data_9MXX
# 
_entry.id   9MXX 
# 
_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   9MXX         pdb_00009mxx 10.2210/pdb9mxx/pdb 
WWPDB D_1000292022 ?            ?                   
# 
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 2025-04-23 ? 
# 
_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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MXX 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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              tezcan@ucsd.edu 
_pdbx_contact_author.name_first         Faik 
_pdbx_contact_author.name_last          Tezcan 
_pdbx_contact_author.name_mi            A. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4733-6500 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Srisantitham, S.' 1 ? 
'Tezcan, F.A.'     2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                12338 
_citation.page_last                 12346 
_citation.title                     'De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.5c03319 
_citation.pdbx_database_id_PubMed   40138671 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Srisantitham, S.' 1 ? 
primary 'Walker, A.L.'     2 ? 
primary 'Markel, U.'       3 ? 
primary 'Tezcan, F.A.'     4 ? 
# 
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 'De novo protein with intramolecular isopeptide bond dnIPB-2' 16969.174 1   ? ? ? ? 
2 non-polymer syn 'SULFATE ION'                                                 96.063    6   ? ? ? ? 
3 water       nat water                                                         18.015    123 ? ? ? ? 
# 
_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       
;SAGMSPVEAAKAEAIAAGKGKLLREEWSEEKTTGEDGLLEIDLETGKKATFQKVDAETGKPLAGAVFRLYRFLFEENGEF
VAERYVLVEVRSPEGYEPVVNTPIARITVTKDPETGKVTYEVEAVKNGASASLDEQPPSLDKTRKIYNKKAVKLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SAGMSPVEAAKAEAIAAGKGKLLREEWSEEKTTGEDGLLEIDLETGKKATFQKVDAETGKPLAGAVFRLYRFLFEENGEF
VAERYVLVEVRSPEGYEPVVNTPIARITVTKDPETGKVTYEVEAVKNGASASLDEQPPSLDKTRKIYNKKAVKLP
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ALA n 
1 3   GLY n 
1 4   MET n 
1 5   SER n 
1 6   PRO n 
1 7   VAL n 
1 8   GLU n 
1 9   ALA n 
1 10  ALA n 
1 11  LYS n 
1 12  ALA n 
1 13  GLU n 
1 14  ALA n 
1 15  ILE n 
1 16  ALA n 
1 17  ALA n 
1 18  GLY n 
1 19  LYS n 
1 20  GLY n 
1 21  LYS n 
1 22  LEU n 
1 23  LEU n 
1 24  ARG n 
1 25  GLU n 
1 26  GLU n 
1 27  TRP n 
1 28  SER n 
1 29  GLU n 
1 30  GLU n 
1 31  LYS n 
1 32  THR n 
1 33  THR n 
1 34  GLY n 
1 35  GLU n 
1 36  ASP n 
1 37  GLY n 
1 38  LEU n 
1 39  LEU n 
1 40  GLU n 
1 41  ILE n 
1 42  ASP n 
1 43  LEU n 
1 44  GLU n 
1 45  THR n 
1 46  GLY n 
1 47  LYS n 
1 48  LYS n 
1 49  ALA n 
1 50  THR n 
1 51  PHE n 
1 52  GLN n 
1 53  LYS n 
1 54  VAL n 
1 55  ASP n 
1 56  ALA n 
1 57  GLU n 
1 58  THR n 
1 59  GLY n 
1 60  LYS n 
1 61  PRO n 
1 62  LEU n 
1 63  ALA n 
1 64  GLY n 
1 65  ALA n 
1 66  VAL n 
1 67  PHE n 
1 68  ARG n 
1 69  LEU n 
1 70  TYR n 
1 71  ARG n 
1 72  PHE n 
1 73  LEU n 
1 74  PHE n 
1 75  GLU n 
1 76  GLU n 
1 77  ASN n 
1 78  GLY n 
1 79  GLU n 
1 80  PHE n 
1 81  VAL n 
1 82  ALA n 
1 83  GLU n 
1 84  ARG n 
1 85  TYR n 
1 86  VAL n 
1 87  LEU n 
1 88  VAL n 
1 89  GLU n 
1 90  VAL n 
1 91  ARG n 
1 92  SER n 
1 93  PRO n 
1 94  GLU n 
1 95  GLY n 
1 96  TYR n 
1 97  GLU n 
1 98  PRO n 
1 99  VAL n 
1 100 VAL n 
1 101 ASN n 
1 102 THR n 
1 103 PRO n 
1 104 ILE n 
1 105 ALA n 
1 106 ARG n 
1 107 ILE n 
1 108 THR n 
1 109 VAL n 
1 110 THR n 
1 111 LYS n 
1 112 ASP n 
1 113 PRO n 
1 114 GLU n 
1 115 THR n 
1 116 GLY n 
1 117 LYS n 
1 118 VAL n 
1 119 THR n 
1 120 TYR n 
1 121 GLU n 
1 122 VAL n 
1 123 GLU n 
1 124 ALA n 
1 125 VAL n 
1 126 LYS n 
1 127 ASN n 
1 128 GLY n 
1 129 ALA n 
1 130 SER n 
1 131 ALA n 
1 132 SER n 
1 133 LEU n 
1 134 ASP n 
1 135 GLU n 
1 136 GLN n 
1 137 PRO n 
1 138 PRO n 
1 139 SER n 
1 140 LEU n 
1 141 ASP n 
1 142 LYS n 
1 143 THR n 
1 144 ARG n 
1 145 LYS n 
1 146 ILE n 
1 147 TYR n 
1 148 ASN n 
1 149 LYS n 
1 150 LYS n 
1 151 ALA n 
1 152 VAL n 
1 153 LYS n 
1 154 LEU n 
1 155 PRO 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                   155 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_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 
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  
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   SER 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   ?   ?   ?   A . n 
A 1 4   MET 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  ILE 15  15  15  ILE ILE A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TRP 27  27  27  TRP TRP A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 TYR 147 147 147 TYR TYR A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 PRO 155 155 ?   ?   ?   A . 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 
B 2 SO4 1   201 1   SO4 SO4 A . 
C 2 SO4 1   202 2   SO4 SO4 A . 
D 2 SO4 1   203 3   SO4 SO4 A . 
E 2 SO4 1   204 4   SO4 SO4 A . 
F 2 SO4 1   205 5   SO4 SO4 A . 
G 2 SO4 1   206 6   SO4 SO4 A . 
H 3 HOH 1   301 93  HOH HOH A . 
H 3 HOH 2   302 117 HOH HOH A . 
H 3 HOH 3   303 57  HOH HOH A . 
H 3 HOH 4   304 12  HOH HOH A . 
H 3 HOH 5   305 25  HOH HOH A . 
H 3 HOH 6   306 56  HOH HOH A . 
H 3 HOH 7   307 51  HOH HOH A . 
H 3 HOH 8   308 119 HOH HOH A . 
H 3 HOH 9   309 88  HOH HOH A . 
H 3 HOH 10  310 45  HOH HOH A . 
H 3 HOH 11  311 96  HOH HOH A . 
H 3 HOH 12  312 106 HOH HOH A . 
H 3 HOH 13  313 22  HOH HOH A . 
H 3 HOH 14  314 7   HOH HOH A . 
H 3 HOH 15  315 84  HOH HOH A . 
H 3 HOH 16  316 55  HOH HOH A . 
H 3 HOH 17  317 33  HOH HOH A . 
H 3 HOH 18  318 101 HOH HOH A . 
H 3 HOH 19  319 27  HOH HOH A . 
H 3 HOH 20  320 1   HOH HOH A . 
H 3 HOH 21  321 10  HOH HOH A . 
H 3 HOH 22  322 107 HOH HOH A . 
H 3 HOH 23  323 67  HOH HOH A . 
H 3 HOH 24  324 122 HOH HOH A . 
H 3 HOH 25  325 6   HOH HOH A . 
H 3 HOH 26  326 58  HOH HOH A . 
H 3 HOH 27  327 85  HOH HOH A . 
H 3 HOH 28  328 73  HOH HOH A . 
H 3 HOH 29  329 89  HOH HOH A . 
H 3 HOH 30  330 21  HOH HOH A . 
H 3 HOH 31  331 77  HOH HOH A . 
H 3 HOH 32  332 69  HOH HOH A . 
H 3 HOH 33  333 79  HOH HOH A . 
H 3 HOH 34  334 11  HOH HOH A . 
H 3 HOH 35  335 26  HOH HOH A . 
H 3 HOH 36  336 14  HOH HOH A . 
H 3 HOH 37  337 82  HOH HOH A . 
H 3 HOH 38  338 59  HOH HOH A . 
H 3 HOH 39  339 109 HOH HOH A . 
H 3 HOH 40  340 98  HOH HOH A . 
H 3 HOH 41  341 113 HOH HOH A . 
H 3 HOH 42  342 31  HOH HOH A . 
H 3 HOH 43  343 110 HOH HOH A . 
H 3 HOH 44  344 81  HOH HOH A . 
H 3 HOH 45  345 47  HOH HOH A . 
H 3 HOH 46  346 120 HOH HOH A . 
H 3 HOH 47  347 41  HOH HOH A . 
H 3 HOH 48  348 29  HOH HOH A . 
H 3 HOH 49  349 54  HOH HOH A . 
H 3 HOH 50  350 28  HOH HOH A . 
H 3 HOH 51  351 35  HOH HOH A . 
H 3 HOH 52  352 18  HOH HOH A . 
H 3 HOH 53  353 104 HOH HOH A . 
H 3 HOH 54  354 115 HOH HOH A . 
H 3 HOH 55  355 76  HOH HOH A . 
H 3 HOH 56  356 121 HOH HOH A . 
H 3 HOH 57  357 103 HOH HOH A . 
H 3 HOH 58  358 23  HOH HOH A . 
H 3 HOH 59  359 65  HOH HOH A . 
H 3 HOH 60  360 32  HOH HOH A . 
H 3 HOH 61  361 53  HOH HOH A . 
H 3 HOH 62  362 24  HOH HOH A . 
H 3 HOH 63  363 9   HOH HOH A . 
H 3 HOH 64  364 68  HOH HOH A . 
H 3 HOH 65  365 62  HOH HOH A . 
H 3 HOH 66  366 44  HOH HOH A . 
H 3 HOH 67  367 61  HOH HOH A . 
H 3 HOH 68  368 123 HOH HOH A . 
H 3 HOH 69  369 30  HOH HOH A . 
H 3 HOH 70  370 118 HOH HOH A . 
H 3 HOH 71  371 71  HOH HOH A . 
H 3 HOH 72  372 3   HOH HOH A . 
H 3 HOH 73  373 52  HOH HOH A . 
H 3 HOH 74  374 78  HOH HOH A . 
H 3 HOH 75  375 63  HOH HOH A . 
H 3 HOH 76  376 20  HOH HOH A . 
H 3 HOH 77  377 19  HOH HOH A . 
H 3 HOH 78  378 4   HOH HOH A . 
H 3 HOH 79  379 92  HOH HOH A . 
H 3 HOH 80  380 86  HOH HOH A . 
H 3 HOH 81  381 66  HOH HOH A . 
H 3 HOH 82  382 46  HOH HOH A . 
H 3 HOH 83  383 90  HOH HOH A . 
H 3 HOH 84  384 39  HOH HOH A . 
H 3 HOH 85  385 102 HOH HOH A . 
H 3 HOH 86  386 83  HOH HOH A . 
H 3 HOH 87  387 13  HOH HOH A . 
H 3 HOH 88  388 97  HOH HOH A . 
H 3 HOH 89  389 72  HOH HOH A . 
H 3 HOH 90  390 70  HOH HOH A . 
H 3 HOH 91  391 49  HOH HOH A . 
H 3 HOH 92  392 48  HOH HOH A . 
H 3 HOH 93  393 94  HOH HOH A . 
H 3 HOH 94  394 40  HOH HOH A . 
H 3 HOH 95  395 75  HOH HOH A . 
H 3 HOH 96  396 50  HOH HOH A . 
H 3 HOH 97  397 112 HOH HOH A . 
H 3 HOH 98  398 38  HOH HOH A . 
H 3 HOH 99  399 87  HOH HOH A . 
H 3 HOH 100 400 43  HOH HOH A . 
H 3 HOH 101 401 74  HOH HOH A . 
H 3 HOH 102 402 8   HOH HOH A . 
H 3 HOH 103 403 111 HOH HOH A . 
H 3 HOH 104 404 60  HOH HOH A . 
H 3 HOH 105 405 114 HOH HOH A . 
H 3 HOH 106 406 80  HOH HOH A . 
H 3 HOH 107 407 42  HOH HOH A . 
H 3 HOH 108 408 95  HOH HOH A . 
H 3 HOH 109 409 116 HOH HOH A . 
H 3 HOH 110 410 5   HOH HOH A . 
H 3 HOH 111 411 16  HOH HOH A . 
H 3 HOH 112 412 105 HOH HOH A . 
H 3 HOH 113 413 37  HOH HOH A . 
H 3 HOH 114 414 64  HOH HOH A . 
H 3 HOH 115 415 15  HOH HOH A . 
H 3 HOH 116 416 2   HOH HOH A . 
H 3 HOH 117 417 91  HOH HOH A . 
H 3 HOH 118 418 17  HOH HOH A . 
H 3 HOH 119 419 34  HOH HOH A . 
H 3 HOH 120 420 99  HOH HOH A . 
H 3 HOH 121 421 108 HOH HOH A . 
H 3 HOH 122 422 36  HOH HOH A . 
H 3 HOH 123 423 100 HOH HOH A . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     ASN 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      148 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     ND2 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    A 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    ASN 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     148 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    ND2 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MXX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.570 
_cell.length_a_esd                 ? 
_cell.length_b                     112.570 
_cell.length_b_esd                 ? 
_cell.length_c                     84.700 
_cell.length_c_esd                 ? 
_cell.volume                       929521.360 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9MXX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                177 
_symmetry.space_group_name_Hall            'P 6 2' 
_symmetry.space_group_name_H-M             'P 6 2 2' 
_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                   9MXX 
_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             4.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          73.05 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              10.5 
_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    '0.2 M lithium sulfate, 0.1 M CHES buffer pH 10.5, and 2.0 M of ammonium sulfate' 
_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 PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-31 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.11583 
_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                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.11583 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          64.29 
_reflns.entry_id                                       9MXX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               48.76 
_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                                     23485 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.56 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                36.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.11 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1366 
_reflns.pdbx_Rpim_I_all                                0.02275 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1346 
_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                                    2.4 
_reflns_shell.d_res_low                                     2.486 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.85 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3793 
_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                               38.6 
_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                               5 
_reflns_shell.pdbx_Rpim_I_all                               0.796 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.734 
_reflns_shell.pdbx_CC_star                                  0.92 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.935 
_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                               108.70 
_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                                 9MXX 
_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                             48.74 
_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                     23485 
_refine.ls_number_reflns_R_free                  2364 
_refine.ls_number_reflns_R_work                  21121 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.79 
_refine.ls_percent_reflns_R_free                 10.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2200 
_refine.ls_R_factor_R_free                       0.2548 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2161 
_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                          1.37 
_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             1.1000 
_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                 32.0897 
_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                            0.3184 
_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                        48.74 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               1310 
_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        1157 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.0022  ? 1274 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4370  ? 1739 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0412  ? 194  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0036  ? 222  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.2382 ? 502  ? f_dihedral_angle_d ? ? 
# 
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 2.45  . . 139 1238 99.64  . . . . 0.3969 . . . . . . . . . . . 0.4269 
'X-RAY DIFFRACTION' 2.45 2.50  . . 147 1267 100.00 . . . . 0.3525 . . . . . . . . . . . 0.4274 
'X-RAY DIFFRACTION' 2.50 2.56  . . 140 1248 100.00 . . . . 0.3378 . . . . . . . . . . . 0.3281 
'X-RAY DIFFRACTION' 2.56 2.62  . . 138 1226 99.93  . . . . 0.3156 . . . . . . . . . . . 0.3677 
'X-RAY DIFFRACTION' 2.62 2.70  . . 137 1230 100.00 . . . . 0.2947 . . . . . . . . . . . 0.3596 
'X-RAY DIFFRACTION' 2.70 2.77  . . 141 1214 99.34  . . . . 0.2986 . . . . . . . . . . . 0.3458 
'X-RAY DIFFRACTION' 2.77 2.86  . . 133 1254 99.14  . . . . 0.2897 . . . . . . . . . . . 0.3378 
'X-RAY DIFFRACTION' 2.86 2.97  . . 144 1233 99.21  . . . . 0.2525 . . . . . . . . . . . 0.2752 
'X-RAY DIFFRACTION' 2.97 3.09  . . 135 1244 99.86  . . . . 0.2412 . . . . . . . . . . . 0.2841 
'X-RAY DIFFRACTION' 3.09 3.23  . . 134 1250 100.00 . . . . 0.2314 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 3.23 3.40  . . 140 1244 100.00 . . . . 0.2194 . . . . . . . . . . . 0.2544 
'X-RAY DIFFRACTION' 3.40 3.61  . . 136 1250 99.86  . . . . 0.2007 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 3.61 3.89  . . 138 1238 99.78  . . . . 0.2042 . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 3.89 4.28  . . 138 1239 100.00 . . . . 0.2020 . . . . . . . . . . . 0.2623 
'X-RAY DIFFRACTION' 4.28 4.89  . . 146 1240 99.93  . . . . 0.1606 . . . . . . . . . . . 0.2042 
'X-RAY DIFFRACTION' 4.90 6.16  . . 141 1244 100.00 . . . . 0.2022 . . . . . . . . . . . 0.1960 
'X-RAY DIFFRACTION' 6.17 48.74 . . 137 1262 99.86  . . . . 0.2021 . . . . . . . . . . . 0.2722 
# 
_struct.entry_id                     9MXX 
_struct.title                        'Computationally Designed protein with isopeptide bond dnIPB-2' 
_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        9MXX 
_struct_keywords.text            'Isopeptide, computational design, DE NOVO PROTEIN' 
_struct_keywords.pdbx_keywords   'DE NOVO PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9MXX 
_struct_ref.pdbx_db_accession          9MXX 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MXX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 155 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9MXX 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  155 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       155 
# 
_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   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 17680 ? 
1 MORE         -684  ? 
1 'SSA (A^2)'  41040 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z         1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_545  -y,x-y-1,z    -0.5000000000 -0.8660254038 0.0000000000 56.2850000000  0.8660254038  
-0.5000000000 0.0000000000 -97.4884797040 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
3 'crystal symmetry operation' 3_655  -x+y+1,-x,z   -0.5000000000 0.8660254038  0.0000000000 112.5700000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
4 'crystal symmetry operation' 10_556 -y,-x,-z+1    0.5000000000  -0.8660254038 0.0000000000 0.0000000000   -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 -1.0000000000 84.7000000000 
5 'crystal symmetry operation' 11_656 -x+y+1,y,-z+1 -1.0000000000 0.0000000000  0.0000000000 112.5700000000 0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 -1.0000000000 84.7000000000 
6 'crystal symmetry operation' 12_546 x,x-y-1,-z+1  0.5000000000  0.8660254038  0.0000000000 56.2850000000  0.8660254038  
-0.5000000000 0.0000000000 -97.4884797040 0.0000000000 0.0000000000 -1.0000000000 84.7000000000 
# 
_struct_conf.conf_type_id            HELX_P 
_struct_conf.id                      HELX_P1 
_struct_conf.pdbx_PDB_helix_id       AA1 
_struct_conf.beg_label_comp_id       PRO 
_struct_conf.beg_label_asym_id       A 
_struct_conf.beg_label_seq_id        6 
_struct_conf.pdbx_beg_PDB_ins_code   ? 
_struct_conf.end_label_comp_id       ILE 
_struct_conf.end_label_asym_id       A 
_struct_conf.end_label_seq_id        15 
_struct_conf.pdbx_end_PDB_ins_code   ? 
_struct_conf.beg_auth_comp_id        PRO 
_struct_conf.beg_auth_asym_id        A 
_struct_conf.beg_auth_seq_id         6 
_struct_conf.end_auth_comp_id        ILE 
_struct_conf.end_auth_asym_id        A 
_struct_conf.end_auth_seq_id         15 
_struct_conf.pdbx_PDB_helix_class    1 
_struct_conf.details                 ? 
