA A 1 25  ? -23.23553 21.86338 4.16804   1.000 57.25537  ? 44  ALA A C   1 
ATOM   160  O O   . ALA A 1 25  ? -22.55863 21.12914 4.89708   1.000 60.92245  ? 44  ALA A O   1 
ATOM   161  C CB  . ALA A 1 25  ? -25.18794 22.61691 5.54257   1.000 60.04553  ? 44  ALA A CB  1 
ATOM   162  N N   . LYS A 1 26  ? -22.71965 22.66466 3.24330   1.000 64.19041  ? 45  LYS A N   1 
ATOM   163  C CA  . LYS A 1 26  ? -21.29360 22.90987 3.10617   1.000 55.57589  ? 45  LYS A CA  1 
ATOM   164  C C   . LYS A 1 26  ? -20.98518 24.23503 3.78843   1.000 55.88128  ? 45  LYS A C   1 
ATOM   165  O O   . LYS A 1 26  ? -21.52504 25.27637 3.39971   1.000 51.84558  ? 45  LYS A O   1 
ATOM   166  C CB  . LYS A 1 26  ? -20.89117 22.93701 1.63228   1.000 53.14324  ? 45  LYS A CB  1 
ATOM   167  C CG  . LYS A 1 26  ? -19.44218 23.28860 1.37650   1.000 58.48574  ? 45  LYS A CG  1 
ATOM   168  C CD  . LYS A 1 26  ? -19.15799 23.32643 -0.11482  1.000 60.77378  ? 45  LYS A CD  1 
ATOM   169  C CE  . LYS A 1 26  ? -17.66814 23.24624 -0.39445  1.000 59.49675  ? 45  LYS A CE  1 
ATOM   170  N NZ  . LYS A 1 26  ? -17.37072 23.38428 -1.84673  1.000 65.87714  ? 45  LYS A NZ  1 
ATOM   171  N N   . LEU A 1 27  ? -20.12437 24.19697 4.80045   1.000 57.78409  ? 46  LEU A N   1 
ATOM   172  C CA  . LEU A 1 27  ? -19.77764 25.39021 5.56489   1.000 50.96944  ? 46  LEU A CA  1 
ATOM   173  C C   . LEU A 1 27  ? -18.62862 26.08743 4.84872   1.000 50.33754  ? 46  LEU A C   1 
ATOM   174  O O   . LEU A 1 27  ? -17.49088 25.60619 4.86499   1.000 53.07294  ? 46  LEU A O   1 
ATOM   175  C CB  . LEU A 1 27  ? -19.41950 25.03147 7.00446   1.000 48.69191  ? 46  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 27  ? -20.59764 24.76028 7.94882   1.000 52.35959  ? 46  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 27  ? -21.35851 23.48429 7.59570   1.000 53.32944  ? 46  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 27  ? -20.11571 24.71029 9.38255   1.000 53.57241  ? 46  LEU A CD2 1 
ATOM   179  N N   . ASP A 1 28  ? -18.93220 27.22392 4.22710   1.000 46.94167  ? 47  ASP A N   1 
ATOM   180  C CA  . ASP A 1 28  ? -18.04908 27.89799 3.27879   1.000 48.72251  ? 47  ASP A CA  1 
ATOM   181  C C   . ASP A 1 28  ? -17.71171 29.27994 3.82855   1.000 48.34480  ? 47  ASP A C   1 
ATOM   182  O O   . ASP A 1 28  ? -18.49527 30.22212 3.67911   1.000 51.80271  ? 47  ASP A O   1 
ATOM   183  C CB  . ASP A 1 28  ? -18.72740 27.98422 1.91147   1.000 48.45533  ? 47  ASP A CB  1 
ATOM   184  C CG  . ASP A 1 28  ? -17.83471 28.57596 0.83885   1.000 51.12489  ? 47  ASP A CG  1 
ATOM   185  O OD1 . ASP A 1 28  ? -16.70077 29.00075 1.15053   1.000 59.43518  ? 47  ASP A OD1 1 
ATOM   186  O OD2 . ASP A 1 28  ? -18.28272 28.62252 -0.32789  1.000 57.37407  ? 47  ASP A OD2 1 
ATOM   187  N N   . THR A 1 29  ? -16.53613 29.40227 4.44795   1.000 46.50937  ? 48  THR A N   1 
ATOM   188  C CA  . THR A 1 29  ? -16.08436 30.68670 4.96714   1.000 43.70815  ? 48  THR A CA  1 
ATOM   189  C C   . THR A 1 29  ? -15.62669 31.63553 3.86772   1.000 48.16808  ? 48  THR A C   1 
ATOM   190  O O   . THR A 1 29  ? -15.41661 32.81972 4.14675   1.000 58.88800  ? 48  THR A O   1 
ATOM   191  C CB  . THR A 1 29  ? -14.95573 30.48574 5.97986   1.000 46.72442  ? 48  THR A CB  1 
ATOM   192  O OG1 . THR A 1 29  ? -13.83016 29.87940 5.33355   1.000 43.36618  ? 48  THR A OG1 1 
ATOM   193  C CG2 . THR A 1 29  ? -15.42156 29.58864 7.11721   1.000 39.05910  ? 48  THR A CG2 1 
ATOM   194  N N   . GLY A 1 30  ? -15.43662 31.14631 2.64306   1.000 47.40460  ? 49  GLY A N   1 
ATOM   195  C CA  . GLY A 1 30  ? -15.07275 32.00795 1.53387   1.000 49.62818  ? 49  GLY A CA  1 
ATOM   196  C C   . GLY A 1 30  ? -16.21859 32.77072 0.90166   1.000 55.42896  ? 49  GLY A C   1 
ATOM   197  O O   . GLY A 1 30  ? -15.97475 33.71186 0.13999   1.000 55.79789  ? 49  GLY A O   1 
ATOM   198  N N   . ALA A 1 31  ? -17.45741 32.39130 1.19410   1.000 52.46405  ? 50  ALA A N   1 
ATOM   199  C CA  . ALA A 1 31  ? -18.63420 33.08439 0.69289   1.000 59.46400  ? 50  ALA A CA  1 
ATOM   200  C C   . ALA A 1 31  ? -19.29480 33.85483 1.82599   1.000 55.63110  ? 50  ALA A C   1 
ATOM   201  O O   . ALA A 1 31  ? -19.37927 33.36358 2.95601   1.000 51.72162  ? 50  ALA A O   1 
ATOM   202  C CB  . ALA A 1 31  ? -19.63408 32.10217 0.07599   1.000 54.08670  ? 50  ALA A CB  1 
ATOM   203  N N   . LYS A 1 32  ? -19.76554 35.06350 1.51934   1.000 53.63180  ? 51  LYS A N   1 
ATOM   204  C CA  . LYS A 1 32  ? -20.41967 35.87399 2.53896   1.000 52.63808  ? 51  LYS A CA  1 
ATOM   205  C C   . LYS A 1 32  ? -21.86646 35.44056 2.74708   1.000 57.14338  ? 51  LYS A C   1 
ATOM   206  O O   . LYS A 1 32  ? -22.30785 35.25487 3.88614   1.000 53.49449  ? 51  LYS A O   1 
ATOM   207  C CB  . LYS A 1 32  ? -20.34531 37.35523 2.16196   1.000 52.91088  ? 51  LYS A CB  1 
ATOM   208  C CG  . LYS A 1 32  ? -18.92970 37.90688 2.11498   1.000 63.34072  ? 51  LYS A CG  1 
ATOM   209  C CD  . LYS A 1 32  ? -18.91905 39.39512 1.79642   1.000 66.05462  ? 51  LYS A CD  1 
ATOM   210  C CE  . LYS A 1 32  ? -19.83488 40.17621 2.73135   1.000 85.80131  ? 51  LYS A CE  1 
ATOM   211  N NZ  . LYS A 1 32  ? -19.44515 40.03311 4.16426   1.000 87.03501  ? 51  LYS A NZ  1 
ATOM   212  N N   . THR A 1 33  ? -22.61153 35.25933 1.66198   1.000 63.64415  ? 52  THR A N   1 
ATOM   213  C CA  . THR A 1 33  ? -24.03393 34.96715 1.74484   1.000 61.08595  ? 52  THR A CA  1 
ATOM   214  C C   . THR A 1 33  ? -24.29376 33.46353 1.69227   1.000 63.99422  ? 52  THR A C   1 
ATOM   215  O O   . THR A 1 33  ? -23.49719 32.68355 1.16478   1.000 67.22678  ? 52  THR A O   1 
ATOM   216  C CB  . THR A 1 33  ? -24.78843 35.66675 0.61455   1.000 65.39247  ? 52  THR A CB  1 
ATOM   217  O OG1 . THR A 1 33  ? -24.22474 35.28001 -0.64431  1.000 68.43275  ? 52  THR A OG1 1 
ATOM   218  C CG2 . THR A 1 33  ? -24.67155 37.17833 0.76239   1.000 60.84445  ? 52  THR A CG2 1 
ATOM   219  N N   . ALA A 1 34  ? -25.43070 33.06606 2.25648   1.000 63.33475  ? 53  ALA A N   1 
ATOM   220  C CA  . ALA A 1 34  ? -25.85301 31.67436 2.27556   1.000 52.90880  ? 53  ALA A CA  1 
ATOM   221  C C   . ALA A 1 34  ? -26.78009 31.37592 1.10343   1.000 64.44058  ? 53  ALA A C   1 
ATOM   222  O O   . ALA A 1 34  ? -27.50291 32.25090 0.62129   1.000 61.61610  ? 53  ALA A O   1 
ATOM   223  C CB  . ALA A 1 34  ? -26.55514 31.34170 3.59234   1.000 49.37088  ? 53  ALA A CB  1 
ATOM   224  N N   . SER A 1 35  ? -26.76221 30.11893 0.65351   1.000 56.91270  ? 54  SER A N   1 
ATOM   225  C CA  . SER A 1 35  ? -27.54923 29.68833 -0.49497  1.000 54.30798  ? 54  SER A CA  1 
ATOM   226  C C   . SER A 1 35  ? -28.29485 28.39939 -0.18088  1.000 65.45430  ? 54  SER A C   1 
ATOM   227  O O   . SER A 1 35  ? -27.76554 27.50779 0.48946   1.000 56.54715  ? 54  SER A O   1 
ATOM   228  C CB  . SER A 1 35  ? -26.66770 29.47594 -1.72772  1.000 57.87484  ? 54  SER A CB  1 
ATOM   229  O OG  . SER A 1 35  ? -26.12678 30.70083 -2.18467  1.000 82.12536  ? 54  SER A OG  1 
ATOM   230  N N   . LEU A 1 36  ? -29.51841 28.29927 -0.69522  1.000 59.04937  ? 55  LEU A N   1 
ATOM   231  C CA  . LEU A 1 36  ? -30.35215 27.11547 -0.54239  1.000 49.67597  ? 55  LEU A CA  1 
ATOM   232  C C   . LEU A 1 36  ? -30.79812 26.67229 -1.92452  1.000 55.55546  ? 55  LEU A C   1 
ATOM   233  O O   . LEU A 1 36  ? -31.38199 27.46364 -2.67391  1.000 63.07188  ? 55  LEU A O   1 
ATOM   234  C CB  . LEU A 1 36  ? -31.56520 27.40041 0.34499   1.000 53.23987  ? 55  LEU A CB  1 
ATOM   235  C CG  . LEU A 1 36  ? -32.49450 26.20981 0.58337   1.000 62.35957  ? 55  LEU A CG  1 
ATOM   236  C CD1 . LEU A 1 36  ? -31.78281 25.14091 1.39559   1.000 59.38625  ? 55  LEU A CD1 1 
ATOM   237  C CD2 . LEU A 1 36  ? -33.78071 26.64753 1.26361   1.000 53.64230  ? 55  LEU A CD2 1 
ATOM   238  N N   . SER A 1 37  ? -30.51431 25.41843 -2.26386  1.000 56.62579  ? 56  SER A N   1 
ATOM   239  C CA  . SER A 1 37  ? -30.91591 24.87835 -3.55365  1.000 72.35972  ? 56  SER A CA  1 
ATOM   240  C C   . SER A 1 37  ? -32.41289 24.59794 -3.52696  1.000 72.79275  ? 56  SER A C   1 
ATOM   241  O O   . SER A 1 37  ? -32.89331 23.83188 -2.68419  1.000 68.00567  ? 56  SER A O   1 
ATOM   242  C CB  . SER A 1 37  ? -30.12187 23.61565 -3.87587  1.000 66.43890  ? 56  SER A CB  1 
ATOM   243  O OG  . SER A 1 37  ? -30.35610 23.19635 -5.20949  1.000 81.11375  ? 56  SER A OG  1 
ATOM   244  N N   . ALA A 1 38  ? -33.14789 25.21376 -4.44716  1.000 67.85563  ? 57  ALA A N   1 
ATOM   245  C CA  . ALA A 1 38  ? -34.59616 25.11533 -4.46779  1.000 70.08456  ? 57  ALA A CA  1 
ATOM   246  C C   . ALA A 1 38  ? -35.05989 24.68315 -5.84941  1.000 68.26058  ? 57  ALA A C   1 
ATOM   247  O O   . ALA A 1 38  ? -34.32596 24.77859 -6.83629  1.000 74.46660  ? 57  ALA A O   1 
ATOM   248  C CB  . ALA A 1 38  ? -35.25646 26.44762 -4.08312  1.000 70.36460  ? 57  ALA A CB  1 
ATOM   249  N N   . ARG A 1 39  ? -36.29817 24.20530 -5.90486  1.000 69.06099  ? 58  ARG A N   1 
ATOM   250  C CA  . ARG A 1 39  ? -36.92316 23.79098 -7.14885  1.000 77.20640  ? 58  ARG A CA  1 
ATOM   251  C C   . ARG A 1 39  ? -38.32414 24.37469 -7.22486  1.000 82.30977  ? 58  ARG A C   1 
ATOM   252  O O   . ARG A 1 39  ? -38.99680 24.54110 -6.20339  1.000 82.31780  ? 58  ARG A O   1 
ATOM   253  C CB  . ARG A 1 39  ? -36.98038 22.26101 -7.25688  1.000 82.91108  ? 58  ARG A CB  1 
ATOM   254  C CG  . ARG A 1 39  ? -37.61170 21.59290 -6.04318  1.000 82.75597  ? 58  ARG A CG  1 
ATOM   255  C CD  . ARG A 1 39  ? -38.03296 20.16262 -6.33311  1.000 85.60864  ? 58  ARG A CD  1 
ATOM   256  N NE  . ARG A 1 39  ? -36.88515 19.28712 -6.53687  1.000 86.43520  ? 58  ARG A NE  1 
ATOM   257  C CZ  . ARG A 1 39  ? -36.57952 18.70682 -7.68979  1.000 97.36798  ? 58  ARG A CZ  1 
ATOM   258  N NH1 . ARG A 1 39  ? -37.33275 18.86778 -8.76664  1.000 91.84091  ? 58  ARG A NH1 1 
ATOM   259  N NH2 . ARG A 1 39  ? -35.49436 17.94040 -7.76250  1.000 94.56593  ? 58  ARG A NH2 1 
ATOM   260  N N   . ASP A 1 40  ? -38.75409 24.67993 -8.44835  1.000 88.35421  ? 59  ASP A N   1 
ATOM   261  C CA  . ASP A 1 40  ? -40.09804 25.18540 -8.72307  1.000 94.04245  ? 59  ASP A CA  1 
ATOM   262  C C   . ASP A 1 40  ? -40.40289 26.41697 -7.86951  1.000 93.86178  ? 59  ASP A C   1 
ATOM   263  O O   . ASP A 1 40  ? -41.38510 26.47717 -7.12750  1.000 87.32093  ? 59  ASP A O   1 
ATOM   264  C CB  . ASP A 1 40  ? -41.14158 24.08558 -8.51646  1.000 100.63764 ? 59  ASP A CB  1 
ATOM   265  C CG  . ASP A 1 40  ? -40.88682 22.87499 -9.39370  1.000 112.55299 ? 59  ASP A CG  1 
ATOM   266  O OD1 . ASP A 1 40  ? -40.74724 23.05032 -10.62254 1.000 120.76367 ? 59  ASP A OD1 1 
ATOM   267  O OD2 . ASP A 1 40  ? -40.80954 21.75143 -8.85507  1.000 110.36560 ? 59  ASP A OD2 1 
ATOM   268  N N   . ILE A 1 41  ? -39.52591 27.40769 -7.99041  1.000 88.01481  ? 60  ILE A N   1 
ATOM   269  C CA  . ILE A 1 41  ? -39.66065 28.65484 -7.24697  1.000 83.72548  ? 60  ILE A CA  1 
ATOM   270  C C   . ILE A 1 41  ? -40.74859 29.49688 -7.89879  1.000 89.24229  ? 60  ILE A C   1 
ATOM   271  O O   . ILE A 1 41  ? -40.65839 29.83834 -9.08265  1.000 95.60595  ? 60  ILE A O   1 
ATOM   272  C CB  . ILE A 1 41  ? -38.32789 29.41409 -7.20077  1.000 89.00328  ? 60  ILE A CB  1 
ATOM   273  C CG1 . ILE A 1 41  ? -37.27477 28.59339 -6.45558  1.000 78.80645  ? 60  ILE A CG1 1 
ATOM   274  C CG2 . ILE A 1 41  ? -38.50670 30.77695 -6.55119  1.000 86.09224  ? 60  ILE A CG2 1 
ATOM   275  C CD1 . ILE A 1 41  ? -35.91118 29.23840 -6.43341  1.000 70.35415  ? 60  ILE A CD1 1 
ATOM   276  N N   . LYS A 1 42  ? -41.78074 29.83173 -7.12859  1.000 91.77541  ? 61  LYS A N   1 
ATOM   277  C CA  . LYS A 1 42  ? -42.88434 30.66052 -7.60445  1.000 91.62418  ? 61  LYS A CA  1 
ATOM   278  C C   . LYS A 1 42  ? -43.00000 31.86844 -6.68526  1.000 93.53177  ? 61  LYS A C   1 
ATOM   279  O O   . LYS A 1 42  ? -43.30489 31.72337 -5.49585  1.000 93.12007  ? 61  LYS A O   1 
ATOM   280  C CB  . LYS A 1 42  ? -44.19416 29.87229 -7.64426  1.000 86.84800  ? 61  LYS A CB  1 
ATOM   281  N N   . ARG A 1 43  ? -42.74907 33.05345 -7.23323  1.000 94.47523  ? 62  ARG A N   1 
ATOM   282  C CA  . ARG A 1 43  ? -42.92783 34.29362 -6.49755  1.000 94.31260  ? 62  ARG A CA  1 
ATOM   283  C C   . ARG A 1 43  ? -44.37957 34.73114 -6.60700  1.000 92.52505  ? 62  ARG A C   1 
ATOM   284  O O   . ARG A 1 43  ? -44.99971 34.59069 -7.66427  1.000 101.41811 ? 62  ARG A O   1 
ATOM   285  C CB  . ARG A 1 43  ? -41.99867 35.37894 -7.04222  1.000 96.86337  ? 62  ARG A CB  1 
ATOM   286  C CG  . ARG A 1 43  ? -41.56340 36.40911 -6.01181  1.000 104.55006 ? 62  ARG A CG  1 
ATOM   287  C CD  . ARG A 1 43  ? -40.52646 37.36438 -6.58904  1.000 107.62043 ? 62  ARG A CD  1 
ATOM   288  N NE  . ARG A 1 43  ? -39.34508 36.66581 -7.08393  1.000 103.76178 ? 62  ARG A NE  1 
ATOM   289  C CZ  . ARG A 1 43  ? -38.29642 37.26319 -7.63475  1.000 106.36805 ? 62  ARG A CZ  1 
ATOM   290  N NH1 . ARG A 1 43  ? -37.26075 36.57047 -8.08076  1.000 104.14465 ? 62  ARG A NH1 1 
ATOM   291  N NH2 . ARG A 1 43  ? -38.28678 38.58903 -7.74178  1.000 111.43152 ? 62  ARG A NH2 1 
ATOM   292  N N   . PHE A 1 44  ? -44.92817 35.24504 -5.50810  1.000 98.69379  ? 63  PHE A N   1 
ATOM   293  C CA  . PHE A 1 44  ? -46.30180 35.73074 -5.51716  1.000 110.85232 ? 63  PHE A CA  1 
ATOM   294  C C   . PHE A 1 44  ? -46.43020 36.88848 -4.53404  1.000 105.43822 ? 63  PHE A C   1 
ATOM   295  O O   . PHE A 1 44  ? -45.44805 37.33733 -3.93815  1.000 104.26789 ? 63  PHE A O   1 
ATOM   296  C CB  . PHE A 1 44  ? -47.29776 34.59979 -5.21788  1.000 102.02363 ? 63  PHE A CB  1 
ATOM   297  C CG  . PHE A 1 44  ? -47.18699 34.02300 -3.83341  1.000 97.03495  ? 63  PHE A CG  1 
ATOM   298  C CD1 . PHE A 1 44  ? -46.25186 33.04232 -3.54665  1.000 100.96858 ? 63  PHE A CD1 1 
ATOM   299  C CD2 . PHE A 1 44  ? -48.04676 34.43671 -2.82799  1.000 98.61378  ? 63  PHE A CD2 1 
ATOM   300  C CE1 . PHE A 1 44  ? -46.15885 32.50155 -2.27446  1.000 97.07826  ? 63  PHE A CE1 1 
ATOM   301  C CE2 . PHE A 1 44  ? -47.96167 33.89985 -1.55698  1.000 98.92117  ? 63  PHE A CE2 1 
ATOM   302  C CZ  . PHE A 1 44  ? -47.01794 32.92829 -1.28016  1.000 101.03467 ? 63  PHE A CZ  1 
ATOM   303  N N   . LYS A 1 45  ? -47.65297 37.39381 -4.39215  1.000 101.10095 ? 64  LYS A N   1 
ATOM   304  C CA  . LYS A 1 45  ? -47.95006 38.50131 -3.49360  1.000 106.99116 ? 64  LYS A CA  1 
ATOM   305  C C   . LYS A 1 45  ? -48.97617 38.06131 -2.46093  1.000 109.64500 ? 64  LYS A C   1 
ATOM   306  O O   . LYS A 1 45  ? -49.99871 37.46287 -2.81267  1.000 117.27999 ? 64  LYS A O   1 
ATOM   307  C CB  . LYS A 1 45  ? -48.47804 39.71497 -4.26737  1.000 109.46372 ? 64  LYS A CB  1 
ATOM   308  C CG  . LYS A 1 45  ? -47.42244 40.48380 -5.04719  1.000 112.90975 ? 64  LYS A CG  1 
ATOM   309  C CD  . LYS A 1 45  ? -46.38528 41.10363 -4.12200  1.000 122.55664 ? 64  LYS A CD  1 
ATOM   310  C CE  . LYS A 1 45  ? -45.57424 42.17525 -4.83824  1.000 120.13887 ? 64  LYS A CE  1 
ATOM   311  N NZ  . LYS A 1 45  ? -44.84277 41.63995 -6.02100  1.000 113.90360 ? 64  LYS A NZ  1 
ATOM   312  N N   . ARG A 1 46  ? -48.70772 38.36741 -1.19294  1.000 110.14661 ? 65  ARG A N   1 
ATOM   313  C CA  . ARG A 1 46  ? -49.64367 38.10881 -0.10556  1.000 111.84748 ? 65  ARG A CA  1 
ATOM   314  C C   . ARG A 1 46  ? -49.78656 39.38456 0.70486   1.000 116.69151 ? 65  ARG A C   1 
ATOM   315  O O   . ARG A 1 46  ? -48.79223 39.90670 1.21677   1.000 117.95825 ? 65  ARG A O   1 
ATOM   316  C CB  . ARG A 1 46  ? -49.18606 36.95757 0.79228   1.000 114.38642 ? 65  ARG A CB  1 
ATOM   317  C CG  . ARG A 1 46  ? -50.07340 36.78548 2.01996   1.000 110.00912 ? 65  ARG A CG  1 
ATOM   318  C CD  . ARG A 1 46  ? -49.83078 35.46719 2.72820   1.000 105.81627 ? 65  ARG A CD  1 
ATOM   319  N NE  . ARG A 1 46  ? -50.01757 34.32001 1.84952   1.000 100.70055 ? 65  ARG A NE  1 
ATOM   320  C CZ  . ARG A 1 46  ? -49.71298 33.07251 2.17877   1.000 104.69632 ? 65  ARG A CZ  1 
ATOM   321  N NH1 . ARG A 1 46  ? -49.19008 32.77802 3.35748   1.000 114.40051 ? 65  ARG A NH1 1 
ATOM   322  N NH2 . ARG A 1 46  ? -49.93293 32.09692 1.30160   1.000 104.53019 ? 65  ARG A NH2 1 
ATOM   323  N N   . ASN A 1 47  ? -51.01001 39.90285 0.78494   1.000 125.50193 ? 66  ASN A N   1 
ATOM   324  C CA  . ASN A 1 47  ? -51.29443 41.14007 1.50992   1.000 129.02822 ? 66  ASN A CA  1 
ATOM   325  C C   . ASN A 1 47  ? -50.38074 42.27240 1.04654   1.000 133.23171 ? 66  ASN A C   1 
ATOM   326  O O   . ASN A 1 47  ? -49.95213 43.11867 1.83368   1.000 134.40663 ? 66  ASN A O   1 
ATOM   327  C CB  . ASN A 1 47  ? -51.16056 40.92175 3.01822   1.000 130.44045 ? 66  ASN A CB  1 
ATOM   328  C CG  . ASN A 1 47  ? -52.02545 39.78408 3.52128   1.000 132.94920 ? 66  ASN A CG  1 
ATOM   329  O OD1 . ASN A 1 47  ? -52.56275 39.00263 2.73581   1.000 127.83151 ? 66  ASN A OD1 1 
ATOM   330  N ND2 . ASN A 1 47  ? -52.15234 39.67582 4.83863   1.000 140.26634 ? 66  ASN A ND2 1 
ATOM   331  N N   . GLY A 1 48  ? -50.06872 42.27723 -0.24920  1.000 129.19086 ? 67  GLY A N   1 
ATOM   332  C CA  . GLY A 1 48  ? -49.23669 43.29923 -0.84526  1.000 127.89634 ? 67  GLY A CA  1 
ATOM   333  C C   . GLY A 1 48  ? -47.74275 43.09378 -0.71500  1.000 125.07043 ? 67  GLY A C   1 
ATOM   334  O O   . GLY A 1 48  ? -46.98100 43.77785 -1.41092  1.000 125.83807 ? 67  GLY A O   1 
ATOM   335  N N   . GLU A 1 49  ? -47.28768 42.18371 0.14118   1.000 122.61088 ? 68  GLU A N   1 
ATOM   336  C CA  . GLU A 1 49  ? -45.86119 41.94346 0.31206   1.000 121.62251 ? 68  GLU A CA  1 
ATOM   337  C C   . GLU A 1 49  ? -45.43528 40.74600 -0.52895  1.000 115.51960 ? 68  GLU A C   1 
ATOM   338  O O   . GLU A 1 49  ? -46.18546 39.77350 -0.67725  1.000 112.63685 ? 68  GLU A O   1 
ATOM   339  C CB  . GLU A 1 49  ? -45.48650 41.73796 1.78482   1.000 114.57413 ? 68  GLU A CB  1 
ATOM   340  C CG  . GLU A 1 49  ? -46.03168 40.48294 2.42916   1.000 120.94787 ? 68  GLU A CG  1 
ATOM   341  C CD  . GLU A 1 49  ? -47.06127 40.77671 3.50365   1.000 129.33162 ? 68  GLU A CD  1 
ATOM   342  O OE1 . GLU A 1 49  ? -47.35860 41.96854 3.73532   1.000 130.89696 ? 68  GLU A OE1 1 
ATOM   343  O OE2 . GLU A 1 49  ? -47.57284 39.81337 4.11457   1.000 125.90868 ? 68  GLU A OE2 1 
ATOM   344  N N   . SER A 1 50  ? -44.23831 40.84164 -1.10445  1.000 114.86469 ? 69  SER A N   1 
ATOM   345  C CA  . SER A 1 50  ? -43.69964 39.75677 -1.91262  1.000 104.61502 ? 69  SER A CA  1 
ATOM   346  C C   . SER A 1 50  ? -43.42362 38.52744 -1.05749  1.000 104.00867 ? 69  SER A C   1 
ATOM   347  O O   . SER A 1 50  ? -42.75675 38.60864 -0.02097  1.000 110.58860 ? 69  SER A O   1 
ATOM   348  C CB  . SER A 1 50  ? -42.41702 40.19775 -2.61721  1.000 97.45927  ? 69  SER A CB  1 
ATOM   349  O OG  . SER A 1 50  ? -42.64178 41.32248 -3.44648  1.000 109.23315 ? 69  SER A OG  1 
ATOM   350  N N   . TRP A 1 51  ? -43.94631 37.38869 -1.50086  1.000 100.76124 ? 70  TRP A N   1 
ATOM   351  C CA  . TRP A 1 51  ? -43.75200 36.09044 -0.88174  1.000 100.20052 ? 70  TRP A CA  1 
ATOM   352  C C   . TRP A 1 51  ? -43.20512 35.14108 -1.93672  1.000 95.16598  ? 70  TRP A C   1 
ATOM   353  O O   . TRP A 1 51  ? -43.24872 35.42193 -3.13804  1.000 101.20418 ? 70  TRP A O   1 
ATOM   354  C CB  . TRP A 1 51  ? -45.06351 35.53589 -0.30666  1.000 93.16996  ? 70  TRP A CB  1 
ATOM   355  C CG  . TRP A 1 51  ? -45.38288 35.96640 1.08639   1.000 92.15389  ? 70  TRP A CG  1 
ATOM   356  C CD1 . TRP A 1 51  ? -45.63051 37.23303 1.52222   1.000 94.35462  ? 70  TRP A CD1 1 
ATOM   357  C CD2 . TRP A 1 51  ? -45.51426 35.11392 2.23073   1.000 92.21199  ? 70  TRP A CD2 1 
ATOM   358  N NE1 . TRP A 1 51  ? -45.89324 37.22564 2.87281   1.000 95.98855  ? 70  TRP A NE1 1 
ATOM   359  C CE2 . TRP A 1 51  ? -45.82879 35.93559 3.33047   1.000 95.12471  ? 70  TRP A CE2 1 
ATOM   360  C CE3 . TRP A 1 51  ? -45.38916 33.73503 2.43233   1.000 90.26171  ? 70  TRP A CE3 1 
ATOM   361  C CZ2 . TRP A 1 51  ? -46.01995 35.42407 4.61457   1.000 94.69163  ? 70  TRP A CZ2 1 
ATOM   362  C CZ3 . TRP A 1 51  ? -45.57834 33.22881 3.70683   1.000 86.61465  ? 70  TRP A CZ3 1 
ATOM   363  C CH2 . TRP A 1 51  ? -45.89040 34.07096 4.78120   1.000 88.09502  ? 70  TRP A CH2 1 
ATOM   364  N N   . VAL A 1 52  ? -42.70432 33.99630 -1.48615  1.000 82.31698  ? 71  VAL A N   1 
ATOM   365  C CA  . VAL A 1 52  ? -42.17879 32.98001 -2.38561  1.000 79.85738  ? 71  VAL A CA  1 
ATOM   366  C C   . VAL A 1 52  ? -42.60707 31.61199 -1.87147  1.000 86.42096  ? 71  VAL A C   1 
ATOM   367  O O   . VAL A 1 52  ? -42.68202 31.38013 -0.65786  1.000 81.06216  ? 71  VAL A O   1 
ATOM   368  C CB  . VAL A 1 52  ? -40.64263 33.08146 -2.52238  1.000 75.86745  ? 71  VAL A CB  1 
ATOM   369  C CG1 . VAL A 1 52  ? -39.95026 32.66339 -1.23757  1.000 64.69730  ? 71  VAL A CG1 1 
ATOM   370  C CG2 . VAL A 1 52  ? -40.15388 32.25552 -3.69752  1.000 87.43443  ? 71  VAL A CG2 1 
ATOM   371  N N   . ARG A 1 53  ? -42.92904 30.71679 -2.80312  1.000 82.93998  ? 72  ARG A N   1 
ATOM   372  C CA  . ARG A 1 53  ? -43.29297 29.34420 -2.48831  1.000 87.13148  ? 72  ARG A CA  1 
ATOM   373  C C   . ARG A 1 53  ? -42.39234 28.43762 -3.31149  1.000 77.83298  ? 72  ARG A C   1 
ATOM   374  O O   . ARG A 1 53  ? -42.23748 28.63991 -4.52043  1.000 80.59320  ? 72  ARG A O   1 
ATOM   375  C CB  . ARG A 1 53  ? -44.77960 29.08294 -2.77221  1.000 85.15344  ? 72  ARG A CB  1 
ATOM   376  C CG  . ARG A 1 53  ? -45.24903 27.64823 -2.55018  1.000 86.67065  ? 72  ARG A CG  1 
ATOM   377  C CD  . ARG A 1 53  ? -46.77378 27.57645 -2.63786  1.000 108.16404 ? 72  ARG A CD  1 
ATOM   378  N NE  . ARG A 1 53  ? -47.31252 26.24710 -2.36685  1.000 114.58176 ? 72  ARG A NE  1 
ATOM   379  C CZ  . ARG A 1 53  ? -47.54174 25.31974 -3.28755  1.000 114.26559 ? 72  ARG A CZ  1 
ATOM   380  N NH1 . ARG A 1 53  ? -48.05130 24.13972 -2.96885  1.000 96.91024  ? 72  ARG A NH1 1 
ATOM   381  N NH2 . ARG A 1 53  ? -47.26672 25.58690 -4.56124  1.000 114.58854 ? 72  ARG A NH2 1 
ATOM   382  N N   . PHE A 1 54  ? -41.78350 27.46062 -2.65125  1.000 69.55079  ? 73  PHE A N   1 
ATOM   383  C CA  . PHE A 1 54  ? -40.76692 26.63458 -3.28568  1.000 78.57026  ? 73  PHE A CA  1 
ATOM   384  C C   . PHE A 1 54  ? -40.63217 25.33377 -2.51194  1.000 75.02658  ? 73  PHE A C   1 
ATOM   385  O O   . PHE A 1 54  ? -41.13953 25.19184 -1.39792  1.000 77.34280  ? 73  PHE A O   1 
ATOM   386  C CB  . PHE A 1 54  ? -39.42396 27.36446 -3.34343  1.000 64.73677  ? 73  PHE A CB  1 
ATOM   387  C CG  . PHE A 1 54  ? -38.80756 27.58301 -1.99557  1.000 65.72600  ? 73  PHE A CG  1 
ATOM   388  C CD1 . PHE A 1 54  ? -39.24332 28.61724 -1.18073  1.000 57.31632  ? 73  PHE A CD1 1 
ATOM   389  C CD2 . PHE A 1 54  ? -37.80077 26.74897 -1.53529  1.000 65.78862  ? 73  PHE A CD2 1 
ATOM   390  C CE1 . PHE A 1 54  ? -38.68518 28.81952 0.06524   1.000 60.29898  ? 73  PHE A CE1 1 
ATOM   391  C CE2 . PHE A 1 54  ? -37.23435 26.94509 -0.29034  1.000 57.77450  ? 73  PHE A CE2 1 
ATOM   392  C CZ  . PHE A 1 54  ? -37.67656 27.98203 0.51216   1.000 70.56291  ? 73  PHE A CZ  1 
ATOM   393  N N   . TYR A 1 55  ? -39.91632 24.39117 -3.11376  1.000 73.33821  ? 74  TYR A N   1 
ATOM   394  C CA  . TYR A 1 55  ? -39.55910 23.14152 -2.46584  1.000 76.52578  ? 74  TYR A CA  1 
ATOM   395  C C   . TYR A 1 55  ? -38.04253 23.02651 -2.39288  1.000 70.83524  ? 74  TYR A C   1 
ATOM   396  O O   . TYR A 1 55  ? -37.32029 23.61013 -3.20732  1.000 68.95040  ? 74  TYR A O   1 
ATOM   397  C CB  . TYR A 1 55  ? -40.13729 21.93979 -3.22603  1.000 76.35051  ? 74  TYR A CB  1 
ATOM   398  C CG  . TYR A 1 55  ? -41.62754 22.02716 -3.48232  1.000 84.75222  ? 74  TYR A CG  1 
ATOM   399  C CD1 . TYR A 1 55  ? -42.54175 21.48859 -2.58650  1.000 85.13392  ? 74  TYR A CD1 1 
ATOM   400  C CD2 . TYR A 1 55  ? -42.12003 22.65019 -4.62408  1.000 89.69061  ? 74  TYR A CD2 1 
ATOM   401  C CE1 . TYR A 1 55  ? -43.90302 21.56725 -2.82103  1.000 80.67865  ? 74  TYR A CE1 1 
ATOM   402  C CE2 . TYR A 1 55  ? -43.48035 22.73375 -4.86599  1.000 87.24765  ? 74  TYR A CE2 1 
ATOM   403  C CZ  . TYR A 1 55  ? -44.36701 22.19060 -3.96154  1.000 89.01967  ? 74  TYR A CZ  1 
ATOM   404  O OH  . TYR A 1 55  ? -45.72174 22.27178 -4.19782  1.000 91.23193  ? 74  TYR A OH  1 
ATOM   405  N N   . LEU A 1 56  ? -37.56164 22.27721 -1.40493  1.000 68.33102  ? 75  LEU A N   1 
ATOM   406  C CA  . LEU A 1 56  ? -36.14851 21.93482 -1.37436  1.000 57.99128  ? 75  LEU A CA  1 
ATOM   407  C C   . LEU A 1 56  ? -35.79614 21.09590 -2.59549  1.000 73.67705  ? 75  LEU A C   1 
ATOM   408  O O   . LEU A 1 56  ? -36.62195 20.34068 -3.11745  1.000 76.06571  ? 75  LEU A O   1 
ATOM   409  C CB  . LEU A 1 56  ? -35.80246 21.18010 -0.09088  1.000 54.75681  ? 75  LEU A CB  1 
ATOM   410  C CG  . LEU A 1 56  ? -36.00401 21.95818 1.21092   1.000 67.22218  ? 75  LEU A CG  1 
ATOM   411  C CD1 . LEU A 1 56  ? -35.54406 21.14715 2.41053   1.000 72.51776  ? 75  LEU A CD1 1 
ATOM   412  C CD2 . LEU A 1 56  ? -35.25807 23.27747 1.15106   1.000 53.58546  ? 75  LEU A CD2 1 
ATOM   413  N N   . ALA A 1 57  ? -34.55355 21.24616 -3.06141  1.000 70.21939  ? 76  ALA A N   1 
ATOM   414  C CA  . ALA A 1 57  ? -34.10782 20.49692 -4.23229  1.000 72.94122  ? 76  ALA A CA  1 
ATOM   415  C C   . ALA A 1 57  ? -34.18846 18.99366 -4.00497  1.000 69.40435  ? 76  ALA A C   1 
ATOM   416  O O   . ALA A 1 57  ? -34.34127 18.22880 -4.96468  1.000 78.01771  ? 76  ALA A O   1 
ATOM   417  C CB  . ALA A 1 57  ? -32.68286 20.90241 -4.60761  1.000 76.98114  ? 76  ALA A CB  1 
ATOM   418  N N   . ILE A 1 58  ? -34.08306 18.55033 -2.75166  1.000 64.31234  ? 77  ILE A N   1 
ATOM   419  C CA  . ILE A 1 58  ? -34.17589 17.12273 -2.47278  1.000 68.10943  ? 77  ILE A CA  1 
ATOM   420  C C   . ILE A 1 58  ? -35.62644 16.64786 -2.51927  1.000 75.65689  ? 77  ILE A C   1 
ATOM   421  O O   . ILE A 1 58  ? -35.88914 15.47711 -2.81589  1.000 79.99973  ? 77  ILE A O   1 
ATOM   422  C CB  . ILE A 1 58  ? -33.52340 16.81122 -1.11512  1.000 63.25692  ? 77  ILE A CB  1 
ATOM   423  C CG1 . ILE A 1 58  ? -33.48150 15.30259 -0.86607  1.000 75.52412  ? 77  ILE A CG1 1 
ATOM   424  C CG2 . ILE A 1 58  ? -34.27838 17.50766 0.01153   1.000 55.15836  ? 77  ILE A CG2 1 
ATOM   425  C CD1 . ILE A 1 58  ? -32.85542 14.92353 0.46093   1.000 74.91360  ? 77  ILE A CD1 1 
ATOM   426  N N   . ASP A 1 59  ? -36.58376 17.53498 -2.23863  1.000 72.11804  ? 78  ASP A N   1 
ATOM   427  C CA  . ASP A 1 59  ? -38.00410 17.18490 -2.20072  1.000 71.80892  ? 78  ASP A CA  1 
ATOM   428  C C   . ASP A 1 59  ? -38.55337 17.15580 -3.62555  1.000 82.37618  ? 78  ASP A C   1 
ATOM   429  O O   . ASP A 1 59  ? -39.25554 18.06303 -4.07966  1.000 85.71385  ? 78  ASP A O   1 
ATOM   430  C CB  . ASP A 1 59  ? -38.76937 18.16715 -1.32320  1.000 72.23796  ? 78  ASP A CB  1 
ATOM   431  C CG  . ASP A 1 59  ? -40.22403 17.77876 -1.13816  1.000 82.33684  ? 78  ASP A CG  1 
ATOM   432  O OD1 . ASP A 1 59  ? -40.60604 16.65340 -1.52885  1.000 88.29726  ? 78  ASP A OD1 1 
ATOM   433  O OD2 . ASP A 1 59  ? -40.98887 18.60503 -0.59969  1.000 86.61550  ? 78  ASP A OD2 1 
ATOM   434  N N   . ALA A 1 60  ? -38.23621 16.07374 -4.34038  1.000 76.71769  ? 79  ALA A N   1 
ATOM   435  C CA  . ALA A 1 60  ? -38.72512 15.92891 -5.70820  1.000 82.49712  ? 79  ALA A CA  1 
ATOM   436  C C   . ALA A 1 60  ? -40.22311 15.65259 -5.74694  1.000 88.90136  ? 79  ALA A C   1 
ATOM   437  O O   . ALA A 1 60  ? -40.90337 16.05656 -6.69733  1.000 85.51750  ? 79  ALA A O   1 
ATOM   438  C CB  . ALA A 1 60  ? -37.96166 14.81927 -6.42943  1.000 83.81717  ? 79  ALA A CB  1 
ATOM   439  N N   . ALA A 1 61  ? -40.75006 14.95727 -4.74230  1.000 83.59769  ? 80  ALA A N   1 
ATOM   440  C CA  . ALA A 1 61  ? -42.16482 14.61223 -4.70198  1.000 87.59137  ? 80  ALA A CA  1 
ATOM   441  C C   . ALA A 1 61  ? -43.05811 15.76469 -4.26294  1.000 89.77679  ? 80  ALA A C   1 
ATOM   442  O O   . ALA A 1 61  ? -44.27853 15.57775 -4.19644  1.000 96.83083  ? 80  ALA A O   1 
ATOM   443  C CB  . ALA A 1 61  ? -42.39079 13.41701 -3.77617  1.000 86.59801  ? 80  ALA A CB  1 
ATOM   444  N N   . HIS A 1 62  ? -42.49143 16.93417 -3.95483  1.000 82.52084  ? 81  HIS A N   1 
ATOM   445  C CA  . HIS A 1 62  ? -43.26681 18.09108 -3.50207  1.000 86.15725  ? 81  HIS A CA  1 
ATOM   446  C C   . HIS A 1 62  ? -44.06098 17.76380 -2.23896  1.000 85.03483  ? 81  HIS A C   1 
ATOM   447  O O   . HIS A 1 62  ? -45.25348 18.05653 -2.13143  1.000 93.57395  ? 81  HIS A O   1 
ATOM   448  C CB  . HIS A 1 62  ? -44.19155 18.60426 -4.60960  1.000 89.25993  ? 81  HIS A CB  1 
ATOM   449  C CG  . HIS A 1 62  ? -43.47803 19.32603 -5.70897  1.000 93.58950  ? 81  HIS A CG  1 
ATOM   450  N ND1 . HIS A 1 62  ? -44.13935 20.08579 -6.64984  1.000 92.85122  ? 81  HIS A ND1 1 
ATOM   451  C CD2 . HIS A 1 62  ? -42.16121 19.41364 -6.01174  1.000 84.88846  ? 81  HIS A CD2 1 
ATOM   452  C CE1 . HIS A 1 62  ? -43.26136 20.60342 -7.48993  1.000 90.54794  ? 81  HIS A CE1 1 
ATOM   453  N NE2 . HIS A 1 62  ? -42.05378 20.21190 -7.12437  1.000 86.36594  ? 81  HIS A NE2 1 
ATOM   454  N N   . SER A 1 63  ? -43.38820 17.13585 -1.27726  1.000 85.68108  ? 82  SER A N   1 
ATOM   455  C CA  . SER A 1 63  ? -44.05481 16.71682 -0.05183  1.000 95.70383  ? 82  SER A CA  1 
ATOM   456  C C   . SER A 1 63  ? -44.09290 17.80893 1.00704   1.000 89.25152  ? 82  SER A C   1 
ATOM   457  O O   . SER A 1 63  ? -45.02010 17.83499 1.82419   1.000 100.40761 ? 82  SER A O   1 
ATOM   458  C CB  . SER A 1 63  ? -43.36691 15.47482 0.52462   1.000 93.97310  ? 82  SER A CB  1 
ATOM   459  O OG  . SER A 1 63  ? -43.56748 14.34426 -0.30753  1.000 90.78134  ? 82  SER A OG  1 
ATOM   460  N N   . HIS A 1 64  ? -43.11537 18.71060 1.01351   1.000 88.66477  ? 83  HIS A N   1 
ATOM   461  C CA  . HIS A 1 64  ? -43.00613 19.76114 2.02539   1.000 89.34778  ? 83  HIS A CA  1 
ATOM   462  C C   . HIS A 1 64  ? -42.93261 21.11925 1.33801   1.000 86.72082  ? 83  HIS A C   1 
ATOM   463  O O   . HIS A 1 64  ? -41.84472 21.68866 1.17491   1.000 83.85889  ? 83  HIS A O   1 
ATOM   464  C CB  . HIS A 1 64  ? -41.80296 19.51411 2.93616   1.000 80.73470  ? 83  HIS A CB  1 
ATOM   465  C CG  . HIS A 1 64  ? -41.85584 18.19920 3.65215   1.000 86.83256  ? 83  HIS A CG  1 
ATOM   466  N ND1 . HIS A 1 64  ? -41.47446 17.01257 3.06278   1.000 84.48708  ? 83  HIS A ND1 1 
ATOM   467  C CD2 . HIS A 1 64  ? -42.25758 17.88311 4.90635   1.000 90.76602  ? 83  HIS A CD2 1 
ATOM   468  C CE1 . HIS A 1 64  ? -41.63425 16.02371 3.92439   1.000 78.48143  ? 83  HIS A CE1 1 
ATOM   469  N NE2 . HIS A 1 64  ? -42.10713 16.52504 5.05103   1.000 85.76555  ? 83  HIS A NE2 1 
ATOM   470  N N   . PRO A 1 65  ? -44.07530 21.66382 0.91494   1.000 87.82126  ? 84  PRO A N   1 
ATOM   471  C CA  . PRO A 1 65  ? -44.07973 23.01611 0.34207   1.000 73.59383  ? 84  PRO A CA  1 
ATOM   472  C C   . PRO A 1 65  ? -43.65401 24.05379 1.36863   1.000 77.44563  ? 84  PRO A C   1 
ATOM   473  O O   . PRO A 1 65  ? -44.03073 23.99036 2.54080   1.000 80.12279  ? 84  PRO A O   1 
ATOM   474  C CB  . PRO A 1 65  ? -45.53920 23.21970 -0.08474  1.000 82.24992  ? 84  PRO A CB  1 
ATOM   475  C CG  . PRO A 1 65  ? -46.13631 21.84747 -0.13210  1.000 89.71547  ? 84  PRO A CG  1 
ATOM   476  C CD  . PRO A 1 65  ? -45.41544 21.05594 0.91085   1.000 85.43180  ? 84  PRO A CD  1 
ATOM   477  N N   . ILE A 1 66  ? -42.84892 25.01031 0.91568   1.000 73.56894  ? 85  ILE A N   1 
ATOM   478  C CA  . ILE A 1 66  ? -42.28944 26.05112 1.76919   1.000 70.65379  ? 85  ILE A CA  1 
ATOM   479  C C   . ILE A 1 66  ? -42.79442 27.39304 1.26602   1.000 75.65112  ? 85  ILE A C   1 
ATOM   480  O O   . ILE A 1 66  ? -42.52549 27.77067 0.11945   1.000 73.41707  ? 85  ILE A O   1 
ATOM   481  C CB  . ILE A 1 66  ? -40.75303 26.02478 1.77067   1.000 70.54051  ? 85  ILE A CB  1 
ATOM   482  C CG1 . ILE A 1 66  ? -40.23884 24.59827 1.95297   1.000 69.45561  ? 85  ILE A CG1 1 
ATOM   483  C CG2 . ILE A 1 66  ? -40.20370 26.93987 2.85344   1.000 73.61235  ? 85  ILE A CG2 1 
ATOM   484  C CD1 . ILE A 1 66  ? -38.73586 24.48714 1.88855   1.000 70.29864  ? 85  ILE A CD1 1 
ATOM   485  N N   . GLU A 1 67  ? -43.50886 28.11805 2.12207   1.000 81.26974  ? 86  GLU A N   1 
ATOM   486  C CA  . GLU A 1 67  ? -43.97451 29.46436 1.81496   1.000 82.19817  ? 86  GLU A CA  1 
ATOM   487  C C   . GLU A 1 67  ? -43.32451 30.42303 2.79760   1.000 80.52519  ? 86  GLU A C   1 
ATOM   488  O O   . GLU A 1 67  ? -43.50760 30.29098 4.01245   1.000 81.05934  ? 86  GLU A O   1 
ATOM   489  C CB  . GLU A 1 67  ? -45.49884 29.57816 1.88973   1.000 88.05626  ? 86  GLU A CB  1 
ATOM   490  C CG  . GLU A 1 67  ? -46.21407 29.26572 0.58817   1.000 93.59782  ? 86  GLU A CG  1 
ATOM   491  C CD  . GLU A 1 67  ? -47.67898 29.63967 0.63223   1.000 93.50041  ? 86  GLU A CD  1 
ATOM   492  O OE1 . GLU A 1 67  ? -48.11796 30.18535 1.66718   1.000 91.73814  ? 86  GLU A OE1 1 
ATOM   493  O OE2 . GLU A 1 67  ? -48.38986 29.38696 -0.36450  1.000 105.96793 ? 86  GLU A OE2 1 
ATOM   494  N N   . ARG A 1 68  ? -42.55506 31.37451 2.27668   1.000 74.02049  ? 87  ARG A N   1 
ATOM   495  C CA  . ARG A 1 68  ? -41.86751 32.31092 3.13906   1.000 78.36067  ? 87  ARG A CA  1 
ATOM   496  C C   . ARG A 1 68  ? -41.99193 33.69667 2.52711   1.000 89.44705  ? 87  ARG A C   1 
ATOM   497  O O   . ARG A 1 68  ? -41.95223 33.83418 1.29566   1.000 89.71020  ? 87  ARG A O   1 
ATOM   498  C CB  . ARG A 1 68  ? -40.38915 31.94506 3.32111   1.000 72.03266  ? 87  ARG A CB  1 
ATOM   499  C CG  . ARG A 1 68  ? -40.18777 30.67598 4.12796   1.000 70.86884  ? 87  ARG A CG  1 
ATOM   500  C CD  . ARG A 1 68  ? -40.58477 30.87464 5.58429   1.000 71.87736  ? 87  ARG A CD  1 
ATOM   501  N NE  . ARG A 1 68  ? -40.48983 29.63401 6.34552   1.000 80.73095  ? 87  ARG A NE  1 
ATOM   502  C CZ  . ARG A 1 68  ? -41.47386 28.75036 6.46722   1.000 89.28667  ? 87  ARG A CZ  1 
ATOM   503  N NH1 . ARG A 1 68  ? -42.68915 28.99425 5.99670   1.000 83.73764  ? 87  ARG A NH1 1 
ATOM   504  N NH2 . ARG A 1 68  ? -41.24324 27.60688 7.10697   1.000 88.37746  ? 87  ARG A NH2 1 
ATOM   505  N N   . PRO A 1 69  ? -42.14505 34.73442 3.34615   1.000 90.10963  ? 88  PRO A N   1 
ATOM   506  C CA  . PRO A 1 69  ? -42.12680 36.09373 2.79887   1.000 87.43507  ? 88  PRO A CA  1 
ATOM   507  C C   . PRO A 1 69  ? -40.75733 36.41526 2.22658   1.000 82.56238  ? 88  PRO A C   1 
ATOM   508  O O   . PRO A 1 69  ? -39.72639 36.00874 2.76759   1.000 82.57231  ? 88  PRO A O   1 
ATOM   509  C CB  . PRO A 1 69  ? -42.44833 36.97207 4.01317   1.000 85.24377  ? 88  PRO A CB  1 
ATOM   510  C CG  . PRO A 1 69  ? -42.00940 36.15425 5.18874   1.000 81.90748  ? 88  PRO A CG  1 
ATOM   511  C CD  . PRO A 1 69  ? -42.28170 34.72508 4.81331   1.000 85.50266  ? 88  PRO A CD  1 
ATOM   512  N N   . LEU A 1 70  ? -40.75581 37.13128 1.10733   1.000 87.43728  ? 89  LEU A N   1 
ATOM   513  C CA  . LEU A 1 70  ? -39.50315 37.55306 0.49946   1.000 81.52181  ? 89  LEU A CA  1 
ATOM   514  C C   . LEU A 1 70  ? -38.88422 38.67581 1.32013   1.000 84.41810  ? 89  LEU A C   1 
ATOM   515  O O   . LEU A 1 70  ? -39.54770 39.67232 1.62244   1.000 93.62186  ? 89  LEU A O   1 
ATOM   516  C CB  . LEU A 1 70  ? -39.74408 38.01439 -0.93651  1.000 82.52224  ? 89  LEU A CB  1 
ATOM   517  C CG  . LEU A 1 70  ? -38.53586 38.01126 -1.86914  1.000 81.66764  ? 89  LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 70  ? -38.00248 36.60148 -1.98687  1.000 81.36082  ? 89  LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 70  ? -38.91372 38.55499 -3.23327  1.000 81.47947  ? 89  LEU A CD2 1 
ATOM   520  N N   . ALA A 1 71  ? -37.60990 38.52511 1.68076   1.000 75.16790  ? 90  ALA A N   1 
ATOM   521  C CA  . ALA A 1 71  ? -36.92992 39.61012 2.37350   1.000 81.86862  ? 90  ALA A CA  1 
ATOM   522  C C   . ALA A 1 71  ? -36.44654 40.65618 1.37810   1.000 93.43625  ? 90  ALA A C   1 
ATOM   523  O O   . ALA A 1 71  ? -36.70242 41.85210 1.54784   1.000 100.15231 ? 90  ALA A O   1 
ATOM   524  C CB  . ALA A 1 71  ? -35.76576 39.06577 3.20157   1.000 76.89345  ? 90  ALA A CB  1 
ATOM   525  N N   . ARG A 1 72  ? -35.78110 40.21867 0.31556   1.000 92.67033  ? 91  ARG A N   1 
ATOM   526  C CA  . ARG A 1 72  ? -35.28876 41.11249 -0.72584  1.000 92.35949  ? 91  ARG A CA  1 
ATOM   527  C C   . ARG A 1 72  ? -34.98035 40.27134 -1.96056  1.000 91.75354  ? 91  ARG A C   1 
ATOM   528  O O   . ARG A 1 72  ? -35.32826 39.08740 -2.02680  1.000 96.27978  ? 91  ARG A O   1 
ATOM   529  C CB  . ARG A 1 72  ? -34.06783 41.89507 -0.23180  1.000 95.55542  ? 91  ARG A CB  1 
ATOM   530  C CG  . ARG A 1 72  ? -32.97064 41.01370 0.33987   1.000 90.22003  ? 91  ARG A CG  1 
ATOM   531  C CD  . ARG A 1 72  ? -31.85177 41.84147 0.94384   1.000 89.36761  ? 91  ARG A CD  1 
ATOM   532  N NE  . ARG A 1 72  ? -30.67395 41.03097 1.22808   1.000 89.06570  ? 91  ARG A NE  1 
ATOM   533  C CZ  . ARG A 1 72  ? -29.72941 40.75528 0.33939   1.000 92.93635  ? 91  ARG A CZ  1 
ATOM   534  N NH1 . ARG A 1 72  ? -28.68077 40.01170 0.65224   1.000 93.05724  ? 91  ARG A NH1 1 
ATOM   535  N NH2 . ARG A 1 72  ? -29.84166 41.23618 -0.89591  1.000 96.07229  ? 91  ARG A NH2 1 
ATOM   536  N N   . VAL A 1 73  ? -34.33273 40.88695 -2.94724  1.000 87.96656  ? 92  VAL A N   1 
ATOM   537  C CA  . VAL A 1 73  ? -33.88964 40.20263 -4.15699  1.000 87.76251  ? 92  VAL A CA  1 
ATOM   538  C C   . VAL A 1 73  ? -32.42433 40.55360 -4.37158  1.000 97.41549  ? 92  VAL A C   1 
ATOM   539  O O   . VAL A 1 73  ? -32.08029 41.73505 -4.49806  1.000 105.33912 ? 92  VAL A O   1 
ATOM   540  C CB  . VAL A 1 73  ? -34.72807 40.59188 -5.38711  1.000 98.54466  ? 92  VAL A CB  1 
ATOM   541  C CG1 . VAL A 1 73  ? -34.25009 39.83630 -6.61387  1.000 103.08875 ? 92  VAL A CG1 1 
ATOM   542  C CG2 . VAL A 1 73  ? -36.20411 40.32320 -5.13848  1.000 97.01538  ? 92  VAL A CG2 1 
ATOM   543  N N   . SER A 1 74  ? -31.56520 39.53678 -4.41124  1.000 90.58759  ? 93  SER A N   1 
ATOM   544  C CA  . SER A 1 74  ? -30.13217 39.76005 -4.52248  1.000 100.60498 ? 93  SER A CA  1 
ATOM   545  C C   . SER A 1 74  ? -29.76609 40.17127 -5.94749  1.000 116.87300 ? 93  SER A C   1 
ATOM   546  O O   . SER A 1 74  ? -30.61673 40.27569 -6.83585  1.000 117.29979 ? 93  SER A O   1 
ATOM   547  C CB  . SER A 1 74  ? -29.36071 38.51089 -4.10046  1.000 98.96978  ? 93  SER A CB  1 
ATOM   548  O OG  . SER A 1 74  ? -29.30995 37.55904 -5.14964  1.000 104.31269 ? 93  SER A OG  1 
ATOM   549  N N   . LYS A 1 75  ? -28.47658 40.40927 -6.16715  1.000 127.75224 ? 94  LYS A N   1 
ATOM   550  C CA  . LYS A 1 75  ? -27.97941 40.79757 -7.48188  1.000 122.65020 ? 94  LYS A CA  1 
ATOM   551  C C   . LYS A 1 75  ? -27.45201 39.58693 -8.24663  1.000 124.78020 ? 94  LYS A C   1 
ATOM   552  O O   . LYS A 1 75  ? -27.06894 38.58001 -7.64863  1.000 117.79458 ? 94  LYS A O   1 
ATOM   553  C CB  . LYS A 1 75  ? -26.88309 41.85562 -7.34920  1.000 113.48713 ? 94  LYS A CB  1 
ATOM   554  N N   . ALA A 1 93  ? -31.83219 39.51550 -8.86420  1.000 126.58617 ? 112 ALA A N   1 
ATOM   555  C CA  . ALA A 1 93  ? -31.80889 38.24170 -9.57315  1.000 120.95073 ? 112 ALA A CA  1 
ATOM   556  C C   . ALA A 1 93  ? -32.40817 37.12355 -8.72130  1.000 113.68095 ? 112 ALA A C   1 
ATOM   557  O O   . ALA A 1 93  ? -33.50530 36.64157 -9.00175  1.000 113.31732 ? 112 ALA A O   1 
ATOM   558  C CB  . ALA A 1 93  ? -30.38563 37.89297 -9.98579  1.000 118.73933 ? 112 ALA A CB  1 
ATOM   559  N N   . ARG A 1 94  ? -31.68354 36.71816 -7.67717  1.000 93.21383  ? 113 ARG A N   1 
ATOM   560  C CA  . ARG A 1 94  ? -32.17302 35.59701 -6.88224  1.000 91.30600  ? 113 ARG A CA  1 
ATOM   561  C C   . ARG A 1 94  ? -33.07668 36.08864 -5.75356  1.000 91.31440  ? 113 ARG A C   1 
ATOM   562  O O   . ARG A 1 94  ? -32.81581 37.14052 -5.16159  1.000 85.28923  ? 113 ARG A O   1 
ATOM   563  C CB  . ARG A 1 94  ? -31.01201 34.80325 -6.28521  1.000 90.15933  ? 113 ARG A CB  1 
ATOM   564  C CG  . ARG A 1 94  ? -30.20800 33.99528 -7.29242  1.000 86.19827  ? 113 ARG A CG  1 
ATOM   565  C CD  . ARG A 1 94  ? -29.10387 33.20350 -6.60591  1.000 64.57701  ? 113 ARG A CD  1 
ATOM   566  N N   . PRO A 1 95  ? -34.13980 35.34629 -5.44525  1.000 85.77233  ? 114 PRO A N   1 
ATOM   567  C CA  . PRO A 1 95  ? -34.95724 35.68607 -4.27576  1.000 72.74169  ? 114 PRO A CA  1 
ATOM   568  C C   . PRO A 1 95  ? -34.20489 35.39793 -2.98654  1.000 78.10030  ? 114 PRO A C   1 
ATOM   569  O O   . PRO A 1 95  ? -33.44910 34.42833 -2.88801  1.000 70.95967  ? 114 PRO A O   1 
ATOM   570  C CB  . PRO A 1 95  ? -36.18609 34.77700 -4.41863  1.000 71.80502  ? 114 PRO A CB  1 
ATOM   571  C CG  . PRO A 1 95  ? -36.15135 34.27330 -5.82893  1.000 80.40876  ? 114 PRO A CG  1 
ATOM   572  C CD  . PRO A 1 95  ? -34.70517 34.21934 -6.20158  1.000 84.44832  ? 114 PRO A CD  1 
ATOM   573  N N   . VAL A 1 96  ? -34.39353 36.27176 -2.00329  1.000 77.28669  ? 115 VAL A N   1 
ATOM   574  C CA  . VAL A 1 96  ? -33.74284 36.15729 -0.70492  1.000 72.55964  ? 115 VAL A CA  1 
ATOM   575  C C   . VAL A 1 96  ? -34.82179 35.99572 0.35433   1.000 66.90360  ? 115 VAL A C   1 
ATOM   576  O O   . VAL A 1 96  ? -35.83590 36.70000 0.32508   1.000 75.47685  ? 115 VAL A O   1 
ATOM   577  C CB  . VAL A 1 96  ? -32.85751 37.38457 -0.40539  1.000 75.13495  ? 115 VAL A CB  1 
ATOM   578  C CG1 . VAL A 1 96  ? -32.11996 37.19842 0.89843   1.000 57.29671  ? 115 VAL A CG1 1 
ATOM   579  C CG2 . VAL A 1 96  ? -31.88223 37.62620 -1.54365  1.000 77.57630  ? 115 VAL A CG2 1 
ATOM   580  N N   . ILE A 1 97  ? -34.61611 35.06390 1.28465   1.000 58.41659  ? 116 ILE A N   1 
ATOM   581  C CA  . ILE A 1 97  ? -35.56213 34.84165 2.37234   1.000 60.11428  ? 116 ILE A CA  1 
ATOM   582  C C   . ILE A 1 97  ? -34.79956 34.63981 3.67497   1.000 61.63766  ? 116 ILE A C   1 
ATOM   583  O O   . ILE A 1 97  ? -33.58129 34.46924 3.69158   1.000 62.71916  ? 116 ILE A O   1 
ATOM   584  C CB  . ILE A 1 97  ? -36.49220 33.63870 2.10659   1.000 60.50289  ? 116 ILE A CB  1 
ATOM   585  C CG1 . ILE A 1 97  ? -35.67135 32.38143 1.82029   1.000 60.39470  ? 116 ILE A CG1 1 
ATOM   586  C CG2 . ILE A 1 97  ? -37.44354 33.93985 0.96387   1.000 61.42245  ? 116 ILE A CG2 1 
ATOM   587  C CD1 . ILE A 1 97  ? -36.49498 31.11597 1.81014   1.000 64.62372  ? 116 ILE A CD1 1 
ATOM   588  N N   . GLU A 1 98  ? -35.53888 34.68035 4.77935   1.000 55.77547  ? 117 GLU A N   1 
ATOM   589  C CA  . GLU A 1 98  ? -35.00918 34.36838 6.09958   1.000 60.01089  ? 117 GLU A CA  1 
ATOM   590  C C   . GLU A 1 98  ? -35.63439 33.06162 6.56810   1.000 62.55485  ? 117 GLU A C   1 
ATOM   591  O O   . GLU A 1 98  ? -36.86237 32.93288 6.59886   1.000 66.79029  ? 117 GLU A O   1 
ATOM   592  C CB  . GLU A 1 98  ? -35.28086 35.49631 7.09547   1.000 69.22691  ? 117 GLU A CB  1 
ATOM   593  C CG  . GLU A 1 98  ? -34.37940 36.70756 6.89578   1.000 82.73779  ? 117 GLU A CG  1 
ATOM   594  C CD  . GLU A 1 98  ? -34.16146 37.50019 8.16910   1.000 89.07868  ? 117 GLU A CD  1 
ATOM   595  O OE1 . GLU A 1 98  ? -35.15144 38.01786 8.72654   1.000 94.61774  ? 117 GLU A OE1 1 
ATOM   596  O OE2 . GLU A 1 98  ? -32.99592 37.59438 8.61531   1.000 88.01593  ? 117 GLU A OE2 1 
ATOM   597  N N   . LEU A 1 99  ? -34.79024 32.09831 6.92236   1.000 57.47992  ? 118 LEU A N   1 
ATOM   598  C CA  . LEU A 1 99  ? -35.21941 30.77427 7.34293   1.000 62.14949  ? 118 LEU A CA  1 
ATOM   599  C C   . LEU A 1 99  ? -34.61132 30.44870 8.69500   1.000 60.27835  ? 118 LEU A C   1 
ATOM   600  O O   . LEU A 1 99  ? -33.43723 30.72965 8.93718   1.000 67.11225  ? 118 LEU A O   1 
ATOM   601  C CB  . LEU A 1 99  ? -34.80414 29.70272 6.33219   1.000 55.96451  ? 118 LEU A CB  1 
ATOM   602  C CG  . LEU A 1 99  ? -35.63156 29.59148 5.05569   1.000 66.94312  ? 118 LEU A CG  1 
ATOM   603  C CD1 . LEU A 1 99  ? -35.01132 28.56407 4.12604   1.000 64.29133  ? 118 LEU A CD1 1 
ATOM   604  C CD2 . LEU A 1 99  ? -37.07667 29.24006 5.37940   1.000 60.06305  ? 118 LEU A CD2 1 
ATOM   605  N N   . ASP A 1 100 ? -35.41198 29.86838 9.58014   1.000 61.86439  ? 119 ASP A N   1 
ATOM   606  C CA  . ASP A 1 100 ? -34.88157 29.34066 10.83048  1.000 65.95217  ? 119 ASP A CA  1 
ATOM   607  C C   . ASP A 1 100 ? -34.22894 27.99637 10.52876  1.000 67.92921  ? 119 ASP A C   1 
ATOM   608  O O   . ASP A 1 100 ? -34.92007 27.00038 10.29112  1.000 64.28337  ? 119 ASP A O   1 
ATOM   609  C CB  . ASP A 1 100 ? -35.98388 29.21856 11.87823  1.000 63.98668  ? 119 ASP A CB  1 
ATOM   610  C CG  . ASP A 1 100 ? -36.44298 30.56782 12.39727  1.000 75.05482  ? 119 ASP A CG  1 
ATOM   611  O OD1 . ASP A 1 100 ? -36.00446 31.59804 11.84241  1.000 70.60474  ? 119 ASP A OD1 1 
ATOM   612  O OD2 . ASP A 1 100 ? -37.23966 30.60304 13.36013  1.000 82.22818  ? 119 ASP A OD2 1 
ATOM   613  N N   . ILE A 1 101 ? -32.89793 27.97429 10.51068  1.000 63.77629  ? 120 ILE A N   1 
ATOM   614  C CA  . ILE A 1 101 ? -32.12243 26.78060 10.19414  1.000 62.99494  ? 120 ILE A CA  1 
ATOM   615  C C   . ILE A 1 101 ? -31.55672 26.20395 11.48296  1.000 67.21942  ? 120 ILE A C   1 
ATOM   616  O O   . ILE A 1 101 ? -31.06946 26.94057 12.35286  1.000 62.77025  ? 120 ILE A O   1 
ATOM   617  C CB  . ILE A 1 101 ? -30.99595 27.09286 9.18999   1.000 67.27159  ? 120 ILE A CB  1 
ATOM   618  C CG1 . ILE A 1 101 ? -31.56514 27.73150 7.92266   1.000 53.82273  ? 120 ILE A CG1 1 
ATOM   619  C CG2 . ILE A 1 101 ? -30.22201 25.82546 8.83829   1.000 53.17664  ? 120 ILE A CG2 1 
ATOM   620  C CD1 . ILE A 1 101 ? -32.49099 26.82265 7.15134   1.000 67.33646  ? 120 ILE A CD1 1 
ATOM   621  N N   . CYS A 1 102 ? -31.62737 24.88199 11.60778  1.000 67.39914  ? 121 CYS A N   1 
ATOM   622  C CA  . CYS A 1 102 ? -31.17938 24.15669 12.78449  1.000 66.64064  ? 121 CYS A CA  1 
ATOM   623  C C   . CYS A 1 102 ? -29.98206 23.29790 12.40917  1.000 63.40669  ? 121 CYS A C   1 
ATOM   624  O O   . CYS A 1 102 ? -30.04324 22.52058 11.44938  1.000 66.66554  ? 121 CYS A O   1 
ATOM   625  C CB  . CYS A 1 102 ? -32.30602 23.28624 13.34378  1.000 75.63358  ? 121 CYS A CB  1 
ATOM   626  S SG  . CYS A 1 102 ? -31.78501 22.04629 14.54348  1.000 80.40317  ? 121 CYS A SG  1 
ATOM   627  N N   . MET A 1 103 ? -28.89968 23.45091 13.16400  1.000 58.42209  ? 122 MET A N   1 
ATOM   628  C CA  . MET A 1 103 ? -27.67117 22.69788 12.95231  1.000 67.30459  ? 122 MET A CA  1 
ATOM   629  C C   . MET A 1 103 ? -27.18217 22.23910 14.31456  1.000 65.30611  ? 122 MET A C   1 
ATOM   630  O O   . MET A 1 103 ? -26.95953 23.06713 15.20414  1.000 61.81920  ? 122 MET A O   1 
ATOM   631  C CB  . MET A 1 103 ? -26.62463 23.55394 12.23570  1.000 58.18812  ? 122 MET A CB  1 
ATOM   632  C CG  . MET A 1 103 ? -25.26844 22.91338 12.06636  1.000 69.05530  ? 122 MET A CG  1 
ATOM   633  S SD  . MET A 1 103 ? -24.30713 23.79706 10.82296  1.000 56.52344  ? 122 MET A SD  1 
ATOM   634  C CE  . MET A 1 103 ? -25.19092 23.28400 9.35826   1.000 63.40942  ? 122 MET A CE  1 
ATOM   635  N N   . GLY A 1 104 ? -27.04407 20.93004 14.48367  1.000 64.80469  ? 123 GLY A N   1 
ATOM   636  C CA  . GLY A 1 104 ? -26.80004 20.39228 15.81041  1.000 65.03715  ? 123 GLY A CA  1 
ATOM   637  C C   . GLY A 1 104 ? -27.96527 20.74067 16.71417  1.000 69.09790  ? 123 GLY A C   1 
ATOM   638  O O   . GLY A 1 104 ? -29.11038 20.34455 16.46858  1.000 82.23996  ? 123 GLY A O   1 
ATOM   639  N N   . SER A 1 105 ? -27.69199 21.51164 17.76517  1.000 70.36361  ? 124 SER A N   1 
ATOM   640  C CA  . SER A 1 105 ? -28.73256 22.00129 18.65910  1.000 74.93506  ? 124 SER A CA  1 
ATOM   641  C C   . SER A 1 105 ? -28.91792 23.50876 18.55821  1.000 79.37063  ? 124 SER A C   1 
ATOM   642  O O   . SER A 1 105 ? -29.56305 24.10282 19.42835  1.000 81.31002  ? 124 SER A O   1 
ATOM   643  C CB  . SER A 1 105 ? -28.42175 21.61531 20.10666  1.000 73.14533  ? 124 SER A CB  1 
ATOM   644  O OG  . SER A 1 105 ? -27.24100 22.25481 20.55993  1.000 84.35154  ? 124 SER A OG  1 
ATOM   645  N N   . ALA A 1 106 ? -28.37126 24.14202 17.52376  1.000 73.48359  ? 125 ALA A N   1 
ATOM   646  C CA  . ALA A 1 106 ? -28.41555 25.59118 17.37986  1.000 74.45993  ? 125 ALA A CA  1 
ATOM   647  C C   . ALA A 1 106 ? -29.42724 25.96142 16.30421  1.000 74.36506  ? 125 ALA A C   1 
ATOM   648  O O   . ALA A 1 106 ? -29.31145 25.51512 15.15752  1.000 68.48237  ? 125 ALA A O   1 
ATOM   649  C CB  . ALA A 1 106 ? -27.03480 26.14997 17.03689  1.000 59.04421  ? 125 ALA A CB  1 
ATOM   650  N N   . MET A 1 107 ? -30.41493 26.76930 16.67991  1.000 71.25836  ? 126 MET A N   1 
ATOM   651  C CA  . MET A 1 107 ? -31.40926 27.30547 15.76028  1.000 70.35186  ? 126 MET A CA  1 
ATOM   652  C C   . MET A 1 107 ? -31.10745 28.77770 15.52317  1.000 63.51445  ? 126 MET A C   1 
ATOM   653  O O   . MET A 1 107 ? -31.00548 29.55303 16.48015  1.000 64.09104  ? 126 MET A O   1 
ATOM   654  C CB  . MET A 1 107 ? -32.82158 27.14120 16.32505  1.000 74.99545  ? 126 MET A CB  1 
ATOM   655  C CG  . MET A 1 107 ? -33.91701 27.76023 15.47348  1.000 79.48353  ? 126 MET A CG  1 
ATOM   656  S SD  . MET A 1 107 ? -34.31727 26.75540 14.03268  1.000 93.40718  ? 126 MET A SD  1 
ATOM   657  C CE  . MET A 1 107 ? -35.03852 25.32271 14.83138  1.000 76.86680  ? 126 MET A CE  1 
ATOM   658  N N   . ARG A 1 108 ? -30.96943 29.16294 14.25611  1.000 63.19348  ? 127 ARG A N   1 
ATOM   659  C CA  . ARG A 1 108 ? -30.62521 30.53540 13.91041  1.000 62.29246  ? 127 ARG A CA  1 
ATOM   660  C C   . ARG A 1 108 ? -31.46547 31.00958 12.73727  1.000 65.60794  ? 127 ARG A C   1 
ATOM   661  O O   . ARG A 1 108 ? -31.70455 30.25502 11.79203  1.000 62.93346  ? 127 ARG A O   1 
ATOM   662  C CB  . ARG A 1 108 ? -29.14056 30.67247 13.54856  1.000 56.18837  ? 127 ARG A CB  1 
ATOM   663  C CG  . ARG A 1 108 ? -28.18230 30.40102 14.68580  1.000 52.72021  ? 127 ARG A CG  1 
ATOM   664  C CD  . ARG A 1 108 ? -28.38542 31.37999 15.82409  1.000 51.08812  ? 127 ARG A CD  1 
ATOM   665  N NE  . ARG A 1 108 ? -27.29990 31.29658 16.79269  1.000 65.97540  ? 127 ARG A NE  1 
ATOM   666  C CZ  . ARG A 1 108 ? -27.22809 30.39791 17.76478  1.000 68.41791  ? 127 ARG A CZ  1 
ATOM   667  N NH1 . ARG A 1 108 ? -28.17630 29.49191 17.94031  1.000 64.94041  ? 127 ARG A NH1 1 
ATOM   668  N NH2 . ARG A 1 108 ? -26.17722 30.40752 18.58011  1.000 75.44154  ? 127 ARG A NH2 1 
ATOM   669  N N   . SER A 1 109 ? -31.90127 32.26591 12.79642  1.000 71.58447  ? 128 SER A N   1 
ATOM   670  C CA  . SER A 1 109 ? -32.52281 32.90206 11.64261  1.000 64.30880  ? 128 SER A CA  1 
ATOM   671  C C   . SER A 1 109 ? -31.42731 33.30660 10.66339  1.000 62.89121  ? 128 SER A C   1 
ATOM   672  O O   . SER A 1 109 ? -30.57075 34.13718 10.98614  1.000 63.90594  ? 128 SER A O   1 
ATOM   673  C CB  . SER A 1 109 ? -33.34827 34.11276 12.07012  1.000 76.56075  ? 128 SER A CB  1 
ATOM   674  O OG  . SER A 1 109 ? -34.01478 34.69209 10.96065  1.000 75.57694  ? 128 SER A OG  1 
ATOM   675  N N   . ILE A 1 110 ? -31.45192 32.71512 9.47433   1.000 58.58362  ? 129 ILE A N   1 
ATOM   676  C CA  . ILE A 1 110 ? -30.39080 32.84350 8.48799   1.000 66.19235  ? 129 ILE A CA  1 
ATOM   677  C C   . ILE A 1 110 ? -30.98732 33.39225 7.20251   1.000 57.02432  ? 129 ILE A C   1 
ATOM   678  O O   . ILE A 1 110 ? -32.05943 32.95838 6.77088   1.000 65.59216  ? 129 ILE A O   1 
ATOM   679  C CB  . ILE A 1 110 ? -29.70317 31.48415 8.23356   1.000 57.46891  ? 129 ILE A CB  1 
ATOM   680  C CG1 . ILE A 1 110 ? -29.01885 30.98456 9.50721   1.000 68.10807  ? 129 ILE A CG1 1 
ATOM   681  C CG2 . ILE A 1 110 ? -28.72025 31.57777 7.08303   1.000 57.49172  ? 129 ILE A CG2 1 
ATOM   682  C CD1 . ILE A 1 110 ? -28.06614 31.98657 10.12061  1.000 56.53095  ? 129 ILE A CD1 1 
ATOM   683  N N   . GLU A 1 111 ? -30.29388 34.34382 6.59248   1.000 57.81045  ? 130 GLU A N   1 
ATOM   684  C CA  . GLU A 1 111 ? -30.67614 34.85333 5.28555   1.000 58.52243  ? 130 GLU A CA  1 
ATOM   685  C C   . GLU A 1 111 ? -30.06928 33.97051 4.19974   1.000 50.31534  ? 130 GLU A C   1 
ATOM   686  O O   . GLU A 1 111 ? -28.86369 33.70347 4.21250   1.000 59.20906  ? 130 GLU A O   1 
ATOM   687  C CB  . GLU A 1 111 ? -30.22008 36.30438 5.13536   1.000 54.74328  ? 130 GLU A CB  1 
ATOM   688  C CG  . GLU A 1 111 ? -30.14913 36.79212 3.70992   1.000 71.75051  ? 130 GLU A CG  1 
ATOM   689  C CD  . GLU A 1 111 ? -29.86160 38.27720 3.61664   1.000 80.03105  ? 130 GLU A CD  1 
ATOM   690  O OE1 . GLU A 1 111 ? -30.49043 39.05565 4.36849   1.000 74.95069  ? 130 GLU A OE1 1 
ATOM   691  O OE2 . GLU A 1 111 ? -29.00193 38.66202 2.79406   1.000 76.37895  ? 130 GLU A OE2 1 
ATOM   692  N N   . VAL A 1 112 ? -30.90836 33.49759 3.27872   1.000 49.50051  ? 131 VAL A N   1 
ATOM   693  C CA  . VAL A 1 112 ? -30.49804 32.55070 2.24798   1.000 56.30184  ? 131 VAL A CA  1 
ATOM   694  C C   . VAL A 1 112 ? -31.05216 32.99479 0.90000   1.000 60.08871  ? 131 VAL A C   1 
ATOM   695  O O   . VAL A 1 112 ? -32.19846 33.45202 0.79995   1.000 62.81965  ? 131 VAL A O   1 
ATOM   696  C CB  . VAL A 1 112 ? -30.93540 31.09904 2.56329   1.000 54.99100  ? 131 VAL A CB  1 
ATOM   697  C CG1 . VAL A 1 112 ? -30.27321 30.59907 3.83863   1.000 50.35937  ? 131 VAL A CG1 1 
ATOM   698  C CG2 . VAL A 1 112 ? -32.44554 30.98126 2.65724   1.000 62.45599  ? 131 VAL A CG2 1 
ATOM   699  N N   . ASN A 1 113 ? -30.21964 32.87440 -0.13247  1.000 65.59135  ? 132 ASN A N   1 
ATOM   700  C CA  . ASN A 1 113 ? -30.63354 33.07052 -1.51352  1.000 66.29898  ? 132 ASN A CA  1 
ATOM   701  C C   . ASN A 1 113 ? -31.13867 31.74477 -2.06748  1.000 62.92450  ? 132 ASN A C   1 
ATOM   702  O O   . ASN A 1 113 ? -30.47617 30.71550 -1.91544  1.000 67.60121  ? 132 ASN A O   1 
ATOM   703  C CB  . ASN A 1 113 ? -29.46422 33.57254 -2.36297  1.000 73.27534  ? 132 ASN A CB  1 
ATOM   704  C CG  . ASN A 1 113 ? -28.83821 34.84301 -1.81489  1.000 83.00393  ? 132 ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 113 ? -28.90693 35.12045 -0.61815  1.000 87.30389  ? 132 ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 113 ? -28.21356 35.61832 -2.69350  1.000 97.15099  ? 132 ASN A ND2 1 
ATOM   707  N N   . LEU A 1 114 ? -32.30019 31.77053 -2.71686  1.000 66.47438  ? 133 LEU A N   1 
ATOM   708  C CA  . LEU A 1 114 ? -32.88081 30.57021 -3.31295  1.000 64.91152  ? 133 LEU A CA  1 
ATOM   709  C C   . LEU A 1 114 ? -32.30075 30.40054 -4.71147  1.000 65.19070  ? 133 LEU A C   1 
ATOM   710  O O   . LEU A 1 114 ? -32.55719 31.21671 -5.60167  1.000 75.71714  ? 133 LEU A O   1 
ATOM   711  C CB  . LEU A 1 114 ? -34.40409 30.66781 -3.35626  1.000 60.80269  ? 133 LEU A CB  1 
ATOM   712  C CG  . LEU A 1 114 ? -35.11290 30.85486 -2.01539  1.000 62.52640  ? 133 LEU A CG  1 
ATOM   713  C CD1 . LEU A 1 114 ? -36.61334 30.97296 -2.21497  1.000 64.07310  ? 133 LEU A CD1 1 
ATOM   714  C CD2 . LEU A 1 114 ? -34.78271 29.69909 -1.08725  1.000 63.44996  ? 133 LEU A CD2 1 
ATOM   715  N N   . THR A 1 115 ? -31.51241 29.34826 -4.90338  1.000 66.43743  ? 134 THR A N   1 
ATOM   716  C CA  . THR A 1 115 ? -30.85813 29.08611 -6.17509  1.000 76.06312  ? 134 THR A CA  1 
ATOM   717  C C   . THR A 1 115 ? -31.34652 27.77809 -6.79061  1.000 82.86807  ? 134 THR A C   1 
ATOM   718  O O   . THR A 1 115 ? -31.67907 26.82181 -6.08394  1.000 74.10486  ? 134 THR A O   1 
ATOM   719  C CB  . THR A 1 115 ? -29.33606 29.06284 -6.00848  1.000 77.52731  ? 134 THR A CB  1 
ATOM   720  O OG1 . THR A 1 115 ? -28.72343 28.58504 -7.21198  1.000 87.36503  ? 134 THR A OG1 1 
ATOM   721  C CG2 . THR A 1 115 ? -28.93788 28.17892 -4.83937  1.000 81.77535  ? 134 THR A CG2 1 
ATOM   722  N N   . ASP A 1 116 ? -31.38709 27.75435 -8.12239  1.000 100.55705 ? 135 ASP A N   1 
ATOM   723  C CA  . ASP A 1 116 ? -31.76653 26.59130 -8.92713  1.000 106.81606 ? 135 ASP A CA  1 
ATOM   724  C C   . ASP A 1 116 ? -30.56481 25.72740 -9.26062  1.000 114.76139 ? 135 ASP A C   1 
ATOM   725  O O   . ASP A 1 116 ? -30.48130 25.19075 -10.36862 1.000 120.37701 ? 135 ASP A O   1 
ATOM   726  C CB  . ASP A 1 116 ? -32.45702 27.03592 -10.21029 1.000 114.77501 ? 135 ASP A CB  1 
ATOM   727  C CG  . ASP A 1 116 ? -32.66596 28.52004 -10.26966 1.000 121.56201 ? 135 ASP A CG  1 
ATOM   728  O OD1 . ASP A 1 116 ? -33.39736 29.04212 -9.40634  1.000 118.33581 ? 135 ASP A OD1 1 
ATOM   729  O OD2 . ASP A 1 116 ? -32.08574 29.16619 -11.16625 1.000 127.27171 ? 135 ASP A OD2 1 
ATOM   730  N N   . ARG A 1 117 ? -29.60817 25.58756 -8.34590  1.000 119.87994 ? 136 ARG A N   1 
ATOM   731  C CA  . ARG A 1 117 ? -28.44309 24.76275 -8.62653  1.000 123.13022 ? 136 ARG A CA  1 
ATOM   732  C C   . ARG A 1 117 ? -28.84198 23.31015 -8.85682  1.000 129.64144 ? 136 ARG A C   1 
ATOM   733  O O   . ARG A 1 117 ? -29.95075 22.87443 -8.53261  1.000 127.74255 ? 136 ARG A O   1 
ATOM   734  C CB  . ARG A 1 117 ? -27.44213 24.81743 -7.47237  1.000 117.04055 ? 136 ARG A CB  1 
ATOM   735  C CG  . ARG A 1 117 ? -26.68168 26.11706 -7.32577  1.000 126.72546 ? 136 ARG A CG  1 
ATOM   736  C CD  . ARG A 1 117 ? -25.87959 26.09515 -6.03459  1.000 124.65598 ? 136 ARG A CD  1 
ATOM   737  N NE  . ARG A 1 117 ? -26.73654 25.81813 -4.88725  1.000 119.22911 ? 136 ARG A NE  1 
ATOM   738  C CZ  . ARG A 1 117 ? -26.30002 25.55825 -3.66235  1.000 117.39955 ? 136 ARG A CZ  1 
ATOM   739  N NH1 . ARG A 1 117 ? -25.00735 25.50754 -3.38442  1.000 123.98457 ? 136 ARG A NH1 1 
ATOM   740  N NH2 . ARG A 1 117 ? -27.18339 25.33896 -2.69232  1.000 103.79829 ? 136 ARG A NH2 1 
ATOM   741  N N   . SER A 1 118 ? -27.91635 22.56310 -9.44991  1.000 125.21116 ? 137 SER A N   1 
ATOM   742  C CA  . SER A 1 118 ? -28.11614 21.13373 -9.61350  1.000 124.21265 ? 137 SER A CA  1 
ATOM   743  C C   . SER A 1 118 ? -28.25463 20.47488 -8.24855  1.000 123.39008 ? 137 SER A C   1 
ATOM   744  O O   . SER A 1 118 ? -27.57566 20.84902 -7.28770  1.000 121.17837 ? 137 SER A O   1 
ATOM   745  C CB  . SER A 1 118 ? -26.94741 20.51750 -10.38584 1.000 124.18227 ? 137 SER A CB  1 
ATOM   746  O OG  . SER A 1 118 ? -25.73259 20.63644 -9.66302  1.000 127.54053 ? 137 SER A OG  1 
ATOM   747  N N   . ALA A 1 119 ? -29.15612 19.49464 -8.16224  1.000 128.40994 ? 138 ALA A N   1 
ATOM   748  C CA  . ALA A 1 119 ? -29.27621 18.69470 -6.95014  1.000 126.09321 ? 138 ALA A CA  1 
ATOM   749  C C   . ALA A 1 119 ? -27.98964 17.95265 -6.62259  1.000 121.33932 ? 138 ALA A C   1 
ATOM   750  O O   . ALA A 1 119 ? -27.85880 17.43118 -5.50940  1.000 109.32316 ? 138 ALA A O   1 
ATOM   751  C CB  . ALA A 1 119 ? -30.43266 17.70219 -7.08620  1.000 115.45239 ? 138 ALA A CB  1 
ATOM   752  N N   . PHE A 1 120 ? -27.04845 17.89208 -7.56683  1.000 133.10007 ? 139 PHE A N   1 
ATOM   753  C CA  . PHE A 1 120 ? -25.74303 17.29741 -7.30762  1.000 127.14977 ? 139 PHE A CA  1 
ATOM   754  C C   . PHE A 1 120 ? -24.99289 18.06717 -6.22602  1.000 123.07502 ? 139 PHE A C   1 
ATOM   755  O O   . PHE A 1 120 ? -24.58904 17.49441 -5.20987  1.000 121.99834 ? 139 PHE A O   1 
ATOM   756  C CB  . PHE A 1 120 ? -24.93802 17.24426 -8.60763  1.000 130.51430 ? 139 PHE A CB  1 
ATOM   757  C CG  . PHE A 1 120 ? -25.59553 16.43649 -9.69583  1.000 132.91422 ? 139 PHE A CG  1 
ATOM   758  C CD1 . PHE A 1 120 ? -26.49682 15.42955 -9.38532  1.000 135.49911 ? 139 PHE A CD1 1 
ATOM   759  C CD2 . PHE A 1 120 ? -25.31475 16.68662 -11.02881 1.000 143.94810 ? 139 PHE A CD2 1 
ATOM   760  C CE1 . PHE A 1 120 ? -27.10451 14.68753 -10.38322 1.000 144.48225 ? 139 PHE A CE1 1 
ATOM   761  C CE2 . PHE A 1 120 ? -25.91874 15.94725 -12.03092 1.000 152.96964 ? 139 PHE A CE2 1 
ATOM   762  C CZ  . PHE A 1 120 ? -26.81425 14.94674 -11.70731 1.000 150.79166 ? 139 PHE A CZ  1 
ATOM   763  N N   . GLN A 1 121 ? -24.79492 19.37192 -6.42884  1.000 112.11979 ? 140 GLN A N   1 
ATOM   764  C CA  . GLN A 1 121 ? -24.08192 20.21272 -5.46948  1.000 96.78553  ? 140 GLN A CA  1 
ATOM   765  C C   . GLN A 1 121 ? -24.75679 20.21236 -4.09996  1.000 84.75750  ? 140 GLN A C   1 
ATOM   766  O O   . GLN A 1 121 ? -25.81545 19.60058 -3.92527  1.000 90.74525  ? 140 GLN A O   1 
ATOM   767  C CB  . GLN A 1 121 ? -23.96602 21.63929 -6.00402  1.000 103.90132 ? 140 GLN A CB  1 
ATOM   768  C CG  . GLN A 1 121 ? -23.16976 21.74195 -7.28920  1.000 110.74411 ? 140 GLN A CG  1 
ATOM   769  C CD  . GLN A 1 121 ? -22.50376 23.09058 -7.44170  1.000 120.79265 ? 140 GLN A CD  1 
ATOM   770  O OE1 . GLN A 1 121 ? -23.08584 24.12374 -7.11067  1.000 123.64810 ? 140 GLN A OE1 1 
ATOM   771  N NE2 . GLN A 1 121 ? -21.26859 23.08840 -7.92920  1.000 117.55264 ? 140 GLN A NE2 1 
ATOM   772  N N   . TYR A 1 122 ? -24.19480 20.93820 -3.13594  1.000 73.90860  ? 141 TYR A N   1 
ATOM   773  C CA  . TYR A 1 122 ? -24.73909 20.88241 -1.78027  1.000 72.21232  ? 141 TYR A CA  1 
ATOM   774  C C   . TYR A 1 122 ? -25.99931 21.73221 -1.68092  1.000 69.87076  ? 141 TYR A C   1 
ATOM   775  O O   . TYR A 1 122 ? -25.98885 22.89824 -2.08629  1.000 82.31159  ? 141 TYR A O   1 
ATOM   776  C CB  . TYR A 1 122 ? -23.70717 21.33735 -0.74845  1.000 55.70229  ? 141 TYR A CB  1 
ATOM   777  C CG  . TYR A 1 122 ? -22.75434 20.24060 -0.33033  1.000 65.50778  ? 141 TYR A CG  1 
ATOM   778  C CD1 . TYR A 1 122 ? -21.52702 20.07634 -0.95275  1.000 66.99503  ? 141 TYR A CD1 1 
ATOM   779  C CD2 . TYR A 1 122 ? -23.11255 19.33205 0.66017   1.000 70.67299  ? 141 TYR A CD2 1 
ATOM   780  C CE1 . TYR A 1 122 ? -20.66581 19.05728 -0.57558  1.000 71.45904  ? 141 TYR A CE1 1 
ATOM   781  C CE2 . TYR A 1 122 ? -22.25938 18.31400 1.04594   1.000 65.85939  ? 141 TYR A CE2 1 
ATOM   782  C CZ  . TYR A 1 122 ? -21.03885 18.17876 0.42297   1.000 67.65459  ? 141 TYR A CZ  1 
ATOM   783  O OH  . TYR A 1 122 ? -20.18718 17.16500 0.80001   1.000 69.02702  ? 141 TYR A OH  1 
ATOM   784  N N   . PRO A 1 123 ? -27.10226 21.16932 -1.17915  1.000 67.47499  ? 142 PRO A N   1 
ATOM   785  C CA  . PRO A 1 123 ? -28.37028 21.91476 -1.14883  1.000 63.60257  ? 142 PRO A CA  1 
ATOM   786  C C   . PRO A 1 123 ? -28.31075 23.18512 -0.32828  1.000 64.63695  ? 142 PRO A C   1 
ATOM   787  O O   . PRO A 1 123 ? -28.98622 24.16295 -0.67178  1.000 67.96625  ? 142 PRO A O   1 
ATOM   788  C CB  . PRO A 1 123 ? -29.34992 20.90333 -0.53858  1.000 64.66701  ? 142 PRO A CB  1 
ATOM   789  C CG  . PRO A 1 123 ? -28.72587 19.56609 -0.78191  1.000 70.38481  ? 142 PRO A CG  1 
ATOM   790  C CD  . PRO A 1 123 ? -27.25239 19.79490 -0.67520  1.000 65.50183  ? 142 PRO A CD  1 
ATOM   791  N N   . LEU A 1 124 ? -27.54586 23.19539 0.75954   1.000 56.89516  ? 143 LEU A N   1 
ATOM   792  C CA  . LEU A 1 124 ? -27.39614 24.37038 1.60586   1.000 58.42917  ? 143 LEU A CA  1 
ATOM   793  C C   . LEU A 1 124 ? -25.92464 24.75060 1.65760   1.000 66.52319  ? 143 LEU A C   1 
ATOM   794  O O   . LEU A 1 124 ? -25.08675 23.95297 2.08997   1.000 58.84311  ? 143 LEU A O   1 
ATOM   795  C CB  . LEU A 1 124 ? -27.93351 24.10973 3.01409   1.000 55.25058  ? 143 LEU A CB  1 
ATOM   796  C CG  . LEU A 1 124 ? -27.76641 25.25266 4.01908   1.000 60.36312  ? 143 LEU A CG  1 
ATOM   797  C CD1 . LEU A 1 124 ? -28.48917 26.51069 3.55608   1.000 49.38154  ? 143 LEU A CD1 1 
ATOM   798  C CD2 . LEU A 1 124 ? -28.24535 24.82502 5.39484   1.000 56.40676  ? 143 LEU A CD2 1 
ATOM   799  N N   . LEU A 1 125 ? -25.61331 25.96493 1.22395   1.000 67.01203  ? 144 LEU A N   1 
ATOM   800  C CA  . LEU A 1 125 ? -24.27541 26.52409 1.34313   1.000 49.71311  ? 144 LEU A CA  1 
ATOM   801  C C   . LEU A 1 125 ? -24.33427 27.60869 2.40755   1.000 50.87791  ? 144 LEU A C   1 
ATOM   802  O O   . LEU A 1 125 ? -25.06588 28.59125 2.25234   1.000 57.68532  ? 144 LEU A O   1 
ATOM   803  C CB  . LEU A 1 125 ? -23.78982 27.07724 0.00404   1.000 55.10640  ? 144 LEU A CB  1 
ATOM   804  C CG  . LEU A 1 125 ? -22.31562 27.47485 -0.06945  1.000 70.17658  ? 144 LEU A CG  1 
ATOM   805  C CD1 . LEU A 1 125 ? -21.75645 27.11995 -1.43663  1.000 69.74364  ? 144 LEU A CD1 1 
ATOM   806  C CD2 . LEU A 1 125 ? -22.12009 28.95759 0.22500   1.000 65.65628  ? 144 LEU A CD2 1 
ATOM   807  N N   . ILE A 1 126 ? -23.58511 27.42522 3.48785   1.000 52.20826  ? 145 ILE A N   1 
ATOM   808  C CA  . ILE A 1 126 ? -23.62578 28.33017 4.63046   1.000 51.15733  ? 145 ILE A CA  1 
ATOM   809  C C   . ILE A 1 126 ? -22.40192 29.23702 4.57129   1.000 51.36953  ? 145 ILE A C   1 
ATOM   810  O O   . ILE A 1 126 ? -21.26954 28.79006 4.78581   1.000 49.24887  ? 145 ILE A O   1 
ATOM   811  C CB  . ILE A 1 126 ? -23.69272 27.55538 5.95074   1.000 44.25955  ? 145 ILE A CB  1 
ATOM   812  C CG1 . ILE A 1 126 ? -24.91851 26.64850 5.95000   1.000 50.60934  ? 145 ILE A CG1 1 
ATOM   813  C CG2 . ILE A 1 126 ? -23.75685 28.50875 7.12619   1.000 53.97543  ? 145 ILE A CG2 1 
ATOM   814  C CD1 . ILE A 1 126 ? -25.16867 25.98967 7.25808   1.000 48.90142  ? 145 ILE A CD1 1 
ATOM   815  N N   . GLY A 1 127 ? -22.63194 30.51686 4.29037   1.000 49.24500  ? 146 GLY A N   1 
ATOM   816  C CA  . GLY A 1 127 ? -21.56042 31.47462 4.13973   1.000 53.54787  ? 146 GLY A CA  1 
ATOM   817  C C   . GLY A 1 127 ? -21.09472 32.04442 5.46628   1.000 51.34662  ? 146 GLY A C   1 
ATOM   818  O O   . GLY A 1 127 ? -21.56410 31.67812 6.54487   1.000 51.29584  ? 146 GLY A O   1 
ATOM   819  N N   . SER A 1 128 ? -20.17380 33.00598 5.36637   1.000 49.69745  ? 147 SER A N   1 
ATOM   820  C CA  . SER A 1 128 ? -19.51607 33.52373 6.56232   1.000 57.93563  ? 147 SER A CA  1 
ATOM   821  C C   . SER A 1 128 ? -20.49304 34.26559 7.46744   1.000 56.58704  ? 147 SER A C   1 
ATOM   822  O O   . SER A 1 128 ? -20.39695 34.16607 8.69401   1.000 58.51433  ? 147 SER A O   1 
ATOM   823  C CB  . SER A 1 128 ? -18.34986 34.43482 6.17333   1.000 54.80060  ? 147 SER A CB  1 
ATOM   824  O OG  . SER A 1 128 ? -18.79560 35.55744 5.43195   1.000 57.97755  ? 147 SER A OG  1 
ATOM   825  N N   . GLU A 1 129 ? -21.43977 35.01103 6.88984   1.000 54.38611  ? 148 GLU A N   1 
ATOM   826  C CA  A GLU A 1 129 ? -22.40199 35.74083 7.71093   0.504 58.09212  ? 148 GLU A CA  1 
ATOM   827  C CA  B GLU A 1 129 ? -22.40114 35.74069 7.71218   0.496 59.46390  ? 148 GLU A CA  1 
ATOM   828  C C   . GLU A 1 129 ? -23.27593 34.78778 8.51735   1.000 51.70356  ? 148 GLU A C   1 
ATOM   829  O O   . GLU A 1 129 ? -23.51813 35.01174 9.71048   1.000 53.20976  ? 148 GLU A O   1 
ATOM   830  C CB  A GLU A 1 129 ? -23.26314 36.64676 6.83085   0.504 57.25292  ? 148 GLU A CB  1 
ATOM   831  C CB  B GLU A 1 129 ? -23.26169 36.65155 6.83597   0.496 61.36999  ? 148 GLU A CB  1 
ATOM   832  C CG  A GLU A 1 129 ? -22.46788 37.65632 6.01987   0.504 66.53626  ? 148 GLU A CG  1 
ATOM   833  C CG  B GLU A 1 129 ? -22.47222 37.71233 6.08680   0.496 61.29245  ? 148 GLU A CG  1 
ATOM   834  C CD  A GLU A 1 129 ? -23.34919 38.53202 5.15212   0.504 71.24349  ? 148 GLU A CD  1 
ATOM   835  C CD  B GLU A 1 129 ? -21.68608 38.62183 7.01284   0.496 65.58849  ? 148 GLU A CD  1 
ATOM   836  O OE1 A GLU A 1 129 ? -23.13852 39.76390 5.14086   0.504 70.20012  ? 148 GLU A OE1 1 
ATOM   837  O OE1 B GLU A 1 129 ? -22.20665 38.97373 8.09297   0.496 62.37088  ? 148 GLU A OE1 1 
ATOM   838  O OE2 A GLU A 1 129 ? -24.25538 37.98781 4.48533   0.504 64.85864  ? 148 GLU A OE2 1 
ATOM   839  O OE2 B GLU A 1 129 ? -20.54274 38.98067 6.66096   0.496 74.40991  ? 148 GLU A OE2 1 
ATOM   840  N N   . ALA A 1 130 ? -23.75601 33.71487 7.88540   1.000 52.00615  ? 149 ALA A N   1 
ATOM   841  C CA  . ALA A 1 130 ? -24.56819 32.74043 8.60737   1.000 57.00397  ? 149 ALA A CA  1 
ATOM   842  C C   . ALA A 1 130 ? -23.74629 32.00631 9.65949   1.000 51.21836  ? 149 ALA A C   1 
ATOM   843  O O   . ALA A 1 130 ? -24.23764 31.73942 10.76259  1.000 50.83552  ? 149 ALA A O   1 
ATOM   844  C CB  . ALA A 1 130 ? -25.20014 31.75273 7.62964   1.000 50.60142  ? 149 ALA A CB  1 
ATOM   845  N N   . LEU A 1 131 ? -22.49558 31.66780 9.33530   1.000 50.14935  ? 150 LEU A N   1 
ATOM   846  C CA  . LEU A 1 131 ? -21.62219 31.03478 10.31899  1.000 51.74483  ? 150 LEU A CA  1 
ATOM   847  C C   . LEU A 1 131 ? -21.38172 31.95422 11.51006  1.000 50.20879  ? 150 LEU A C   1 
ATOM   848  O O   . LEU A 1 131 ? -21.26727 31.49135 12.65124  1.000 51.89135  ? 150 LEU A O   1 
ATOM   849  C CB  . LEU A 1 131 ? -20.29520 30.65344 9.66613   1.000 49.38028  ? 150 LEU A CB  1 
ATOM   850  C CG  . LEU A 1 131 ? -20.32567 29.55170 8.60786   1.000 48.77684  ? 150 LEU A CG  1 
ATOM   851  C CD1 . LEU A 1 131 ? -18.99796 29.49393 7.86387   1.000 46.61796  ? 150 LEU A CD1 1 
ATOM   852  C CD2 . LEU A 1 131 ? -20.65185 28.21746 9.24231   1.000 42.06159  ? 150 LEU A CD2 1 
ATOM   853  N N   . LYS A 1 132 ? -21.29652 33.26289 11.25965  1.000 52.73702  ? 151 LYS A N   1 
ATOM   854  C CA  . LYS A 1 132 ? -21.20410 34.23064 12.34680  1.000 56.75196  ? 151 LYS A CA  1 
ATOM   855  C C   . LYS A 1 132 ? -22.47809 34.23782 13.17840  1.000 59.56224  ? 151 LYS A C   1 
ATOM   856  O O   . LYS A 1 132 ? -22.42099 34.29432 14.41217  1.000 62.55282  ? 151 LYS A O   1 
ATOM   857  C CB  . LYS A 1 132 ? -20.92936 35.62318 11.77952  1.000 57.05715  ? 151 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 132 ? -19.52837 35.80862 11.23118  1.000 62.16874  ? 151 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 132 ? -19.37954 37.14681 10.52716  1.000 66.07332  ? 151 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 132 ? -19.84322 38.29660 11.39406  1.000 64.35051  ? 151 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 132 ? -19.89206 39.55591 10.60759  1.000 84.00355  ? 151 LYS A NZ  1 
ATOM   862  N N   . ARG A 1 133 ? -23.63855 34.17774 12.52039  1.000 51.52423  ? 152 ARG A N   1 
ATOM   863  C CA  . ARG A 1 133 ? -24.89092 34.09366 13.26256  1.000 56.86391  ? 152 ARG A CA  1 
ATOM   864  C C   . ARG A 1 133 ? -24.95595 32.82122 14.09790  1.000 56.76162  ? 152 ARG A C   1 
ATOM   865  O O   . ARG A 1 133 ? -25.56103 32.81403 15.17541  1.000 59.92758  ? 152 ARG A O   1 
ATOM   866  C CB  . ARG A 1 133 ? -26.07584 34.16937 12.30083  1.000 62.14783  ? 152 ARG A CB  1 
ATOM   867  C CG  . ARG A 1 133 ? -26.23635 35.52585 11.63328  1.000 63.55440  ? 152 ARG A CG  1 
ATOM   868  C CD  . ARG A 1 133 ? -27.66653 35.75159 11.17838  1.000 69.83669  ? 152 ARG A CD  1 
ATOM   869  N NE  . ARG A 1 133 ? -27.81556 36.99376 10.42974  1.000 77.88576  ? 152 ARG A NE  1 
ATOM   870  C CZ  . ARG A 1 133 ? -28.91116 37.33847 9.76719   1.000 84.06303  ? 152 ARG A CZ  1 
ATOM   871  N NH1 . ARG A 1 133 ? -29.00123 38.49706 9.13275   1.000 91.84220  ? 152 ARG A NH1 1 
ATOM   872  N NH2 . ARG A 1 133 ? -29.94215 36.49897 9.73928   1.000 79.31114  ? 152 ARG A NH2 1 
ATOM   873  N N   . PHE A 1 134 ? -24.32038 31.74850 13.63483  1.000 61.52428  ? 153 PHE A N   1 
ATOM   874  C CA  . PHE A 1 134 ? -24.30438 30.48659 14.36069  1.000 60.09338  ? 153 PHE A CA  1 
ATOM   875  C C   . PHE A 1 134 ? -23.25458 30.44000 15.46136  1.000 61.88630  ? 153 PHE A C   1 
ATOM   876  O O   . PHE A 1 134 ? -23.18526 29.43398 16.17694  1.000 63.09606  ? 153 PHE A O   1 
ATOM   877  C CB  . PHE A 1 134 ? -24.06348 29.32513 13.39446  1.000 56.21168  ? 153 PHE A CB  1 
ATOM   878  C CG  . PHE A 1 134 ? -25.32081 28.71284 12.85607  1.000 52.11063  ? 153 PHE A CG  1 
ATOM   879  C CD1 . PHE A 1 134 ? -26.02954 27.79120 13.60425  1.000 61.56411  ? 153 PHE A CD1 1 
ATOM   880  C CD2 . PHE A 1 134 ? -25.78443 29.04599 11.59578  1.000 52.16191  ? 153 PHE A CD2 1 
ATOM   881  C CE1 . PHE A 1 134 ? -27.18927 27.22245 13.11104  1.000 69.67022  ? 153 PHE A CE1 1 
ATOM   882  C CE2 . PHE A 1 134 ? -26.93855 28.48049 11.09456  1.000 58.74885  ? 153 PHE A CE2 1 
ATOM   883  C CZ  . PHE A 1 134 ? -27.64381 27.56737 11.85228  1.000 60.69257  ? 153 PHE A CZ  1 
ATOM   884  N N   . ASP A 1 135 ? -22.44836 31.49003 15.61992  1.000 66.50454  ? 154 ASP A N   1 
ATOM   885  C CA  . ASP A 1 135 ? -21.33244 31.48066 16.56416  1.000 70.44504  ? 154 ASP A CA  1 
ATOM   886  C C   . ASP A 1 135 ? -20.42663 30.28387 16.28589  1.000 64.09173  ? 154 ASP A C   1 
ATOM   887  O O   . ASP A 1 135 ? -20.04877 29.53048 17.18489  1.000 70.53012  ? 154 ASP A O   1 
ATOM   888  C CB  . ASP A 1 135 ? -21.82891 31.46777 18.01166  1.000 75.74675  ? 154 ASP A CB  1 
ATOM   889  C CG  . ASP A 1 135 ? -22.89968 32.50582 18.27190  1.000 72.95785  ? 154 ASP A CG  1 
ATOM   890  O OD1 . ASP A 1 135 ? -22.72848 33.66248 17.83514  1.000 76.85919  ? 154 ASP A OD1 1 
ATOM   891  O OD2 . ASP A 1 135 ? -23.91476 32.16261 18.91391  1.000 71.97036  ? 154 ASP A OD2 1 
ATOM   892  N N   . ALA A 1 136 ? -20.09563 30.10031 15.01299  1.000 47.35063  ? 155 ALA A N   1 
ATOM   893  C CA  . ALA A 1 136 ? -19.45846 28.87878 14.55181  1.000 64.30851  ? 155 ALA A CA  1 
ATOM   894  C C   . ALA A 1 136 ? -17.95675 29.05742 14.36589  1.000 60.57559  ? 155 ALA A C   1 
ATOM   895  O O   . ALA A 1 136 ? -17.47086 30.13223 14.00537  1.000 57.37844  ? 155 ALA A O   1 
ATOM   896  C CB  . ALA A 1 136 ? -20.08423 28.40549 13.23776  1.000 53.89565  ? 155 ALA A CB  1 
ATOM   897  N N   . LEU A 1 137 ? -17.22927 27.98029 14.64061  1.000 58.55193  ? 156 LEU A N   1 
ATOM   898  C CA  . LEU A 1 137 ? -15.84195 27.81069 14.24037  1.000 45.88305  ? 156 LEU A CA  1 
ATOM   899  C C   . LEU A 1 137 ? -15.78519 26.62348 13.29365  1.000 52.10430  ? 156 LEU A C   1 
ATOM   900  O O   . LEU A 1 137 ? -16.28433 25.54362 13.62229  1.000 55.88502  ? 156 LEU A O   1 
ATOM   901  C CB  . LEU A 1 137 ? -14.92803 27.56864 15.44316  1.000 50.33593  ? 156 LEU A CB  1 
ATOM   902  C CG  . LEU A 1 137 ? -15.00233 28.54330 16.61580  1.000 62.62779  ? 156 LEU A CG  1 
ATOM   903  C CD1 . LEU A 1 137 ? -13.99212 28.16232 17.68998  1.000 55.16042  ? 156 LEU A CD1 1 
ATOM   904  C CD2 . LEU A 1 137 ? -14.77994 29.96614 16.14313  1.000 54.37504  ? 156 LEU A CD2 1 
ATOM   905  N N   . VAL A 1 138 ? -15.20509 26.82324 12.11820  1.000 49.74046  ? 157 VAL A N   1 
ATOM   906  C CA  . VAL A 1 138 ? -15.16390 25.78488 11.09599  1.000 53.04414  ? 157 VAL A CA  1 
ATOM   907  C C   . VAL A 1 138 ? -13.84349 25.03067 11.19405  1.000 47.01309  ? 157 VAL A C   1 
ATOM   908  O O   . VAL A 1 138 ? -12.76990 25.60411 10.98466  1.000 54.96320  ? 157 VAL A O   1 
ATOM   909  C CB  . VAL A 1 138 ? -15.36578 26.37481 9.69362   1.000 57.53629  ? 157 VAL A CB  1 
ATOM   910  C CG1 . VAL A 1 138 ? -15.29730 25.27426 8.64999   1.000 50.22021  ? 157 VAL A CG1 1 
ATOM   911  C CG2 . VAL A 1 138 ? -16.71127 27.07449 9.62199   1.000 52.52662  ? 157 VAL A CG2 1 
ATOM   912  N N   . ASP A 1 139 ? -13.92911 23.73929 11.51792  1.000 56.07798  ? 158 ASP A N   1 
ATOM   913  C CA  . ASP A 1 139 ? -12.79427 22.83375 11.51249  1.000 57.53444  ? 158 ASP A CA  1 
ATOM   914  C C   . ASP A 1 139 ? -12.77299 22.10287 10.18114  1.000 54.18314  ? 158 ASP A C   1 
ATOM   915  O O   . ASP A 1 139 ? -13.64634 21.25738 9.93756   1.000 57.03996  ? 158 ASP A O   1 
ATOM   916  C CB  . ASP A 1 139 ? -12.89550 21.83707 12.66655  1.000 56.85011  ? 158 ASP A CB  1 
ATOM   917  C CG  . ASP A 1 139 ? -11.61534 21.04450 12.87577  1.000 56.73047  ? 158 ASP A CG  1 
ATOM   918  O OD1 . ASP A 1 139 ? -10.84548 20.86458 11.90652  1.000 60.91208  ? 158 ASP A OD1 1 
ATOM   919  O OD2 . ASP A 1 139 ? -11.37771 20.60071 14.02033  1.000 56.75177  ? 158 ASP A OD2 1 
ATOM   920  N N   . PRO A 1 140 ? -11.82359 22.39379 9.28937   1.000 56.07061  ? 159 PRO A N   1 
ATOM   921  C CA  . PRO A 1 140 ? -11.77087 21.67624 8.00772   1.000 55.46066  ? 159 PRO A CA  1 
ATOM   922  C C   . PRO A 1 140 ? -11.41684 20.20261 8.13785   1.000 62.42615  ? 159 PRO A C   1 
ATOM   923  O O   . PRO A 1 140 ? -11.58059 19.46199 7.15946   1.000 63.83567  ? 159 PRO A O   1 
ATOM   924  C CB  . PRO A 1 140 ? -10.69942 22.44115 7.22269   1.000 53.00154  ? 159 PRO A CB  1 
ATOM   925  C CG  . PRO A 1 140 ? -9.86061  23.08814 8.27264   1.000 55.48094  ? 159 PRO A CG  1 
ATOM   926  C CD  . PRO A 1 140 ? -10.80140 23.44727 9.37788   1.000 46.93463  ? 159 PRO A CD  1 
ATOM   927  N N   . SER A 1 141 ? -10.93160 19.75055 9.29278   1.000 55.04156  ? 160 SER A N   1 
ATOM   928  C CA  . SER A 1 141 ? -10.63463 18.33670 9.47338   1.000 66.83531  ? 160 SER A CA  1 
ATOM   929  C C   . SER A 1 141 ? -11.84679 17.52194 9.90953   1.000 60.72213  ? 160 SER A C   1 
ATOM   930  O O   . SER A 1 141 ? -11.74630 16.29339 9.98994   1.000 57.66692  ? 160 SER A O   1 
ATOM   931  C CB  . SER A 1 141 ? -9.50330  18.15277 10.49259  1.000 52.26159  ? 160 SER A CB  1 
ATOM   932  O OG  . SER A 1 141 ? -9.91182  18.55673 11.78728  1.000 57.93305  ? 160 SER A OG  1 
ATOM   933  N N   . LEU A 1 142 ? -12.98220 18.16284 10.17604  1.000 62.87959  ? 161 LEU A N   1 
ATOM   934  C CA  . LEU A 1 142 ? -14.17857 17.48559 10.65451  1.000 59.81333  ? 161 LEU A CA  1 
ATOM   935  C C   . LEU A 1 142 ? -15.28434 17.50557 9.60544   1.000 59.20151  ? 161 LEU A C   1 
ATOM   936  O O   . LEU A 1 142 ? -15.35285 18.39077 8.74699   1.000 57.73484  ? 161 LEU A O   1 
ATOM   937  C CB  . LEU A 1 142 ? -14.69677 18.12551 11.94812  1.000 52.29136  ? 161 LEU A CB  1 
ATOM   938  C CG  . LEU A 1 142 ? -13.80586 18.06765 13.18924  1.000 56.80743  ? 161 LEU A CG  1 
ATOM   939  C CD1 . LEU A 1 142 ? -14.49359 18.76152 14.35404  1.000 51.62264  ? 161 LEU A CD1 1 
ATOM   940  C CD2 . LEU A 1 142 ? -13.46598 16.62795 13.54275  1.000 47.71795  ? 161 LEU A CD2 1 
ATOM   941  N N   . LYS A 1 143 ? -16.16945 16.51512 9.71145   1.000 55.57887  ? 162 LYS A N   1 
ATOM   942  C CA  . LYS A 1 143 ? -17.33673 16.38570 8.85186   1.000 53.94384  ? 162 LYS A CA  1 
ATOM   943  C C   . LYS A 1 143 ? -18.50012 15.86017 9.67332   1.000 54.99770  ? 162 LYS A C   1 
ATOM   944  O O   . LYS A 1 143 ? -18.36478 14.84802 10.36663  1.000 65.25600  ? 162 LYS A O   1 
ATOM   945  C CB  . LYS A 1 143 ? -17.06851 15.44452 7.67244   1.000 59.65058  ? 162 LYS A CB  1 
ATOM   946  C CG  . LYS A 1 143 ? -16.73988 16.13530 6.36229   1.000 58.00701  ? 162 LYS A CG  1 
ATOM   947  C CD  . LYS A 1 143 ? -16.64842 15.12060 5.23145   1.000 58.48721  ? 162 LYS A CD  1 
ATOM   948  C CE  . LYS A 1 143 ? -16.47539 15.79324 3.87983   1.000 60.33828  ? 162 LYS A CE  1 
ATOM   949  N NZ  . LYS A 1 143 ? -15.30706 16.71123 3.84230   1.000 71.78986  ? 162 LYS A NZ  1 
ATOM   950  N N   . TYR A 1 144 ? -19.62846 16.56231 9.60652   1.000 55.73992  ? 163 TYR A N   1 
ATOM   951  C CA  . TYR A 1 144 ? -20.85147 16.17148 10.30694  1.000 65.67677  ? 163 TYR A CA  1 
ATOM   952  C C   . TYR A 1 144 ? -20.58224 15.97421 11.79737  1.000 64.95344  ? 163 TYR A C   1 
ATOM   953  O O   . TYR A 1 144 ? -21.00069 14.99211 12.41184  1.000 69.09344  ? 163 TYR A O   1 
ATOM   954  C CB  . TYR A 1 144 ? -21.46407 14.92001 9.67151   1.000 54.42000  ? 163 TYR A CB  1 
ATOM   955  C CG  . TYR A 1 144 ? -21.58341 15.04641 8.16802   1.000 62.13026  ? 163 TYR A CG  1 
ATOM   956  C CD1 . TYR A 1 144 ? -22.59940 15.80137 7.59233   1.000 60.98267  ? 163 TYR A CD1 1 
ATOM   957  C CD2 . TYR A 1 144 ? -20.67556 14.41548 7.32328   1.000 58.26424  ? 163 TYR A CD2 1 
ATOM   958  C CE1 . TYR A 1 144 ? -22.70324 15.93141 6.21757   1.000 60.06569  ? 163 TYR A CE1 1 
ATOM   959  C CE2 . TYR A 1 144 ? -20.77268 14.53586 5.94696   1.000 53.03250  ? 163 TYR A CE2 1 
ATOM   960  C CZ  . TYR A 1 144 ? -21.78821 15.29503 5.39994   1.000 62.91135  ? 163 TYR A CZ  1 
ATOM   961  O OH  . TYR A 1 144 ? -21.89161 15.42227 4.03302   1.000 57.76271  ? 163 TYR A OH  1 
ATOM   962  N N   . ALA A 1 145 ? -19.85563 16.93053 12.37823  1.000 66.54638  ? 164 ALA A N   1 
ATOM   963  C CA  . ALA A 1 145 ? -19.53431 16.86569 13.79692  1.000 65.51026  ? 164 ALA A CA  1 
ATOM   964  C C   . ALA A 1 145 ? -20.72717 17.20330 14.68058  1.000 57.91689  ? 164 ALA A C   1 
ATOM   965  O O   . ALA A 1 145 ? -20.77238 16.76093 15.83215  1.000 56.96385  ? 164 ALA A O   1 
ATOM   966  C CB  . ALA A 1 145 ? -18.37071 17.80658 14.11297  1.000 62.23802  ? 164 ALA A CB  1 
ATOM   967  N N   . ALA A 1 146 ? -21.69313 17.96796 14.17340  1.000 63.96616  ? 165 ALA A N   1 
ATOM   968  C CA  . ALA A 1 146 ? -22.84224 18.35516 14.98023  1.000 68.63561  ? 165 ALA A CA  1 
ATOM   969  C C   . ALA A 1 146 ? -23.91568 17.27826 15.04601  1.000 68.82398  ? 165 ALA A C   1 
ATOM   970  O O   . ALA A 1 146 ? -24.89340 17.44959 15.78173  1.000 68.43336  ? 165 ALA A O   1 
ATOM   971  C CB  . ALA A 1 146 ? -23.45348 19.65080 14.44223  1.000 75.25533  ? 165 ALA A CB  1 
ATOM   972  N N   . GLY A 1 147 ? -23.76033 16.18151 14.30689  1.000 73.26360  ? 166 GLY A N   1 
ATOM   973  C CA  . GLY A 1 147 ? -24.76911 15.14165 14.30463  1.000 72.11264  ? 166 GLY A CA  1 
ATOM   974  C C   . GLY A 1 147 ? -26.04942 15.58823 13.61497  1.000 73.80721  ? 166 GLY A C   1 
ATOM   975  O O   . GLY A 1 147 ? -26.07855 16.54094 12.83186  1.000 79.67401  ? 166 GLY A O   1 
ATOM   976  N N   . LYS A 1 148 ? -27.12723 14.87499 13.92621  1.000 75.30543  ? 167 LYS A N   1 
ATOM   977  C CA  . LYS A 1 148 ? -28.41567 15.18883 13.33686  1.000 72.36660  ? 167 LYS A CA  1 
ATOM   978  C C   . LYS A 1 148 ? -28.99565 16.45135 13.97320  1.000 76.22691  ? 167 LYS A C   1 
ATOM   979  O O   . LYS A 1 148 ? -28.72913 16.74582 15.14129  1.000 79.72675  ? 167 LYS A O   1 
ATOM   980  C CB  . LYS A 1 148 ? -29.38431 14.02549 13.51947  1.000 66.40125  ? 167 LYS A CB  1 
ATOM   981  N N   . PRO A 1 149 ? -29.77467 17.22445 13.21833  1.000 71.17471  ? 168 PRO A N   1 
ATOM   982  C CA  . PRO A 1 149 ? -30.42387 18.40684 13.79973  1.000 71.64499  ? 168 PRO A CA  1 
ATOM   983  C C   . PRO A 1 149 ? -31.39680 18.00543 14.89881  1.000 83.58996  ? 168 PRO A C   1 
ATOM   984  O O   . PRO A 1 149 ? -32.22590 17.10931 14.72215  1.000 88.99112  ? 168 PRO A O   1 
ATOM   985  C CB  . PRO A 1 149 ? -31.14749 19.03797 12.60442  1.000 75.37736  ? 168 PRO A CB  1 
ATOM   986  C CG  . PRO A 1 149 ? -30.43264 18.51246 11.40023  1.000 69.96813  ? 168 PRO A CG  1 
ATOM   987  C CD  . PRO A 1 149 ? -29.99748 17.12722 11.76576  1.000 76.87326  ? 168 PRO A CD  1 
ATOM   988  N N   . ALA A 1 150 ? -31.28323 18.66756 16.04480  1.000 86.21895  ? 169 ALA A N   1 
ATOM   989  C CA  . ALA A 1 150 ? -32.11608 18.34652 17.19749  1.000 100.67799 ? 169 ALA A CA  1 
ATOM   990  C C   . ALA A 1 150 ? -32.43792 19.62365 17.97381  1.000 108.05329 ? 169 ALA A C   1 
ATOM   991  O O   . ALA A 1 150 ? -32.16354 19.75385 19.16506  1.000 117.10494 ? 169 ALA A O   1 
ATOM   992  C CB  . ALA A 1 150 ? -31.42938 17.30519 18.07671  1.000 95.97048  ? 169 ALA A CB  1 
ATOM   993  N N   . CYS A 1 151 ? -33.03572 20.59721 17.29717  1.000 93.08282  ? 170 CYS A N   1 
ATOM   994  C CA  . CYS A 1 151 ? -33.44016 21.83135 17.95689  1.000 96.82310  ? 170 CYS A CA  1 
ATOM   995  C C   . CYS A 1 151 ? -34.89017 21.75491 18.42141  1.000 95.40615  ? 170 CYS A C   1 
ATOM   996  O O   . CYS A 1 151 ? -35.17617 21.85903 19.61457  1.000 105.94572 ? 170 CYS A O   1 
ATOM   997  C CB  . CYS A 1 151 ? -33.24208 23.02605 17.02374  1.000 84.51889  ? 170 CYS A CB  1 
ATOM   998  S SG  . CYS A 1 151 ? -31.60684 23.10477 16.26765  1.000 85.06310  ? 170 CYS A SG  1 
ATOM   999  N N   . GLU B 1 4   ? -1.86258  20.36297 18.03955  1.000 111.74895 ? 23  GLU B N   1 
ATOM   1000 C CA  . GLU B 1 4   ? -2.37611  21.69845 18.32507  1.000 107.07991 ? 23  GLU B CA  1 
ATOM   1001 C C   . GLU B 1 4   ? -3.60340  22.01637 17.47349  1.000 101.78894 ? 23  GLU B C   1 
ATOM   1002 O O   . GLU B 1 4   ? -3.94070  21.27060 16.55477  1.000 100.63366 ? 23  GLU B O   1 
ATOM   1003 C CB  . GLU B 1 4   ? -1.28863  22.74901 18.09143  1.000 100.77856 ? 23  GLU B CB  1 
ATOM   1004 N N   . LYS B 1 5   ? -4.26800  23.13160 17.79160  1.000 95.40568  ? 24  LYS B N   1 
ATOM   1005 C CA  . LYS B 1 5   ? -5.46226  23.55485 17.05814  1.000 85.40774  ? 24  LYS B CA  1 
ATOM   1006 C C   . LYS B 1 5   ? -5.61932  25.05820 17.29559  1.000 69.48168  ? 24  LYS B C   1 
ATOM   1007 O O   . LYS B 1 5   ? -6.07638  25.46982 18.36507  1.000 80.52687  ? 24  LYS B O   1 
ATOM   1008 C CB  . LYS B 1 5   ? -6.68769  22.78121 17.51728  1.000 85.50762  ? 24  LYS B CB  1 
ATOM   1009 C CG  . LYS B 1 5   ? -7.86337  22.87166 16.57010  1.000 79.56011  ? 24  LYS B CG  1 
ATOM   1010 C CD  . LYS B 1 5   ? -7.65942  21.99221 15.34977  1.000 63.32520  ? 24  LYS B CD  1 
ATOM   1011 C CE  . LYS B 1 5   ? -8.01093  20.55090 15.64749  1.000 63.12602  ? 24  LYS B CE  1 
ATOM   1012 N NZ  . LYS B 1 5   ? -7.92775  19.71346 14.41908  1.000 70.14649  ? 24  LYS B NZ  1 
ATOM   1013 N N   . THR B 1 6   ? -5.26726  25.85533 16.28892  1.000 63.15711  ? 25  THR B N   1 
ATOM   1014 C CA  . THR B 1 6   ? -5.22306  27.30823 16.40022  1.000 62.73610  ? 25  THR B CA  1 
ATOM   1015 C C   . THR B 1 6   ? -6.39818  27.96071 15.68043  1.000 57.66801  ? 25  THR B C   1 
ATOM   1016 O O   . THR B 1 6   ? -6.80252  27.51725 14.60389  1.000 52.98140  ? 25  THR B O   1 
ATOM   1017 C CB  . THR B 1 6   ? -3.90648  27.84149 15.82830  1.000 57.08115  ? 25  THR B CB  1 
ATOM   1018 O OG1 . THR B 1 6   ? -2.81058  27.12796 16.41647  1.000 69.77733  ? 25  THR B OG1 1 
ATOM   1019 C CG2 . THR B 1 6   ? -3.75053  29.32662 16.12486  1.000 53.57294  ? 25  THR B CG2 1 
ATOM   1020 N N   . VAL B 1 7   ? -6.92928  29.02961 16.26855  1.000 54.25775  ? 26  VAL B N   1 
ATOM   1021 C CA  . VAL B 1 7   ? -8.05268  29.76052 15.69339  1.000 53.37941  ? 26  VAL B CA  1 
ATOM   1022 C C   . VAL B 1 7   ? -7.51521  30.89443 14.83066  1.000 59.38956  ? 26  VAL B C   1 
ATOM   1023 O O   . VAL B 1 7   ? -6.73346  31.73004 15.30092  1.000 63.81769  ? 26  VAL B O   1 
ATOM   1024 C CB  . VAL B 1 7   ? -8.97887  30.30173 16.79551  1.000 49.77475  ? 26  VAL B CB  1 
ATOM   1025 C CG1 . VAL B 1 7   ? -10.03833 31.21622 16.19629  1.000 51.89351  ? 26  VAL B CG1 1 
ATOM   1026 C CG2 . VAL B 1 7   ? -9.62966  29.15546 17.55283  1.000 49.44261  ? 26  VAL B CG2 1 
ATOM   1027 N N   . TYR B 1 8   ? -7.93797  30.93005 13.57277  1.000 50.61705  ? 27  TYR B N   1 
ATOM   1028 C CA  . TYR B 1 8   ? -7.63905  32.02657 12.66064  1.000 52.37600  ? 27  TYR B CA  1 
ATOM   1029 C C   . TYR B 1 8   ? -8.94962  32.63810 12.17446  1.000 51.35146  ? 27  TYR B C   1 
ATOM   1030 O O   . TYR B 1 8   ? -10.03257 32.14142 12.47895  1.000 55.32522  ? 27  TYR B O   1 
ATOM   1031 C CB  . TYR B 1 8   ? -6.77624  31.54436 11.48989  1.000 44.96653  ? 27  TYR B CB  1 
ATOM   1032 C CG  . TYR B 1 8   ? -5.46218  30.91633 11.90516  1.000 49.82940  ? 27  TYR B CG  1 
ATOM   1033 C CD1 . TYR B 1 8   ? -4.35297  31.70399 12.19300  1.000 50.76040  ? 27  TYR B CD1 1 
ATOM   1034 C CD2 . TYR B 1 8   ? -5.32653  29.53820 11.99878  1.000 49.43152  ? 27  TYR B CD2 1 
ATOM   1035 C CE1 . TYR B 1 8   ? -3.14786  31.13711 12.57310  1.000 47.75701  ? 27  TYR B CE1 1 
ATOM   1036 C CE2 . TYR B 1 8   ? -4.12487  28.96111 12.37596  1.000 56.08831  ? 27  TYR B CE2 1 
ATOM   1037 C CZ  . TYR B 1 8   ? -3.03825  29.76558 12.66183  1.000 56.98385  ? 27  TYR B CZ  1 
ATOM   1038 O OH  . TYR B 1 8   ? -1.83870  29.19833 13.03654  1.000 56.66416  ? 27  TYR B OH  1 
ATOM   1039 N N   . GLY B 1 9   ? -8.85001  33.73140 11.41544  1.000 45.02939  ? 28  GLY B N   1 
ATOM   1040 C CA  . GLY B 1 9   ? -10.00292 34.43717 10.92046  1.000 45.73357  ? 28  GLY B CA  1 
ATOM   1041 C C   . GLY B 1 9   ? -10.22464 34.23756 9.43251   1.000 46.77079  ? 28  GLY B C   1 
ATOM   1042 O O   . GLY B 1 9   ? -9.54510  33.45179 8.77175   1.000 50.56948  ? 28  GLY B O   1 
ATOM   1043 N N   . LEU B 1 10  ? -11.19842 34.98353 8.90452   1.000 48.38302  ? 29  LEU B N   1 
ATOM   1044 C CA  . LEU B 1 10  ? -11.48756 34.91417 7.47444   1.000 48.40327  ? 29  LEU B CA  1 
ATOM   1045 C C   . LEU B 1 10  ? -10.28012 35.32745 6.64693   1.000 45.94427  ? 29  LEU B C   1 
ATOM   1046 O O   . LEU B 1 10  ? -10.04271 34.78706 5.56015   1.000 51.13704  ? 29  LEU B O   1 
ATOM   1047 C CB  . LEU B 1 10  ? -12.68052 35.80431 7.13439   1.000 43.47603  ? 29  LEU B CB  1 
ATOM   1048 C CG  . LEU B 1 10  ? -14.04620 35.35430 7.63674   1.000 52.32316  ? 29  LEU B CG  1 
ATOM   1049 C CD1 . LEU B 1 10  ? -15.11280 36.36765 7.23636   1.000 39.12821  ? 29  LEU B CD1 1 
ATOM   1050 C CD2 . LEU B 1 10  ? -14.37502 33.96747 7.10464   1.000 48.35639  ? 29  LEU B CD2 1 
ATOM   1051 N N   . ASN B 1 11  ? -9.51595  36.29279 7.14115   1.000 49.92482  ? 30  ASN B N   1 
ATOM   1052 C CA  . ASN B 1 11  ? -8.31982  36.78288 6.48062   1.000 48.87558  ? 30  ASN B CA  1 
ATOM   1053 C C   . ASN B 1 11  ? -7.20128  36.86033 7.50101   1.000 51.01929  ? 30  ASN B C   1 
ATOM   1054 O O   . ASN B 1 11  ? -7.43470  37.17688 8.67058   1.000 55.05417  ? 30  ASN B O   1 
ATOM   1055 C CB  . ASN B 1 11  ? -8.55003  38.15381 5.84096   1.000 53.80705  ? 30  ASN B CB  1 
ATOM   1056 C CG  . ASN B 1 11  ? -9.57161  38.11034 4.72817   1.000 50.92863  ? 30  ASN B CG  1 
ATOM   1057 O OD1 . ASN B 1 11  ? -10.70427 38.55625 4.88945   1.000 59.93762  ? 30  ASN B OD1 1 
ATOM   1058 N ND2 . ASN B 1 11  ? -9.17445  37.56681 3.58782   1.000 60.35676  ? 30  ASN B ND2 1 
ATOM   1059 N N   . GLU B 1 12  ? -5.99604  36.52405 7.06324   1.000 55.60204  ? 31  GLU B N   1 
ATOM   1060 C CA  . GLU B 1 12  ? -4.82558  36.59105 7.92157   1.000 56.60406  ? 31  GLU B CA  1 
ATOM   1061 C C   . GLU B 1 12  ? -3.64469  37.11614 7.12024   1.000 56.20611  ? 31  GLU B C   1 
ATOM   1062 O O   . GLU B 1 12  ? -3.70497  37.25805 5.89853   1.000 52.15418  ? 31  GLU B O   1 
ATOM   1063 C CB  . GLU B 1 12  ? -4.49373  35.22408 8.53262   1.000 45.52601  ? 31  GLU B CB  1 
ATOM   1064 C CG  . GLU B 1 12  ? -5.57331  34.66185 9.43754   1.000 52.61958  ? 31  GLU B CG  1 
ATOM   1065 C CD  . GLU B 1 12  ? -5.71822  35.42363 10.74123  1.000 55.02098  ? 31  GLU B CD  1 