_struct_conf.pdbx_PDB_helix_length   10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 4 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY A 20  ? TRP A 27  ? GLY A 20  TRP A 27  
AA1 2 VAL A 66  ? GLU A 76  ? VAL A 66  GLU A 76  
AA1 3 LYS A 31  ? THR A 32  ? LYS A 31  THR A 32  
AA2 1 GLY A 20  ? TRP A 27  ? GLY A 20  TRP A 27  
AA2 2 VAL A 66  ? GLU A 76  ? VAL A 66  GLU A 76  
AA2 3 PHE A 80  ? ARG A 91  ? PHE A 80  ARG A 91  
AA2 4 THR A 102 ? LYS A 111 ? THR A 102 LYS A 111 
AA2 5 VAL A 118 ? ALA A 124 ? VAL A 118 ALA A 124 
AA3 1 LEU A 38  ? ASP A 42  ? LEU A 38  ASP A 42  
AA3 2 LYS A 48  ? ASP A 55  ? LYS A 48  ASP A 55  
AA3 3 ARG A 144 ? ASN A 148 ? ARG A 144 ASN A 148 
AA3 4 ALA A 131 ? LEU A 133 ? ALA A 131 LEU A 133 
# 
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 GLU A 26  ? N GLU A 26  O ARG A 71  ? O ARG A 71  
AA1 2 3 O PHE A 67  ? O PHE A 67  N LYS A 31  ? N LYS A 31  
AA2 1 2 N GLU A 26  ? N GLU A 26  O ARG A 71  ? O ARG A 71  
AA2 2 3 N PHE A 74  ? N PHE A 74  O ALA A 82  ? O ALA A 82  
AA2 3 4 N TYR A 85  ? N TYR A 85  O ILE A 107 ? O ILE A 107 
AA2 4 5 N ARG A 106 ? N ARG A 106 O GLU A 123 ? O GLU A 123 
AA3 1 2 N LEU A 39  ? N LEU A 39  O PHE A 51  ? O PHE A 51  
AA3 2 3 N GLN A 52  ? N GLN A 52  O ILE A 146 ? O ILE A 146 
AA3 3 4 O TYR A 147 ? O TYR A 147 N SER A 132 ? N SER A 132 
# 
_pdbx_entry_details.entry_id                   9MXX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NZ 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    53 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   CG 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASN 
_pdbx_validate_close_contact.auth_seq_id_2    148 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.31 
# 
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 GLU A 57  ? ? -107.98 -60.02 
2 1 ASN A 77  ? ? 56.56   18.22  
3 1 GLU A 79  ? ? -137.92 -30.81 
4 1 ILE A 104 ? ? -122.39 -54.75 
5 1 LEU A 140 ? ? -87.25  36.95  
6 1 LEU A 140 ? ? -88.33  38.26  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1  1 A HOH 318 ? H HOH . 
2  1 A HOH 320 ? H HOH . 
3  1 A HOH 323 ? H HOH . 
4  1 A HOH 337 ? H HOH . 
5  1 A HOH 373 ? H HOH . 
6  1 A HOH 383 ? H HOH . 
7  1 A HOH 393 ? H HOH . 
8  1 A HOH 410 ? H HOH . 
9  1 A HOH 416 ? H HOH . 
10 1 A HOH 421 ? H HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z      
2  x-y,x,z    
3  y,-x+y,z   
4  -y,x-y,z   
5  -x+y,-x,z  
6  x-y,-y,-z  
7  -x,-x+y,-z 
8  -x,-y,z    
9  y,x,-z     
10 -y,-x,-z   
11 -x+y,y,-z  
12 x,x-y,-z   
# 
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 49.5437739217 -31.7245504425 24.0656486267 1.431233181    ? -0.328569487947    ? 0.0117025291024  
? 2.52187097649  ? -0.0152674381028 ? 0.721835461945   ? 6.45787078408 ? -5.29304795247   ? -3.43680456371  ? 9.2002428082   ? 
3.81658018396   ? 2.037728393   ? 1.1613338572     ? 2.6854453539    ? 0.0902991428421 ? -3.55946276241   ? -0.257344316696  ? 
0.114427385134   ? -2.54816650325  ? 0.00893314290008 ? -1.07318241765   ? 
2  'X-RAY DIFFRACTION' ? refined 49.047919644  -29.3757396846 33.9201185574 0.697853222141 ? -0.0287738030391   ? -0.0341659238164 
? 0.929648396919 ? 0.0755637772674  ? 0.392351180231   ? 2.63713946905 ? -1.254279193     ? -1.25077432676  ? 6.12642824159  ? 
5.12761442159   ? 4.30772293315 ? 0.136113671501   ? 0.0555731897403 ? 0.269162815737  ? 0.195349927709   ? -0.219735288466  ? 
-0.0903750668056 ? -0.260040102958 ? 0.666726729063   ? -0.165571762313  ? 
3  'X-RAY DIFFRACTION' ? refined 40.066250413  -50.4007801361 22.8582714101 0.890581294242 ? -0.177582914499    ? 0.0788722577244  
? 1.68970183157  ? -0.304325379627  ? 0.644445910477   ? 4.12987111296 ? 4.76231469928    ? 4.45216886396   ? 1.99476117164  ? 
2.91938782675   ? 5.81091673014 ? -1.20665266634   ? 1.31679905264   ? -1.82178638045  ? -0.0543389295969 ? 1.05724660973    ? 
-1.53787462798   ? 1.00352129042   ? 1.11530616271    ? -0.733202983507  ? 
4  'X-RAY DIFFRACTION' ? refined 34.6717373572 -42.833050501  31.1204458567 1.82998724878  ? -0.626699301826    ? -0.118606510998  
? 1.77776545252  ? 0.00665586167392 ? 0.548276058538   ? 3.69246224693 ? -2.16174787733   ? -0.663051788609 ? 1.56253882721  ? 
-0.17442717027  ? 1.1562402769  ? -0.145047709266  ? -0.939565135356 ? 0.0584211381964 ? 1.85744260325    ? 0.0645941728933  ? 
0.122754536201   ? 0.169529818727  ? 0.391573033819   ? -0.17244304471   ? 
5  'X-RAY DIFFRACTION' ? refined 33.3597076722 -45.6207982563 14.1870834774 1.14729391124  ? -0.770178461386    ? 0.0226811428205  
? 1.79430094664  ? -0.093540156284  ? -0.0113101467829 ? 2.14458869395 ? -2.6625082006    ? 0.986029626638  ? 4.78926235385  ? 
1.71131713078   ? 7.15904549745 ? -0.0517570137624 ? 0.656907443766  ? -0.415624740405 ? -0.676482533232  ? 0.0145363813964  ? 
-0.131443716572  ? 0.750093189974  ? 0.529914052797   ? 0.371714110944   ? 
6  'X-RAY DIFFRACTION' ? refined 44.9505497976 -32.1368281158 31.9198982654 0.659944063553 ? -0.000904403698226 ? 0.018943024501   
? 0.870376466656 ? 0.13287674823    ? 0.257377688016   ? 3.77733326157 ? 2.95480976982    ? 1.78874551242   ? 5.44188250722  ? 
4.8496517671    ? 5.22623062326 ? -0.178420997943  ? 0.626228420948  ? 0.231469271812  ? -0.912654850954  ? 0.56622972206    ? 
0.184222934742   ? -1.0207900821   ? 0.00291435489303 ? -0.397566724427  ? 
7  'X-RAY DIFFRACTION' ? refined 43.2447991512 -36.5636378037 26.8246628885 0.577738523147 ? -0.098602689652    ? 0.0496666259161  
? 0.955868010145 ? 0.0762936421906  ? 0.327321077495   ? 2.74524357496 ? 2.28041342717    ? 0.59109026815   ? 1.95955407791  ? 
0.859965467791  ? 2.84899991905 ? -0.0909007915793 ? 1.28704794557   ? 0.268566267646  ? -0.36863629997   ? 0.858652805568   ? 
-0.219619988609  ? 0.15266611991   ? -0.808250638232  ? -0.0514919219861 ? 
8  'X-RAY DIFFRACTION' ? refined 42.2432536913 -39.4646123167 18.3990222782 0.980917438008 ? -0.348340104649    ? -0.155973326239  
? 1.74048278253  ? -0.10806583717   ? 0.0875800403512  ? 3.72861550102 ? 0.299741061468   ? 0.929453837255  ? 3.1872703749   ? 
1.73058148146   ? 2.47694240843 ? -1.22053328198   ? 1.43531261832   ? 0.803005620296  ? -0.689325616897  ? 0.970765508842   ? 
-0.460771486537  ? 0.51150337285   ? 1.05324275313    ? 1.50864229957    ? 
9  'X-RAY DIFFRACTION' ? refined 30.877595641  -28.4006088567 34.3573891412 1.37352585079  ? 0.48709699842      ? -0.0225723693854 
? 1.5055793244   ? -0.296763810758  ? 1.17647978728    ? 7.80757101959 ? 4.64225291379    ? -1.35361324117  ? 8.68815913638  ? 
0.26396595609   ? 2.36658219595 ? 0.182294236004   ? -1.51279621999  ? 3.58458645075   ? 1.31169393829    ? 0.791077828787   ? 
2.00533530301    ? -1.81901255911  ? -0.86988443217   ? -0.0605677051922 ? 
10 'X-RAY DIFFRACTION' ? refined 41.0158453214 -33.8980175665 12.998745157  1.58968076656  ? -0.877908399431    ? -0.285347017613  
? 2.43031873434  ? 0.233639020228   ? 0.801223068311   ? 1.66618429155 ? -1.86398855472   ? -2.08347444866  ? 2.73434824822  ? 
3.23126284516   ? 3.86402539233 ? -1.14091022223   ? 0.582754821963  ? 1.12193013657   ? -1.51250195002   ? 1.02522126608    ? 
-1.14745689452   ? -3.13905637846  ? 4.46560715239    ? -0.0353702445635 ? 
11 'X-RAY DIFFRACTION' ? refined 27.7946233218 -34.6475070281 21.7247047908 0.968476736443 ? -0.0584303899984   ? -0.357822338697  
? 1.49264276926  ? 0.2047410638     ? 1.27576440448    ? 5.61569357387 ? 5.25866123258    ? 5.45757590218   ? 8.55866866249  ? 
5.90690198281   ? 8.73968081869 ? 0.217897287085   ? 0.60956132037   ? 2.46918564974   ? -0.642187061879  ? -0.283038694361  ? 
1.0983111312     ? -0.712045130972 ? -0.281707341554  ? 0.205269132511   ? 
12 'X-RAY DIFFRACTION' ? refined 37.5152321496 -43.3669206525 7.35756007427 1.33490861812  ? -0.453564662714    ? 0.035995069243   
? 1.79943241231  ? 0.0264533170694  ? 0.508089818372   ? 3.64280603045 ? -0.0715811567872 ? -3.84738188269  ? 0.168827083133 ? 
-0.442382578876 ? 5.48019077958 ? -0.229542656962  ? 1.05697965029   ? -0.533312857306 ? -1.60968857053   ? -0.0478530746585 ? 
0.270507942576   ? 0.957043160999  ? -0.178620907435  ? -0.0909815512155 ? 
# 
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 6   ? A 9   A 14  ? ? 
;chain 'A' and (resid 6 through 14 )
;
2  'X-RAY DIFFRACTION' 2  A 10  A 15  ? A 22  A 27  ? ? 
;chain 'A' and (resid 15 through 27 )
;
3  'X-RAY DIFFRACTION' 3  A 23  A 28  ? A 32  A 37  ? ? 
;chain 'A' and (resid 28 through 37 )
;
4  'X-RAY DIFFRACTION' 4  A 33  A 38  ? A 42  A 47  ? ? 
;chain 'A' and (resid 38 through 47 )
;
5  'X-RAY DIFFRACTION' 5  A 43  A 48  ? A 60  A 65  ? ? 
;chain 'A' and (resid 48 through 65 )
;
6  'X-RAY DIFFRACTION' 6  A 61  A 66  ? A 74  A 79  ? ? 
;chain 'A' and (resid 66 through 79 )
;
7  'X-RAY DIFFRACTION' 7  A 75  A 80  ? A 86  A 91  ? ? 
;chain 'A' and (resid 80 through 91 )
;
8  'X-RAY DIFFRACTION' 8  A 87  A 92  ? A 106 A 111 ? ? 
;chain 'A' and (resid 92 through 111 )
;
9  'X-RAY DIFFRACTION' 9  A 107 A 112 ? A 119 A 124 ? ? 
;chain 'A' and (resid 112 through 124 )
;
10 'X-RAY DIFFRACTION' 10 A 120 A 125 ? A 128 A 133 ? ? 
;chain 'A' and (resid 125 through 133 )
;
11 'X-RAY DIFFRACTION' 11 A 129 A 134 ? A 138 A 143 ? ? 
;chain 'A' and (resid 134 through 143 )
;
12 'X-RAY DIFFRACTION' 12 A 139 A 144 ? A 149 A 154 ? ? 
;chain 'A' and (resid 144 through 154 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 421 ? 6.00 . 
2 1 O ? A HOH 422 ? 6.60 . 
3 1 O ? A HOH 423 ? 8.74 . 
# 
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 SER 1   ? A SER 1   
2 1 Y 1 A ALA 2   ? A ALA 2   
3 1 Y 1 A GLY 3   ? A GLY 3   
4 1 Y 1 A MET 4   ? A MET 4   
5 1 Y 1 A SER 5   ? A SER 5   
6 1 Y 1 A PRO 155 ? A PRO 155 
# 
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  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HOH O    O N N 123 
HOH H1   H N N 124 
HOH H2   H N N 125 
ILE N    N N N 126 
ILE CA   C N S 127 
ILE C    C N N 128 
ILE O    O N N 129 
ILE CB   C N S 130 
ILE CG1  C N N 131 
ILE CG2  C N N 132 
ILE CD1  C N N 133 
ILE OXT  O N N 134 
ILE H    H N N 135 
ILE H2   H N N 136 
ILE HA   H N N 137 
ILE HB   H N N 138 
ILE HG12 H N N 139 
ILE HG13 H N N 140 
ILE HG21 H N N 141 
ILE HG22 H N N 142 
ILE HG23 H N N 143 
ILE HD11 H N N 144 
ILE HD12 H N N 145 
ILE HD13 H N N 146 
ILE HXT  H N N 147 
LEU N    N N N 148 
LEU CA   C N S 149 
LEU C    C N N 150 
LEU O    O N N 151 
LEU CB   C N N 152 
LEU CG   C N N 153 
LEU CD1  C N N 154 
LEU CD2  C N N 155 
LEU OXT  O N N 156 
LEU H    H N N 157 
LEU H2   H N N 158 
LEU HA   H N N 159 
LEU HB2  H N N 160 
LEU HB3  H N N 161 
LEU HG   H N N 162 
LEU HD11 H N N 163 
LEU HD12 H N N 164 
LEU HD13 H N N 165 
LEU HD21 H N N 166 
LEU HD22 H N N 167 
LEU HD23 H N N 168 
LEU HXT  H N N 169 
LYS N    N N N 170 
LYS CA   C N S 171 
LYS C    C N N 172 
LYS O    O N N 173 
LYS CB   C N N 174 
LYS CG   C N N 175 
LYS CD   C N N 176 
LYS CE   C N N 177 
LYS NZ   N N N 178 
LYS OXT  O N N 179 
LYS H    H N N 180 
LYS H2   H N N 181 
LYS HA   H N N 182 
LYS HB2  H N N 183 
LYS HB3  H N N 184 
LYS HG2  H N N 185 
LYS HG3  H N N 186 
LYS HD2  H N N 187 
LYS HD3  H N N 188 
LYS HE2  H N N 189 
LYS HE3  H N N 190 
LYS HZ1  H N N 191 
LYS HZ2  H N N 192 
LYS HZ3  H N N 193 
LYS HXT  H N N 194 
MET N    N N N 195 
MET CA   C N S 196 
MET C    C N N 197 
MET O    O N N 198 
MET CB   C N N 199 
MET CG   C N N 200 
MET SD   S N N 201 
MET CE   C N N 202 
MET OXT  O N N 203 
MET H    H N N 204 
MET H2   H N N 205 
MET HA   H N N 206 
MET HB2  H N N 207 
MET HB3  H N N 208 
MET HG2  H N N 209 
MET HG3  H N N 210 
MET HE1  H N N 211 
MET HE2  H N N 212 
MET HE3  H N N 213 
MET HXT  H N N 214 
PHE N    N N N 215 
PHE CA   C N S 216 
PHE C    C N N 217 
PHE O    O N N 218 
PHE CB   C N N 219 
PHE CG   C Y N 220 
PHE CD1  C Y N 221 
PHE CD2  C Y N 222 
PHE CE1  C Y N 223 
PHE CE2  C Y N 224 
PHE CZ   C Y N 225 
PHE OXT  O N N 226 
PHE H    H N N 227 
PHE H2   H N N 228 
PHE HA   H N N 229 
PHE HB2  H N N 230 
PHE HB3  H N N 231 
PHE HD1  H N N 232 
PHE HD2  H N N 233 
PHE HE1  H N N 234 
PHE HE2  H N N 235 
PHE HZ   H N N 236 
PHE HXT  H N N 237 
PRO N    N N N 238 
PRO CA   C N S 239 
PRO C    C N N 240 
PRO O    O N N 241 
PRO CB   C N N 242 
PRO CG   C N N 243 
PRO CD   C N N 244 
PRO OXT  O N N 245 
PRO H    H N N 246 
PRO HA   H N N 247 
PRO HB2  H N N 248 
PRO HB3  H N N 249 
PRO HG2  H N N 250 
PRO HG3  H N N 251 
PRO HD2  H N N 252 
PRO HD3  H N N 253 
PRO HXT  H N N 254 
SER N    N N N 255 
SER CA   C N S 256 
SER C    C N N 257 
SER O    O N N 258 
SER CB   C N N 259 
SER OG   O N N 260 
SER OXT  O N N 261 
SER H    H N N 262 
SER H2   H N N 263 
SER HA   H N N 264 
SER HB2  H N N 265 
SER HB3  H N N 266 
SER HG   H N N 267 
SER HXT  H N N 268 
SO4 S    S N N 269 
SO4 O1   O N N 270 
SO4 O2   O N N 271 
SO4 O3   O N N 272 
SO4 O4   O N N 273 
THR N    N N N 274 
THR CA   C N S 275 
THR C    C N N 276 
THR O    O N N 277 
THR CB   C N R 278 
THR OG1  O N N 279 
THR CG2  C N N 280 
THR OXT  O N N 281 
THR H    H N N 282 
THR H2   H N N 283 
THR HA   H N N 284 
THR HB   H N N 285 
THR HG1  H N N 286 
THR HG21 H N N 287 
THR HG22 H N N 288 
THR HG23 H N N 289 
THR HXT  H N N 290 
TRP N    N N N 291 
TRP CA   C N S 292 
TRP C    C N N 293 
TRP O    O N N 294 
TRP CB   C N N 295 
TRP CG   C Y N 296 
TRP CD1  C Y N 297 
TRP CD2  C Y N 298 
TRP NE1  N Y N 299 
TRP CE2  C Y N 300 