ATOM   1066 O OE1 . GLU B 1 12  ? -4.77814  36.15203 11.12377  1.000 55.90380  ? 31  GLU B OE1 1 
ATOM   1067 O OE2 . GLU B 1 12  ? -6.78100  35.29230 11.38517  1.000 53.63725  ? 31  GLU B OE2 1 
ATOM   1068 N N   . TYR B 1 13  ? -2.55890  37.40769 7.82372   1.000 47.46837  ? 32  TYR B N   1 
ATOM   1069 C CA  . TYR B 1 13  ? -1.28905  37.67681 7.17095   1.000 57.29906  ? 32  TYR B CA  1 
ATOM   1070 C C   . TYR B 1 13  ? -0.48788  36.38699 7.11742   1.000 55.67944  ? 32  TYR B C   1 
ATOM   1071 O O   . TYR B 1 13  ? -0.33720  35.70046 8.13269   1.000 60.78487  ? 32  TYR B O   1 
ATOM   1072 C CB  . TYR B 1 13  ? -0.48937  38.75067 7.90790   1.000 57.92082  ? 32  TYR B CB  1 
ATOM   1073 C CG  . TYR B 1 13  ? -0.93257  40.16318 7.63085   1.000 62.20841  ? 32  TYR B CG  1 
ATOM   1074 C CD1 . TYR B 1 13  ? -0.88859  40.67827 6.34217   1.000 63.32502  ? 32  TYR B CD1 1 
ATOM   1075 C CD2 . TYR B 1 13  ? -1.36349  40.99251 8.65449   1.000 60.83429  ? 32  TYR B CD2 1 
ATOM   1076 C CE1 . TYR B 1 13  ? -1.27911  41.97352 6.07608   1.000 62.50703  ? 32  TYR B CE1 1 
ATOM   1077 C CE2 . TYR B 1 13  ? -1.75254  42.29183 8.39846   1.000 67.26074  ? 32  TYR B CE2 1 
ATOM   1078 C CZ  . TYR B 1 13  ? -1.71088  42.77697 7.10626   1.000 67.57933  ? 32  TYR B CZ  1 
ATOM   1079 O OH  . TYR B 1 13  ? -2.09806  44.07013 6.83694   1.000 86.09691  ? 32  TYR B OH  1 
ATOM   1080 N N   . ALA B 1 14  ? -0.00344  36.04647 5.92980   1.000 50.34776  ? 33  ALA B N   1 
ATOM   1081 C CA  . ALA B 1 14  ? 0.83828   34.88237 5.73695   1.000 57.94519  ? 33  ALA B CA  1 
ATOM   1082 C C   . ALA B 1 14  ? 2.15294   35.34512 5.13485   1.000 56.66675  ? 33  ALA B C   1 
ATOM   1083 O O   . ALA B 1 14  ? 2.22503   36.39294 4.49081   1.000 59.94273  ? 33  ALA B O   1 
ATOM   1084 C CB  . ALA B 1 14  ? 0.17442   33.83377 4.83289   1.000 45.21864  ? 33  ALA B CB  1 
ATOM   1085 N N   . ALA B 1 15  ? 3.19878   34.56998 5.37131   1.000 64.16164  ? 34  ALA B N   1 
ATOM   1086 C CA  . ALA B 1 15  ? 4.51018   34.85041 4.81402   1.000 59.25541  ? 34  ALA B CA  1 
ATOM   1087 C C   . ALA B 1 15  ? 4.93950   33.64264 4.00347   1.000 50.50857  ? 34  ALA B C   1 
ATOM   1088 O O   . ALA B 1 15  ? 4.82678   32.50563 4.47001   1.000 55.81987  ? 34  ALA B O   1 
ATOM   1089 C CB  . ALA B 1 15  ? 5.53244   35.15356 5.91358   1.000 54.49989  ? 34  ALA B CB  1 
ATOM   1090 N N   . LEU B 1 16  ? 5.40119   33.88535 2.78428   1.000 64.05643  ? 35  LEU B N   1 
ATOM   1091 C CA  . LEU B 1 16  ? 5.98733   32.81699 1.98796   1.000 63.16537  ? 35  LEU B CA  1 
ATOM   1092 C C   . LEU B 1 16  ? 7.43864   32.70664 2.42997   1.000 71.69427  ? 35  LEU B C   1 
ATOM   1093 O O   . LEU B 1 16  ? 8.29204   33.49102 2.00957   1.000 77.04493  ? 35  LEU B O   1 
ATOM   1094 C CB  . LEU B 1 16  ? 5.85291   33.13095 0.50443   1.000 60.96384  ? 35  LEU B CB  1 
ATOM   1095 C CG  . LEU B 1 16  ? 4.39154   33.27899 0.07116   1.000 67.58548  ? 35  LEU B CG  1 
ATOM   1096 C CD1 . LEU B 1 16  ? 4.29404   33.62766 -1.40078  1.000 74.20370  ? 35  LEU B CD1 1 
ATOM   1097 C CD2 . LEU B 1 16  ? 3.59804   32.01519 0.38341   1.000 68.26339  ? 35  LEU B CD2 1 
ATOM   1098 N N   . ASP B 1 17  ? 7.70421   31.74066 3.30671   1.000 72.09760  ? 36  ASP B N   1 
ATOM   1099 C CA  . ASP B 1 17  ? 9.03185   31.56113 3.87887   1.000 90.33356  ? 36  ASP B CA  1 
ATOM   1100 C C   . ASP B 1 17  ? 10.07468  31.36735 2.78577   1.000 90.64817  ? 36  ASP B C   1 
ATOM   1101 O O   . ASP B 1 17  ? 9.84408   30.65714 1.80319   1.000 94.09015  ? 36  ASP B O   1 
ATOM   1102 C CB  . ASP B 1 17  ? 9.04396   30.37643 4.84761   1.000 89.62853  ? 36  ASP B CB  1 
ATOM   1103 C CG  . ASP B 1 17  ? 10.41470  30.12184 5.43619   1.000 93.23039  ? 36  ASP B CG  1 
ATOM   1104 O OD1 . ASP B 1 17  ? 11.02026  31.08583 5.95307   1.000 99.84803  ? 36  ASP B OD1 1 
ATOM   1105 O OD2 . ASP B 1 17  ? 10.88218  28.96297 5.39419   1.000 94.19216  ? 36  ASP B OD2 1 
ATOM   1106 N N   . GLY B 1 18  ? 11.21653  32.03500 2.94672   1.000 96.53162  ? 37  GLY B N   1 
ATOM   1107 C CA  . GLY B 1 18  ? 12.30045  31.99805 1.99820   1.000 102.42366 ? 37  GLY B CA  1 
ATOM   1108 C C   . GLY B 1 18  ? 12.31293  33.16666 1.03672   1.000 113.42694 ? 37  GLY B C   1 
ATOM   1109 O O   . GLY B 1 18  ? 13.39062  33.59782 0.61114   1.000 118.38687 ? 37  GLY B O   1 
ATOM   1110 N N   . ILE B 1 19  ? 11.13707  33.68992 0.68791   1.000 111.52004 ? 38  ILE B N   1 
ATOM   1111 C CA  . ILE B 1 19  ? 11.04487  34.84644 -0.19361  1.000 112.51606 ? 38  ILE B CA  1 
ATOM   1112 C C   . ILE B 1 19  ? 10.83074  36.12412 0.59565   1.000 114.31145 ? 38  ILE B C   1 
ATOM   1113 O O   . ILE B 1 19  ? 10.88136  37.21839 0.00894   1.000 122.60313 ? 38  ILE B O   1 
ATOM   1114 C CB  . ILE B 1 19  ? 9.92056   34.67152 -1.23716  1.000 104.54152 ? 38  ILE B CB  1 
ATOM   1115 N N   . ASN B 1 20  ? 10.62138  36.01855 1.90444   1.000 113.27158 ? 39  ASN B N   1 
ATOM   1116 C CA  . ASN B 1 20  ? 10.40088  37.14554 2.80376   1.000 119.41306 ? 39  ASN B CA  1 
ATOM   1117 C C   . ASN B 1 20  ? 9.39848   38.12865 2.20957   1.000 109.08509 ? 39  ASN B C   1 
ATOM   1118 O O   . ASN B 1 20  ? 9.70631   39.28398 1.91689   1.000 115.20337 ? 39  ASN B O   1 
ATOM   1119 C CB  . ASN B 1 20  ? 11.72175  37.83731 3.13792   1.000 121.52733 ? 39  ASN B CB  1 
ATOM   1120 N N   . LEU B 1 21  ? 8.17459   37.63957 2.03157   1.000 96.01472  ? 40  LEU B N   1 
ATOM   1121 C CA  . LEU B 1 21  ? 7.10170   38.45972 1.49045   1.000 97.82084  ? 40  LEU B CA  1 
ATOM   1122 C C   . LEU B 1 21  ? 5.83418   38.18743 2.28238   1.000 90.39196  ? 40  LEU B C   1 
ATOM   1123 O O   . LEU B 1 21  ? 5.43682   37.02940 2.44323   1.000 77.29252  ? 40  LEU B O   1 
ATOM   1124 C CB  . LEU B 1 21  ? 6.87659   38.17370 -0.00038  1.000 92.37145  ? 40  LEU B CB  1 
ATOM   1125 N N   . GLU B 1 22  ? 5.20925   39.25449 2.77352   1.000 86.15036  ? 41  GLU B N   1 
ATOM   1126 C CA  . GLU B 1 22  ? 3.94721   39.16489 3.49586   1.000 81.44271  ? 41  GLU B CA  1 
ATOM   1127 C C   . GLU B 1 22  ? 2.79011   39.35734 2.52122   1.000 81.95649  ? 41  GLU B C   1 
ATOM   1128 O O   . GLU B 1 22  ? 2.71314   40.38005 1.83222   1.000 89.95101  ? 41  GLU B O   1 
ATOM   1129 C CB  . GLU B 1 22  ? 3.90138   40.19975 4.61752   1.000 91.51400  ? 41  GLU B CB  1 
ATOM   1130 C CG  . GLU B 1 22  ? 2.72705   40.04960 5.56273   1.000 83.66785  ? 41  GLU B CG  1 
ATOM   1131 C CD  . GLU B 1 22  ? 2.86871   40.93261 6.78310   1.000 90.27531  ? 41  GLU B CD  1 
ATOM   1132 O OE1 . GLU B 1 22  ? 3.90725   40.83116 7.47078   1.000 89.11439  ? 41  GLU B OE1 1 
ATOM   1133 O OE2 . GLU B 1 22  ? 1.95323   41.74004 7.04353   1.000 96.08194  ? 41  GLU B OE2 1 
ATOM   1134 N N   . VAL B 1 23  ? 1.90007   38.37426 2.46133   1.000 67.46758  ? 42  VAL B N   1 
ATOM   1135 C CA  . VAL B 1 23  ? 0.71589   38.40942 1.61569   1.000 62.71143  ? 42  VAL B CA  1 
ATOM   1136 C C   . VAL B 1 23  ? -0.52436  38.29953 2.49296   1.000 63.15168  ? 42  VAL B C   1 
ATOM   1137 O O   . VAL B 1 23  ? -0.51052  37.64246 3.54157   1.000 61.19846  ? 42  VAL B O   1 
ATOM   1138 C CB  . VAL B 1 23  ? 0.74117   37.29765 0.54456   1.000 61.97180  ? 42  VAL B CB  1 
ATOM   1139 C CG1 . VAL B 1 23  ? 2.03949   37.36440 -0.25150  1.000 60.73095  ? 42  VAL B CG1 1 
ATOM   1140 C CG2 . VAL B 1 23  ? 0.57473   35.92802 1.18089   1.000 58.51293  ? 42  VAL B CG2 1 
ATOM   1141 N N   . ALA B 1 24  ? -1.57934  38.99832 2.09595   1.000 60.70067  ? 43  ALA B N   1 
ATOM   1142 C CA  . ALA B 1 24  ? -2.86476  38.84924 2.75790   1.000 57.23462  ? 43  ALA B CA  1 
ATOM   1143 C C   . ALA B 1 24  ? -3.55253  37.60158 2.21870   1.000 59.42999  ? 43  ALA B C   1 
ATOM   1144 O O   . ALA B 1 24  ? -3.69072  37.43430 1.00343   1.000 65.29272  ? 43  ALA B O   1 
ATOM   1145 C CB  . ALA B 1 24  ? -3.73569  40.08441 2.53753   1.000 49.02782  ? 43  ALA B CB  1 
ATOM   1146 N N   . ALA B 1 25  ? -3.95724  36.71457 3.12130   1.000 48.44437  ? 44  ALA B N   1 
ATOM   1147 C CA  . ALA B 1 25  ? -4.53561  35.43039 2.76965   1.000 53.43574  ? 44  ALA B CA  1 
ATOM   1148 C C   . ALA B 1 25  ? -6.00006  35.38163 3.17566   1.000 53.73654  ? 44  ALA B C   1 
ATOM   1149 O O   . ALA B 1 25  ? -6.36850  35.82445 4.26858   1.000 56.18746  ? 44  ALA B O   1 
ATOM   1150 C CB  . ALA B 1 25  ? -3.77349  34.28335 3.43663   1.000 47.96576  ? 44  ALA B CB  1 
ATOM   1151 N N   . LYS B 1 26  ? -6.83133  34.87990 2.26827   1.000 54.72822  ? 45  LYS B N   1 
ATOM   1152 C CA  . LYS B 1 26  ? -8.23329  34.59982 2.54199   1.000 55.06323  ? 45  LYS B CA  1 
ATOM   1153 C C   . LYS B 1 26  ? -8.38062  33.11954 2.87793   1.000 53.12729  ? 45  LYS B C   1 
ATOM   1154 O O   . LYS B 1 26  ? -7.99012  32.25798 2.08302   1.000 47.89731  ? 45  LYS B O   1 
ATOM   1155 C CB  . LYS B 1 26  ? -9.10907  34.96694 1.34539   1.000 54.27714  ? 45  LYS B CB  1 
ATOM   1156 C CG  . LYS B 1 26  ? -10.56348 34.57719 1.52028   1.000 55.62956  ? 45  LYS B CG  1 
ATOM   1157 C CD  . LYS B 1 26  ? -11.38110 34.89093 0.28384   1.000 51.62732  ? 45  LYS B CD  1 
ATOM   1158 C CE  . LYS B 1 26  ? -12.86112 34.87221 0.60651   1.000 55.19406  ? 45  LYS B CE  1 
ATOM   1159 N NZ  . LYS B 1 26  ? -13.70686 35.05300 -0.60309  1.000 57.36360  ? 45  LYS B NZ  1 
ATOM   1160 N N   . LEU B 1 27  ? -8.90598  32.83143 4.06764   1.000 48.15973  ? 46  LEU B N   1 
ATOM   1161 C CA  . LEU B 1 27  ? -9.10496  31.46152 4.53315   1.000 49.22274  ? 46  LEU B CA  1 
ATOM   1162 C C   . LEU B 1 27  ? -10.47923 30.99082 4.05933   1.000 56.56736  ? 46  LEU B C   1 
ATOM   1163 O O   . LEU B 1 27  ? -11.51240 31.47128 4.54040   1.000 48.70525  ? 46  LEU B O   1 
ATOM   1164 C CB  . LEU B 1 27  ? -8.96460  31.38170 6.05192   1.000 42.17190  ? 46  LEU B CB  1 
ATOM   1165 C CG  . LEU B 1 27  ? -7.53470  31.37046 6.61699   1.000 46.92519  ? 46  LEU B CG  1 
ATOM   1166 C CD1 . LEU B 1 27  ? -6.79985  32.69448 6.40125   1.000 46.92664  ? 46  LEU B CD1 1 
ATOM   1167 C CD2 . LEU B 1 27  ? -7.55647  31.02794 8.09143   1.000 41.46750  ? 46  LEU B CD2 1 
ATOM   1168 N N   . ASP B 1 28  ? -10.48883 30.07665 3.09193   1.000 46.66704  ? 47  ASP B N   1 
ATOM   1169 C CA  . ASP B 1 28  ? -11.69266 29.68713 2.35846   1.000 46.24629  ? 47  ASP B CA  1 
ATOM   1170 C C   . ASP B 1 28  ? -11.92948 28.19071 2.56317   1.000 51.36488  ? 47  ASP B C   1 
ATOM   1171 O O   . ASP B 1 28  ? -11.30379 27.36082 1.89555   1.000 45.68284  ? 47  ASP B O   1 
ATOM   1172 C CB  . ASP B 1 28  ? -11.53769 30.04392 0.88129   1.000 46.27287  ? 47  ASP B CB  1 
ATOM   1173 C CG  . ASP B 1 28  ? -12.79181 29.78761 0.07205   1.000 54.89205  ? 47  ASP B CG  1 
ATOM   1174 O OD1 . ASP B 1 28  ? -13.77619 29.24703 0.62279   1.000 61.78245  ? 47  ASP B OD1 1 
ATOM   1175 O OD2 . ASP B 1 28  ? -12.79080 30.14238 -1.12655  1.000 54.13821  ? 47  ASP B OD2 1 
ATOM   1176 N N   . THR B 1 29  ? -12.84529 27.84233 3.47201   1.000 41.56282  ? 48  THR B N   1 
ATOM   1177 C CA  . THR B 1 29  ? -13.15886 26.43591 3.70340   1.000 52.09365  ? 48  THR B CA  1 
ATOM   1178 C C   . THR B 1 29  ? -13.98328 25.81806 2.58081   1.000 52.53070  ? 48  THR B C   1 
ATOM   1179 O O   . THR B 1 29  ? -14.06740 24.58707 2.50696   1.000 51.57230  ? 48  THR B O   1 
ATOM   1180 C CB  . THR B 1 29  ? -13.90259 26.26490 5.02941   1.000 41.96642  ? 48  THR B CB  1 
ATOM   1181 O OG1 . THR B 1 29  ? -15.14463 26.97837 4.97887   1.000 43.31265  ? 48  THR B OG1 1 
ATOM   1182 C CG2 . THR B 1 29  ? -13.05927 26.78138 6.18592   1.000 46.21907  ? 48  THR B CG2 1 
ATOM   1183 N N   . GLY B 1 30  ? -14.56761 26.62996 1.69970   1.000 44.70739  ? 49  GLY B N   1 
ATOM   1184 C CA  . GLY B 1 30  ? -15.32086 26.11436 0.57279   1.000 47.66424  ? 49  GLY B CA  1 
ATOM   1185 C C   . GLY B 1 30  ? -14.48304 25.62828 -0.58765  1.000 51.71628  ? 49  GLY B C   1 
ATOM   1186 O O   . GLY B 1 30  ? -15.01251 24.96722 -1.48597  1.000 52.92213  ? 49  GLY B O   1 
ATOM   1187 N N   . ALA B 1 31  ? -13.19567 25.95435 -0.60169  1.000 49.50370  ? 50  ALA B N   1 
ATOM   1188 C CA  . ALA B 1 31  ? -12.26781 25.47601 -1.61481  1.000 53.25315  ? 50  ALA B CA  1 
ATOM   1189 C C   . ALA B 1 31  ? -11.34049 24.44371 -0.98818  1.000 47.44261  ? 50  ALA B C   1 
ATOM   1190 O O   . ALA B 1 31  ? -10.90352 24.60601 0.15497   1.000 52.87411  ? 50  ALA B O   1 
ATOM   1191 C CB  . ALA B 1 31  ? -11.45612 26.63147 -2.20914  1.000 44.88370  ? 50  ALA B CB  1 
ATOM   1192 N N   . LYS B 1 32  ? -11.04816 23.37568 -1.73161  1.000 48.71822  ? 51  LYS B N   1 
ATOM   1193 C CA  . LYS B 1 32  ? -10.16977 22.33785 -1.20087  1.000 51.24355  ? 51  LYS B CA  1 
ATOM   1194 C C   . LYS B 1 32  ? -8.70685  22.73523 -1.33568  1.000 53.17163  ? 51  LYS B C   1 
ATOM   1195 O O   . LYS B 1 32  ? -7.93851  22.65175 -0.37233  1.000 46.85234  ? 51  LYS B O   1 
ATOM   1196 C CB  . LYS B 1 32  ? -10.42260 21.01043 -1.91682  1.000 49.56228  ? 51  LYS B CB  1 
ATOM   1197 C CG  . LYS B 1 32  ? -11.81552 20.44672 -1.71786  1.000 67.12107  ? 51  LYS B CG  1 
ATOM   1198 C CD  . LYS B 1 32  ? -11.96192 19.09875 -2.40543  1.000 69.19872  ? 51  LYS B CD  1 
ATOM   1199 C CE  . LYS B 1 32  ? -13.42079 18.78010 -2.67172  1.000 68.14992  ? 51  LYS B CE  1 
ATOM   1200 N NZ  . LYS B 1 32  ? -14.22939 18.88187 -1.42876  1.000 84.76262  ? 51  LYS B NZ  1 
ATOM   1201 N N   . THR B 1 33  ? -8.31748  23.19242 -2.51761  1.000 50.57226  ? 52  THR B N   1 
ATOM   1202 C CA  . THR B 1 33  ? -6.93448  23.50140 -2.83123  1.000 53.24021  ? 52  THR B CA  1 
ATOM   1203 C C   . THR B 1 33  ? -6.64995  24.97877 -2.59593  1.000 53.79670  ? 52  THR B C   1 
ATOM   1204 O O   . THR B 1 33  ? -7.55140  25.82053 -2.59880  1.000 57.15361  ? 52  THR B O   1 
ATOM   1205 C CB  . THR B 1 33  ? -6.61726  23.13841 -4.28128  1.000 59.78919  ? 52  THR B CB  1 
ATOM   1206 O OG1 . THR B 1 33  ? -7.54324  23.80523 -5.14933  1.000 65.16553  ? 52  THR B OG1 1 
ATOM   1207 C CG2 . THR B 1 33  ? -6.72758  21.63228 -4.48807  1.000 56.55934  ? 52  THR B CG2 1 
ATOM   1208 N N   . ALA B 1 34  ? -5.37486  25.27902 -2.37222  1.000 51.34498  ? 53  ALA B N   1 
ATOM   1209 C CA  . ALA B 1 34  ? -4.91201  26.64063 -2.16329  1.000 45.62490  ? 53  ALA B CA  1 
ATOM   1210 C C   . ALA B 1 34  ? -4.44433  27.24990 -3.47916  1.000 52.57466  ? 53  ALA B C   1 
ATOM   1211 O O   . ALA B 1 34  ? -3.97695  26.54646 -4.37640  1.000 52.32947  ? 53  ALA B O   1 
ATOM   1212 C CB  . ALA B 1 34  ? -3.77481  26.67212 -1.14062  1.000 40.68007  ? 53  ALA B CB  1 
ATOM   1213 N N   . SER B 1 35  ? -4.56694  28.57482 -3.58458  1.000 50.44957  ? 54  SER B N   1 
ATOM   1214 C CA  . SER B 1 35  ? -4.21418  29.29881 -4.79940  1.000 46.31040  ? 54  SER B CA  1 
ATOM   1215 C C   . SER B 1 35  ? -3.36325  30.51641 -4.47380  1.000 55.93555  ? 54  SER B C   1 
ATOM   1216 O O   . SER B 1 35  ? -3.58124  31.19177 -3.46328  1.000 50.55128  ? 54  SER B O   1 
ATOM   1217 C CB  . SER B 1 35  ? -5.45822  29.75109 -5.57366  1.000 42.57072  ? 54  SER B CB  1 
ATOM   1218 O OG  . SER B 1 35  ? -6.16030  28.64298 -6.10297  1.000 73.18860  ? 54  SER B OG  1 
ATOM   1219 N N   . LEU B 1 36  ? -2.40196  30.79547 -5.34980  1.000 52.36321  ? 55  LEU B N   1 
ATOM   1220 C CA  . LEU B 1 36  ? -1.53307  31.95712 -5.24142  1.000 54.20037  ? 55  LEU B CA  1 
ATOM   1221 C C   . LEU B 1 36  ? -1.56611  32.71002 -6.56266  1.000 55.28224  ? 55  LEU B C   1 
ATOM   1222 O O   . LEU B 1 36  ? -1.34358  32.11750 -7.62648  1.000 57.70183  ? 55  LEU B O   1 
ATOM   1223 C CB  . LEU B 1 36  ? -0.10108  31.54501 -4.88746  1.000 51.33111  ? 55  LEU B CB  1 
ATOM   1224 C CG  . LEU B 1 36  ? 0.95022   32.63977 -4.70238  1.000 55.72276  ? 55  LEU B CG  1 
ATOM   1225 C CD1 . LEU B 1 36  ? 0.62439   33.50052 -3.49191  1.000 54.78156  ? 55  LEU B CD1 1 
ATOM   1226 C CD2 . LEU B 1 36  ? 2.32491   32.01325 -4.55685  1.000 54.83914  ? 55  LEU B CD2 1 
ATOM   1227 N N   . SER B 1 37  ? -1.87355  34.00356 -6.49547  1.000 52.19559  ? 56  SER B N   1 
ATOM   1228 C CA  . SER B 1 37  ? -1.89792  34.83443 -7.69216  1.000 64.40697  ? 56  SER B CA  1 
ATOM   1229 C C   . SER B 1 37  ? -0.46988  35.12369 -8.13645  1.000 56.26798  ? 56  SER B C   1 
ATOM   1230 O O   . SER B 1 37  ? 0.33655   35.64330 -7.35764  1.000 55.48661  ? 56  SER B O   1 
ATOM   1231 C CB  . SER B 1 37  ? -2.65496  36.13295 -7.42686  1.000 51.88792  ? 56  SER B CB  1 
ATOM   1232 O OG  . SER B 1 37  ? -2.85546  36.85330 -8.63151  1.000 76.76081  ? 56  SER B OG  1 
ATOM   1233 N N   . ALA B 1 38  ? -0.15117  34.76805 -9.37877  1.000 63.99533  ? 57  ALA B N   1 
ATOM   1234 C CA  . ALA B 1 38  ? 1.19917   34.89362 -9.90355  1.000 67.38011  ? 57  ALA B CA  1 
ATOM   1235 C C   . ALA B 1 38  ? 1.19144   35.63472 -11.23480 1.000 67.68334  ? 57  ALA B C   1 
ATOM   1236 O O   . ALA B 1 38  ? 0.15596   35.78021 -11.88977 1.000 65.08904  ? 57  ALA B O   1 
ATOM   1237 C CB  . ALA B 1 38  ? 1.86100   33.52086 -10.07890 1.000 60.97441  ? 57  ALA B CB  1 
ATOM   1238 N N   . ARG B 1 39  ? 2.37732   36.10245 -11.62292 1.000 71.88113  ? 58  ARG B N   1 
ATOM   1239 C CA  . ARG B 1 39  ? 2.60339   36.77210 -12.89500 1.000 75.50863  ? 58  ARG B CA  1 
ATOM   1240 C C   . ARG B 1 39  ? 3.84661   36.18470 -13.55056 1.000 67.24323  ? 58  ARG B C   1 
ATOM   1241 O O   . ARG B 1 39  ? 4.76324   35.71955 -12.86805 1.000 64.31763  ? 58  ARG B O   1 
ATOM   1242 C CB  . ARG B 1 39  ? 2.77417   38.29916 -12.72475 1.000 70.58236  ? 58  ARG B CB  1 
ATOM   1243 C CG  . ARG B 1 39  ? 3.83867   38.68558 -11.70222 1.000 77.49106  ? 58  ARG B CG  1 
ATOM   1244 C CD  . ARG B 1 39  ? 4.33022   40.13021 -11.84329 1.000 72.10473  ? 58  ARG B CD  1 
ATOM   1245 N NE  . ARG B 1 39  ? 3.33102   41.12813 -11.48183 1.000 83.47272  ? 58  ARG B NE  1 
ATOM   1246 C CZ  . ARG B 1 39  ? 2.78115   41.98537 -12.33203 1.000 88.95744  ? 58  ARG B CZ  1 
ATOM   1247 N NH1 . ARG B 1 39  ? 1.88589   42.87419 -11.93390 1.000 74.81895  ? 58  ARG B NH1 1 
ATOM   1248 N NH2 . ARG B 1 39  ? 3.14922   41.95933 -13.61060 1.000 90.43029  ? 58  ARG B NH2 1 
ATOM   1249 N N   . ASP B 1 40  ? 3.85344   36.18869 -14.88455 1.000 73.38737  ? 59  ASP B N   1 
ATOM   1250 C CA  . ASP B 1 40  ? 4.99596   35.75206 -15.68961 1.000 73.19663  ? 59  ASP B CA  1 
ATOM   1251 C C   . ASP B 1 40  ? 5.43396   34.33436 -15.31535 1.000 75.87316  ? 59  ASP B C   1 
ATOM   1252 O O   . ASP B 1 40  ? 6.59048   34.07364 -14.97571 1.000 76.12772  ? 59  ASP B O   1 
ATOM   1253 C CB  . ASP B 1 40  ? 6.16151   36.73880 -15.56060 1.000 79.24282  ? 59  ASP B CB  1 
ATOM   1254 C CG  . ASP B 1 40  ? 5.77881   38.15016 -15.96315 1.000 82.76624  ? 59  ASP B CG  1 
ATOM   1255 O OD1 . ASP B 1 40  ? 5.16294   38.85497 -15.13744 1.000 82.10560  ? 59  ASP B OD1 1 
ATOM   1256 O OD2 . ASP B 1 40  ? 6.08821   38.55255 -17.10516 1.000 88.09490  ? 59  ASP B OD2 1 
ATOM   1257 N N   . ILE B 1 41  ? 4.47840   33.41535 -15.38607 1.000 74.73053  ? 60  ILE B N   1 
ATOM   1258 C CA  . ILE B 1 41  ? 4.73290   32.01462 -15.06926 1.000 67.33288  ? 60  ILE B CA  1 
ATOM   1259 C C   . ILE B 1 41  ? 5.46351   31.37544 -16.24396 1.000 77.23796  ? 60  ILE B C   1 
ATOM   1260 O O   . ILE B 1 41  ? 4.96392   31.37636 -17.37382 1.000 79.47361  ? 60  ILE B O   1 
ATOM   1261 C CB  . ILE B 1 41  ? 3.42481   31.27492 -14.75424 1.000 70.64128  ? 60  ILE B CB  1 
ATOM   1262 C CG1 . ILE B 1 41  ? 2.76602   31.87796 -13.51030 1.000 66.39272  ? 60  ILE B CG1 1 
ATOM   1263 C CG2 . ILE B 1 41  ? 3.67743   29.78825 -14.56623 1.000 64.91504  ? 60  ILE B CG2 1 
ATOM   1264 C CD1 . ILE B 1 41  ? 1.42912   31.26746 -13.16542 1.000 73.59303  ? 60  ILE B CD1 1 
ATOM   1265 N N   . LYS B 1 42  ? 6.65794   30.84817 -15.98250 1.000 72.49618  ? 61  LYS B N   1 
ATOM   1266 C CA  . LYS B 1 42  ? 7.47491   30.17481 -16.98506 1.000 77.48011  ? 61  LYS B CA  1 
ATOM   1267 C C   . LYS B 1 42  ? 7.81694   28.77511 -16.49136 1.000 73.98719  ? 61  LYS B C   1 
ATOM   1268 O O   . LYS B 1 42  ? 8.49497   28.62219 -15.46980 1.000 69.35808  ? 61  LYS B O   1 
ATOM   1269 C CB  . LYS B 1 42  ? 8.75077   30.96927 -17.28418 1.000 79.15442  ? 61  LYS B CB  1 
ATOM   1270 C CG  . LYS B 1 42  ? 8.55015   32.16582 -18.20963 1.000 86.74111  ? 61  LYS B CG  1 
ATOM   1271 C CD  . LYS B 1 42  ? 9.88138   32.81662 -18.57428 1.000 92.03068  ? 61  LYS B CD  1 
ATOM   1272 C CE  . LYS B 1 42  ? 9.71725   33.85586 -19.67680 1.000 88.49062  ? 61  LYS B CE  1 
ATOM   1273 N NZ  . LYS B 1 42  ? 8.77557   34.94394 -19.29448 1.000 86.42591  ? 61  LYS B NZ  1 
ATOM   1274 N N   . ARG B 1 43  ? 7.33462   27.76009 -17.20233 1.000 73.59325  ? 62  ARG B N   1 
ATOM   1275 C CA  . ARG B 1 43  ? 7.69074   26.37815 -16.91411 1.000 69.01221  ? 62  ARG B CA  1 
ATOM   1276 C C   . ARG B 1 43  ? 8.99111   26.02293 -17.62226 1.000 69.99469  ? 62  ARG B C   1 
ATOM   1277 O O   . ARG B 1 43  ? 9.20778   26.41335 -18.77244 1.000 79.82019  ? 62  ARG B O   1 
ATOM   1278 C CB  . ARG B 1 43  ? 6.57787   25.43539 -17.36963 1.000 68.06427  ? 62  ARG B CB  1 
ATOM   1279 C CG  . ARG B 1 43  ? 5.20844   25.79558 -16.83371 1.000 70.21879  ? 62  ARG B CG  1 
ATOM   1280 C CD  . ARG B 1 43  ? 4.91331   25.05644 -15.54601 1.000 74.64546  ? 62  ARG B CD  1 
ATOM   1281 N NE  . ARG B 1 43  ? 4.68331   23.63679 -15.78718 1.000 85.75215  ? 62  ARG B NE  1 
ATOM   1282 C CZ  . ARG B 1 43  ? 3.50072   23.10868 -16.07180 1.000 83.33061  ? 62  ARG B CZ  1 
ATOM   1283 N NH1 . ARG B 1 43  ? 2.41204   23.85678 -16.15746 1.000 79.34649  ? 62  ARG B NH1 1 
ATOM   1284 N NH2 . ARG B 1 43  ? 3.40810   21.79746 -16.27574 1.000 88.68755  ? 62  ARG B NH2 1 
ATOM   1285 N N   . PHE B 1 44  ? 9.85847   25.28138 -16.93540 1.000 75.19777  ? 63  PHE B N   1 
ATOM   1286 C CA  . PHE B 1 44  ? 11.10810  24.84126 -17.54652 1.000 70.94032  ? 63  PHE B CA  1 
ATOM   1287 C C   . PHE B 1 44  ? 11.51595  23.50101 -16.94708 1.000 67.15556  ? 63  PHE B C   1 
ATOM   1288 O O   . PHE B 1 44  ? 10.80727  22.92440 -16.11982 1.000 67.11203  ? 63  PHE B O   1 
ATOM   1289 C CB  . PHE B 1 44  ? 12.20629  25.90539 -17.39983 1.000 69.87299  ? 63  PHE B CB  1 
ATOM   1290 C CG  . PHE B 1 44  ? 12.61927  26.18313 -15.97896 1.000 73.87671  ? 63  PHE B CG  1 
ATOM   1291 C CD1 . PHE B 1 44  ? 11.89951  27.06777 -15.19224 1.000 62.02197  ? 63  PHE B CD1 1 
ATOM   1292 C CD2 . PHE B 1 44  ? 13.74839  25.58812 -15.44213 1.000 78.88298  ? 63  PHE B CD2 1 
ATOM   1293 C CE1 . PHE B 1 44  ? 12.28590  27.33396 -13.88956 1.000 59.85365  ? 63  PHE B CE1 1 
ATOM   1294 C CE2 . PHE B 1 44  ? 14.13851  25.85213 -14.14074 1.000 68.93690  ? 63  PHE B CE2 1 
ATOM   1295 C CZ  . PHE B 1 44  ? 13.40806  26.72757 -13.36558 1.000 57.05617  ? 63  PHE B CZ  1 
ATOM   1296 N N   . LYS B 1 45  ? 12.66616  22.99770 -17.38543 1.000 74.54124  ? 64  LYS B N   1 
ATOM   1297 C CA  . LYS B 1 45  ? 13.20682  21.73083 -16.91136 1.000 74.31149  ? 64  LYS B CA  1 
ATOM   1298 C C   . LYS B 1 45  ? 14.56365  21.98014 -16.27290 1.000 77.85467  ? 64  LYS B C   1 
ATOM   1299 O O   . LYS B 1 45  ? 15.38203  22.72530 -16.81979 1.000 82.02230  ? 64  LYS B O   1 
ATOM   1300 C CB  . LYS B 1 45  ? 13.33448  20.70974 -18.04855 1.000 74.89038  ? 64  LYS B CB  1 
ATOM   1301 C CG  . LYS B 1 45  ? 12.01132  20.10982 -18.50098 1.000 79.09711  ? 64  LYS B CG  1 
ATOM   1302 C CD  . LYS B 1 45  ? 11.34803  19.31602 -17.38423 1.000 81.07477  ? 64  LYS B CD  1 
ATOM   1303 C CE  . LYS B 1 45  ? 10.24222  18.41722 -17.91959 1.000 77.33653  ? 64  LYS B CE  1 
ATOM   1304 N NZ  . LYS B 1 45  ? 10.76365  17.37335 -18.84667 1.000 82.11780  ? 64  LYS B NZ  1 
ATOM   1305 N N   . ARG B 1 46  ? 14.78750  21.37777 -15.10724 1.000 80.70011  ? 65  ARG B N   1 
ATOM   1306 C CA  . ARG B 1 46  ? 16.06933  21.44859 -14.41409 1.000 81.06052  ? 65  ARG B CA  1 
ATOM   1307 C C   . ARG B 1 46  ? 16.48922  20.03190 -14.04539 1.000 78.20686  ? 65  ARG B C   1 
ATOM   1308 O O   . ARG B 1 46  ? 15.84279  19.38938 -13.21175 1.000 74.18133  ? 65  ARG B O   1 
ATOM   1309 C CB  . ARG B 1 46  ? 15.95635  22.33870 -13.17758 1.000 70.46514  ? 65  ARG B CB  1 
ATOM   1310 C CG  . ARG B 1 46  ? 17.18078  22.36445 -12.29364 1.000 71.49237  ? 65  ARG B CG  1 
ATOM   1311 C CD  . ARG B 1 46  ? 17.10693  23.52942 -11.32517 1.000 66.19674  ? 65  ARG B CD  1 
ATOM   1312 N NE  . ARG B 1 46  ? 16.97917  24.80856 -12.01408 1.000 61.19825  ? 65  ARG B NE  1 
ATOM   1313 C CZ  . ARG B 1 46  ? 16.71806  25.96005 -11.41109 1.000 68.08488  ? 65  ARG B CZ  1 
ATOM   1314 N NH1 . ARG B 1 46  ? 16.52008  26.02642 -10.10530 1.000 68.01420  ? 65  ARG B NH1 1 
ATOM   1315 N NH2 . ARG B 1 46  ? 16.65780  27.07371 -12.13558 1.000 68.14195  ? 65  ARG B NH2 1 
ATOM   1316 N N   . ASN B 1 47  ? 17.58429  19.56069 -14.64844 1.000 78.82497  ? 66  ASN B N   1 
ATOM   1317 C CA  . ASN B 1 47  ? 18.08112  18.19611 -14.44469 1.000 86.91543  ? 66  ASN B CA  1 
ATOM   1318 C C   . ASN B 1 47  ? 16.97314  17.16344 -14.63762 1.000 80.85085  ? 66  ASN B C   1 
ATOM   1319 O O   . ASN B 1 47  ? 16.87988  16.17728 -13.90394 1.000 76.76938  ? 66  ASN B O   1 
ATOM   1320 C CB  . ASN B 1 47  ? 18.74887  18.02775 -13.07809 1.000 94.74111  ? 66  ASN B CB  1 
ATOM   1321 C CG  . ASN B 1 47  ? 19.91101  18.97835 -12.87355 1.000 103.56868 ? 66  ASN B CG  1 
ATOM   1322 O OD1 . ASN B 1 47  ? 20.08782  19.93715 -13.62686 1.000 104.50056 ? 66  ASN B OD1 1 
ATOM   1323 N ND2 . ASN B 1 47  ? 20.73797  18.69047 -11.87256 1.000 92.06365  ? 66  ASN B ND2 1 
ATOM   1324 N N   . GLY B 1 48  ? 16.10945  17.40114 -15.62541 1.000 79.04119  ? 67  GLY B N   1 
ATOM   1325 C CA  . GLY B 1 48  ? 15.02423  16.49147 -15.91707 1.000 79.21909  ? 67  GLY B CA  1 
ATOM   1326 C C   . GLY B 1 48  ? 13.75898  16.69967 -15.11161 1.000 87.39429  ? 67  GLY B C   1 
ATOM   1327 O O   . GLY B 1 48  ? 12.73710  16.07829 -15.42971 1.000 92.86226  ? 67  GLY B O   1 
ATOM   1328 N N   . GLU B 1 49  ? 13.78746  17.54200 -14.08130 1.000 82.36854  ? 68  GLU B N   1 
ATOM   1329 C CA  . GLU B 1 49  ? 12.61801  17.77366 -13.24567 1.000 73.71119  ? 68  GLU B CA  1 
ATOM   1330 C C   . GLU B 1 49  ? 11.85589  18.99578 -13.73669 1.000 72.14914  ? 68  GLU B C   1 
ATOM   1331 O O   . GLU B 1 49  ? 12.45597  20.00612 -14.11254 1.000 72.09148  ? 68  GLU B O   1 
ATOM   1332 C CB  . GLU B 1 49  ? 13.02961  17.98455 -11.78667 1.000 75.06469  ? 68  GLU B CB  1 
ATOM   1333 C CG  . GLU B 1 49  ? 14.28033  17.23026 -11.36975 1.000 89.00961  ? 68  GLU B CG  1 
ATOM   1334 C CD  . GLU B 1 49  ? 14.95446  17.84415 -10.15213 1.000 91.33052  ? 68  GLU B CD  1 
ATOM   1335 O OE1 . GLU B 1 49  ? 14.43959  18.85717 -9.62715  1.000 80.32047  ? 68  GLU B OE1 1 
ATOM   1336 O OE2 . GLU B 1 49  ? 16.00275  17.31462 -9.72346  1.000 91.58790  ? 68  GLU B OE2 1 
ATOM   1337 N N   . SER B 1 50  ? 10.52912  18.89252 -13.74711 1.000 74.02011  ? 69  SER B N   1 
ATOM   1338 C CA  . SER B 1 50  ? 9.69938   20.03328 -14.10951 1.000 65.55031  ? 69  SER B CA  1 
ATOM   1339 C C   . SER B 1 50  ? 9.77478   21.09722 -13.02148 1.000 63.51959  ? 69  SER B C   1 
ATOM   1340 O O   . SER B 1 50  ? 9.54168   20.81223 -11.84228 1.000 62.23449  ? 69  SER B O   1 
ATOM   1341 C CB  . SER B 1 50  ? 8.25415   19.59582 -14.33102 1.000 64.24239  ? 69  SER B CB  1 
ATOM   1342 O OG  . SER B 1 50  ? 8.17590   18.61443 -15.35030 1.000 79.02708  ? 69  SER B OG  1 
ATOM   1343 N N   . TRP B 1 51  ? 10.10021  22.32491 -13.41737 1.000 58.55344  ? 70  TRP B N   1 
ATOM   1344 C CA  . TRP B 1 51  ? 10.19042  23.45612 -12.51266 1.000 60.79764  ? 70  TRP B CA  1 
ATOM   1345 C C   . TRP B 1 51  ? 9.33620   24.59335 -13.05200 1.000 59.66479  ? 70  TRP B C   1 
ATOM   1346 O O   . TRP B 1 51  ? 8.94542   24.61125 -14.22384 1.000 58.54969  ? 70  TRP B O   1 
ATOM   1347 C CB  . TRP B 1 51  ? 11.63978  23.92909 -12.35930 1.000 51.34030  ? 70  TRP B CB  1 
ATOM   1348 C CG  . TRP B 1 51  ? 12.44661  23.15456 -11.36872 1.000 61.37567  ? 70  TRP B CG  1 
ATOM   1349 C CD1 . TRP B 1 51  ? 12.78460  21.83543 -11.44269 1.000 54.35273  ? 70  TRP B CD1 1 
ATOM   1350 C CD2 . TRP B 1 51  ? 13.05098  23.65746 -10.17121 1.000 58.42793  ? 70  TRP B CD2 1 
ATOM   1351 N NE1 . TRP B 1 51  ? 13.54679  21.48130 -10.35819 1.000 64.79892  ? 70  TRP B NE1 1 
ATOM   1352 C CE2 . TRP B 1 51  ? 13.72729  22.58212 -9.56305  1.000 57.58055  ? 70  TRP B CE2 1 
ATOM   1353 C CE3 . TRP B 1 51  ? 13.08132  24.91153 -9.55187  1.000 55.49339  ? 70  TRP B CE3 1 
ATOM   1354 C CZ2 . TRP B 1 51  ? 14.42431  22.71992 -8.36399  1.000 54.88602  ? 70  TRP B CZ2 1 
ATOM   1355 C CZ3 . TRP B 1 51  ? 13.77115  25.04781 -8.36152  1.000 60.28341  ? 70  TRP B CZ3 1 
ATOM   1356 C CH2 . TRP B 1 51  ? 14.43559  23.95745 -7.77989  1.000 67.18270  ? 70  TRP B CH2 1 
ATOM   1357 N N   . VAL B 1 52  ? 9.09900   25.57835 -12.19307 1.000 58.49986  ? 71  VAL B N   1 
ATOM   1358 C CA  . VAL B 1 52  ? 8.33003   26.76197 -12.54789 1.000 66.11877  ? 71  VAL B CA  1 
ATOM   1359 C C   . VAL B 1 52  ? 8.99661   27.98228 -11.92550 1.000 64.80193  ? 71  VAL B C   1 
ATOM   1360 O O   . VAL B 1 52  ? 9.55641   27.91511 -10.82381 1.000 59.42379  ? 71  VAL B O   1 
ATOM   1361 C CB  . VAL B 1 52  ? 6.85508   26.63595 -12.10728 1.000 60.81226  ? 71  VAL B CB  1 
ATOM   1362 C CG1 . VAL B 1 52  ? 6.73313   26.68800 -10.59501 1.000 53.86406  ? 71  VAL B CG1 1 
ATOM   1363 C CG2 . VAL B 1 52  ? 6.00728   27.70623 -12.76275 1.000 62.57320  ? 71  VAL B CG2 1 
ATOM   1364 N N   . ARG B 1 53  ? 8.96187   29.09043 -12.66026 1.000 71.08379  ? 72  ARG B N   1 
ATOM   1365 C CA  . ARG B 1 53  ? 9.48676   30.37599 -12.22889 1.000 68.09107  ? 72  ARG B CA  1 
ATOM   1366 C C   . ARG B 1 53  ? 8.38175   31.40905 -12.35737 1.000 73.78220  ? 72  ARG B C   1 
ATOM   1367 O O   . ARG B 1 53  ? 7.72732   31.48983 -13.39996 1.000 85.75944  ? 72  ARG B O   1 
ATOM   1368 C CB  . ARG B 1 53  ? 10.69040  30.78872 -13.07652 1.000 75.72587  ? 72  ARG B CB  1 
ATOM   1369 C CG  . ARG B 1 53  ? 11.18658  32.18850 -12.79991 1.000 77.24387  ? 72  ARG B CG  1 
ATOM   1370 C CD  . ARG B 1 53  ? 12.47285  32.47100 -13.55056 1.000 90.39876  ? 72  ARG B CD  1 
ATOM   1371 N NE  . ARG B 1 53  ? 12.95351  33.81663 -13.26932 1.000 100.83849 ? 72  ARG B NE  1 
ATOM   1372 C CZ  . ARG B 1 53  ? 12.60645  34.88897 -13.96778 1.000 101.54144 ? 72  ARG B CZ  1 
ATOM   1373 N NH1 . ARG B 1 53  ? 11.78047  34.80421 -14.99902 1.000 99.58353  ? 72  ARG B NH1 1 
ATOM   1374 N NH2 . ARG B 1 53  ? 13.09156  36.07681 -13.61713 1.000 97.70588  ? 72  ARG B NH2 1 
ATOM   1375 N N   . PHE B 1 54  ? 8.16909   32.19106 -11.30562 1.000 61.12451  ? 73  PHE B N   1 
ATOM   1376 C CA  . PHE B 1 54  ? 7.05272   33.12662 -11.30152 1.000 59.69156  ? 73  PHE B CA  1 
ATOM   1377 C C   . PHE B 1 54  ? 7.33276   34.22412 -10.28840 1.000 60.08650  ? 73  PHE B C   1 
ATOM   1378 O O   . PHE B 1 54  ? 8.23829   34.11855 -9.46037  1.000 55.37021  ? 73  PHE B O   1 
ATOM   1379 C CB  . PHE B 1 54  ? 5.73307   32.42157 -10.96882 1.000 49.31063  ? 73  PHE B CB  1 
ATOM   1380 C CG  . PHE B 1 54  ? 5.65517   31.93336 -9.54907  1.000 59.78299  ? 73  PHE B CG  1 
ATOM   1381 C CD1 . PHE B 1 54  ? 4.96676   32.65685 -8.59015  1.000 47.24309  ? 73  PHE B CD1 1 
ATOM   1382 C CD2 . PHE B 1 54  ? 6.28967   30.75928 -9.16817  1.000 58.34743  ? 73  PHE B CD2 1 
ATOM   1383 C CE1 . PHE B 1 54  ? 4.90100   32.21451 -7.28248  1.000 58.97674  ? 73  PHE B CE1 1 
ATOM   1384 C CE2 . PHE B 1 54  ? 6.22792   30.31259 -7.86184  1.000 48.67738  ? 73  PHE B CE2 1 
ATOM   1385 C CZ  . PHE B 1 54  ? 5.53397   31.04002 -6.91802  1.000 53.73608  ? 73  PHE B CZ  1 
ATOM   1386 N N   . TYR B 1 55  ? 6.52746   35.27880 -10.36132 1.000 54.70024  ? 74  TYR B N   1 
ATOM   1387 C CA  . TYR B 1 55  ? 6.51124   36.33547 -9.36470  1.000 51.65209  ? 74  TYR B CA  1 
ATOM   1388 C C   . TYR B 1 55  ? 5.12305   36.39944 -8.74991  1.000 55.93037  ? 74  TYR B C   1 
ATOM   1389 O O   . TYR B 1 55  ? 4.13442   36.00158 -9.37238  1.000 62.67217  ? 74  TYR B O   1 
ATOM   1390 C CB  . TYR B 1 55  ? 6.85684   37.71254 -9.95553  1.000 59.40685  ? 74  TYR B CB  1 
ATOM   1391 C CG  . TYR B 1 55  ? 8.16247   37.80409 -10.71051 1.000 60.67177  ? 74  TYR B CG  1 
ATOM   1392 C CD1 . TYR B 1 55  ? 8.22598   37.51987 -12.06767 1.000 63.49376  ? 74  TYR B CD1 1 
ATOM   1393 C CD2 . TYR B 1 55  ? 9.32433   38.21566 -10.07229 1.000 60.72239  ? 74  TYR B CD2 1 
ATOM   1394 C CE1 . TYR B 1 55  ? 9.41671   37.61917 -12.76309 1.000 79.54850  ? 74  TYR B CE1 1 
ATOM   1395 C CE2 . TYR B 1 55  ? 10.51764  38.31978 -10.75778 1.000 64.47679  ? 74  TYR B CE2 1 
ATOM   1396 C CZ  . TYR B 1 55  ? 10.56052  38.02044 -12.10232 1.000 79.58651  ? 74  TYR B CZ  1 
ATOM   1397 O OH  . TYR B 1 55  ? 11.75228  38.12203 -12.78538 1.000 82.09399  ? 74  TYR B OH  1 
ATOM   1398 N N   . LEU B 1 56  ? 5.05366   36.89233 -7.51910  1.000 51.22056  ? 75  LEU B N   1 
ATOM   1399 C CA  . LEU B 1 56  ? 3.75880   37.19950 -6.93663  1.000 53.01398  ? 75  LEU B CA  1 
ATOM   1400 C C   . LEU B 1 56  ? 3.08407   38.29395 -7.75118  1.000 61.75539  ? 75  LEU B C   1 
ATOM   1401 O O   . LEU B 1 56  ? 3.74588   39.14984 -8.34412  1.000 67.54645  ? 75  LEU B O   1 
ATOM   1402 C CB  . LEU B 1 56  ? 3.91762   37.65229 -5.48871  1.000 54.12163  ? 75  LEU B CB  1 
ATOM   1403 C CG  . LEU B 1 56  ? 4.53221   36.63459 -4.53346  1.000 60.49360  ? 75  LEU B CG  1 
ATOM   1404 C CD1 . LEU B 1 56  ? 4.53265   37.18236 -3.11688  1.000 66.01788  ? 75  LEU B CD1 1 
ATOM   1405 C CD2 . LEU B 1 56  ? 3.78567   35.31771 -4.61022  1.000 44.97181  ? 75  LEU B CD2 1 
ATOM   1406 N N   . ALA B 1 57  ? 1.75044   38.25385 -7.79874  1.000 57.38685  ? 76  ALA B N   1 
ATOM   1407 C CA  . ALA B 1 57  ? 1.03019   39.28290 -8.53981  1.000 58.30383  ? 76  ALA B CA  1 
ATOM   1408 C C   . ALA B 1 57  ? 1.30496   40.66675 -7.96911  1.000 56.48359  ? 76  ALA B C   1 
ATOM   1409 O O   . ALA B 1 57  ? 1.29219   41.65839 -8.70633  1.000 65.72928  ? 76  ALA B O   1 
ATOM   1410 C CB  . ALA B 1 57  ? -0.47007  38.99117 -8.53155  1.000 72.31799  ? 76  ALA B CB  1 
ATOM   1411 N N   . ILE B 1 58  ? 1.59011   40.74726 -6.66869  1.000 56.59007  ? 77  ILE B N   1 
ATOM   1412 C CA  . ILE B 1 58  ? 1.88732   42.02554 -6.03275  1.000 64.49034  ? 77  ILE B CA  1 
ATOM   1413 C C   . ILE B 1 58  ? 3.29507   42.51260 -6.36056  1.000 73.54251  ? 77  ILE B C   1 
ATOM   1414 O O   . ILE B 1 58  ? 3.54241   43.72420 -6.34374  1.000 66.55090  ? 77  ILE B O   1 
ATOM   1415 C CB  . ILE B 1 58  ? 1.66998   41.91565 -4.51212  1.000 64.94988  ? 77  ILE B CB  1 
ATOM   1416 C CG1 . ILE B 1 58  ? 1.88188   43.26879 -3.82477  1.000 81.84334  ? 77  ILE B CG1 1 
ATOM   1417 C CG2 . ILE B 1 58  ? 2.55985   40.83259 -3.91127  1.000 60.91913  ? 77  ILE B CG2 1 
ATOM   1418 C CD1 . ILE B 1 58  ? 1.70210   43.22698 -2.31963  1.000 85.34443  ? 77  ILE B CD1 1 
ATOM   1419 N N   . ASP B 1 59  ? 4.21535   41.60666 -6.69915  1.000 76.05731  ? 78  ASP B N   1 
ATOM   1420 C CA  . ASP B 1 59  ? 5.60898   41.95822 -6.98184  1.000 64.20518  ? 78  ASP B CA  1 
ATOM   1421 C C   . ASP B 1 59  ? 5.68000   42.57358 -8.37661  1.000 65.35089  ? 78  ASP B C   1 
ATOM   1422 O O   . ASP B 1 59  ? 6.08493   41.94489 -9.35798  1.000 68.69175  ? 78  ASP B O   1 
ATOM   1423 C CB  . ASP B 1 59  ? 6.50432   40.72986 -6.85870  1.000 61.21585  ? 78  ASP B CB  1 
ATOM   1424 C CG  . ASP B 1 59  ? 7.98343   41.05047 -7.03214  1.000 73.68902  ? 78  ASP B CG  1 
ATOM   1425 O OD1 . ASP B 1 59  ? 8.34750   42.24893 -7.06791  1.000 72.56810  ? 78  ASP B OD1 1 
ATOM   1426 O OD2 . ASP B 1 59  ? 8.78383   40.09258 -7.13764  1.000 60.26843  ? 78  ASP B OD2 1 
ATOM   1427 N N   . ALA B 1 60  ? 5.27601   43.84431 -8.45331  1.000 73.58396  ? 79  ALA B N   1 
ATOM   1428 C CA  . ALA B 1 60  ? 5.30414   44.55881 -9.72419  1.000 73.15582  ? 79  ALA B CA  1 
ATOM   1429 C C   . ALA B 1 60  ? 6.72621   44.86109 -10.17225 1.000 70.57389  ? 79  ALA B C   1 
ATOM   1430 O O   . ALA B 1 60  ? 7.01177   44.85222 -11.37578 1.000 70.19001  ? 79  ALA B O   1 
ATOM   1431 C CB  . ALA B 1 60  ? 4.50998   45.85730 -9.60941  1.000 71.55353  ? 79  ALA B CB  1 
ATOM   1432 N N   . ALA B 1 61  ? 7.62748   45.12141 -9.22879  1.000 68.69372  ? 80  ALA B N   1 
ATOM   1433 C CA  . ALA B 1 61  ? 9.00528   45.44906 -9.56359  1.000 70.59604  ? 80  ALA B CA  1 
ATOM   1434 C C   . ALA B 1 61  ? 9.83078   44.22578 -9.92559  1.000 69.32245  ? 80  ALA B C   1 
ATOM   1435 O O   . ALA B 1 61  ? 11.00350  44.37926 -10.28576 1.000 68.95239  ? 80  ALA B O   1 
ATOM   1436 C CB  . ALA B 1 61  ? 9.66679   46.18631 -8.39685  1.000 72.48874  ? 80  ALA B CB  1 
ATOM   1437 N N   . HIS B 1 62  ? 9.24492   43.02812 -9.84985  1.000 71.14308  ? 81  HIS B N   1 
ATOM   1438 C CA  . HIS B 1 62  ? 9.95103   41.78371 -10.14621 1.000 67.05753  ? 81  HIS B CA  1 
ATOM   1439 C C   . HIS B 1 62  ? 11.19063  41.64108 -9.26847  1.000 66.83108  ? 81  HIS B C   1 
ATOM   1440 O O   . HIS B 1 62  ? 12.27403  41.28953 -9.73915  1.000 67.81462  ? 81  HIS B O   1 
ATOM   1441 C CB  . HIS B 1 62  ? 10.31188  41.69093 -11.62909 1.000 69.86690  ? 81  HIS B CB  1 
ATOM   1442 C CG  . HIS B 1 62  ? 9.14129   41.41375 -12.51752 1.000 71.38036  ? 81  HIS B CG  1 
ATOM   1443 N ND1 . HIS B 1 62  ? 9.27989   41.02800 -13.83334 1.000 82.08754  ? 81  HIS B ND1 1 
ATOM   1444 C CD2 . HIS B 1 62  ? 7.81035   41.45157 -12.27447 1.000 78.83887  ? 81  HIS B CD2 1 
ATOM   1445 C CE1 . HIS B 1 62  ? 8.08443   40.84664 -14.36488 1.000 82.10671  ? 81  HIS B CE1 1 
ATOM   1446 N NE2 . HIS B 1 62  ? 7.17532   41.09680 -13.43985 1.000 92.14382  ? 81  HIS B NE2 1 
ATOM   1447 N N   . SER B 1 63  ? 11.02659  41.92670 -7.97815  1.000 67.58355  ? 82  SER B N   1 
ATOM   1448 C CA  . SER B 1 63  ? 12.13744  41.89842 -7.03735  1.000 74.14804  ? 82  SER B CA  1 
ATOM   1449 C C   . SER B 1 63  ? 12.36853  40.52392 -6.42308  1.000 75.69071  ? 82  SER B C   1 
ATOM   1450 O O   . SER B 1 63  ? 13.50261  40.21044 -6.04629  1.000 80.30501  ? 82  SER B O   1 
ATOM   1451 C CB  . SER B 1 63  ? 11.91157  42.92609 -5.92480  1.000 70.58999  ? 82  SER B CB  1 
ATOM   1452 O OG  . SER B 1 63  ? 10.73341  42.63359 -5.19561  1.000 73.49236  ? 82  SER B OG  1 
ATOM   1453 N N   . HIS B 1 64  ? 11.33408  39.68742 -6.30717  1.000 62.25198  ? 83  HIS B N   1 
ATOM   1454 C CA  . HIS B 1 64  ? 11.45677  38.37988 -5.66531  1.000 65.44932  ? 83  HIS B CA  1 
ATOM   1455 C C   . HIS B 1 64  ? 11.02306  37.28872 -6.63839  1.000 65.47950  ? 83  HIS B C   1 
ATOM   1456 O O   . HIS B 1 64  ? 9.93400   36.71274 -6.49454  1.000 54.15913  ? 83  HIS B O   1 
ATOM   1457 C CB  . HIS B 1 64  ? 10.62331  38.30781 -4.38665  1.000 67.00716  ? 83  HIS B CB  1 
ATOM   1458 C CG  . HIS B 1 64  ? 10.98390  39.34199 -3.36729  1.000 81.03127  ? 83  HIS B CG  1 
ATOM   1459 N ND1 . HIS B 1 64  ? 10.52113  40.63912 -3.42679  1.000 85.23608  ? 83  HIS B ND1 1 
ATOM   1460 C CD2 . HIS B 1 64  ? 11.74827  39.26614 -2.25235  1.000 84.71457  ? 83  HIS B CD2 1 
ATOM   1461 C CE1 . HIS B 1 64  ? 10.99433  41.32090 -2.39889  1.000 79.20931  ? 83  HIS B CE1 1 
ATOM   1462 N NE2 . HIS B 1 64  ? 11.74024  40.51037 -1.66986  1.000 84.52172  ? 83  HIS B NE2 1 
ATOM   1463 N N   . PRO B 1 65  ? 11.85970  36.95693 -7.62021  1.000 58.96194  ? 84  PRO B N   1 
ATOM   1464 C CA  . PRO B 1 65  ? 11.54799  35.80766 -8.47489  1.000 61.41183  ? 84  PRO B CA  1 
ATOM   1465 C C   . PRO B 1 65  ? 11.58369  34.52699 -7.65880  1.000 60.78920  ? 84  PRO B C   1 
ATOM   1466 O O   . PRO B 1 65  ? 12.46154  34.32944 -6.81554  1.000 63.28962  ? 84  PRO B O   1 
ATOM   1467 C CB  . PRO B 1 65  ? 12.65391  35.83949 -9.53619  1.000 65.76667  ? 84  PRO B CB  1 
ATOM   1468 C CG  . PRO B 1 65  ? 13.76681  36.60722 -8.90034  1.000 63.89726  ? 84  PRO B CG  1 
ATOM   1469 C CD  . PRO B 1 65  ? 13.10566  37.62635 -8.02714  1.000 57.68246  ? 84  PRO B CD  1 
ATOM   1470 N N   . ILE B 1 66  ? 10.60761  33.66152 -7.90757  1.000 54.99701  ? 85  ILE B N   1 
ATOM   1471 C CA  . ILE B 1 66  ? 10.43364  32.42019 -7.16328  1.000 59.92327  ? 85  ILE B CA  1 
ATOM   1472 C C   . ILE B 1 66  ? 10.56949  31.26171 -8.13757  1.000 55.44339  ? 85  ILE B C   1 
ATOM   1473 O O   . ILE B 1 66  ? 9.81992   31.17593 -9.11924  1.000 54.30250  ? 85  ILE B O   1 
ATOM   1474 C CB  . ILE B 1 66  ? 9.08142   32.37504 -6.43554  1.000 69.78133  ? 85  ILE B CB  1 
ATOM   1475 C CG1 . ILE B 1 66  ? 8.83766   33.69118 -5.69281  1.000 62.12157  ? 85  ILE B CG1 1 
ATOM   1476 C CG2 . ILE B 1 66  ? 9.02686   31.19135 -5.48085  1.000 71.19379  ? 85  ILE B CG2 1 
ATOM   1477 C CD1 . ILE B 1 66  ? 7.50134   33.76354 -4.99995  1.000 61.06634  ? 85  ILE B CD1 1 
ATOM   1478 N N   . GLU B 1 67  ? 11.52766  30.37875 -7.86842  1.000 63.11184  ? 86  GLU B N   1 
ATOM   1479 C CA  . GLU B 1 67  ? 11.76320  29.18121 -8.66450  1.000 52.95639  ? 86  GLU B CA  1 
ATOM   1480 C C   . GLU B 1 67  ? 11.52777  27.95793 -7.78873  1.000 50.99046  ? 86  GLU B C   1 
ATOM   1481 O O   . GLU B 1 67  ? 12.18975  27.79189 -6.75906  1.000 57.34222  ? 86  GLU B O   1 
ATOM   1482 C CB  . GLU B 1 67  ? 13.18077  29.18822 -9.23597  1.000 53.48798  ? 86  GLU B CB  1 
ATOM   1483 C CG  . GLU B 1 67  ? 13.28682  29.90090 -10.56989 1.000 61.51132  ? 86  GLU B CG  1 
ATOM   1484 C CD  . GLU B 1 67  ? 14.64180  29.72468 -11.21669 1.000 65.75025  ? 86  GLU B CD  1 
ATOM   1485 O OE1 . GLU B 1 67  ? 15.49109  29.02084 -10.63220 1.000 72.26669  ? 86  GLU B OE1 1 
ATOM   1486 O OE2 . GLU B 1 67  ? 14.85573  30.28521 -12.31236 1.000 72.44111  ? 86  GLU B OE2 1 
ATOM   1487 N N   . ARG B 1 68  ? 10.57396  27.11454 -8.18841  1.000 52.89132  ? 87  ARG B N   1 
ATOM   1488 C CA  . ARG B 1 68  ? 10.20305  25.92523 -7.42489  1.000 48.34184  ? 87  ARG B CA  1 
ATOM   1489 C C   . ARG B 1 68  ? 9.99693   24.71580 -8.32390  1.000 52.56443  ? 87  ARG B C   1 
ATOM   1490 O O   . ARG B 1 68  ? 9.47398   24.85139 -9.43843  1.000 53.90121  ? 87  ARG B O   1 
ATOM   1491 C CB  . ARG B 1 68  ? 8.91804   26.13452 -6.61375  1.000 46.21183  ? 87  ARG B CB  1 
ATOM   1492 C CG  . ARG B 1 68  ? 9.03004   27.02114 -5.39998  1.000 54.21050  ? 87  ARG B CG  1 
ATOM   1493 C CD  . ARG B 1 68  ? 9.84549   26.33387 -4.32112  1.000 55.53683  ? 87  ARG B CD  1 
ATOM   1494 N NE  . ARG B 1 68  ? 9.99069   27.16842 -3.13675  1.000 68.88023  ? 87  ARG B NE  1 
ATOM   1495 C CZ  . ARG B 1 68  ? 10.94492  28.07274 -2.97248  1.000 65.70987  ? 87  ARG B CZ  1 
ATOM   1496 N NH1 . ARG B 1 68  ? 11.92220  28.21457 -3.85391  1.000 75.10298  ? 87  ARG B NH1 1 
ATOM   1497 N NH2 . ARG B 1 68  ? 10.94380  28.82317 -1.87497  1.000 76.18268  ? 87  ARG B NH2 1 
ATOM   1498 N N   . PRO B 1 69  ? 10.38462  23.52840 -7.86649  1.000 52.54287  ? 88  PRO B N   1 
ATOM   1499 C CA  . PRO B 1 69  ? 10.02311  22.30951 -8.59359  1.000 54.42116  ? 88  PRO B CA  1 
ATOM   1500 C C   . PRO B 1 69  ? 8.51826   22.09903 -8.56329  1.000 54.64256  ? 88  PRO B C   1 
ATOM   1501 O O   . PRO B 1 69  ? 7.83862   22.44300 -7.59276  1.000 46.36310  ? 88  PRO B O   1 
ATOM   1502 C CB  . PRO B 1 69  ? 10.75326  21.20370 -7.82482  1.000 49.85105  ? 88  PRO B CB  1 
ATOM   1503 C CG  . PRO B 1 69  ? 10.92217  21.75761 -6.45349  1.000 50.67179  ? 88  PRO B CG  1 
ATOM   1504 C CD  . PRO B 1 69  ? 11.12844  23.23523 -6.63028  1.000 54.33553  ? 88  PRO B CD  1 
ATOM   1505 N N   . LEU B 1 70  ? 7.99578   21.54392 -9.65297  1.000 58.04657  ? 89  LEU B N   1 
ATOM   1506 C CA  . LEU B 1 70  ? 6.57403   21.23455 -9.71865  1.000 56.55834  ? 89  LEU B CA  1 
ATOM   1507 C C   . LEU B 1 70  ? 6.24244   20.07363 -8.78847  1.000 55.25608  ? 89  LEU B C   1 
ATOM   1508 O O   . LEU B 1 70  ? 6.91760   19.04093 -8.79947  1.000 60.99062  ? 89  LEU B O   1 
ATOM   1509 C CB  . LEU B 1 70  ? 6.16631   20.88973 -11.14931 1.000 53.13258  ? 89  LEU B CB  1 
ATOM   1510 C CG  . LEU B 1 70  ? 5.27556   21.90306 -11.86446 1.000 56.40219  ? 89  LEU B CG  1 
ATOM   1511 C CD1 . LEU B 1 70  ? 6.01928   23.20471 -12.04797 1.000 62.64447  ? 89  LEU B CD1 1 
ATOM   1512 C CD2 . LEU B 1 70  ? 4.81113   21.35675 -13.20161 1.000 63.87485  ? 89  LEU B CD2 1 
ATOM   1513 N N   . ALA B 1 71  ? 5.20826   20.25083 -7.97349  1.000 67.43165  ? 90  ALA B N   1 
ATOM   1514 C CA  . ALA B 1 71  ? 4.73415   19.18843 -7.09543  1.000 66.02601  ? 90  ALA B CA  1 
ATOM   1515 C C   . ALA B 1 71  ? 3.84123   18.22125 -7.86482  1.000 66.58419  ? 90  ALA B C   1 
ATOM   1516 O O   . ALA B 1 71  ? 4.19470   17.06054 -8.06389  1.000 73.33765  ? 90  ALA B O   1 
ATOM   1517 C CB  . ALA B 1 71  ? 3.98396   19.77413 -5.90851  1.000 63.38237  ? 90  ALA B CB  1 
ATOM   1518 N N   . THR B 1 92  ? -8.90471  25.41601 -16.64556 1.000 115.56310 ? 111 THR B N   1 
ATOM   1519 C CA  . THR B 1 92  ? -8.55985  25.33137 -15.23077 1.000 128.16981 ? 111 THR B CA  1 