TRP CE3  C Y N 301 
TRP CZ2  C Y N 302 
TRP CZ3  C Y N 303 
TRP CH2  C Y N 304 
TRP OXT  O N N 305 
TRP H    H N N 306 
TRP H2   H N N 307 
TRP HA   H N N 308 
TRP HB2  H N N 309 
TRP HB3  H N N 310 
TRP HD1  H N N 311 
TRP HE1  H N N 312 
TRP HE3  H N N 313 
TRP HZ2  H N N 314 
TRP HZ3  H N N 315 
TRP HH2  H N N 316 
TRP HXT  H N N 317 
TYR N    N N N 318 
TYR CA   C N S 319 
TYR C    C N N 320 
TYR O    O N N 321 
TYR CB   C N N 322 
TYR CG   C Y N 323 
TYR CD1  C Y N 324 
TYR CD2  C Y N 325 
TYR CE1  C Y N 326 
TYR CE2  C Y N 327 
TYR CZ   C Y N 328 
TYR OH   O N N 329 
TYR OXT  O N N 330 
TYR H    H N N 331 
TYR H2   H N N 332 
TYR HA   H N N 333 
TYR HB2  H N N 334 
TYR HB3  H N N 335 
TYR HD1  H N N 336 
TYR HD2  H N N 337 
TYR HE1  H N N 338 
TYR HE2  H N N 339 
TYR HH   H N N 340 
TYR HXT  H N N 341 
VAL N    N N N 342 
VAL CA   C N S 343 
VAL C    C N N 344 
VAL O    O N N 345 
VAL CB   C N N 346 
VAL CG1  C N N 347 
VAL CG2  C N N 348 
VAL OXT  O N N 349 
VAL H    H N N 350 
VAL H2   H N N 351 
VAL HA   H N N 352 
VAL HB   H N N 353 
VAL HG11 H N N 354 
VAL HG12 H N N 355 
VAL HG13 H N N 356 
VAL HG21 H N N 357 
VAL HG22 H N N 358 
VAL HG23 H N N 359 
VAL HXT  H N N 360 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HOH O   H1   sing N N 116 
HOH O   H2   sing N N 117 
ILE N   CA   sing N N 118 
ILE N   H    sing N N 119 
ILE N   H2   sing N N 120 
ILE CA  C    sing N N 121 
ILE CA  CB   sing N N 122 
ILE CA  HA   sing N N 123 
ILE C   O    doub N N 124 
ILE C   OXT  sing N N 125 
ILE CB  CG1  sing N N 126 
ILE CB  CG2  sing N N 127 
ILE CB  HB   sing N N 128 
ILE CG1 CD1  sing N N 129 
ILE CG1 HG12 sing N N 130 
ILE CG1 HG13 sing N N 131 
ILE CG2 HG21 sing N N 132 
ILE CG2 HG22 sing N N 133 
ILE CG2 HG23 sing N N 134 
ILE CD1 HD11 sing N N 135 
ILE CD1 HD12 sing N N 136 
ILE CD1 HD13 sing N N 137 
ILE OXT HXT  sing N N 138 
LEU N   CA   sing N N 139 
LEU N   H    sing N N 140 
LEU N   H2   sing N N 141 
LEU CA  C    sing N N 142 
LEU CA  CB   sing N N 143 
LEU CA  HA   sing N N 144 
LEU C   O    doub N N 145 
LEU C   OXT  sing N N 146 
LEU CB  CG   sing N N 147 
LEU CB  HB2  sing N N 148 
LEU CB  HB3  sing N N 149 
LEU CG  CD1  sing N N 150 
LEU CG  CD2  sing N N 151 
LEU CG  HG   sing N N 152 
LEU CD1 HD11 sing N N 153 
LEU CD1 HD12 sing N N 154 
LEU CD1 HD13 sing N N 155 
LEU CD2 HD21 sing N N 156 
LEU CD2 HD22 sing N N 157 
LEU CD2 HD23 sing N N 158 
LEU OXT HXT  sing N N 159 
LYS N   CA   sing N N 160 
LYS N   H    sing N N 161 
LYS N   H2   sing N N 162 
LYS CA  C    sing N N 163 
LYS CA  CB   sing N N 164 
LYS CA  HA   sing N N 165 
LYS C   O    doub N N 166 
LYS C   OXT  sing N N 167 
LYS CB  CG   sing N N 168 
LYS CB  HB2  sing N N 169 
LYS CB  HB3  sing N N 170 
LYS CG  CD   sing N N 171 
LYS CG  HG2  sing N N 172 
LYS CG  HG3  sing N N 173 
LYS CD  CE   sing N N 174 
LYS CD  HD2  sing N N 175 
LYS CD  HD3  sing N N 176 
LYS CE  NZ   sing N N 177 
LYS CE  HE2  sing N N 178 
LYS CE  HE3  sing N N 179 
LYS NZ  HZ1  sing N N 180 
LYS NZ  HZ2  sing N N 181 
LYS NZ  HZ3  sing N N 182 
LYS OXT HXT  sing N N 183 
MET N   CA   sing N N 184 
MET N   H    sing N N 185 
MET N   H2   sing N N 186 
MET CA  C    sing N N 187 
MET CA  CB   sing N N 188 
MET CA  HA   sing N N 189 
MET C   O    doub N N 190 
MET C   OXT  sing N N 191 
MET CB  CG   sing N N 192 
MET CB  HB2  sing N N 193 
MET CB  HB3  sing N N 194 
MET CG  SD   sing N N 195 
MET CG  HG2  sing N N 196 
MET CG  HG3  sing N N 197 
MET SD  CE   sing N N 198 
MET CE  HE1  sing N N 199 
MET CE  HE2  sing N N 200 
MET CE  HE3  sing N N 201 
MET OXT HXT  sing N N 202 
PHE N   CA   sing N N 203 
PHE N   H    sing N N 204 
PHE N   H2   sing N N 205 
PHE CA  C    sing N N 206 
PHE CA  CB   sing N N 207 
PHE CA  HA   sing N N 208 
PHE C   O    doub N N 209 
PHE C   OXT  sing N N 210 
PHE CB  CG   sing N N 211 
PHE CB  HB2  sing N N 212 
PHE CB  HB3  sing N N 213 
PHE CG  CD1  doub Y N 214 
PHE CG  CD2  sing Y N 215 
PHE CD1 CE1  sing Y N 216 
PHE CD1 HD1  sing N N 217 
PHE CD2 CE2  doub Y N 218 
PHE CD2 HD2  sing N N 219 
PHE CE1 CZ   doub Y N 220 
PHE CE1 HE1  sing N N 221 
PHE CE2 CZ   sing Y N 222 
PHE CE2 HE2  sing N N 223 
PHE CZ  HZ   sing N N 224 
PHE OXT HXT  sing N N 225 
PRO N   CA   sing N N 226 
PRO N   CD   sing N N 227 
PRO N   H    sing N N 228 
PRO CA  C    sing N N 229 
PRO CA  CB   sing N N 230 
PRO CA  HA   sing N N 231 
PRO C   O    doub N N 232 
PRO C   OXT  sing N N 233 
PRO CB  CG   sing N N 234 
PRO CB  HB2  sing N N 235 
PRO CB  HB3  sing N N 236 
PRO CG  CD   sing N N 237 
PRO CG  HG2  sing N N 238 
PRO CG  HG3  sing N N 239 
PRO CD  HD2  sing N N 240 
PRO CD  HD3  sing N N 241 
PRO OXT HXT  sing N N 242 
SER N   CA   sing N N 243 
SER N   H    sing N N 244 
SER N   H2   sing N N 245 
SER CA  C    sing N N 246 
SER CA  CB   sing N N 247 
SER CA  HA   sing N N 248 
SER C   O    doub N N 249 
SER C   OXT  sing N N 250 
SER CB  OG   sing N N 251 
SER CB  HB2  sing N N 252 
SER CB  HB3  sing N N 253 
SER OG  HG   sing N N 254 
SER OXT HXT  sing N N 255 
SO4 S   O1   doub N N 256 
SO4 S   O2   doub N N 257 
SO4 S   O3   sing N N 258 
SO4 S   O4   sing N N 259 
THR N   CA   sing N N 260 
THR N   H    sing N N 261 
THR N   H2   sing N N 262 
THR CA  C    sing N N 263 
THR CA  CB   sing N N 264 
THR CA  HA   sing N N 265 
THR C   O    doub N N 266 
THR C   OXT  sing N N 267 
THR CB  OG1  sing N N 268 
THR CB  CG2  sing N N 269 
THR CB  HB   sing N N 270 
THR OG1 HG1  sing N N 271 
THR CG2 HG21 sing N N 272 
THR CG2 HG22 sing N N 273 
THR CG2 HG23 sing N N 274 
THR OXT HXT  sing N N 275 
TRP N   CA   sing N N 276 
TRP N   H    sing N N 277 
TRP N   H2   sing N N 278 
TRP CA  C    sing N N 279 
TRP CA  CB   sing N N 280 
TRP CA  HA   sing N N 281 
TRP C   O    doub N N 282 
TRP C   OXT  sing N N 283 
TRP CB  CG   sing N N 284 
TRP CB  HB2  sing N N 285 
TRP CB  HB3  sing N N 286 
TRP CG  CD1  doub Y N 287 
TRP CG  CD2  sing Y N 288 
TRP CD1 NE1  sing Y N 289 
TRP CD1 HD1  sing N N 290 
TRP CD2 CE2  doub Y N 291 
TRP CD2 CE3  sing Y N 292 
TRP NE1 CE2  sing Y N 293 
TRP NE1 HE1  sing N N 294 
TRP CE2 CZ2  sing Y N 295 
TRP CE3 CZ3  doub Y N 296 
TRP CE3 HE3  sing N N 297 
TRP CZ2 CH2  doub Y N 298 
TRP CZ2 HZ2  sing N N 299 
TRP CZ3 CH2  sing Y N 300 
TRP CZ3 HZ3  sing N N 301 
TRP CH2 HH2  sing N N 302 
TRP OXT HXT  sing N N 303 
TYR N   CA   sing N N 304 
TYR N   H    sing N N 305 
TYR N   H2   sing N N 306 
TYR CA  C    sing N N 307 
TYR CA  CB   sing N N 308 
TYR CA  HA   sing N N 309 
TYR C   O    doub N N 310 
TYR C   OXT  sing N N 311 
TYR CB  CG   sing N N 312 
TYR CB  HB2  sing N N 313 
TYR CB  HB3  sing N N 314 
TYR CG  CD1  doub Y N 315 
TYR CG  CD2  sing Y N 316 
TYR CD1 CE1  sing Y N 317 
TYR CD1 HD1  sing N N 318 
TYR CD2 CE2  doub Y N 319 
TYR CD2 HD2  sing N N 320 
TYR CE1 CZ   doub Y N 321 
TYR CE1 HE1  sing N N 322 
TYR CE2 CZ   sing Y N 323 
TYR CE2 HE2  sing N N 324 
TYR CZ  OH   sing N N 325 
TYR OH  HH   sing N N 326 
TYR OXT HXT  sing N N 327 
VAL N   CA   sing N N 328 
VAL N   H    sing N N 329 
VAL N   H2   sing N N 330 
VAL CA  C    sing N N 331 
VAL CA  CB   sing N N 332 
VAL CA  HA   sing N N 333 
VAL C   O    doub N N 334 
VAL C   OXT  sing N N 335 
VAL CB  CG1  sing N N 336 
VAL CB  CG2  sing N N 337 
VAL CB  HB   sing N N 338 
VAL CG1 HG11 sing N N 339 
VAL CG1 HG12 sing N N 340 
VAL CG1 HG13 sing N N 341 
VAL CG2 HG21 sing N N 342 
VAL CG2 HG22 sing N N 343 
VAL CG2 HG23 sing N N 344 
VAL OXT HXT  sing N N 345 
# 
_pdbx_audit_support.funding_organization   'Department of Energy (DOE, United States)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 6 2 2' 
_space_group.name_Hall        'P 6 2' 
_space_group.IT_number        177 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MXX 
_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]   0.008883 
_atom_sites.fract_transf_matrix[1][2]   0.005129 
_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]   0.010258 
_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]   0.011806 
_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   . PRO A 1 6   ? 52.80228 -36.40946 20.58632 1.000 140.79254 ? 6   PRO A N   1 
ATOM   2    C CA  . PRO A 1 6   ? 51.67699 -37.02355 21.29218 1.000 148.89445 ? 6   PRO A CA  1 
ATOM   3    C C   . PRO A 1 6   ? 51.37295 -36.39724 22.65589 1.000 145.90335 ? 6   PRO A C   1 
ATOM   4    O O   . PRO A 1 6   ? 50.34072 -35.74143 22.80607 1.000 125.73226 ? 6   PRO A O   1 
ATOM   5    C CB  . PRO A 1 6   ? 52.12707 -38.48154 21.45355 1.000 140.60497 ? 6   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 6   ? 53.33149 -38.65870 20.50508 1.000 156.88063 ? 6   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 6   ? 53.47495 -37.38717 19.71963 1.000 165.57476 ? 6   PRO A CD  1 
ATOM   8    N N   . VAL A 1 7   ? 52.25784 -36.60139 23.63530 1.000 152.04185 ? 7   VAL A N   1 
ATOM   9    C CA  . VAL A 1 7   ? 51.95754 -36.18767 25.00493 1.000 145.51861 ? 7   VAL A CA  1 
ATOM   10   C C   . VAL A 1 7   ? 51.88300 -34.67084 25.10081 1.000 140.50440 ? 7   VAL A C   1 
ATOM   11   O O   . VAL A 1 7   ? 51.05482 -34.11833 25.83429 1.000 128.34422 ? 7   VAL A O   1 
ATOM   12   C CB  . VAL A 1 7   ? 53.00006 -36.76228 25.98262 1.000 115.46437 ? 7   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 7   ? 52.56034 -36.53160 27.42438 1.000 113.99549 ? 7   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 7   ? 53.22657 -38.24034 25.71459 1.000 127.52646 ? 7   VAL A CG2 1 
ATOM   15   N N   . GLU A 1 8   ? 52.74080 -33.97470 24.36110 1.000 129.81572 ? 8   GLU A N   1 
ATOM   16   C CA  . GLU A 1 8   ? 52.76733 -32.52066 24.39196 1.000 134.29708 ? 8   GLU A CA  1 
ATOM   17   C C   . GLU A 1 8   ? 51.73083 -31.91407 23.45487 1.000 134.64507 ? 8   GLU A C   1 
ATOM   18   O O   . GLU A 1 8   ? 51.12737 -30.88653 23.78473 1.000 135.83385 ? 8   GLU A O   1 
ATOM   19   C CB  . GLU A 1 8   ? 54.16900 -32.01705 24.04312 1.000 151.20647 ? 8   GLU A CB  1 
ATOM   20   C CG  . GLU A 1 8   ? 54.26960 -30.51878 23.96954 1.000 149.11562 ? 8   GLU A CG  1 
ATOM   21   C CD  . GLU A 1 8   ? 54.10015 -29.99999 22.56084 1.000 169.73156 ? 8   GLU A CD  1 
ATOM   22   O OE1 . GLU A 1 8   ? 55.00468 -30.21949 21.72783 1.000 165.02417 ? 8   GLU A OE1 1 
ATOM   23   O OE2 . GLU A 1 8   ? 53.05074 -29.38402 22.28662 1.000 169.93578 ? 8   GLU A OE2 1 
ATOM   24   N N   . ALA A 1 9   ? 51.51967 -32.51921 22.28225 1.000 137.83571 ? 9   ALA A N   1 
ATOM   25   C CA  . ALA A 1 9   ? 50.40038 -32.10399 21.44439 1.000 144.94402 ? 9   ALA A CA  1 
ATOM   26   C C   . ALA A 1 9   ? 49.08759 -32.24263 22.20242 1.000 132.99840 ? 9   ALA A C   1 
ATOM   27   O O   . ALA A 1 9   ? 48.19269 -31.39864 22.07567 1.000 144.21051 ? 9   ALA A O   1 
ATOM   28   C CB  . ALA A 1 9   ? 50.37216 -32.92160 20.15374 1.000 144.03232 ? 9   ALA A CB  1 
ATOM   29   N N   . ALA A 1 10  ? 48.96226 -33.30088 23.00716 1.000 125.69770 ? 10  ALA A N   1 
ATOM   30   C CA  . ALA A 1 10  ? 47.82850 -33.41133 23.91663 1.000 120.67795 ? 10  ALA A CA  1 
ATOM   31   C C   . ALA A 1 10  ? 47.85741 -32.30434 24.96200 1.000 117.06651 ? 10  ALA A C   1 
ATOM   32   O O   . ALA A 1 10  ? 46.81103 -31.75520 25.32503 1.000 116.69657 ? 10  ALA A O   1 
ATOM   33   C CB  . ALA A 1 10  ? 47.82803 -34.78380 24.58866 1.000 114.22062 ? 10  ALA A CB  1 
ATOM   34   N N   . LYS A 1 11  ? 49.05005 -31.96004 25.45528 1.000 114.80418 ? 11  LYS A N   1 
ATOM   35   C CA  . LYS A 1 11  ? 49.16169 -30.90251 26.45476 1.000 111.94090 ? 11  LYS A CA  1 
ATOM   36   C C   . LYS A 1 11  ? 48.81655 -29.54265 25.85948 1.000 118.43709 ? 11  LYS A C   1 
ATOM   37   O O   . LYS A 1 11  ? 48.18870 -28.70962 26.52348 1.000 116.93703 ? 11  LYS A O   1 
ATOM   38   C CB  . LYS A 1 11  ? 50.57176 -30.89111 27.04481 1.000 109.21428 ? 11  LYS A CB  1 
ATOM   39   C CG  . LYS A 1 11  ? 50.72259 -30.05548 28.30424 1.000 105.23296 ? 11  LYS A CG  1 
ATOM   40   C CD  . LYS A 1 11  ? 52.17742 -29.99720 28.74580 1.000 117.57255 ? 11  LYS A CD  1 
ATOM   41   C CE  . LYS A 1 11  ? 52.79002 -31.38804 28.82053 1.000 102.82372 ? 11  LYS A CE  1 
ATOM   42   N NZ  . LYS A 1 11  ? 54.23378 -31.34933 29.18921 1.000 100.74219 ? 11  LYS A NZ  1 
ATOM   43   N N   . ALA A 1 12  ? 49.21148 -29.30456 24.60523 1.000 126.12939 ? 12  ALA A N   1 
ATOM   44   C CA  . ALA A 1 12  ? 48.92061 -28.02703 23.96159 1.000 133.45871 ? 12  ALA A CA  1 
ATOM   45   C C   . ALA A 1 12  ? 47.42306 -27.83727 23.75236 1.000 135.32340 ? 12  ALA A C   1 
ATOM   46   O O   . ALA A 1 12  ? 46.90316 -26.72751 23.91847 1.000 137.53080 ? 12  ALA A O   1 
ATOM   47   C CB  . ALA A 1 12  ? 49.66600 -27.92981 22.63135 1.000 142.05814 ? 12  ALA A CB  1 
ATOM   48   N N   . GLU A 1 13  ? 46.71329 -28.90506 23.38085 1.000 134.94690 ? 13  GLU A N   1 
ATOM   49   C CA  . GLU A 1 13  ? 45.26506 -28.80794 23.23883 1.000 136.86572 ? 13  GLU A CA  1 
ATOM   50   C C   . GLU A 1 13  ? 44.57862 -28.67748 24.59198 1.000 129.24920 ? 13  GLU A C   1 
ATOM   51   O O   . GLU A 1 13  ? 43.49710 -28.08580 24.68310 1.000 130.93663 ? 13  GLU A O   1 
ATOM   52   C CB  . GLU A 1 13  ? 44.72707 -30.02498 22.48573 1.000 139.17976 ? 13  GLU A CB  1 
ATOM   53   C CG  . GLU A 1 13  ? 45.37823 -30.25081 21.13270 1.000 148.13862 ? 13  GLU A CG  1 
ATOM   54   C CD  . GLU A 1 13  ? 45.23508 -29.05621 20.21313 1.000 156.61673 ? 13  GLU A CD  1 
ATOM   55   O OE1 . GLU A 1 13  ? 44.10831 -28.53161 20.08962 1.000 159.95299 ? 13  GLU A OE1 1 
ATOM   56   O OE2 . GLU A 1 13  ? 46.25152 -28.63607 19.62133 1.000 161.23222 ? 13  GLU A OE2 1 
ATOM   57   N N   . ALA A 1 14  ? 45.19168 -29.21102 25.65025 1.000 122.81740 ? 14  ALA A N   1 
ATOM   58   C CA  . ALA A 1 14  ? 44.57149 -29.17840 26.96883 1.000 114.44184 ? 14  ALA A CA  1 
ATOM   59   C C   . ALA A 1 14  ? 44.80215 -27.85494 27.68725 1.000 113.43185 ? 14  ALA A C   1 
ATOM   60   O O   . ALA A 1 14  ? 43.99289 -27.47474 28.54089 1.000 123.14153 ? 14  ALA A O   1 
ATOM   61   C CB  . ALA A 1 14  ? 45.09150 -30.33622 27.82201 1.000 107.20843 ? 14  ALA A CB  1 
ATOM   62   N N   . ILE A 1 15  ? 45.88928 -27.14690 27.36843 1.000 102.10685 ? 15  ILE A N   1 
ATOM   63   C CA  . ILE A 1 15  ? 46.16250 -25.87221 28.02258 1.000 95.30002  ? 15  ILE A CA  1 
ATOM   64   C C   . ILE A 1 15  ? 45.07861 -24.87042 27.65631 1.000 100.94818 ? 15  ILE A C   1 
ATOM   65   O O   . ILE A 1 15  ? 44.80449 -24.62665 26.47395 1.000 115.53802 ? 15  ILE A O   1 
ATOM   66   C CB  . ILE A 1 15  ? 47.55696 -25.35485 27.63880 1.000 98.05012  ? 15  ILE A CB  1 
ATOM   67   C CG1 . ILE A 1 15  ? 48.64663 -26.19596 28.30700 1.000 104.72353 ? 15  ILE A CG1 1 
ATOM   68   C CG2 . ILE A 1 15  ? 47.70830 -23.89858 28.03337 1.000 94.18275  ? 15  ILE A CG2 1 
ATOM   69   C CD1 . ILE A 1 15  ? 50.05002 -25.81392 27.89006 1.000 120.95686 ? 15  ILE A CD1 1 
ATOM   70   N N   . ALA A 1 16  ? 44.45237 -24.28682 28.67569 1.000 106.95397 ? 16  ALA A N   1 
ATOM   71   C CA  . ALA A 1 16  ? 43.38525 -23.32243 28.47785 1.000 113.49476 ? 16  ALA A CA  1 
ATOM   72   C C   . ALA A 1 16  ? 43.96400 -21.91922 28.31557 1.000 116.33515 ? 16  ALA A C   1 
ATOM   73   O O   . ALA A 1 16  ? 45.17990 -21.71829 28.25776 1.000 112.34530 ? 16  ALA A O   1 
ATOM   74   C CB  . ALA A 1 16  ? 42.39404 -23.37759 29.63891 1.000 114.28147 ? 16  ALA A CB  1 
ATOM   75   N N   . ALA A 1 17  ? 43.07539 -20.93244 28.24077 1.000 131.67494 ? 17  ALA A N   1 
ATOM   76   C CA  . ALA A 1 17  ? 43.47249 -19.54113 28.08321 1.000 129.42554 ? 17  ALA A CA  1 
ATOM   77   C C   . ALA A 1 17  ? 43.68737 -18.90482 29.45063 1.000 135.42792 ? 17  ALA A C   1 
ATOM   78   O O   . ALA A 1 17  ? 42.82385 -19.00066 30.32870 1.000 142.50246 ? 17  ALA A O   1 
ATOM   79   C CB  . ALA A 1 17  ? 42.41715 -18.76420 27.29533 1.000 124.85093 ? 17  ALA A CB  1 
ATOM   80   N N   . GLY A 1 18  ? 44.83302 -18.26243 29.62412 1.000 106.06206 ? 18  GLY A N   1 
ATOM   81   C CA  . GLY A 1 18  ? 45.18106 -17.60389 30.86773 1.000 92.73703  ? 18  GLY A CA  1 
ATOM   82   C C   . GLY A 1 18  ? 46.43193 -18.19154 31.49511 1.000 77.76001  ? 18  GLY A C   1 
ATOM   83   O O   . GLY A 1 18  ? 46.99625 -19.18354 31.03695 1.000 74.99164  ? 18  GLY A O   1 
ATOM   84   N N   . LYS A 1 19  ? 46.85905 -17.53180 32.57237 1.000 88.51707  ? 19  LYS A N   1 
ATOM   85   C CA  . LYS A 1 19  ? 47.99145 -18.00945 33.35441 1.000 82.14539  ? 19  LYS A CA  1 
ATOM   86   C C   . LYS A 1 19  ? 47.75049 -19.44167 33.81266 1.000 74.34493  ? 19  LYS A C   1 
ATOM   87   O O   . LYS A 1 19  ? 46.63426 -19.81017 34.18698 1.000 73.36029  ? 19  LYS A O   1 
ATOM   88   C CB  . LYS A 1 19  ? 48.21368 -17.10415 34.56756 1.000 91.22965  ? 19  LYS A CB  1 
ATOM   89   C CG  . LYS A 1 19  ? 48.51870 -15.65596 34.22439 1.000 106.41884 ? 19  LYS A CG  1 
ATOM   90   C CD  . LYS A 1 19  ? 48.45817 -14.77433 35.46369 1.000 127.06241 ? 19  LYS A CD  1 
ATOM   91   C CE  . LYS A 1 19  ? 49.28189 -15.35828 36.60056 1.000 128.96142 ? 19  LYS A CE  1 
ATOM   92   N NZ  . LYS A 1 19  ? 49.12025 -14.58413 37.86268 1.000 122.78351 ? 19  LYS A NZ  1 
ATOM   93   N N   . GLY A 1 20  ? 48.80322 -20.25459 33.78030 1.000 68.10173  ? 20  GLY A N   1 
ATOM   94   C CA  . GLY A 1 20  ? 48.62559 -21.65653 34.10720 1.000 59.90733  ? 20  GLY A CA  1 
ATOM   95   C C   . GLY A 1 20  ? 49.92310 -22.30983 34.52050 1.000 59.93699  ? 20  GLY A C   1 
ATOM   96   O O   . GLY A 1 20  ? 51.01485 -21.78203 34.30265 1.000 61.89084  ? 20  GLY A O   1 
ATOM   97   N N   . LYS A 1 21  ? 49.77564 -23.48239 35.13206 1.000 58.28551  ? 21  LYS A N   1 
ATOM   98   C CA  A LYS A 1 21  ? 50.90594 -24.27243 35.60007 0.476 72.65703  ? 21  LYS A CA  1 
ATOM   99   C CA  B LYS A 1 21  ? 50.90826 -24.27043 35.59127 0.524 69.81096  ? 21  LYS A CA  1 
ATOM   100  C C   . LYS A 1 21  ? 50.57081 -25.74600 35.43936 1.000 58.97067  ? 21  LYS A C   1 
ATOM   101  O O   . LYS A 1 21  ? 49.41816 -26.15349 35.60184 1.000 66.84787  ? 21  LYS A O   1 
ATOM   102  C CB  A LYS A 1 21  ? 51.24554 -23.97936 37.06797 0.476 72.19794  ? 21  LYS A CB  1 
ATOM   103  C CB  B LYS A 1 21  ? 51.25863 -23.94731 37.05004 0.524 75.77868  ? 21  LYS A CB  1 
ATOM   104  C CG  A LYS A 1 21  ? 51.76751 -22.58030 37.34090 0.476 79.93538  ? 21  LYS A CG  1 
ATOM   105  C CG  B LYS A 1 21  ? 52.54040 -24.59189 37.54622 0.524 76.17383  ? 21  LYS A CG  1 
ATOM   106  C CD  A LYS A 1 21  ? 51.92425 -22.35620 38.83227 0.476 79.59542  ? 21  LYS A CD  1 
ATOM   107  C CD  B LYS A 1 21  ? 52.78566 -24.25410 39.00427 0.524 67.27749  ? 21  LYS A CD  1 
ATOM   108  C CE  A LYS A 1 21  ? 52.75730 -23.45839 39.46002 0.476 74.32370  ? 21  LYS A CE  1 
ATOM   109  C CE  B LYS A 1 21  ? 54.15884 -24.71478 39.44885 0.524 100.65339 ? 21  LYS A CE  1 
ATOM   110  N NZ  A LYS A 1 21  ? 52.78752 -23.35200 40.94166 0.476 103.95072 ? 21  LYS A NZ  1 
ATOM   111  N NZ  B LYS A 1 21  ? 54.38362 -24.46635 40.90009 0.524 100.12988 ? 21  LYS A NZ  1 
ATOM   112  N N   . LEU A 1 22  ? 51.58690 -26.54287 35.12182 1.000 57.47157  ? 22  LEU A N   1 
ATOM   113  C CA  . LEU A 1 22  ? 51.40611 -27.97908 34.96628 1.000 69.30728  ? 22  LEU A CA  1 
ATOM   114  C C   . LEU A 1 22  ? 51.62568 -28.67488 36.30321 1.000 70.75072  ? 22  LEU A C   1 
ATOM   115  O O   . LEU A 1 22  ? 52.67044 -28.49949 36.93950 1.000 60.91188  ? 22  LEU A O   1 
ATOM   116  C CB  . LEU A 1 22  ? 52.36205 -28.54583 33.91893 1.000 58.66429  ? 22  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 22  ? 52.20309 -30.05192 33.70463 1.000 61.39942  ? 22  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 22  ? 50.82372 -30.36982 33.14076 1.000 54.04679  ? 22  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 22  ? 53.30152 -30.59743 32.80777 1.000 61.23628  ? 22  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 23  ? 50.64247 -29.46809 36.72044 1.000 60.03927  ? 23  LEU A N   1 
ATOM   121  C CA  . LEU A 1 23  ? 50.69892 -30.19107 37.98553 1.000 65.13982  ? 23  LEU A CA  1 
ATOM   122  C C   . LEU A 1 23  ? 50.90222 -31.68832 37.82207 1.000 65.34652  ? 23  LEU A C   1 
ATOM   123  O O   . LEU A 1 23  ? 51.72656 -32.26856 38.53052 1.000 74.47883  ? 23  LEU A O   1 
ATOM   124  C CB  . LEU A 1 23  ? 49.42049 -29.93762 38.79614 1.000 55.72971  ? 23  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 23  ? 49.19232 -28.48486 39.23261 1.000 69.39894  ? 23  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 23  ? 47.91317 -28.36010 40.04581 1.000 58.40190  ? 23  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 23  ? 50.38802 -27.96668 40.01743 1.000 57.92891  ? 23  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 24  ? 50.18011 -32.33369 36.90611 1.000 57.42741  ? 24  ARG A N   1 
ATOM   129  C CA  . ARG A 1 24  ? 50.26135 -33.77982 36.74947 1.000 60.70841  ? 24  ARG A CA  1 
ATOM   130  C C   . ARG A 1 24  ? 49.99047 -34.16019 35.30159 1.000 58.72747  ? 24  ARG A C   1 
ATOM   131  O O   . ARG A 1 24  ? 49.14284 -33.55374 34.64117 1.000 56.52664  ? 24  ARG A O   1 
ATOM   132  C CB  . ARG A 1 24  ? 49.26065 -34.50372 37.66532 1.000 55.53557  ? 24  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 24  ? 49.63330 -34.50152 39.13974 1.000 107.33384 ? 24  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 24  ? 48.44078 -34.81695 40.02808 1.000 113.47942 ? 24  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 24  ? 48.04005 -36.21633 39.95312 1.000 116.62314 ? 24  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 24  ? 47.10009 -36.76489 40.71088 1.000 118.76626 ? 24  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 24  ? 46.43575 -36.05648 41.60836 1.000 112.01369 ? 24  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 24  ? 46.81959 -38.05686 40.56432 1.000 123.37662 ? 24  ARG A NH2 1 
ATOM   139  N N   . GLU A 1 25  ? 50.71295 -35.17171 34.82177 1.000 66.04947  ? 25  GLU A N   1 
ATOM   140  C CA  . GLU A 1 25  ? 50.45847 -35.80451 33.53188 1.000 60.67044  ? 25  GLU A CA  1 
ATOM   141  C C   . GLU A 1 25  ? 50.13906 -37.27187 33.77697 1.000 59.06442  ? 25  GLU A C   1 
ATOM   142  O O   . GLU A 1 25  ? 50.98371 -38.01323 34.29054 1.000 64.20518  ? 25  GLU A O   1 
ATOM   143  C CB  . GLU A 1 25  ? 51.66316 -35.68486 32.59441 1.000 61.87757  ? 25  GLU A CB  1 
ATOM   144  C CG  . GLU A 1 25  ? 52.10680 -34.27136 32.26863 1.000 93.85145  ? 25  GLU A CG  1 
ATOM   145  C CD  . GLU A 1 25  ? 53.23724 -34.25319 31.25309 1.000 105.11913 ? 25  GLU A CD  1 
ATOM   146  O OE1 . GLU A 1 25  ? 53.38850 -35.25014 30.51527 1.000 109.06182 ? 25  GLU A OE1 1 
ATOM   147  O OE2 . GLU A 1 25  ? 53.97909 -33.25107 31.19348 1.000 111.27199 ? 25  GLU A OE2 1 
ATOM   148  N N   . GLU A 1 26  ? 48.93148 -37.69128 33.40748 1.000 52.51064  ? 26  GLU A N   1 
ATOM   149  C CA  . GLU A 1 26  ? 48.51278 -39.07702 33.55465 1.000 66.24657  ? 26  GLU A CA  1 
ATOM   150  C C   . GLU A 1 26  ? 47.92651 -39.57637 32.24261 1.000 64.88987  ? 26  GLU A C   1 
ATOM   151  O O   . GLU A 1 26  ? 47.48350 -38.79534 31.39703 1.000 53.44483  ? 26  GLU A O   1 
ATOM   152  C CB  . GLU A 1 26  ? 47.47313 -39.24958 34.67032 1.000 53.93427  ? 26  GLU A CB  1 
ATOM   153  C CG  . GLU A 1 26  ? 47.88293 -38.70335 36.02054 1.000 91.49461  ? 26  GLU A CG  1 
ATOM   154  C CD  . GLU A 1 26  ? 46.80577 -38.90692 37.06686 1.000 107.33502 ? 26  GLU A CD  1 
ATOM   155  O OE1 . GLU A 1 26  ? 45.79241 -39.56875 36.75656 1.000 92.88782  ? 26  GLU A OE1 1 
ATOM   156  O OE2 . GLU A 1 26  ? 46.96889 -38.40501 38.19724 1.000 118.98853 ? 26  GLU A OE2 1 
ATOM   157  N N   . TRP A 1 27  ? 47.91297 -40.89886 32.09327 1.000 55.80118  ? 27  TRP A N   1 
ATOM   158  C CA  . TRP A 1 27  ? 47.35424 -41.53806 30.91234 1.000 68.44314  ? 27  TRP A CA  1 
ATOM   159  C C   . TRP A 1 27  ? 46.77109 -42.88715 31.30083 1.000 68.62482  ? 27  TRP A C   1 
ATOM   160  O O   . TRP A 1 27  ? 47.21476 -43.52126 32.26189 1.000 76.14546  ? 27  TRP A O   1 
ATOM   161  C CB  . TRP A 1 27  ? 48.40509 -41.72367 29.81604 1.000 53.68141  ? 27  TRP A CB  1 
ATOM   162  C CG  . TRP A 1 27  ? 49.65853 -42.33473 30.32421 1.000 53.07857  ? 27  TRP A CG  1 
ATOM   163  C CD1 . TRP A 1 27  ? 49.92372 -43.66401 30.47192 1.000 59.50565  ? 27  TRP A CD1 1 
ATOM   164  C CD2 . TRP A 1 27  ? 50.82648 -41.63885 30.76614 1.000 61.61312  ? 27  TRP A CD2 1 
ATOM   165  N NE1 . TRP A 1 27  ? 51.18963 -43.83954 30.97501 1.000 63.79229  ? 27  TRP A NE1 1 
ATOM   166  C CE2 . TRP A 1 27  ? 51.76440 -42.61024 31.16613 1.000 67.26356  ? 27  TRP A CE2 1 
ATOM   167  C CE3 . TRP A 1 27  ? 51.17149 -40.28718 30.86054 1.000 55.90934  ? 27  TRP A CE3 1 
ATOM   168  C CZ2 . TRP A 1 27  ? 53.02452 -42.27327 31.65298 1.000 56.69419  ? 27  TRP A CZ2 1 
ATOM   169  C CZ3 . TRP A 1 27  ? 52.42223 -39.95457 31.34419 1.000 54.55050  ? 27  TRP A CZ3 1 
ATOM   170  C CH2 . TRP A 1 27  ? 53.33326 -40.94307 31.73413 1.000 57.82147  ? 27  TRP A CH2 1 
ATOM   171  N N   . SER A 1 28  ? 45.77693 -43.32025 30.53547 1.000 79.39990  ? 28  SER A N   1 
ATOM   172  C CA  . SER A 1 28  ? 45.12583 -44.60040 30.75399 1.000 73.32369  ? 28  SER A CA  1 
ATOM   173  C C   . SER A 1 28  ? 45.87479 -45.69606 29.99789 1.000 77.58331  ? 28  SER A C   1 
ATOM   174  O O   . SER A 1 28  ? 46.99069 -45.50116 29.50847 1.000 80.33725  ? 28  SER A O   1 
ATOM   175  C CB  . SER A 1 28  ? 43.66546 -44.52489 30.31725 1.000 90.02042  ? 28  SER A CB  1 
ATOM   176  O OG  . SER A 1 28  ? 43.57289 -44.37961 28.90937 1.000 82.57028  ? 28  SER A OG  1 
ATOM   177  N N   . GLU A 1 29  ? 45.26148 -46.86946 29.90665 1.000 89.17075  ? 29  GLU A N   1 
ATOM   178  C CA  A GLU A 1 29  ? 45.80426 -47.94296 29.09220 0.565 89.13840  ? 29  GLU A CA  1 
ATOM   179  C CA  B GLU A 1 29  ? 45.79529 -47.95133 29.09607 0.435 89.82244  ? 29  GLU A CA  1 
ATOM   180  C C   . GLU A 1 29  ? 45.36478 -47.77197 27.64501 1.000 84.90304  ? 29  GLU A C   1 
ATOM   181  O O   . GLU A 1 29  ? 44.34043 -47.14940 27.35304 1.000 81.04955  ? 29  GLU A O   1 
ATOM   182  C CB  A GLU A 1 29  ? 45.34179 -49.30172 29.61450 0.565 88.79087  ? 29  GLU A CB  1 
ATOM   183  C CB  B GLU A 1 29  ? 45.31136 -49.30253 29.62991 0.435 89.46630  ? 29  GLU A CB  1 
ATOM   184  C CG  A GLU A 1 29  ? 43.83303 -49.46345 29.59140 0.565 83.94696  ? 29  GLU A CG  1 
ATOM   185  C CG  B GLU A 1 29  ? 45.97013 -50.51891 28.99696 0.435 100.25271 ? 29  GLU A CG  1 
ATOM   186  C CD  A GLU A 1 29  ? 43.38337 -50.86045 29.95574 0.565 94.53116  ? 29  GLU A CD  1 
ATOM   187  C CD  B GLU A 1 29  ? 45.33945 -51.82088 29.44413 0.435 109.32079 ? 29  GLU A CD  1 
ATOM   188  O OE1 A GLU A 1 29  ? 44.25088 -51.71551 30.22926 0.565 115.39483 ? 29  GLU A OE1 1 
ATOM   189  O OE1 B GLU A 1 29  ? 44.23205 -51.77538 30.01832 0.435 114.33464 ? 29  GLU A OE1 1 
ATOM   190  O OE2 A GLU A 1 29  ? 42.15816 -51.10239 29.96583 0.565 98.60087  ? 29  GLU A OE2 1 