ATOM   1520 C C   . THR B 1 92  ? -7.56687  24.19626 -14.97204 1.000 128.09118 ? 111 THR B C   1 
ATOM   1521 O O   . THR B 1 92  ? -7.96150  23.11165 -14.54557 1.000 133.61789 ? 111 THR B O   1 
ATOM   1522 C CB  . THR B 1 92  ? -9.81236  25.12984 -14.35842 1.000 125.59664 ? 111 THR B CB  1 
ATOM   1523 N N   . ALA B 1 93  ? -6.27900  24.45781 -15.22142 1.000 115.62343 ? 112 ALA B N   1 
ATOM   1524 C CA  . ALA B 1 93  ? -5.22317  23.47833 -14.97484 1.000 113.19525 ? 112 ALA B CA  1 
ATOM   1525 C C   . ALA B 1 93  ? -3.89268  24.17734 -14.69188 1.000 114.60757 ? 112 ALA B C   1 
ATOM   1526 O O   . ALA B 1 93  ? -3.05246  24.33109 -15.58741 1.000 108.45664 ? 112 ALA B O   1 
ATOM   1527 C CB  . ALA B 1 93  ? -5.08132  22.53051 -16.16453 1.000 109.09816 ? 112 ALA B CB  1 
ATOM   1528 N N   . ARG B 1 94  ? -3.68853  24.60292 -13.44449 1.000 109.67894 ? 113 ARG B N   1 
ATOM   1529 C CA  . ARG B 1 94  ? -2.58883  25.38147 -12.88610 1.000 92.68067  ? 113 ARG B CA  1 
ATOM   1530 C C   . ARG B 1 94  ? -1.47320  24.46933 -12.38116 1.000 96.79880  ? 113 ARG B C   1 
ATOM   1531 O O   . ARG B 1 94  ? -1.74828  23.37865 -11.86998 1.000 97.03117  ? 113 ARG B O   1 
ATOM   1532 C CB  . ARG B 1 94  ? -3.09229  26.25210 -11.74057 1.000 84.71424  ? 113 ARG B CB  1 
ATOM   1533 N N   . PRO B 1 95  ? -0.21705  24.89413 -12.52385 1.000 83.93506  ? 114 PRO B N   1 
ATOM   1534 C CA  . PRO B 1 95  ? 0.88639   24.14104 -11.91675 1.000 73.67092  ? 114 PRO B CA  1 
ATOM   1535 C C   . PRO B 1 95  ? 0.84903   24.26077 -10.40198 1.000 68.22481  ? 114 PRO B C   1 
ATOM   1536 O O   . PRO B 1 95  ? 0.50391   25.30950 -9.85297  1.000 65.79164  ? 114 PRO B O   1 
ATOM   1537 C CB  . PRO B 1 95  ? 2.13645   24.80461 -12.50310 1.000 65.48613  ? 114 PRO B CB  1 
ATOM   1538 C CG  . PRO B 1 95  ? 1.69511   26.19163 -12.83160 1.000 78.00184  ? 114 PRO B CG  1 
ATOM   1539 C CD  . PRO B 1 95  ? 0.25993   26.07107 -13.26883 1.000 71.87002  ? 114 PRO B CD  1 
ATOM   1540 N N   . VAL B 1 96  ? 1.21780   23.17595 -9.72589  1.000 65.62560  ? 115 VAL B N   1 
ATOM   1541 C CA  . VAL B 1 96  ? 1.15845   23.09446 -8.27167  1.000 56.41786  ? 115 VAL B CA  1 
ATOM   1542 C C   . VAL B 1 96  ? 2.56840   22.95657 -7.71485  1.000 60.89764  ? 115 VAL B C   1 
ATOM   1543 O O   . VAL B 1 96  ? 3.38532   22.18699 -8.23656  1.000 57.86597  ? 115 VAL B O   1 
ATOM   1544 C CB  . VAL B 1 96  ? 0.27214   21.91740 -7.82034  1.000 53.90361  ? 115 VAL B CB  1 
ATOM   1545 C CG1 . VAL B 1 96  ? 0.12134   21.90998 -6.30654  1.000 58.25980  ? 115 VAL B CG1 1 
ATOM   1546 C CG2 . VAL B 1 96  ? -1.08017  21.98714 -8.50209  1.000 57.18522  ? 115 VAL B CG2 1 
ATOM   1547 N N   . ILE B 1 97  ? 2.84614   23.69660 -6.64035  1.000 54.68596  ? 116 ILE B N   1 
ATOM   1548 C CA  . ILE B 1 97  ? 4.13965   23.66275 -5.97024  1.000 61.88677  ? 116 ILE B CA  1 
ATOM   1549 C C   . ILE B 1 97  ? 3.91335   23.57562 -4.46629  1.000 56.78379  ? 116 ILE B C   1 
ATOM   1550 O O   . ILE B 1 97  ? 2.80679   23.76561 -3.96398  1.000 52.62732  ? 116 ILE B O   1 
ATOM   1551 C CB  . ILE B 1 97  ? 5.01774   24.88842 -6.30374  1.000 53.11952  ? 116 ILE B CB  1 
ATOM   1552 C CG1 . ILE B 1 97  ? 4.28560   26.18541 -5.96181  1.000 48.02836  ? 116 ILE B CG1 1 
ATOM   1553 C CG2 . ILE B 1 97  ? 5.42558   24.87038 -7.76504  1.000 50.46939  ? 116 ILE B CG2 1 
ATOM   1554 C CD1 . ILE B 1 97  ? 5.17434   27.40580 -6.00667  1.000 55.31197  ? 116 ILE B CD1 1 
ATOM   1555 N N   . GLU B 1 98  ? 4.99296   23.30005 -3.74563  1.000 55.21734  ? 117 GLU B N   1 
ATOM   1556 C CA  . GLU B 1 98  ? 4.97848   23.26069 -2.29134  1.000 58.36988  ? 117 GLU B CA  1 
ATOM   1557 C C   . GLU B 1 98  ? 5.73600   24.46223 -1.74656  1.000 57.13046  ? 117 GLU B C   1 
ATOM   1558 O O   . GLU B 1 98  ? 6.89077   24.69808 -2.11817  1.000 62.62996  ? 117 GLU B O   1 
ATOM   1559 C CB  . GLU B 1 98  ? 5.59275   21.96017 -1.77149  1.000 63.59315  ? 117 GLU B CB  1 
ATOM   1560 C CG  . GLU B 1 98  ? 4.68674   20.75217 -1.92873  1.000 76.34828  ? 117 GLU B CG  1 
ATOM   1561 C CD  . GLU B 1 98  ? 4.98820   19.66393 -0.91973  1.000 83.94559  ? 117 GLU B CD  1 
ATOM   1562 O OE1 . GLU B 1 98  ? 6.12513   19.14628 -0.93483  1.000 88.16435  ? 117 GLU B OE1 1 
ATOM   1563 O OE2 . GLU B 1 98  ? 4.09112   19.32548 -0.11710  1.000 80.75447  ? 117 GLU B OE2 1 
ATOM   1564 N N   . LEU B 1 99  ? 5.07619   25.22357 -0.88006  1.000 56.18665  ? 118 LEU B N   1 
ATOM   1565 C CA  . LEU B 1 99  ? 5.63959   26.43026 -0.29797  1.000 56.44283  ? 118 LEU B CA  1 
ATOM   1566 C C   . LEU B 1 99  ? 5.55033   26.33671 1.21529   1.000 60.09418  ? 118 LEU B C   1 
ATOM   1567 O O   . LEU B 1 99  ? 4.53644   25.88777 1.75387   1.000 56.99810  ? 118 LEU B O   1 
ATOM   1568 C CB  . LEU B 1 99  ? 4.89841   27.67854 -0.77941  1.000 53.71910  ? 118 LEU B CB  1 
ATOM   1569 C CG  . LEU B 1 99  ? 5.20357   28.14777 -2.19939  1.000 58.02596  ? 118 LEU B CG  1 
ATOM   1570 C CD1 . LEU B 1 99  ? 4.31113   29.32683 -2.56770  1.000 51.51419  ? 118 LEU B CD1 1 
ATOM   1571 C CD2 . LEU B 1 99  ? 6.67663   28.49316 -2.34840  1.000 62.81977  ? 118 LEU B CD2 1 
ATOM   1572 N N   . ASP B 1 100 ? 6.61636   26.73730 1.90011   1.000 49.55844  ? 119 ASP B N   1 
ATOM   1573 C CA  . ASP B 1 100 ? 6.57324   26.87264 3.35436   1.000 52.91778  ? 119 ASP B CA  1 
ATOM   1574 C C   . ASP B 1 100 ? 5.87665   28.18959 3.68220   1.000 55.06144  ? 119 ASP B C   1 
ATOM   1575 O O   . ASP B 1 100 ? 6.43318   29.26879 3.46867   1.000 68.81172  ? 119 ASP B O   1 
ATOM   1576 C CB  . ASP B 1 100 ? 7.97541   26.81397 3.94921   1.000 60.54198  ? 119 ASP B CB  1 
ATOM   1577 C CG  . ASP B 1 100 ? 8.57867   25.41794 3.89522   1.000 64.91453  ? 119 ASP B CG  1 
ATOM   1578 O OD1 . ASP B 1 100 ? 7.97202   24.51861 3.27160   1.000 62.89596  ? 119 ASP B OD1 1 
ATOM   1579 O OD2 . ASP B 1 100 ? 9.66208   25.22416 4.48438   1.000 72.45759  ? 119 ASP B OD2 1 
ATOM   1580 N N   . ILE B 1 101 ? 4.63228   28.11248 4.15189   1.000 54.82813  ? 120 ILE B N   1 
ATOM   1581 C CA  . ILE B 1 101 ? 3.83867   29.28883 4.48562   1.000 58.58903  ? 120 ILE B CA  1 
ATOM   1582 C C   . ILE B 1 101 ? 3.74506   29.42148 5.99934   1.000 59.82071  ? 120 ILE B C   1 
ATOM   1583 O O   . ILE B 1 101 ? 3.48894   28.43941 6.70853   1.000 59.76968  ? 120 ILE B O   1 
ATOM   1584 C CB  . ILE B 1 101 ? 2.43897   29.21509 3.84990   1.000 52.33131  ? 120 ILE B CB  1 
ATOM   1585 C CG1 . ILE B 1 101 ? 2.55902   29.03172 2.33741   1.000 50.33224  ? 120 ILE B CG1 1 
ATOM   1586 C CG2 . ILE B 1 101 ? 1.63959   30.47154 4.17204   1.000 53.72961  ? 120 ILE B CG2 1 
ATOM   1587 C CD1 . ILE B 1 101 ? 1.22898   28.97160 1.61815   1.000 61.04710  ? 120 ILE B CD1 1 
ATOM   1588 N N   . CYS B 1 102 ? 3.92087   30.64583 6.48688   1.000 55.69923  ? 121 CYS B N   1 
ATOM   1589 C CA  . CYS B 1 102 ? 3.89391   30.95073 7.90939   1.000 55.43548  ? 121 CYS B CA  1 
ATOM   1590 C C   . CYS B 1 102 ? 2.67859   31.81154 8.20815   1.000 56.98688  ? 121 CYS B C   1 
ATOM   1591 O O   . CYS B 1 102 ? 2.46173   32.83427 7.55258   1.000 58.39522  ? 121 CYS B O   1 
ATOM   1592 C CB  . CYS B 1 102 ? 5.16567   31.67802 8.35015   1.000 66.08067  ? 121 CYS B CB  1 
ATOM   1593 S SG  . CYS B 1 102 ? 5.03682   32.46007 9.98207   1.000 70.96003  ? 121 CYS B SG  1 
ATOM   1594 N N   . MET B 1 103 ? 1.88949   31.39011 9.18945   1.000 59.09362  ? 122 MET B N   1 
ATOM   1595 C CA  . MET B 1 103 ? 0.69323   32.11181 9.59905   1.000 56.30649  ? 122 MET B CA  1 
ATOM   1596 C C   . MET B 1 103 ? 0.67577   32.15310 11.11639  1.000 57.03415  ? 122 MET B C   1 
ATOM   1597 O O   . MET B 1 103 ? 0.68405   31.10251 11.76602  1.000 56.90991  ? 122 MET B O   1 
ATOM   1598 C CB  . MET B 1 103 ? -0.56228  31.43656 9.04798   1.000 61.88782  ? 122 MET B CB  1 
ATOM   1599 C CG  . MET B 1 103 ? -1.85978  32.03983 9.52024   1.000 55.24362  ? 122 MET B CG  1 
ATOM   1600 S SD  . MET B 1 103 ? -3.22504  31.48526 8.49093   1.000 54.61657  ? 122 MET B SD  1 
ATOM   1601 C CE  . MET B 1 103 ? -2.86637  32.39680 6.99955   1.000 54.63364  ? 122 MET B CE  1 
ATOM   1602 N N   . GLY B 1 104 ? 0.66572   33.35628 11.67350  1.000 64.00772  ? 123 GLY B N   1 
ATOM   1603 C CA  . GLY B 1 104 ? 0.87365   33.49376 13.10392  1.000 61.37877  ? 123 GLY B CA  1 
ATOM   1604 C C   . GLY B 1 104 ? 2.23769   32.94323 13.46712  1.000 64.55383  ? 123 GLY B C   1 
ATOM   1605 O O   . GLY B 1 104 ? 3.27347   33.42307 12.99343  1.000 60.86912  ? 123 GLY B O   1 
ATOM   1606 N N   . SER B 1 105 ? 2.24950   31.89926 14.29334  1.000 67.70896  ? 124 SER B N   1 
ATOM   1607 C CA  . SER B 1 105 ? 3.47656   31.20775 14.66060  1.000 66.00371  ? 124 SER B CA  1 
ATOM   1608 C C   . SER B 1 105 ? 3.53968   29.79714 14.09035  1.000 64.21394  ? 124 SER B C   1 
ATOM   1609 O O   . SER B 1 105 ? 4.37862   29.00060 14.52301  1.000 65.44016  ? 124 SER B O   1 
ATOM   1610 C CB  . SER B 1 105 ? 3.62440   31.16761 16.18324  1.000 65.33879  ? 124 SER B CB  1 
ATOM   1611 O OG  . SER B 1 105 ? 2.58424   30.41053 16.77602  1.000 69.63351  ? 124 SER B OG  1 
ATOM   1612 N N   . ALA B 1 106 ? 2.67847   29.46762 13.13267  1.000 63.24114  ? 125 ALA B N   1 
ATOM   1613 C CA  . ALA B 1 106 ? 2.60599   28.12580 12.57050  1.000 52.15939  ? 125 ALA B CA  1 
ATOM   1614 C C   . ALA B 1 106 ? 3.22407   28.13387 11.18108  1.000 55.22002  ? 125 ALA B C   1 
ATOM   1615 O O   . ALA B 1 106 ? 2.79509   28.89596 10.30938  1.000 57.98868  ? 125 ALA B O   1 
ATOM   1616 C CB  . ALA B 1 106 ? 1.16313   27.62662 12.51399  1.000 54.07551  ? 125 ALA B CB  1 
ATOM   1617 N N   . MET B 1 107 ? 4.23092   27.29412 10.98278  1.000 52.11836  ? 126 MET B N   1 
ATOM   1618 C CA  . MET B 1 107 ? 4.86582   27.10534 9.68811   1.000 58.01817  ? 126 MET B CA  1 
ATOM   1619 C C   . MET B 1 107 ? 4.41725   25.77155 9.11811   1.000 52.81746  ? 126 MET B C   1 
ATOM   1620 O O   . MET B 1 107 ? 4.54141   24.74115 9.78648   1.000 52.04784  ? 126 MET B O   1 
ATOM   1621 C CB  . MET B 1 107 ? 6.39192   27.13285 9.80985   1.000 62.20510  ? 126 MET B CB  1 
ATOM   1622 C CG  . MET B 1 107 ? 7.10431   26.81008 8.50986   1.000 56.53024  ? 126 MET B CG  1 
ATOM   1623 S SD  . MET B 1 107 ? 7.05553   28.19860 7.36747   1.000 79.12924  ? 126 MET B SD  1 
ATOM   1624 C CE  . MET B 1 107 ? 8.09280   29.37243 8.23715   1.000 79.99411  ? 126 MET B CE  1 
ATOM   1625 N N   . ARG B 1 108 ? 3.88975   25.78793 7.89642   1.000 45.25838  ? 127 ARG B N   1 
ATOM   1626 C CA  . ARG B 1 108 ? 3.40871   24.56295 7.27756   1.000 51.99632  ? 127 ARG B CA  1 
ATOM   1627 C C   . ARG B 1 108 ? 3.81975   24.52367 5.81622   1.000 55.15098  ? 127 ARG B C   1 
ATOM   1628 O O   . ARG B 1 108 ? 3.78913   25.54662 5.12867   1.000 47.49156  ? 127 ARG B O   1 
ATOM   1629 C CB  . ARG B 1 108 ? 1.88358   24.43051 7.38404   1.000 49.74097  ? 127 ARG B CB  1 
ATOM   1630 C CG  . ARG B 1 108 ? 1.36597   24.29024 8.80112   1.000 53.96962  ? 127 ARG B CG  1 
ATOM   1631 C CD  . ARG B 1 108 ? 1.91465   23.04390 9.48887   1.000 48.54572  ? 127 ARG B CD  1 
ATOM   1632 N NE  . ARG B 1 108 ? 1.20784   22.79291 10.73867  1.000 50.11253  ? 127 ARG B NE  1 
ATOM   1633 C CZ  . ARG B 1 108 ? 1.47255   23.40458 11.88550  1.000 58.86005  ? 127 ARG B CZ  1 
ATOM   1634 N NH1 . ARG B 1 108 ? 2.43913   24.30378 11.98277  1.000 54.25608  ? 127 ARG B NH1 1 
ATOM   1635 N NH2 . ARG B 1 108 ? 0.73745   23.12020 12.95760  1.000 53.46762  ? 127 ARG B NH2 1 
ATOM   1636 N N   . SER B 1 109 ? 4.20870   23.33752 5.35117   1.000 47.22830  ? 128 SER B N   1 
ATOM   1637 C CA  . SER B 1 109 ? 4.40411   23.09883 3.92664   1.000 48.85349  ? 128 SER B CA  1 
ATOM   1638 C C   . SER B 1 109 ? 3.04071   22.90761 3.26833   1.000 50.25849  ? 128 SER B C   1 
ATOM   1639 O O   . SER B 1 109 ? 2.30326   21.97750 3.61283   1.000 66.14847  ? 128 SER B O   1 
ATOM   1640 C CB  . SER B 1 109 ? 5.29748   21.88212 3.70080   1.000 46.85021  ? 128 SER B CB  1 
ATOM   1641 O OG  . SER B 1 109 ? 5.54587   21.70024 2.31890   1.000 53.26794  ? 128 SER B OG  1 
ATOM   1642 N N   . ILE B 1 110 ? 2.70294   23.78999 2.33213   1.000 52.08516  ? 129 ILE B N   1 
ATOM   1643 C CA  . ILE B 1 110 ? 1.37273   23.87403 1.74631   1.000 52.63342  ? 129 ILE B CA  1 
ATOM   1644 C C   . ILE B 1 110 ? 1.48260   23.68907 0.24087   1.000 50.75922  ? 129 ILE B C   1 
ATOM   1645 O O   . ILE B 1 110 ? 2.39276   24.22914 -0.39767  1.000 57.46394  ? 129 ILE B O   1 
ATOM   1646 C CB  . ILE B 1 110 ? 0.70538   25.22616 2.08397   1.000 50.95965  ? 129 ILE B CB  1 
ATOM   1647 C CG1 . ILE B 1 110 ? 0.51222   25.35553 3.59474   1.000 50.95921  ? 129 ILE B CG1 1 
ATOM   1648 C CG2 . ILE B 1 110 ? -0.60566  25.40057 1.33750   1.000 55.59936  ? 129 ILE B CG2 1 
ATOM   1649 C CD1 . ILE B 1 110 ? -0.21110  24.18789 4.21341   1.000 49.65053  ? 129 ILE B CD1 1 
ATOM   1650 N N   . GLU B 1 111 ? 0.56287   22.91164 -0.31938  1.000 52.32867  ? 130 GLU B N   1 
ATOM   1651 C CA  . GLU B 1 111 ? 0.46286   22.77428 -1.76303  1.000 52.34658  ? 130 GLU B CA  1 
ATOM   1652 C C   . GLU B 1 111 ? -0.38356  23.90942 -2.31887  1.000 56.48635  ? 130 GLU B C   1 
ATOM   1653 O O   . GLU B 1 111 ? -1.48635  24.17517 -1.82913  1.000 59.31142  ? 130 GLU B O   1 
ATOM   1654 C CB  . GLU B 1 111 ? -0.13257  21.42113 -2.13593  1.000 58.46698  ? 130 GLU B CB  1 
ATOM   1655 C CG  . GLU B 1 111 ? 0.85767   20.28387 -1.99720  1.000 73.89414  ? 130 GLU B CG  1 
ATOM   1656 C CD  . GLU B 1 111 ? 0.36778   19.00925 -2.63887  1.000 66.60118  ? 130 GLU B CD  1 
ATOM   1657 O OE1 . GLU B 1 111 ? -0.86381  18.81949 -2.72187  1.000 70.00833  ? 130 GLU B OE1 1 
ATOM   1658 O OE2 . GLU B 1 111 ? 1.21714   18.20257 -3.06835  1.000 78.02025  ? 130 GLU B OE2 1 
ATOM   1659 N N   . VAL B 1 112 ? 0.14145   24.58366 -3.33469  1.000 49.31592  ? 131 VAL B N   1 
ATOM   1660 C CA  . VAL B 1 112 ? -0.44677  25.80106 -3.86819  1.000 49.93894  ? 131 VAL B CA  1 
ATOM   1661 C C   . VAL B 1 112 ? -0.48743  25.71222 -5.38744  1.000 52.50629  ? 131 VAL B C   1 
ATOM   1662 O O   . VAL B 1 112 ? 0.48994   25.29621 -6.02049  1.000 58.98689  ? 131 VAL B O   1 
ATOM   1663 C CB  . VAL B 1 112 ? 0.36489   27.02922 -3.40212  1.000 44.44118  ? 131 VAL B CB  1 
ATOM   1664 C CG1 . VAL B 1 112 ? 0.38966   28.09613 -4.46650  1.000 56.77676  ? 131 VAL B CG1 1 
ATOM   1665 C CG2 . VAL B 1 112 ? -0.19728  27.56770 -2.09473  1.000 49.41797  ? 131 VAL B CG2 1 
ATOM   1666 N N   . ASN B 1 113 ? -1.62469  26.09361 -5.96834  1.000 49.82425  ? 132 ASN B N   1 
ATOM   1667 C CA  . ASN B 1 113 ? -1.76544  26.24612 -7.40812  1.000 56.12066  ? 132 ASN B CA  1 
ATOM   1668 C C   . ASN B 1 113 ? -1.41065  27.67406 -7.79969  1.000 62.68281  ? 132 ASN B C   1 
ATOM   1669 O O   . ASN B 1 113 ? -1.90163  28.63054 -7.19359  1.000 56.50755  ? 132 ASN B O   1 
ATOM   1670 C CB  . ASN B 1 113 ? -3.19393  25.92985 -7.85836  1.000 56.44958  ? 132 ASN B CB  1 
ATOM   1671 C CG  . ASN B 1 113 ? -3.64468  24.53057 -7.47032  1.000 74.55658  ? 132 ASN B CG  1 
ATOM   1672 O OD1 . ASN B 1 113 ? -3.83006  23.66880 -8.33070  1.000 83.97103  ? 132 ASN B OD1 1 
ATOM   1673 N ND2 . ASN B 1 113 ? -3.83503  24.30068 -6.17555  1.000 80.11714  ? 132 ASN B ND2 1 
ATOM   1674 N N   . LEU B 1 114 ? -0.57183  27.81458 -8.81718  1.000 67.98273  ? 133 LEU B N   1 
ATOM   1675 C CA  . LEU B 1 114 ? -0.18307  29.12064 -9.33144  1.000 65.14923  ? 133 LEU B CA  1 
ATOM   1676 C C   . LEU B 1 114 ? -1.19524  29.55245 -10.38704 1.000 66.39840  ? 133 LEU B C   1 
ATOM   1677 O O   . LEU B 1 114 ? -1.33049  28.88847 -11.42059 1.000 66.32986  ? 133 LEU B O   1 
ATOM   1678 C CB  . LEU B 1 114 ? 1.22499   29.06469 -9.92339  1.000 61.27939  ? 133 LEU B CB  1 
ATOM   1679 C CG  . LEU B 1 114 ? 2.35251   28.60410 -8.99704  1.000 53.12442  ? 133 LEU B CG  1 
ATOM   1680 C CD1 . LEU B 1 114 ? 3.67105   28.57357 -9.75059  1.000 54.08133  ? 133 LEU B CD1 1 
ATOM   1681 C CD2 . LEU B 1 114 ? 2.45359   29.48651 -7.76285  1.000 56.66138  ? 133 LEU B CD2 1 
ATOM   1682 N N   . THR B 1 115 ? -1.91493  30.64643 -10.13593 1.000 59.65659  ? 134 THR B N   1 
ATOM   1683 C CA  . THR B 1 115 ? -2.90953  31.12297 -11.08870 1.000 74.86338  ? 134 THR B CA  1 
ATOM   1684 C C   . THR B 1 115 ? -2.44243  32.43377 -11.70516 1.000 76.43874  ? 134 THR B C   1 
ATOM   1685 O O   . THR B 1 115 ? -1.89971  33.29876 -11.01073 1.000 74.86176  ? 134 THR B O   1 
ATOM   1686 C CB  . THR B 1 115 ? -4.27564  31.33008 -10.42581 1.000 72.89628  ? 134 THR B CB  1 
ATOM   1687 O OG1 . THR B 1 115 ? -4.24525  32.51423 -9.61937  1.000 83.10874  ? 134 THR B OG1 1 
ATOM   1688 C CG2 . THR B 1 115 ? -4.63543  30.13765 -9.55054  1.000 73.08986  ? 134 THR B CG2 1 
ATOM   1689 N N   . ASP B 1 116 ? -2.70618  32.59957 -13.00002 1.000 92.80851  ? 135 ASP B N   1 
ATOM   1690 C CA  . ASP B 1 116 ? -2.30984  33.80867 -13.70574 1.000 98.62716  ? 135 ASP B CA  1 
ATOM   1691 C C   . ASP B 1 116 ? -3.38133  34.88370 -13.65473 1.000 106.67541 ? 135 ASP B C   1 
ATOM   1692 O O   . ASP B 1 116 ? -3.17848  35.97131 -14.20506 1.000 107.58655 ? 135 ASP B O   1 
ATOM   1693 C CB  . ASP B 1 116 ? -1.98477  33.48242 -15.16817 1.000 103.35548 ? 135 ASP B CB  1 
ATOM   1694 C CG  . ASP B 1 116 ? -0.77758  34.24328 -15.68602 1.000 111.33128 ? 135 ASP B CG  1 
ATOM   1695 O OD1 . ASP B 1 116 ? 0.23269   33.59457 -16.03410 1.000 105.61174 ? 135 ASP B OD1 1 
ATOM   1696 O OD2 . ASP B 1 116 ? -0.83223  35.49001 -15.73943 1.000 123.25495 ? 135 ASP B OD2 1 
ATOM   1697 N N   . ARG B 1 117 ? -4.51105  34.60500 -13.01218 1.000 110.00059 ? 136 ARG B N   1 
ATOM   1698 C CA  . ARG B 1 117 ? -5.51632  35.62834 -12.80531 1.000 120.86523 ? 136 ARG B CA  1 
ATOM   1699 C C   . ARG B 1 117 ? -5.00773  36.65523 -11.80028 1.000 125.31484 ? 136 ARG B C   1 
ATOM   1700 O O   . ARG B 1 117 ? -4.07303  36.40825 -11.03203 1.000 109.15482 ? 136 ARG B O   1 
ATOM   1701 C CB  . ARG B 1 117 ? -6.82602  35.01007 -12.31586 1.000 114.42341 ? 136 ARG B CB  1 
ATOM   1702 N N   . SER B 1 118 ? -5.65101  37.81687 -11.80050 1.000 139.91936 ? 137 SER B N   1 
ATOM   1703 C CA  . SER B 1 118 ? -5.35328  38.83666 -10.80682 1.000 142.89829 ? 137 SER B CA  1 
ATOM   1704 C C   . SER B 1 118 ? -6.59781  39.46605 -10.20788 1.000 147.46789 ? 137 SER B C   1 
ATOM   1705 O O   . SER B 1 118 ? -6.47552  40.18833 -9.21370  1.000 144.37883 ? 137 SER B O   1 
ATOM   1706 C CB  . SER B 1 118 ? -4.46580  39.93606 -11.40854 1.000 142.16192 ? 137 SER B CB  1 
ATOM   1707 O OG  . SER B 1 118 ? -3.20389  39.41380 -11.79107 1.000 130.78910 ? 137 SER B OG  1 
ATOM   1708 N N   . ALA B 1 119 ? -7.78688  39.22015 -10.76743 1.000 145.24379 ? 138 ALA B N   1 
ATOM   1709 C CA  . ALA B 1 119 ? -9.01991  39.68227 -10.14277 1.000 141.80459 ? 138 ALA B CA  1 
ATOM   1710 C C   . ALA B 1 119 ? -9.22351  39.07743 -8.76165  1.000 138.74949 ? 138 ALA B C   1 
ATOM   1711 O O   . ALA B 1 119 ? -10.05619 39.57620 -7.99654  1.000 131.92115 ? 138 ALA B O   1 
ATOM   1712 C CB  . ALA B 1 119 ? -10.21790 39.35899 -11.03675 1.000 139.41088 ? 138 ALA B CB  1 
ATOM   1713 N N   . PHE B 1 120 ? -8.48918  38.01525 -8.42827  1.000 139.16558 ? 139 PHE B N   1 
ATOM   1714 C CA  . PHE B 1 120 ? -8.50665  37.47947 -7.07585  1.000 133.21365 ? 139 PHE B CA  1 
ATOM   1715 C C   . PHE B 1 120 ? -7.96206  38.54841 -6.14117  1.000 136.44829 ? 139 PHE B C   1 
ATOM   1716 O O   . PHE B 1 120 ? -6.76162  38.84210 -6.16200  1.000 134.05055 ? 139 PHE B O   1 
ATOM   1717 C CB  . PHE B 1 120 ? -7.68215  36.19446 -6.98155  1.000 122.43383 ? 139 PHE B CB  1 
ATOM   1718 N N   . GLN B 1 121 ? -8.84184  39.14408 -5.33259  1.000 140.27625 ? 140 GLN B N   1 
ATOM   1719 C CA  . GLN B 1 121 ? -8.42435  40.22331 -4.44377  1.000 127.34660 ? 140 GLN B CA  1 
ATOM   1720 C C   . GLN B 1 121 ? -7.29268  39.77404 -3.53024  1.000 128.57867 ? 140 GLN B C   1 
ATOM   1721 O O   . GLN B 1 121 ? -6.26730  40.45486 -3.41163  1.000 123.27317 ? 140 GLN B O   1 
ATOM   1722 C CB  . GLN B 1 121 ? -9.61812  40.71539 -3.62185  1.000 126.58507 ? 140 GLN B CB  1 
ATOM   1723 C CG  . GLN B 1 121 ? -9.26253  41.73601 -2.54764  1.000 128.83369 ? 140 GLN B CG  1 
ATOM   1724 C CD  . GLN B 1 121 ? -10.41725 42.02148 -1.60246  1.000 131.53993 ? 140 GLN B CD  1 
ATOM   1725 O OE1 . GLN B 1 121 ? -11.50079 41.45216 -1.73627  1.000 130.52935 ? 140 GLN B OE1 1 
ATOM   1726 N NE2 . GLN B 1 121 ? -10.18755 42.90553 -0.63769  1.000 133.18917 ? 140 GLN B NE2 1 
ATOM   1727 N N   . TYR B 1 122 ? -7.46417  38.63519 -2.87121  1.000 116.72628 ? 141 TYR B N   1 
ATOM   1728 C CA  . TYR B 1 122 ? -6.45280  38.20386 -1.91547  1.000 99.27274  ? 141 TYR B CA  1 
ATOM   1729 C C   . TYR B 1 122 ? -5.35021  37.42887 -2.63118  1.000 87.28243  ? 141 TYR B C   1 
ATOM   1730 O O   . TYR B 1 122 ? -5.64758  36.47850 -3.36526  1.000 87.04484  ? 141 TYR B O   1 
ATOM   1731 C CB  . TYR B 1 122 ? -7.09010  37.36737 -0.81790  1.000 85.50836  ? 141 TYR B CB  1 
ATOM   1732 C CG  . TYR B 1 122 ? -7.86082  38.26221 0.12476   1.000 90.90161  ? 141 TYR B CG  1 
ATOM   1733 C CD1 . TYR B 1 122 ? -7.21443  38.97743 1.12413   1.000 92.62412  ? 141 TYR B CD1 1 
ATOM   1734 C CD2 . TYR B 1 122 ? -9.23262  38.43401 -0.02262  1.000 95.70331  ? 141 TYR B CD2 1 
ATOM   1735 C CE1 . TYR B 1 122 ? -7.91652  39.82450 1.96552   1.000 98.09927  ? 141 TYR B CE1 1 
ATOM   1736 C CE2 . TYR B 1 122 ? -9.94386  39.27017 0.81591   1.000 100.89684 ? 141 TYR B CE2 1 
ATOM   1737 C CZ  . TYR B 1 122 ? -9.28232  39.96562 1.80780   1.000 103.37311 ? 141 TYR B CZ  1 
ATOM   1738 O OH  . TYR B 1 122 ? -9.98957  40.79921 2.64695   1.000 99.25039  ? 141 TYR B OH  1 
ATOM   1739 N N   . PRO B 1 123 ? -4.08344  37.81869 -2.45429  1.000 71.72135  ? 142 PRO B N   1 
ATOM   1740 C CA  . PRO B 1 123 ? -2.98994  37.15250 -3.18486  1.000 62.58610  ? 142 PRO B CA  1 
ATOM   1741 C C   . PRO B 1 123 ? -2.87293  35.67082 -2.89492  1.000 60.16215  ? 142 PRO B C   1 
ATOM   1742 O O   . PRO B 1 123 ? -2.45596  34.90518 -3.77399  1.000 59.03638  ? 142 PRO B O   1 
ATOM   1743 C CB  . PRO B 1 123 ? -1.74264  37.90989 -2.70889  1.000 65.88422  ? 142 PRO B CB  1 
ATOM   1744 C CG  . PRO B 1 123 ? -2.25567  39.22982 -2.23874  1.000 75.95039  ? 142 PRO B CG  1 
ATOM   1745 C CD  . PRO B 1 123 ? -3.60028  38.94794 -1.64539  1.000 71.43413  ? 142 PRO B CD  1 
ATOM   1746 N N   . LEU B 1 124 ? -3.19498  35.24862 -1.67643  1.000 55.42889  ? 143 LEU B N   1 
ATOM   1747 C CA  . LEU B 1 124 ? -3.12495  33.85135 -1.27345  1.000 52.97632  ? 143 LEU B CA  1 
ATOM   1748 C C   . LEU B 1 124 ? -4.50928  33.39202 -0.84230  1.000 50.79178  ? 143 LEU B C   1 
ATOM   1749 O O   . LEU B 1 124 ? -5.11753  33.99148 0.04956   1.000 56.08760  ? 143 LEU B O   1 
ATOM   1750 C CB  . LEU B 1 124 ? -2.11588  33.65602 -0.14227  1.000 43.45564  ? 143 LEU B CB  1 
ATOM   1751 C CG  . LEU B 1 124 ? -2.01324  32.22992 0.39621   1.000 46.59446  ? 143 LEU B CG  1 
ATOM   1752 C CD1 . LEU B 1 124 ? -1.60081  31.27756 -0.70825  1.000 50.24763  ? 143 LEU B CD1 1 
ATOM   1753 C CD2 . LEU B 1 124 ? -1.03172  32.17237 1.55159   1.000 52.47172  ? 143 LEU B CD2 1 
ATOM   1754 N N   . LEU B 1 125 ? -5.00584  32.34056 -1.48003  1.000 48.85332  ? 144 LEU B N   1 
ATOM   1755 C CA  . LEU B 1 125 ? -6.25586  31.69907 -1.09668  1.000 48.85573  ? 144 LEU B CA  1 
ATOM   1756 C C   . LEU B 1 125 ? -5.91674  30.38012 -0.41773  1.000 51.13161  ? 144 LEU B C   1 
ATOM   1757 O O   . LEU B 1 125 ? -5.29487  29.50736 -1.03165  1.000 50.78692  ? 144 LEU B O   1 
ATOM   1758 C CB  . LEU B 1 125 ? -7.15184  31.46354 -2.31239  1.000 47.27722  ? 144 LEU B CB  1 
ATOM   1759 C CG  . LEU B 1 125 ? -8.57292  30.98591 -2.00942  1.000 55.55311  ? 144 LEU B CG  1 
ATOM   1760 C CD1 . LEU B 1 125 ? -9.39052  32.09780 -1.36643  1.000 60.03509  ? 144 LEU B CD1 1 
ATOM   1761 C CD2 . LEU B 1 125 ? -9.25054  30.47614 -3.27305  1.000 65.78541  ? 144 LEU B CD2 1 
ATOM   1762 N N   . ILE B 1 126 ? -6.29796  30.24751 0.84770   1.000 47.66402  ? 145 ILE B N   1 
ATOM   1763 C CA  . ILE B 1 126 ? -5.98306  29.06884 1.64560   1.000 47.53216  ? 145 ILE B CA  1 
ATOM   1764 C C   . ILE B 1 126 ? -7.23521  28.20667 1.73813   1.000 46.39529  ? 145 ILE B C   1 
ATOM   1765 O O   . ILE B 1 126 ? -8.20602  28.57082 2.41046   1.000 47.97104  ? 145 ILE B O   1 
ATOM   1766 C CB  . ILE B 1 126 ? -5.46294  29.45432 3.03314   1.000 52.15783  ? 145 ILE B CB  1 
ATOM   1767 C CG1 . ILE B 1 126 ? -4.21743  30.32551 2.88633   1.000 52.41041  ? 145 ILE B CG1 1 
ATOM   1768 C CG2 . ILE B 1 126 ? -5.16778  28.20746 3.85506   1.000 48.00245  ? 145 ILE B CG2 1 
ATOM   1769 C CD1 . ILE B 1 126 ? -3.53559  30.60924 4.17271   1.000 44.83437  ? 145 ILE B CD1 1 
ATOM   1770 N N   . GLY B 1 127 ? -7.20393  27.05288 1.07949   1.000 44.94004  ? 146 GLY B N   1 
ATOM   1771 C CA  . GLY B 1 127 ? -8.34197  26.16434 1.02507   1.000 43.44423  ? 146 GLY B CA  1 
ATOM   1772 C C   . GLY B 1 127 ? -8.43522  25.26070 2.23992   1.000 47.78903  ? 146 GLY B C   1 
ATOM   1773 O O   . GLY B 1 127 ? -7.69996  25.39081 3.21921   1.000 46.96832  ? 146 GLY B O   1 
ATOM   1774 N N   . SER B 1 128 ? -9.38909  24.32783 2.16904   1.000 56.12029  ? 147 SER B N   1 
ATOM   1775 C CA  . SER B 1 128 ? -9.67349  23.46991 3.31551   1.000 45.41121  ? 147 SER B CA  1 
ATOM   1776 C C   . SER B 1 128 ? -8.51742  22.51805 3.60884   1.000 50.02552  ? 147 SER B C   1 
ATOM   1777 O O   . SER B 1 128 ? -8.21624  22.24648 4.77554   1.000 51.19317  ? 147 SER B O   1 
ATOM   1778 C CB  . SER B 1 128 ? -10.97234 22.69715 3.08306   1.000 46.32790  ? 147 SER B CB  1 
ATOM   1779 O OG  . SER B 1 128 ? -10.88960 21.87120 1.93746   1.000 51.50081  ? 147 SER B OG  1 
ATOM   1780 N N   . GLU B 1 129 ? -7.85508  22.00196 2.57060   1.000 46.72201  ? 148 GLU B N   1 
ATOM   1781 C CA  . GLU B 1 129 ? -6.75631  21.06578 2.79544   1.000 49.43240  ? 148 GLU B CA  1 
ATOM   1782 C C   . GLU B 1 129 ? -5.57620  21.74352 3.48247   1.000 49.42050  ? 148 GLU B C   1 
ATOM   1783 O O   . GLU B 1 129 ? -5.00583  21.19658 4.43807   1.000 46.07425  ? 148 GLU B O   1 
ATOM   1784 C CB  . GLU B 1 129 ? -6.33497  20.43201 1.47121   1.000 54.23894  ? 148 GLU B CB  1 
ATOM   1785 C CG  . GLU B 1 129 ? -7.32508  19.37773 0.98937   1.000 56.31371  ? 148 GLU B CG  1 
ATOM   1786 C CD  . GLU B 1 129 ? -7.03247  18.87773 -0.40834  1.000 70.24270  ? 148 GLU B CD  1 
ATOM   1787 O OE1 . GLU B 1 129 ? -7.92763  18.24702 -1.00873  1.000 80.29015  ? 148 GLU B OE1 1 
ATOM   1788 O OE2 . GLU B 1 129 ? -5.91467  19.11575 -0.90953  1.000 87.17047  ? 148 GLU B OE2 1 
ATOM   1789 N N   . ALA B 1 130 ? -5.20553  22.94286 3.02555   1.000 51.79498  ? 149 ALA B N   1 
ATOM   1790 C CA  . ALA B 1 130 ? -4.13689  23.67611 3.69191   1.000 42.86962  ? 149 ALA B CA  1 
ATOM   1791 C C   . ALA B 1 130 ? -4.52504  24.02138 5.12149   1.000 47.66378  ? 149 ALA B C   1 
ATOM   1792 O O   . ALA B 1 130 ? -3.71301  23.87863 6.04350   1.000 49.27284  ? 149 ALA B O   1 
ATOM   1793 C CB  . ALA B 1 130 ? -3.79637  24.94153 2.90607   1.000 51.71186  ? 149 ALA B CB  1 
ATOM   1794 N N   . LEU B 1 131 ? -5.78053  24.43183 5.33072   1.000 45.53997  ? 150 LEU B N   1 
ATOM   1795 C CA  . LEU B 1 131 ? -6.25517  24.72763 6.67858   1.000 38.70723  ? 150 LEU B CA  1 
ATOM   1796 C C   . LEU B 1 131 ? -6.19512  23.50103 7.57780   1.000 47.38360  ? 150 LEU B C   1 
ATOM   1797 O O   . LEU B 1 131 ? -5.94151  23.62971 8.78167   1.000 44.24605  ? 150 LEU B O   1 
ATOM   1798 C CB  . LEU B 1 131 ? -7.67543  25.28997 6.62060   1.000 41.93330  ? 150 LEU B CB  1 
ATOM   1799 C CG  . LEU B 1 131 ? -7.80199  26.68934 6.01269   1.000 45.32196  ? 150 LEU B CG  1 
ATOM   1800 C CD1 . LEU B 1 131 ? -9.25028  27.04207 5.72256   1.000 52.65388  ? 150 LEU B CD1 1 
ATOM   1801 C CD2 . LEU B 1 131 ? -7.18483  27.70989 6.94405   1.000 43.30330  ? 150 LEU B CD2 1 
ATOM   1802 N N   . LYS B 1 132 ? -6.43437  22.30780 7.02444   1.000 45.95610  ? 151 LYS B N   1 
ATOM   1803 C CA  . LYS B 1 132 ? -6.22330  21.09932 7.81156   1.000 48.29059  ? 151 LYS B CA  1 
ATOM   1804 C C   . LYS B 1 132 ? -4.75101  20.93464 8.15136   1.000 52.21875  ? 151 LYS B C   1 
ATOM   1805 O O   . LYS B 1 132 ? -4.40754  20.57952 9.28557   1.000 48.35304  ? 151 LYS B O   1 
ATOM   1806 C CB  . LYS B 1 132 ? -6.73385  19.85817 7.07476   1.000 49.47965  ? 151 LYS B CB  1 
ATOM   1807 C CG  . LYS B 1 132 ? -8.24655  19.75587 6.99481   1.000 63.98050  ? 151 LYS B CG  1 
ATOM   1808 C CD  . LYS B 1 132 ? -8.70794  18.53920 6.19807   1.000 70.19001  ? 151 LYS B CD  1 
ATOM   1809 C CE  . LYS B 1 132 ? -8.01739  18.41045 4.85430   1.000 75.63033  ? 151 LYS B CE  1 
ATOM   1810 N NZ  . LYS B 1 132 ? -8.46508  17.17735 4.14154   1.000 73.47006  ? 151 LYS B NZ  1 
ATOM   1811 N N   . ARG B 1 133 ? -3.86569  21.20136 7.18298   1.000 48.52461  ? 152 ARG B N   1 
ATOM   1812 C CA  . ARG B 1 133 ? -2.43499  21.13750 7.47091   1.000 52.61535  ? 152 ARG B CA  1 
ATOM   1813 C C   . ARG B 1 133 ? -2.03540  22.14820 8.53810   1.000 55.96781  ? 152 ARG B C   1 
ATOM   1814 O O   . ARG B 1 133 ? -1.10252  21.89759 9.30860   1.000 48.35645  ? 152 ARG B O   1 
ATOM   1815 C CB  . ARG B 1 133 ? -1.61492  21.36454 6.19954   1.000 50.98179  ? 152 ARG B CB  1 
ATOM   1816 C CG  . ARG B 1 133 ? -1.70266  20.23831 5.17957   1.000 54.81923  ? 152 ARG B CG  1 
ATOM   1817 C CD  . ARG B 1 133 ? -0.47151  20.23516 4.28454   1.000 56.54868  ? 152 ARG B CD  1 
ATOM   1818 N NE  . ARG B 1 133 ? -0.54442  19.25059 3.21042   1.000 68.67220  ? 152 ARG B NE  1 
ATOM   1819 C CZ  . ARG B 1 133 ? 0.32847   19.16882 2.21431   1.000 72.09622  ? 152 ARG B CZ  1 
ATOM   1820 N NH1 . ARG B 1 133 ? 1.35129   20.00337 2.12227   1.000 66.34408  ? 152 ARG B NH1 1 
ATOM   1821 N NH2 . ARG B 1 133 ? 0.17645   18.22162 1.29221   1.000 66.09604  ? 152 ARG B NH2 1 
ATOM   1822 N N   . PHE B 1 134 ? -2.73347  23.28314 8.61160   1.000 53.10822  ? 153 PHE B N   1 
ATOM   1823 C CA  . PHE B 1 134 ? -2.42833  24.29785 9.61136   1.000 51.96454  ? 153 PHE B CA  1 
ATOM   1824 C C   . PHE B 1 134 ? -3.05310  24.01684 10.97113  1.000 47.80338  ? 153 PHE B C   1 
ATOM   1825 O O   . PHE B 1 134 ? -2.81069  24.78738 11.90684  1.000 54.25423  ? 153 PHE B O   1 
ATOM   1826 C CB  . PHE B 1 134 ? -2.87686  25.67943 9.12530   1.000 51.63803  ? 153 PHE B CB  1 
ATOM   1827 C CG  . PHE B 1 134 ? -1.80851  26.43341 8.39407   1.000 47.43023  ? 153 PHE B CG  1 
ATOM   1828 C CD1 . PHE B 1 134 ? -0.82311  27.10986 9.09510   1.000 51.87101  ? 153 PHE B CD1 1 
ATOM   1829 C CD2 . PHE B 1 134 ? -1.78784  26.47101 7.01049   1.000 49.61457  ? 153 PHE B CD2 1 
ATOM   1830 C CE1 . PHE B 1 134 ? 0.17351   27.80271 8.43077   1.000 53.04772  ? 153 PHE B CE1 1 
ATOM   1831 C CE2 . PHE B 1 134 ? -0.79867  27.16907 6.33895   1.000 58.33192  ? 153 PHE B CE2 1 
ATOM   1832 C CZ  . PHE B 1 134 ? 0.18509   27.83373 7.05111   1.000 53.40201  ? 153 PHE B CZ  1 
ATOM   1833 N N   . ASP B 1 135 ? -3.83262  22.94394 11.10807  1.000 50.57490  ? 154 ASP B N   1 
ATOM   1834 C CA  . ASP B 1 135 ? -4.56404  22.65427 12.34147  1.000 53.14775  ? 154 ASP B CA  1 
ATOM   1835 C C   . ASP B 1 135 ? -5.43199  23.84715 12.73963  1.000 57.18476  ? 154 ASP B C   1 
ATOM   1836 O O   . ASP B 1 135 ? -5.45867  24.27883 13.89423  1.000 59.32597  ? 154 ASP B O   1 
ATOM   1837 C CB  . ASP B 1 135 ? -3.60652  22.27003 13.47113  1.000 60.18065  ? 154 ASP B CB  1 
ATOM   1838 C CG  . ASP B 1 135 ? -2.59716  21.21512 13.05265  1.000 68.01748  ? 154 ASP B CG  1 
ATOM   1839 O OD1 . ASP B 1 135 ? -2.99656  20.21456 12.41906  1.000 71.75017  ? 154 ASP B OD1 1 
ATOM   1840 O OD2 . ASP B 1 135 ? -1.39874  21.39285 13.35518  1.000 73.29456  ? 154 ASP B OD2 1 
ATOM   1841 N N   . ALA B 1 136 ? -6.15058  24.38341 11.76126  1.000 46.50800  ? 155 ALA B N   1 
ATOM   1842 C CA  . ALA B 1 136 ? -6.83538  25.65529 11.91370  1.000 49.95274  ? 155 ALA B CA  1 
ATOM   1843 C C   . ALA B 1 136 ? -8.31952  25.45716 12.19013  1.000 54.14823  ? 155 ALA B C   1 
ATOM   1844 O O   . ALA B 1 136 ? -8.94537  24.51257 11.70493  1.000 49.94649  ? 155 ALA B O   1 
ATOM   1845 C CB  . ALA B 1 136 ? -6.66214  26.51821 10.66161  1.000 44.04046  ? 155 ALA B CB  1 
ATOM   1846 N N   . LEU B 1 137 ? -8.86615  26.36261 12.99455  1.000 59.41579  ? 156 LEU B N   1 
ATOM   1847 C CA  . LEU B 1 137 ? -10.29985 26.56815 13.13577  1.000 50.15103  ? 156 LEU B CA  1 
ATOM   1848 C C   . LEU B 1 137 ? -10.59849 27.97214 12.64138  1.000 53.12148  ? 156 LEU B C   1 
ATOM   1849 O O   . LEU B 1 137 ? -9.99491  28.93889 13.11756  1.000 55.71112  ? 156 LEU B O   1 
ATOM   1850 C CB  . LEU B 1 137 ? -10.76488 26.42219 14.58686  1.000 48.49921  ? 156 LEU B CB  1 
ATOM   1851 C CG  . LEU B 1 137 ? -10.39680 25.17719 15.38620  1.000 60.22496  ? 156 LEU B CG  1 
ATOM   1852 C CD1 . LEU B 1 137 ? -10.99682 25.26168 16.78015  1.000 59.98783  ? 156 LEU B CD1 1 
ATOM   1853 C CD2 . LEU B 1 137 ? -10.88145 23.93133 14.67463  1.000 59.67844  ? 156 LEU B CD2 1 
ATOM   1854 N N   . VAL B 1 138 ? -11.52149 28.09004 11.69712  1.000 54.37298  ? 157 VAL B N   1 
ATOM   1855 C CA  . VAL B 1 138 ? -11.81250 29.37659 11.07875  1.000 50.97764  ? 157 VAL B CA  1 
ATOM   1856 C C   . VAL B 1 138 ? -12.97893 30.02537 11.81304  1.000 53.63176  ? 157 VAL B C   1 
ATOM   1857 O O   . VAL B 1 138 ? -14.09600 29.49758 11.81643  1.000 50.87250  ? 157 VAL B O   1 
ATOM   1858 C CB  . VAL B 1 138 ? -12.11336 29.22148 9.58182   1.000 43.95680  ? 157 VAL B CB  1 
ATOM   1859 C CG1 . VAL B 1 138 ? -12.40942 30.57807 8.96516   1.000 47.13370  ? 157 VAL B CG1 1 
ATOM   1860 C CG2 . VAL B 1 138 ? -10.94032 28.55918 8.87745   1.000 43.65638  ? 157 VAL B CG2 1 
ATOM   1861 N N   . ASP B 1 139 ? -12.71066 31.16738 12.44772  1.000 49.09005  ? 158 ASP B N   1 
ATOM   1862 C CA  . ASP B 1 139 ? -13.74568 31.98190 13.06395  1.000 50.86509  ? 158 ASP B CA  1 
ATOM   1863 C C   . ASP B 1 139 ? -14.15803 33.04100 12.05590  1.000 52.72945  ? 158 ASP B C   1 
ATOM   1864 O O   . ASP B 1 139 ? -13.37339 33.96414 11.78718  1.000 52.49812  ? 158 ASP B O   1 
ATOM   1865 C CB  . ASP B 1 139 ? -13.23198 32.63434 14.33978  1.000 50.25448  ? 158 ASP B CB  1 
ATOM   1866 C CG  . ASP B 1 139 ? -14.33998 33.27875 15.15833  1.000 52.05714  ? 158 ASP B CG  1 
ATOM   1867 O OD1 . ASP B 1 139 ? -15.37642 33.66434 14.57870  1.000 55.53739  ? 158 ASP B OD1 1 
ATOM   1868 O OD2 . ASP B 1 139 ? -14.16923 33.41163 16.38818  1.000 57.13951  ? 158 ASP B OD2 1 
ATOM   1869 N N   . PRO B 1 140 ? -15.35561 32.95645 11.46758  1.000 50.29311  ? 159 PRO B N   1 
ATOM   1870 C CA  . PRO B 1 140 ? -15.76680 33.96384 10.48097  1.000 60.53767  ? 159 PRO B CA  1 
ATOM   1871 C C   . PRO B 1 140 ? -15.98726 35.34715 11.06809  1.000 57.71803  ? 159 PRO B C   1 
ATOM   1872 O O   . PRO B 1 140 ? -16.06712 36.31489 10.30114  1.000 59.67789  ? 159 PRO B O   1 
ATOM   1873 C CB  . PRO B 1 140 ? -17.07487 33.39005 9.91933   1.000 50.32915  ? 159 PRO B CB  1 
ATOM   1874 C CG  . PRO B 1 140 ? -17.58880 32.51340 11.00705  1.000 54.02374  ? 159 PRO B CG  1 
ATOM   1875 C CD  . PRO B 1 140 ? -16.37664 31.91253 11.65145  1.000 51.32206  ? 159 PRO B CD  1 
ATOM   1876 N N   . SER B 1 141 ? -16.09109 35.47810 12.38845  1.000 58.97290  ? 160 SER B N   1 
ATOM   1877 C CA  . SER B 1 141 ? -16.26657 36.78434 13.00481  1.000 58.31287  ? 160 SER B CA  1 
ATOM   1878 C C   . SER B 1 141 ? -14.94645 37.50251 13.25104  1.000 55.73092  ? 160 SER B C   1 
ATOM   1879 O O   . SER B 1 141 ? -14.96223 38.66098 13.68196  1.000 49.81284  ? 160 SER B O   1 
ATOM   1880 C CB  . SER B 1 141 ? -17.04674 36.65212 14.31973  1.000 49.13885  ? 160 SER B CB  1 
ATOM   1881 O OG  . SER B 1 141 ? -16.31231 35.94371 15.30011  1.000 47.89098  ? 160 SER B OG  1 
ATOM   1882 N N   . LEU B 1 142 ? -13.81707 36.85062 12.98207  1.000 49.81443  ? 161 LEU B N   1 
ATOM   1883 C CA  . LEU B 1 142 ? -12.49568 37.41334 13.21140  1.000 56.18232  ? 161 LEU B CA  1 
ATOM   1884 C C   . LEU B 1 142 ? -11.77379 37.66386 11.89311  1.000 54.96036  ? 161 LEU B C   1 
ATOM   1885 O O   . LEU B 1 142 ? -12.02020 36.99117 10.88692  1.000 49.37153  ? 161 LEU B O   1 
ATOM   1886 C CB  . LEU B 1 142 ? -11.64555 36.48357 14.08191  1.000 51.12959  ? 161 LEU B CB  1 
ATOM   1887 C CG  . LEU B 1 142 ? -12.12723 36.22379 15.50863  1.000 58.80465  ? 161 LEU B CG  1 
ATOM   1888 C CD1 . LEU B 1 142 ? -11.17588 35.27368 16.22357  1.000 57.18435  ? 161 LEU B CD1 1 
ATOM   1889 C CD2 . LEU B 1 142 ? -12.25532 37.53467 16.26748  1.000 47.06420  ? 161 LEU B CD2 1 
ATOM   1890 N N   . LYS B 1 143 ? -10.85170 38.62398 11.92540  1.000 56.55565  ? 162 LYS B N   1 
ATOM   1891 C CA  . LYS B 1 143 ? -10.00898 38.95756 10.78580  1.000 55.03275  ? 162 LYS B CA  1 
ATOM   1892 C C   . LYS B 1 143 ? -8.62980  39.32781 11.30860  1.000 52.36689  ? 162 LYS B C   1 
ATOM   1893 O O   . LYS B 1 143 ? -8.51528  40.16508 12.20789  1.000 63.30236  ? 162 LYS B O   1 
ATOM   1894 C CB  . LYS B 1 143 ? -10.60870 40.11034 9.97377   1.000 50.45904  ? 162 LYS B CB  1 
ATOM   1895 C CG  . LYS B 1 143 ? -11.41666 39.64941 8.77708   1.000 49.16888  ? 162 LYS B CG  1 
ATOM   1896 C CD  . LYS B 1 143 ? -11.87308 40.80788 7.91494   1.000 51.50120  ? 162 LYS B CD  1 
ATOM   1897 C CE  . LYS B 1 143 ? -12.57906 40.29762 6.67046   1.000 58.38771  ? 162 LYS B CE  1 
ATOM   1898 N NZ  . LYS B 1 143 ? -13.05030 41.38903 5.77809   1.000 68.76242  ? 162 LYS B NZ  1 
ATOM   1899 N N   . TYR B 1 144 ? -7.59197  38.69279 10.75731  1.000 59.71646  ? 163 TYR B N   1 
ATOM   1900 C CA  . TYR B 1 144 ? -6.20320  38.92873 11.16755  1.000 51.80615  ? 163 TYR B CA  1 
ATOM   1901 C C   . TYR B 1 144 ? -6.02795  38.70993 12.67002  1.000 55.50657  ? 163 TYR B C   1 
ATOM   1902 O O   . TYR B 1 144 ? -5.42438  39.51903 13.37731  1.000 52.92664  ? 163 TYR B O   1 
ATOM   1903 C CB  . TYR B 1 144 ? -5.72169  40.32017 10.74793  1.000 48.26371  ? 163 TYR B CB  1 
ATOM   1904 C CG  . TYR B 1 144 ? -5.94104  40.60729 9.28205   1.000 54.42214  ? 163 TYR B CG  1 
ATOM   1905 C CD1 . TYR B 1 144 ? -5.07944  40.09238 8.32041   1.000 53.73347  ? 163 TYR B CD1 1 
ATOM   1906 C CD2 . TYR B 1 144 ? -7.00788  41.38807 8.85691   1.000 49.37913  ? 163 TYR B CD2 1 
ATOM   1907 C CE1 . TYR B 1 144 ? -5.27615  40.34412 6.97605   1.000 54.35546  ? 163 TYR B CE1 1 
ATOM   1908 C CE2 . TYR B 1 144 ? -7.21219  41.64752 7.51445   1.000 50.76684  ? 163 TYR B CE2 1 
ATOM   1909 C CZ  . TYR B 1 144 ? -6.34408  41.12264 6.57902   1.000 51.53943  ? 163 TYR B CZ  1 
ATOM   1910 O OH  . TYR B 1 144 ? -6.54316  41.37452 5.24146   1.000 59.69400  ? 163 TYR B OH  1 
ATOM   1911 N N   . ALA B 1 145 ? -6.57373  37.59250 13.15762  1.000 55.70808  ? 164 ALA B N   1 
ATOM   1912 C CA  . ALA B 1 145 ? -6.46824  37.26381 14.57392  1.000 53.99785  ? 164 ALA B CA  1 
ATOM   1913 C C   . ALA B 1 145 ? -5.07237  36.79251 14.95836  1.000 55.73866  ? 164 ALA B C   1 
ATOM   1914 O O   . ALA B 1 145 ? -4.69192  36.91243 16.12805  1.000 56.28593  ? 164 ALA B O   1 
ATOM   1915 C CB  . ALA B 1 145 ? -7.49672  36.19258 14.94280  1.000 53.24068  ? 164 ALA B CB  1 
ATOM   1916 N N   . ALA B 1 146 ? -4.30494  36.25793 14.00794  1.000 56.65300  ? 165 ALA B N   1 
ATOM   1917 C CA  . ALA B 1 146 ? -2.96698  35.75847 14.29738  1.000 52.70224  ? 165 ALA B CA  1 
ATOM   1918 C C   . ALA B 1 146 ? -1.90597  36.84932 14.30342  1.000 63.48839  ? 165 ALA B C   1 
ATOM   1919 O O   . ALA B 1 146 ? -0.74898  36.56096 14.63119  1.000 64.95163  ? 165 ALA B O   1 
ATOM   1920 C CB  . ALA B 1 146 ? -2.57741  34.68235 13.28328  1.000 52.32438  ? 165 ALA B CB  1 
ATOM   1921 N N   . GLY B 1 147 ? -2.26043  38.08250 13.95161  1.000 58.29424  ? 166 GLY B N   1 
ATOM   1922 C CA  . GLY B 1 147 ? -1.24536  39.11116 13.89252  1.000 55.55433  ? 166 GLY B CA  1 
ATOM   1923 C C   . GLY B 1 147 ? -0.28189  38.86132 12.74030  1.000 59.09681  ? 166 GLY B C   1 
ATOM   1924 O O   . GLY B 1 147 ? -0.56031  38.11707 11.79737  1.000 62.29798  ? 166 GLY B O   1 
ATOM   1925 N N   . LYS B 1 148 ? 0.88343   39.48756 12.84143  1.000 59.92011  ? 167 LYS B N   1 
ATOM   1926 C CA  . LYS B 1 148 ? 1.88508   39.34490 11.80036  1.000 69.58846  ? 167 LYS B CA  1 
ATOM   1927 C C   . LYS B 1 148 ? 2.54875   37.96927 11.88005  1.000 61.08036  ? 167 LYS B C   1 
ATOM   1928 O O   . LYS B 1 148 ? 2.64696   37.37814 12.95888  1.000 62.46632  ? 167 LYS B O   1 
ATOM   1929 C CB  . LYS B 1 148 ? 2.94048   40.44245 11.91663  1.000 69.17110  ? 167 LYS B CB  1 
ATOM   1930 C CG  . LYS B 1 148 ? 2.41767   41.84427 11.62413  1.000 81.64494  ? 167 LYS B CG  1 
ATOM   1931 C CD  . LYS B 1 148 ? 1.80192   41.92767 10.23339  1.000 78.64834  ? 167 LYS B CD  1 
ATOM   1932 C CE  . LYS B 1 148 ? 1.31976   43.33789 9.91248   1.000 78.11956  ? 167 LYS B CE  1 
ATOM   1933 N NZ  . LYS B 1 148 ? 2.43759   44.32390 9.87777   1.000 86.71997  ? 167 LYS B NZ  1 
ATOM   1934 N N   . PRO B 1 149 ? 2.99745   37.43259 10.74662  1.000 56.60193  ? 168 PRO B N   1 
ATOM   1935 C CA  . PRO B 1 149 ? 3.69761   36.14089 10.77041  1.000 67.10800  ? 168 PRO B CA  1 
ATOM   1936 C C   . PRO B 1 149 ? 4.98499   36.23277 11.57585  1.000 73.06822  ? 168 PRO B C   1 
ATOM   1937 O O   . PRO B 1 149 ? 5.79188   37.14673 11.38800  1.000 76.80899  ? 168 PRO B O   1 
ATOM   1938 C CB  . PRO B 1 149 ? 3.97418   35.86010 9.28885   1.000 59.51427  ? 168 PRO B CB  1 
ATOM   1939 C CG  . PRO B 1 149 ? 2.97703   36.69059 8.54711   1.000 61.49052  ? 168 PRO B CG  1 
ATOM   1940 C CD  . PRO B 1 149 ? 2.78590   37.92355 9.37449   1.000 55.13259  ? 168 PRO B CD  1 
ATOM   1941 N N   . ALA B 1 150 ? 5.16900   35.27832 12.48251  1.000 66.91610  ? 169 ALA B N   1 
ATOM   1942 C CA  . ALA B 1 150 ? 6.32096   35.26371 13.37382  1.000 72.08991  ? 169 ALA B CA  1 
ATOM   1943 C C   . ALA B 1 150 ? 6.75208   33.82057 13.63602  1.000 83.15754  ? 169 ALA B C   1 
ATOM   1944 O O   . ALA B 1 150 ? 6.80666   33.34931 14.77117  1.000 93.48095  ? 169 ALA B O   1 
ATOM   1945 C CB  . ALA B 1 150 ? 6.00160   36.00257 14.67064  1.000 68.22379  ? 169 ALA B CB  1 
ATOM   1946 N N   . CYS B 1 151 ? 7.06914   33.08933 12.57251  1.000 74.82508  ? 170 CYS B N   1 
ATOM   1947 C CA  . CYS B 1 151 ? 7.55386   31.72216 12.71915  1.000 77.39229  ? 170 CYS B CA  1 
ATOM   1948 C C   . CYS B 1 151 ? 9.07463   31.68386 12.77880  1.000 76.61906  ? 170 CYS B C   1 
ATOM   1949 O O   . CYS B 1 151 ? 9.66207   31.75228 13.85915  1.000 94.42858  ? 170 CYS B O   1 
ATOM   1950 C CB  . CYS B 1 151 ? 7.05308   30.84193 11.57321  1.000 84.07134  ? 170 CYS B CB  1 
ATOM   1951 S SG  . CYS B 1 151 ? 5.27636   30.91616 11.28097  1.000 75.86534  ? 170 CYS B SG  1 
HETATM 1952 O O   . HOH C 2 .   ? -26.97425 19.25245 12.77181  1.000 69.79695  ? 201 HOH A O   1 
HETATM 1953 O O   . HOH C 2 .   ? -26.58608 34.48339 5.18703   1.000 54.39726  ? 202 HOH A O   1 
HETATM 1954 O O   . HOH C 2 .   ? -24.14899 17.21058 10.84408  1.000 54.29246  ? 203 HOH A O   1 
HETATM 1955 O O   . HOH C 2 .   ? -12.90314 33.88302 3.77909   1.000 51.81631  ? 204 HOH A O   1 
HETATM 1956 O O   . HOH C 2 .   ? -16.72055 35.08165 3.26583   1.000 49.53071  ? 205 HOH A O   1 
HETATM 1957 O O   . HOH C 2 .   ? -23.89268 27.03815 17.80062  1.000 62.10670  ? 206 HOH A O   1 
HETATM 1958 O O   . HOH C 2 .   ? -25.23493 23.00699 17.72434  1.000 64.37840  ? 207 HOH A O   1 
HETATM 1959 O O   . HOH C 2 .   ? -24.07178 33.31654 5.07202   1.000 48.67402  ? 208 HOH A O   1 
HETATM 1960 O O   . HOH C 2 .   ? -35.74027 20.52441 6.68468   1.000 66.63907  ? 209 HOH A O   1 
HETATM 1961 O O   . HOH C 2 .   ? -27.39002 35.48301 7.23833   1.000 62.02301  ? 210 HOH A O   1 
HETATM 1962 O O   . HOH D 2 .   ? -0.00150  35.86300 10.46114  1.000 55.46758  ? 201 HOH B O   1 
HETATM 1963 O O   . HOH D 2 .   ? 7.01411   22.05149 -5.29379  1.000 48.19919  ? 202 HOH B O   1 
HETATM 1964 O O   . HOH D 2 .   ? -1.85486  26.74222 13.36734  1.000 51.29519  ? 203 HOH B O   1 
HETATM 1965 O O   . HOH D 2 .   ? 6.71965   45.61889 -6.90085  1.000 70.97067  ? 204 HOH B O   1 
HETATM 1966 O O   . HOH D 2 .   ? -2.82915  37.77649 10.33471  1.000 44.74127  ? 205 HOH B O   1 
HETATM 1967 O O   . HOH D 2 .   ? -3.44217  23.25405 -0.44736  1.000 48.18101  ? 206 HOH B O   1 
HETATM 1968 O O   . HOH D 2 .   ? 7.51710   37.75842 -6.46640  1.000 51.71649  ? 207 HOH B O   1 
HETATM 1969 O O   . HOH D 2 .   ? -13.49393 22.73804 0.64136   1.000 50.30001  ? 208 HOH B O   1 
HETATM 1970 O O   . HOH D 2 .   ? -5.84948  24.24237 0.21517   1.000 45.84171  ? 209 HOH B O   1 
HETATM 1971 O O   . HOH D 2 .   ? -10.41280 19.17541 2.30659   1.000 60.67246  ? 210 HOH B O   1 
HETATM 1972 O O   . HOH D 2 .   ? -1.48700  21.61197 1.01411   1.000 63.50181  ? 211 HOH B O   1 
HETATM 1973 O O   . HOH D 2 .   ? -0.19324  30.62571 14.84322  1.000 62.02039  ? 212 HOH B O   1 