ATOM   191  O OE2 B GLU A 1 29  ? 45.95041 -52.88823 29.22254 0.435 101.48776 ? 29  GLU A OE2 1 
ATOM   192  N N   . GLU A 1 30  ? 46.16167 -48.31518 26.73106 1.000 90.34669  ? 30  GLU A N   1 
ATOM   193  C CA  . GLU A 1 30  ? 45.76849 -48.31967 25.32882 1.000 92.39837  ? 30  GLU A CA  1 
ATOM   194  C C   . GLU A 1 30  ? 44.58749 -49.26416 25.14850 1.000 90.44314  ? 30  GLU A C   1 
ATOM   195  O O   . GLU A 1 30  ? 44.66869 -50.44532 25.50146 1.000 94.46158  ? 30  GLU A O   1 
ATOM   196  C CB  . GLU A 1 30  ? 46.93549 -48.73794 24.44062 1.000 96.83079  ? 30  GLU A CB  1 
ATOM   197  C CG  . GLU A 1 30  ? 47.93628 -47.62891 24.17355 1.000 97.94826  ? 30  GLU A CG  1 
ATOM   198  C CD  . GLU A 1 30  ? 49.03384 -48.05842 23.22296 1.000 111.48923 ? 30  GLU A CD  1 
ATOM   199  O OE1 . GLU A 1 30  ? 49.03655 -49.23945 22.81760 1.000 124.50869 ? 30  GLU A OE1 1 
ATOM   200  O OE2 . GLU A 1 30  ? 49.89215 -47.21770 22.88076 1.000 109.19014 ? 30  GLU A OE2 1 
ATOM   201  N N   . LYS A 1 31  ? 43.48514 -48.74207 24.62270 1.000 86.77999  ? 31  LYS A N   1 
ATOM   202  C CA  . LYS A 1 31  ? 42.27576 -49.51903 24.39955 1.000 91.17200  ? 31  LYS A CA  1 
ATOM   203  C C   . LYS A 1 31  ? 42.09905 -49.76932 22.90945 1.000 88.30653  ? 31  LYS A C   1 
ATOM   204  O O   . LYS A 1 31  ? 42.41057 -48.90461 22.08470 1.000 88.14429  ? 31  LYS A O   1 
ATOM   205  C CB  . LYS A 1 31  ? 41.04616 -48.79887 24.95799 1.000 80.71627  ? 31  LYS A CB  1 
ATOM   206  C CG  . LYS A 1 31  ? 41.18620 -48.35330 26.40548 1.000 107.82543 ? 31  LYS A CG  1 
ATOM   207  C CD  . LYS A 1 31  ? 39.96540 -47.56244 26.84913 1.000 122.33346 ? 31  LYS A CD  1 
ATOM   208  C CE  . LYS A 1 31  ? 40.14088 -46.99462 28.24784 1.000 112.14350 ? 31  LYS A CE  1 
ATOM   209  N NZ  . LYS A 1 31  ? 38.96735 -46.17255 28.65510 1.000 112.16356 ? 31  LYS A NZ  1 
ATOM   210  N N   . THR A 1 32  ? 41.59935 -50.95390 22.57011 1.000 99.56216  ? 32  THR A N   1 
ATOM   211  C CA  . THR A 1 32  ? 41.40957 -51.36682 21.18487 1.000 93.26995  ? 32  THR A CA  1 
ATOM   212  C C   . THR A 1 32  ? 39.91905 -51.51335 20.91300 1.000 90.00252  ? 32  THR A C   1 
ATOM   213  O O   . THR A 1 32  ? 39.23176 -52.28049 21.59674 1.000 89.40299  ? 32  THR A O   1 
ATOM   214  C CB  . THR A 1 32  ? 42.14149 -52.67797 20.89757 1.000 99.62438  ? 32  THR A CB  1 
ATOM   215  O OG1 . THR A 1 32  ? 43.52828 -52.53535 21.23323 1.000 102.94416 ? 32  THR A OG1 1 
ATOM   216  C CG2 . THR A 1 32  ? 42.02022 -53.04681 19.42609 1.000 102.64962 ? 32  THR A CG2 1 
ATOM   217  N N   . THR A 1 33  ? 39.42649 -50.78017 19.91842 1.000 92.71469  ? 33  THR A N   1 
ATOM   218  C CA  . THR A 1 33  ? 38.00657 -50.81011 19.59880 1.000 87.76262  ? 33  THR A CA  1 
ATOM   219  C C   . THR A 1 33  ? 37.60374 -52.17709 19.06102 1.000 88.28479  ? 33  THR A C   1 
ATOM   220  O O   . THR A 1 33  ? 38.31699 -52.78316 18.25649 1.000 95.18084  ? 33  THR A O   1 
ATOM   221  C CB  . THR A 1 33  ? 37.66659 -49.72894 18.57296 1.000 93.25311  ? 33  THR A CB  1 
ATOM   222  O OG1 . THR A 1 33  ? 38.37140 -49.98903 17.35202 1.000 92.30151  ? 33  THR A OG1 1 
ATOM   223  C CG2 . THR A 1 33  ? 38.05975 -48.35653 19.09674 1.000 89.31239  ? 33  THR A CG2 1 
ATOM   224  N N   . GLY A 1 34  ? 36.45130 -52.66313 19.51692 1.000 86.07462  ? 34  GLY A N   1 
ATOM   225  C CA  . GLY A 1 34  ? 35.88836 -53.90225 19.02852 1.000 90.67967  ? 34  GLY A CA  1 
ATOM   226  C C   . GLY A 1 34  ? 35.00534 -53.68315 17.81481 1.000 87.25347  ? 34  GLY A C   1 
ATOM   227  O O   . GLY A 1 34  ? 34.98505 -52.61399 17.20236 1.000 87.89327  ? 34  GLY A O   1 
ATOM   228  N N   . GLU A 1 35  ? 34.25384 -54.73077 17.46804 1.000 89.96399  ? 35  GLU A N   1 
ATOM   229  C CA  . GLU A 1 35  ? 33.39325 -54.66755 16.29189 1.000 91.66009  ? 35  GLU A CA  1 
ATOM   230  C C   . GLU A 1 35  ? 32.30513 -53.61035 16.42057 1.000 97.17062  ? 35  GLU A C   1 
ATOM   231  O O   . GLU A 1 35  ? 31.80411 -53.12718 15.39936 1.000 81.72984  ? 35  GLU A O   1 
ATOM   232  C CB  . GLU A 1 35  ? 32.76499 -56.03565 16.02488 1.000 94.76663  ? 35  GLU A CB  1 
ATOM   233  C CG  . GLU A 1 35  ? 33.76647 -57.11078 15.64333 1.000 99.83423  ? 35  GLU A CG  1 
ATOM   234  C CD  . GLU A 1 35  ? 34.54717 -56.76625 14.38959 1.000 114.11154 ? 35  GLU A CD  1 
ATOM   235  O OE1 . GLU A 1 35  ? 33.98983 -56.08245 13.50399 1.000 126.95983 ? 35  GLU A OE1 1 
ATOM   236  O OE2 . GLU A 1 35  ? 35.72307 -57.17676 14.29265 1.000 151.44916 ? 35  GLU A OE2 1 
ATOM   237  N N   . ASP A 1 36  ? 31.92731 -53.23969 17.64201 1.000 79.85575  ? 36  ASP A N   1 
ATOM   238  C CA  . ASP A 1 36  ? 30.96992 -52.16001 17.83611 1.000 75.35831  ? 36  ASP A CA  1 
ATOM   239  C C   . ASP A 1 36  ? 31.60034 -50.78146 17.67419 1.000 74.09913  ? 36  ASP A C   1 
ATOM   240  O O   . ASP A 1 36  ? 30.87753 -49.77963 17.69300 1.000 71.88463  ? 36  ASP A O   1 
ATOM   241  C CB  . ASP A 1 36  ? 30.31051 -52.28284 19.21543 1.000 74.68698  ? 36  ASP A CB  1 
ATOM   242  C CG  . ASP A 1 36  ? 31.32433 -52.38646 20.35404 1.000 96.29911  ? 36  ASP A CG  1 
ATOM   243  O OD1 . ASP A 1 36  ? 32.51969 -52.09268 20.14297 1.000 82.44690  ? 36  ASP A OD1 1 
ATOM   244  O OD2 . ASP A 1 36  ? 30.91920 -52.76576 21.47352 1.000 96.47018  ? 36  ASP A OD2 1 
ATOM   245  N N   . GLY A 1 37  ? 32.92077 -50.70905 17.50717 1.000 76.62904  ? 37  GLY A N   1 
ATOM   246  C CA  . GLY A 1 37  ? 33.61652 -49.44753 17.35615 1.000 75.95079  ? 37  GLY A CA  1 
ATOM   247  C C   . GLY A 1 37  ? 33.63776 -48.58794 18.59567 1.000 80.22537  ? 37  GLY A C   1 
ATOM   248  O O   . GLY A 1 37  ? 34.06706 -47.43188 18.52651 1.000 71.98204  ? 37  GLY A O   1 
ATOM   249  N N   . LEU A 1 38  ? 33.21371 -49.12773 19.73427 1.000 88.15033  ? 38  LEU A N   1 
ATOM   250  C CA  . LEU A 1 38  ? 32.95856 -48.33586 20.92738 1.000 89.61633  ? 38  LEU A CA  1 
ATOM   251  C C   . LEU A 1 38  ? 34.22023 -48.14101 21.75457 1.000 90.80831  ? 38  LEU A C   1 
ATOM   252  O O   . LEU A 1 38  ? 35.06387 -49.03658 21.85310 1.000 91.45435  ? 38  LEU A O   1 
ATOM   253  C CB  . LEU A 1 38  ? 31.88970 -49.00231 21.79099 1.000 91.69887  ? 38  LEU A CB  1 
ATOM   254  C CG  . LEU A 1 38  ? 30.49291 -49.08012 21.18759 1.000 96.46106  ? 38  LEU A CG  1 
ATOM   255  C CD1 . LEU A 1 38  ? 29.57014 -49.77152 22.17421 1.000 101.08142 ? 38  LEU A CD1 1 
ATOM   256  C CD2 . LEU A 1 38  ? 30.00243 -47.68302 20.84082 1.000 89.58579  ? 38  LEU A CD2 1 
ATOM   257  N N   . LEU A 1 39  ? 34.33187 -46.96040 22.35818 1.000 91.28483  ? 39  LEU A N   1 
ATOM   258  C CA  A LEU A 1 39  ? 35.42771 -46.62466 23.26185 0.365 92.85648  ? 39  LEU A CA  1 
ATOM   259  C CA  B LEU A 1 39  ? 35.42518 -46.63217 23.26534 0.635 92.86591  ? 39  LEU A CA  1 
ATOM   260  C C   . LEU A 1 39  ? 34.82388 -45.95923 24.49153 1.000 94.96772  ? 39  LEU A C   1 
ATOM   261  O O   . LEU A 1 39  ? 34.34405 -44.82283 24.41257 1.000 94.40308  ? 39  LEU A O   1 
ATOM   262  C CB  A LEU A 1 39  ? 36.44790 -45.70783 22.58281 0.365 91.36736  ? 39  LEU A CB  1 
ATOM   263  C CB  B LEU A 1 39  ? 36.45754 -45.73313 22.58426 0.635 91.37864  ? 39  LEU A CB  1 
ATOM   264  C CG  A LEU A 1 39  ? 37.72140 -45.40349 23.37541 0.365 93.01570  ? 39  LEU A CG  1 
ATOM   265  C CG  B LEU A 1 39  ? 37.92801 -46.01742 22.90685 0.635 97.08876  ? 39  LEU A CG  1 
ATOM   266  C CD1 A LEU A 1 39  ? 38.68554 -46.57801 23.31827 0.365 93.39599  ? 39  LEU A CD1 1 
ATOM   267  C CD1 B LEU A 1 39  ? 38.27842 -45.57793 24.31559 0.635 95.04285  ? 39  LEU A CD1 1 
ATOM   268  C CD2 A LEU A 1 39  ? 38.36963 -44.13769 22.85597 0.365 91.97202  ? 39  LEU A CD2 1 
ATOM   269  C CD2 B LEU A 1 39  ? 38.23841 -47.49361 22.71724 0.635 97.12704  ? 39  LEU A CD2 1 
ATOM   270  N N   . GLU A 1 40  ? 34.83612 -46.66499 25.61777 1.000 97.54892  ? 40  GLU A N   1 
ATOM   271  C CA  . GLU A 1 40  ? 34.29641 -46.15501 26.87331 1.000 100.00687 ? 40  GLU A CA  1 
ATOM   272  C C   . GLU A 1 40  ? 35.45701 -45.71048 27.75712 1.000 101.96007 ? 40  GLU A C   1 
ATOM   273  O O   . GLU A 1 40  ? 36.27400 -46.53386 28.18239 1.000 103.33301 ? 40  GLU A O   1 
ATOM   274  C CB  . GLU A 1 40  ? 33.44684 -47.21220 27.57735 1.000 102.00496 ? 40  GLU A CB  1 
ATOM   275  C CG  . GLU A 1 40  ? 32.23017 -47.68012 26.78834 1.000 110.40355 ? 40  GLU A CG  1 
ATOM   276  C CD  . GLU A 1 40  ? 32.54068 -48.84146 25.86200 1.000 138.16972 ? 40  GLU A CD  1 
ATOM   277  O OE1 . GLU A 1 40  ? 33.73250 -49.18302 25.71347 1.000 144.01543 ? 40  GLU A OE1 1 
ATOM   278  O OE2 . GLU A 1 40  ? 31.59239 -49.41743 25.28741 1.000 147.09994 ? 40  GLU A OE2 1 
ATOM   279  N N   . ILE A 1 41  ? 35.52760 -44.41227 28.03741 1.000 102.28477 ? 41  ILE A N   1 
ATOM   280  C CA  . ILE A 1 41  ? 36.55342 -43.84920 28.90573 1.000 109.77524 ? 41  ILE A CA  1 
ATOM   281  C C   . ILE A 1 41  ? 35.89091 -43.40143 30.20172 1.000 121.68531 ? 41  ILE A C   1 
ATOM   282  O O   . ILE A 1 41  ? 34.88754 -42.67603 30.18312 1.000 107.04865 ? 41  ILE A O   1 
ATOM   283  C CB  . ILE A 1 41  ? 37.31123 -42.69315 28.22522 1.000 135.04398 ? 41  ILE A CB  1 
ATOM   284  C CG1 . ILE A 1 41  ? 36.36202 -41.57901 27.78186 1.000 123.33578 ? 41  ILE A CG1 1 
ATOM   285  C CG2 . ILE A 1 41  ? 38.09985 -43.20221 27.02960 1.000 109.05274 ? 41  ILE A CG2 1 
ATOM   286  C CD1 . ILE A 1 41  ? 37.07525 -40.35778 27.24410 1.000 129.26574 ? 41  ILE A CD1 1 
ATOM   287  N N   . ASP A 1 42  ? 36.43611 -43.85680 31.32419 1.000 110.49712 ? 42  ASP A N   1 
ATOM   288  C CA  A ASP A 1 42  ? 35.92688 -43.50891 32.64518 0.678 124.73195 ? 42  ASP A CA  1 
ATOM   289  C CA  B ASP A 1 42  ? 35.92735 -43.51259 32.64602 0.322 124.86184 ? 42  ASP A CA  1 
ATOM   290  C C   . ASP A 1 42  ? 36.80728 -42.40881 33.22229 1.000 115.64157 ? 42  ASP A C   1 
ATOM   291  O O   . ASP A 1 42  ? 37.98461 -42.63691 33.51890 1.000 126.99154 ? 42  ASP A O   1 
ATOM   292  C CB  A ASP A 1 42  ? 35.90017 -44.72751 33.56475 0.678 127.92980 ? 42  ASP A CB  1 
ATOM   293  C CB  B ASP A 1 42  ? 35.91218 -44.73867 33.55669 0.322 127.85671 ? 42  ASP A CB  1 
ATOM   294  C CG  A ASP A 1 42  ? 34.90458 -45.77600 33.11375 0.678 137.04998 ? 42  ASP A CG  1 
ATOM   295  C CG  B ASP A 1 42  ? 34.82629 -44.66974 34.61254 0.322 127.44541 ? 42  ASP A CG  1 
ATOM   296  O OD1 A ASP A 1 42  ? 34.32503 -45.61582 32.01916 0.678 139.25127 ? 42  ASP A OD1 1 
ATOM   297  O OD1 B ASP A 1 42  ? 33.64138 -44.84447 34.25913 0.322 130.90187 ? 42  ASP A OD1 1 
ATOM   298  O OD2 A ASP A 1 42  ? 34.69739 -46.75800 33.85646 0.678 123.06964 ? 42  ASP A OD2 1 
ATOM   299  O OD2 B ASP A 1 42  ? 35.15706 -44.44619 35.79540 0.322 135.38790 ? 42  ASP A OD2 1 
ATOM   300  N N   . LEU A 1 43  ? 36.23890 -41.21691 33.37416 1.000 115.90022 ? 43  LEU A N   1 
ATOM   301  C CA  . LEU A 1 43  ? 36.97967 -40.11388 33.96053 1.000 136.79594 ? 43  LEU A CA  1 
ATOM   302  C C   . LEU A 1 43  ? 37.19075 -40.36517 35.45378 1.000 122.67720 ? 43  LEU A C   1 
ATOM   303  O O   . LEU A 1 43  ? 36.63551 -41.29919 36.04049 1.000 125.93180 ? 43  LEU A O   1 
ATOM   304  C CB  . LEU A 1 43  ? 36.24155 -38.79571 33.72913 1.000 117.95360 ? 43  LEU A CB  1 
ATOM   305  C CG  . LEU A 1 43  ? 35.67167 -38.59297 32.32123 1.000 113.23746 ? 43  LEU A CG  1 
ATOM   306  C CD1 . LEU A 1 43  ? 34.88660 -37.29322 32.23624 1.000 120.23784 ? 43  LEU A CD1 1 
ATOM   307  C CD2 . LEU A 1 43  ? 36.77440 -38.62573 31.27300 1.000 110.96151 ? 43  LEU A CD2 1 
ATOM   308  N N   . GLU A 1 44  ? 38.01535 -39.51813 36.07517 1.000 143.66520 ? 44  GLU A N   1 
ATOM   309  C CA  . GLU A 1 44  ? 38.27271 -39.68035 37.50236 1.000 160.82412 ? 44  GLU A CA  1 
ATOM   310  C C   . GLU A 1 44  ? 37.00680 -39.47446 38.32324 1.000 172.36571 ? 44  GLU A C   1 
ATOM   311  O O   . GLU A 1 44  ? 36.87022 -40.04765 39.41008 1.000 181.95677 ? 44  GLU A O   1 
ATOM   312  C CB  . GLU A 1 44  ? 39.36270 -38.71476 37.96478 1.000 148.76432 ? 44  GLU A CB  1 
ATOM   313  C CG  . GLU A 1 44  ? 39.86612 -39.01342 39.36686 1.000 162.51348 ? 44  GLU A CG  1 
ATOM   314  C CD  . GLU A 1 44  ? 40.64145 -37.86506 39.97053 1.000 166.37604 ? 44  GLU A CD  1 
ATOM   315  O OE1 . GLU A 1 44  ? 40.73380 -36.80256 39.32238 1.000 169.12327 ? 44  GLU A OE1 1 
ATOM   316  O OE2 . GLU A 1 44  ? 41.15489 -38.02484 41.09738 1.000 164.91138 ? 44  GLU A OE2 1 
ATOM   317  N N   . THR A 1 45  ? 36.06795 -38.67480 37.81829 1.000 184.15738 ? 45  THR A N   1 
ATOM   318  C CA  . THR A 1 45  ? 34.81628 -38.42585 38.51975 1.000 184.72702 ? 45  THR A CA  1 
ATOM   319  C C   . THR A 1 45  ? 33.84099 -39.59259 38.43109 1.000 175.01646 ? 45  THR A C   1 
ATOM   320  O O   . THR A 1 45  ? 32.82208 -39.57859 39.13001 1.000 179.22595 ? 45  THR A O   1 
ATOM   321  C CB  . THR A 1 45  ? 34.14806 -37.16399 37.96925 1.000 182.35309 ? 45  THR A CB  1 
ATOM   322  O OG1 . THR A 1 45  ? 33.71759 -37.40034 36.62256 1.000 165.87373 ? 45  THR A OG1 1 
ATOM   323  C CG2 . THR A 1 45  ? 35.12294 -35.99569 37.98334 1.000 178.24805 ? 45  THR A CG2 1 
ATOM   324  N N   . GLY A 1 46  ? 34.12109 -40.59194 37.59543 1.000 154.08850 ? 46  GLY A N   1 
ATOM   325  C CA  . GLY A 1 46  ? 33.26297 -41.74689 37.44714 1.000 141.50545 ? 46  GLY A CA  1 
ATOM   326  C C   . GLY A 1 46  ? 32.35458 -41.71796 36.23706 1.000 132.61936 ? 46  GLY A C   1 
ATOM   327  O O   . GLY A 1 46  ? 31.76024 -42.75202 35.90662 1.000 128.35975 ? 46  GLY A O   1 
ATOM   328  N N   . LYS A 1 47  ? 32.23234 -40.57523 35.56848 1.000 135.34145 ? 47  LYS A N   1 
ATOM   329  C CA  A LYS A 1 47  ? 31.36840 -40.49080 34.40182 0.460 134.61572 ? 47  LYS A CA  1 
ATOM   330  C CA  B LYS A 1 47  ? 31.37739 -40.46733 34.39510 0.540 134.62479 ? 47  LYS A CA  1 
ATOM   331  C C   . LYS A 1 47  ? 32.00500 -41.18776 33.20567 1.000 125.34301 ? 47  LYS A C   1 
ATOM   332  O O   . LYS A 1 47  ? 33.22900 -41.24970 33.06626 1.000 120.01993 ? 47  LYS A O   1 
ATOM   333  C CB  A LYS A 1 47  ? 31.06778 -39.03257 34.06113 0.460 130.89599 ? 47  LYS A CB  1 
ATOM   334  C CB  B LYS A 1 47  ? 31.13908 -38.99495 34.05365 0.540 130.85694 ? 47  LYS A CB  1 
ATOM   335  C CG  A LYS A 1 47  ? 30.32495 -38.28994 35.15685 0.460 135.19786 ? 47  LYS A CG  1 
ATOM   336  C CG  B LYS A 1 47  ? 30.09591 -38.74393 32.97745 0.540 131.62593 ? 47  LYS A CG  1 
ATOM   337  C CD  A LYS A 1 47  ? 28.92642 -38.84324 35.37270 0.460 129.09671 ? 47  LYS A CD  1 
ATOM   338  C CD  B LYS A 1 47  ? 28.68393 -38.92254 33.50630 0.540 130.06805 ? 47  LYS A CD  1 
ATOM   339  C CE  A LYS A 1 47  ? 28.02178 -38.55026 34.18807 0.460 125.42930 ? 47  LYS A CE  1 
ATOM   340  C CE  B LYS A 1 47  ? 27.65787 -38.62747 32.42442 0.540 136.06860 ? 47  LYS A CE  1 
ATOM   341  N NZ  A LYS A 1 47  ? 26.62692 -39.01052 34.43428 0.460 126.74932 ? 47  LYS A NZ  1 
ATOM   342  N NZ  B LYS A 1 47  ? 27.84048 -37.26870 31.84300 0.540 138.76385 ? 47  LYS A NZ  1 
ATOM   343  N N   . LYS A 1 48  ? 31.15130 -41.72747 32.33880 1.000 116.91402 ? 48  LYS A N   1 
ATOM   344  C CA  . LYS A 1 48  ? 31.57954 -42.44362 31.14415 1.000 122.79750 ? 48  LYS A CA  1 
ATOM   345  C C   . LYS A 1 48  ? 31.34693 -41.56523 29.92172 1.000 107.87394 ? 48  LYS A C   1 
ATOM   346  O O   . LYS A 1 48  ? 30.20633 -41.18519 29.63163 1.000 108.17065 ? 48  LYS A O   1 
ATOM   347  C CB  . LYS A 1 48  ? 30.82824 -43.76680 30.99636 1.000 110.66823 ? 48  LYS A CB  1 
ATOM   348  C CG  . LYS A 1 48  ? 31.10573 -44.78137 32.09224 1.000 136.90210 ? 48  LYS A CG  1 
ATOM   349  C CD  . LYS A 1 48  ? 30.37010 -46.08315 31.81716 1.000 140.73574 ? 48  LYS A CD  1 
ATOM   350  C CE  . LYS A 1 48  ? 30.59012 -47.09722 32.92453 1.000 164.72800 ? 48  LYS A CE  1 
ATOM   351  N NZ  . LYS A 1 48  ? 29.86415 -48.36728 32.64925 1.000 162.18632 ? 48  LYS A NZ  1 
ATOM   352  N N   . ALA A 1 49  ? 32.42428 -41.24654 29.21174 1.000 95.45138  ? 49  ALA A N   1 
ATOM   353  C CA  . ALA A 1 49  ? 32.34629 -40.57725 27.92109 1.000 106.21525 ? 49  ALA A CA  1 
ATOM   354  C C   . ALA A 1 49  ? 32.47631 -41.62389 26.82232 1.000 82.37457  ? 49  ALA A C   1 
ATOM   355  O O   . ALA A 1 49  ? 33.43485 -42.40316 26.81209 1.000 88.61576  ? 49  ALA A O   1 
ATOM   356  C CB  . ALA A 1 49  ? 33.43705 -39.51426 27.78440 1.000 98.20799  ? 49  ALA A CB  1 
ATOM   357  N N   . THR A 1 50  ? 31.51202 -41.64675 25.90821 1.000 91.13301  ? 50  THR A N   1 
ATOM   358  C CA  . THR A 1 50  ? 31.42279 -42.68129 24.88693 1.000 100.41052 ? 50  THR A CA  1 
ATOM   359  C C   . THR A 1 50  ? 31.81647 -42.11586 23.52922 1.000 92.76672  ? 50  THR A C   1 
ATOM   360  O O   . THR A 1 50  ? 31.32414 -41.05724 23.12398 1.000 82.44905  ? 50  THR A O   1 
ATOM   361  C CB  . THR A 1 50  ? 30.00934 -43.26335 24.82538 1.000 101.34791 ? 50  THR A CB  1 
ATOM   362  O OG1 . THR A 1 50  ? 29.08466 -42.23427 24.45496 1.000 133.25116 ? 50  THR A OG1 1 
ATOM   363  C CG2 . THR A 1 50  ? 29.60993 -43.82630 26.18230 1.000 114.58800 ? 50  THR A CG2 1 
ATOM   364  N N   . PHE A 1 51  ? 32.70408 -42.82578 22.83568 1.000 100.93694 ? 51  PHE A N   1 
ATOM   365  C CA  . PHE A 1 51  ? 33.10849 -42.49524 21.47795 1.000 69.17246  ? 51  PHE A CA  1 
ATOM   366  C C   . PHE A 1 51  ? 32.92285 -43.72280 20.59754 1.000 78.28133  ? 51  PHE A C   1 
ATOM   367  O O   . PHE A 1 51  ? 32.92047 -44.85834 21.07959 1.000 70.85524  ? 51  PHE A O   1 
ATOM   368  C CB  . PHE A 1 51  ? 34.56731 -42.02259 21.41545 1.000 69.59642  ? 51  PHE A CB  1 
ATOM   369  C CG  . PHE A 1 51  ? 34.83914 -40.78021 22.21283 1.000 85.65057  ? 51  PHE A CG  1 
ATOM   370  C CD1 . PHE A 1 51  ? 35.03818 -40.84982 23.58255 1.000 91.47937  ? 51  PHE A CD1 1 
ATOM   371  C CD2 . PHE A 1 51  ? 34.90627 -39.54328 21.59230 1.000 71.57585  ? 51  PHE A CD2 1 
ATOM   372  C CE1 . PHE A 1 51  ? 35.28947 -39.70938 24.31941 1.000 68.04166  ? 51  PHE A CE1 1 
ATOM   373  C CE2 . PHE A 1 51  ? 35.15985 -38.39732 22.32543 1.000 89.63680  ? 51  PHE A CE2 1 
ATOM   374  C CZ  . PHE A 1 51  ? 35.35211 -38.48131 23.69002 1.000 86.84172  ? 51  PHE A CZ  1 
ATOM   375  N N   . GLN A 1 52  ? 32.76923 -43.48860 19.29403 1.000 82.55143  ? 52  GLN A N   1 
ATOM   376  C CA  . GLN A 1 52  ? 32.56222 -44.57353 18.33936 1.000 72.27147  ? 52  GLN A CA  1 
ATOM   377  C C   . GLN A 1 52  ? 33.38070 -44.30727 17.08560 1.000 87.77947  ? 52  GLN A C   1 
ATOM   378  O O   . GLN A 1 52  ? 33.20391 -43.27337 16.43350 1.000 75.72254  ? 52  GLN A O   1 
ATOM   379  C CB  . GLN A 1 52  ? 31.08156 -44.73335 17.98502 1.000 72.31756  ? 52  GLN A CB  1 
ATOM   380  C CG  . GLN A 1 52  ? 30.76058 -46.05956 17.31093 1.000 73.86155  ? 52  GLN A CG  1 
ATOM   381  C CD  . GLN A 1 52  ? 29.30750 -46.17517 16.90539 1.000 74.27722  ? 52  GLN A CD  1 
ATOM   382  O OE1 . GLN A 1 52  ? 28.68839 -45.19743 16.48723 1.000 96.99096  ? 52  GLN A OE1 1 
ATOM   383  N NE2 . GLN A 1 52  ? 28.75244 -47.37461 17.03006 1.000 76.11934  ? 52  GLN A NE2 1 
ATOM   384  N N   . LYS A 1 53  ? 34.26754 -45.24282 16.75127 1.000 81.43740  ? 53  LYS A N   1 
ATOM   385  C CA  . LYS A 1 53  ? 35.09244 -45.15583 15.55258 1.000 76.59997  ? 53  LYS A CA  1 
ATOM   386  C C   . LYS A 1 53  ? 34.32060 -45.74484 14.37783 1.000 80.08797  ? 53  LYS A C   1 
ATOM   387  O O   . LYS A 1 53  ? 34.01341 -46.94231 14.36992 1.000 78.85148  ? 53  LYS A O   1 
ATOM   388  C CB  . LYS A 1 53  ? 36.41365 -45.89586 15.75923 1.000 78.28289  ? 53  LYS A CB  1 
ATOM   389  C CG  . LYS A 1 53  ? 37.29588 -45.98781 14.52510 1.000 84.98924  ? 53  LYS A CG  1 
ATOM   390  C CD  . LYS A 1 53  ? 38.52977 -45.10860 14.65459 1.000 81.80260  ? 53  LYS A CD  1 
ATOM   391  C CE  . LYS A 1 53  ? 38.26489 -43.69063 14.17906 1.000 87.09312  ? 53  LYS A CE  1 
ATOM   392  N NZ  . LYS A 1 53  ? 37.99056 -43.63885 12.71686 1.000 86.04814  ? 53  LYS A NZ  1 
ATOM   393  N N   . VAL A 1 54  ? 34.00665 -44.90646 13.38830 1.000 78.45026  ? 54  VAL A N   1 
ATOM   394  C CA  . VAL A 1 54  ? 33.20520 -45.32054 12.24547 1.000 83.82650  ? 54  VAL A CA  1 
ATOM   395  C C   . VAL A 1 54  ? 33.89162 -44.89701 10.95365 1.000 82.01360  ? 54  VAL A C   1 
ATOM   396  O O   . VAL A 1 54  ? 34.73483 -43.99749 10.92970 1.000 82.14963  ? 54  VAL A O   1 
ATOM   397  C CB  . VAL A 1 54  ? 31.77256 -44.74520 12.29911 1.000 83.85720  ? 54  VAL A CB  1 
ATOM   398  C CG1 . VAL A 1 54  ? 31.04780 -45.22734 13.54450 1.000 77.35391  ? 54  VAL A CG1 1 
ATOM   399  C CG2 . VAL A 1 54  ? 31.80960 -43.22659 12.25043 1.000 97.07380  ? 54  VAL A CG2 1 
ATOM   400  N N   . ASP A 1 55  ? 33.50983 -45.56797 9.86898  1.000 105.04066 ? 55  ASP A N   1 
ATOM   401  C CA  . ASP A 1 55  ? 34.00366 -45.22148 8.54318  1.000 86.50384  ? 55  ASP A CA  1 
ATOM   402  C C   . ASP A 1 55  ? 33.40487 -43.89041 8.10292  1.000 86.38668  ? 55  ASP A C   1 
ATOM   403  O O   . ASP A 1 55  ? 32.20270 -43.65596 8.25805  1.000 85.42079  ? 55  ASP A O   1 
ATOM   404  C CB  . ASP A 1 55  ? 33.65280 -46.33446 7.55359  1.000 88.86864  ? 55  ASP A CB  1 
ATOM   405  C CG  . ASP A 1 55  ? 34.31543 -46.15532 6.19724  1.000 105.80443 ? 55  ASP A CG  1 
ATOM   406  O OD1 . ASP A 1 55  ? 34.03727 -45.14521 5.51738  1.000 92.72897  ? 55  ASP A OD1 1 
ATOM   407  O OD2 . ASP A 1 55  ? 35.11346 -47.03318 5.80514  1.000 94.11887  ? 55  ASP A OD2 1 
ATOM   408  N N   . ALA A 1 56  ? 34.24814 -43.01565 7.55052  1.000 87.77677  ? 56  ALA A N   1 
ATOM   409  C CA  . ALA A 1 56  ? 33.79759 -41.67674 7.18643  1.000 99.81767  ? 56  ALA A CA  1 
ATOM   410  C C   . ALA A 1 56  ? 32.79206 -41.68492 6.04144  1.000 94.61022  ? 56  ALA A C   1 
ATOM   411  O O   . ALA A 1 56  ? 32.08807 -40.68814 5.84488  1.000 90.45330  ? 56  ALA A O   1 
ATOM   412  C CB  . ALA A 1 56  ? 34.99582 -40.80245 6.81889  1.000 89.75929  ? 56  ALA A CB  1 
ATOM   413  N N   . GLU A 1 57  ? 32.70774 -42.77681 5.28146  1.000 95.92817  ? 57  GLU A N   1 
ATOM   414  C CA  A GLU A 1 57  ? 31.77211 -42.88579 4.16951  0.703 111.47981 ? 57  GLU A CA  1 
ATOM   415  C CA  B GLU A 1 57  ? 31.77106 -42.88395 4.17087  0.297 111.16237 ? 57  GLU A CA  1 
ATOM   416  C C   . GLU A 1 57  ? 30.62239 -43.83779 4.48031  1.000 108.67292 ? 57  GLU A C   1 
ATOM   417  O O   . GLU A 1 57  ? 29.45920 -43.42756 4.46846  1.000 105.35201 ? 57  GLU A O   1 
ATOM   418  C CB  A GLU A 1 57  ? 32.50636 -43.33447 2.89753  0.703 99.89627  ? 57  GLU A CB  1 
ATOM   419  C CB  B GLU A 1 57  ? 32.50784 -43.32764 2.89895  0.297 100.61922 ? 57  GLU A CB  1 
ATOM   420  C CG  A GLU A 1 57  ? 33.42367 -42.27690 2.30369  0.703 115.37499 ? 57  GLU A CG  1 
ATOM   421  C CG  B GLU A 1 57  ? 31.59291 -43.61951 1.71851  0.297 119.40867 ? 57  GLU A CG  1 
ATOM   422  C CD  A GLU A 1 57  ? 33.94082 -42.65922 0.93112  0.703 118.43963 ? 57  GLU A CD  1 
ATOM   423  C CD  B GLU A 1 57  ? 30.85003 -42.39081 1.22949  0.297 122.53303 ? 57  GLU A CD  1 
ATOM   424  O OE1 A GLU A 1 57  ? 33.82115 -43.84528 0.55945  0.703 125.52125 ? 57  GLU A OE1 1 
ATOM   425  O OE1 B GLU A 1 57  ? 31.33973 -41.26378 1.45359  0.297 124.57477 ? 57  GLU A OE1 1 
ATOM   426  O OE2 A GLU A 1 57  ? 34.46084 -41.77300 0.22109  0.703 115.68192 ? 57  GLU A OE2 1 
ATOM   427  O OE2 B GLU A 1 57  ? 29.77241 -42.55334 0.62026  0.297 122.77891 ? 57  GLU A OE2 1 
ATOM   428  N N   . THR A 1 58  ? 30.91971 -45.10717 4.76181  1.000 104.92919 ? 58  THR A N   1 
ATOM   429  C CA  . THR A 1 58  ? 29.86217 -46.07366 5.03082  1.000 95.53742  ? 58  THR A CA  1 
ATOM   430  C C   . THR A 1 58  ? 29.27089 -45.93236 6.42731  1.000 89.75102  ? 58  THR A C   1 
ATOM   431  O O   . THR A 1 58  ? 28.12520 -46.34146 6.64267  1.000 109.05975 ? 58  THR A O   1 
ATOM   432  C CB  . THR A 1 58  ? 30.38344 -47.50180 4.84281  1.000 94.28954  ? 58  THR A CB  1 
ATOM   433  O OG1 . THR A 1 58  ? 31.28166 -47.83289 5.90839  1.000 102.10327 ? 58  THR A OG1 1 
ATOM   434  C CG2 . THR A 1 58  ? 31.11647 -47.63047 3.51567  1.000 97.54248  ? 58  THR A CG2 1 
ATOM   435  N N   . GLY A 1 59  ? 30.01365 -45.36486 7.37504  1.000 98.19391  ? 59  GLY A N   1 
ATOM   436  C CA  . GLY A 1 59  ? 29.55570 -45.28895 8.74588  1.000 84.80884  ? 59  GLY A CA  1 
ATOM   437  C C   . GLY A 1 59  ? 29.68111 -46.57567 9.53059  1.000 86.03845  ? 59  GLY A C   1 
ATOM   438  O O   . GLY A 1 59  ? 29.26524 -46.61324 10.69526 1.000 85.00214  ? 59  GLY A O   1 
ATOM   439  N N   . LYS A 1 60  ? 30.23885 -47.62430 8.93505  1.000 86.29005  ? 60  LYS A N   1 
ATOM   440  C CA  . LYS A 1 60  ? 30.37209 -48.89888 9.62180  1.000 89.89181  ? 60  LYS A CA  1 
ATOM   441  C C   . LYS A 1 60  ? 31.29997 -48.75300 10.82681 1.000 84.98440  ? 60  LYS A C   1 
ATOM   442  O O   . LYS A 1 60  ? 32.35039 -48.10788 10.72657 1.000 84.45191  ? 60  LYS A O   1 
ATOM   443  C CB  . LYS A 1 60  ? 30.91643 -49.95894 8.66205  1.000 90.30551  ? 60  LYS A CB  1 
ATOM   444  C CG  . LYS A 1 60  ? 31.17484 -51.31201 9.29638  1.000 97.06990  ? 60  LYS A CG  1 
ATOM   445  C CD  . LYS A 1 60  ? 32.08388 -52.16019 8.42192  1.000 94.81121  ? 60  LYS A CD  1 
ATOM   446  C CE  . LYS A 1 60  ? 32.51046 -53.43612 9.13237  1.000 114.83754 ? 60  LYS A CE  1 
ATOM   447  N NZ  . LYS A 1 60  ? 33.51085 -54.20501 8.33961  1.000 120.97213 ? 60  LYS A NZ  1 
ATOM   448  N N   . PRO A 1 61  ? 30.94032 -49.31964 11.97791 1.000 84.24539  ? 61  PRO A N   1 
ATOM   449  C CA  . PRO A 1 61  ? 31.84877 -49.28719 13.12981 1.000 86.79317  ? 61  PRO A CA  1 
ATOM   450  C C   . PRO A 1 61  ? 33.11970 -50.06592 12.83589 1.000 84.84841  ? 61  PRO A C   1 
ATOM   451  O O   . PRO A 1 61  ? 33.10502 -51.08889 12.14722 1.000 96.88889  ? 61  PRO A O   1 
ATOM   452  C CB  . PRO A 1 61  ? 31.03430 -49.94708 14.25115 1.000 82.61768  ? 61  PRO A CB  1 
ATOM   453  C CG  . PRO A 1 61  ? 29.60869 -49.85888 13.80025 1.000 85.61366  ? 61  PRO A CG  1 
ATOM   454  C CD  . PRO A 1 61  ? 29.64963 -49.94636 12.30545 1.000 85.06770  ? 61  PRO A CD  1 
ATOM   455  N N   . LEU A 1 62  ? 34.23149 -49.56721 13.36793 1.000 83.92911  ? 62  LEU A N   1 
ATOM   456  C CA  . LEU A 1 62  ? 35.55472 -50.06453 13.01962 1.000 86.13684  ? 62  LEU A CA  1 
ATOM   457  C C   . LEU A 1 62  ? 36.23477 -50.66419 14.24014 1.000 86.28029  ? 62  LEU A C   1 
ATOM   458  O O   . LEU A 1 62  ? 36.26188 -50.04640 15.31010 1.000 99.26538  ? 62  LEU A O   1 
ATOM   459  C CB  . LEU A 1 62  ? 36.41884 -48.94497 12.43574 1.000 86.06818  ? 62  LEU A CB  1 
ATOM   460  C CG  . LEU A 1 62  ? 35.80812 -48.20402 11.24684 1.000 103.67001 ? 62  LEU A CG  1 
ATOM   461  C CD1 . LEU A 1 62  ? 36.74858 -47.11500 10.76042 1.000 91.59418  ? 62  LEU A CD1 1 
ATOM   462  C CD2 . LEU A 1 62  ? 35.47394 -49.17669 10.12801 1.000 88.89309  ? 62  LEU A CD2 1 
ATOM   463  N N   . ALA A 1 63  ? 36.78673 -51.86013 14.06965 1.000 89.13308  ? 63  ALA A N   1 
ATOM   464  C CA  . ALA A 1 63  ? 37.60722 -52.51300 15.07648 1.000 96.69810  ? 63  ALA A CA  1 
ATOM   465  C C   . ALA A 1 63  ? 39.08145 -52.38467 14.71154 1.000 101.84344 ? 63  ALA A C   1 