HETATM 1974 O O   . HOH D 2 .   ? 8.66443   23.28652 -3.81848  1.000 60.16251  ? 213 HOH B O   1 
HETATM 1975 O O   . HOH D 2 .   ? 7.38226   19.39499 -3.65869  1.000 55.50808  ? 214 HOH B O   1 
HETATM 1976 O O   . HOH D 2 .   ? -4.94157  33.66058 16.88040  1.000 51.15648  ? 215 HOH B O   1 
HETATM 1977 O O   . HOH D 2 .   ? 3.08464   25.32960 14.95347  1.000 55.27492  ? 216 HOH B O   1 
HETATM 1978 O O   . HOH D 2 .   ? -2.60777  19.40747 -0.07593  1.000 55.95634  ? 217 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 4   ? 1.32515 1.55431 0.94323 0.04781  -0.24880 -0.13022 23  GLU A N   
2    C CA  . GLU A 4   ? 1.35003 1.59256 0.97694 0.04001  -0.20859 -0.09479 23  GLU A CA  
3    C C   . GLU A 4   ? 1.20668 1.39361 0.90446 0.02582  -0.20176 -0.06187 23  GLU A C   
4    O O   . GLU A 4   ? 1.13611 1.31622 0.85377 0.02230  -0.17320 -0.04628 23  GLU A O   
5    C CB  . GLU A 4   ? 1.24097 1.50425 0.85642 0.05980  -0.18388 -0.13366 23  GLU A CB  
6    N N   . LYS A 5   ? 1.16479 1.31822 0.90118 0.01827  -0.22849 -0.05369 24  LYS A N   
7    C CA  . LYS A 5   ? 1.10655 1.21634 0.91113 0.00746  -0.22085 -0.02798 24  LYS A CA  
8    C C   . LYS A 5   ? 1.01418 1.13279 0.82416 -0.00458 -0.20823 0.02202  24  LYS A C   
9    O O   . LYS A 5   ? 1.05907 1.19041 0.86399 -0.01036 -0.23002 0.04744  24  LYS A O   
10   C CB  . LYS A 5   ? 1.03696 1.12117 0.88947 0.00314  -0.25213 -0.03699 24  LYS A CB  
11   C CG  . LYS A 5   ? 1.02276 1.07689 0.89310 0.00928  -0.26381 -0.08017 24  LYS A CG  
12   C CD  . LYS A 5   ? 1.03585 1.05700 0.93286 0.01000  -0.23379 -0.07898 24  LYS A CD  
13   C CE  . LYS A 5   ? 1.07809 1.06565 0.98244 0.01864  -0.24764 -0.11942 24  LYS A CE  
14   N NZ  . LYS A 5   ? 1.00853 0.96975 0.95929 0.00709  -0.28127 -0.13059 24  LYS A NZ  
15   N N   . THR A 6   ? 0.92813 1.03649 0.75000 -0.00796 -0.17773 0.03570  25  THR A N   
16   C CA  . THR A 6   ? 0.93780 1.04496 0.76927 -0.01983 -0.16695 0.07872  25  THR A CA  
17   C C   . THR A 6   ? 0.82895 0.89271 0.72460 -0.02127 -0.16119 0.08769  25  THR A C   
18   O O   . THR A 6   ? 0.78649 0.82787 0.70616 -0.01663 -0.14859 0.06566  25  THR A O   
19   C CB  . THR A 6   ? 0.90262 1.03265 0.70634 -0.02451 -0.13922 0.08490  25  THR A CB  
20   O OG1 . THR A 6   ? 1.07675 1.25893 0.82333 -0.01948 -0.13836 0.06877  25  THR A OG1 
21   C CG2 . THR A 6   ? 0.80228 0.92796 0.61563 -0.04126 -0.13445 0.13150  25  THR A CG2 
22   N N   . VAL A 7   ? 0.75830 0.81157 0.68068 -0.02644 -0.17077 0.12032  26  VAL A N   
23   C CA  . VAL A 7   ? 0.70236 0.72284 0.68755 -0.02330 -0.16452 0.12457  26  VAL A CA  
24   C C   . VAL A 7   ? 0.75078 0.75099 0.73993 -0.02744 -0.14071 0.13419  26  VAL A C   
25   O O   . VAL A 7   ? 0.87868 0.88196 0.84898 -0.03686 -0.14317 0.16076  26  VAL A O   
26   C CB  . VAL A 7   ? 0.76262 0.78119 0.78618 -0.02063 -0.19232 0.14836  26  VAL A CB  
27   C CG1 . VAL A 7   ? 0.68601 0.67840 0.77809 -0.01280 -0.18148 0.14870  26  VAL A CG1 
28   C CG2 . VAL A 7   ? 0.66682 0.70657 0.69404 -0.01774 -0.22048 0.13499  26  VAL A CG2 
29   N N   . TYR A 8   ? 0.69725 0.67731 0.70928 -0.02275 -0.11951 0.11403  27  TYR A N   
30   C CA  . TYR A 8   ? 0.68802 0.64479 0.70946 -0.02445 -0.10104 0.11594  27  TYR A CA  
31   C C   . TYR A 8   ? 0.70530 0.64056 0.77863 -0.01431 -0.09370 0.10757  27  TYR A C   
32   O O   . TYR A 8   ? 0.63111 0.57584 0.73583 -0.00848 -0.09926 0.10195  27  TYR A O   
33   C CB  . TYR A 8   ? 0.66534 0.62535 0.65538 -0.02609 -0.08150 0.09638  27  TYR A CB  
34   C CG  . TYR A 8   ? 0.71708 0.70993 0.66296 -0.03148 -0.08351 0.09700  27  TYR A CG  
35   C CD1 . TYR A 8   ? 0.78449 0.79216 0.71480 -0.04397 -0.08065 0.11672  27  TYR A CD1 
36   C CD2 . TYR A 8   ? 0.75961 0.77122 0.68355 -0.02411 -0.08798 0.07609  27  TYR A CD2 
37   C CE1 . TYR A 8   ? 0.82308 0.87530 0.71632 -0.04833 -0.07683 0.11629  27  TYR A CE1 
38   C CE2 . TYR A 8   ? 0.73328 0.78233 0.61827 -0.02367 -0.08714 0.06928  27  TYR A CE2 
39   C CZ  . TYR A 8   ? 0.90295 0.97814 0.77227 -0.03542 -0.07882 0.08971  27  TYR A CZ  
40   O OH  . TYR A 8   ? 0.79963 0.92599 0.63331 -0.03445 -0.07266 0.08204  27  TYR A OH  
41   N N   . GLY A 9   ? 0.78327 0.69417 0.86774 -0.01223 -0.08067 0.10365  28  GLY A N   
42   C CA  . GLY A 9   ? 0.57671 0.47317 0.70612 0.00100  -0.06969 0.09020  28  GLY A CA  
43   C C   . GLY A 9   ? 0.56207 0.45566 0.67601 0.00358  -0.04206 0.06577  28  GLY A C   
44   O O   . GLY A 9   ? 0.60927 0.50842 0.68292 -0.00383 -0.03522 0.06052  28  GLY A O   
45   N N   . LEU A 10  ? 0.57597 0.46310 0.72245 0.01647  -0.02687 0.05029  29  LEU A N   
46   C CA  . LEU A 10  ? 0.59100 0.47802 0.71451 0.01889  0.00022  0.02946  29  LEU A CA  
47   C C   . LEU A 10  ? 0.71054 0.57617 0.78704 0.01226  0.00006  0.02261  29  LEU A C   
48   O O   . LEU A 10  ? 0.67778 0.54622 0.71637 0.00880  0.01298  0.01394  29  LEU A O   
49   C CB  . LEU A 10  ? 0.54219 0.43362 0.70465 0.03653  0.01885  0.00986  29  LEU A CB  
50   C CG  . LEU A 10  ? 0.77875 0.70652 0.99595 0.04341  0.02879  0.01145  29  LEU A CG  
51   C CD1 . LEU A 10  ? 0.53730 0.47777 0.79366 0.06527  0.05142  -0.01381 29  LEU A CD1 
52   C CD2 . LEU A 10  ? 0.66373 0.61399 0.86057 0.02798  0.04296  0.01922  29  LEU A CD2 
53   N N   . ASN A 11  ? 0.73967 0.58384 0.82200 0.00897  -0.01706 0.02888  30  ASN A N   
54   C CA  . ASN A 11  ? 0.71945 0.54794 0.76963 -0.00115 -0.02104 0.02380  30  ASN A CA  
55   C C   . ASN A 11  ? 0.73659 0.56769 0.78548 -0.01766 -0.04137 0.05091  30  ASN A C   
56   O O   . ASN A 11  ? 0.75943 0.58429 0.83631 -0.01862 -0.05676 0.07144  30  ASN A O   
57   C CB  . ASN A 11  ? 0.72278 0.51937 0.78565 0.00790  -0.02002 -0.00014 30  ASN A CB  
58   C CG  . ASN A 11  ? 0.75334 0.55769 0.80638 0.02439  0.00517  -0.02904 30  ASN A CG  
59   O OD1 . ASN A 11  ? 0.82490 0.63091 0.91429 0.04176  0.01434  -0.04195 30  ASN A OD1 
60   N ND2 . ASN A 11  ? 0.80893 0.62282 0.81338 0.01970  0.01664  -0.03793 30  ASN A ND2 
61   N N   . GLU A 12  ? 0.72653 0.57212 0.74350 -0.03041 -0.04136 0.05287  31  GLU A N   
62   C CA  . GLU A 12  ? 0.73936 0.60092 0.75278 -0.04877 -0.05414 0.07868  31  GLU A CA  
63   C C   . GLU A 12  ? 0.86070 0.72359 0.86381 -0.06208 -0.05509 0.07165  31  GLU A C   
64   O O   . GLU A 12  ? 0.78574 0.63815 0.77609 -0.05497 -0.04868 0.04578  31  GLU A O   
65   C CB  . GLU A 12  ? 0.70605 0.60882 0.69648 -0.04971 -0.05259 0.08918  31  GLU A CB  
66   C CG  . GLU A 12  ? 0.73274 0.63846 0.73533 -0.04040 -0.05857 0.09703  31  GLU A CG  
67   C CD  . GLU A 12  ? 0.77572 0.67226 0.79959 -0.04739 -0.07707 0.12696  31  GLU A CD  
68   O OE1 . GLU A 12  ? 0.80008 0.69484 0.82153 -0.06443 -0.08431 0.14858  31  GLU A OE1 
69   O OE2 . GLU A 12  ? 0.82560 0.71763 0.87224 -0.03719 -0.08658 0.13193  31  GLU A OE2 
70   N N   . TYR A 13  ? 0.75677 0.63656 0.76619 -0.08342 -0.06424 0.09701  32  TYR A N   
71   C CA  . TYR A 13  ? 0.80719 0.70482 0.81539 -0.10007 -0.06575 0.09395  32  TYR A CA  
72   C C   . TYR A 13  ? 0.80395 0.76262 0.78911 -0.10031 -0.05516 0.09615  32  TYR A C   
73   O O   . TYR A 13  ? 0.91656 0.90702 0.89211 -0.10296 -0.05221 0.11592  32  TYR A O   
74   C CB  . TYR A 13  ? 0.84916 0.73136 0.88868 -0.12766 -0.08153 0.12199  32  TYR A CB  
75   C CG  . TYR A 13  ? 0.78475 0.60034 0.85121 -0.12391 -0.09615 0.10591  32  TYR A CG  
76   C CD1 . TYR A 13  ? 0.82653 0.62206 0.88692 -0.11545 -0.09672 0.06716  32  TYR A CD1 
77   C CD2 . TYR A 13  ? 0.84001 0.61244 0.93613 -0.12524 -0.11165 0.12638  32  TYR A CD2 
78   C CE1 . TYR A 13  ? 0.83437 0.57118 0.91498 -0.10777 -0.10966 0.04353  32  TYR A CE1 
79   C CE2 . TYR A 13  ? 0.82558 0.53543 0.95082 -0.11583 -0.12623 0.10401  32  TYR A CE2 
80   C CZ  . TYR A 13  ? 0.82253 0.51612 0.93849 -0.10660 -0.12371 0.05960  32  TYR A CZ  
81   O OH  . TYR A 13  ? 1.08753 0.72108 1.22849 -0.09374 -0.13798 0.02923  32  TYR A OH  
82   N N   . ALA A 14  ? 0.74844 0.72349 0.72343 -0.09420 -0.05156 0.07294  33  ALA A N   
83   C CA  . ALA A 14  ? 0.82694 0.85850 0.78858 -0.08845 -0.04400 0.06759  33  ALA A CA  
84   C C   . ALA A 14  ? 0.88246 0.94986 0.86411 -0.10420 -0.04801 0.06618  33  ALA A C   
85   O O   . ALA A 14  ? 0.76901 0.80767 0.76598 -0.11470 -0.05944 0.05912  33  ALA A O   
86   C CB  . ALA A 14  ? 0.77424 0.79493 0.71146 -0.06196 -0.04040 0.04212  33  ALA A CB  
87   N N   . ALA A 15  ? 0.75622 0.89130 0.74073 -0.10519 -0.03932 0.07008  34  ALA A N   
88   C CA  . ALA A 15  ? 0.76823 0.95738 0.78149 -0.11840 -0.04073 0.06823  34  ALA A CA  
89   C C   . ALA A 15  ? 0.84448 1.08096 0.85117 -0.09109 -0.03610 0.04228  34  ALA A C   
90   O O   . ALA A 15  ? 0.77583 1.03327 0.76184 -0.07201 -0.02610 0.03567  34  ALA A O   
91   C CB  . ALA A 15  ? 0.73904 0.98256 0.77694 -0.15053 -0.03212 0.10302  34  ALA A CB  
92   N N   . LEU A 16  ? 0.80440 1.05438 0.83044 -0.08748 -0.04777 0.02535  35  LEU A N   
93   C CA  . LEU A 16  ? 0.74413 1.04572 0.77818 -0.06136 -0.04822 0.00258  35  LEU A CA  
94   C C   . LEU A 16  ? 0.69990 1.09955 0.77278 -0.07526 -0.03329 0.01191  35  LEU A C   
95   O O   . LEU A 16  ? 0.85175 1.28352 0.96455 -0.10515 -0.03670 0.02654  35  LEU A O   
96   C CB  . LEU A 16  ? 0.76579 1.04661 0.80545 -0.05071 -0.07089 -0.01630 35  LEU A CB  
97   C CG  . LEU A 16  ? 0.95486 1.15264 0.95075 -0.03531 -0.08330 -0.02590 35  LEU A CG  
98   C CD1 . LEU A 16  ? 0.89892 1.03618 0.87922 -0.05582 -0.08312 -0.01588 35  LEU A CD1 
99   C CD2 . LEU A 16  ? 0.83059 1.03071 0.82848 -0.02101 -0.10704 -0.04262 35  LEU A CD2 
100  N N   . ASP A 17  ? 0.65404 1.10291 0.71548 -0.05589 -0.01610 0.00357  36  ASP A N   
101  C CA  . ASP A 17  ? 0.71429 1.26855 0.80414 -0.06731 0.00590  0.01210  36  ASP A CA  
102  C C   . ASP A 17  ? 0.65952 1.28196 0.81016 -0.07509 0.00086  0.00572  36  ASP A C   
103  O O   . ASP A 17  ? 0.62239 1.24076 0.78828 -0.04707 -0.01691 -0.02296 36  ASP A O   
104  C CB  . ASP A 17  ? 0.72436 1.32146 0.79122 -0.03081 0.01991  -0.01530 36  ASP A CB  
105  C CG  . ASP A 17  ? 0.85311 1.57473 0.94627 -0.03583 0.04748  -0.01438 36  ASP A CG  
106  O OD1 . ASP A 17  ? 0.90043 1.66114 0.99586 -0.07472 0.06462  0.02425  36  ASP A OD1 
107  O OD2 . ASP A 17  ? 0.68683 1.46940 0.80051 -0.00045 0.05205  -0.05141 36  ASP A OD2 
108  N N   . GLY A 18  ? 0.53380 1.22054 0.72260 -0.11528 0.01419  0.03606  37  GLY A N   
109  C CA  . GLY A 18  ? 0.63930 1.39531 0.89695 -0.13264 0.00808  0.03590  37  GLY A CA  
110  C C   . GLY A 18  ? 0.67322 1.36350 0.95196 -0.16684 -0.01990 0.05135  37  GLY A C   
111  O O   . GLY A 18  ? 0.56261 1.30819 0.90328 -0.20143 -0.02424 0.06661  37  GLY A O   
112  N N   . ILE A 19  ? 0.62021 1.19736 0.85168 -0.15735 -0.03936 0.04449  38  ILE A N   
113  C CA  . ILE A 19  ? 0.76238 1.26756 1.00311 -0.18171 -0.06742 0.04817  38  ILE A CA  
114  C C   . ILE A 19  ? 0.63380 1.08088 0.85993 -0.21367 -0.06333 0.08169  38  ILE A C   
115  O O   . ILE A 19  ? 0.78236 1.18853 0.96120 -0.19944 -0.05100 0.08857  38  ILE A O   
116  C CB  . ILE A 19  ? 0.67453 1.10068 0.87165 -0.14768 -0.09009 0.01608  38  ILE A CB  
117  C CG1 . ILE A 19  ? 0.82758 1.30647 1.03840 -0.11274 -0.09798 -0.01160 38  ILE A CG1 
118  C CG2 . ILE A 19  ? 0.72322 1.08559 0.92549 -0.16907 -0.11910 0.01100  38  ILE A CG2 
119  C CD1 . ILE A 19  ? 0.79838 1.20496 0.95598 -0.07661 -0.11495 -0.03401 38  ILE A CD1 
120  N N   . ASN A 20  ? 0.77769 1.21868 1.04975 -0.25685 -0.07799 0.10252  39  ASN A N   
121  C CA  . ASN A 20  ? 0.79436 1.17359 1.06468 -0.28917 -0.08160 0.13707  39  ASN A CA  
122  C C   . ASN A 20  ? 0.85735 1.12454 1.10770 -0.28156 -0.11058 0.11325  39  ASN A C   
123  O O   . ASN A 20  ? 0.98878 1.21674 1.27529 -0.31088 -0.13629 0.11484  39  ASN A O   
124  C CB  . ASN A 20  ? 0.91901 1.35290 1.25566 -0.34367 -0.08199 0.17756  39  ASN A CB  
125  C CG  . ASN A 20  ? 0.98543 1.35436 1.32274 -0.37772 -0.08821 0.22154  39  ASN A CG  
126  O OD1 . ASN A 20  ? 0.97723 1.28762 1.26459 -0.35787 -0.08327 0.22692  39  ASN A OD1 
127  N ND2 . ASN A 20  ? 1.05864 1.43672 1.45858 -0.43009 -0.10248 0.25493  39  ASN A ND2 
128  N N   . LEU A 21  ? 0.80128 1.01977 0.99408 -0.24100 -0.10589 0.08840  40  LEU A N   
129  C CA  . LEU A 21  ? 0.81992 0.94551 0.98404 -0.22600 -0.12498 0.06115  40  LEU A CA  
130  C C   . LEU A 21  ? 0.87596 0.95148 0.99619 -0.20340 -0.11020 0.06593  40  LEU A C   
131  O O   . LEU A 21  ? 0.79786 0.90479 0.89020 -0.18143 -0.09020 0.06833  40  LEU A O   
132  C CB  . LEU A 21  ? 0.74426 0.87042 0.88451 -0.19836 -0.13739 0.02104  40  LEU A CB  
133  C CG  . LEU A 21  ? 0.89677 1.05404 1.07933 -0.21771 -0.16404 0.00697  40  LEU A CG  
134  C CD1 . LEU A 21  ? 0.81366 0.95655 0.95732 -0.18683 -0.18097 -0.03010 40  LEU A CD1 
135  C CD2 . LEU A 21  ? 0.94196 1.04841 1.16006 -0.25383 -0.18802 0.01084  40  LEU A CD2 
136  N N   . GLU A 22  ? 0.95485 0.95397 1.07494 -0.20786 -0.12253 0.06452  41  GLU A N   
137  C CA  . GLU A 22  ? 0.93855 0.89142 1.02786 -0.18529 -0.11185 0.06589  41  GLU A CA  
138  C C   . GLU A 22  ? 0.94675 0.87029 0.99401 -0.15125 -0.10918 0.02643  41  GLU A C   
139  O O   . GLU A 22  ? 1.09540 0.98572 1.13832 -0.14905 -0.12499 -0.00267 41  GLU A O   
140  C CB  . GLU A 22  ? 1.05104 0.93675 1.16635 -0.19995 -0.12753 0.07934  41  GLU A CB  
141  C CG  . GLU A 22  ? 1.19133 1.08991 1.35054 -0.24041 -0.13664 0.12484  41  GLU A CG  
142  C CD  . GLU A 22  ? 1.33573 1.15002 1.52639 -0.25188 -0.16188 0.13106  41  GLU A CD  
143  O OE1 . GLU A 22  ? 1.37967 1.13534 1.56278 -0.22940 -0.17319 0.08846  41  GLU A OE1 
144  O OE2 . GLU A 22  ? 1.46208 1.26825 1.68375 -0.28176 -0.17094 0.17801  41  GLU A OE2 
145  N N   . VAL A 23  ? 0.79645 0.73296 0.81123 -0.12671 -0.09052 0.02599  42  VAL A N   
146  C CA  . VAL A 23  ? 0.88121 0.79204 0.85640 -0.09883 -0.08490 -0.00173 42  VAL A CA  
147  C C   . VAL A 23  ? 0.93127 0.80799 0.89958 -0.08511 -0.07286 0.00268  42  VAL A C   
148  O O   . VAL A 23  ? 0.82444 0.71762 0.80078 -0.08652 -0.06509 0.02609  42  VAL A O   
149  C CB  . VAL A 23  ? 0.85693 0.80957 0.80784 -0.08266 -0.07774 -0.00639 42  VAL A CB  
150  C CG1 . VAL A 23  ? 0.87280 0.79594 0.78153 -0.05969 -0.07347 -0.02610 42  VAL A CG1 
151  C CG2 . VAL A 23  ? 0.94360 0.94058 0.91414 -0.09401 -0.09134 -0.01029 42  VAL A CG2 
152  N N   . ALA A 24  ? 0.86361 0.69961 0.81690 -0.07068 -0.07141 -0.02168 43  ALA A N   
153  C CA  . ALA A 24  ? 0.81905 0.63342 0.77293 -0.05443 -0.05780 -0.02162 43  ALA A CA  
154  C C   . ALA A 24  ? 0.78653 0.62231 0.70889 -0.03865 -0.04061 -0.02203 43  ALA A C   
155  O O   . ALA A 24  ? 0.90980 0.74762 0.79793 -0.03072 -0.03766 -0.03772 43  ALA A O   
156  C CB  . ALA A 24  ? 0.84288 0.61391 0.79891 -0.04341 -0.05990 -0.05135 43  ALA A CB  
157  N N   . ALA A 25  ? 0.84433 0.69317 0.77782 -0.03550 -0.03297 -0.00331 44  ALA A N   
158  C CA  . ALA A 25  ? 0.78175 0.64582 0.69509 -0.02468 -0.02161 -0.00124 44  ALA A CA  
159  C C   . ALA A 25  ? 0.79866 0.65049 0.72630 -0.01463 -0.00878 -0.00192 44  ALA A C   
160  O O   . ALA A 25  ? 0.83615 0.68211 0.79651 -0.01529 -0.01270 0.00720  44  ALA A O   
161  C CB  . ALA A 25  ? 0.82323 0.71852 0.73971 -0.02890 -0.02642 0.01498  44  ALA A CB  
162  N N   . LYS A 26  ? 0.89386 0.74514 0.79995 -0.00625 0.00551  -0.00986 45  LYS A N   
163  C CA  . LYS A 26  ? 0.77745 0.63184 0.70234 0.00086  0.02174  -0.00818 45  LYS A CA  
164  C C   . LYS A 26  ? 0.77588 0.64401 0.70334 -0.00280 0.02001  0.00820  45  LYS A C   
165  O O   . LYS A 26  ? 0.73485 0.60210 0.63295 -0.00418 0.01860  0.01087  45  LYS A O   
166  C CB  . LYS A 26  ? 0.75607 0.60791 0.65522 0.00849  0.04172  -0.02430 45  LYS A CB  
167  C CG  . LYS A 26  ? 0.81018 0.67938 0.73263 0.01351  0.06451  -0.02094 45  LYS A CG  
168  C CD  . LYS A 26  ? 0.84856 0.72564 0.73493 0.01971  0.08889  -0.03551 45  LYS A CD  
169  C CE  . LYS A 26  ? 0.81035 0.71651 0.73375 0.02684  0.11682  -0.03831 45  LYS A CE  
170  N NZ  . LYS A 26  ? 0.89892 0.82482 0.77929 0.03148  0.14656  -0.05005 45  LYS A NZ  
171  N N   . LEU A 27  ? 0.78477 0.66203 0.74873 -0.00349 0.01553  0.01803  46  LEU A N   
172  C CA  . LEU A 27  ? 0.69296 0.58017 0.66347 -0.00739 0.00804  0.02819  46  LEU A CA  
173  C C   . LEU A 27  ? 0.67817 0.56968 0.66474 -0.00892 0.02431  0.03168  46  LEU A C   
174  O O   . LEU A 27  ? 0.69503 0.59979 0.72171 -0.00650 0.03328  0.03238  46  LEU A O   
175  C CB  . LEU A 27  ? 0.65151 0.55014 0.64842 -0.00893 -0.00869 0.03682  46  LEU A CB  
176  C CG  . LEU A 27  ? 0.70241 0.60908 0.67793 -0.01256 -0.02332 0.04052  46  LEU A CG  
177  C CD1 . LEU A 27  ? 0.71882 0.61655 0.69091 -0.01581 -0.02211 0.04104  46  LEU A CD1 
178  C CD2 . LEU A 27  ? 0.70786 0.63087 0.69678 -0.01478 -0.03983 0.05171  46  LEU A CD2 
179  N N   . ASP A 28  ? 0.64696 0.52970 0.60690 -0.01350 0.02714  0.03636  47  ASP A N   
180  C CA  . ASP A 28  ? 0.66636 0.55348 0.63139 -0.02048 0.04643  0.04654  47  ASP A CA  
181  C C   . ASP A 28  ? 0.65886 0.53759 0.64043 -0.03135 0.03185  0.05975  47  ASP A C   
182  O O   . ASP A 28  ? 0.72014 0.57550 0.67262 -0.03250 0.01872  0.06385  47  ASP A O   
183  C CB  . ASP A 28  ? 0.68381 0.56076 0.59651 -0.01907 0.05904  0.04607  47  ASP A CB  
184  C CG  . ASP A 28  ? 0.71516 0.60380 0.62355 -0.02879 0.08417  0.06188  47  ASP A CG  
185  O OD1 . ASP A 28  ? 0.79917 0.70518 0.75392 -0.03895 0.09214  0.07407  47  ASP A OD1 
186  O OD2 . ASP A 28  ? 0.81258 0.69709 0.67028 -0.02801 0.09536  0.06382  47  ASP A OD2 
187  N N   . THR A 29  ? 0.61262 0.50860 0.64593 -0.03836 0.03046  0.06469  48  THR A N   
188  C CA  . THR A 29  ? 0.57264 0.45795 0.63012 -0.05154 0.01277  0.07414  48  THR A CA  
189  C C   . THR A 29  ? 0.63140 0.50944 0.68933 -0.06875 0.02813  0.09661  48  THR A C   
190  O O   . THR A 29  ? 0.76875 0.62485 0.84387 -0.08240 0.00955  0.10707  48  THR A O   
191  C CB  . THR A 29  ? 0.58298 0.49274 0.69960 -0.05566 0.00160  0.07211  48  THR A CB  
192  O OG1 . THR A 29  ? 0.51467 0.45945 0.67360 -0.05907 0.02848  0.07945  48  THR A OG1 
193  C CG2 . THR A 29  ? 0.48684 0.40212 0.59511 -0.04123 -0.01637 0.05779  48  THR A CG2 
194  N N   . GLY A 30  ? 0.62205 0.51785 0.66126 -0.06953 0.06043  0.10459  49  GLY A N   
195  C CA  . GLY A 30  ? 0.65460 0.54873 0.68232 -0.08828 0.07828  0.13253  49  GLY A CA  
196  C C   . GLY A 30  ? 0.76295 0.61435 0.72875 -0.08777 0.06504  0.14420  49  GLY A C   
197  O O   . GLY A 30  ? 0.77538 0.61368 0.73100 -0.10664 0.07016  0.17539  49  GLY A O   
198  N N   . ALA A 31  ? 0.74440 0.57621 0.67278 -0.06780 0.04682  0.12318  50  ALA A N   
199  C CA  . ALA A 31  ? 0.86193 0.65711 0.74033 -0.06221 0.02817  0.13041  50  ALA A CA  
200  C C   . ALA A 31  ? 0.81793 0.58281 0.71299 -0.05338 -0.00891 0.11750  50  ALA A C   
201  O O   . ALA A 31  ? 0.75597 0.53533 0.67389 -0.04359 -0.01799 0.09333  50  ALA A O   
202  C CB  . ALA A 31  ? 0.80764 0.61153 0.63588 -0.04547 0.03430  0.11331  50  ALA A CB  
203  N N   . LYS A 32  ? 0.81095 0.53405 0.69276 -0.05543 -0.03123 0.13347  51  LYS A N   
204  C CA  . LYS A 32  ? 0.80266 0.49607 0.70128 -0.04169 -0.06727 0.11422  51  LYS A CA  
205  C C   . LYS A 32  ? 0.86667 0.56863 0.73590 -0.01504 -0.07859 0.08866  51  LYS A C   
206  O O   . LYS A 32  ? 0.81031 0.52765 0.69459 -0.00044 -0.09010 0.05929  51  LYS A O   
207  C CB  . LYS A 32  ? 0.82204 0.46021 0.72812 -0.05183 -0.09197 0.13936  51  LYS A CB  
208  C CG  . LYS A 32  ? 0.94211 0.57336 0.89119 -0.08353 -0.08514 0.16596  51  LYS A CG  
209  C CD  . LYS A 32  ? 0.99400 0.56032 0.95546 -0.09681 -0.11562 0.19402  51  LYS A CD  
210  C CE  . LYS A 32  ? 1.25521 0.77693 1.22792 -0.06993 -0.16036 0.15959  51  LYS A CE  
211  N NZ  . LYS A 32  ? 1.25188 0.79134 1.26371 -0.06326 -0.17148 0.11817  51  LYS A NZ  
212  N N   . THR A 33  ? 0.96402 0.66275 0.79142 -0.00978 -0.07530 0.10001  52  THR A N   
213  C CA  . THR A 33  ? 0.93437 0.64401 0.74261 0.01320  -0.08984 0.07875  52  THR A CA  
214  C C   . THR A 33  ? 0.96089 0.71417 0.75643 0.01402  -0.06820 0.06356  52  THR A C   
215  O O   . THR A 33  ? 1.00011 0.76687 0.78732 0.00094  -0.04279 0.07165  52  THR A O   
216  C CB  . THR A 33  ? 1.01063 0.68988 0.78410 0.01962  -0.10812 0.09911  52  THR A CB  
217  O OG1 . THR A 33  ? 1.06137 0.74325 0.79551 0.00204  -0.08564 0.12679  52  THR A OG1 
218  C CG2 . THR A 33  ? 0.96438 0.58979 0.75764 0.02130  -0.13765 0.11377  52  THR A CG2 
219  N N   . ALA A 34  ? 0.94349 0.72012 0.74283 0.02982  -0.07920 0.04028  53  ALA A N   
220  C CA  . ALA A 34  ? 0.80130 0.61349 0.59550 0.02816  -0.06565 0.02737  53  ALA A CA  
221  C C   . ALA A 34  ? 0.95836 0.77160 0.71849 0.03241  -0.07265 0.02879  53  ALA A C   
222  O O   . ALA A 34  ? 0.93226 0.72971 0.67917 0.04374  -0.09437 0.03451  53  ALA A O   
223  C CB  . ALA A 34  ? 0.73629 0.58250 0.55708 0.03682  -0.07159 0.00606  53  ALA A CB  
224  N N   . SER A 35  ? 0.86167 0.69121 0.60955 0.02457  -0.05852 0.02178  54  SER A N   
225  C CA  . SER A 35  ? 0.83991 0.67134 0.55221 0.02652  -0.06711 0.01807  54  SER A CA  
226  C C   . SER A 35  ? 0.96575 0.82549 0.69572 0.02310  -0.06881 -0.00264 54  SER A C   
227  O O   . SER A 35  ? 0.84196 0.71015 0.59643 0.01457  -0.05394 -0.00843 54  SER A O   
228  C CB  . SER A 35  ? 0.90493 0.72058 0.57347 0.01828  -0.04933 0.02869  54  SER A CB  
229  O OG  . SER A 35  ? 1.22673 1.01768 0.87598 0.01624  -0.04992 0.05599  54  SER A OG  
230  N N   . LEU A 36  ? 0.88320 0.75622 0.60419 0.02828  -0.09025 -0.01109 55  LEU A N   
231  C CA  . LEU A 36  ? 0.74855 0.64823 0.49068 0.02025  -0.09677 -0.02829 55  LEU A CA  
232  C C   . LEU A 36  ? 0.83962 0.73034 0.54090 0.01911  -0.11127 -0.03792 55  LEU A C   
233  O O   . LEU A 36  ? 0.94520 0.83268 0.61856 0.02964  -0.13194 -0.03207 55  LEU A O   
234  C CB  . LEU A 36  ? 0.76566 0.70651 0.55070 0.02606  -0.11174 -0.03328 55  LEU A CB  
235  C CG  . LEU A 36  ? 0.85844 0.83467 0.67627 0.01136  -0.11833 -0.04482 55  LEU A CG  
236  C CD1 . LEU A 36  ? 0.81493 0.78791 0.65357 -0.00628 -0.09836 -0.04142 55  LEU A CD1 
237  C CD2 . LEU A 36  ? 0.71550 0.74649 0.57617 0.01892  -0.13115 -0.04921 55  LEU A CD2 
238  N N   . SER A 37  ? 0.85702 0.74085 0.55365 0.00795  -0.10408 -0.05389 56  SER A N   
239  C CA  . SER A 37  ? 1.07329 0.94860 0.72745 0.00717  -0.11989 -0.07156 56  SER A CA  
240  C C   . SER A 37  ? 1.05956 0.96375 0.74248 0.00295  -0.15224 -0.08240 56  SER A C   
241  O O   . SER A 37  ? 0.97366 0.89859 0.71166 -0.01035 -0.15408 -0.08786 56  SER A O   
242  C CB  . SER A 37  ? 1.00736 0.86289 0.65412 0.00013  -0.10435 -0.09288 56  SER A CB  
243  O OG  . SER A 37  ? 1.21467 1.05990 0.80738 0.00289  -0.11799 -0.11568 56  SER A OG  
244  N N   . ALA A 38  ? 1.00694 0.91590 0.65537 0.01263  -0.17888 -0.08219 57  ALA A N   
245  C CA  . ALA A 38  ? 1.01156 0.95665 0.69469 0.01122  -0.21305 -0.09135 57  ALA A CA  
246  C C   . ALA A 38  ? 1.00820 0.94450 0.64089 0.01029  -0.24274 -0.11042 57  ALA A C   
247  O O   . ALA A 38  ? 1.12166 1.02714 0.68059 0.01590  -0.23635 -0.11192 57  ALA A O   
248  C CB  . ALA A 38  ? 1.00004 0.96849 0.70500 0.02995  -0.22693 -0.07367 57  ALA A CB  
249  N N   . ARG A 39  ? 0.99353 0.96339 0.66708 0.00211  -0.27546 -0.12558 58  ARG A N   
250  C CA  . ARG A 39  ? 1.11092 1.07864 0.74393 0.00040  -0.31324 -0.14767 58  ARG A CA  
251  C C   . ARG A 39  ? 1.14681 1.16152 0.81907 0.00794  -0.35426 -0.14348 58  ARG A C   
252  O O   . ARG A 39  ? 1.10489 1.16455 0.85826 0.00566  -0.35211 -0.13597 58  ARG A O   
253  C CB  . ARG A 39  ? 1.17986 1.13700 0.83339 -0.02269 -0.31942 -0.18061 58  ARG A CB  
254  C CG  . ARG A 39  ? 1.13317 1.12390 0.88728 -0.04497 -0.31712 -0.17767 58  ARG A CG  
255  C CD  . ARG A 39  ? 1.16321 1.14320 0.94633 -0.07109 -0.34128 -0.20817 58  ARG A CD  
256  N NE  . ARG A 39  ? 1.20424 1.12631 0.95359 -0.07376 -0.32090 -0.22690 58  ARG A NE  
257  C CZ  . ARG A 39  ? 1.37554 1.26000 1.06400 -0.06900 -0.33711 -0.26381 58  ARG A CZ  
258  N NH1 . ARG A 39  ? 1.31559 1.21128 0.96267 -0.06456 -0.37681 -0.28432 58  ARG A NH1 
259  N NH2 . ARG A 39  ? 1.36241 1.19966 1.03100 -0.06637 -0.31462 -0.28320 58  ARG A NH2 
260  N N   . ASP A 40  ? 1.24477 1.25409 0.85820 0.01833  -0.39177 -0.14894 59  ASP A N   
261  C CA  . ASP A 40  ? 1.29040 1.34429 0.93849 0.02843  -0.43986 -0.14759 59  ASP A CA  
262  C C   . ASP A 40  ? 1.26228 1.34204 0.96200 0.05026  -0.43335 -0.12044 59  ASP A C   
263  O O   . ASP A 40  ? 1.12998 1.26830 0.91952 0.05149  -0.44412 -0.12442 59  ASP A O   
264  C CB  . ASP A 40  ? 1.33330 1.43184 1.05863 0.00447  -0.46573 -0.17525 59  ASP A CB  
265  C CG  . ASP A 40  ? 1.50916 1.57548 1.19186 -0.01630 -0.47058 -0.20503 59  ASP A CG  
266  O OD1 . ASP A 40  ? 1.64625 1.69131 1.25091 -0.00787 -0.47973 -0.20774 59  ASP A OD1 
267  O OD2 . ASP A 40  ? 1.46770 1.52955 1.19614 -0.04101 -0.46531 -0.22550 59  ASP A OD2 
268  N N   . ILE A 41  ? 1.22124 1.25805 0.86487 0.06750  -0.41500 -0.09429 60  ILE A N   
269  C CA  . ILE A 41  ? 1.15089 1.19560 0.83469 0.09116  -0.41138 -0.07210 60  ILE A CA  
270  C C   . ILE A 41  ? 1.21170 1.27616 0.90294 0.11571  -0.46480 -0.06404 60  ILE A C   
271  O O   . ILE A 41  ? 1.32495 1.35905 0.94859 0.11759  -0.47906 -0.04743 60  ILE A O   
272  C CB  . ILE A 41  ? 1.25633 1.24222 0.88317 0.09673  -0.37874 -0.04557 60  ILE A CB  
273  C CG1 . ILE A 41  ? 1.12890 1.10281 0.76257 0.07556  -0.32838 -0.05425 60  ILE A CG1 
274  C CG2 . ILE A 41  ? 1.20767 1.19021 0.87323 0.12302  -0.38512 -0.02632 60  ILE A CG2 
275  C CD1 . ILE A 41  ? 1.05427 0.97852 0.64035 0.07702  -0.29610 -0.03012 60  ILE A CD1 
276  N N   . LYS A 42  ? 1.19281 1.31580 0.97844 0.13069  -0.47922 -0.07262 61  LYS A N   
277  C CA  . LYS A 42  ? 1.17084 1.31938 0.99109 0.15325  -0.51483 -0.06408 61  LYS A CA  
278  C C   . LYS A 42  ? 1.17514 1.32901 1.04962 0.18648  -0.51156 -0.05651 61  LYS A C   
279  O O   . LYS A 42  ? 1.12584 1.33435 1.07794 0.19204  -0.49520 -0.07640 61  LYS A O   
280  C CB  . LYS A 42  ? 1.06008 1.28487 0.95488 0.14124  -0.53704 -0.08765 61  LYS A CB  
281  N N   . ARG A 43  ? 1.21878 1.31746 1.05338 0.20759  -0.52633 -0.02862 62  ARG A N   
282  C CA  . ARG A 43  ? 1.20151 1.29340 1.08854 0.24183  -0.53034 -0.02463 62  ARG A CA  
283  C C   . ARG A 43  ? 1.13460 1.28250 1.09843 0.26598  -0.56312 -0.03547 62  ARG A C   
284  O O   . ARG A 43  ? 1.25164 1.40637 1.19541 0.26091  -0.59326 -0.02615 62  ARG A O   
285  C CB  . ARG A 43  ? 1.28743 1.28853 1.10441 0.24921  -0.53384 0.01304  62  ARG A CB  
286  C CG  . ARG A 43  ? 1.38239 1.35280 1.23724 0.27315  -0.52297 0.01253  62  ARG A CG  
287  C CD  . ARG A 43  ? 1.47526 1.35228 1.26154 0.26926  -0.52448 0.05458  62  ARG A CD  
288  N NE  . ARG A 43  ? 1.46659 1.31032 1.16557 0.23512  -0.49720 0.07397  62  ARG A NE  
289  C CZ  . ARG A 43  ? 1.54408 1.31946 1.17796 0.22150  -0.48813 0.11345  62  ARG A CZ  
290  N NH1 . ARG A 43  ? 1.54650 1.30462 1.10590 0.19161  -0.45814 0.12672  62  ARG A NH1 
291  N NH2 . ARG A 43  ? 1.61976 1.34589 1.26824 0.23704  -0.50803 0.13958  62  ARG A NH2 
292  N N   . PHE A 44  ? 1.16830 1.36141 1.22020 0.29307  -0.55612 -0.05767 63  PHE A N   
293  C CA  . PHE A 44  ? 1.27601 1.52706 1.40881 0.31995  -0.58312 -0.07085 63  PHE A CA  
294  C C   . PHE A 44  ? 1.18854 1.43763 1.38000 0.35976  -0.57628 -0.08618 63  PHE A C   
295  O O   . PHE A 44  ? 1.20005 1.39678 1.36488 0.36456  -0.55525 -0.08427 63  PHE A O   
296  C CB  . PHE A 44  ? 1.10551 1.46165 1.30927 0.30185  -0.57812 -0.09677 63  PHE A CB  
297  C CG  . PHE A 44  ? 1.00127 1.42274 1.26288 0.29417  -0.53560 -0.12324 63  PHE A CG  
298  C CD1 . PHE A 44  ? 1.06970 1.47831 1.28834 0.26017  -0.50730 -0.12261 63  PHE A CD1 
299  C CD2 . PHE A 44  ? 0.96234 1.46383 1.32070 0.32045  -0.52263 -0.14902 63  PHE A CD2 
300  C CE1 . PHE A 44  ? 0.98124 1.45533 1.25196 0.25089  -0.46886 -0.14269 63  PHE A CE1 
301  C CE2 . PHE A 44  ? 0.92697 1.49859 1.33299 0.31110  -0.47943 -0.17062 63  PHE A CE2 
302  C CZ  . PHE A 44  ? 0.97254 1.53134 1.33497 0.27513  -0.45346 -0.16515 63  PHE A CZ  
303  N N   . LYS A 45  ? 1.08825 1.39318 1.35994 0.38898  -0.59581 -0.10358 64  LYS A N   
304  C CA  . LYS A 45  ? 1.14101 1.45032 1.47384 0.43063  -0.59163 -0.12697 64  LYS A CA  
305  C C   . LYS A 45  ? 1.10001 1.53244 1.53355 0.44085  -0.56766 -0.16766 64  LYS A C   
306  O O   . LYS A 45  ? 1.15545 1.66387 1.63678 0.43202  -0.58024 -0.17130 64  LYS A O   
307  C CB  . LYS A 45  ? 1.18743 1.44614 1.52555 0.46213  -0.63753 -0.11087 64  LYS A CB  
308  C CG  . LYS A 45  ? 1.30200 1.43723 1.55082 0.45660  -0.65565 -0.06920 64  LYS A CG  
309  C CD  . LYS A 45  ? 1.44778 1.52456 1.68425 0.46362  -0.62972 -0.07792 64  LYS A CD  
310  C CE  . LYS A 45  ? 1.47726 1.43596 1.65151 0.46319  -0.65368 -0.03628 64  LYS A CE  
311  N NZ  . LYS A 45  ? 1.44545 1.35962 1.52275 0.42509  -0.65740 0.01167  64  LYS A NZ  
312  N N   . ARG A 46  ? 1.08842 1.54361 1.55304 0.45762  -0.53250 -0.19746 65  ARG A N   
313  C CA  . ARG A 46  ? 1.03949 1.61525 1.59496 0.46985  -0.50251 -0.23611 65  ARG A CA  
314  C C   . ARG A 46  ? 1.09436 1.65616 1.68323 0.51701  -0.49874 -0.26838 65  ARG A C   
315  O O   . ARG A 46  ? 1.14758 1.64110 1.69320 0.52393  -0.48605 -0.27391 65  ARG A O   
316  C CB  . ARG A 46  ? 1.05056 1.69020 1.60540 0.43564  -0.45338 -0.24470 65  ARG A CB  
317  C CG  . ARG A 46  ? 0.92462 1.69044 1.56478 0.44623  -0.41460 -0.28067 65  ARG A CG  
318  C CD  . ARG A 46  ? 0.84411 1.68658 1.48985 0.40216  -0.36992 -0.27800 65  ARG A CD  
319  N NE  . ARG A 46  ? 0.77627 1.63200 1.41790 0.35759  -0.38675 -0.25053 65  ARG A NE  
320  C CZ  . ARG A 46  ? 0.81368 1.71222 1.45208 0.31058  -0.35932 -0.23983 65  ARG A CZ  
321  N NH1 . ARG A 46  ? 0.92446 1.86208 1.56015 0.30053  -0.31167 -0.24866 65  ARG A NH1 
322  N NH2 . ARG A 46  ? 0.81261 1.71138 1.44768 0.27135  -0.38199 -0.21974 65  ARG A NH2 
323  N N   . ASN A 47  ? 1.16010 1.78270 1.82570 0.54905  -0.51306 -0.29065 66  ASN A N   
324  C CA  . ASN A 47  ? 1.19545 1.80841 1.89863 0.59704  -0.51437 -0.32763 66  ASN A CA  
325  C C   . ASN A 47  ? 1.31720 1.78584 1.95916 0.61241  -0.54720 -0.31097 66  ASN A C   
326  O O   . ASN A 47  ? 1.34621 1.77512 1.98551 0.63608  -0.53876 -0.33887 66  ASN A O   
327  C CB  . ASN A 47  ? 1.18146 1.86867 1.90601 0.60037  -0.45903 -0.36879 66  ASN A CB  
328  C CG  . ASN A 47  ? 1.14483 1.97729 1.92935 0.57784  -0.42192 -0.37781 66  ASN A CG  
329  O OD1 . ASN A 47  ? 1.06033 1.93086 1.86582 0.55212  -0.43716 -0.35178 66  ASN A OD1 
330  N ND2 . ASN A 47  ? 1.20203 2.11606 2.01139 0.58366  -0.37340 -0.41291 66  ASN A ND2 
331  N N   . GLY A 48  ? 1.30945 1.70000 1.89921 0.59512  -0.58506 -0.26361 67  GLY A N   
332  C CA  . GLY A 48  ? 1.35725 1.61388 1.88834 0.60131  -0.61704 -0.23574 67  GLY A CA  
333  C C   . GLY A 48  ? 1.37443 1.55273 1.82494 0.57069  -0.59618 -0.21468 67  GLY A C   
334  O O   . GLY A 48  ? 1.43933 1.50812 1.83383 0.56376  -0.62165 -0.17870 67  GLY A O   
335  N N   . GLU A 49  ? 1.32725 1.55984 1.77156 0.55058  -0.55083 -0.23261 68  GLU A N   
336  C CA  . GLU A 49  ? 1.36111 1.52554 1.73445 0.52293  -0.53101 -0.21396 68  GLU A CA  
337  C C   . GLU A 49  ? 1.30155 1.46874 1.61893 0.48015  -0.52640 -0.17547 68  GLU A C   
338  O O   . GLU A 49  ? 1.22657 1.48078 1.57233 0.46699  -0.51954 -0.18024 68  GLU A O   
339  C CB  . GLU A 49  ? 1.24933 1.46236 1.64160 0.52785  -0.48666 -0.25608 68  GLU A CB  
340  C CG  . GLU A 49  ? 1.27528 1.61677 1.70342 0.51286  -0.44746 -0.27577 68  GLU A CG  
341  C CD  . GLU A 49  ? 1.32323 1.76411 1.82667 0.54413  -0.42653 -0.32657 68  GLU A CD  
342  O OE1 . GLU A 49  ? 1.34657 1.75298 1.87393 0.58126  -0.44589 -0.35151 68  GLU A OE1 
343  O OE2 . GLU A 49  ? 1.23041 1.78499 1.76855 0.52924  -0.39042 -0.34028 68  GLU A OE2 
344  N N   . SER A 50  ? 1.35146 1.42274 1.59013 0.45653  -0.53120 -0.13758 69  SER A N   
345  C CA  . SER A 50  ? 1.24566 1.31017 1.41907 0.41621  -0.52551 -0.10412 69  SER A CA  
346  C C   . SER A 50  ? 1.21070 1.34795 1.39320 0.39541  -0.48498 -0.12541 69  SER A C   
347  O O   . SER A 50  ? 1.29275 1.42889 1.48022 0.39941  -0.45762 -0.14386 69  SER A O   
348  C CB  . SER A 50  ? 1.22108 1.17282 1.30911 0.39563  -0.53245 -0.05985 69  SER A CB  
349  O OG  . SER A 50  ? 1.39541 1.28153 1.47342 0.40939  -0.56965 -0.03317 69  SER A OG  
350  N N   . TRP A 51  ? 1.14760 1.34778 1.33308 0.37132  -0.48342 -0.12257 70  TRP A N   
351  C CA  . TRP A 51  ? 1.11500 1.38368 1.30848 0.34295  -0.45015 -0.13577 70  TRP A CA  
352  C C   . TRP A 51  ? 1.08957 1.31924 1.20706 0.30158  -0.45400 -0.10697 70  TRP A C   
353  O O   . TRP A 51  ? 1.19921 1.37683 1.26925 0.30015  -0.48594 -0.08203 70  TRP A O   
354  C CB  . TRP A 51  ? 0.95433 1.34697 1.23874 0.34597  -0.43939 -0.16507 70  TRP A CB  
355  C CG  . TRP A 51  ? 0.89791 1.35626 1.24726 0.37233  -0.40912 -0.20063 70  TRP A CG  
356  C CD1 . TRP A 51  ? 0.92386 1.36091 1.30028 0.41440  -0.41594 -0.22109 70  TRP A CD1 
357  C CD2 . TRP A 51  ? 0.85132 1.41005 1.24226 0.35594  -0.36550 -0.22092 70  TRP A CD2 
358  N NE1 . TRP A 51  ? 0.90132 1.41920 1.32661 0.42749  -0.37772 -0.25752 70  TRP A NE1 
359  C CE2 . TRP A 51  ? 0.86118 1.45816 1.29496 0.39120  -0.34436 -0.25464 70  TRP A CE2 
360  C CE3 . TRP A 51  ? 0.81613 1.41594 1.19746 0.30346  -0.33236 -0.20771 70  TRP A CE3 
361  C CZ2 . TRP A 51  ? 0.80988 1.50756 1.28041 0.38359  -0.29681 -0.27723 70  TRP A CZ2 
362  C CZ3 . TRP A 51  ? 0.72768 1.41589 1.14739 0.29056  -0.28506 -0.22274 70  TRP A CZ3 
363  C CH2 . TRP A 51  ? 0.71342 1.45774 1.17606 0.33166  -0.26753 -0.25697 70  TRP A CH2 
364  N N   . VAL A 52  ? 0.92506 1.17573 1.02688 0.26145  -0.41068 -0.10941 71  VAL A N   
365  C CA  . VAL A 52  ? 0.92750 1.14403 0.96269 0.22215  -0.40744 -0.09146 71  VAL A CA  
366  C C   . VAL A 52  ? 0.97205 1.26204 1.04952 0.18890  -0.38240 -0.10706 71  VAL A C   
367  O O   . VAL A 52  ? 0.87041 1.21278 0.99681 0.18450  -0.34782 -0.12005 71  VAL A O   
368  C CB  . VAL A 52  ? 0.93404 1.06131 0.88726 0.20494  -0.38074 -0.06924 71  VAL A CB  
369  C CG1 . VAL A 52  ? 0.78170 0.92379 0.75271 0.18927  -0.33122 -0.07950 71  VAL A CG1 
370  C CG2 . VAL A 52  ? 1.11820 1.20744 0.99647 0.17573  -0.38491 -0.05397 71  VAL A CG2 
371  N N   . ARG A 53  ? 0.93292 1.22715 0.99127 0.16487  -0.40307 -0.10530 72  ARG A N   
372  C CA  . ARG A 53  ? 0.95554 1.30323 1.05183 0.12731  -0.38707 -0.11623 72  ARG A CA  
373  C C   . ARG A 53  ? 0.88703 1.16642 0.90386 0.09661  -0.38276 -0.10909 72  ARG A C   
374  O O   . ARG A 53  ? 0.95933 1.19141 0.91143 0.10265  -0.41302 -0.10327 72  ARG A O   
375  C CB  . ARG A 53  ? 0.87617 1.30929 1.04998 0.12894  -0.42372 -0.13084 72  ARG A CB  
376  C CG  . ARG A 53  ? 0.86177 1.34807 1.08325 0.08421  -0.41491 -0.13882 72  ARG A CG  
377  C CD  . ARG A 53  ? 1.06745 1.65549 1.38680 0.08766  -0.44853 -0.15266 72  ARG A CD  
378  N NE  . ARG A 53  ? 1.10964 1.75441 1.48953 0.04031  -0.44236 -0.15680 72  ARG A NE  
379  C CZ  . ARG A 53  ? 1.11589 1.74153 1.48416 0.01022  -0.47634 -0.16346 72  ARG A CZ  
380  N NH1 . ARG A 53  ? 0.85813 1.53183 1.29219 -0.03524 -0.47313 -0.16573 72  ARG A NH1 
381  N NH2 . ARG A 53  ? 1.17285 1.72411 1.45689 0.02341  -0.50998 -0.16425 72  ARG A NH2 
382  N N   . PHE A 54  ? 0.78259 1.05776 0.80227 0.06607  -0.34561 -0.10968 73  PHE A N   
383  C CA  . PHE A 54  ? 0.94267 1.15044 0.89220 0.04306  -0.33536 -0.10769 73  PHE A CA  
384  C C   . PHE A 54  ? 0.87854 1.10467 0.86746 0.00764  -0.30934 -0.11196 73  PHE A C   
385  O O   . PHE A 54  ? 0.86466 1.15154 0.92247 -0.00038 -0.29178 -0.10904 73  PHE A O   
386  C CB  . PHE A 54  ? 0.81404 0.95201 0.69365 0.05687  -0.31145 -0.09170 73  PHE A CB  
387  C CG  . PHE A 54  ? 0.81512 0.95953 0.72264 0.05729  -0.27174 -0.08490 73  PHE A CG  
388  C CD1 . PHE A 54  ? 0.68308 0.86192 0.63276 0.08267  -0.27033 -0.08492 73  PHE A CD1 
389  C CD2 . PHE A 54  ? 0.83020 0.94710 0.72237 0.03489  -0.23899 -0.08159 73  PHE A CD2 
390  C CE1 . PHE A 54  ? 0.71210 0.89903 0.67995 0.08382  -0.23668 -0.08318 73  PHE A CE1 
391  C CE2 . PHE A 54  ? 0.71902 0.84378 0.63237 0.03519  -0.20734 -0.07450 73  PHE A CE2 
392  C CZ  . PHE A 54  ? 0.85778 1.01828 0.80500 0.05868  -0.20598 -0.07601 73  PHE A CZ  
393  N N   . TYR A 55  ? 0.89048 1.06297 0.83307 -0.01253 -0.30685 -0.11819 74  TYR A N   
394  C CA  . TYR A 55  ? 0.92331 1.08988 0.89443 -0.04448 -0.28535 -0.11890 74  TYR A CA  
395  C C   . TYR A 55  ? 0.89289 0.99229 0.80623 -0.04176 -0.25392 -0.11269 74  TYR A C   
396  O O   . TYR A 55  ? 0.90689 0.96171 0.75121 -0.02325 -0.25364 -0.11342 74  TYR A O   
397  C CB  . TYR A 55  ? 0.91762 1.08013 0.90322 -0.07126 -0.31699 -0.13929 74  TYR A CB  
398  C CG  . TYR A 55  ? 0.98117 1.21247 1.02656 -0.07559 -0.35478 -0.14747 74  TYR A CG  
399  C CD1 . TYR A 55  ? 0.93064 1.23291 1.07116 -0.10193 -0.35202 -0.14030 74  TYR A CD1 
400  C CD2 . TYR A 55  ? 1.05617 1.28681 1.06486 -0.05435 -0.39404 -0.15950 74  TYR A CD2 
401  C CE1 . TYR A 55  ? 0.82750 1.20361 1.03431 -0.10653 -0.38588 -0.14829 74  TYR A CE1 
402  C CE2 . TYR A 55  ? 0.98200 1.28019 1.05283 -0.05634 -0.43302 -0.16773 74  TYR A CE2 
403  C CZ  . TYR A 55  ? 0.94476 1.31827 1.11932 -0.08223 -0.42806 -0.16381 74  TYR A CZ  
404  O OH  . TYR A 55  ? 0.92235 1.37385 1.17020 -0.08493 -0.46601 -0.17245 74  TYR A OH  
405  N N   . LEU A 56  ? 0.85163 0.94851 0.79612 -0.06120 -0.22787 -0.10339 75  LEU A N   
406  C CA  . LEU A 56  ? 0.75458 0.79152 0.65730 -0.06056 -0.20308 -0.10086 75  LEU A CA  
407  C C   . LEU A 56  ? 0.98398 0.97099 0.84443 -0.06553 -0.21913 -0.12564 75  LEU A C   
408  O O   . LEU A 56  ? 1.00517 0.99935 0.88563 -0.08151 -0.24865 -0.14376 75  LEU A O   
409  C CB  . LEU A 56  ? 0.69603 0.74025 0.64423 -0.08117 -0.18030 -0.08423 75  LEU A CB  
410  C CG  . LEU A 56  ? 0.82658 0.92233 0.80523 -0.07506 -0.15976 -0.06352 75  LEU A CG  
411  C CD1 . LEU A 56  ? 0.88297 0.98133 0.89105 -0.09671 -0.13906 -0.04311 75  LEU A CD1 
412  C CD2 . LEU A 56  ? 0.67509 0.75167 0.60925 -0.04436 -0.14750 -0.06146 75  LEU A CD2 
413  N N   . ALA A 57  ? 0.97490 0.91509 0.77803 -0.05134 -0.19971 -0.12919 76  ALA A N   
414  C CA  . ALA A 57  ? 1.03951 0.93736 0.79457 -0.05031 -0.20916 -0.15868 76  ALA A CA  
415  C C   . ALA A 57  ? 0.98730 0.86311 0.78664 -0.07293 -0.21937 -0.17694 76  ALA A C   
416  O O   . ALA A 57  ? 1.11276 0.96202 0.88954 -0.07606 -0.24234 -0.21087 76  ALA A O   
417  C CB  . ALA A 57  ? 1.12059 0.98590 0.81844 -0.03204 -0.17798 -0.15670 76  ALA A CB  
418  N N   . ILE A 58  ? 0.90018 0.78330 0.76010 -0.08903 -0.20548 -0.15490 77  ILE A N   
419  C CA  . ILE A 58  ? 0.94156 0.79657 0.84972 -0.11369 -0.21908 -0.16405 77  ILE A CA  
420  C C   . ILE A 58  ? 1.00945 0.89659 0.96858 -0.14114 -0.25381 -0.16761 77  ILE A C   
421  O O   . ILE A 58  ? 1.06575 0.92019 1.05369 -0.16204 -0.27948 -0.18743 77  ILE A O   
422  C CB  . ILE A 58  ? 0.86752 0.71840 0.81756 -0.12314 -0.19456 -0.13176 77  ILE A CB  
423  C CG1 . ILE A 58  ? 1.02120 0.82852 1.01985 -0.14774 -0.21171 -0.13624 77  ILE A CG1 
424  C CG2 . ILE A 58  ? 0.73080 0.64710 0.71787 -0.13371 -0.18479 -0.09634 77  ILE A CG2 
425  C CD1 . ILE A 58  ? 1.00316 0.80344 1.03977 -0.15825 -0.19342 -0.09889 77  ILE A CD1 
426  N N   . ASP A 59  ? 0.93688 0.88868 0.91460 -0.14114 -0.25731 -0.15075 78  ASP A N   
427  C CA  . ASP A 59  ? 0.89610 0.89677 0.93554 -0.16744 -0.28761 -0.15096 78  ASP A CA  
428  C C   . ASP A 59  ? 1.04526 1.03510 1.04956 -0.16055 -0.32729 -0.18834 78  ASP A C   
429  O O   . ASP A 59  ? 1.07777 1.11036 1.06860 -0.14540 -0.34242 -0.19005 78  ASP A O   
430  C CB  . ASP A 59  ? 0.86154 0.94391 0.93926 -0.16403 -0.27360 -0.12297 78  ASP A CB  
431  C CG  . ASP A 59  ? 0.94043 1.09020 1.09779 -0.19335 -0.29868 -0.11939 78  ASP A CG  
432  O OD1 . ASP A 59  ? 1.01224 1.13985 1.20280 -0.22379 -0.32721 -0.13248 78  ASP A OD1 
433  O OD2 . ASP A 59  ? 0.95722 1.18438 1.14939 -0.18560 -0.29074 -0.10550 78  ASP A OD2 
434  N N   . ALA A 60  ? 0.99850 0.92864 0.98778 -0.17029 -0.34812 -0.22081 79  ALA A N   
435  C CA  . ALA A 60  ? 1.08975 1.00711 1.03765 -0.16477 -0.38936 -0.26211 79  ALA A CA  
436  C C   . ALA A 60  ? 1.12932 1.09956 1.14897 -0.19343 -0.43156 -0.26439 79  ALA A C   
437  O O   . ALA A 60  ? 1.08865 1.08080 1.07983 -0.18364 -0.46634 -0.28554 79  ALA A O   
438  C CB  . ALA A 60  ? 1.14393 0.98359 1.05715 -0.16425 -0.40046 -0.30470 79  ALA A CB  
439  N N   . ALA A 61  ? 1.02258 1.01735 1.13640 -0.23042 -0.43061 -0.24056 80  ALA A N   
440  C CA  . ALA A 61  ? 1.02517 1.07956 1.22335 -0.26409 -0.46774 -0.23926 80  ALA A CA  
441  C C   . ALA A 61  ? 1.00824 1.16174 1.24113 -0.25334 -0.45926 -0.21338 80  ALA A C   
442  O O   . ALA A 61  ? 1.04866 1.26907 1.36141 -0.27901 -0.48724 -0.21094 80  ALA A O   
443  C CB  . ALA A 61  ? 0.98465 1.03241 1.27327 -0.31195 -0.46596 -0.21618 80  ALA A CB  
444  N N   . HIS A 62  ? 0.92896 1.09470 1.11176 -0.21619 -0.42337 -0.19607 81  HIS A N   
445  C CA  . HIS A 62  ? 0.93492 1.18773 1.15093 -0.19843 -0.41530 -0.17667 81  HIS A CA  
446  C C   . HIS A 62  ? 0.85843 1.19249 1.18002 -0.23100 -0.39767 -0.14711 81  HIS A C   
447  O O   . HIS A 62  ? 0.91357 1.33597 1.30584 -0.23736 -0.41417 -0.14473 81  HIS A O   
448  C CB  . HIS A 62  ? 0.96625 1.25061 1.17461 -0.18301 -0.46373 -0.20008 81  HIS A CB  
449  C CG  . HIS A 62  ? 1.07793 1.30409 1.17396 -0.14460 -0.47297 -0.21644 81  HIS A CG  
450  N ND1 . HIS A 62  ? 1.06972 1.31973 1.13847 -0.12124 -0.51194 -0.22716 81  HIS A ND1 
451  C CD2 . HIS A 62  ? 1.02303 1.17370 1.02864 -0.12682 -0.44705 -0.21962 81  HIS A CD2 
452  C CE1 . HIS A 62  ? 1.09710 1.28621 1.05710 -0.09349 -0.50632 -0.23162 81  HIS A CE1 
453  N NE2 . HIS A 62  ? 1.07550 1.20780 0.99821 -0.09667 -0.46815 -0.22986 81  HIS A NE2 
454  N N   . SER A 63  ? 0.87118 1.17993 1.20437 -0.25195 -0.36385 -0.12282 82  SER A N   
455  C CA  . SER A 63  ? 0.94299 1.32713 1.36619 -0.28830 -0.34355 -0.08839 82  SER A CA  
456  C C   . SER A 63  ? 0.83524 1.29268 1.26323 -0.26333 -0.30055 -0.06595 82  SER A C   
457  O O   . SER A 63  ? 0.91757 1.47468 1.42278 -0.28259 -0.28693 -0.04610 82  SER A O   
458  C CB  . SER A 63  ? 0.93825 1.26011 1.37219 -0.32518 -0.33254 -0.06723 82  SER A CB  
459  O OG  . SER A 63  ? 0.91002 1.17476 1.36450 -0.35477 -0.37643 -0.08966 82  SER A OG  
460  N N   . HIS A 64  ? 0.86825 1.28237 1.21824 -0.22154 -0.27894 -0.07059 83  HIS A N   
461  C CA  . HIS A 64  ? 0.86001 1.32823 1.20657 -0.19481 -0.24118 -0.05601 83  HIS A CA  
462  C C   . HIS A 64  ? 0.84562 1.30505 1.14433 -0.14413 -0.25202 -0.07808 83  HIS A C   
463  O O   . HIS A 64  ? 0.85608 1.24846 1.08172 -0.11758 -0.23976 -0.08047 83  HIS A O   
464  C CB  . HIS A 64  ? 0.78002 1.20068 1.08685 -0.19871 -0.20509 -0.03350 83  HIS A CB  
465  C CG  . HIS A 64  ? 0.84135 1.26428 1.19361 -0.24833 -0.19781 -0.00410 83  HIS A CG  
466  N ND1 . HIS A 64  ? 0.83861 1.18239 1.18913 -0.27549 -0.22173 -0.00700 83  HIS A ND1 
467  C CD2 . HIS A 64  ? 0.85153 1.34537 1.25179 -0.27617 -0.17083 0.03048  83  HIS A CD2 
468  C CE1 . HIS A 64  ? 0.74135 1.09916 1.14142 -0.31910 -0.21324 0.02792  83  HIS A CE1 
469  N NE2 . HIS A 64  ? 0.79317 1.24459 1.22094 -0.32227 -0.18091 0.05439  83  HIS A NE2 
470  N N   . PRO A 65  ? 0.82235 1.34870 1.16576 -0.13080 -0.27755 -0.09188 84  PRO A N   
471  C CA  . PRO A 65  ? 0.65776 1.17583 0.96264 -0.08143 -0.29174 -0.10691 84  PRO A CA  
472  C C   . PRO A 65  ? 0.70383 1.24093 0.99782 -0.05054 -0.25533 -0.10006 84  PRO A C   
473  O O   . PRO A 65  ? 0.69567 1.30730 1.04134 -0.05937 -0.22546 -0.09084 84  PRO A O   
474  C CB  . PRO A 65  ? 0.71405 1.31760 1.09348 -0.07761 -0.32727 -0.12001 84  PRO A CB  
475  C CG  . PRO A 65  ? 0.77925 1.41066 1.21887 -0.12978 -0.34063 -0.11648 84  PRO A CG  
476  C CD  . PRO A 65  ? 0.73213 1.34426 1.16963 -0.16138 -0.29857 -0.09246 84  PRO A CD  
477  N N   . ILE A 66  ? 0.70062 1.17001 0.92465 -0.01576 -0.25855 -0.10462 85  ILE A N   
478  C CA  . ILE A 66  ? 0.67076 1.13745 0.87631 0.01451  -0.23116 -0.10256 85  ILE A CA  
479  C C   . ILE A 66  ? 0.73072 1.20480 0.93888 0.05975  -0.25837 -0.11610 85  ILE A C   
480  O O   . ILE A 66  ? 0.74056 1.15131 0.89764 0.07277  -0.28813 -0.11559 85  ILE A O   
481  C CB  . ILE A 66  ? 0.72640 1.09925 0.85457 0.01245  -0.21147 -0.09181 85  ILE A CB  
482  C CG1 . ILE A 66  ? 0.72215 1.07066 0.84619 -0.02928 -0.19702 -0.07977 85  ILE A CG1 
483  C CG2 . ILE A 66  ? 0.76637 1.14417 0.88640 0.03575  -0.18384 -0.09089 85  ILE A CG2 
484  C CD1 . ILE A 66  ? 0.78294 1.04673 0.84135 -0.02953 -0.17974 -0.07176 85  ILE A CD1 
485  N N   . GLU A 67  ? 0.75707 1.30806 1.02275 0.08505  -0.24867 -0.12784 86  GLU A N   
486  C CA  . GLU A 67  ? 0.76299 1.31862 1.04155 0.13413  -0.27529 -0.14287 86  GLU A CA  
487  C C   . GLU A 67  ? 0.75288 1.29173 1.01499 0.16277  -0.24935 -0.15073 86  GLU A C   
488  O O   . GLU A 67  ? 0.72497 1.33241 1.02250 0.16036  -0.21510 -0.15957 86  GLU A O   
489  C CB  . GLU A 67  ? 0.76822 1.43530 1.14222 0.14823  -0.29371 -0.16002 86  GLU A CB  
490  C CG  . GLU A 67  ? 0.83471 1.50095 1.22063 0.14177  -0.34319 -0.15898 86  GLU A CG  
491  C CD  . GLU A 67  ? 0.76296 1.53932 1.25030 0.16578  -0.36743 -0.17770 86  GLU A CD  
492  O OE1 . GLU A 67  ? 0.69501 1.54892 1.24171 0.19096  -0.34202 -0.19395 86  GLU A OE1 
493  O OE2 . GLU A 67  ? 0.91246 1.69637 1.41747 0.15943  -0.40942 -0.17685 86  GLU A OE2 
494  N N   . ARG A 68  ? 0.71918 1.16767 0.92560 0.18735  -0.26644 -0.14659 87  ARG A N   
495  C CA  . ARG A 68  ? 0.78887 1.20882 0.97966 0.21237  -0.24881 -0.15619 87  ARG A CA  
496  C C   . ARG A 68  ? 0.94754 1.31627 1.13477 0.25663  -0.28799 -0.16213 87  ARG A C   
497  O O   . ARG A 68  ? 0.98054 1.29394 1.13410 0.25599  -0.32169 -0.14327 87  ARG A O   
498  C CB  . ARG A 68  ? 0.75733 1.10037 0.87921 0.18543  -0.22342 -0.13710 87  ARG A CB  
499  C CG  . ARG A 68  ? 0.72596 1.11259 0.85415 0.14661  -0.18659 -0.12971 87  ARG A CG  
500  C CD  . ARG A 68  ? 0.69792 1.16634 0.86675 0.15808  -0.15827 -0.14830 87  ARG A CD  
501  N NE  . ARG A 68  ? 0.79291 1.30671 0.96779 0.11773  -0.12607 -0.13267 87  ARG A NE  
502  C CZ  . ARG A 68  ? 0.85677 1.45223 1.08349 0.09362  -0.11961 -0.12696 87  ARG A CZ  
503  N NH1 . ARG A 68  ? 0.74669 1.40370 1.03126 0.10869  -0.14034 -0.14111 87  ARG A NH1 
504  N NH2 . ARG A 68  ? 0.83794 1.45581 1.06419 0.05260  -0.09392 -0.10447 87  ARG A NH2 
505  N N   . PRO A 69  ? 0.94055 1.32376 1.15945 0.29580  -0.28699 -0.18793 88  PRO A N   
506  C CA  . PRO A 69  ? 0.93066 1.24536 1.14611 0.33719  -0.32823 -0.19035 88  PRO A CA  
507  C C   . PRO A 69  ? 0.93525 1.13041 1.07133 0.31964  -0.33263 -0.15902 88  PRO A C   
508  O O   . PRO A 69  ? 0.95610 1.12634 1.05493 0.29281  -0.29909 -0.15226 88  PRO A O   
509  C CB  . PRO A 69  ? 0.87193 1.22868 1.13826 0.37947  -0.31887 -0.23260 88  PRO A CB  
510  C CG  . PRO A 69  ? 0.81573 1.22492 1.07146 0.35077  -0.26628 -0.24098 88  PRO A CG  
511  C CD  . PRO A 69  ? 0.84607 1.30313 1.09951 0.30414  -0.24954 -0.21631 88  PRO A CD  
512  N N   . LEU A 70  ? 1.02805 1.15408 1.14009 0.33356  -0.37496 -0.13664 89  LEU A N   
513  C CA  . LEU A 70  ? 1.01235 1.03148 1.05363 0.31646  -0.37927 -0.10218 89  LEU A CA  
514  C C   . LEU A 70  ? 1.06199 1.03011 1.11541 0.33882  -0.38001 -0.11593 89  LEU A C   
515  O O   . LEU A 70  ? 1.16162 1.13051 1.26507 0.38275  -0.40915 -0.13999 89  LEU A O   
516  C CB  . LEU A 70  ? 1.05421 1.01935 1.06191 0.32309  -0.42546 -0.06872 89  LEU A CB  
517  C CG  . LEU A 70  ? 1.10078 0.97986 1.02236 0.29098  -0.42163 -0.02372 89  LEU A CG  
518  C CD1 . LEU A 70  ? 1.10034 1.00838 0.98262 0.24858  -0.38110 -0.02075 89  LEU A CD1 
519  C CD2 . LEU A 70  ? 1.12540 0.95987 1.01057 0.30100  -0.47034 0.01091  89  LEU A CD2 
520  N N   . ALA A 71  ? 0.97337 0.89664 0.98603 0.31033  -0.35127 -0.10385 90  ALA A N   
521  C CA  . ALA A 71  ? 1.07448 0.93963 1.09653 0.32673  -0.35809 -0.11576 90  ALA A CA  
522  C C   . ALA A 71  ? 1.26459 1.02564 1.25991 0.32937  -0.39675 -0.07757 90  ALA A C   
523  O O   . ALA A 71  ? 1.35352 1.06883 1.38298 0.36424  -0.43289 -0.08973 90  ALA A O   
524  C CB  . ALA A 71  ? 1.02031 0.88398 1.01731 0.29505  -0.31675 -0.11796 90  ALA A CB  
525  N N   . ARG A 72  ? 1.28738 1.01133 1.22233 0.29352  -0.39067 -0.03092 91  ARG A N   
526  C CA  . ARG A 72  ? 1.32583 0.95833 1.22508 0.28781  -0.42253 0.01646  91  ARG A CA  
527  C C   . ARG A 72  ? 1.34066 0.97532 1.17024 0.25325  -0.40974 0.05734  91  ARG A C   
528  O O   . ARG A 72  ? 1.37919 1.08019 1.19881 0.24100  -0.38627 0.04277  91  ARG A O   
529  C CB  . ARG A 72  ? 1.39023 0.95105 1.28939 0.27409  -0.41760 0.02643  91  ARG A CB  
530  C CG  . ARG A 72  ? 1.32092 0.90725 1.19978 0.23716  -0.36681 0.02242  91  ARG A CG  
531  C CD  . ARG A 72  ? 1.32631 0.85018 1.21907 0.22613  -0.36798 0.02563  91  ARG A CD  
532  N NE  . ARG A 72  ? 1.32386 0.86604 1.19418 0.18762  -0.32445 0.03379  91  ARG A NE  
533  C CZ  . ARG A 72  ? 1.39479 0.91332 1.22305 0.15117  -0.30648 0.07923  91  ARG A CZ  
534  N NH1 . ARG A 72  ? 1.39169 0.93321 1.21086 0.12170  -0.26824 0.08143  91  ARG A NH1 
535  N NH2 . ARG A 72  ? 1.46025 0.93542 1.25464 0.14552  -0.32754 0.12398  91  ARG A NH2 
536  N N   . VAL A 73  ? 1.33315 0.89531 1.11387 0.23690  -0.42603 0.10834  92  VAL A N   
537  C CA  . VAL A 73  ? 1.35645 0.91820 1.05993 0.20457  -0.41114 0.14705  92  VAL A CA  
538  C C   . VAL A 73  ? 1.50878 1.01560 1.17697 0.16987  -0.38732 0.18612  92  VAL A C   
539  O O   . VAL A 73  ? 1.62470 1.07129 1.30641 0.16787  -0.40610 0.21326  92  VAL A O   
540  C CB  . VAL A 73  ? 1.50414 1.05917 1.18094 0.21301  -0.44586 0.17349  92  VAL A CB  
541  C CG1 . VAL A 73  ? 1.58842 1.15085 1.17764 0.18153  -0.42791 0.20639  92  VAL A CG1 
542  C CG2 . VAL A 73  ? 1.44732 1.06350 1.17532 0.24632  -0.47009 0.13370  92  VAL A CG2 
543  N N   . SER A 74  ? 1.42171 0.96142 1.05878 0.13875  -0.33920 0.18449  93  SER A N   
544  C CA  . SER A 74  ? 1.56658 1.07265 1.18330 0.10525  -0.31039 0.21648  93  SER A CA  
545  C C   . SER A 74  ? 1.80880 1.27797 1.35387 0.08509  -0.31850 0.27678  93  SER A C   
546  O O   . SER A 74  ? 1.82390 1.29690 1.33606 0.09727  -0.34491 0.28971  93  SER A O   
547  C CB  . SER A 74  ? 1.52924 1.08789 1.14328 0.08388  -0.25831 0.19247  93  SER A CB  
548  O OG  . SER A 74  ? 1.60769 1.19712 1.15860 0.06986  -0.23875 0.20186  93  SER A OG  
549  N N   . LYS A 75  ? 1.95953 1.40674 1.48773 0.05146  -0.29020 0.31206  94  LYS A N   
550  C CA  . LYS A 75  ? 1.91645 1.35510 1.38860 0.02650  -0.27973 0.36594  94  LYS A CA  
551  C C   . LYS A 75  ? 1.95140 1.43978 1.34990 0.00662  -0.23755 0.36873  94  LYS A C   
552  O O   . LYS A 75  ? 1.84372 1.37302 1.25892 0.00376  -0.20404 0.32994  94  LYS A O   
553  C CB  . LYS A 75  ? 1.80162 1.20075 1.30962 -0.00004 -0.26966 0.40221  94  LYS A CB  
554  N N   . ALA A 93  ? 1.95553 1.48279 1.37137 0.10215  -0.36292 0.30334  112 ALA A N   
555  C CA  . ALA A 93  ? 1.89015 1.46525 1.24018 0.09050  -0.34098 0.28932  112 ALA A CA  
556  C C   . ALA A 93  ? 1.77478 1.38929 1.15529 0.10489  -0.34096 0.23341  112 ALA A C   
557  O O   . ALA A 93  ? 1.75591 1.40734 1.14229 0.12007  -0.36519 0.20839  112 ALA A O   
558  C CB  . ALA A 93  ? 1.87990 1.45559 1.17607 0.05716  -0.29131 0.31297  112 ALA A CB  
559  N N   . ARG A 94  ? 1.49452 1.12331 0.92387 0.09495  -0.30106 0.20827  113 ARG A N   
560  C CA  . ARG A 94  ? 1.43668 1.12008 0.91245 0.10081  -0.28619 0.15575  113 ARG A CA  
561  C C   . ARG A 94  ? 1.40536 1.10018 0.96399 0.12759  -0.31015 0.12998  113 ARG A C   
562  O O   . ARG A 94  ? 1.32993 0.98751 0.92316 0.13715  -0.31960 0.14071  113 ARG A O   
563  C CB  . ARG A 94  ? 1.41333 1.11221 0.90010 0.07904  -0.23432 0.14092  113 ARG A CB  
564  C CG  . ARG A 94  ? 1.38340 1.09182 0.79993 0.05791  -0.20375 0.14854  113 ARG A CG  
565  C CD  . ARG A 94  ? 1.09455 0.82078 0.53830 0.04240  -0.15683 0.13015  113 ARG A CD  
566  N N   . PRO A 95  ? 1.30551 1.05428 0.89917 0.13951  -0.32013 0.09421  114 PRO A N   
567  C CA  . PRO A 95  ? 1.10326 0.88190 0.77870 0.16419  -0.33215 0.06468  114 PRO A CA  
568  C C   . PRO A 95  ? 1.15451 0.94535 0.86760 0.15421  -0.29269 0.04514  114 PRO A C   
569  O O   . PRO A 95  ? 1.06644 0.86903 0.76068 0.12930  -0.25742 0.04140  114 PRO A O   
570  C CB  . PRO A 95  ? 1.06172 0.90574 0.76080 0.16968  -0.34663 0.03715  114 PRO A CB  
571  C CG  . PRO A 95  ? 1.19982 1.03156 0.82379 0.15505  -0.35893 0.05456  114 PRO A CG  
572  C CD  . PRO A 95  ? 1.28648 1.07375 0.84843 0.13106  -0.32439 0.07889  114 PRO A CD  
573  N N   . VAL A 96  ? 1.12841 0.91432 0.89381 0.17619  -0.30187 0.03121  115 VAL A N   
574  C CA  . VAL A 96  ? 1.05368 0.85150 0.85175 0.17069  -0.27161 0.01107  115 VAL A CA  
575  C C   . VAL A 96  ? 0.93919 0.80443 0.79841 0.19335  -0.27342 -0.02824 115 VAL A C   
576  O O   . VAL A 96  ? 1.03226 0.91006 0.92546 0.22488  -0.30484 -0.04060 115 VAL A O   
577  C CB  . VAL A 96  ? 1.10725 0.83895 0.90859 0.17443  -0.27925 0.02548  115 VAL A CB  
578  C CG1 . VAL A 96  ? 0.86759 0.61368 0.69574 0.16675  -0.25111 0.00325  115 VAL A CG1 
579  C CG2 . VAL A 96  ? 1.17623 0.85056 0.92075 0.14967  -0.27703 0.07140  115 VAL A CG2 
580  N N   . ILE A 97  ? 0.81056 0.72340 0.68560 0.17791  -0.23987 -0.04619 116 ILE A N   
581  C CA  . ILE A 97  ? 0.78907 0.77728 0.71772 0.19378  -0.23329 -0.07926 116 ILE A CA  
582  C C   . ILE A 97  ? 0.80175 0.80323 0.73697 0.18447  -0.20286 -0.09214 116 ILE A C   
583  O O   . ILE A 97  ? 0.84007 0.79824 0.74474 0.16312  -0.18739 -0.07582 116 ILE A O   
584  C CB  . ILE A 97  ? 0.76632 0.82172 0.71080 0.17967  -0.22801 -0.08367 116 ILE A CB  
585  C CG1 . ILE A 97  ? 0.78158 0.82386 0.68928 0.14125  -0.20252 -0.06735 116 ILE A CG1 
586  C CG2 . ILE A 97  ? 0.77712 0.83255 0.72411 0.19502  -0.26568 -0.07827 116 ILE A CG2 
587  C CD1 . ILE A 97  ? 0.80654 0.91011 0.73876 0.12237  -0.19670 -0.07419 116 ILE A CD1 
588  N N   . GLU A 98  ? 0.69153 0.75998 0.66770 0.20190  -0.19489 -0.12216 117 GLU A N   
589  C CA  . GLU A 98  ? 0.73487 0.83283 0.71244 0.19337  -0.16693 -0.13548 117 GLU A CA  
590  C C   . GLU A 98  ? 0.73452 0.91386 0.72842 0.17202  -0.14184 -0.13427 117 GLU A C   
591  O O   . GLU A 98  ? 0.75259 0.99983 0.78531 0.18351  -0.14529 -0.14752 117 GLU A O   
592  C CB  . GLU A 98  ? 0.83824 0.95075 0.84132 0.22999  -0.17552 -0.17245 117 GLU A CB  
593  C CG  . GLU A 98  ? 1.04478 1.06551 1.03336 0.24229  -0.19931 -0.17182 117 GLU A CG  
594  C CD  . GLU A 98  ? 1.11891 1.14582 1.11986 0.26607  -0.20057 -0.21108 117 GLU A CD  
595  O OE1 . GLU A 98  ? 1.16088 1.23801 1.19615 0.30287  -0.20742 -0.25000 117 GLU A OE1 
596  O OE2 . GLU A 98  ? 1.12679 1.11262 1.10480 0.24911  -0.19544 -0.20611 117 GLU A OE2 
597  N N   . LEU A 99  ? 0.68030 0.85297 0.65071 0.14023  -0.11887 -0.11628 118 LEU A N   
598  C CA  . LEU A 99  ? 0.71467 0.94811 0.69862 0.11303  -0.09781 -0.10605 118 LEU A CA  
599  C C   . LEU A 99  ? 0.68621 0.94461 0.65948 0.10244  -0.07441 -0.10540 118 LEU A C   
600  O O   . LEU A 99  ? 0.79948 1.00572 0.74476 0.10048  -0.07379 -0.10114 118 LEU A O   
601  C CB  . LEU A 99  ? 0.65586 0.84945 0.62109 0.08278  -0.09854 -0.08081 118 LEU A CB  
602  C CG  . LEU A 99  ? 0.79316 0.98393 0.76644 0.08455  -0.12061 -0.08018 118 LEU A CG  
603  C CD1 . LEU A 99  ? 0.78474 0.92912 0.72891 0.05752  -0.12005 -0.06307 118 LEU A CD1 
604  C CD2 . LEU A 99  ? 0.65939 0.93786 0.68487 0.08483  -0.12213 -0.09088 118 LEU A CD2 
605  N N   . ASP A 100 ? 0.67054 1.01335 0.66667 0.09423  -0.05615 -0.10745 119 ASP A N   
606  C CA  . ASP A 100 ? 0.71892 1.09031 0.69665 0.07787  -0.03440 -0.09765 119 ASP A CA  
607  C C   . ASP A 100 ? 0.75923 1.09580 0.72597 0.03910  -0.02919 -0.06093 119 ASP A C   
608  O O   . ASP A 100 ? 0.69415 1.06289 0.68543 0.01477  -0.02465 -0.04361 119 ASP A O   
609  C CB  . ASP A 100 ? 0.64938 1.13033 0.65149 0.08115  -0.01385 -0.10852 119 ASP A CB  
610  C CG  . ASP A 100 ? 0.77540 1.29085 0.78549 0.12601  -0.01720 -0.15354 119 ASP A CG  
611  O OD1 . ASP A 100 ? 0.74464 1.19051 0.74752 0.15261  -0.04095 -0.17290 119 ASP A OD1 
612  O OD2 . ASP A 100 ? 0.82893 1.44154 0.85383 0.13486  0.00381  -0.16979 119 ASP A OD2 
613  N N   . ILE A 101 ? 0.73882 1.00876 0.67563 0.03406  -0.03248 -0.05095 120 ILE A N   
614  C CA  . ILE A 101 ? 0.74495 0.97355 0.67502 0.00507  -0.03034 -0.02184 120 ILE A CA  
615  C C   . ILE A 101 ? 0.79564 1.04609 0.71230 -0.01006 -0.01894 -0.00324 120 ILE A C   
616  O O   . ILE A 101 ? 0.74333 1.00246 0.63920 0.00482  -0.01810 -0.01558 120 ILE A O   
617  C CB  . ILE A 101 ? 0.83211 0.97920 0.74471 0.01070  -0.04093 -0.02217 120 ILE A CB  
618  C CG1 . ILE A 101 ? 0.66796 0.79419 0.58286 0.02541  -0.05438 -0.03548 120 ILE A CG1 
619  C CG2 . ILE A 101 ? 0.66615 0.77602 0.57830 -0.01317 -0.03798 0.00043  120 ILE A CG2 
620  C CD1 . ILE A 101 ? 0.82762 0.97100 0.75985 0.01042  -0.05861 -0.03029 120 ILE A CD1 
621  N N   . CYS A 102 ? 0.79225 1.04841 0.72020 -0.04003 -0.01425 0.02684  121 CYS A N   
622  C CA  . CYS A 102 ? 0.78040 1.05593 0.69571 -0.05886 -0.00721 0.05494  121 CYS A CA  
623  C C   . CYS A 102 ? 0.76346 0.96708 0.67863 -0.07151 -0.01767 0.07584  121 CYS A C   
624  O O   . CYS A 102 ? 0.81040 0.97608 0.74651 -0.08339 -0.02393 0.08173  121 CYS A O   
625  C CB  . CYS A 102 ? 0.86451 1.20890 0.80032 -0.08614 0.00510  0.07986  121 CYS A CB  
626  S SG  . CYS A 102 ? 0.92686 1.27928 0.84881 -0.11987 0.00827  0.13184  121 CYS A SG  
627  N N   . MET A 103 ? 0.71269 0.90038 0.60671 -0.06651 -0.02161 0.08282  122 MET A N   
628  C CA  . MET A 103 ? 0.84255 0.97106 0.74366 -0.07332 -0.03237 0.10076  122 MET A CA  
629  C C   . MET A 103 ? 0.81589 0.96557 0.69987 -0.08425 -0.03680 0.12995  122 MET A C   
630  O O   . MET A 103 ? 0.77098 0.95191 0.62596 -0.07200 -0.03685 0.11895  122 MET A O   
631  C CB  . MET A 103 ? 0.74324 0.82516 0.64249 -0.05186 -0.03766 0.07656  122 MET A CB  
632  C CG  . MET A 103 ? 0.89170 0.92623 0.80586 -0.05367 -0.04613 0.08965  122 MET A CG  
633  S SD  . MET A 103 ? 0.74491 0.73584 0.66689 -0.03534 -0.04401 0.06389  122 MET A SD  
634  C CE  . MET A 103 ? 0.83674 0.80881 0.76371 -0.03889 -0.03708 0.05422  122 MET A CE  
635  N N   . GLY A 104 ? 0.81050 0.94116 0.71063 -0.10689 -0.04392 0.16658  123 GLY A N   
636  C CA  . GLY A 104 ? 0.81173 0.96806 0.69133 -0.12188 -0.05003 0.20440  123 GLY A CA  
637  C C   . GLY A 104 ? 0.84431 1.08489 0.69620 -0.13128 -0.03209 0.20980  123 GLY A C   
638  O O   . GLY A 104 ? 0.99338 1.26670 0.86466 -0.14920 -0.01956 0.21858  123 GLY A O   
639  N N   . SER A 105 ? 0.86092 1.14327 0.66931 -0.11837 -0.03066 0.20078  124 SER A N   
640  C CA  . SER A 105 ? 0.89927 1.27203 0.67589 -0.11948 -0.00982 0.19501  124 SER A CA  
641  C C   . SER A 105 ? 0.95261 1.34776 0.71535 -0.08422 -0.00365 0.13597  124 SER A C   
642  O O   . SER A 105 ? 0.96270 1.43303 0.69368 -0.07485 0.01127  0.11893  124 SER A O   
643  C CB  . SER A 105 ? 0.87934 1.29353 0.60631 -0.13329 -0.01305 0.23159  124 SER A CB  
644  O OG  . SER A 105 ? 1.04026 1.42761 0.73710 -0.11146 -0.03376 0.21236  124 SER A OG  
645  N N   . ALA A 106 ? 0.89122 1.22363 0.67719 -0.06419 -0.01498 0.10465  125 ALA A N   
646  C CA  . ALA A 106 ? 0.90532 1.24064 0.68318 -0.03187 -0.01657 0.05306  125 ALA A CA  
647  C C   . ALA A 106 ? 0.89204 1.23030 0.70319 -0.02270 -0.00731 0.03144  125 ALA A C   
648  O O   . ALA A 106 ? 0.82469 1.11223 0.66510 -0.03071 -0.01203 0.04080  125 ALA A O   
649  C CB  . ALA A 106 ? 0.73252 0.99774 0.51315 -0.01890 -0.03836 0.03877  125 ALA A CB  
650  N N   . MET A 107 ? 0.83359 1.23415 0.63976 -0.00359 0.00420  0.00032  126 MET A N   
651  C CA  . MET A 107 ? 0.80777 1.21783 0.64744 0.01189  0.00767  -0.02468 126 MET A CA  
652  C C   . MET A 107 ? 0.73403 1.10962 0.56961 0.04825  -0.00764 -0.07043 126 MET A C   
653  O O   . MET A 107 ? 0.74034 1.14425 0.55057 0.06852  -0.00908 -0.09959 126 MET A O   
654  C CB  . MET A 107 ? 0.82850 1.34089 0.68010 0.00951  0.03072  -0.02725 126 MET A CB  
655  C CG  . MET A 107 ? 0.86434 1.39828 0.75740 0.03018  0.03063  -0.05631 126 MET A CG  
656  S SD  . MET A 107 ? 1.03915 1.53418 0.97572 0.00250  0.02266  -0.02693 126 MET A SD  
657  C CE  . MET A 107 ? 0.79820 1.37294 0.74945 -0.04205 0.04542  0.01869  126 MET A CE  
658  N N   . ARG A 108 ? 0.74321 1.05636 0.60149 0.05576  -0.02098 -0.07647 127 ARG A N   
659  C CA  . ARG A 108 ? 0.74710 1.01354 0.60619 0.08499  -0.03972 -0.11045 127 ARG A CA  
660  C C   . ARG A 108 ? 0.78431 1.03640 0.67209 0.09961  -0.04720 -0.12093 127 ARG A C   
661  O O   . ARG A 108 ? 0.75052 0.98909 0.65158 0.08197  -0.04481 -0.09722 127 ARG A O   
662  C CB  . ARG A 108 ? 0.69907 0.88616 0.54967 0.07597  -0.05464 -0.09829 127 ARG A CB  
663  C CG  . ARG A 108 ? 0.66101 0.85527 0.48685 0.06635  -0.05681 -0.09178 127 ARG A CG  
664  C CD  . ARG A 108 ? 0.63572 0.86529 0.44011 0.09084  -0.06366 -0.13194 127 ARG A CD  
665  N NE  . ARG A 108 ? 0.83500 1.05909 0.61268 0.08311  -0.07481 -0.12908 127 ARG A NE  
666  C CZ  . ARG A 108 ? 0.85946 1.13203 0.60807 0.06735  -0.06535 -0.10677 127 ARG A CZ  
667  N NH1 . ARG A 108 ? 0.79715 1.12828 0.54201 0.05415  -0.04186 -0.08325 127 ARG A NH1 
668  N NH2 . ARG A 108 ? 0.95977 1.22220 0.68447 0.06257  -0.08249 -0.10483 127 ARG A NH2 
669  N N   . SER A 109 ? 0.85704 1.10877 0.75408 0.13350  -0.06038 -0.15818 128 SER A N   
670  C CA  . SER A 109 ? 0.76631 0.98858 0.68855 0.15113  -0.07673 -0.16580 128 SER A CA  
671  C C   . SER A 109 ? 0.78380 0.91006 0.69572 0.14324  -0.09467 -0.14843 128 SER A C   
672  O O   . SER A 109 ? 0.81461 0.89522 0.71831 0.15108  -0.10833 -0.16036 128 SER A O   
673  C CB  . SER A 109 ? 0.90552 1.15604 0.84740 0.19350  -0.08849 -0.21158 128 SER A CB  
674  O OG  . SER A 109 ? 0.89302 1.11626 0.86230 0.21199  -0.10895 -0.21464 128 SER A OG  
675  N N   . ILE A 110 ? 0.73781 0.83764 0.65046 0.12624  -0.09452 -0.12106 129 ILE A N   
676  C CA  . ILE A 110 ? 0.86414 0.88873 0.76213 0.11268  -0.10224 -0.09831 129 ILE A CA  
677  C C   . ILE A 110 ? 0.75724 0.75123 0.65819 0.12427  -0.12013 -0.09339 129 ILE A C   
678  O O   . ILE A 110 ? 0.84972 0.88090 0.76158 0.12762  -0.12115 -0.09459 129 ILE A O   
679  C CB  . ILE A 110 ? 0.75841 0.78034 0.64481 0.08128  -0.08384 -0.07044 129 ILE A CB  
680  C CG1 . ILE A 110 ? 0.88674 0.93206 0.76899 0.07045  -0.07241 -0.06928 129 ILE A CG1 
681  C CG2 . ILE A 110 ? 0.78405 0.74339 0.65698 0.07001  -0.08638 -0.05023 129 ILE A CG2 
682  C CD1 . ILE A 110 ? 0.75172 0.76615 0.63004 0.07946  -0.08424 -0.08217 129 ILE A CD1 
683  N N   . GLU A 111 ? 0.79212 0.71977 0.68464 0.12814  -0.13656 -0.08479 130 GLU A N   
684  C CA  . GLU A 111 ? 0.81647 0.70618 0.70093 0.13480  -0.15547 -0.06969 130 GLU A CA  
685  C C   . GLU A 111 ? 0.72886 0.59953 0.58337 0.10752  -0.14121 -0.03948 130 GLU A C   
686  O O   . GLU A 111 ? 0.85276 0.70044 0.69648 0.08785  -0.12588 -0.02510 130 GLU A O   
687  C CB  . GLU A 111 ? 0.78878 0.61331 0.67790 0.14838  -0.18111 -0.06849 130 GLU A CB  
688  C CG  . GLU A 111 ? 1.02928 0.79971 0.89720 0.14401  -0.19813 -0.03628 130 GLU A CG  
689  C CD  . GLU A 111 ? 1.15275 0.85492 1.03314 0.15705  -0.22930 -0.03132 130 GLU A CD  
690  O OE1 . GLU A 111 ? 1.07732 0.78099 0.98948 0.18783  -0.25076 -0.06429 130 GLU A OE1 
691  O OE2 . GLU A 111 ? 1.13116 0.77921 0.99168 0.13617  -0.23218 0.00524  130 GLU A OE2 
692  N N   . VAL A 112 ? 0.71720 0.60261 0.56099 0.10801  -0.14714 -0.03389 131 VAL A N   
693  C CA  . VAL A 112 ? 0.81747 0.69254 0.62921 0.08622  -0.13456 -0.01537 131 VAL A CA  
694  C C   . VAL A 112 ? 0.88282 0.73407 0.66621 0.09363  -0.15707 -0.00186 131 VAL A C   
695  O O   . VAL A 112 ? 0.90628 0.77445 0.70613 0.11403  -0.18194 -0.01150 131 VAL A O   
696  C CB  . VAL A 112 ? 0.78101 0.70439 0.60401 0.07247  -0.11903 -0.02538 131 VAL A CB  
697  C CG1 . VAL A 112 ? 0.70972 0.65186 0.55185 0.06247  -0.09862 -0.02982 131 VAL A CG1 
698  C CG2 . VAL A 112 ? 0.85029 0.82323 0.69953 0.08456  -0.13446 -0.04078 131 VAL A CG2 
699  N N   . ASN A 113 ? 0.97829 0.79501 0.71887 0.07819  -0.14851 0.02086  132 ASN A N   
700  C CA  . ASN A 113 ? 1.00801 0.80631 0.70474 0.08026  -0.16666 0.03738  132 ASN A CA  
701  C C   . ASN A 113 ? 0.96009 0.79102 0.63973 0.07129  -0.16168 0.02297  132 ASN A C   
702  O O   . ASN A 113 ? 1.01685 0.85720 0.69448 0.05529  -0.13545 0.01509  132 ASN A O   
703  C CB  . ASN A 113 ? 1.12568 0.87975 0.77870 0.06574  -0.15554 0.06988  132 ASN A CB  
704  C CG  . ASN A 113 ? 1.25402 0.96883 0.93092 0.06778  -0.16243 0.08612  132 ASN A CG  
705  O OD1 . ASN A 113 ? 1.29041 1.01269 1.01405 0.07738  -0.16522 0.06585  132 ASN A OD1 
706  N ND2 . ASN A 113 ? 1.45832 1.13145 1.10153 0.05694  -0.16603 0.12319  132 ASN A ND2 
707  N N   . LEU A 114 ? 1.00285 0.84835 0.67453 0.08230  -0.19094 0.01826  133 LEU A N   
708  C CA  . LEU A 114 ? 0.97841 0.85139 0.63655 0.07278  -0.19484 0.00160  133 LEU A CA  
709  C C   . LEU A 114 ? 1.01686 0.86060 0.59949 0.06423  -0.19294 0.01487  133 LEU A C   
710  O O   . LEU A 114 ? 1.17097 0.99390 0.71203 0.07314  -0.21678 0.03549  133 LEU A O   
711  C CB  . LEU A 114 ? 0.90295 0.81359 0.59368 0.08741  -0.22991 -0.01154 133 LEU A CB  
712  C CG  . LEU A 114 ? 0.88483 0.84077 0.65012 0.09851  -0.22895 -0.02753 133 LEU A CG  
713  C CD1 . LEU A 114 ? 0.87619 0.87911 0.67919 0.11413  -0.26321 -0.04023 133 LEU A CD1 
714  C CD2 . LEU A 114 ? 0.87768 0.86152 0.67160 0.07729  -0.19782 -0.03995 133 LEU A CD2 
715  N N   . THR A 115 ? 1.03910 0.88255 0.60267 0.04853  -0.16514 0.00324  134 THR A N   
716  C CA  . THR A 115 ? 1.19134 1.01739 0.68132 0.04207  -0.15516 0.00855  134 THR A CA  
717  C C   . THR A 115 ? 1.27852 1.12040 0.74970 0.03683  -0.16364 -0.02471 134 THR A C   
718  O O   . THR A 115 ? 1.14477 1.00359 0.66729 0.03024  -0.16230 -0.04877 134 THR A O   
719  C CB  . THR A 115 ? 1.21675 1.02910 0.69984 0.03216  -0.11346 0.01941  134 THR A CB  
720  O OG1 . THR A 115 ? 1.36461 1.17512 0.77974 0.02719  -0.09701 0.01579  134 THR A OG1 
721  C CG2 . THR A 115 ? 1.24552 1.07127 0.79030 0.02626  -0.09278 -0.00108 134 THR A CG2 
722  N N   . ASP A 116 ? 1.53047 1.36500 0.92523 0.03841  -0.17462 -0.02476 135 ASP A N   
723  C CA  . ASP A 116 ? 1.61811 1.46106 0.97935 0.03493  -0.18698 -0.06111 135 ASP A CA  
724  C C   . ASP A 116 ? 1.73108 1.56626 1.06307 0.02999  -0.14857 -0.08161 135 ASP A C   
725  O O   . ASP A 116 ? 1.82480 1.65980 1.08917 0.03212  -0.15155 -0.10450 135 ASP A O   
726  C CB  . ASP A 116 ? 1.74422 1.58701 1.02970 0.04208  -0.22269 -0.05418 135 ASP A CB  
727  C CG  . ASP A 116 ? 1.83798 1.66916 1.11166 0.05128  -0.23912 -0.00813 135 ASP A CG  
728  O OD1 . ASP A 116 ? 1.77145 1.61031 1.11446 0.05883  -0.25849 -0.00091 135 ASP A OD1 
729  O OD2 . ASP A 116 ? 1.94139 1.75628 1.13808 0.05107  -0.23218 0.02121  135 ASP A OD2 
730  N N   . ARG A 117 ? 1.86983 1.55613 1.12893 0.12882  -0.51668 -0.06707 136 ARG A N   
731  C CA  . ARG A 117 ? 1.94296 1.59823 1.13719 0.11726  -0.48151 -0.09203 136 ARG A CA  
732  C C   . ARG A 117 ? 1.99642 1.67642 1.25295 0.10541  -0.52048 -0.14840 136 ARG A C   
733  O O   . ARG A 117 ? 1.91821 1.64426 1.29116 0.09805  -0.56717 -0.16467 136 ARG A O   
734  C CB  . ARG A 117 ? 1.85099 1.50633 1.08968 0.09221  -0.42123 -0.07320 136 ARG A CB  
735  C CG  . ARG A 117 ? 2.00430 1.62768 1.18301 0.09805  -0.36254 -0.02296 136 ARG A CG  
736  C CD  . ARG A 117 ? 1.93612 1.58496 1.21528 0.06851  -0.30240 -0.00960 136 ARG A CD  
737  N NE  . ARG A 117 ? 1.80112 1.50748 1.22156 0.05320  -0.32563 -0.01150 136 ARG A NE  
738  C CZ  . ARG A 117 ? 1.73599 1.47262 1.25204 0.02886  -0.28918 -0.00581 136 ARG A CZ  
739  N NH1 . ARG A 117 ? 1.83015 1.54965 1.33105 0.01635  -0.23437 -0.00161 136 ARG A NH1 
740  N NH2 . ARG A 117 ? 1.50915 1.29558 1.13914 0.01808  -0.30816 -0.00416 136 ARG A NH2 
741  N N   . SER A 118 ? 1.97500 1.62329 1.15917 0.10362  -0.49581 -0.17867 137 SER A N   
742  C CA  . SER A 118 ? 1.93565 1.59972 1.18414 0.09052  -0.52425 -0.23370 137 SER A CA  
743  C C   . SER A 118 ? 1.86152 1.56204 1.26470 0.05815  -0.52552 -0.23799 137 SER A C   
744  O O   . SER A 118 ? 1.82365 1.52577 1.25481 0.04335  -0.47819 -0.20679 137 SER A O   
745  C CB  . SER A 118 ? 1.98309 1.60520 1.13007 0.09537  -0.48657 -0.26450 137 SER A CB  
746  O OG  . SER A 118 ? 2.03636 1.63761 1.17199 0.08203  -0.42594 -0.24972 137 SER A OG  
747  N N   . ALA A 119 ? 1.87466 1.61010 1.39423 0.04504  -0.56749 -0.26946 138 ALA A N   
748  C CA  . ALA A 119 ? 1.78355 1.55128 1.45614 0.01180  -0.56175 -0.27170 138 ALA A CA  
749  C C   . ALA A 119 ? 1.73692 1.47352 1.39990 -0.00353 -0.52043 -0.28788 138 ALA A C   
750  O O   . ALA A 119 ? 1.53742 1.29728 1.31909 -0.03023 -0.49484 -0.27247 138 ALA A O   
751  C CB  . ALA A 119 ? 1.59723 1.39936 1.39008 0.00126  -0.60592 -0.30189 138 ALA A CB  
752  N N   . PHE A 120 ? 1.94426 1.63500 1.47793 0.01450  -0.49839 -0.31046 139 PHE A N   
753  C CA  . PHE A 120 ? 1.87735 1.54472 1.40905 0.00458  -0.44282 -0.32026 139 PHE A CA  
754  C C   . PHE A 120 ? 1.81015 1.49309 1.37305 -0.00722 -0.37674 -0.26297 139 PHE A C   
755  O O   . PHE A 120 ? 1.75665 1.45617 1.42256 -0.02888 -0.35079 -0.25245 139 PHE A O   
756  C CB  . PHE A 120 ? 1.98817 1.60586 1.36492 0.03035  -0.42827 -0.35593 139 PHE A CB  
757  C CG  . PHE A 120 ? 2.02167 1.64126 1.38721 0.04123  -0.47094 -0.40124 139 PHE A CG  
758  C CD1 . PHE A 120 ? 1.99925 1.64798 1.50112 0.02322  -0.51440 -0.42409 139 PHE A CD1 
759  C CD2 . PHE A 120 ? 2.21931 1.81065 1.43941 0.06845  -0.46371 -0.41773 139 PHE A CD2 
760  C CE1 . PHE A 120 ? 2.11664 1.76338 1.60964 0.03289  -0.55530 -0.46754 139 PHE A CE1 
761  C CE2 . PHE A 120 ? 2.33889 1.92969 1.54357 0.07858  -0.50648 -0.46165 139 PHE A CE2 
762  C CZ  . PHE A 120 ? 2.25681 1.87415 1.59843 0.06111  -0.55483 -0.48892 139 PHE A CZ  
763  N N   . GLN A 121 ? 1.70395 1.37822 1.17788 0.00788  -0.35176 -0.22567 140 GLN A N   
764  C CA  . GLN A 121 ? 1.49717 1.18323 0.99701 -0.00187 -0.29373 -0.17693 140 GLN A CA  
765  C C   . GLN A 121 ? 1.28521 1.01775 0.91744 -0.02241 -0.30187 -0.14941 140 GLN A C   
766  O O   . GLN A 121 ? 1.32706 1.08448 1.03637 -0.03045 -0.34822 -0.16366 140 GLN A O   
767  C CB  . GLN A 121 ? 1.63155 1.29530 1.02093 0.01797  -0.27485 -0.14303 140 GLN A CB  
768  C CG  . GLN A 121 ? 1.78218 1.39699 1.02860 0.03804  -0.25013 -0.15978 140 GLN A CG  
769  C CD  . GLN A 121 ? 1.94386 1.53378 1.11193 0.04663  -0.19762 -0.11398 140 GLN A CD  
770  O OE1 . GLN A 121 ? 1.97613 1.57210 1.14984 0.05087  -0.20812 -0.07559 140 GLN A OE1 
771  N NE2 . GLN A 121 ? 1.93324 1.49496 1.03827 0.04872  -0.13790 -0.11839 140 GLN A NE2 
772  N N   . TYR A 122 ? 1.13464 0.87989 0.79366 -0.03033 -0.25708 -0.11085 141 TYR A N   
773  C CA  . TYR A 122 ? 1.06181 0.84889 0.83303 -0.04782 -0.25760 -0.08623 141 TYR A CA  
774  C C   . TYR A 122 ? 1.01894 0.83131 0.80452 -0.03943 -0.28756 -0.06721 141 TYR A C   
775  O O   . TYR A 122 ? 1.20559 1.00273 0.91915 -0.02211 -0.28115 -0.04893 141 TYR A O   
776  C CB  . TYR A 122 ? 0.84435 0.63647 0.63562 -0.05641 -0.20587 -0.05822 141 TYR A CB  
777  C CG  . TYR A 122 ? 0.95513 0.74181 0.79206 -0.06909 -0.18652 -0.07227 141 TYR A CG  
778  C CD1 . TYR A 122 ? 1.00022 0.75793 0.78736 -0.06309 -0.15739 -0.09065 141 TYR A CD1 
779  C CD2 . TYR A 122 ? 0.98075 0.79006 0.91443 -0.08569 -0.19667 -0.06604 141 TYR A CD2 
780  C CE1 . TYR A 122 ? 1.04049 0.79434 0.88029 -0.07115 -0.14329 -0.10536 141 TYR A CE1 
781  C CE2 . TYR A 122 ? 0.90876 0.70768 0.88592 -0.09412 -0.18366 -0.07531 141 TYR A CE2 
782  C CZ  . TYR A 122 ? 0.95499 0.72717 0.88841 -0.08567 -0.15977 -0.09691 141 TYR A CZ  
783  O OH  . TYR A 122 ? 0.95786 0.72067 0.94418 -0.09056 -0.14974 -0.10780 141 TYR A OH  
784  N N   . PRO A 123 ? 0.94322 0.79309 0.82743 -0.05077 -0.31933 -0.07067 142 PRO A N   
785  C CA  . PRO A 123 ? 0.87407 0.75454 0.78799 -0.04054 -0.35069 -0.05818 142 PRO A CA  
786  C C   . PRO A 123 ? 0.88361 0.77710 0.79520 -0.03410 -0.31650 -0.02000 142 PRO A C   
787  O O   . PRO A 123 ? 0.93234 0.82944 0.82063 -0.01468 -0.33628 -0.00938 142 PRO A O   
788  C CB  . PRO A 123 ? 0.82936 0.75246 0.87523 -0.06132 -0.37445 -0.06746 142 PRO A CB  
789  C CG  . PRO A 123 ? 0.90573 0.80467 0.96390 -0.07645 -0.37602 -0.09598 142 PRO A CG  
790  C CD  . PRO A 123 ? 0.88125 0.74551 0.86202 -0.07323 -0.32751 -0.08627 142 PRO A CD  
791  N N   . LEU A 124 ? 0.77492 0.67433 0.71251 -0.04777 -0.27016 -0.00131 143 LEU A N   
792  C CA  . LEU A 124 ? 0.79203 0.70088 0.72714 -0.04191 -0.23806 0.02750  143 LEU A CA  
793  C C   . LEU A 124 ? 0.92732 0.80095 0.79931 -0.04283 -0.19759 0.03333  143 LEU A C   
794  O O   . LEU A 124 ? 0.82481 0.69552 0.71544 -0.05708 -0.17830 0.02750  143 LEU A O   
795  C CB  . LEU A 124 ? 0.70483 0.65970 0.73474 -0.05580 -0.22211 0.04284  143 LEU A CB  
796  C CG  . LEU A 124 ? 0.76694 0.73254 0.79405 -0.04872 -0.18878 0.06511  143 LEU A CG  
797  C CD1 . LEU A 124 ? 0.63478 0.59965 0.64185 -0.02593 -0.20406 0.07062  143 LEU A CD1 
798  C CD2 . LEU A 124 ? 0.67680 0.68526 0.78114 -0.06135 -0.16902 0.07869  143 LEU A CD2 
799  N N   . LEU A 125 ? 0.96421 0.81088 0.77106 -0.02759 -0.18537 0.04577  144 LEU A N   
800  C CA  . LEU A 125 ? 0.76840 0.58633 0.53414 -0.03023 -0.14361 0.05347  144 LEU A CA  
801  C C   . LEU A 125 ? 0.76827 0.59991 0.56495 -0.02812 -0.12431 0.07257  144 LEU A C   
802  O O   . LEU A 125 ? 0.85896 0.68719 0.64563 -0.01271 -0.13522 0.08475  144 LEU A O   
803  C CB  . LEU A 125 ? 0.88528 0.65480 0.55370 -0.01672 -0.13745 0.05463  144 LEU A CB  
804  C CG  . LEU A 125 ? 1.09668 0.83688 0.73282 -0.02319 -0.08902 0.05924  144 LEU A CG  
805  C CD1 . LEU A 125 ? 1.13239 0.83461 0.68293 -0.01641 -0.07998 0.04737  144 LEU A CD1 
806  C CD2 . LEU A 125 ? 1.04862 0.77077 0.67526 -0.01752 -0.06630 0.08474  144 LEU A CD2 
807  N N   . ILE A 126 ? 0.76797 0.61374 0.60197 -0.04087 -0.09962 0.07272  145 ILE A N   
808  C CA  . ILE A 126 ? 0.74004 0.60106 0.60264 -0.03845 -0.08421 0.08275  145 ILE A CA  
809  C C   . ILE A 126 ? 0.76309 0.59133 0.59738 -0.03936 -0.05589 0.08407  145 ILE A C   
810  O O   . ILE A 126 ? 0.73497 0.55927 0.57700 -0.05091 -0.03911 0.07556  145 ILE A O   
811  C CB  . ILE A 126 ? 0.62212 0.52069 0.53885 -0.04930 -0.08031 0.08228  145 ILE A CB  
812  C CG1 . ILE A 126 ? 0.67831 0.60788 0.63674 -0.05237 -0.10271 0.08386  145 ILE A CG1 
813  C CG2 . ILE A 126 ? 0.73535 0.64843 0.66704 -0.04304 -0.06531 0.08703  145 ILE A CG2 
814  C CD1 . ILE A 126 ? 0.62903 0.59263 0.63638 -0.06179 -0.09288 0.09267  145 ILE A CD1 
815  N N   . GLY A 127 ? 0.75140 0.55604 0.56364 -0.02712 -0.05126 0.09479  146 GLY A N   
816  C CA  . GLY A 127 ? 0.82353 0.59213 0.61891 -0.02997 -0.02300 0.09855  146 GLY A CA  
817  C C   . GLY A 127 ? 0.77511 0.55854 0.61729 -0.03478 -0.01112 0.08941  146 GLY A C   
818  O O   . GLY A 127 ? 0.75122 0.57200 0.62578 -0.03409 -0.02151 0.08201  146 GLY A O   
819  N N   . SER A 128 ? 0.76451 0.51553 0.60824 -0.03912 0.01180  0.08991  147 SER A N   
820  C CA  . SER A 128 ? 0.84998 0.61174 0.73957 -0.04499 0.01885  0.07296  147 SER A CA  
821  C C   . SER A 128 ? 0.82335 0.59850 0.72820 -0.02996 0.00610  0.06832  147 SER A C   
822  O O   . SER A 128 ? 0.83010 0.63378 0.75940 -0.02987 0.00083  0.05047  147 SER A O   
823  C CB  . SER A 128 ? 0.81860 0.54145 0.72213 -0.05539 0.04594  0.07259  147 SER A CB  
824  O OG  . SER A 128 ? 0.88211 0.56016 0.76061 -0.04580 0.05465  0.09310  147 SER A OG  
825  N N   . GLU A 129 ? 0.80794 0.56252 0.69596 -0.01426 0.00057  0.08331  148 GLU A N   
826  C CA  A GLU A 129 ? 0.84237 0.61137 0.75350 0.00327  -0.00837 0.07572  148 GLU A CA  
827  C CA  B GLU A 129 ? 0.85973 0.62875 0.77088 0.00326  -0.00836 0.07569  148 GLU A CA  
828  C C   . GLU A 129 ? 0.73796 0.56358 0.66296 0.00705  -0.02029 0.06955  148 GLU A C   
829  O O   . GLU A 129 ? 0.74191 0.59311 0.68670 0.01360  -0.01704 0.05315  148 GLU A O   
830  C CB  A GLU A 129 ? 0.84756 0.58321 0.74458 0.02246  -0.01600 0.09545  148 GLU A CB  
831  C CB  B GLU A 129 ? 0.89965 0.63527 0.79685 0.02247  -0.01595 0.09535  148 GLU A CB  
832  C CG  A GLU A 129 ? 0.99244 0.66349 0.87215 0.01921  0.00110  0.11047  148 GLU A CG  
833  C CG  B GLU A 129 ? 0.92504 0.59620 0.80759 0.01961  0.00128  0.10925  148 GLU A CG  
834  C CD  A GLU A 129 ? 1.07252 0.70412 0.93028 0.04220  -0.01061 0.13632  148 GLU A CD  
835  C CD  B GLU A 129 ? 0.96998 0.62576 0.89632 0.01282  0.01638  0.08670  148 GLU A CD  
836  O OE1 A GLU A 129 ? 1.07016 0.65425 0.94287 0.04853  0.00020  0.14250  148 GLU A OE1 
837  O OE1 B GLU A 129 ? 0.91095 0.59103 0.86783 0.02460  0.00814  0.06344  148 GLU A OE1 
838  O OE2 A GLU A 129 ? 0.99601 0.64234 0.82599 0.05481  -0.03413 0.14976  148 GLU A OE2 
839  O OE2 B GLU A 129 ? 1.09120 0.71169 1.02435 -0.00426 0.03735  0.08957  148 GLU A OE2 
840  N N   . ALA A 130 ? 0.73922 0.58314 0.65363 0.00286  -0.03229 0.08181  149 ALA A N   
841  C CA  . ALA A 130 ? 0.77733 0.67238 0.71618 0.00202  -0.03920 0.08044  149 ALA A CA  
842  C C   . ALA A 130 ? 0.69663 0.61076 0.63867 -0.01127 -0.02982 0.07111  149 ALA A C   
843  O O   . ALA A 130 ? 0.67568 0.62436 0.63148 -0.00745 -0.02474 0.06840  149 ALA A O   
844  C CB  . ALA A 130 ? 0.69356 0.59852 0.63055 -0.00187 -0.05816 0.09167  149 ALA A CB  
845  N N   . LEU A 131 ? 0.69478 0.58705 0.62361 -0.02497 -0.02657 0.06739  150 LEU A N   
846  C CA  . LEU A 131 ? 0.70790 0.61536 0.64281 -0.03382 -0.02470 0.05826  150 LEU A CA  
847  C C   . LEU A 131 ? 0.68655 0.59819 0.62296 -0.02474 -0.02070 0.04039  150 LEU A C   
848  O O   . LEU A 131 ? 0.70192 0.63749 0.63222 -0.02272 -0.02352 0.03547  150 LEU A O   
849  C CB  . LEU A 131 ? 0.68547 0.57025 0.62051 -0.04735 -0.02166 0.05359  150 LEU A CB  
850  C CG  . LEU A 131 ? 0.68170 0.56193 0.60966 -0.05540 -0.02551 0.06280  150 LEU A CG  
851  C CD1 . LEU A 131 ? 0.66266 0.51773 0.59088 -0.06494 -0.01259 0.05458  150 LEU A CD1 
852  C CD2 . LEU A 131 ? 0.58188 0.49079 0.52548 -0.05992 -0.03662 0.06880  150 LEU A CD2 
853  N N   . LYS A 132 ? 0.72633 0.61049 0.66694 -0.01784 -0.01533 0.03020  151 LYS A N   
854  C CA  . LYS A 132 ? 0.77557 0.66016 0.72058 -0.00672 -0.01428 0.00597  151 LYS A CA  
855  C C   . LYS A 132 ? 0.80249 0.72049 0.74012 0.01055  -0.01034 0.00576  151 LYS A C   
856  O O   . LYS A 132 ? 0.83924 0.77614 0.76134 0.01900  -0.00926 -0.01177 151 LYS A O   
857  C CB  . LYS A 132 ? 0.78851 0.62929 0.75011 -0.00383 -0.00837 -0.00257 151 LYS A CB  
858  C CG  . LYS A 132 ? 0.85730 0.66746 0.83737 -0.02210 -0.00349 -0.00720 151 LYS A CG  
859  C CD  . LYS A 132 ? 0.91745 0.67744 0.91559 -0.02140 0.00854  -0.00492 151 LYS A CD  
860  C CE  . LYS A 132 ? 0.89298 0.64401 0.90804 -0.00490 0.00384  -0.02965 151 LYS A CE  
861  N NZ  . LYS A 132 ? 1.15406 0.84910 1.18860 -0.00192 0.01496  -0.01940 151 LYS A NZ  
862  N N   . ARG A 133 ? 0.69380 0.62129 0.64260 0.01738  -0.00799 0.02388  152 ARG A N   
863  C CA  . ARG A 133 ? 0.74487 0.71238 0.70333 0.03225  0.00145  0.02484  152 ARG A CA  
864  C C   . ARG A 133 ? 0.73570 0.74013 0.68086 0.02391  0.00758  0.03593  152 ARG A C   
865  O O   . ARG A 133 ? 0.76840 0.80324 0.70533 0.03544  0.02388  0.03161  152 ARG A O   
866  C CB  . ARG A 133 ? 0.79912 0.77426 0.78795 0.03986  -0.00362 0.04163  152 ARG A CB  
867  C CG  . ARG A 133 ? 0.82626 0.76331 0.82521 0.05537  -0.00920 0.03589  152 ARG A CG  
868  C CD  . ARG A 133 ? 0.88602 0.84466 0.92280 0.07363  -0.01619 0.04566  152 ARG A CD  
869  N NE  . ARG A 133 ? 1.00056 0.91498 1.04377 0.09095  -0.02648 0.04706  152 ARG A NE  
870  C CZ  . ARG A 133 ? 1.06659 0.98669 1.14074 0.11030  -0.04261 0.05800  152 ARG A CZ  
871  N NH1 . ARG A 133 ? 1.18050 1.05289 1.25619 0.12866  -0.05317 0.06344  152 ARG A NH1 
872  N NH2 . ARG A 133 ? 0.97628 0.95007 1.08712 0.11152  -0.05021 0.06464  152 ARG A NH2 
873  N N   . PHE A 134 ? 0.79927 0.79825 0.74013 0.00540  -0.00245 0.05100  153 PHE A N   
874  C CA  . PHE A 134 ? 0.77602 0.79990 0.70736 -0.00304 0.00125  0.06704  153 PHE A CA  
875  C C   . PHE A 134 ? 0.81341 0.83198 0.70601 -0.00044 -0.00274 0.05486  153 PHE A C   
876  O O   . PHE A 134 ? 0.82980 0.86319 0.70437 -0.00387 -0.00093 0.07216  153 PHE A O   
877  C CB  . PHE A 134 ? 0.72350 0.73959 0.67270 -0.02147 -0.01116 0.08472  153 PHE A CB  
878  C CG  . PHE A 134 ? 0.65104 0.69056 0.63837 -0.02568 -0.01003 0.10184  153 PHE A CG  
879  C CD1 . PHE A 134 ? 0.75373 0.82524 0.76019 -0.03085 0.00320  0.12133  153 PHE A CD1 
880  C CD2 . PHE A 134 ? 0.64925 0.67762 0.65505 -0.02449 -0.02355 0.09933  153 PHE A CD2 
881  C CE1 . PHE A 134 ? 0.82996 0.92655 0.89064 -0.03766 0.00290  0.13398  153 PHE A CE1 
882  C CE2 . PHE A 134 ? 0.70992 0.76297 0.75930 -0.02761 -0.03102 0.10953  153 PHE A CE2 
883  C CZ  . PHE A 134 ? 0.71031 0.79978 0.79595 -0.03573 -0.01792 0.12485  153 PHE A CZ  
884  N N   . ASP A 135 ? 0.88282 0.87882 0.76523 0.00598  -0.01085 0.02625  154 ASP A N   
885  C CA  . ASP A 135 ? 0.94412 0.93468 0.79779 0.00874  -0.02553 0.00799  154 ASP A CA  
886  C C   . ASP A 135 ? 0.86247 0.84882 0.72391 -0.00620 -0.04080 0.02410  154 ASP A C   
887  O O   . ASP A 135 ? 0.95020 0.94641 0.78321 -0.00254 -0.05097 0.03194  154 ASP A O   
888  C CB  . ASP A 135 ? 1.02015 1.03439 0.82349 0.02670  -0.01670 0.00381  154 ASP A CB  
889  C CG  . ASP A 135 ? 0.98151 1.00591 0.78464 0.04396  0.00481  -0.01202 154 ASP A CG  
890  O OD1 . ASP A 135 ? 1.03045 1.03189 0.85796 0.04823  -0.00011 -0.03824 154 ASP A OD1 
891  O OD2 . ASP A 135 ? 0.96521 1.01971 0.74963 0.05357  0.02932  0.00279  154 ASP A OD2 
892  N N   . ALA A 136 ? 0.64436 0.61358 0.54117 -0.02058 -0.04190 0.02977  155 ALA A N   
893  C CA  . ALA A 136 ? 0.85488 0.82093 0.76761 -0.03337 -0.05103 0.04455  155 ALA A CA  
894  C C   . ALA A 136 ? 0.80494 0.75528 0.74137 -0.03913 -0.06455 0.02356  155 ALA A C   
895  O O   . ALA A 136 ? 0.76385 0.69817 0.71810 -0.04096 -0.06091 0.00250  155 ALA A O   
896  C CB  . ALA A 136 ? 0.71833 0.67798 0.65148 -0.04372 -0.04278 0.06053  155 ALA A CB  
897  N N   . LEU A 137 ? 0.77470 0.72976 0.72025 -0.04183 -0.07958 0.03056  156 LEU A N   
898  C CA  . LEU A 137 ? 0.60276 0.54946 0.59113 -0.04876 -0.09026 0.01423  156 LEU A CA  
899  C C   . LEU A 137 ? 0.67629 0.61690 0.68654 -0.05818 -0.08428 0.03049  156 LEU A C   
900  O O   . LEU A 137 ? 0.72623 0.67236 0.72479 -0.05647 -0.09065 0.05293  156 LEU A O   
901  C CB  . LEU A 137 ? 0.65545 0.61350 0.64359 -0.03838 -0.12092 0.00245  156 LEU A CB  
902  C CG  . LEU A 137 ? 0.82087 0.78572 0.77298 -0.02448 -0.13507 -0.01839 156 LEU A CG  
903  C CD1 . LEU A 137 ? 0.72425 0.69882 0.67277 -0.01208 -0.17470 -0.03116 156 LEU A CD1 
904  C CD2 . LEU A 137 ? 0.71045 0.66276 0.69279 -0.03057 -0.12421 -0.04816 156 LEU A CD2 
905  N N   . VAL A 138 ? 0.64091 0.56736 0.68164 -0.06788 -0.06939 0.01913  157 VAL A N   
906  C CA  . VAL A 138 ? 0.68112 0.59851 0.73581 -0.07460 -0.06146 0.02639  157 VAL A CA  
907  C C   . VAL A 138 ? 0.58684 0.50829 0.69115 -0.07431 -0.07197 0.01411  157 VAL A C   
908  O O   . VAL A 138 ? 0.67374 0.59654 0.81808 -0.07746 -0.06514 -0.00693 157 VAL A O   
909  C CB  . VAL A 138 ? 0.74836 0.64575 0.79200 -0.08140 -0.03593 0.02237  157 VAL A CB  
910  C CG1 . VAL A 138 ? 0.65766 0.54456 0.70592 -0.08537 -0.02996 0.02236  157 VAL A CG1 
911  C CG2 . VAL A 138 ? 0.69932 0.59411 0.70234 -0.07760 -0.03287 0.03522  157 VAL A CG2 
912  N N   . ASP A 139 ? 0.69863 0.62183 0.81024 -0.07047 -0.08814 0.02789  158 ASP A N   
913  C CA  . ASP A 139 ? 0.69894 0.62326 0.86385 -0.06674 -0.10036 0.01831  158 ASP A CA  
914  C C   . ASP A 139 ? 0.65598 0.56457 0.83817 -0.07299 -0.08059 0.01086  158 ASP A C   
915  O O   . ASP A 139 ? 0.70182 0.59916 0.86628 -0.07493 -0.08391 0.02547  158 ASP A O   
916  C CB  . ASP A 139 ? 0.69102 0.61795 0.85108 -0.05596 -0.13113 0.04092  158 ASP A CB  
917  C CG  . ASP A 139 ? 0.66826 0.59753 0.88971 -0.04639 -0.15297 0.03064  158 ASP A CG  
918  O OD1 . ASP A 139 ? 0.70391 0.63183 0.97864 -0.05012 -0.13748 0.00742  158 ASP A OD1 
919  O OD2 . ASP A 139 ? 0.66974 0.60210 0.88447 -0.03279 -0.18536 0.04631  158 ASP A OD2 
920  N N   . PRO A 140 ? 0.66873 0.57578 0.88591 -0.07638 -0.05806 -0.01335 159 PRO A N   
921  C CA  . PRO A 140 ? 0.66523 0.55568 0.88635 -0.07872 -0.03680 -0.02527 159 PRO A CA  
922  C C   . PRO A 140 ? 0.74027 0.62613 1.00552 -0.07106 -0.05502 -0.02833 159 PRO A C   
923  O O   . PRO A 140 ? 0.76484 0.63321 1.02742 -0.07137 -0.04312 -0.04068 159 PRO A O   
924  C CB  . PRO A 140 ? 0.62319 0.51666 0.87397 -0.08297 -0.00176 -0.04806 159 PRO A CB  
925  C CG  . PRO A 140 ? 0.62966 0.54652 0.93183 -0.08189 -0.01728 -0.05335 159 PRO A CG  
926  C CD  . PRO A 140 ? 0.53623 0.45600 0.79107 -0.07913 -0.04698 -0.03229 159 PRO A CD  
927  N N   . SER A 141 ? 0.63043 0.52750 0.93339 -0.06204 -0.08573 -0.01873 160 SER A N   
928  C CA  . SER A 141 ? 0.76886 0.65451 1.11606 -0.05252 -0.10614 -0.01585 160 SER A CA  
929  C C   . SER A 141 ? 0.70912 0.57581 1.02223 -0.05508 -0.12394 0.01577  160 SER A C   
930  O O   . SER A 141 ? 0.66427 0.51231 1.01450 -0.04923 -0.13949 0.02186  160 SER A O   
931  C CB  . SER A 141 ? 0.55919 0.46173 0.96478 -0.03800 -0.13593 -0.01671 160 SER A CB  
932  O OG  . SER A 141 ? 0.64258 0.55278 1.00583 -0.03384 -0.16382 0.01000  160 SER A OG  
933  N N   . LEU A 142 ? 0.75496 0.62548 1.00869 -0.06382 -0.11986 0.03565  161 LEU A N   
934  C CA  . LEU A 142 ? 0.72689 0.58630 0.95944 -0.06892 -0.13046 0.06766  161 LEU A CA  
935  C C   . LEU A 142 ? 0.72906 0.58052 0.93981 -0.08165 -0.11548 0.06012  161 LEU A C   
936  O O   . LEU A 142 ? 0.71825 0.57462 0.90079 -0.08469 -0.09772 0.03982  161 LEU A O   
937  C CB  . LEU A 142 ? 0.64106 0.51668 0.82909 -0.06612 -0.13815 0.09732  161 LEU A CB  
938  C CG  . LEU A 142 ? 0.69514 0.57702 0.88626 -0.05033 -0.16330 0.10911  161 LEU A CG  
939  C CD1 . LEU A 142 ? 0.64611 0.54185 0.77347 -0.04648 -0.16551 0.13335  161 LEU A CD1 
940  C CD2 . LEU A 142 ? 0.57495 0.43330 0.80481 -0.04233 -0.18477 0.12988  161 LEU A CD2 
941  N N   . LYS A 143 ? 0.68264 0.52003 0.90907 -0.08872 -0.12522 0.07876  162 LYS A N   
942  C CA  . LYS A 143 ? 0.66609 0.49879 0.88474 -0.10072 -0.12159 0.07160  162 LYS A CA  
943  C C   . LYS A 143 ? 0.67363 0.50950 0.90653 -0.11070 -0.12778 0.10893  162 LYS A C   
944  O O   . LYS A 143 ? 0.79745 0.61660 1.06538 -0.11110 -0.13725 0.13319  162 LYS A O   
945  C CB  . LYS A 143 ? 0.73682 0.54322 0.98641 -0.10150 -0.12610 0.03805  162 LYS A CB  
946  C CG  . LYS A 143 ? 0.72937 0.53445 0.94018 -0.09754 -0.11042 -0.00002 162 LYS A CG  
947  C CD  . LYS A 143 ? 0.73825 0.51575 0.96824 -0.09632 -0.11584 -0.03641 162 LYS A CD  
948  C CE  . LYS A 143 ? 0.78334 0.55583 0.95342 -0.09065 -0.09781 -0.07065 162 LYS A CE  
949  N NZ  . LYS A 143 ? 0.93054 0.71437 1.08277 -0.08283 -0.06777 -0.07492 162 LYS A NZ  
950  N N   . TYR A 144 ? 0.68370 0.54051 0.89365 -0.11783 -0.12019 0.11580  163 TYR A N   
951  C CA  . TYR A 144 ? 0.79817 0.66620 1.03105 -0.12925 -0.11751 0.14957  163 TYR A CA  
952  C C   . TYR A 144 ? 0.79240 0.66210 1.01344 -0.12368 -0.11134 0.19098  163 TYR A C   
953  O O   . TYR A 144 ? 0.83797 0.69495 1.09232 -0.13170 -0.11047 0.22449  163 TYR A O   
954  C CB  . TYR A 144 ? 0.64112 0.48881 0.93779 -0.14399 -0.13073 0.14356  163 TYR A CB  
955  C CG  . TYR A 144 ? 0.74243 0.58327 1.03497 -0.14446 -0.14321 0.09675  163 TYR A CG  
956  C CD1 . TYR A 144 ? 0.72553 0.58935 1.00218 -0.14742 -0.14599 0.08594  163 TYR A CD1 
957  C CD2 . TYR A 144 ? 0.70097 0.51165 1.00116 -0.13868 -0.15267 0.06265  163 TYR A CD2 
958  C CE1 . TYR A 144 ? 0.72425 0.57778 0.98020 -0.14390 -0.16159 0.04543  163 TYR A CE1 
959  C CE2 . TYR A 144 ? 0.64515 0.44674 0.92310 -0.13597 -0.16171 0.01923  163 TYR A CE2 
960  C CZ  . TYR A 144 ? 0.77309 0.59445 1.02281 -0.13830 -0.16802 0.01232  163 TYR A CZ  
961  O OH  . TYR A 144 ? 0.72473 0.53323 0.93676 -0.13200 -0.18119 -0.02838 163 TYR A OH  
962  N N   . ALA A 145 ? 0.82514 0.70760 0.99572 -0.10913 -0.10804 0.18857  164 ALA A N   
963  C CA  . ALA A 145 ? 0.82172 0.70557 0.96180 -0.09866 -0.10808 0.22249  164 ALA A CA  
964  C C   . ALA A 145 ? 0.72689 0.63345 0.84024 -0.10229 -0.08585 0.25488  164 ALA A C   
965  O O   . ALA A 145 ? 0.72479 0.62562 0.81395 -0.09694 -0.08072 0.29390  164 ALA A O   
966  C CB  . ALA A 145 ? 0.79036 0.68236 0.89205 -0.08181 -0.11743 0.20105  164 ALA A CB  
967  N N   . ALA A 146 ? 0.79420 0.72595 0.91027 -0.10908 -0.07137 0.24084  165 ALA A N   
968  C CA  . ALA A 146 ? 0.84879 0.80873 0.95032 -0.11063 -0.04520 0.26660  165 ALA A CA  
969  C C   . ALA A 146 ? 0.83041 0.79101 0.99358 -0.12981 -0.03140 0.29852  165 ALA A C   
970  O O   . ALA A 146 ? 0.81705 0.80347 0.97964 -0.13279 -0.00216 0.32510  165 ALA A O   
971  C CB  . ALA A 146 ? 0.92663 0.91468 1.01805 -0.10701 -0.03720 0.23829  165 ALA A CB  
972  N N   . GLY A 147 ? 0.87601 0.80921 1.09846 -0.14309 -0.04918 0.29449  166 GLY A N   
973  C CA  . GLY A 147 ? 0.83710 0.76770 1.13514 -0.16479 -0.03884 0.32083  166 GLY A CA  