ATOM   466  O O   . ALA A 1 63  ? 39.44260 -52.15189 13.55562 1.000 101.88975 ? 63  ALA A O   1 
ATOM   467  C CB  . ALA A 1 63  ? 37.22820 -53.98961 15.21687 1.000 92.68153  ? 63  ALA A CB  1 
ATOM   468  N N   . GLY A 1 64  ? 39.93573 -52.53975 15.71946 1.000 92.68320  ? 64  GLY A N   1 
ATOM   469  C CA  . GLY A 1 64  ? 41.36613 -52.46049 15.52093 1.000 95.15021  ? 64  GLY A CA  1 
ATOM   470  C C   . GLY A 1 64  ? 41.97781 -51.09457 15.74119 1.000 95.82221  ? 64  GLY A C   1 
ATOM   471  O O   . GLY A 1 64  ? 43.20497 -50.96227 15.64676 1.000 110.42703 ? 64  GLY A O   1 
ATOM   472  N N   . ALA A 1 65  ? 41.17187 -50.07564 16.02412 1.000 92.24891  ? 65  ALA A N   1 
ATOM   473  C CA  . ALA A 1 65  ? 41.70085 -48.75342 16.32512 1.000 89.36300  ? 65  ALA A CA  1 
ATOM   474  C C   . ALA A 1 65  ? 42.15715 -48.69818 17.77743 1.000 88.84971  ? 65  ALA A C   1 
ATOM   475  O O   . ALA A 1 65  ? 41.44202 -49.14371 18.68085 1.000 89.24938  ? 65  ALA A O   1 
ATOM   476  C CB  . ALA A 1 65  ? 40.64754 -47.68074 16.05559 1.000 86.31506  ? 65  ALA A CB  1 
ATOM   477  N N   . VAL A 1 66  ? 43.35028 -48.15587 18.00085 1.000 75.09138  ? 66  VAL A N   1 
ATOM   478  C CA  . VAL A 1 66  ? 43.94409 -48.06949 19.32940 1.000 82.57787  ? 66  VAL A CA  1 
ATOM   479  C C   . VAL A 1 66  ? 43.86258 -46.62608 19.80433 1.000 83.54471  ? 66  VAL A C   1 
ATOM   480  O O   . VAL A 1 66  ? 44.27427 -45.70463 19.08857 1.000 77.58293  ? 66  VAL A O   1 
ATOM   481  C CB  . VAL A 1 66  ? 45.39842 -48.57049 19.33348 1.000 81.26348  ? 66  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 66  ? 45.95287 -48.56186 20.74722 1.000 68.10316  ? 66  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 66  ? 45.47945 -49.96531 18.73233 1.000 84.62304  ? 66  VAL A CG2 1 
ATOM   484  N N   . PHE A 1 67  ? 43.32899 -46.43185 21.00723 1.000 71.42057  ? 67  PHE A N   1 
ATOM   485  C CA  . PHE A 1 67  ? 43.22116 -45.11927 21.62097 1.000 71.86696  ? 67  PHE A CA  1 
ATOM   486  C C   . PHE A 1 67  ? 43.92544 -45.10947 22.97025 1.000 70.08497  ? 67  PHE A C   1 
ATOM   487  O O   . PHE A 1 67  ? 44.16043 -46.15263 23.58604 1.000 84.79101  ? 67  PHE A O   1 
ATOM   488  C CB  . PHE A 1 67  ? 41.75857 -44.70349 21.81480 1.000 65.11974  ? 67  PHE A CB  1 
ATOM   489  C CG  . PHE A 1 67  ? 41.03161 -44.40927 20.53453 1.000 69.47272  ? 67  PHE A CG  1 
ATOM   490  C CD1 . PHE A 1 67  ? 40.42225 -45.42517 19.82030 1.000 69.67509  ? 67  PHE A CD1 1 
ATOM   491  C CD2 . PHE A 1 67  ? 40.94372 -43.11296 20.05556 1.000 60.40594  ? 67  PHE A CD2 1 
ATOM   492  C CE1 . PHE A 1 67  ? 39.74766 -45.15709 18.64551 1.000 73.14443  ? 67  PHE A CE1 1 
ATOM   493  C CE2 . PHE A 1 67  ? 40.27138 -42.83688 18.88293 1.000 74.12383  ? 67  PHE A CE2 1 
ATOM   494  C CZ  . PHE A 1 67  ? 39.67176 -43.86073 18.17560 1.000 88.67252  ? 67  PHE A CZ  1 
ATOM   495  N N   . ARG A 1 68  ? 44.25719 -43.90499 23.42294 1.000 71.78914  ? 68  ARG A N   1 
ATOM   496  C CA  . ARG A 1 68  ? 44.79769 -43.68307 24.75449 1.000 68.53937  ? 68  ARG A CA  1 
ATOM   497  C C   . ARG A 1 68  ? 44.29754 -42.33789 25.25450 1.000 70.99067  ? 68  ARG A C   1 
ATOM   498  O O   . ARG A 1 68  ? 44.27680 -41.35806 24.50379 1.000 63.48088  ? 68  ARG A O   1 
ATOM   499  C CB  . ARG A 1 68  ? 46.33238 -43.71952 24.76274 1.000 67.13946  ? 68  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 68  ? 46.95885 -43.27135 26.07539 1.000 84.62717  ? 68  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 68  ? 48.42491 -43.66424 26.15797 1.000 85.02367  ? 68  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 68  ? 48.59958 -45.03280 26.63065 1.000 87.18660  ? 68  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 68  ? 49.73509 -45.71319 26.55180 1.000 78.56290  ? 68  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 68  ? 50.81440 -45.19236 25.99251 1.000 94.24046  ? 68  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 68  ? 49.78644 -46.95011 27.03914 1.000 96.34127  ? 68  ARG A NH2 1 
ATOM   506  N N   . LEU A 1 69  ? 43.88097 -42.29838 26.51621 1.000 74.98213  ? 69  LEU A N   1 
ATOM   507  C CA  . LEU A 1 69  ? 43.33947 -41.09344 27.13078 1.000 58.05557  ? 69  LEU A CA  1 
ATOM   508  C C   . LEU A 1 69  ? 44.38466 -40.49899 28.06555 1.000 60.55942  ? 69  LEU A C   1 
ATOM   509  O O   . LEU A 1 69  ? 44.83029 -41.16403 29.00716 1.000 68.91088  ? 69  LEU A O   1 
ATOM   510  C CB  . LEU A 1 69  ? 42.05038 -41.40277 27.89025 1.000 63.30107  ? 69  LEU A CB  1 
ATOM   511  C CG  . LEU A 1 69  ? 41.29775 -40.19436 28.44784 1.000 73.09195  ? 69  LEU A CG  1 
ATOM   512  C CD1 . LEU A 1 69  ? 40.81240 -39.30465 27.31692 1.000 62.07289  ? 69  LEU A CD1 1 
ATOM   513  C CD2 . LEU A 1 69  ? 40.13781 -40.63376 29.32810 1.000 73.53687  ? 69  LEU A CD2 1 
ATOM   514  N N   . TYR A 1 70  ? 44.77505 -39.25522 27.80240 1.000 65.32702  ? 70  TYR A N   1 
ATOM   515  C CA  . TYR A 1 70  ? 45.71794 -38.53278 28.64416 1.000 51.78675  ? 70  TYR A CA  1 
ATOM   516  C C   . TYR A 1 70  ? 44.96536 -37.55893 29.54106 1.000 68.80988  ? 70  TYR A C   1 
ATOM   517  O O   . TYR A 1 70  ? 44.01776 -36.89949 29.10346 1.000 62.46842  ? 70  TYR A O   1 
ATOM   518  C CB  . TYR A 1 70  ? 46.74459 -37.77447 27.80159 1.000 52.78186  ? 70  TYR A CB  1 
ATOM   519  C CG  . TYR A 1 70  ? 47.70861 -38.66146 27.04715 1.000 77.38884  ? 70  TYR A CG  1 
ATOM   520  C CD1 . TYR A 1 70  ? 47.36257 -39.21150 25.81792 1.000 65.97243  ? 70  TYR A CD1 1 
ATOM   521  C CD2 . TYR A 1 70  ? 48.96835 -38.94166 27.55853 1.000 51.01145  ? 70  TYR A CD2 1 
ATOM   522  C CE1 . TYR A 1 70  ? 48.24307 -40.02036 25.12390 1.000 64.73206  ? 70  TYR A CE1 1 
ATOM   523  C CE2 . TYR A 1 70  ? 49.85618 -39.74880 26.87142 1.000 74.23441  ? 70  TYR A CE2 1 
ATOM   524  C CZ  . TYR A 1 70  ? 49.48811 -40.28533 25.65467 1.000 71.08153  ? 70  TYR A CZ  1 
ATOM   525  O OH  . TYR A 1 70  ? 50.36684 -41.08951 24.96527 1.000 91.84428  ? 70  TYR A OH  1 
ATOM   526  N N   . ARG A 1 71  ? 45.39162 -37.47571 30.79824 1.000 65.93598  ? 71  ARG A N   1 
ATOM   527  C CA  . ARG A 1 71  ? 44.77094 -36.61143 31.79266 1.000 53.30135  ? 71  ARG A CA  1 
ATOM   528  C C   . ARG A 1 71  ? 45.80037 -35.60786 32.28792 1.000 53.22870  ? 71  ARG A C   1 
ATOM   529  O O   . ARG A 1 71  ? 46.89939 -35.99408 32.70065 1.000 55.79760  ? 71  ARG A O   1 
ATOM   530  C CB  . ARG A 1 71  ? 44.21439 -37.43163 32.96051 1.000 68.62165  ? 71  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 71  ? 43.56677 -36.60830 34.06217 1.000 83.79220  ? 71  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 71  ? 43.03216 -37.50650 35.16923 1.000 85.10835  ? 71  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 71  ? 42.47995 -36.74238 36.28102 1.000 96.19960  ? 71  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 71  ? 43.14332 -36.44838 37.39077 1.000 101.82966 ? 71  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 71  ? 44.38866 -36.85332 37.57979 1.000 104.20054 ? 71  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 71  ? 42.54144 -35.73121 38.33522 1.000 100.46463 ? 71  ARG A NH2 1 
ATOM   537  N N   . PHE A 1 72  ? 45.44491 -34.32575 32.24128 1.000 51.54167  ? 72  PHE A N   1 
ATOM   538  C CA  . PHE A 1 72  ? 46.32503 -33.24252 32.65970 1.000 52.89620  ? 72  PHE A CA  1 
ATOM   539  C C   . PHE A 1 72  ? 45.65629 -32.43790 33.76486 1.000 69.51890  ? 72  PHE A C   1 
ATOM   540  O O   . PHE A 1 72  ? 44.47365 -32.09659 33.65873 1.000 75.18684  ? 72  PHE A O   1 
ATOM   541  C CB  . PHE A 1 72  ? 46.66698 -32.32283 31.48526 1.000 53.41662  ? 72  PHE A CB  1 
ATOM   542  C CG  . PHE A 1 72  ? 47.40003 -33.00694 30.36625 1.000 67.61804  ? 72  PHE A CG  1 
ATOM   543  C CD1 . PHE A 1 72  ? 48.77951 -33.12135 30.39474 1.000 50.70054  ? 72  PHE A CD1 1 
ATOM   544  C CD2 . PHE A 1 72  ? 46.71187 -33.52166 29.27780 1.000 68.22198  ? 72  PHE A CD2 1 
ATOM   545  C CE1 . PHE A 1 72  ? 49.46013 -33.74540 29.36513 1.000 65.65271  ? 72  PHE A CE1 1 
ATOM   546  C CE2 . PHE A 1 72  ? 47.38669 -34.14719 28.24465 1.000 62.09274  ? 72  PHE A CE2 1 
ATOM   547  C CZ  . PHE A 1 72  ? 48.76320 -34.25907 28.28931 1.000 61.14360  ? 72  PHE A CZ  1 
ATOM   548  N N   . LEU A 1 73  ? 46.41293 -32.12942 34.81563 1.000 64.17849  ? 73  LEU A N   1 
ATOM   549  C CA  . LEU A 1 73  ? 45.95217 -31.26416 35.89546 1.000 55.65735  ? 73  LEU A CA  1 
ATOM   550  C C   . LEU A 1 73  ? 46.70190 -29.94272 35.81453 1.000 62.65065  ? 73  LEU A C   1 
ATOM   551  O O   . LEU A 1 73  ? 47.93735 -29.92215 35.86098 1.000 49.63605  ? 73  LEU A O   1 
ATOM   552  C CB  . LEU A 1 73  ? 46.15963 -31.91864 37.26164 1.000 62.94365  ? 73  LEU A CB  1 
ATOM   553  C CG  . LEU A 1 73  ? 45.03541 -32.83586 37.74561 1.000 76.15577  ? 73  LEU A CG  1 
ATOM   554  C CD1 . LEU A 1 73  ? 45.28247 -33.30000 39.17293 1.000 93.77509  ? 73  LEU A CD1 1 
ATOM   555  C CD2 . LEU A 1 73  ? 43.69911 -32.12425 37.64096 1.000 75.77684  ? 73  LEU A CD2 1 
ATOM   556  N N   . PHE A 1 74  ? 45.95703 -28.84790 35.69492 1.000 52.31793  ? 74  PHE A N   1 
ATOM   557  C CA  . PHE A 1 74  ? 46.53038 -27.51632 35.57863 1.000 62.59871  ? 74  PHE A CA  1 
ATOM   558  C C   . PHE A 1 74  ? 46.05846 -26.63623 36.72566 1.000 75.32887  ? 74  PHE A C   1 
ATOM   559  O O   . PHE A 1 74  ? 44.90291 -26.72231 37.15322 1.000 74.21306  ? 74  PHE A O   1 
ATOM   560  C CB  . PHE A 1 74  ? 46.14288 -26.84286 34.25558 1.000 50.84752  ? 74  PHE A CB  1 
ATOM   561  C CG  . PHE A 1 74  ? 46.52962 -27.61904 33.03311 1.000 75.24869  ? 74  PHE A CG  1 
ATOM   562  C CD1 . PHE A 1 74  ? 47.85799 -27.73252 32.65593 1.000 102.16191 ? 74  PHE A CD1 1 
ATOM   563  C CD2 . PHE A 1 74  ? 45.56097 -28.20938 32.23951 1.000 92.27257  ? 74  PHE A CD2 1 
ATOM   564  C CE1 . PHE A 1 74  ? 48.21473 -28.43774 31.51767 1.000 107.99403 ? 74  PHE A CE1 1 
ATOM   565  C CE2 . PHE A 1 74  ? 45.90984 -28.91446 31.10022 1.000 96.46821  ? 74  PHE A CE2 1 
ATOM   566  C CZ  . PHE A 1 74  ? 47.23875 -29.02694 30.73862 1.000 80.24163  ? 74  PHE A CZ  1 
ATOM   567  N N   . GLU A 1 75  ? 46.95517 -25.78177 37.20985 1.000 71.62373  ? 75  GLU A N   1 
ATOM   568  C CA  . GLU A 1 75  ? 46.58015 -24.66640 38.06836 1.000 75.30228  ? 75  GLU A CA  1 
ATOM   569  C C   . GLU A 1 75  ? 46.28289 -23.46969 37.17376 1.000 79.21043  ? 75  GLU A C   1 
ATOM   570  O O   . GLU A 1 75  ? 47.16657 -22.99764 36.45195 1.000 79.30649  ? 75  GLU A O   1 
ATOM   571  C CB  . GLU A 1 75  ? 47.69129 -24.33792 39.06443 1.000 59.45755  ? 75  GLU A CB  1 
ATOM   572  C CG  . GLU A 1 75  ? 47.40085 -23.12298 39.93469 1.000 81.45934  ? 75  GLU A CG  1 
ATOM   573  C CD  . GLU A 1 75  ? 48.56146 -22.76061 40.84489 1.000 104.49206 ? 75  GLU A CD  1 
ATOM   574  O OE1 . GLU A 1 75  ? 49.55350 -23.51879 40.88181 1.000 100.22968 ? 75  GLU A OE1 1 
ATOM   575  O OE2 . GLU A 1 75  ? 48.48336 -21.71406 41.52346 1.000 98.49963  ? 75  GLU A OE2 1 
ATOM   576  N N   . GLU A 1 76  ? 45.04591 -22.98660 37.21318 1.000 76.35656  ? 76  GLU A N   1 
ATOM   577  C CA  A GLU A 1 76  ? 44.60373 -21.90026 36.34989 0.504 72.57370  ? 76  GLU A CA  1 
ATOM   578  C CA  B GLU A 1 76  ? 44.59156 -21.90375 36.35150 0.496 72.45808  ? 76  GLU A CA  1 
ATOM   579  C C   . GLU A 1 76  ? 44.47669 -20.61293 37.15196 1.000 86.32070  ? 76  GLU A C   1 
ATOM   580  O O   . GLU A 1 76  ? 43.85444 -20.59573 38.21972 1.000 93.24733  ? 76  GLU A O   1 
ATOM   581  C CB  A GLU A 1 76  ? 43.27154 -22.23603 35.67609 0.504 79.61574  ? 76  GLU A CB  1 
ATOM   582  C CB  B GLU A 1 76  ? 43.24296 -22.25256 35.72019 0.496 80.91851  ? 76  GLU A CB  1 
ATOM   583  C CG  A GLU A 1 76  ? 43.36849 -23.32294 34.61915 0.504 86.82271  ? 76  GLU A CG  1 
ATOM   584  C CG  B GLU A 1 76  ? 42.64722 -21.14965 34.86595 0.496 100.14526 ? 76  GLU A CG  1 
ATOM   585  C CD  A GLU A 1 76  ? 42.31481 -23.17793 33.53636 0.504 103.14356 ? 76  GLU A CD  1 
ATOM   586  C CD  B GLU A 1 76  ? 41.20228 -21.41965 34.49707 0.496 110.35367 ? 76  GLU A CD  1 
ATOM   587  O OE1 A GLU A 1 76  ? 41.74364 -22.07499 33.40336 0.504 113.38428 ? 76  GLU A OE1 1 
ATOM   588  O OE1 B GLU A 1 76  ? 40.54847 -22.21868 35.20064 0.496 87.12891  ? 76  GLU A OE1 1 
ATOM   589  O OE2 A GLU A 1 76  ? 42.05858 -24.16449 32.81569 0.504 97.96617  ? 76  GLU A OE2 1 
ATOM   590  O OE2 B GLU A 1 76  ? 40.72095 -20.83597 33.50323 0.496 102.42023 ? 76  GLU A OE2 1 
ATOM   591  N N   . ASN A 1 77  ? 45.07540 -19.53974 36.63149 1.000 82.62891  ? 77  ASN A N   1 
ATOM   592  C CA  . ASN A 1 77  ? 45.00847 -18.19478 37.20441 1.000 88.92103  ? 77  ASN A CA  1 
ATOM   593  C C   . ASN A 1 77  ? 45.49244 -18.13526 38.65055 1.000 90.03076  ? 77  ASN A C   1 
ATOM   594  O O   . ASN A 1 77  ? 45.20129 -17.16889 39.36245 1.000 105.23158 ? 77  ASN A O   1 
ATOM   595  C CB  . ASN A 1 77  ? 43.58817 -17.62480 37.10569 1.000 102.75883 ? 77  ASN A CB  1 
ATOM   596  C CG  . ASN A 1 77  ? 43.08586 -17.55622 35.67660 1.000 118.00823 ? 77  ASN A CG  1 
ATOM   597  O OD1 . ASN A 1 77  ? 41.99899 -18.04236 35.36295 1.000 116.73019 ? 77  ASN A OD1 1 
ATOM   598  N ND2 . ASN A 1 77  ? 43.87955 -16.95211 34.79993 1.000 132.50431 ? 77  ASN A ND2 1 
ATOM   599  N N   . GLY A 1 78  ? 46.23863 -19.14044 39.10156 1.000 98.02740  ? 78  GLY A N   1 
ATOM   600  C CA  . GLY A 1 78  ? 46.66221 -19.18073 40.49071 1.000 87.63545  ? 78  GLY A CA  1 
ATOM   601  C C   . GLY A 1 78  ? 45.51754 -19.26846 41.47341 1.000 88.52988  ? 78  GLY A C   1 