974  C C   . GLY A 147 ? 0.82933 0.79679 1.17822 -0.17704 -0.03278 0.30206  166 GLY A C   
975  O O   . GLY A 147 ? 0.90513 0.88919 1.23292 -0.16845 -0.04510 0.26440  166 GLY A O   
976  N N   . LYS A 148 ? 0.81970 0.79922 1.24235 -0.19713 -0.01382 0.33143  167 LYS A N   
977  C CA  . LYS A 148 ? 0.74564 0.76588 1.23808 -0.20931 -0.01153 0.31457  167 LYS A CA  
978  C C   . LYS A 148 ? 0.79238 0.85959 1.24431 -0.19502 0.01828  0.32010  167 LYS A C   
979  O O   . LYS A 148 ? 0.85701 0.92699 1.24525 -0.18358 0.04882  0.35051  167 LYS A O   
980  C CB  . LYS A 148 ? 0.63747 0.66026 1.22521 -0.23025 0.00160  0.33444  167 LYS A CB  
981  N N   . PRO A 149 ? 0.70607 0.80823 1.19002 -0.19224 0.00705  0.28866  168 PRO A N   
982  C CA  . PRO A 149 ? 0.70450 0.85155 1.16614 -0.17711 0.03587  0.29109  168 PRO A CA  
983  C C   . PRO A 149 ? 0.82727 1.00786 1.34091 -0.18905 0.08625  0.33405  168 PRO A C   
984  O O   . PRO A 149 ? 0.85602 1.04961 1.47563 -0.21363 0.09177  0.34803  168 PRO A O   
985  C CB  . PRO A 149 ? 0.72758 0.89966 1.23676 -0.17365 0.00492  0.25145  168 PRO A CB  
986  C CG  . PRO A 149 ? 0.67591 0.80604 1.17652 -0.17811 -0.04166 0.22195  168 PRO A CG  
987  C CD  . PRO A 149 ? 0.76481 0.86243 1.29359 -0.19733 -0.03714 0.24580  168 PRO A CD  
988  N N   . ALA A 150 ? 0.88099 1.07465 1.32029 -0.17175 0.12495  0.35382  169 ALA A N   
989  C CA  . ALA A 150 ? 1.04561 1.26884 1.51085 -0.17920 0.18351  0.39831  169 ALA A CA  
990  C C   . ALA A 150 ? 1.14691 1.40739 1.55124 -0.15300 0.21866  0.39014  169 ALA A C   
991  O O   . ALA A 150 ? 1.29172 1.54745 1.61029 -0.13979 0.25566  0.41661  169 ALA A O   
992  C CB  . ALA A 150 ? 1.01936 1.19640 1.43068 -0.18408 0.19781  0.44176  169 ALA A CB  
993  N N   . CYS A 151 ? 0.93200 1.22753 1.37719 -0.14241 0.20502  0.35128  170 CYS A N   
994  C CA  . CYS A 151 ? 0.98088 1.31177 1.38619 -0.11625 0.23746  0.33761  170 CYS A CA  
995  C C   . CYS A 151 ? 0.90847 1.30243 1.41410 -0.12354 0.29104  0.35526  170 CYS A C   
996  O O   . CYS A 151 ? 1.04889 1.46245 1.51411 -0.11495 0.35030  0.38066  170 CYS A O   
997  C CB  . CYS A 151 ? 0.83002 1.15872 1.22260 -0.09647 0.19483  0.28834  170 CYS A CB  
998  S SG  . CYS A 151 ? 0.88966 1.15059 1.19177 -0.09249 0.13717  0.26612  170 CYS A SG  
999  N N   . GLU B 4   ? 1.50149 1.39137 1.35309 0.25555  -0.21018 0.22422  23  GLU B N   
1000 C CA  . GLU B 4   ? 1.45393 1.34463 1.26999 0.21448  -0.22190 0.19391  23  GLU B CA  
1001 C C   . GLU B 4   ? 1.40340 1.24247 1.22164 0.19227  -0.18590 0.16472  23  GLU B C   
1002 O O   . GLU B 4   ? 1.38562 1.20074 1.23726 0.20350  -0.15640 0.16336  23  GLU B O   
1003 C CB  . GLU B 4   ? 1.33398 1.30519 1.18996 0.19530  -0.25512 0.17858  23  GLU B CB  
1004 N N   . LYS B 5   ? 1.33912 1.16375 1.12212 0.16026  -0.18757 0.14124  24  LYS B N   
1005 C CA  . LYS B 5   ? 1.22439 1.00934 1.01137 0.14147  -0.15764 0.11631  24  LYS B CA  
1006 C C   . LYS B 5   ? 1.02565 0.82011 0.79423 0.10883  -0.16755 0.09324  24  LYS B C   
1007 O O   . LYS B 5   ? 1.19341 0.96044 0.90581 0.09508  -0.16897 0.09034  24  LYS B O   
1008 C CB  . LYS B 5   ? 1.26166 0.97895 1.00829 0.14772  -0.12769 0.12036  24  LYS B CB  
1009 C CG  . LYS B 5   ? 1.18788 0.87849 0.95655 0.13558  -0.09656 0.09791  24  LYS B CG  
1010 C CD  . LYS B 5   ? 0.96090 0.66305 0.78212 0.14923  -0.08065 0.09853  24  LYS B CD  
1011 C CE  . LYS B 5   ? 0.97834 0.63502 0.78515 0.16908  -0.05309 0.11301  24  LYS B CE  
1012 N NZ  . LYS B 5   ? 1.04959 0.71068 0.90498 0.17574  -0.02944 0.10725  24  LYS B NZ  
1013 N N   . THR B 6   ? 0.92040 0.74625 0.73303 0.09593  -0.16885 0.07666  25  THR B N   
1014 C CA  . THR B 6   ? 0.91573 0.75027 0.71769 0.06618  -0.17340 0.05556  25  THR B CA  
1015 C C   . THR B 6   ? 0.86221 0.66003 0.66889 0.05542  -0.14528 0.03957  25  THR B C   
1016 O O   . THR B 6   ? 0.79235 0.58770 0.63300 0.06673  -0.13105 0.03995  25  THR B O   
1017 C CB  . THR B 6   ? 0.80919 0.70404 0.65559 0.05880  -0.19212 0.04907  25  THR B CB  
1018 O OG1 . THR B 6   ? 0.95188 0.89277 0.80657 0.07445  -0.22018 0.06711  25  THR B OG1 
1019 C CG2 . THR B 6   ? 0.76908 0.66871 0.59774 0.02473  -0.19319 0.02594  25  THR B CG2 
1020 N N   . VAL B 7   ? 0.83882 0.61082 0.61191 0.03330  -0.13665 0.02562  26  VAL B N   
1021 C CA  . VAL B 7   ? 0.83618 0.57611 0.61589 0.02666  -0.11001 0.01414  26  VAL B CA  
1022 C C   . VAL B 7   ? 0.89596 0.65669 0.70387 0.01412  -0.10809 0.00313  26  VAL B C   
1023 O O   . VAL B 7   ? 0.95215 0.72542 0.74721 -0.00666 -0.11560 -0.00744 26  VAL B O   
1024 C CB  . VAL B 7   ? 0.82273 0.51474 0.55375 0.01173  -0.09316 0.00605  26  VAL B CB  
1025 C CG1 . VAL B 7   ? 0.85278 0.51882 0.60011 0.00770  -0.06543 -0.00361 26  VAL B CG1 
1026 C CG2 . VAL B 7   ? 0.83833 0.50071 0.53956 0.02421  -0.08806 0.01657  26  VAL B CG2 
1027 N N   . TYR B 8   ? 0.77225 0.53600 0.61497 0.02459  -0.09629 0.00451  27  TYR B N   
1028 C CA  . TYR B 8   ? 0.78552 0.55614 0.64839 0.01589  -0.08744 -0.00259 27  TYR B CA  
1029 C C   . TYR B 8   ? 0.78249 0.52225 0.64638 0.02156  -0.06359 -0.00159 27  TYR B C   
1030 O O   . TYR B 8   ? 0.84096 0.56287 0.69828 0.03075  -0.05576 0.00179  27  TYR B O   
1031 C CB  . TYR B 8   ? 0.66603 0.47441 0.56809 0.02471  -0.09693 0.00138  27  TYR B CB  
1032 C CG  . TYR B 8   ? 0.71086 0.55757 0.62486 0.02407  -0.11963 0.00296  27  TYR B CG  
1033 C CD1 . TYR B 8   ? 0.71294 0.58475 0.63098 0.00460  -0.12860 -0.00822 27  TYR B CD1 
1034 C CD2 . TYR B 8   ? 0.69780 0.55771 0.62266 0.04335  -0.12975 0.01561  27  TYR B CD2 
1035 C CE1 . TYR B 8   ? 0.65257 0.57212 0.58986 0.00610  -0.15250 -0.00565 27  TYR B CE1 
1036 C CE2 . TYR B 8   ? 0.76353 0.66234 0.70524 0.04884  -0.15036 0.02205  27  TYR B CE2 
1037 C CZ  . TYR B 8   ? 0.76029 0.69417 0.71067 0.03108  -0.16441 0.01200  27  TYR B CZ  
1038 O OH  . TYR B 8   ? 0.73095 0.71589 0.70613 0.03843  -0.18803 0.01938  27  TYR B OH  
1039 N N   . GLY B 9   ? 0.70084 0.43517 0.57490 0.01716  -0.05026 -0.00359 28  GLY B N   
1040 C CA  . GLY B 9   ? 0.71642 0.42642 0.59483 0.02710  -0.02845 0.00238  28  GLY B CA  
1041 C C   . GLY B 9   ? 0.71253 0.44631 0.61824 0.04413  -0.03046 0.01338  28  GLY B C   
1042 O O   . GLY B 9   ? 0.74556 0.50972 0.66612 0.04644  -0.04538 0.01392  28  GLY B O   
1043 N N   . LEU B 10  ? 0.73572 0.45555 0.64706 0.05654  -0.01373 0.02309  29  LEU B N   
1044 C CA  . LEU B 10  ? 0.72161 0.46658 0.65091 0.07247  -0.01709 0.03566  29  LEU B CA  
1045 C C   . LEU B 10  ? 0.68969 0.43902 0.61695 0.06480  -0.01737 0.03551  29  LEU B C   
1046 O O   . LEU B 10  ? 0.74315 0.51982 0.68000 0.07001  -0.02694 0.03961  29  LEU B O   
1047 C CB  . LEU B 10  ? 0.66151 0.39343 0.59695 0.09059  0.00014  0.05071  29  LEU B CB  
1048 C CG  . LEU B 10  ? 0.76614 0.50557 0.71633 0.10147  0.00189  0.05152  29  LEU B CG  
1049 C CD1 . LEU B 10  ? 0.59633 0.32904 0.56132 0.12347  0.01955  0.06996  29  LEU B CD1 
1050 C CD2 . LEU B 10  ? 0.69519 0.48039 0.66174 0.10419  -0.01850 0.04702  29  LEU B CD2 
1051 N N   . ASN B 11  ? 0.75396 0.47519 0.66777 0.04907  -0.00338 0.02791  30  ASN B N   
1052 C CA  . ASN B 11  ? 0.74059 0.46213 0.65432 0.03713  0.00215  0.02327  30  ASN B CA  
1053 C C   . ASN B 11  ? 0.76827 0.49187 0.67836 0.01116  -0.00198 0.00280  30  ASN B C   
1054 O O   . ASN B 11  ? 0.83119 0.53543 0.72519 0.00005  0.00292  -0.00583 30  ASN B O   
1055 C CB  . ASN B 11  ? 0.82003 0.50322 0.72117 0.04285  0.03170  0.03478  30  ASN B CB  
1056 C CG  . ASN B 11  ? 0.77953 0.47194 0.68359 0.07104  0.03072  0.05903  30  ASN B CG  
1057 O OD1 . ASN B 11  ? 0.89825 0.57644 0.80267 0.08901  0.04082  0.07322  30  ASN B OD1 
1058 N ND2 . ASN B 11  ? 0.88871 0.60873 0.79584 0.07443  0.01872  0.06346  30  ASN B ND2 
1059 N N   . GLU B 12  ? 0.81162 0.56341 0.73759 0.00079  -0.01169 -0.00565 31  GLU B N   
1060 C CA  . GLU B 12  ? 0.81668 0.58674 0.74728 -0.02361 -0.01988 -0.02504 31  GLU B CA  
1061 C C   . GLU B 12  ? 0.80312 0.58239 0.75006 -0.03863 -0.00825 -0.03536 31  GLU B C   
1062 O O   . GLU B 12  ? 0.75400 0.52326 0.70436 -0.02855 0.00436  -0.02570 31  GLU B O   
1063 C CB  . GLU B 12  ? 0.65760 0.46950 0.60269 -0.01793 -0.05122 -0.02493 31  GLU B CB  
1064 C CG  . GLU B 12  ? 0.75868 0.55682 0.68381 -0.00682 -0.05908 -0.01747 31  GLU B CG  
1065 C CD  . GLU B 12  ? 0.80773 0.58116 0.70165 -0.02616 -0.05229 -0.02888 31  GLU B CD  
1066 O OE1 . GLU B 12  ? 0.81773 0.59846 0.70790 -0.05121 -0.04944 -0.04545 31  GLU B OE1 
1067 O OE2 . GLU B 12  ? 0.80605 0.55294 0.67898 -0.01928 -0.04730 -0.02398 31  GLU B OE2 
1068 N N   . TYR B 13  ? 0.68230 0.48325 0.63803 -0.06485 -0.01217 -0.05638 32  TYR B N   
1069 C CA  . TYR B 13  ? 0.79029 0.61383 0.77298 -0.08167 -0.00439 -0.07068 32  TYR B CA  
1070 C C   . TYR B 13  ? 0.73616 0.62082 0.75858 -0.07323 -0.03477 -0.06982 32  TYR B C   
1071 O O   . TYR B 13  ? 0.78772 0.70621 0.81561 -0.07138 -0.06205 -0.07006 32  TYR B O   
1072 C CB  . TYR B 13  ? 0.80025 0.62217 0.77831 -0.11886 0.01083  -0.09840 32  TYR B CB  
1073 C CG  . TYR B 13  ? 0.88759 0.64145 0.83460 -0.13059 0.05545  -0.10230 32  TYR B CG  
1074 C CD1 . TYR B 13  ? 0.91343 0.63332 0.85931 -0.12304 0.08457  -0.09338 32  TYR B CD1 
1075 C CD2 . TYR B 13  ? 0.89220 0.61114 0.80809 -0.14945 0.07254  -0.11433 32  TYR B CD2 
1076 C CE1 . TYR B 13  ? 0.93574 0.58750 0.85174 -0.12918 0.12938  -0.09217 32  TYR B CE1 
1077 C CE2 . TYR B 13  ? 1.00534 0.65503 0.89523 -0.15812 0.12045  -0.11649 32  TYR B CE2 
1078 C CZ  . TYR B 13  ? 1.02034 0.63613 0.91124 -0.14569 0.14873  -0.10342 32  TYR B CZ  
1079 O OH  . TYR B 13  ? 1.28904 0.82995 1.15230 -0.14949 0.20012  -0.10059 32  TYR B OH  
1080 N N   . ALA B 14  ? 0.65701 0.55160 0.70438 -0.06646 -0.02727 -0.06678 33  ALA B N   
1081 C CA  . ALA B 14  ? 0.72094 0.66800 0.81271 -0.05797 -0.04680 -0.06641 33  ALA B CA  
1082 C C   . ALA B 14  ? 0.68526 0.65488 0.81294 -0.07892 -0.03121 -0.08555 33  ALA B C   
1083 O O   . ALA B 14  ? 0.74471 0.67702 0.85583 -0.09448 -0.00076 -0.09407 33  ALA B O   
1084 C CB  . ALA B 14  ? 0.56263 0.50085 0.65463 -0.03198 -0.04791 -0.04792 33  ALA B CB  
1085 N N   . ALA B 15  ? 0.74296 0.77317 0.92173 -0.07824 -0.04970 -0.09151 34  ALA B N   
1086 C CA  . ALA B 15  ? 0.65419 0.71688 0.88037 -0.09719 -0.03553 -0.11133 34  ALA B CA  
1087 C C   . ALA B 15  ? 0.52118 0.60797 0.78995 -0.07646 -0.03669 -0.10147 34  ALA B C   
1088 O O   . ALA B 15  ? 0.57327 0.68811 0.85953 -0.05277 -0.06067 -0.08595 34  ALA B O   
1089 C CB  . ALA B 15  ? 0.56107 0.68801 0.82167 -0.11951 -0.05509 -0.13200 34  ALA B CB  
1090 N N   . LEU B 16  ? 0.69481 0.76321 0.97583 -0.08568 -0.00602 -0.11017 35  LEU B N   
1091 C CA  . LEU B 16  ? 0.66098 0.75162 0.98740 -0.07239 0.00056  -0.10681 35  LEU B CA  
1092 C C   . LEU B 16  ? 0.71912 0.88310 1.12183 -0.08277 -0.00751 -0.12394 35  LEU B C   
1093 O O   . LEU B 16  ? 0.77606 0.94816 1.20313 -0.10906 0.01543  -0.14716 35  LEU B O   
1094 C CB  . LEU B 16  ? 0.65910 0.69743 0.95982 -0.08024 0.03812  -0.10962 35  LEU B CB  
1095 C CG  . LEU B 16  ? 0.78703 0.76593 1.01499 -0.06848 0.04102  -0.09082 35  LEU B CG  
1096 C CD1 . LEU B 16  ? 0.89735 0.82942 1.09263 -0.07620 0.07494  -0.09112 35  LEU B CD1 
1097 C CD2 . LEU B 16  ? 0.79332 0.78209 1.01828 -0.04261 0.01815  -0.07300 35  LEU B CD2 
1098 N N   . ASP B 17  ? 0.69312 0.91233 1.13394 -0.06137 -0.03968 -0.11165 36  ASP B N   
1099 C CA  . ASP B 17  ? 0.86976 1.17452 1.38799 -0.06522 -0.05637 -0.12271 36  ASP B CA  
1100 C C   . ASP B 17  ? 0.84672 1.16890 1.42860 -0.07169 -0.02522 -0.13708 36  ASP B C   
1101 O O   . ASP B 17  ? 0.90346 1.18773 1.48381 -0.05735 -0.00151 -0.12775 36  ASP B O   
1102 C CB  . ASP B 17  ? 0.83640 1.18916 1.37992 -0.03108 -0.09345 -0.09742 36  ASP B CB  
1103 C CG  . ASP B 17  ? 0.82024 1.27308 1.44901 -0.02859 -0.11560 -0.10312 36  ASP B CG  
1104 O OD1 . ASP B 17  ? 0.88455 1.38268 1.52654 -0.05940 -0.12597 -0.12735 36  ASP B OD1 
1105 O OD2 . ASP B 17  ? 0.80207 1.29043 1.48637 0.00389  -0.12133 -0.08372 36  ASP B OD2 
1106 N N   . GLY B 18  ? 0.88408 1.26303 1.52065 -0.09758 -0.02205 -0.16340 37  GLY B N   
1107 C CA  . GLY B 18  ? 0.92935 1.32963 1.63265 -0.10923 0.01062  -0.18246 37  GLY B CA  
1108 C C   . GLY B 18  ? 1.10196 1.43951 1.76824 -0.14525 0.05579  -0.20744 37  GLY B C   
1109 O O   . GLY B 18  ? 1.13597 1.50386 1.85833 -0.16996 0.08112  -0.23489 37  GLY B O   
1110 N N   . ILE B 19  ? 1.13722 1.38839 1.71164 -0.14742 0.06805  -0.19732 38  ILE B N   
1111 C CA  . ILE B 19  ? 1.18839 1.37070 1.71601 -0.17642 0.11177  -0.21403 38  ILE B CA  
1112 C C   . ILE B 19  ? 1.22754 1.39767 1.71810 -0.20288 0.10988  -0.22887 38  ILE B C   
1113 O O   . ILE B 19  ? 1.36268 1.47670 1.81898 -0.22937 0.15035  -0.24485 38  ILE B O   
1114 C CB  . ILE B 19  ? 1.14222 1.23721 1.59267 -0.16084 0.13128  -0.19156 38  ILE B CB  
1115 N N   . ASN B 20  ? 1.19772 1.41446 1.69162 -0.19777 0.06841  -0.22465 39  ASN B N   
1116 C CA  . ASN B 20  ? 1.29029 1.49854 1.74832 -0.22524 0.06591  -0.24101 39  ASN B CA  
1117 C C   . ASN B 20  ? 1.22295 1.32539 1.59640 -0.23146 0.10245  -0.23436 39  ASN B C   
1118 O O   . ASN B 20  ? 1.31863 1.38280 1.67577 -0.26344 0.14208  -0.25730 39  ASN B O   
1119 C CB  . ASN B 20  ? 1.27541 1.54775 1.79433 -0.26647 0.07629  -0.28198 39  ASN B CB  
1120 N N   . LEU B 21  ? 1.09028 1.14634 1.41151 -0.19900 0.09029  -0.20146 40  LEU B N   
1121 C CA  . LEU B 21  ? 1.16919 1.13391 1.41365 -0.19564 0.11828  -0.18728 40  LEU B CA  
1122 C C   . LEU B 21  ? 1.09425 1.04431 1.29592 -0.17184 0.08831  -0.16310 40  LEU B C   
1123 O O   . LEU B 21  ? 0.91560 0.89327 1.12789 -0.14436 0.05689  -0.14398 40  LEU B O   
1124 C CB  . LEU B 21  ? 1.12320 1.04039 1.34611 -0.18089 0.14420  -0.17162 40  LEU B CB  
1125 N N   . GLU B 22  ? 1.07200 0.97454 1.22678 -0.18346 0.10338  -0.16533 41  GLU B N   
1126 C CA  . GLU B 22  ? 1.03422 0.91345 1.14678 -0.16354 0.08361  -0.14451 41  GLU B CA  
1127 C C   . GLU B 22  ? 1.07997 0.89155 1.14245 -0.13807 0.10218  -0.11586 41  GLU B C   
1128 O O   . GLU B 22  ? 1.21074 0.96431 1.24268 -0.14598 0.14152  -0.11527 41  GLU B O   
1129 C CB  . GLU B 22  ? 1.17302 1.03897 1.26513 -0.19107 0.09271  -0.16401 41  GLU B CB  
1130 C CG  . GLU B 22  ? 1.09126 0.94077 1.14697 -0.17476 0.07209  -0.14750 41  GLU B CG  
1131 C CD  . GLU B 22  ? 1.18153 1.02786 1.22066 -0.20828 0.07961  -0.17278 41  GLU B CD  
1132 O OE1 . GLU B 22  ? 1.13441 1.04483 1.20670 -0.23538 0.06199  -0.19908 41  GLU B OE1 
1133 O OE2 . GLU B 22  ? 1.29147 1.07353 1.28568 -0.20851 0.10456  -0.16716 41  GLU B OE2 
1134 N N   . VAL B 23  ? 0.89616 0.71709 0.95021 -0.10768 0.07488  -0.09193 42  VAL B N   
1135 C CA  . VAL B 23  ? 0.86517 0.64084 0.87674 -0.08232 0.08305  -0.06448 42  VAL B CA  
1136 C C   . VAL B 23  ? 0.88091 0.64844 0.87013 -0.06487 0.06398  -0.04951 42  VAL B C   
1137 O O   . VAL B 23  ? 0.83812 0.64187 0.84528 -0.06494 0.03641  -0.05518 42  VAL B O   
1138 C CB  . VAL B 23  ? 0.84551 0.64113 0.86800 -0.06668 0.07365  -0.05401 42  VAL B CB  
1139 C CG1 . VAL B 23  ? 0.81806 0.62183 0.86761 -0.08612 0.09587  -0.07181 42  VAL B CG1 
1140 C CG2 . VAL B 23  ? 0.77571 0.62032 0.82720 -0.05288 0.03782  -0.05123 42  VAL B CG2 
1141 N N   . ALA B 24  ? 0.87919 0.59797 0.82919 -0.04948 0.08105  -0.02960 43  ALA B N   
1142 C CA  . ALA B 24  ? 0.84302 0.55471 0.77693 -0.02997 0.06642  -0.01395 43  ALA B CA  
1143 C C   . ALA B 24  ? 0.85858 0.60125 0.79824 -0.00686 0.04009  0.00150  43  ALA B C   
1144 O O   . ALA B 24  ? 0.93739 0.67716 0.86628 0.00289  0.04535  0.01324  43  ALA B O   
1145 C CB  . ALA B 24  ? 0.77053 0.42316 0.66914 -0.01903 0.09674  0.00325  43  ALA B CB  
1146 N N   . ALA B 25  ? 0.70576 0.47626 0.65865 -0.00104 0.01434  -0.00035 44  ALA B N   
1147 C CA  . ALA B 25  ? 0.75636 0.55580 0.71815 0.01527  -0.00656 0.00806  44  ALA B CA  
1148 C C   . ALA B 25  ? 0.76829 0.55853 0.71493 0.03277  -0.01300 0.02164  44  ALA B C   
1149 O O   . ALA B 25  ? 0.80696 0.58086 0.74704 0.03043  -0.01142 0.01922  44  ALA B O   
1150 C CB  . ALA B 25  ? 0.66405 0.50158 0.65685 0.00988  -0.02666 -0.00406 44  ALA B CB  
1151 N N   . LYS B 26  ? 0.77857 0.58109 0.71977 0.04776  -0.01825 0.03389  45  LYS B N   
1152 C CA  . LYS B 26  ? 0.78174 0.59067 0.71974 0.06375  -0.02676 0.04388  45  LYS B CA  
1153 C C   . LYS B 26  ? 0.74149 0.58017 0.69694 0.06274  -0.04365 0.03416  45  LYS B C   
1154 O O   . LYS B 26  ? 0.66560 0.52541 0.62886 0.05902  -0.04723 0.02910  45  LYS B O   
1155 C CB  . LYS B 26  ? 0.77511 0.58911 0.69807 0.07968  -0.02379 0.06253  45  LYS B CB  
1156 C CG  . LYS B 26  ? 0.78246 0.61864 0.71258 0.09525  -0.03478 0.07037  45  LYS B CG  
1157 C CD  . LYS B 26  ? 0.72906 0.58578 0.64676 0.11165  -0.03795 0.09006  45  LYS B CD  
1158 C CE  . LYS B 26  ? 0.76130 0.64142 0.69440 0.12936  -0.04554 0.09957  45  LYS B CE  
1159 N NZ  . LYS B 26  ? 0.77883 0.69667 0.70406 0.14648  -0.05576 0.11950  45  LYS B NZ  
1160 N N   . LEU B 27  ? 0.67916 0.51287 0.63782 0.06469  -0.04896 0.03086  46  LEU B N   
1161 C CA  . LEU B 27  ? 0.68307 0.53367 0.65350 0.06514  -0.05906 0.02343  46  LEU B CA  
1162 C C   . LEU B 27  ? 0.76999 0.63671 0.74259 0.07415  -0.05984 0.02641  46  LEU B C   
1163 O O   . LEU B 27  ? 0.67387 0.53267 0.64404 0.08189  -0.05677 0.03160  46  LEU B O   
1164 C CB  . LEU B 27  ? 0.60089 0.43515 0.56631 0.06154  -0.06270 0.01900  46  LEU B CB  
1165 C CG  . LEU B 27  ? 0.65800 0.49664 0.62831 0.05106  -0.06966 0.01283  46  LEU B CG  
1166 C CD1 . LEU B 27  ? 0.66298 0.49146 0.62856 0.03934  -0.06114 0.00975  46  LEU B CD1 
1167 C CD2 . LEU B 27  ? 0.59606 0.42548 0.55404 0.04918  -0.07776 0.01084  46  LEU B CD2 
1168 N N   . ASP B 28  ? 0.63394 0.52584 0.61336 0.07105  -0.06180 0.02104  47  ASP B N   
1169 C CA  . ASP B 28  ? 0.61838 0.53867 0.60009 0.07399  -0.06394 0.02022  47  ASP B CA  
1170 C C   . ASP B 28  ? 0.67582 0.60656 0.66926 0.06567  -0.06044 0.00401  47  ASP B C   
1171 O O   . ASP B 28  ? 0.60039 0.53876 0.59659 0.05601  -0.05532 -0.00533 47  ASP B O   
1172 C CB  . ASP B 28  ? 0.61622 0.55612 0.58582 0.07247  -0.06553 0.02607  47  ASP B CB  
1173 C CG  . ASP B 28  ? 0.71163 0.69301 0.68101 0.07469  -0.07296 0.02647  47  ASP B CG  
1174 O OD1 . ASP B 28  ? 0.78813 0.78554 0.77378 0.07531  -0.07458 0.01848  47  ASP B OD1 
1175 O OD2 . ASP B 28  ? 0.70162 0.70206 0.65333 0.07472  -0.07705 0.03437  47  ASP B OD2 
1176 N N   . THR B 29  ? 0.55120 0.47700 0.55099 0.06848  -0.05772 -0.00026 48  THR B N   
1177 C CA  . THR B 29  ? 0.68131 0.60858 0.68943 0.06002  -0.04753 -0.01610 48  THR B CA  
1178 C C   . THR B 29  ? 0.67089 0.63854 0.68650 0.04849  -0.04476 -0.03015 48  THR B C   
1179 O O   . THR B 29  ? 0.65718 0.62412 0.67821 0.03597  -0.03005 -0.04750 48  THR B O   
1180 C CB  . THR B 29  ? 0.56066 0.46491 0.56896 0.06414  -0.04095 -0.01788 48  THR B CB  
1181 O OG1 . THR B 29  ? 0.56812 0.49215 0.58541 0.06895  -0.04347 -0.01591 48  THR B OG1 
1182 C CG2 . THR B 29  ? 0.63180 0.49914 0.62518 0.07073  -0.04464 -0.00682 48  THR B CG2 
1183 N N   . GLY B 30  ? 0.56060 0.56346 0.57462 0.05180  -0.05704 -0.02292 49  GLY B N   
1184 C CA  . GLY B 30  ? 0.58042 0.63314 0.59746 0.03843  -0.05969 -0.03639 49  GLY B CA  
1185 C C   . GLY B 30  ? 0.63474 0.69456 0.63569 0.02282  -0.05568 -0.04475 49  GLY B C   
1186 O O   . GLY B 30  ? 0.63813 0.73637 0.63630 0.00412  -0.05378 -0.06255 49  GLY B O   
1187 N N   . ALA B 31  ? 0.62130 0.64738 0.61224 0.02727  -0.05264 -0.03483 50  ALA B N   
1188 C CA  . ALA B 31  ? 0.67337 0.69756 0.65244 0.01227  -0.04270 -0.04376 50  ALA B CA  
1189 C C   . ALA B 31  ? 0.60627 0.59533 0.60101 0.00840  -0.02288 -0.05384 50  ALA B C   
1190 O O   . ALA B 31  ? 0.68050 0.64211 0.68636 0.02276  -0.02463 -0.04347 50  ALA B O   
1191 C CB  . ALA B 31  ? 0.57675 0.59111 0.53752 0.02016  -0.04983 -0.02536 50  ALA B CB  
1192 N N   . LYS B 32  ? 0.62214 0.61242 0.61651 -0.01076 -0.00268 -0.07335 51  LYS B N   
1193 C CA  . LYS B 32  ? 0.65939 0.61497 0.67266 -0.00993 0.02063  -0.07936 51  LYS B CA  
1194 C C   . LYS B 32  ? 0.68659 0.62524 0.70845 -0.00176 0.02191  -0.06780 51  LYS B C   
1195 O O   . LYS B 32  ? 0.60663 0.52506 0.64848 0.01452  0.02145  -0.05636 51  LYS B O   
1196 C CB  . LYS B 32  ? 0.63810 0.59429 0.65075 -0.03460 0.05048  -0.10662 51  LYS B CB  
1197 C CG  . LYS B 32  ? 0.85490 0.82940 0.86599 -0.04762 0.05514  -0.12447 51  LYS B CG  
1198 C CD  . LYS B 32  ? 0.88345 0.85274 0.89305 -0.07742 0.09188  -0.15628 51  LYS B CD  
1199 C CE  . LYS B 32  ? 0.85824 0.86845 0.86269 -0.10105 0.09165  -0.18100 51  LYS B CE  
1200 N NZ  . LYS B 32  ? 1.06554 1.06960 1.08546 -0.08498 0.08445  -0.17350 51  LYS B NZ  
1201 N N   . THR B 33  ? 0.65511 0.60508 0.66133 -0.01356 0.02303  -0.07073 52  THR B N   
1202 C CA  . THR B 33  ? 0.68997 0.62571 0.70720 -0.01140 0.03080  -0.06550 52  THR B CA  
1203 C C   . THR B 33  ? 0.69939 0.63632 0.70831 0.00072  0.00923  -0.04674 52  THR B C   
1204 O O   . THR B 33  ? 0.74551 0.69379 0.73227 0.00544  -0.00834 -0.03732 52  THR B O   
1205 C CB  . THR B 33  ? 0.77795 0.71600 0.77776 -0.03490 0.05196  -0.08195 52  THR B CB  
1206 O OG1 . THR B 33  ? 0.85138 0.81441 0.81020 -0.04534 0.03673  -0.08160 52  THR B OG1 
1207 C CG2 . THR B 33  ? 0.73674 0.66469 0.74757 -0.05032 0.08295  -0.10423 52  THR B CG2 
1208 N N   . ALA B 34  ? 0.66475 0.59040 0.69573 0.00571  0.01379  -0.04209 53  ALA B N   
1209 C CA  . ALA B 34  ? 0.59539 0.51707 0.62108 0.01160  0.00164  -0.02972 53  ALA B CA  
1210 C C   . ALA B 34  ? 0.69276 0.60892 0.69591 -0.00161 0.01419  -0.03221 53  ALA B C   
1211 O O   . ALA B 34  ? 0.68988 0.60405 0.69435 -0.01542 0.03443  -0.04512 53  ALA B O   
1212 C CB  . ALA B 34  ? 0.52045 0.44091 0.58430 0.02057  -0.00129 -0.02649 53  ALA B CB  
1213 N N   . SER B 35  ? 0.67669 0.58416 0.65601 0.00225  0.00660  -0.01962 54  SER B N   
1214 C CA  . SER B 35  ? 0.63935 0.53342 0.58681 -0.00781 0.02000  -0.01741 54  SER B CA  
1215 C C   . SER B 35  ? 0.76644 0.63944 0.71942 -0.00621 0.02606  -0.01132 54  SER B C   
1216 O O   . SER B 35  ? 0.69708 0.56609 0.65755 0.00405  0.01438  -0.00321 54  SER B O   
1217 C CB  . SER B 35  ? 0.60581 0.50739 0.50430 -0.00440 0.00969  -0.00470 54  SER B CB  
1218 O OG  . SER B 35  ? 0.98819 0.91443 0.87821 -0.01445 0.00779  -0.01665 54  SER B OG  
1219 N N   . LEU B 36  ? 0.60720 0.65387 0.72850 0.10234  -0.13960 -0.03481 55  LEU B N   
1220 C CA  . LEU B 36  ? 0.63539 0.66215 0.76183 0.11042  -0.13031 -0.01871 55  LEU B CA  
1221 C C   . LEU B 36  ? 0.64875 0.68533 0.76640 0.12651  -0.13508 0.00363  55  LEU B C   
1222 O O   . LEU B 36  ? 0.68341 0.73449 0.77450 0.12700  -0.14334 0.00590  55  LEU B O   
1223 C CB  . LEU B 36  ? 0.61090 0.61968 0.71977 0.10246  -0.12108 -0.02251 55  LEU B CB  
1224 C CG  . LEU B 36  ? 0.66914 0.66454 0.78353 0.10145  -0.10804 -0.01409 55  LEU B CG  
1225 C CD1 . LEU B 36  ? 0.65100 0.63782 0.79263 0.09434  -0.09718 -0.02177 55  LEU B CD1 
1226 C CD2 . LEU B 36  ? 0.66231 0.66126 0.76006 0.09570  -0.10319 -0.01856 55  LEU B CD2 
1227 N N   . SER B 37  ? 0.60648 0.63281 0.74391 0.14050  -0.12669 0.02069  56  SER B N   
1228 C CA  . SER B 37  ? 0.76397 0.79302 0.89019 0.16148  -0.12638 0.04945  56  SER B CA  
1229 C C   . SER B 37  ? 0.67899 0.67786 0.78107 0.15517  -0.11258 0.05723  56  SER B C   
1230 O O   . SER B 37  ? 0.67623 0.64400 0.78801 0.14273  -0.09361 0.05011  56  SER B O   
1231 C CB  . SER B 37  ? 0.60021 0.61636 0.75493 0.18270  -0.11375 0.06849  56  SER B CB  
1232 O OG  . SER B 37  ? 0.91748 0.94064 1.05844 0.21049  -0.11377 0.10296  56  SER B OG  
1233 N N   . ALA B 38  ? 0.78207 0.79667 0.85279 0.16047  -0.12108 0.06839  57  ALA B N   
1234 C CA  . ALA B 38  ? 0.84016 0.83310 0.88688 0.15313  -0.10805 0.07361  57  ALA B CA  
1235 C C   . ALA B 38  ? 0.85257 0.84460 0.87448 0.17231  -0.10453 0.10571  57  ALA B C   
1236 O O   . ALA B 38  ? 0.81113 0.83330 0.82865 0.19289  -0.11855 0.12342  57  ALA B O   
1237 C CB  . ALA B 38  ? 0.76086 0.76891 0.78698 0.13819  -0.11631 0.05259  57  ALA B CB  
1238 N N   . ARG B 39  ? 0.92100 0.88402 0.92614 0.16560  -0.08473 0.11376  58  ARG B N   
1239 C CA  . ARG B 39  ? 0.98035 0.93436 0.95427 0.18113  -0.07557 0.14549  58  ARG B CA  
1240 C C   . ARG B 39  ? 0.88458 0.84074 0.82962 0.16482  -0.07043 0.13629  58  ARG B C   
1241 O O   . ARG B 39  ? 0.84506 0.79649 0.80224 0.14402  -0.06359 0.11130  58  ARG B O   
1242 C CB  . ARG B 39  ? 0.93285 0.83230 0.91666 0.19038  -0.04273 0.16997  58  ARG B CB  
1243 C CG  . ARG B 39  ? 1.02529 0.88830 1.03071 0.16091  -0.01621 0.14576  58  ARG B CG  
1244 C CD  . ARG B 39  ? 0.97835 0.77962 0.98168 0.16003  0.02620  0.16530  58  ARG B CD  
1245 N NE  . ARG B 39  ? 1.12792 0.89343 1.15024 0.18201  0.04218  0.18495  58  ARG B NE  
1246 C CZ  . ARG B 39  ? 1.21291 0.94938 1.21768 0.21598  0.05733  0.22862  58  ARG B CZ  
1247 N NH1 . ARG B 39  ? 1.03803 0.74063 1.06411 0.24025  0.07556  0.24717  58  ARG B NH1 
1248 N NH2 . ARG B 39  ? 1.24362 0.98518 1.20713 0.22837  0.05661  0.25631  58  ARG B NH2 
1249 N N   . ASP B 40  ? 0.97053 0.94094 0.87692 0.17654  -0.07390 0.15747  59  ASP B N   
1250 C CA  . ASP B 40  ? 0.97827 0.94951 0.85336 0.16366  -0.06498 0.15238  59  ASP B CA  
1251 C C   . ASP B 40  ? 1.00307 0.99707 0.88269 0.14542  -0.07623 0.11564  59  ASP B C   
1252 O O   . ASP B 40  ? 1.00722 0.99133 0.89395 0.13081  -0.06180 0.10016  59  ASP B O   
1253 C CB  . ASP B 40  ? 1.06872 0.99457 0.94757 0.15284  -0.03046 0.16049  59  ASP B CB  
1254 C CG  . ASP B 40  ? 1.12957 1.01587 0.99930 0.17200  -0.00928 0.19940  59  ASP B CG  
1255 O OD1 . ASP B 40  ? 1.11944 0.98117 1.01903 0.17938  -0.00190 0.20419  59  ASP B OD1 
1256 O OD2 . ASP B 40  ? 1.21331 1.08973 1.04416 0.18128  0.00324  0.22653  59  ASP B OD2 
1257 N N   . ILE B 41  ? 0.97888 1.00562 0.85492 0.14738  -0.09951 0.10220  60  ILE B N   
1258 C CA  . ILE B 41  ? 0.88154 0.91898 0.75783 0.13271  -0.10455 0.06946  60  ILE B CA  
1259 C C   . ILE B 41  ? 1.01718 1.06368 0.85383 0.12655  -0.09776 0.06396  60  ILE B C   
1260 O O   . ILE B 41  ? 1.04816 1.12036 0.85111 0.13016  -0.10656 0.07292  60  ILE B O   
1261 C CB  . ILE B 41  ? 0.91182 0.97527 0.79696 0.13105  -0.12482 0.05316  60  ILE B CB  
1262 C CG1 . ILE B 41  ? 0.84775 0.90089 0.77398 0.13639  -0.12823 0.05629  60  ILE B CG1 
1263 C CG2 . ILE B 41  ? 0.84239 0.90410 0.71998 0.11568  -0.12174 0.02084  60  ILE B CG2 
1264 C CD1 . ILE B 41  ? 0.92495 1.00695 0.86430 0.13373  -0.14587 0.04077  60  ILE B CD1 
1265 N N   . LYS B 42  ? 0.96076 0.99249 0.80127 0.11853  -0.08139 0.04965  61  LYS B N   
1266 C CA  . LYS B 42  ? 1.03333 1.06959 0.84097 0.11289  -0.06935 0.04083  61  LYS B CA  
1267 C C   . LYS B 42  ? 0.98892 1.01905 0.80320 0.10796  -0.06254 0.01214  61  LYS B C   
1268 O O   . LYS B 42  ? 0.92351 0.94408 0.76770 0.11157  -0.05420 0.00786  61  LYS B O   
1269 C CB  . LYS B 42  ? 1.05883 1.08367 0.86500 0.11211  -0.04817 0.05519  61  LYS B CB  
1270 C CG  . LYS B 42  ? 1.16482 1.18553 0.94542 0.11754  -0.04490 0.08593  61  LYS B CG  
1271 C CD  . LYS B 42  ? 1.23849 1.24411 1.01415 0.11063  -0.01735 0.09500  61  LYS B CD  
1272 C CE  . LYS B 42  ? 1.21005 1.20410 0.94809 0.11746  -0.00826 0.12847  61  LYS B CE  
1273 N NZ  . LYS B 42  ? 1.18624 1.16129 0.93626 0.13161  -0.01333 0.15530  61  LYS B NZ  
1274 N N   . ARG B 43  ? 0.99140 1.02833 0.77648 0.09994  -0.06364 -0.00734 62  ARG B N   
1275 C CA  . ARG B 43  ? 0.94026 0.95791 0.72398 0.09642  -0.04745 -0.03361 62  ARG B CA  
1276 C C   . ARG B 43  ? 0.96078 0.97185 0.72685 0.09878  -0.02341 -0.03717 62  ARG B C   
1277 O O   . ARG B 43  ? 1.09083 1.11596 0.82601 0.09317  -0.02097 -0.03153 62  ARG B O   
1278 C CB  . ARG B 43  ? 0.93445 0.95739 0.69429 0.08016  -0.05191 -0.05962 62  ARG B CB  
1279 C CG  . ARG B 43  ? 0.94937 0.99181 0.72681 0.07634  -0.07603 -0.05793 62  ARG B CG  
1280 C CD  . ARG B 43  ? 1.00579 1.01976 0.81063 0.07593  -0.06982 -0.07171 62  ARG B CD  
1281 N NE  . ARG B 43  ? 1.16101 1.15283 0.94435 0.05937  -0.04994 -0.10492 62  ARG B NE  
1282 C CZ  . ARG B 43  ? 1.12850 1.13733 0.90035 0.03636  -0.05517 -0.13048 62  ARG B CZ  
1283 N NH1 . ARG B 43  ? 1.05829 1.11601 0.84050 0.03197  -0.08354 -0.12391 62  ARG B NH1 
1284 N NH2 . ARG B 43  ? 1.21375 1.19145 0.96452 0.01706  -0.02817 -0.16457 62  ARG B NH2 
1285 N N   . PHE B 44  ? 1.02624 1.01954 0.81139 0.10973  -0.00446 -0.04445 63  PHE B N   
1286 C CA  . PHE B 44  ? 0.97669 0.96771 0.75101 0.11585  0.02141  -0.04908 63  PHE B CA  
1287 C C   . PHE B 44  ? 0.93487 0.89836 0.71838 0.13009  0.04463  -0.06346 63  PHE B C   
1288 O O   . PHE B 44  ? 0.93827 0.88048 0.73120 0.13233  0.04159  -0.06959 63  PHE B O   
1289 C CB  . PHE B 44  ? 0.94745 0.96262 0.74479 0.12245  0.02384  -0.02884 63  PHE B CB  
1290 C CG  . PHE B 44  ? 0.97864 1.00622 0.82212 0.13457  0.01919  -0.01992 63  PHE B CG  
1291 C CD1 . PHE B 44  ? 0.82058 0.85199 0.68398 0.12922  -0.00160 -0.00969 63  PHE B CD1 
1292 C CD2 . PHE B 44  ? 1.02940 1.07171 0.89608 0.15242  0.03669  -0.02154 63  PHE B CD2 
1293 C CE1 . PHE B 44  ? 0.77445 0.82329 0.67643 0.13608  -0.00499 -0.00539 63  PHE B CE1 
1294 C CE2 . PHE B 44  ? 0.88133 0.95042 0.78754 0.16285  0.03019  -0.01366 63  PHE B CE2 
1295 C CZ  . PHE B 44  ? 0.72454 0.79672 0.64662 0.15190  0.00929  -0.00756 63  PHE B CZ  
1296 N N   . LYS B 45  ? 1.03026 0.99195 0.81002 0.14180  0.07158  -0.06712 64  LYS B N   
1297 C CA  . LYS B 45  ? 1.03442 0.96714 0.82194 0.16384  0.10083  -0.07498 64  LYS B CA  
1298 C C   . LYS B 45  ? 1.05468 1.02304 0.88040 0.19152  0.10853  -0.05588 64  LYS B C   
1299 O O   . LYS B 45  ? 1.09356 1.09804 0.92487 0.18763  0.10917  -0.04992 64  LYS B O   
1300 C CB  . LYS B 45  ? 1.06590 0.96496 0.81463 0.15608  0.13348  -0.10053 64  LYS B CB  
1301 C CG  . LYS B 45  ? 1.14172 1.00861 0.85499 0.12739  0.13321  -0.12798 64  LYS B CG  
1302 C CD  . LYS B 45  ? 1.17570 1.00216 0.90262 0.13480  0.13967  -0.13185 64  LYS B CD  
1303 C CE  . LYS B 45  ? 1.15291 0.94160 0.84393 0.10275  0.15486  -0.16891 64  LYS B CE  
1304 N NZ  . LYS B 45  ? 1.23763 0.98610 0.89637 0.09721  0.20049  -0.19676 64  LYS B NZ  
1305 N N   . ARG B 46  ? 1.08355 1.04776 0.93493 0.21860  0.11478  -0.04595 65  ARG B N   
1306 C CA  . ARG B 46  ? 1.05911 1.07234 0.94849 0.24917  0.12192  -0.02823 65  ARG B CA  
1307 C C   . ARG B 46  ? 1.03367 1.01463 0.92321 0.28713  0.15551  -0.02449 65  ARG B C   
1308 O O   . ARG B 46  ? 0.99595 0.94003 0.88257 0.29885  0.15784  -0.01947 65  ARG B O   
1309 C CB  . ARG B 46  ? 0.89879 0.95675 0.82181 0.24847  0.09219  -0.01298 65  ARG B CB  
1310 C CG  . ARG B 46  ? 0.87594 1.00115 0.83930 0.27815  0.09575  0.00297  65  ARG B CG  
1311 C CD  . ARG B 46  ? 0.78153 0.95994 0.77370 0.26230  0.06669  0.00885  65  ARG B CD  
1312 N NE  . ARG B 46  ? 0.71648 0.90323 0.70555 0.22518  0.05517  0.00036  65  ARG B NE  
1313 C CZ  . ARG B 46  ? 0.78962 1.00112 0.79618 0.20246  0.03584  0.00047  65  ARG B CZ  
1314 N NH1 . ARG B 46  ? 0.77313 1.01011 0.80100 0.20868  0.02205  0.00509  65  ARG B NH1 
1315 N NH2 . ARG B 46  ? 0.79401 1.00118 0.79390 0.17313  0.03396  -0.00370 65  ARG B NH2 
1316 N N   . ASN B 47  ? 1.03636 1.02909 0.92954 0.30834  0.18499  -0.02504 66  ASN B N   
1317 C CA  . ASN B 47  ? 1.15154 1.10701 1.04385 0.35067  0.22576  -0.01902 66  ASN B CA  
1318 C C   . ASN B 47  ? 1.12074 0.97838 0.97284 0.33951  0.24846  -0.03705 66  ASN B C   
1319 O O   . ASN B 47  ? 1.08457 0.89643 0.93588 0.37070  0.27339  -0.02555 66  ASN B O   
1320 C CB  . ASN B 47  ? 1.22076 1.22645 1.15252 0.39673  0.22186  0.01259  66  ASN B CB  
1321 C CG  . ASN B 47  ? 1.28193 1.39655 1.25666 0.40369  0.20340  0.02401  66  ASN B CG  
1322 O OD1 . ASN B 47  ? 1.28341 1.42840 1.25873 0.36887  0.19005  0.00989  66  ASN B OD1 
1323 N ND2 . ASN B 47  ? 1.10366 1.28092 1.11342 0.44911  0.20574  0.04977  66  ASN B ND2 
1324 N N   . GLY B 48  ? 1.11917 0.94771 0.93633 0.29355  0.24137  -0.06553 67  GLY B N   
1325 C CA  . GLY B 48  ? 1.16067 0.90937 0.93992 0.27178  0.26266  -0.09154 67  GLY B CA  
1326 C C   . GLY B 48  ? 1.26906 1.00401 1.04751 0.25200  0.23520  -0.09154 67  GLY B C   
1327 O O   . GLY B 48  ? 1.36667 1.04704 1.11464 0.22344  0.24897  -0.11892 67  GLY B O   
1328 N N   . GLU B 49  ? 1.17755 0.96319 0.98889 0.26314  0.19942  -0.06546 68  GLU B N   
1329 C CA  . GLU B 49  ? 1.07052 0.84593 0.88424 0.24649  0.17490  -0.06468 68  GLU B CA  
1330 C C   . GLU B 49  ? 1.03794 0.85375 0.84965 0.20793  0.13380  -0.07395 68  GLU B C   
1331 O O   . GLU B 49  ? 1.01553 0.88360 0.84002 0.20548  0.11466  -0.06438 68  GLU B O   
1332 C CB  . GLU B 49  ? 1.06558 0.87326 0.91328 0.28003  0.16188  -0.03235 68  GLU B CB  
1333 C CG  . GLU B 49  ? 1.23589 1.04837 1.09770 0.33141  0.19248  -0.00916 68  GLU B CG  
1334 C CD  . GLU B 49  ? 1.22710 1.11613 1.12691 0.35972  0.16785  0.02189  68  GLU B CD  
1335 O OE1 . GLU B 49  ? 1.07011 0.99803 0.98367 0.33572  0.13048  0.02201  68  GLU B OE1 
1336 O OE2 . GLU B 49  ? 1.21627 1.13122 1.13244 0.40632  0.18735  0.04528  68  GLU B OE2 
1337 N N   . SER B 50  ? 1.07503 0.86662 0.87077 0.17880  0.12372  -0.09194 69  SER B N   
1338 C CA  . SER B 50  ? 0.95388 0.78645 0.75028 0.15004  0.08513  -0.09516 69  SER B CA  
1339 C C   . SER B 50  ? 0.90265 0.77511 0.73569 0.16146  0.05501  -0.06926 69  SER B C   
1340 O O   . SER B 50  ? 0.88498 0.74524 0.73441 0.17391  0.05496  -0.06042 69  SER B O   
1341 C CB  . SER B 50  ? 0.95187 0.76156 0.72749 0.11814  0.08268  -0.12203 69  SER B CB  
1342 O OG  . SER B 50  ? 1.16248 0.93818 0.90201 0.10020  0.11379  -0.15306 69  SER B OG  
1343 N N   . TRP B 51  ? 0.82164 0.73855 0.66458 0.15543  0.03327  -0.05814 70  TRP B N   
1344 C CA  . TRP B 51  ? 0.82735 0.77980 0.70288 0.15909  0.00971  -0.03942 70  TRP B CA  
1345 C C   . TRP B 51  ? 0.80903 0.77796 0.67999 0.13764  -0.01473 -0.03793 70  TRP B C   
1346 O O   . TRP B 51  ? 0.80469 0.77268 0.64725 0.12403  -0.01582 -0.04630 70  TRP B O   
1347 C CB  . TRP B 51  ? 0.68777 0.67804 0.58489 0.17501  0.01598  -0.02537 70  TRP B CB  
1348 C CG  . TRP B 51  ? 0.80589 0.80423 0.72188 0.20438  0.03068  -0.01637 70  TRP B CG  
1349 C CD1 . TRP B 51  ? 0.73226 0.69786 0.63503 0.22665  0.05877  -0.01854 70  TRP B CD1 
1350 C CD2 . TRP B 51  ? 0.74122 0.78766 0.69112 0.21703  0.02058  -0.00222 70  TRP B CD2 
1351 N NE1 . TRP B 51  ? 0.84803 0.83967 0.77436 0.25868  0.06529  -0.00062 70  TRP B NE1 
1352 C CE2 . TRP B 51  ? 0.72797 0.77670 0.68313 0.25157  0.03972  0.00812  70  TRP B CE2 
1353 C CE3 . TRP B 51  ? 0.68173 0.77016 0.65661 0.20184  0.00009  0.00153  70  TRP B CE3 
1354 C CZ2 . TRP B 51  ? 0.66540 0.77084 0.64918 0.27260  0.03358  0.02378  70  TRP B CZ2 
1355 C CZ3 . TRP B 51  ? 0.71551 0.85621 0.71878 0.21556  -0.00380 0.01023  70  TRP B CZ3 
1356 C CH2 . TRP B 51  ? 0.79652 0.95235 0.80377 0.25130  0.01018  0.02211  70  TRP B CH2 
1357 N N   . VAL B 52  ? 0.77910 0.76635 0.67728 0.13674  -0.03226 -0.02575 71  VAL B N   
1358 C CA  . VAL B 52  ? 0.87149 0.87016 0.77056 0.12413  -0.05109 -0.01806 71  VAL B CA  
1359 C C   . VAL B 52  ? 0.83905 0.85688 0.76625 0.12487  -0.05327 -0.00397 71  VAL B C   
1360 O O   . VAL B 52  ? 0.75839 0.78898 0.71047 0.13085  -0.05018 -0.00414 71  VAL B O   
1361 C CB  . VAL B 52  ? 0.80560 0.79668 0.70831 0.11669  -0.06641 -0.02503 71  VAL B CB  
1362 C CG1 . VAL B 52  ? 0.70836 0.69689 0.64133 0.12190  -0.06941 -0.02301 71  VAL B CG1 
1363 C CG2 . VAL B 52  ? 0.82386 0.83125 0.72238 0.11054  -0.08344 -0.01455 71  VAL B CG2 
1364 N N   . ARG B 53  ? 0.91975 0.94096 0.84015 0.11787  -0.05556 0.00780  72  ARG B N   
1365 C CA  . ARG B 53  ? 0.87189 0.90051 0.81475 0.11182  -0.05054 0.01797  72  ARG B CA  
1366 C C   . ARG B 53  ? 0.94908 0.96235 0.89195 0.10963  -0.05997 0.03106  72  ARG B C   
1367 O O   . ARG B 53  ? 1.11102 1.12022 1.02724 0.11359  -0.06635 0.04094  72  ARG B O   
1368 C CB  . ARG B 53  ? 0.96898 1.00657 0.90169 0.10720  -0.03271 0.02303  72  ARG B CB  
1369 C CG  . ARG B 53  ? 0.98197 1.01963 0.93331 0.09399  -0.02039 0.03042  72  ARG B CG  
1370 C CD  . ARG B 53  ? 1.14659 1.19733 1.09082 0.08574  0.00119  0.03115  72  ARG B CD  
1371 N NE  . ARG B 53  ? 1.27469 1.32034 1.23638 0.06669  0.01961  0.03374  72  ARG B NE  
1372 C CZ  . ARG B 53  ? 1.30250 1.31006 1.24555 0.06145  0.03232  0.05203  72  ARG B CZ  
1373 N NH1 . ARG B 53  ? 1.29758 1.28206 1.20408 0.07633  0.02341  0.07182  72  ARG B NH1 
1374 N NH2 . ARG B 53  ? 1.25279 1.24675 1.21283 0.04070  0.05691  0.05047  72  ARG B NH2 
1375 N N   . PHE B 54  ? 0.78042 0.78961 0.75242 0.10490  -0.05957 0.03137  73  PHE B N   
1376 C CA  . PHE B 54  ? 0.76655 0.75798 0.74347 0.10824  -0.06499 0.04462  73  PHE B CA  
1377 C C   . PHE B 54  ? 0.76539 0.74534 0.77228 0.09718  -0.05067 0.04237  73  PHE B C   
1378 O O   . PHE B 54  ? 0.69373 0.69149 0.71860 0.08485  -0.04293 0.02669  73  PHE B O   
1379 C CB  . PHE B 54  ? 0.63202 0.62956 0.61199 0.11516  -0.08517 0.03811  73  PHE B CB  
1380 C CG  . PHE B 54  ? 0.75478 0.75641 0.76030 0.11012  -0.08791 0.02107  73  PHE B CG  
1381 C CD1 . PHE B 54  ? 0.58966 0.58420 0.62116 0.10772  -0.08874 0.02033  73  PHE B CD1 
1382 C CD2 . PHE B 54  ? 0.73473 0.74598 0.73623 0.11022  -0.08646 0.00786  73  PHE B CD2 
1383 C CE1 . PHE B 54  ? 0.72981 0.73121 0.77983 0.10221  -0.09058 0.00530  73  PHE B CE1 
1384 C CE2 . PHE B 54  ? 0.60450 0.62101 0.62400 0.10936  -0.08781 -0.00236 73  PHE B CE2 
1385 C CZ  . PHE B 54  ? 0.66186 0.67570 0.70416 0.10366  -0.09105 -0.00436 73  PHE B CZ  
1386 N N   . TYR B 55  ? 0.70416 0.65808 0.71612 0.10234  -0.04549 0.05763  74  TYR B N   
1387 C CA  . TYR B 55  ? 0.66310 0.59641 0.70304 0.09070  -0.02800 0.05206  74  TYR B CA  
1388 C C   . TYR B 55  ? 0.71367 0.64126 0.77017 0.10230  -0.04064 0.05343  74  TYR B C   
1389 O O   . TYR B 55  ? 0.79979 0.73653 0.84494 0.12096  -0.05897 0.06615  74  TYR B O   
1390 C CB  . TYR B 55  ? 0.77712 0.66953 0.81054 0.08712  0.00241  0.06999  74  TYR B CB  
1391 C CG  . TYR B 55  ? 0.79810 0.69319 0.81396 0.07408  0.01975  0.07065  74  TYR B CG  
1392 C CD1 . TYR B 55  ? 0.84555 0.74064 0.82628 0.08856  0.01515  0.09165  74  TYR B CD1 
1393 C CD2 . TYR B 55  ? 0.78951 0.69358 0.82408 0.04482  0.04233  0.04822  74  TYR B CD2 
1394 C CE1 . TYR B 55  ? 1.05350 0.95068 1.01830 0.07576  0.03391  0.09155  74  TYR B CE1 
1395 C CE2 . TYR B 55  ? 0.83807 0.75097 0.86079 0.03101  0.06032  0.04673  74  TYR B CE2 
1396 C CZ  . TYR B 55  ? 1.04349 0.94907 1.03137 0.04731  0.05695  0.06923  74  TYR B CZ  
1397 O OH  . TYR B 55  ? 1.07614 0.99069 1.05237 0.03267  0.07734  0.06681  74  TYR B OH  
1398 N N   . LEU B 56  ? 0.64742 0.56727 0.73146 0.08884  -0.03005 0.03734  75  LEU B N   
1399 C CA  . LEU B 56  ? 0.66747 0.57629 0.77053 0.09933  -0.03456 0.03925  75  LEU B CA  
1400 C C   . LEU B 56  ? 0.79112 0.66483 0.89047 0.12041  -0.02057 0.06910  75  LEU B C   
1401 O O   . LEU B 56  ? 0.87918 0.72056 0.96672 0.11810  0.00436  0.08310  75  LEU B O   
1402 C CB  . LEU B 56  ? 0.67410 0.57827 0.80401 0.07769  -0.01977 0.01452  75  LEU B CB  
1403 C CG  . LEU B 56  ? 0.73999 0.68560 0.87289 0.06215  -0.03301 -0.00994 75  LEU B CG  
1404 C CD1 . LEU B 56  ? 0.80148 0.74957 0.95734 0.04073  -0.01908 -0.03373 75  LEU B CD1 
1405 C CD2 . LEU B 56  ? 0.53958 0.50581 0.66334 0.07793  -0.06038 -0.00774 75  LEU B CD2 
1406 N N   . ALA B 57  ? 0.72949 0.61226 0.83870 0.14305  -0.03486 0.08083  76  ALA B N   
1407 C CA  . ALA B 57  ? 0.75007 0.60775 0.85747 0.17231  -0.02215 0.11537  76  ALA B CA  
1408 C C   . ALA B 57  ? 0.74216 0.53778 0.86619 0.16598  0.02040  0.11753  76  ALA B C   
1409 O O   . ALA B 57  ? 0.87719 0.63072 0.98950 0.18531  0.04567  0.14898  76  ALA B O   
1410 C CB  . ALA B 57  ? 0.91017 0.80374 1.03385 0.19758  -0.04513 0.12386  76  ALA B CB  
1411 N N   . ILE B 58  ? 0.73829 0.52576 0.88612 0.13753  0.03240  0.08381  77  ILE B N   
1412 C CA  . ILE B 58  ? 0.85268 0.58145 1.01621 0.12202  0.07764  0.07547  77  ILE B CA  
1413 C C   . ILE B 58  ? 0.98176 0.68417 1.12835 0.09407  0.10591  0.06859  77  ILE B C   
1414 O O   . ILE B 58  ? 0.91336 0.55260 1.06266 0.08581  0.15175  0.07235  77  ILE B O   
1415 C CB  . ILE B 58  ? 0.84523 0.58531 1.03726 0.09727  0.07999  0.03743  77  ILE B CB  
1416 C CG1 . ILE B 58  ? 1.07453 0.75228 1.28286 0.07685  0.13160  0.02247  77  ILE B CG1 
1417 C CG2 . ILE B 58  ? 0.77800 0.57237 0.96427 0.06756  0.05629  0.00660  77  ILE B CG2 
1418 C CD1 . ILE B 58  ? 1.10606 0.79831 1.33833 0.04859  0.13675  -0.01814 77  ILE B CD1 
1419 N N   . ASP B 59  ? 1.00444 0.75135 1.13404 0.07967  0.08391  0.05869  78  ASP B N   
1420 C CA  . ASP B 59  ? 0.86129 0.59903 0.97919 0.05054  0.10852  0.04795  78  ASP B CA  
1421 C C   . ASP B 59  ? 0.89989 0.59400 0.98915 0.07198  0.12711  0.08725  78  ASP B C   
1422 O O   . ASP B 59  ? 0.94218 0.66238 1.00541 0.08129  0.10879  0.10187  78  ASP B O   
1423 C CB  . ASP B 59  ? 0.80249 0.60822 0.91522 0.03526  0.07896  0.02721  78  ASP B CB  
1424 C CG  . ASP B 59  ? 0.95917 0.77302 1.06765 0.00312  0.10326  0.01109  78  ASP B CG  
1425 O OD1 . ASP B 59  ? 0.96055 0.72494 1.07177 -0.01694 0.14630  0.00795  78  ASP B OD1 
1426 O OD2 . ASP B 59  ? 0.77234 0.64184 0.87575 -0.00211 0.08253  0.00091  78  ASP B OD2 
1427 N N   . ALA B 60  ? 1.02712 0.64971 1.11902 0.08103  0.16827  0.10562  79  ALA B N   
1428 C CA  . ALA B 60  ? 1.04887 0.62084 1.10988 0.10559  0.19293  0.14935  79  ALA B CA  
1429 C C   . ALA B 60  ? 1.02782 0.58279 1.07088 0.07104  0.22287  0.13861  79  ALA B C   
1430 O O   . ALA B 60  ? 1.03707 0.58396 1.04586 0.08721  0.22465  0.16984  79  ALA B O   
1431 C CB  . ALA B 60  ? 1.05281 0.54387 1.12203 0.12841  0.23657  0.17461  79  ALA B CB  
1432 N N   . ALA B 61  ? 0.99576 0.55323 1.06106 0.02188  0.24661  0.09322  80  ALA B N   
1433 C CA  . ALA B 61  ? 1.02511 0.57682 1.08040 -0.01692 0.27813  0.07648  80  ALA B CA  
1434 C C   . ALA B 61  ? 0.98350 0.61928 1.03116 -0.02381 0.23842  0.06468  80  ALA B C   
1435 O O   . ALA B 61  ? 0.97793 0.62283 1.01912 -0.05336 0.26057  0.05138  80  ALA B O   
1436 C CB  . ALA B 61  ? 1.04362 0.58248 1.12815 -0.07149 0.31873  0.02671  80  ALA B CB  
1437 N N   . HIS B 62  ? 0.98673 0.68079 1.03559 0.00230  0.18513  0.06848  81  HIS B N   
1438 C CA  . HIS B 62  ? 0.91320 0.67949 0.95518 0.00051  0.15101  0.05782  81  HIS B CA  
1439 C C   . HIS B 62  ? 0.88431 0.70273 0.95224 -0.04184 0.15987  0.01426  81  HIS B C   
1440 O O   . HIS B 62  ? 0.88629 0.74174 0.94862 -0.05524 0.16267  0.00630  81  HIS B O   
1441 C CB  . HIS B 62  ? 0.96542 0.71995 0.96926 0.01580  0.15492  0.08784  81  HIS B CB  
1442 C CG  . HIS B 62  ? 0.99801 0.74013 0.97399 0.05982  0.13053  0.12729  81  HIS B CG  
1443 N ND1 . HIS B 62  ? 1.14363 0.89464 1.08068 0.07728  0.12169  0.15245  81  HIS B ND1 
1444 C CD2 . HIS B 62  ? 1.09345 0.82626 1.07582 0.08831  0.11261  0.14341  81  HIS B CD2 
1445 C CE1 . HIS B 62  ? 1.14903 0.90214 1.06851 0.11340  0.09789  0.18166  81  HIS B CE1 
1446 N NE2 . HIS B 62  ? 1.26945 1.01342 1.21818 0.12163  0.09173  0.17726  81  HIS B NE2 
1447 N N   . SER B 63  ? 0.88060 0.70962 0.97765 -0.06277 0.16471  -0.01475 82  SER B N   
1448 C CA  . SER B 63  ? 0.93424 0.82610 1.05695 -0.10463 0.17304  -0.05789 82  SER B CA  
1449 C C   . SER B 63  ? 0.92085 0.90108 1.05397 -0.09314 0.12839  -0.06985 82  SER B C   
1450 O O   . SER B 63  ? 0.95006 1.00314 1.09802 -0.11526 0.12775  -0.09445 82  SER B O   
1451 C CB  . SER B 63  ? 0.89071 0.75557 1.03582 -0.13783 0.20450  -0.08730 82  SER B CB  
1452 O OG  . SER B 63  ? 0.92756 0.78464 1.08017 -0.11570 0.18115  -0.08311 82  SER B OG  
1453 N N   . HIS B 64  ? 0.75364 0.73184 0.87981 -0.05836 0.09370  -0.05249 83  HIS B N   
1454 C CA  . HIS B 64  ? 0.76932 0.81573 0.90173 -0.04495 0.05807  -0.06055 83  HIS B CA  
1455 C C   . HIS B 64  ? 0.78028 0.81951 0.88813 -0.00781 0.03172  -0.03335 83  HIS B C   
1456 O O   . HIS B 64  ? 0.64394 0.66804 0.74583 0.01452  0.00997  -0.02283 83  HIS B O   
1457 C CB  . HIS B 64  ? 0.78201 0.83456 0.92939 -0.04618 0.04643  -0.07373 83  HIS B CB  
1458 C CG  . HIS B 64  ? 0.94914 1.01143 1.11824 -0.08663 0.07361  -0.10631 83  HIS B CG  
1459 N ND1 . HIS B 64  ? 1.02459 1.01656 1.19744 -0.10348 0.10876  -0.10953 83  HIS B ND1 
1460 C CD2 . HIS B 64  ? 0.96512 1.10171 1.15194 -0.11425 0.07314  -0.13853 83  HIS B CD2 
1461 C CE1 . HIS B 64  ? 0.93376 0.95024 1.12559 -0.14503 0.13176  -0.14732 83  HIS B CE1 
1462 N NE2 . HIS B 64  ? 0.96661 1.07784 1.16699 -0.15348 0.10819  -0.16630 83  HIS B NE2 
1463 N N   . PRO B 65  ? 0.69785 0.75101 0.79143 -0.00395 0.03536  -0.02555 84  PRO B N   
1464 C CA  . PRO B 65  ? 0.73706 0.78998 0.80633 0.02615  0.01316  -0.00748 84  PRO B CA  
1465 C C   . PRO B 65  ? 0.71154 0.80918 0.78899 0.04021  -0.00976 -0.01659 84  PRO B C   
1466 O O   . PRO B 65  ? 0.71815 0.87090 0.81567 0.03105  -0.00841 -0.03259 84  PRO B O   
1467 C CB  . PRO B 65  ? 0.79289 0.85696 0.84899 0.02086  0.02917  -0.00357 84  PRO B CB  
1468 C CG  . PRO B 65  ? 0.74839 0.84801 0.83140 -0.01186 0.05254  -0.02648 84  PRO B CG  
1469 C CD  . PRO B 65  ? 0.67496 0.74340 0.77331 -0.03012 0.06374  -0.03581 84  PRO B CD  
1470 N N   . ILE B 66  ? 0.65083 0.72716 0.71164 0.06254  -0.02881 -0.00589 85  ILE B N   
1471 C CA  . ILE B 66  ? 0.70498 0.80406 0.76776 0.07786  -0.04486 -0.01082 85  ILE B CA  
1472 C C   . ILE B 66  ? 0.65870 0.75136 0.69654 0.09689  -0.04846 -0.00338 85  ILE B C   
1473 O O   . ILE B 66  ? 0.66261 0.72272 0.67792 0.10146  -0.05260 0.00468  85  ILE B O   
1474 C CB  . ILE B 66  ? 0.83645 0.91152 0.90340 0.08085  -0.05742 -0.01159 85  ILE B CB  
1475 C CG1 . ILE B 66  ? 0.73464 0.80254 0.82316 0.06075  -0.04763 -0.01955 85  ILE B CG1 
1476 C CG2 . ILE B 66  ? 0.84686 0.94291 0.91527 0.09330  -0.06727 -0.01646 85  ILE B CG2 
1477 C CD1 . ILE B 66  ? 0.72628 0.77172 0.82224 0.06376  -0.05667 -0.02093 85  ILE B CD1 
1478 N N   . GLU B 67  ? 0.74283 0.87070 0.78444 0.10863  -0.04507 -0.00655 86  GLU B N   
1479 C CA  . GLU B 67  ? 0.62491 0.74268 0.64451 0.12762  -0.04126 -0.00270 86  GLU B CA  
1480 C C   . GLU B 67  ? 0.60028 0.71774 0.61939 0.14769  -0.04460 -0.00241 86  GLU B C   
1481 O O   . GLU B 67  ? 0.66031 0.82021 0.69822 0.15673  -0.04424 -0.00123 86  GLU B O   
1482 C CB  . GLU B 67  ? 0.61818 0.77184 0.64227 0.12979  -0.02619 -0.00299 86  GLU B CB  
1483 C CG  . GLU B 67  ? 0.73293 0.86545 0.73877 0.11614  -0.01715 0.00029  86  GLU B CG  
1484 C CD  . GLU B 67  ? 0.77490 0.94056 0.78275 0.11873  0.00048  -0.00172 86  GLU B CD  
1485 O OE1 . GLU B 67  ? 0.83640 1.04630 0.86310 0.13474  0.00457  -0.00477 86  GLU B OE1 
1486 O OE2 . GLU B 67  ? 0.87062 1.02103 0.86079 0.10715  0.01144  0.00173  86  GLU B OE2 
1487 N N   . ARG B 68  ? 0.64700 0.71957 0.64307 0.15349  -0.04591 -0.00367 87  ARG B N   
1488 C CA  . ARG B 68  ? 0.59743 0.65195 0.58739 0.17005  -0.04210 -0.00310 87  ARG B CA  
1489 C C   . ARG B 68  ? 0.67482 0.68672 0.63567 0.17852  -0.02673 -0.00823 87  ARG B C   
1490 O O   . ARG B 68  ? 0.70442 0.69689 0.64669 0.16368  -0.02851 -0.01675 87  ARG B O   
1491 C CB  . ARG B 68  ? 0.57508 0.61093 0.56983 0.15903  -0.05471 -0.00710 87  ARG B CB  
1492 C CG  . ARG B 68  ? 0.65603 0.72705 0.67667 0.15217  -0.06413 -0.00579 87  ARG B CG  
1493 C CD  . ARG B 68  ? 0.65971 0.76420 0.68623 0.17300  -0.05850 0.00239  87  ARG B CD  
1494 N NE  . ARG B 68  ? 0.80649 0.95592 0.85473 0.16208  -0.06752 -0.00081 87  ARG B NE  
1495 C CZ  . ARG B 68  ? 0.74112 0.94589 0.80966 0.15044  -0.06847 -0.00609 87  ARG B CZ  
1496 N NH1 . ARG B 68  ? 0.85207 1.07759 0.92391 0.15199  -0.06111 -0.00538 87  ARG B NH1 
1497 N NH2 . ARG B 68  ? 0.85537 1.09833 0.94089 0.13400  -0.07406 -0.01536 87  ARG B NH2 
1498 N N   . PRO B 69  ? 0.68179 0.67864 0.63597 0.20232  -0.00882 -0.00325 88  PRO B N   
1499 C CA  . PRO B 69  ? 0.73386 0.67541 0.65849 0.20570  0.01335  -0.01333 88  PRO B CA  
1500 C C   . PRO B 69  ? 0.75369 0.65720 0.66528 0.18284  0.00749  -0.02855 88  PRO B C   
1501 O O   . PRO B 69  ? 0.64239 0.55144 0.56776 0.17757  -0.00610 -0.02555 88  PRO B O   
1502 C CB  . PRO B 69  ? 0.67989 0.61008 0.60414 0.24161  0.03749  0.00159  88  PRO B CB  
1503 C CG  . PRO B 69  ? 0.66668 0.64306 0.61557 0.25112  0.02004  0.01732  88  PRO B CG  
1504 C CD  . PRO B 69  ? 0.68786 0.71764 0.65900 0.22807  -0.00526 0.01255  88  PRO B CD  
1505 N N   . LEU B 70  ? 0.81611 0.68789 0.70151 0.16657  0.01860  -0.04795 89  LEU B N   
1506 C CA  . LEU B 70  ? 0.80926 0.65633 0.68337 0.14132  0.01541  -0.06778 89  LEU B CA  
1507 C C   . LEU B 70  ? 0.81185 0.60866 0.67897 0.14947  0.04078  -0.07005 89  LEU B C   
1508 O O   . LEU B 70  ? 0.90297 0.65968 0.75471 0.16900  0.07361  -0.06705 89  LEU B O   
1509 C CB  . LEU B 70  ? 0.77829 0.61672 0.62378 0.11812  0.02237  -0.09230 89  LEU B CB  
1510 C CG  . LEU B 70  ? 0.80486 0.68677 0.65139 0.09544  -0.00853 -0.09807 89  LEU B CG  
1511 C CD1 . LEU B 70  ? 0.86598 0.78652 0.72771 0.10740  -0.02788 -0.07406 89  LEU B CD1 
1512 C CD2 . LEU B 70  ? 0.91063 0.79274 0.72358 0.07101  -0.00016 -0.12548 89  LEU B CD2 
1513 N N   . ALA B 71  ? 0.96277 0.75862 0.84071 0.13664  0.02921  -0.07345 90  ALA B N   
1514 C CA  . ALA B 71  ? 0.96591 0.70924 0.83355 0.13956  0.05569  -0.07611 90  ALA B CA  
1515 C C   . ALA B 71  ? 0.99683 0.69424 0.83882 0.10899  0.08078  -0.11029 90  ALA B C   
1516 O O   . ALA B 71  ? 1.11052 0.74793 0.92805 0.11570  0.12140  -0.11705 90  ALA B O   
1517 C CB  . ALA B 71  ? 0.91882 0.68169 0.80774 0.13468  0.03602  -0.06883 90  ALA B CB  
1518 N N   . THR B 92  ? 1.24756 1.95370 1.18962 -0.04105 -0.26546 -0.20599 111 THR B N   
1519 C CA  . THR B 92  ? 1.43208 2.03519 1.40259 -0.03671 -0.24364 -0.20260 111 THR B CA  
1520 C C   . THR B 92  ? 1.47627 1.97485 1.41576 -0.06528 -0.20809 -0.23067 111 THR B C   
1521 O O   . THR B 92  ? 1.55281 2.03013 1.49394 -0.10428 -0.18567 -0.27450 111 THR B O   
1522 C CB  . THR B 92  ? 1.36962 2.01497 1.38751 -0.05274 -0.24548 -0.22644 111 THR B CB  
1523 N N   . ALA B 93  ? 1.34935 1.78215 1.26167 -0.04411 -0.19964 -0.20398 112 ALA B N   
1524 C CA  . ALA B 93  ? 1.35963 1.69564 1.24563 -0.05979 -0.16538 -0.22189 112 ALA B CA  
1525 C C   . ALA B 93  ? 1.40107 1.67021 1.28329 -0.02331 -0.16108 -0.17971 112 ALA B C   
1526 O O   . ALA B 93  ? 1.33522 1.59974 1.18589 -0.01545 -0.15975 -0.16814 112 ALA B O   
1527 C CB  . ALA B 93  ? 1.31656 1.67152 1.15714 -0.09424 -0.15218 -0.25983 112 ALA B CB  
1528 N N   . ARG B 94  ? 1.34372 1.56596 1.25762 -0.00411 -0.15741 -0.15947 113 ARG B N   
1529 C CA  . ARG B 94  ? 1.14275 1.31386 1.06483 0.02620  -0.15409 -0.12363 113 ARG B CA  
1530 C C   . ARG B 94  ? 1.22502 1.32094 1.13195 0.02273  -0.12501 -0.13238 113 ARG B C   
1531 O O   . ARG B 94  ? 1.23952 1.30379 1.14344 0.00359  -0.10493 -0.15899 113 ARG B O   
1532 C CB  . ARG B 94  ? 1.02770 1.19877 0.99228 0.04297  -0.16357 -0.10482 113 ARG B CB  
1533 N N   . PRO B 95  ? 1.07439 1.14278 0.97199 0.04228  -0.11967 -0.10926 114 PRO B N   
1534 C CA  . PRO B 95  ? 0.96649 0.97538 0.85729 0.04796  -0.09392 -0.11083 114 PRO B CA  
1535 C C   . PRO B 95  ? 0.89592 0.87994 0.81637 0.05772  -0.09104 -0.10162 114 PRO B C   
1536 O O   . PRO B 95  ? 0.84925 0.85382 0.79672 0.06670  -0.10787 -0.08529 114 PRO B O   
1537 C CB  . PRO B 95  ? 0.86658 0.87453 0.74706 0.06565  -0.09384 -0.08779 114 PRO B CB  
1538 C CG  . PRO B 95  ? 1.00746 1.05559 0.90067 0.07477  -0.11791 -0.06499 114 PRO B CG  
1539 C CD  . PRO B 95  ? 0.91506 1.00813 0.80755 0.06071  -0.13400 -0.07983 114 PRO B CD  
1540 N N   . VAL B 96  ? 0.88113 0.81856 0.79379 0.05725  -0.06630 -0.11120 115 VAL B N   
1541 C CA  . VAL B 96  ? 0.76532 0.68041 0.69790 0.06572  -0.06068 -0.10321 115 VAL B CA  
1542 C C   . VAL B 96  ? 0.83025 0.72304 0.76054 0.09048  -0.04766 -0.08320 115 VAL B C   
1543 O O   . VAL B 96  ? 0.80713 0.67575 0.71576 0.09817  -0.02774 -0.08486 115 VAL B O   
1544 C CB  . VAL B 96  ? 0.74719 0.62953 0.67138 0.04653  -0.03989 -0.12750 115 VAL B CB  
1545 C CG1 . VAL B 96  ? 0.80304 0.66619 0.74437 0.05548  -0.03495 -0.11649 115 VAL B CG1 
1546 C CG2 . VAL B 96  ? 0.77423 0.69612 0.70243 0.01822  -0.05273 -0.15275 115 VAL B CG2 
1547 N N   . ILE B 97  ? 0.73905 0.64599 0.69278 0.10261  -0.05754 -0.06606 116 ILE B N   
1548 C CA  . ILE B 97  ? 0.82897 0.73679 0.78566 0.12514  -0.04939 -0.04783 116 ILE B CA  
1549 C C   . ILE B 97  ? 0.76132 0.66631 0.72989 0.13095  -0.04756 -0.04112 116 ILE B C   
1550 O O   . ILE B 97  ? 0.70617 0.60871 0.68472 0.11646  -0.05392 -0.05012 116 ILE B O   
1551 C CB  . ILE B 97  ? 0.70012 0.64652 0.67166 0.13013  -0.06351 -0.03530 116 ILE B CB  
1552 C CG1 . ILE B 97  ? 0.62034 0.58865 0.61587 0.11849  -0.08241 -0.03422 116 ILE B CG1 
1553 C CG2 . ILE B 97  ? 0.67227 0.61955 0.62579 0.12776  -0.06097 -0.03818 116 ILE B CG2 
1554 C CD1 . ILE B 97  ? 0.69851 0.69372 0.70938 0.12004  -0.08740 -0.02356 116 ILE B CD1 
1555 N N   . GLU B 98  ? 0.73905 0.65238 0.70658 0.15353  -0.03881 -0.02450 117 GLU B N   
1556 C CA  . GLU B 98  ? 0.77356 0.69663 0.74760 0.16229  -0.03805 -0.01434 117 GLU B CA  
1557 C C   . GLU B 98  ? 0.73042 0.71227 0.72801 0.16303  -0.05532 -0.00747 117 GLU B C   
1558 O O   . GLU B 98  ? 0.78805 0.80154 0.79006 0.17394  -0.05592 -0.00005 117 GLU B O   
1559 C CB  . GLU B 98  ? 0.85618 0.75218 0.80790 0.19076  -0.01268 0.00209  117 GLU B CB  
1560 C CG  . GLU B 98  ? 1.04927 0.87514 0.97648 0.18423  0.01333  -0.00784 117 GLU B CG  
1561 C CD  . GLU B 98  ? 1.16394 0.95580 1.06980 0.21258  0.04093  0.01386  117 GLU B CD  
1562 O OE1 . GLU B 98  ? 1.21905 1.01482 1.11597 0.24707  0.05497  0.03554  117 GLU B OE1 
1563 O OE2 . GLU B 98  ? 1.13603 0.89850 1.03377 0.20275  0.05049  0.01133  117 GLU B OE2 
1564 N N   . LEU B 99  ? 0.70812 0.70513 0.72158 0.14814  -0.06601 -0.01356 118 LEU B N   
1565 C CA  . LEU B 99  ? 0.68726 0.73461 0.72270 0.13986  -0.07726 -0.01498 118 LEU B CA  
1566 C C   . LEU B 99  ? 0.72617 0.79568 0.76146 0.14176  -0.07650 -0.01232 118 LEU B C   
1567 O O   . LEU B 99  ? 0.69987 0.73832 0.72748 0.13777  -0.07185 -0.01515 118 LEU B O   
1568 C CB  . LEU B 99  ? 0.64781 0.69034 0.70293 0.11721  -0.08677 -0.02762 118 LEU B CB  
1569 C CG  . LEU B 99  ? 0.70422 0.74111 0.75939 0.11505  -0.08907 -0.02643 118 LEU B CG  
1570 C CD1 . LEU B 99  ? 0.61946 0.64669 0.69116 0.10048  -0.09525 -0.03175 118 LEU B CD1 
1571 C CD2 . LEU B 99  ? 0.75126 0.82512 0.81049 0.11929  -0.08560 -0.02149 118 LEU B CD2 
1572 N N   . ASP B 100 ? 0.57030 0.69980 0.61290 0.14608  -0.08012 -0.00825 119 ASP B N   
1573 C CA  . ASP B 100 ? 0.60079 0.76737 0.64247 0.14298  -0.08199 -0.00882 119 ASP B CA  
1574 C C   . ASP B 100 ? 0.61966 0.78910 0.68332 0.10964  -0.08693 -0.03221 119 ASP B C   
1575 O O   . ASP B 100 ? 0.77731 0.97707 0.86015 0.09174  -0.08909 -0.04510 119 ASP B O   
1576 C CB  . ASP B 100 ? 0.67071 0.91709 0.71252 0.15844  -0.08507 0.00158  119 ASP B CB  
1577 C CG  . ASP B 100 ? 0.73504 0.97746 0.75396 0.20072  -0.07542 0.03083  119 ASP B CG  
1578 O OD1 . ASP B 100 ? 0.73988 0.90804 0.74183 0.21284  -0.06270 0.03870  119 ASP B OD1 
1579 O OD2 . ASP B 100 ? 0.80604 1.12262 0.82440 0.22191  -0.07819 0.04516  119 ASP B OD2 
1580 N N   . ILE B 101 ? 0.62957 0.76219 0.69146 0.10065  -0.08419 -0.03870 120 ILE B N   
1581 C CA  . ILE B 101 ? 0.67146 0.79919 0.75546 0.07396  -0.08419 -0.05947 120 ILE B CA  
1582 C C   . ILE B 101 ? 0.67749 0.83897 0.75646 0.06382  -0.08114 -0.06759 120 ILE B C   
1583 O O   . ILE B 101 ? 0.68592 0.84290 0.74216 0.07739  -0.07788 -0.05543 120 ILE B O   
1584 C CB  . ILE B 101 ? 0.60799 0.68090 0.69946 0.07065  -0.08320 -0.06338 120 ILE B CB  
1585 C CG1 . ILE B 101 ? 0.59065 0.64072 0.68102 0.07991  -0.08739 -0.05570 120 ILE B CG1 
1586 C CG2 . ILE B 101 ? 0.61832 0.68679 0.73637 0.05020  -0.07998 -0.08112 120 ILE B CG2 
1587 C CD1 . ILE B 101 ? 0.73502 0.75126 0.83323 0.07637  -0.08956 -0.06051 120 ILE B CD1 
1588 N N   . CYS B 102 ? 0.60932 0.80020 0.70679 0.03821  -0.07828 -0.08913 121 CYS B N   
1589 C CA  . CYS B 102 ? 0.59403 0.82584 0.68643 0.02150  -0.07410 -0.10371 121 CYS B CA  
1590 C C   . CYS B 102 ? 0.61994 0.81361 0.73170 -0.00071 -0.06313 -0.12520 121 CYS B C   
1591 O O   . CYS B 102 ? 0.63828 0.80564 0.77483 -0.01330 -0.05604 -0.13727 121 CYS B O   
1592 C CB  . CYS B 102 ? 0.70180 1.00935 0.79961 0.00349  -0.07467 -0.11900 121 CYS B CB  
1593 S SG  . CYS B 102 ? 0.74656 1.10722 0.84238 -0.03180 -0.06563 -0.15090 121 CYS B SG  
1594 N N   . MET B 103 ? 0.65218 0.84113 0.75198 -0.00274 -0.05873 -0.12760 122 MET B N   
1595 C CA  . MET B 103 ? 0.62061 0.77882 0.73996 -0.02132 -0.04604 -0.14819 122 MET B CA  
1596 C C   . MET B 103 ? 0.62232 0.82008 0.72464 -0.03838 -0.03853 -0.16289 122 MET B C   
1597 O O   . MET B 103 ? 0.62614 0.83835 0.69783 -0.02452 -0.04220 -0.14609 122 MET B O   
1598 C CB  . MET B 103 ? 0.70710 0.81253 0.83182 -0.00685 -0.04656 -0.13718 122 MET B CB  
1599 C CG  . MET B 103 ? 0.62275 0.70576 0.77050 -0.02105 -0.03342 -0.15604 122 MET B CG  
1600 S SD  . MET B 103 ? 0.62280 0.66320 0.78918 -0.00637 -0.03713 -0.14698 122 MET B SD  
1601 C CE  . MET B 103 ? 0.61864 0.64814 0.80905 0.00357  -0.04464 -0.13997 122 MET B CE  
1602 N N   . GLY B 104 ? 0.70019 0.91275 0.81906 -0.06844 -0.02456 -0.19384 123 GLY B N   
1603 C CA  . GLY B 104 ? 0.65585 0.92147 0.75479 -0.09028 -0.01765 -0.21294 123 GLY B CA  
1604 C C   . GLY B 104 ? 0.67916 1.02367 0.74991 -0.08292 -0.03313 -0.20053 123 GLY B C   
1605 O O   . GLY B 104 ? 0.61710 0.99735 0.69830 -0.09048 -0.03746 -0.20721 123 GLY B O   
1606 N N   . SER B 105 ? 0.72124 1.09548 0.75591 -0.06527 -0.03991 -0.17960 124 SER B N   
1607 C CA  . SER B 105 ? 0.68255 1.13684 0.68845 -0.04601 -0.05517 -0.15785 124 SER B CA  
1608 C C   . SER B 105 ? 0.67806 1.09822 0.66356 0.00098  -0.06314 -0.11179 124 SER B C   
1609 O O   . SER B 105 ? 0.68429 1.16159 0.64055 0.02817  -0.07169 -0.08419 124 SER B O   
1610 C CB  . SER B 105 ? 0.65988 1.18944 0.63326 -0.05961 -0.05344 -0.16679 124 SER B CB  
1611 O OG  . SER B 105 ? 0.73825 1.22098 0.68652 -0.04690 -0.04437 -0.15032 124 SER B OG  
1612 N N   . ALA B 106 ? 0.69047 1.02213 0.69027 0.01158  -0.05820 -0.10335 125 ALA B N   
1613 C CA  . ALA B 106 ? 0.57203 0.85804 0.55175 0.04893  -0.05811 -0.06702 125 ALA B CA  
1614 C C   . ALA B 106 ? 0.60943 0.87975 0.60893 0.06176  -0.06644 -0.05995 125 ALA B C   
1615 O O   . ALA B 106 ? 0.64589 0.88113 0.67629 0.04493  -0.06672 -0.07838 125 ALA B O   
1616 C CB  . ALA B 106 ? 0.62346 0.82947 0.60169 0.04636  -0.04401 -0.06720 125 ALA B CB  
1617 N N   . MET B 107 ? 0.56728 0.86513 0.54785 0.09416  -0.07136 -0.03126 126 MET B N   
1618 C CA  . MET B 107 ? 0.64283 0.92510 0.63649 0.11011  -0.07619 -0.02168 126 MET B CA  
1619 C C   . MET B 107 ? 0.60866 0.81683 0.58133 0.13904  -0.06422 0.00397  126 MET B C   
1620 O O   . MET B 107 ? 0.61096 0.81579 0.55083 0.16630  -0.05391 0.03103  126 MET B O   
1621 C CB  . MET B 107 ? 0.66652 1.03814 0.65885 0.12589  -0.08650 -0.01083 126 MET B CB  
1622 C CG  . MET B 107 ? 0.59614 0.95261 0.59914 0.14580  -0.08823 0.00136  126 MET B CG  
1623 S SD  . MET B 107 ? 0.87518 1.21403 0.91734 0.10872  -0.09213 -0.03154 126 MET B SD  
1624 C CE  . MET B 107 ? 0.84389 1.29316 0.90236 0.07864  -0.09836 -0.05751 126 MET B CE  
1625 N N   . ARG B 108 ? 0.52728 0.67616 0.51617 0.13246  -0.06251 -0.00470 127 ARG B N   
1626 C CA  . ARG B 108 ? 0.64274 0.72022 0.61266 0.15052  -0.04726 0.01030  127 ARG B CA  
1627 C C   . ARG B 108 ? 0.68522 0.74314 0.66713 0.15579  -0.05067 0.00891  127 ARG B C   
1628 O O   . ARG B 108 ? 0.57485 0.64597 0.58365 0.13626  -0.06334 -0.00915 127 ARG B O   
1629 C CB  . ARG B 108 ? 0.63246 0.65284 0.60463 0.12871  -0.03705 -0.00566 127 ARG B CB  
1630 C CG  . ARG B 108 ? 0.68940 0.71704 0.64416 0.12352  -0.02792 -0.00342 127 ARG B CG  
1631 C CD  . ARG B 108 ? 0.63821 0.65646 0.54985 0.15738  -0.01069 0.03121  127 ARG B CD  
1632 N NE  . ARG B 108 ? 0.66818 0.67850 0.55736 0.15078  0.00273  0.03447  127 ARG B NE  
1633 C CZ  . ARG B 108 ? 0.75944 0.83447 0.64250 0.14495  -0.00647 0.03313  127 ARG B CZ  
1634 N NH1 . ARG B 108 ? 0.66899 0.82423 0.56827 0.14218  -0.02809 0.02599  127 ARG B NH1 
1635 N NH2 . ARG B 108 ? 0.70374 0.76473 0.56306 0.13753  0.00866  0.03555  127 ARG B NH2 
1636 N N   . SER B 109 ? 0.60427 0.62674 0.56345 0.18318  -0.03544 0.02900  128 SER B N   
1637 C CA  . SER B 109 ? 0.63364 0.62495 0.59762 0.18557  -0.03306 0.02475  128 SER B CA  
1638 C C   . SER B 109 ? 0.67058 0.60201 0.63700 0.16097  -0.02657 0.00404  128 SER B C   
1639 O O   . SER B 109 ? 0.89517 0.77643 0.84174 0.16037  -0.00597 0.00518  128 SER B O   
1640 C CB  . SER B 109 ? 0.62312 0.59499 0.56199 0.22346  -0.01332 0.05094  128 SER B CB  
1641 O OG  . SER B 109 ? 0.71187 0.65769 0.65438 0.22294  -0.00964 0.04323  128 SER B OG  
1642 N N   . ILE B 110 ? 0.68262 0.62355 0.67283 0.14066  -0.04235 -0.01436 129 ILE B N   
1643 C CA  . ILE B 110 ? 0.69582 0.60799 0.69602 0.11670  -0.04329 -0.03513 129 ILE B CA  
1644 C C   . ILE B 110 ? 0.67752 0.57609 0.67501 0.11475  -0.04481 -0.04161 129 ILE B C   
1645 O O   . ILE B 110 ? 0.75231 0.67579 0.75527 0.12286  -0.05469 -0.03523 129 ILE B O   
1646 C CB  . ILE B 110 ? 0.65357 0.59754 0.68513 0.09767  -0.06050 -0.04823 129 ILE B CB  
1647 C CG1 . ILE B 110 ? 0.64957 0.60642 0.68024 0.09497  -0.05598 -0.04678 129 ILE B CG1 
1648 C CG2 . ILE B 110 ? 0.71111 0.64293 0.75849 0.07941  -0.06483 -0.06609 129 ILE B CG2 
1649 C CD1 . ILE B 110 ? 0.65392 0.57039 0.66218 0.09461  -0.03581 -0.04533 129 ILE B CD1 
1650 N N   . GLU B 111 ? 0.71276 0.57523 0.70026 0.10079  -0.03291 -0.05681 130 GLU B N   
1651 C CA  . GLU B 111 ? 0.71582 0.57418 0.69893 0.09228  -0.03548 -0.06885 130 GLU B CA  
1652 C C   . GLU B 111 ? 0.74635 0.64336 0.75651 0.07632  -0.05980 -0.07994 130 GLU B C   
1653 O O   . GLU B 111 ? 0.77305 0.67956 0.80096 0.06237  -0.06392 -0.09089 130 GLU B O   
1654 C CB  . GLU B 111 ? 0.81789 0.62672 0.77687 0.07932  -0.00856 -0.08563 130 GLU B CB  
1655 C CG  . GLU B 111 ? 1.03935 0.80038 0.96792 0.10212  0.02131  -0.07094 130 GLU B CG  
1656 C CD  . GLU B 111 ? 0.97507 0.67779 0.87768 0.08529  0.05467  -0.09248 130 GLU B CD  
1657 O OE1 . GLU B 111 ? 1.01842 0.71602 0.92556 0.05313  0.05872  -0.11907 130 GLU B OE1 
1658 O OE2 . GLU B 111 ? 1.14036 0.80461 1.01945 0.10269  0.07948  -0.08527 130 GLU B OE2 
1659 N N   . VAL B 112 ? 0.64702 0.56670 0.66006 0.08126  -0.07347 -0.07460 131 VAL B N   
1660 C CA  . VAL B 112 ? 0.63550 0.59040 0.67155 0.07626  -0.09415 -0.07472 131 VAL B CA  
1661 C C   . VAL B 112 ? 0.66873 0.63582 0.69045 0.07287  -0.10044 -0.07891 131 VAL B C   
1662 O O   . VAL B 112 ? 0.76225 0.71678 0.76220 0.07960  -0.09282 -0.07453 131 VAL B O   
1663 C CB  . VAL B 112 ? 0.55486 0.52598 0.60772 0.08700  -0.10141 -0.05865 131 VAL B CB  
1664 C CG1 . VAL B 112 ? 0.70219 0.69243 0.76263 0.09002  -0.11324 -0.05037 131 VAL B CG1 
1665 C CG2 . VAL B 112 ? 0.60865 0.58501 0.68400 0.08220  -0.10140 -0.06164 131 VAL B CG2 
1666 N N   . ASN B 113 ? 0.62029 0.61875 0.65405 0.06354  -0.11397 -0.08725 132 ASN B N   
1667 C CA  . ASN B 113 ? 0.69493 0.72218 0.71522 0.06181  -0.12488 -0.08805 132 ASN B CA  
1668 C C   . ASN B 113 ? 0.76770 0.81427 0.79969 0.07985  -0.13823 -0.06246 132 ASN B C   
1669 O O   . ASN B 113 ? 0.67687 0.73311 0.73705 0.08743  -0.14414 -0.05269 132 ASN B O   
1670 C CB  . ASN B 113 ? 0.68329 0.75087 0.71066 0.04423  -0.13365 -0.10895 132 ASN B CB  
1671 C CG  . ASN B 113 ? 0.92503 0.96703 0.94076 0.01946  -0.11341 -0.13894 132 ASN B CG  
1672 O OD1 . ASN B 113 ? 1.05042 1.09739 1.04270 -0.00013 -0.10535 -0.16175 132 ASN B OD1 
1673 N ND2 . ASN B 113 ? 1.00086 1.01303 1.03020 0.01800  -0.10140 -0.14044 132 ASN B ND2 
1674 N N   . LEU B 114 ? 0.84232 0.88929 0.85142 0.08597  -0.13827 -0.05229 133 LEU B N   
1675 C CA  . LEU B 114 ? 0.80186 0.85842 0.81509 0.10147  -0.14448 -0.02683 133 LEU B CA  
1676 C C   . LEU B 114 ? 0.80387 0.90555 0.81342 0.10701  -0.16100 -0.01928 133 LEU B C   
1677 O O   . LEU B 114 ? 0.80397 0.92994 0.78632 0.09852  -0.16592 -0.02954 133 LEU B O   
1678 C CB  . LEU B 114 ? 0.76682 0.80532 0.75620 0.10476  -0.13405 -0.01885 133 LEU B CB  
1679 C CG  . LEU B 114 ? 0.67142 0.68279 0.66428 0.10430  -0.11910 -0.02332 133 LEU B CG  
1680 C CD1 . LEU B 114 ? 0.69170 0.69842 0.66472 0.10855  -0.10916 -0.01619 133 LEU B CD1 
1681 C CD2 . LEU B 114 ? 0.70774 0.71441 0.73073 0.10654  -0.11732 -0.01696 133 LEU B CD2 
1682 N N   . THR B 115 ? 0.70447 0.82172 0.74049 0.12226  -0.16802 -0.00167 134 THR B N   
1683 C CA  . THR B 115 ? 0.87923 1.05054 0.91469 0.13601  -0.18467 0.01226  134 THR B CA  
1684 C C   . THR B 115 ? 0.90553 1.06503 0.93376 0.16158  -0.18028 0.05009  134 THR B C   
1685 O O   . THR B 115 ? 0.89532 1.00924 0.93985 0.16869  -0.16412 0.06288  134 THR B O   
1686 C CB  . THR B 115 ? 0.83018 1.03596 0.90359 0.14033  -0.19356 0.00680  134 THR B CB  
1687 O OG1 . THR B 115 ? 0.96046 1.13436 1.06294 0.15880  -0.18282 0.02713  134 THR B OG1 
1688 C CG2 . THR B 115 ? 0.83184 1.03103 0.91421 0.11263  -0.18926 -0.02968 134 THR B CG2 
1689 N N   . ASP B 116 ? 1.46494 1.42853 0.63283 -0.26751 0.01747  0.07464  135 ASP B N   
1690 C CA  . ASP B 116 ? 1.58913 1.49161 0.66665 -0.26259 0.04242  0.13392  135 ASP B CA  
1691 C C   . ASP B 116 ? 1.70888 1.60237 0.74194 -0.20727 0.00417  0.21347  135 ASP B C   
1692 O O   . ASP B 116 ? 1.76695 1.59849 0.72236 -0.19416 0.02512  0.27543  135 ASP B O   
1693 C CB  . ASP B 116 ? 1.67201 1.61146 0.64357 -0.30520 0.06638  0.12236  135 ASP B CB  
1694 C CG  . ASP B 116 ? 1.81869 1.67199 0.73940 -0.33108 0.12825  0.13996  135 ASP B CG  
1695 O OD1 . ASP B 116 ? 1.74064 1.59463 0.67749 -0.38079 0.17281  0.08033  135 ASP B OD1 
1696 O OD2 . ASP B 116 ? 2.01041 1.79220 0.88052 -0.30246 0.13723  0.21135  135 ASP B OD2 
1697 N N   . ARG B 117 ? 1.71520 1.66570 0.79862 -0.17393 -0.04703 0.21351  136 ARG B N   
1698 C CA  . ARG B 117 ? 1.86156 1.80344 0.92732 -0.11585 -0.08229 0.28411  136 ARG B CA  
1699 C C   . ARG B 117 ? 1.93510 1.76696 1.05933 -0.09297 -0.05474 0.31071  136 ARG B C   
1700 O O   . ARG B 117 ? 1.72081 1.50877 0.91781 -0.11828 -0.02298 0.26526  136 ARG B O   
1701 C CB  . ARG B 117 ? 1.73017 1.76806 0.84934 -0.09143 -0.13913 0.26535  136 ARG B CB  
1702 N N   . SER B 118 ? 2.14235 1.93546 1.23849 -0.04297 -0.06722 0.38301  137 SER B N   
1703 C CA  . SER B 118 ? 2.19201 1.88644 1.35103 -0.01978 -0.04113 0.40420  137 SER B CA  
1704 C C   . SER B 118 ? 2.23330 1.93975 1.43006 0.04085  -0.08119 0.44628  137 SER B C   
1705 O O   . SER B 118 ? 2.19387 1.83163 1.46024 0.05810  -0.06226 0.44992  137 SER B O   
1706 C CB  . SER B 118 ? 2.24158 1.82506 1.33487 -0.02748 0.01732  0.45126  137 SER B CB  
1707 O OG  . SER B 118 ? 2.10751 1.67488 1.18700 -0.08681 0.06240  0.40236  137 SER B OG  
1708 N N   . ALA B 119 ? 2.18683 1.98579 1.34598 0.07232  -0.13457 0.47229  138 ALA B N   
1709 C CA  . ALA B 119 ? 2.11550 1.94398 1.32844 0.12955  -0.17532 0.50081  138 ALA B CA  
1710 C C   . ALA B 119 ? 2.02993 1.88195 1.35997 0.11966  -0.18526 0.43703  138 ALA B C   
1711 O O   . ALA B 119 ? 1.92208 1.77650 1.31383 0.16105  -0.20455 0.45205  138 ALA B O   
1712 C CB  . ALA B 119 ? 2.06296 1.99004 1.24398 0.14746  -0.23001 0.49844  138 ALA B CB  
1713 N N   . PHE B 120 ? 2.01934 1.88803 1.38028 0.06783  -0.17054 0.36834  139 PHE B N   
1714 C CA  . PHE B 120 ? 1.90840 1.78357 1.36954 0.05831  -0.17239 0.31516  139 PHE B CA  
1715 C C   . PHE B 120 ? 1.96640 1.74246 1.47555 0.07166  -0.13801 0.32857  139 PHE B C   
1716 O O   . PHE B 120 ? 1.96200 1.66841 1.46290 0.04390  -0.09410 0.31920  139 PHE B O   
1717 C CB  . PHE B 120 ? 1.75809 1.65694 1.23689 0.00572  -0.15737 0.24909  139 PHE B CB  
1718 N N   . GLN B 121 ? 1.99706 1.77164 1.56116 0.11124  -0.15458 0.34449  140 GLN B N   
1719 C CA  . GLN B 121 ? 1.84675 1.53166 1.46017 0.12275  -0.11902 0.35195  140 GLN B CA  
1720 C C   . GLN B 121 ? 1.85355 1.51555 1.51630 0.07977  -0.09028 0.29147  140 GLN B C   
1721 O O   . GLN B 121 ? 1.80990 1.39731 1.47661 0.06206  -0.04572 0.28779  140 GLN B O   
1722 C CB  . GLN B 121 ? 1.80967 1.51374 1.48624 0.16710  -0.14238 0.36344  140 GLN B CB  
1723 C CG  . GLN B 121 ? 1.84415 1.46641 1.58454 0.17347  -0.10371 0.35573  140 GLN B CG  
1724 C CD  . GLN B 121 ? 1.84401 1.49692 1.65699 0.20889  -0.12431 0.35055  140 GLN B CD  
1725 O OE1 . GLN B 121 ? 1.80069 1.53827 1.62056 0.22950  -0.16825 0.35281  140 GLN B OE1 
1726 N NE2 . GLN B 121 ? 1.86651 1.45564 1.73844 0.21225  -0.08908 0.33676  140 GLN B NE2 
1727 N N   . TYR B 122 ? 1.66831 1.39593 1.37083 0.06363  -0.11370 0.24377  141 TYR B N   
1728 C CA  . TYR B 122 ? 1.43518 1.15045 1.18628 0.03287  -0.09286 0.19256  141 TYR B CA  
1729 C C   . TYR B 122 ? 1.29291 1.01215 1.01128 -0.00543 -0.07603 0.16895  141 TYR B C   
1730 O O   . TYR B 122 ? 1.28404 1.05437 0.96890 -0.01576 -0.09506 0.16332  141 TYR B O   
1731 C CB  . TYR B 122 ? 1.22391 0.99587 1.02915 0.03656  -0.11965 0.15921  141 TYR B CB  
1732 C CG  . TYR B 122 ? 1.28157 1.03904 1.13325 0.06615  -0.12228 0.16893  141 TYR B CG  
1733 C CD1 . TYR B 122 ? 1.30335 1.01733 1.19861 0.06007  -0.09429 0.14822  141 TYR B CD1 
1734 C CD2 . TYR B 122 ? 1.32880 1.12248 1.18501 0.09925  -0.15069 0.19432  141 TYR B CD2 
1735 C CE1 . TYR B 122 ? 1.36245 1.06221 1.30266 0.08366  -0.09064 0.15107  141 TYR B CE1 
1736 C CE2 . TYR B 122 ? 1.38239 1.16265 1.28858 0.12704  -0.14882 0.20003  141 TYR B CE2 
1737 C CZ  . TYR B 122 ? 1.41726 1.14639 1.36405 0.11804  -0.11665 0.17804  141 TYR B CZ  
1738 O OH  . TYR B 122 ? 1.35176 1.06777 1.35154 0.14201  -0.10939 0.17689  141 TYR B OH  
1739 N N   . PRO B 123 ? 1.10694 0.77830 0.83984 -0.02911 -0.03765 0.14914  142 PRO B N   
1740 C CA  . PRO B 123 ? 0.99789 0.67332 0.70678 -0.06517 -0.01657 0.12418  142 PRO B CA  
1741 C C   . PRO B 123 ? 0.93714 0.67445 0.67430 -0.07913 -0.03627 0.08267  142 PRO B C   
1742 O O   . PRO B 123 ? 0.92648 0.68291 0.63372 -0.10274 -0.02851 0.06815  142 PRO B O   
1743 C CB  . PRO B 123 ? 1.04428 0.66872 0.79030 -0.08478 0.02658  0.10066  142 PRO B CB  
1744 C CG  . PRO B 123 ? 1.18502 0.75704 0.94371 -0.06064 0.03735  0.13004  142 PRO B CG  
1745 C CD  . PRO B 123 ? 1.10794 0.72263 0.88360 -0.02669 -0.00719 0.14393  142 PRO B CD  
1746 N N   . LEU B 124 ? 0.84943 0.61360 0.64301 -0.06618 -0.05617 0.06279  143 LEU B N   
1747 C CA  . LEU B 124 ? 0.79339 0.60308 0.61639 -0.07413 -0.07005 0.03031  143 LEU B CA  
1748 C C   . LEU B 124 ? 0.75148 0.59766 0.58072 -0.05458 -0.10223 0.03981  143 LEU B C   
1749 O O   . LEU B 124 ? 0.81169 0.65395 0.66544 -0.03335 -0.11334 0.05037  143 LEU B O   
1750 C CB  . LEU B 124 ? 0.65257 0.46352 0.53503 -0.07712 -0.06051 -0.00209 143 LEU B CB  
1751 C CG  . LEU B 124 ? 0.66956 0.51665 0.58416 -0.07662 -0.07225 -0.02617 143 LEU B CG  
1752 C CD1 . LEU B 124 ? 0.71883 0.57463 0.61572 -0.09873 -0.05854 -0.04178 143 LEU B CD1 
1753 C CD2 . LEU B 124 ? 0.72272 0.58034 0.69062 -0.07076 -0.06894 -0.04994 143 LEU B CD2 
1754 N N   . LEU B 125 ? 0.72024 0.60432 0.53164 -0.06557 -0.11254 0.02998  144 LEU B N   
1755 C CA  . LEU B 125 ? 0.70148 0.62739 0.52743 -0.05570 -0.13660 0.02700  144 LEU B CA  
1756 C C   . LEU B 125 ? 0.71446 0.64876 0.57955 -0.06733 -0.12856 -0.00514 144 LEU B C   
1757 O O   . LEU B 125 ? 0.71028 0.64725 0.57214 -0.08913 -0.11218 -0.02761 144 LEU B O   
1758 C CB  . LEU B 125 ? 0.68121 0.65231 0.46280 -0.06217 -0.15163 0.03376  144 LEU B CB  
1759 C CG  . LEU B 125 ? 0.76093 0.78708 0.56275 -0.05312 -0.17640 0.02722  144 LEU B CG  
1760 C CD1 . LEU B 125 ? 0.81323 0.83637 0.63146 -0.01811 -0.19486 0.05741  144 LEU B CD1 
1761 C CD2 . LEU B 125 ? 0.88202 0.97225 0.64528 -0.06918 -0.18922 0.01715  144 LEU B CD2 
1762 N N   . ILE B 126 ? 0.65851 0.59305 0.55946 -0.05187 -0.13628 -0.00592 145 ILE B N   
1763 C CA  . ILE B 126 ? 0.64676 0.57914 0.58011 -0.05506 -0.12707 -0.02488 145 ILE B CA  
1764 C C   . ILE B 126 ? 0.62127 0.58048 0.56106 -0.06056 -0.13199 -0.03318 145 ILE B C   
1765 O O   . ILE B 126 ? 0.63352 0.60699 0.58217 -0.04780 -0.14514 -0.02416 145 ILE B O   
1766 C CB  . ILE B 126 ? 0.70126 0.61893 0.66156 -0.03634 -0.12900 -0.02012 145 ILE B CB  
1767 C CG1 . ILE B 126 ? 0.70934 0.61001 0.67200 -0.03736 -0.12019 -0.02251 145 ILE B CG1 
1768 C CG2 . ILE B 126 ? 0.64162 0.55606 0.62620 -0.03235 -0.12112 -0.02881 145 ILE B CG2 
1769 C CD1 . ILE B 126 ? 0.60255 0.50624 0.59471 -0.02392 -0.12218 -0.02878 145 ILE B CD1 
1770 N N   . GLY B 127 ? 0.59969 0.56651 0.54132 -0.08278 -0.11625 -0.05631 146 GLY B N   
1771 C CA  . GLY B 127 ? 0.56782 0.56224 0.52062 -0.09725 -0.11256 -0.07469 146 GLY B CA  
1772 C C   . GLY B 127 ? 0.62168 0.58762 0.60646 -0.09173 -0.09562 -0.07666 146 GLY B C   
1773 O O   . GLY B 127 ? 0.61882 0.55304 0.61272 -0.07106 -0.09447 -0.05924 146 GLY B O   
1774 N N   . SER B 128 ? 0.71683 0.69857 0.71691 -0.11175 -0.08076 -0.09916 147 SER B N   
1775 C CA  . SER B 128 ? 0.58461 0.53268 0.60813 -0.10836 -0.05856 -0.09649 147 SER B CA  
1776 C C   . SER B 128 ? 0.65710 0.54884 0.69480 -0.10235 -0.03069 -0.09231 147 SER B C   
1777 O O   . SER B 128 ? 0.68234 0.53780 0.72497 -0.07994 -0.02378 -0.06789 147 SER B O   
1778 C CB  . SER B 128 ? 0.58041 0.55739 0.62245 -0.13760 -0.04109 -0.12806 147 SER B CB  
1779 O OG  . SER B 128 ? 0.63891 0.62931 0.68857 -0.17006 -0.01993 -0.16554 147 SER B OG  
1780 N N   . GLU B 129 ? 0.61449 0.50192 0.65882 -0.11984 -0.01421 -0.11525 148 GLU B N   
1781 C CA  . GLU B 129 ? 0.65745 0.49331 0.72744 -0.10996 0.01454  -0.11320 148 GLU B CA  
1782 C C   . GLU B 129 ? 0.66155 0.48687 0.72933 -0.07355 -0.00651 -0.08251 148 GLU B C   
1783 O O   . GLU B 129 ? 0.62494 0.41628 0.70938 -0.04618 0.00251  -0.06032 148 GLU B O   
1784 C CB  . GLU B 129 ? 0.71263 0.55277 0.79543 -0.14052 0.04007  -0.15284 148 GLU B CB  
1785 C CG  . GLU B 129 ? 0.73180 0.57528 0.83258 -0.17878 0.07442  -0.19251 148 GLU B CG  
1786 C CD  . GLU B 129 ? 0.89898 0.76352 1.00640 -0.21662 0.09815  -0.24150 148 GLU B CD  
1787 O OE1 . GLU B 129 ? 1.01365 0.90657 1.13043 -0.25615 0.11981  -0.28521 148 GLU B OE1 
1788 O OE2 . GLU B 129 ? 1.11611 0.97499 1.22098 -0.21038 0.09746  -0.24180 148 GLU B OE2 
1789 N N   . ALA B 130 ? 0.68796 0.54476 0.73526 -0.07230 -0.03332 -0.08077 149 ALA B N   
1790 C CA  . ALA B 130 ? 0.57353 0.43048 0.62484 -0.04444 -0.05089 -0.06169 149 ALA B CA  
1791 C C   . ALA B 130 ? 0.63647 0.49390 0.68064 -0.01936 -0.06793 -0.03475 149 ALA B C   
1792 O O   . ALA B 130 ? 0.65444 0.50687 0.71083 0.00765  -0.07244 -0.01908 149 ALA B O   
1793 C CB  . ALA B 130 ? 0.68448 0.56576 0.71457 -0.05408 -0.06702 -0.06703 149 ALA B CB  
1794 N N   . LEU B 131 ? 0.61134 0.48202 0.63695 -0.02760 -0.07710 -0.03129 150 LEU B N   
1795 C CA  . LEU B 131 ? 0.52709 0.39966 0.54395 -0.00942 -0.08749 -0.01117 150 LEU B CA  
1796 C C   . LEU B 131 ? 0.64671 0.48496 0.66869 0.00382  -0.06647 0.00523  150 LEU B C   
1797 O O   . LEU B 131 ? 0.61067 0.44972 0.62075 0.02766  -0.07541 0.02763  150 LEU B O   
1798 C CB  . LEU B 131 ? 0.56371 0.45918 0.57039 -0.02254 -0.09559 -0.01641 150 LEU B CB  
1799 C CG  . LEU B 131 ? 0.60020 0.52345 0.59838 -0.02312 -0.11827 -0.01892 150 LEU B CG  
1800 C CD1 . LEU B 131 ? 0.68319 0.63611 0.68130 -0.03198 -0.12610 -0.02494 150 LEU B CD1 
1801 C CD2 . LEU B 131 ? 0.57423 0.49987 0.57123 -0.00375 -0.13160 -0.00828 150 LEU B CD2 
1802 N N   . LYS B 132 ? 0.63394 0.44098 0.67120 -0.01173 -0.03548 -0.00543 151 LYS B N   
1803 C CA  . LYS B 132 ? 0.67760 0.43549 0.72173 0.00524  -0.00784 0.01649  151 LYS B CA  
1804 C C   . LYS B 132 ? 0.72486 0.47663 0.78259 0.04073  -0.01624 0.03560  151 LYS B C   
1805 O O   . LYS B 132 ? 0.68453 0.42149 0.73117 0.07363  -0.01787 0.07014  151 LYS B O   
1806 C CB  . LYS B 132 ? 0.69781 0.41675 0.76544 -0.02261 0.03608  -0.00586 151 LYS B CB  
1807 C CG  . LYS B 132 ? 0.87973 0.60906 0.94217 -0.05599 0.05031  -0.02609 151 LYS B CG  
1808 C CD  . LYS B 132 ? 0.95800 0.65800 1.05090 -0.09130 0.09790  -0.06088 151 LYS B CD  
1809 C CE  . LYS B 132 ? 1.01493 0.73067 1.12800 -0.10798 0.10076  -0.09419 151 LYS B CE  
1810 N NZ  . LYS B 132 ? 0.98523 0.67430 1.13199 -0.14679 0.15320  -0.13632 151 LYS B NZ  
1811 N N   . ARG B 133 ? 0.66432 0.43414 0.74526 0.03530  -0.02201 0.01319  152 ARG B N   
1812 C CA  . ARG B 133 ? 0.70459 0.48446 0.81009 0.06842  -0.03207 0.02353  152 ARG B CA  
1813 C C   . ARG B 133 ? 0.73798 0.56422 0.82432 0.09306  -0.06944 0.04048  152 ARG B C   
1814 O O   . ARG B 133 ? 0.63221 0.47404 0.73108 0.12993  -0.08098 0.05997  152 ARG B O   
1815 C CB  . ARG B 133 ? 0.66897 0.46504 0.80307 0.05053  -0.02741 -0.01087 152 ARG B CB  
1816 C CG  . ARG B 133 ? 0.72147 0.47861 0.88281 0.02826  0.01344  -0.03468 152 ARG B CG  
1817 C CD  . ARG B 133 ? 0.72602 0.49768 0.92489 0.02518  0.02190  -0.06219 152 ARG B CD  
1818 N NE  . ARG B 133 ? 0.88106 0.62208 1.10609 -0.00313 0.06424  -0.09515 152 ARG B NE  
1819 C CZ  . ARG B 133 ? 0.91099 0.66290 1.16543 -0.01827 0.08127  -0.12922 152 ARG B CZ  
1820 N NH1 . ARG B 133 ? 0.82218 0.61252 1.08607 -0.00862 0.06128  -0.13437 152 ARG B NH1 
1821 N NH2 . ARG B 133 ? 0.83608 0.56142 1.11385 -0.04778 0.12410  -0.16451 152 ARG B NH2 
1822 N N   . PHE B 134 ? 0.70163 0.55514 0.76111 0.07450  -0.08786 0.03133  153 PHE B N   
1823 C CA  . PHE B 134 ? 0.67711 0.57532 0.72198 0.09025  -0.11686 0.03726  153 PHE B CA  
1824 C C   . PHE B 134 ? 0.63656 0.53173 0.64803 0.10783  -0.12006 0.06636  153 PHE B C   
1825 O O   . PHE B 134 ? 0.70885 0.64772 0.70484 0.11950  -0.14252 0.06785  153 PHE B O   
1826 C CB  . PHE B 134 ? 0.66851 0.58880 0.70470 0.06475  -0.12843 0.01484  153 PHE B CB  
1827 C CG  . PHE B 134 ? 0.59999 0.54245 0.65969 0.05747  -0.13365 -0.00865 153 PHE B CG  
1828 C CD1 . PHE B 134 ? 0.63653 0.62291 0.71143 0.07103  -0.14993 -0.01849 153 PHE B CD1 
1829 C CD2 . PHE B 134 ? 0.63183 0.55638 0.69692 0.03370  -0.11958 -0.02455 153 PHE B CD2 
1830 C CE1 . PHE B 134 ? 0.63595 0.64169 0.73793 0.05920  -0.14757 -0.04542 153 PHE B CE1 
1831 C CE2 . PHE B 134 ? 0.73176 0.67078 0.81381 0.02353  -0.11747 -0.04540 153 PHE B CE2 
1832 C CZ  . PHE B 134 ? 0.64956 0.62600 0.75348 0.03533  -0.12919 -0.05669 153 PHE B CZ  
1833 N N   . ASP B 135 ? 0.69225 0.53790 0.69147 0.10634  -0.09383 0.08579  154 ASP B N   
1834 C CA  . ASP B 135 ? 0.74202 0.57571 0.70164 0.11661  -0.08816 0.11428  154 ASP B CA  
1835 C C   . ASP B 135 ? 0.78815 0.65772 0.72689 0.09689  -0.10287 0.09735  154 ASP B C   
1836 O O   . ASP B 135 ? 0.81564 0.71432 0.72416 0.10917  -0.11592 0.10839  154 ASP B O   
1837 C CB  . ASP B 135 ? 0.83135 0.68152 0.77372 0.16077  -0.10244 0.14966  154 ASP B CB  
1838 C CG  . ASP B 135 ? 0.92851 0.75028 0.90557 0.18889  -0.09110 0.16578  154 ASP B CG  
1839 O OD1 . ASP B 135 ? 0.99203 0.74799 0.98617 0.17808  -0.05376 0.16889  154 ASP B OD1 
1840 O OD2 . ASP B 135 ? 0.97357 0.84364 0.96765 0.22096  -0.11756 0.17037  154 ASP B OD2 
1841 N N   . ALA B 136 ? 0.64674 0.51773 0.60263 0.06737  -0.10001 0.06957  155 ALA B N   
1842 C CA  . ALA B 136 ? 0.68051 0.58542 0.63205 0.05378  -0.11460 0.05130  155 ALA B CA  
1843 C C   . ALA B 136 ? 0.74032 0.63456 0.68251 0.03605  -0.09689 0.04923  155 ALA B C   
1844 O O   . ALA B 136 ? 0.69452 0.55897 0.64425 0.02147  -0.07307 0.04820  155 ALA B O   
1845 C CB  . ALA B 136 ? 0.59327 0.51123 0.56884 0.03958  -0.12529 0.02779  155 ALA B CB  
1846 N N   . LEU B 137 ? 0.80104 0.72377 0.73272 0.03465  -0.10494 0.04234  156 LEU B N   
1847 C CA  . LEU B 137 ? 0.67939 0.60902 0.61710 0.01644  -0.09222 0.02917  156 LEU B CA  
1848 C C   . LEU B 137 ? 0.69742 0.65956 0.66139 0.01343  -0.11092 0.00723  156 LEU B C   
1849 O O   . LEU B 137 ? 0.72456 0.70542 0.68679 0.02271  -0.12430 0.00173  156 LEU B O   
1850 C CB  . LEU B 137 ? 0.66861 0.60065 0.57349 0.01799  -0.07825 0.03930  156 LEU B CB  
1851 C CG  . LEU B 137 ? 0.84302 0.73814 0.70711 0.02943  -0.05859 0.07345  156 LEU B CG  
1852 C CD1 . LEU B 137 ? 0.85067 0.75530 0.67329 0.02667  -0.04425 0.08133  156 LEU B CD1 
1853 C CD2 . LEU B 137 ? 0.84777 0.69339 0.72635 0.01524  -0.02750 0.07826  156 LEU B CD2 
1854 N N   . VAL B 138 ? 0.70165 0.67266 0.69162 0.00140  -0.11029 -0.00592 157 VAL B N   
1855 C CA  . VAL B 138 ? 0.64273 0.63710 0.65709 0.00597  -0.12741 -0.01699 157 VAL B CA  
1856 C C   . VAL B 138 ? 0.66142 0.68109 0.69525 0.00513  -0.12177 -0.03069 157 VAL B C   
1857 O O   . VAL B 138 ? 0.61637 0.65139 0.66516 -0.00649 -0.11003 -0.04064 157 VAL B O   
1858 C CB  . VAL B 138 ? 0.54676 0.54873 0.57467 -0.00040 -0.13554 -0.02004 157 VAL B CB  
1859 C CG1 . VAL B 138 ? 0.57508 0.59491 0.62088 0.01201  -0.15276 -0.02001 157 VAL B CG1 
1860 C CG2 . VAL B 138 ? 0.55676 0.53365 0.56834 -0.00324 -0.13496 -0.01260 157 VAL B CG2 
1861 N N   . ASP B 139 ? 0.59953 0.62620 0.63947 0.01456  -0.12581 -0.03735 158 ASP B N   
1862 C CA  . ASP B 139 ? 0.60452 0.65472 0.67340 0.01556  -0.11800 -0.05537 158 ASP B CA  
1863 C C   . ASP B 139 ? 0.61258 0.67013 0.72076 0.03017  -0.13092 -0.05583 158 ASP B C   
1864 O O   . ASP B 139 ? 0.61518 0.65366 0.72584 0.03990  -0.13600 -0.05168 158 ASP B O   
1865 C CB  . ASP B 139 ? 0.59954 0.65430 0.65560 0.01519  -0.10969 -0.06805 158 ASP B CB  
1866 C CG  . ASP B 139 ? 0.60474 0.68372 0.68948 0.01103  -0.09296 -0.09267 158 ASP B CG  
1867 O OD1 . ASP B 139 ? 0.62905 0.72152 0.75959 0.01741  -0.09337 -0.09949 158 ASP B OD1 
1868 O OD2 . ASP B 139 ? 0.67238 0.76367 0.73500 0.00225  -0.07964 -0.10703 158 ASP B OD2 
1869 N N   . PRO B 140 ? 0.56139 0.64802 0.70150 0.03332  -0.13530 -0.05999 159 PRO B N   
1870 C CA  . PRO B 140 ? 0.67652 0.77412 0.84952 0.05603  -0.15149 -0.05120 159 PRO B CA  
1871 C C   . PRO B 140 ? 0.63082 0.72114 0.84106 0.07338  -0.14204 -0.05946 159 PRO B C   
1872 O O   . PRO B 140 ? 0.65181 0.73162 0.88406 0.09759  -0.15075 -0.04341 159 PRO B O   
1873 C CB  . PRO B 140 ? 0.51964 0.67049 0.72214 0.05471  -0.15980 -0.06035 159 PRO B CB  
1874 C CG  . PRO B 140 ? 0.56254 0.72457 0.76555 0.03051  -0.13614 -0.08331 159 PRO B CG  
1875 C CD  . PRO B 140 ? 0.56221 0.67673 0.71107 0.01660  -0.12439 -0.07318 159 PRO B CD  
1876 N N   . SER B 141 ? 0.64371 0.73688 0.86011 0.06185  -0.12112 -0.08349 160 SER B N   
1877 C CA  . SER B 141 ? 0.62435 0.70993 0.88135 0.07306  -0.10487 -0.10088 160 SER B CA  
1878 C C   . SER B 141 ? 0.61125 0.65719 0.84908 0.06876  -0.09631 -0.10330 160 SER B C   
1879 O O   . SER B 141 ? 0.52874 0.56028 0.80365 0.07458  -0.07686 -0.12200 160 SER B O   
1880 C CB  . SER B 141 ? 0.49253 0.60820 0.76633 0.05762  -0.08178 -0.13433 160 SER B CB  
1881 O OG  . SER B 141 ? 0.49677 0.60864 0.71424 0.03274  -0.07222 -0.14183 160 SER B OG  
1882 N N   . LEU B 142 ? 0.55760 0.58842 0.74671 0.05756  -0.10687 -0.08994 161 LEU B N   
1883 C CA  . LEU B 142 ? 0.65069 0.65792 0.82606 0.04950  -0.09945 -0.09898 161 LEU B CA  
1884 C C   . LEU B 142 ? 0.64989 0.62133 0.81703 0.05827  -0.10860 -0.07294 161 LEU B C   
1885 O O   . LEU B 142 ? 0.58452 0.55673 0.73464 0.06498  -0.12625 -0.04676 161 LEU B O   
1886 C CB  . LEU B 142 ? 0.59502 0.62329 0.72439 0.03148  -0.10324 -0.10761 161 LEU B CB  
1887 C CG  . LEU B 142 ? 0.68467 0.74723 0.80241 0.01933  -0.09107 -0.13083 161 LEU B CG  
1888 C CD1 . LEU B 142 ? 0.67601 0.75773 0.73900 0.01064  -0.09984 -0.12585 161 LEU B CD1 
1889 C CD2 . LEU B 142 ? 0.52108 0.59110 0.67605 0.01342  -0.06823 -0.16935 161 LEU B CD2 
1890 N N   . LYS B 143 ? 0.67604 0.61869 0.85413 0.05340  -0.09227 -0.08526 162 LYS B N   
1891 C CA  . LYS B 143 ? 0.67386 0.57653 0.84060 0.05565  -0.09147 -0.06473 162 LYS B CA  
1892 C C   . LYS B 143 ? 0.64133 0.54035 0.80803 0.03383  -0.07538 -0.09525 162 LYS B C   
1893 O O   . LYS B 143 ? 0.76860 0.67138 0.96522 0.02384  -0.05310 -0.13069 162 LYS B O   
1894 C CB  . LYS B 143 ? 0.62104 0.47944 0.81673 0.07869  -0.07890 -0.04225 162 LYS B CB  
1895 C CG  . LYS B 143 ? 0.60832 0.47339 0.78648 0.10085  -0.10409 -0.00074 162 LYS B CG  
1896 C CD  . LYS B 143 ? 0.64598 0.46731 0.84352 0.13108  -0.09468 0.03202  162 LYS B CD  
1897 C CE  . LYS B 143 ? 0.73401 0.58018 0.90428 0.15265  -0.12611 0.07239  162 LYS B CE  
1898 N NZ  . LYS B 143 ? 0.87475 0.68342 1.05449 0.19071  -0.12220 0.11560  162 LYS B NZ  
1899 N N   . TYR B 144 ? 0.74346 0.64317 0.88233 0.02460  -0.08512 -0.08778 163 TYR B N   
1900 C CA  . TYR B 144 ? 0.63709 0.54920 0.78211 0.00417  -0.07375 -0.12024 163 TYR B CA  
1901 C C   . TYR B 144 ? 0.66332 0.63455 0.81112 -0.00572 -0.07816 -0.15670 163 TYR B C   
1902 O O   . TYR B 144 ? 0.61610 0.60546 0.78941 -0.02288 -0.05944 -0.19921 163 TYR B O   
1903 C CB  . TYR B 144 ? 0.59850 0.46059 0.77471 -0.00537 -0.03847 -0.13410 163 TYR B CB  
1904 C CG  . TYR B 144 ? 0.70190 0.50277 0.86312 0.00766  -0.03244 -0.09008 163 TYR B CG  
1905 C CD1 . TYR B 144 ? 0.70589 0.49696 0.83878 -0.00085 -0.03662 -0.07579 163 TYR B CD1 
1906 C CD2 . TYR B 144 ? 0.64806 0.40583 0.82230 0.03053  -0.02259 -0.06209 163 TYR B CD2 
1907 C CE1 . TYR B 144 ? 0.73918 0.47982 0.84626 0.00902  -0.03069 -0.03479 163 TYR B CE1 
1908 C CE2 . TYR B 144 ? 0.68974 0.39917 0.84000 0.04691  -0.02092 -0.01561 163 TYR B CE2 
1909 C CZ  . TYR B 144 ? 0.71521 0.41659 0.82646 0.03404  -0.02476 -0.00213 163 TYR B CZ  
1910 O OH  . TYR B 144 ? 0.84455 0.50306 0.92049 0.04818  -0.02251 0.04455  163 TYR B OH  
1911 N N   . ALA B 145 ? 0.66508 0.66808 0.78350 0.00323  -0.10041 -0.14102 164 ALA B N   
1912 C CA  . ALA B 145 ? 0.62932 0.68867 0.73368 -0.00294 -0.10616 -0.16535 164 ALA B CA  
1913 C C   . ALA B 145 ? 0.64012 0.74596 0.73173 -0.00788 -0.12000 -0.18008 164 ALA B C   
1914 O O   . ALA B 145 ? 0.62983 0.79382 0.71496 -0.01559 -0.12293 -0.21061 164 ALA B O   
1915 C CB  . ALA B 145 ? 0.62728 0.69539 0.70023 0.00773  -0.11855 -0.13887 164 ALA B CB  
1916 N N   . ALA B 146 ? 0.65775 0.74767 0.74713 -0.00295 -0.12902 -0.16152 165 ALA B N   
1917 C CA  . ALA B 146 ? 0.59123 0.73134 0.67987 -0.00227 -0.14360 -0.17517 165 ALA B CA  
1918 C C   . ALA B 146 ? 0.70651 0.86953 0.83623 -0.02374 -0.12710 -0.22348 165 ALA B C   
1919 O O   . ALA B 146 ? 0.70143 0.92460 0.84183 -0.02450 -0.13995 -0.24536 165 ALA B O   
1920 C CB  . ALA B 146 ? 0.59822 0.71348 0.67639 0.01042  -0.15472 -0.14143 165 ALA B CB  
1921 N N   . GLY B 147 ? 0.64641 0.76423 0.80428 -0.04022 -0.09655 -0.24160 166 GLY B N   
1922 C CA  . GLY B 147 ? 0.59379 0.72216 0.79485 -0.06610 -0.07072 -0.29043 166 GLY B CA  
1923 C C   . GLY B 147 ? 0.64298 0.74892 0.85351 -0.06998 -0.06652 -0.28120 166 GLY B C   
1924 O O   . GLY B 147 ? 0.70590 0.77094 0.89020 -0.05450 -0.07720 -0.23569 166 GLY B O   
1925 N N   . LYS B 148 ? 0.62825 0.76859 0.87985 -0.09509 -0.04771 -0.33226 167 LYS B N   
1926 C CA  . LYS B 148 ? 0.75067 0.87503 1.01835 -0.10482 -0.03629 -0.33359 167 LYS B CA  
1927 C C   . LYS B 148 ? 0.62504 0.81316 0.88257 -0.08334 -0.07524 -0.32053 167 LYS B C   
1928 O O   . LYS B 148 ? 0.61935 0.88451 0.86958 -0.06701 -0.10707 -0.32774 167 LYS B O   
1929 C CB  . LYS B 148 ? 0.71931 0.86553 1.04334 -0.14276 0.00174  -0.40007 167 LYS B CB  
1930 C CG  . LYS B 148 ? 0.90045 0.95983 1.24185 -0.16458 0.05367  -0.40985 167 LYS B CG  
1931 C CD  . LYS B 148 ? 0.91122 0.85892 1.21814 -0.15223 0.07050  -0.34666 167 LYS B CD  
1932 C CE  . LYS B 148 ? 0.93000 0.78352 1.25467 -0.16567 0.12421  -0.34683 167 LYS B CE  
1933 N NZ  . LYS B 148 ? 1.02370 0.87437 1.39689 -0.20500 0.17669  -0.40047 167 LYS B NZ  
1934 N N   . PRO B 149 ? 0.58012 0.73522 0.83527 -0.08126 -0.07098 -0.29918 168 PRO B N   
1935 C CA  . PRO B 149 ? 0.69399 0.90348 0.95233 -0.05922 -0.10110 -0.28987 168 PRO B CA  
1936 C C   . PRO B 149 ? 0.71698 1.03308 1.02620 -0.06439 -0.11162 -0.34510 168 PRO B C   
1937 O O   . PRO B 149 ? 0.74339 1.07654 1.09845 -0.09665 -0.08256 -0.39650 168 PRO B O   
1938 C CB  . PRO B 149 ? 0.61935 0.76779 0.87412 -0.06758 -0.08068 -0.27096 168 PRO B CB  
1939 C CG  . PRO B 149 ? 0.68557 0.74278 0.90801 -0.08022 -0.05466 -0.24498 168 PRO B CG  
1940 C CD  . PRO B 149 ? 0.59620 0.65920 0.83939 -0.09560 -0.03783 -0.27691 168 PRO B CD  
1941 N N   . ALA B 150 ? 0.61678 1.00758 0.91814 -0.03189 -0.15205 -0.33425 169 ALA B N   
1942 C CA  . ALA B 150 ? 0.62654 1.14088 0.97167 -0.02727 -0.17355 -0.38199 169 ALA B CA  
1943 C C   . ALA B 150 ? 0.75177 1.31567 1.09216 0.02050  -0.21302 -0.34640 169 ALA B C   
1944 O O   . ALA B 150 ? 0.87063 1.49616 1.18506 0.04986  -0.24181 -0.33070 169 ALA B O   
1945 C CB  . ALA B 150 ? 0.56741 1.12981 0.89498 -0.03533 -0.17548 -0.40592 169 ALA B CB  
1946 N N   . CYS B 151 ? 0.65683 1.17423 1.01195 0.02981  -0.20385 -0.32391 170 CYS B N   
1947 C CA  . CYS B 151 ? 0.67437 1.22760 1.03858 0.07647  -0.23256 -0.29211 170 CYS B CA  
1948 C C   . CYS B 151 ? 0.60364 1.26250 1.04503 0.08321  -0.24222 -0.34019 170 CYS B C   
1949 O O   . CYS B 151 ? 0.80661 1.53971 1.24153 0.09872  -0.25820 -0.34901 170 CYS B O   
1950 C CB  . CYS B 151 ? 0.79981 1.25003 1.14449 0.08302  -0.21419 -0.24717 170 CYS B CB  
1951 S SG  . CYS B 151 ? 0.75999 1.09566 1.02689 0.07016  -0.19981 -0.19984 170 CYS B SG  
# 