ATOM   602  O O   . GLY A 1 78  ? 45.65740 -18.83448 42.62169 1.000 106.27156 ? 78  GLY A O   1 
ATOM   603  N N   . GLU A 1 79  ? 44.37620 -19.80995 41.04644 1.000 72.02627  ? 79  GLU A N   1 
ATOM   604  C CA  . GLU A 1 79  ? 43.19678 -19.92245 41.89926 1.000 82.65919  ? 79  GLU A CA  1 
ATOM   605  C C   . GLU A 1 79  ? 42.46473 -21.25202 41.77994 1.000 93.97991  ? 79  GLU A C   1 
ATOM   606  O O   . GLU A 1 79  ? 41.86926 -21.68941 42.76960 1.000 78.20607  ? 79  GLU A O   1 
ATOM   607  C CB  . GLU A 1 79  ? 42.20437 -18.79191 41.59320 1.000 92.76905  ? 79  GLU A CB  1 
ATOM   608  C CG  . GLU A 1 79  ? 42.75141 -17.38811 41.78547 1.000 135.19255 ? 79  GLU A CG  1 
ATOM   609  C CD  . GLU A 1 79  ? 41.76309 -16.32564 41.35205 1.000 155.93836 ? 79  GLU A CD  1 
ATOM   610  O OE1 . GLU A 1 79  ? 40.59512 -16.67919 41.08625 1.000 154.80542 ? 79  GLU A OE1 1 
ATOM   611  O OE2 . GLU A 1 79  ? 42.15186 -15.14142 41.27131 1.000 170.57356 ? 79  GLU A OE2 1 
ATOM   612  N N   . PHE A 1 80  ? 42.47719 -21.91040 40.62376 1.000 73.86353  ? 80  PHE A N   1 
ATOM   613  C CA  . PHE A 1 80  ? 41.70518 -23.12152 40.40129 1.000 76.10555  ? 80  PHE A CA  1 
ATOM   614  C C   . PHE A 1 80  ? 42.61806 -24.26186 39.97240 1.000 70.22993  ? 80  PHE A C   1 
ATOM   615  O O   . PHE A 1 80  ? 43.76703 -24.05315 39.57461 1.000 80.45542  ? 80  PHE A O   1 
ATOM   616  C CB  . PHE A 1 80  ? 40.62285 -22.90235 39.33387 1.000 70.80567  ? 80  PHE A CB  1 
ATOM   617  C CG  . PHE A 1 80  ? 39.83058 -21.64139 39.52212 1.000 76.33192  ? 80  PHE A CG  1 
ATOM   618  C CD1 . PHE A 1 80  ? 38.84975 -21.56154 40.49677 1.000 95.48949  ? 80  PHE A CD1 1 
ATOM   619  C CD2 . PHE A 1 80  ? 40.06210 -20.53730 38.71866 1.000 97.32768  ? 80  PHE A CD2 1 
ATOM   620  C CE1 . PHE A 1 80  ? 38.11825 -20.40154 40.67051 1.000 89.83157  ? 80  PHE A CE1 1 
ATOM   621  C CE2 . PHE A 1 80  ? 39.33398 -19.37522 38.88650 1.000 103.58435 ? 80  PHE A CE2 1 
ATOM   622  C CZ  . PHE A 1 80  ? 38.36095 -19.30712 39.86348 1.000 97.84053  ? 80  PHE A CZ  1 
ATOM   623  N N   . VAL A 1 81  ? 42.08422 -25.47767 40.05873 1.000 83.25598  ? 81  VAL A N   1 
ATOM   624  C CA  . VAL A 1 81  ? 42.73241 -26.67734 39.54144 1.000 78.83775  ? 81  VAL A CA  1 
ATOM   625  C C   . VAL A 1 81  ? 41.85920 -27.20376 38.41273 1.000 83.23962  ? 81  VAL A C   1 
ATOM   626  O O   . VAL A 1 81  ? 40.74112 -27.67687 38.65396 1.000 93.02563  ? 81  VAL A O   1 
ATOM   627  C CB  . VAL A 1 81  ? 42.93281 -27.74722 40.62250 1.000 71.39417  ? 81  VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 81  ? 43.43629 -29.03993 39.99611 1.000 88.81778  ? 81  VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 81  ? 43.90357 -27.26167 41.67819 1.000 80.45057  ? 81  VAL A CG2 1 
ATOM   630  N N   . ALA A 1 82  ? 42.36073 -27.12371 37.18498 1.000 75.54625  ? 82  ALA A N   1 
ATOM   631  C CA  . ALA A 1 82  ? 41.62986 -27.58214 36.01312 1.000 75.62904  ? 82  ALA A CA  1 
ATOM   632  C C   . ALA A 1 82  ? 42.05251 -28.99871 35.64986 1.000 69.21239  ? 82  ALA A C   1 
ATOM   633  O O   . ALA A 1 82  ? 43.23971 -29.33499 35.68850 1.000 65.18485  ? 82  ALA A O   1 
ATOM   634  C CB  . ALA A 1 82  ? 41.85934 -26.65015 34.82290 1.000 81.30984  ? 82  ALA A CB  1 
ATOM   635  N N   . GLU A 1 83  ? 41.07187 -29.82521 35.29933 1.000 83.36079  ? 83  GLU A N   1 
ATOM   636  C CA  . GLU A 1 83  ? 41.29766 -31.20443 34.88078 1.000 87.35480  ? 83  GLU A CA  1 
ATOM   637  C C   . GLU A 1 83  ? 40.88687 -31.31792 33.41807 1.000 79.35003  ? 83  GLU A C   1 
ATOM   638  O O   . GLU A 1 83  ? 39.69541 -31.25754 33.09647 1.000 92.17626  ? 83  GLU A O   1 
ATOM   639  C CB  . GLU A 1 83  ? 40.50948 -32.17405 35.75831 1.000 78.75817  ? 83  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 83  ? 40.82211 -33.63973 35.52146 1.000 86.51391  ? 83  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 83  ? 39.99036 -34.55200 36.40110 1.000 120.72311 ? 83  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 83  ? 39.06441 -34.04733 37.07122 1.000 136.16006 ? 83  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 83  ? 40.26151 -35.77067 36.42524 1.000 124.86185 ? 83  GLU A OE2 1 
ATOM   644  N N   . ARG A 1 84  ? 41.87060 -31.47896 32.53623 1.000 77.88485  ? 84  ARG A N   1 
ATOM   645  C CA  . ARG A 1 84  ? 41.64661 -31.49810 31.09570 1.000 70.47314  ? 84  ARG A CA  1 
ATOM   646  C C   . ARG A 1 84  ? 42.07876 -32.84949 30.54314 1.000 74.87350  ? 84  ARG A C   1 
ATOM   647  O O   . ARG A 1 84  ? 43.23706 -33.24824 30.70618 1.000 73.39844  ? 84  ARG A O   1 
ATOM   648  C CB  . ARG A 1 84  ? 42.41360 -30.36318 30.41165 1.000 75.51874  ? 84  ARG A CB  1 
ATOM   649  C CG  . ARG A 1 84  ? 42.25874 -29.00600 31.09425 1.000 93.37356  ? 84  ARG A CG  1 
ATOM   650  C CD  . ARG A 1 84  ? 41.18409 -28.14294 30.44183 1.000 104.29107 ? 84  ARG A CD  1 
ATOM   651  N NE  . ARG A 1 84  ? 40.90182 -26.94761 31.22973 1.000 97.63374  ? 84  ARG A NE  1 
ATOM   652  C CZ  . ARG A 1 84  ? 40.18372 -25.91479 30.80783 1.000 116.41133 ? 84  ARG A CZ  1 
ATOM   653  N NH1 . ARG A 1 84  ? 39.67480 -25.87687 29.58767 1.000 116.89207 ? 84  ARG A NH1 1 
ATOM   654  N NH2 . ARG A 1 84  ? 39.97545 -24.89043 31.63022 1.000 122.65490 ? 84  ARG A NH2 1 
ATOM   655  N N   . TYR A 1 85  ? 41.14963 -33.55054 29.89885 1.000 78.04098  ? 85  TYR A N   1 
ATOM   656  C CA  . TYR A 1 85  ? 41.42486 -34.82173 29.24543 1.000 70.36411  ? 85  TYR A CA  1 
ATOM   657  C C   . TYR A 1 85  ? 41.63717 -34.60719 27.75163 1.000 72.67272  ? 85  TYR A C   1 
ATOM   658  O O   . TYR A 1 85  ? 41.05930 -33.69871 27.14891 1.000 80.88833  ? 85  TYR A O   1 
ATOM   659  C CB  . TYR A 1 85  ? 40.27723 -35.81368 29.45752 1.000 72.96999  ? 85  TYR A CB  1 
ATOM   660  C CG  . TYR A 1 85  ? 40.09188 -36.28978 30.88225 1.000 67.18715  ? 85  TYR A CG  1 
ATOM   661  C CD1 . TYR A 1 85  ? 39.34448 -35.55148 31.79170 1.000 83.13353  ? 85  TYR A CD1 1 
ATOM   662  C CD2 . TYR A 1 85  ? 40.64400 -37.49040 31.31058 1.000 75.06829  ? 85  TYR A CD2 1 
ATOM   663  C CE1 . TYR A 1 85  ? 39.16548 -35.98847 33.09080 1.000 76.19684  ? 85  TYR A CE1 1 
ATOM   664  C CE2 . TYR A 1 85  ? 40.46973 -37.93487 32.60765 1.000 76.95644  ? 85  TYR A CE2 1 
ATOM   665  C CZ  . TYR A 1 85  ? 39.73005 -37.18019 33.49281 1.000 87.47711  ? 85  TYR A CZ  1 
ATOM   666  O OH  . TYR A 1 85  ? 39.55401 -37.61925 34.78493 1.000 103.38909 ? 85  TYR A OH  1 
ATOM   667  N N   . VAL A 1 86  ? 42.47354 -35.45666 27.15526 1.000 67.76117  ? 86  VAL A N   1 
ATOM   668  C CA  . VAL A 1 86  ? 42.71887 -35.42995 25.71586 1.000 56.76578  ? 86  VAL A CA  1 
ATOM   669  C C   . VAL A 1 86  ? 42.71325 -36.86218 25.19963 1.000 66.00974  ? 86  VAL A C   1 
ATOM   670  O O   . VAL A 1 86  ? 43.51892 -37.68843 25.64246 1.000 64.32071  ? 86  VAL A O   1 
ATOM   671  C CB  . VAL A 1 86  ? 44.04575 -34.74138 25.35207 1.000 64.64017  ? 86  VAL A CB  1 
ATOM   672  C CG1 . VAL A 1 86  ? 44.30162 -34.85865 23.85583 1.000 74.50949  ? 86  VAL A CG1 1 
ATOM   673  C CG2 . VAL A 1 86  ? 44.02005 -33.28184 25.77324 1.000 65.36608  ? 86  VAL A CG2 1 
ATOM   674  N N   . LEU A 1 87  ? 41.81300 -37.15479 24.26537 1.000 79.26057  ? 87  LEU A N   1 
ATOM   675  C CA  . LEU A 1 87  ? 41.75103 -38.45991 23.62384 1.000 63.87805  ? 87  LEU A CA  1 
ATOM   676  C C   . LEU A 1 87  ? 42.68477 -38.47948 22.42042 1.000 72.91249  ? 87  LEU A C   1 
ATOM   677  O O   . LEU A 1 87  ? 42.62914 -37.58643 21.56881 1.000 73.04384  ? 87  LEU A O   1 
ATOM   678  C CB  . LEU A 1 87  ? 40.31983 -38.77902 23.19222 1.000 75.32220  ? 87  LEU A CB  1 
ATOM   679  C CG  . LEU A 1 87  ? 40.10028 -40.11673 22.48649 1.000 72.34160  ? 87  LEU A CG  1 
ATOM   680  C CD1 . LEU A 1 87  ? 40.47756 -41.26965 23.40264 1.000 64.17960  ? 87  LEU A CD1 1 
ATOM   681  C CD2 . LEU A 1 87  ? 38.65836 -40.24391 22.01823 1.000 69.88769  ? 87  LEU A CD2 1 
ATOM   682  N N   . VAL A 1 88  ? 43.54000 -39.49628 22.35485 1.000 64.30961  ? 88  VAL A N   1 
ATOM   683  C CA  . VAL A 1 88  ? 44.53547 -39.63403 21.29868 1.000 71.08099  ? 88  VAL A CA  1 
ATOM   684  C C   . VAL A 1 88  ? 44.32359 -40.97354 20.60850 1.000 80.06374  ? 88  VAL A C   1 
ATOM   685  O O   . VAL A 1 88  ? 44.15636 -42.00053 21.27671 1.000 81.69367  ? 88  VAL A O   1 
ATOM   686  C CB  . VAL A 1 88  ? 45.96827 -39.52839 21.85405 1.000 78.92712  ? 88  VAL A CB  1 
ATOM   687  C CG1 . VAL A 1 88  ? 46.98731 -39.83780 20.76860 1.000 65.52098  ? 88  VAL A CG1 1 
ATOM   688  C CG2 . VAL A 1 88  ? 46.21200 -38.14508 22.44129 1.000 64.08045  ? 88  VAL A CG2 1 
ATOM   689  N N   . GLU A 1 89  ? 44.32735 -40.96195 19.27608 1.000 89.57248  ? 89  GLU A N   1 
ATOM   690  C CA  . GLU A 1 89  ? 44.25390 -42.18795 18.48757 1.000 69.66654  ? 89  GLU A CA  1 
ATOM   691  C C   . GLU A 1 89  ? 45.67404 -42.66768 18.21593 1.000 65.57313  ? 89  GLU A C   1 
ATOM   692  O O   . GLU A 1 89  ? 46.42939 -42.01797 17.48466 1.000 71.76918  ? 89  GLU A O   1 
ATOM   693  C CB  . GLU A 1 89  ? 43.48954 -41.96278 17.18594 1.000 72.65663  ? 89  GLU A CB  1 
ATOM   694  C CG  . GLU A 1 89  ? 43.40742 -43.20085 16.30853 1.000 82.84508  ? 89  GLU A CG  1 
ATOM   695  C CD  . GLU A 1 89  ? 42.27520 -43.13485 15.30232 1.000 96.82557  ? 89  GLU A CD  1 
ATOM   696  O OE1 . GLU A 1 89  ? 41.53748 -42.12827 15.29462 1.000 73.77022  ? 89  GLU A OE1 1 
ATOM   697  O OE2 . GLU A 1 89  ? 42.11902 -44.09526 14.52013 1.000 100.30104 ? 89  GLU A OE2 1 
ATOM   698  N N   . VAL A 1 90  ? 46.03469 -43.80716 18.80544 1.000 78.91889  ? 90  VAL A N   1 
ATOM   699  C CA  . VAL A 1 90  ? 47.39808 -44.31075 18.68650 1.000 83.05809  ? 90  VAL A CA  1 
ATOM   700  C C   . VAL A 1 90  ? 47.61977 -44.96509 17.32957 1.000 76.88086  ? 90  VAL A C   1 
ATOM   701  O O   . VAL A 1 90  ? 48.65012 -44.74348 16.68372 1.000 98.20369  ? 90  VAL A O   1 
ATOM   702  C CB  . VAL A 1 90  ? 47.70337 -45.27988 19.84314 1.000 74.29525  ? 90  VAL A CB  1 
ATOM   703  C CG1 . VAL A 1 90  ? 49.10451 -45.85417 19.70371 1.000 73.76240  ? 90  VAL A CG1 1 
ATOM   704  C CG2 . VAL A 1 90  ? 47.54320 -44.57248 21.18052 1.000 69.57985  ? 90  VAL A CG2 1 
ATOM   705  N N   . ARG A 1 91  ? 46.66619 -45.77521 16.87309 1.000 90.20476  ? 91  ARG A N   1 
ATOM   706  C CA  A ARG A 1 91  ? 46.78433 -46.47940 15.60215 0.487 87.81995  ? 91  ARG A CA  1 
ATOM   707  C CA  B ARG A 1 91  ? 46.78676 -46.46411 15.59645 0.513 87.94059  ? 91  ARG A CA  1 
ATOM   708  C C   . ARG A 1 91  ? 45.42215 -46.55231 14.93313 1.000 93.33873  ? 91  ARG A C   1 
ATOM   709  O O   . ARG A 1 91  ? 44.43616 -46.93141 15.57210 1.000 86.59603  ? 91  ARG A O   1 
ATOM   710  C CB  A ARG A 1 91  ? 47.34252 -47.89470 15.79825 0.487 93.14033  ? 91  ARG A CB  1 
ATOM   711  C CB  B ARG A 1 91  ? 47.38348 -47.86578 15.77647 0.513 92.85597  ? 91  ARG A CB  1 
ATOM   712  C CG  A ARG A 1 91  ? 48.81457 -47.94671 16.16221 0.487 104.30445 ? 91  ARG A CG  1 
ATOM   713  C CG  B ARG A 1 91  ? 47.35034 -48.72052 14.52147 0.513 97.04432  ? 91  ARG A CG  1 
ATOM   714  C CD  A ARG A 1 91  ? 49.25816 -49.36770 16.46129 0.487 114.79411 ? 91  ARG A CD  1 
ATOM   715  C CD  B ARG A 1 91  ? 48.11526 -50.02021 14.70812 0.513 107.96135 ? 91  ARG A CD  1 
ATOM   716  N NE  A ARG A 1 91  ? 49.00779 -50.27058 15.34455 0.487 109.52103 ? 91  ARG A NE  1 
ATOM   717  N NE  B ARG A 1 91  ? 47.84629 -50.96244 13.62824 0.513 132.43213 ? 91  ARG A NE  1 
ATOM   718  C CZ  A ARG A 1 91  ? 49.33149 -51.55633 15.33727 0.487 122.95032 ? 91  ARG A CZ  1 
ATOM   719  C CZ  B ARG A 1 91  ? 48.53167 -52.07760 13.41616 0.513 134.91902 ? 91  ARG A CZ  1 
ATOM   720  N NH1 A ARG A 1 91  ? 49.93013 -52.12387 16.37159 0.487 111.42342 ? 91  ARG A NH1 1 
ATOM   721  N NH1 B ARG A 1 91  ? 49.55703 -52.41510 14.18086 0.513 144.45990 ? 91  ARG A NH1 1 
ATOM   722  N NH2 A ARG A 1 91  ? 49.04772 -52.29115 14.26565 0.487 143.76000 ? 91  ARG A NH2 1 
ATOM   723  N NH2 B ARG A 1 91  ? 48.18179 -52.87237 12.40890 0.513 106.05987 ? 91  ARG A NH2 1 
ATOM   724  N N   A SER A 1 92  ? 45.37046 -46.19088 13.65387 0.628 98.64141  ? 92  SER A N   1 
ATOM   725  N N   B SER A 1 92  ? 45.37508 -46.19869 13.65108 0.372 98.65424  ? 92  SER A N   1 
ATOM   726  C CA  A SER A 1 92  ? 44.14658 -46.32939 12.88923 0.628 90.18468  ? 92  SER A CA  1 
ATOM   727  C CA  B SER A 1 92  ? 44.16108 -46.32249 12.86636 0.372 90.25076  ? 92  SER A CA  1 
ATOM   728  C C   A SER A 1 92  ? 43.88182 -47.80440 12.60040 0.628 91.80257  ? 92  SER A C   1 
ATOM   729  C C   B SER A 1 92  ? 43.89236 -47.79476 12.55481 0.372 91.91380  ? 92  SER A C   1 
ATOM   730  O O   A SER A 1 92  ? 44.80180 -48.62636 12.62549 0.628 93.71784  ? 92  SER A O   1 
ATOM   731  O O   B SER A 1 92  ? 44.81945 -48.60813 12.52039 0.372 93.96879  ? 92  SER A O   1 
ATOM   732  C CB  A SER A 1 92  ? 44.24308 -45.54400 11.58391 0.628 92.87409  ? 92  SER A CB  1 
ATOM   733  C CB  B SER A 1 92  ? 44.29544 -45.51793 11.57493 0.372 92.94354  ? 92  SER A CB  1 
ATOM   734  O OG  A SER A 1 92  ? 45.18208 -46.13637 10.70369 0.628 96.79797  ? 92  SER A OG  1 
ATOM   735  O OG  B SER A 1 92  ? 43.03256 -45.17841 11.02805 0.372 102.18884 ? 92  SER A OG  1 
ATOM   736  N N   . PRO A 1 93  ? 42.62904 -48.16956 12.34087 1.000 91.19773  ? 93  PRO A N   1 
ATOM   737  C CA  . PRO A 1 93  ? 42.32924 -49.56320 11.99225 1.000 92.97274  ? 93  PRO A CA  1 
ATOM   738  C C   . PRO A 1 93  ? 42.98288 -49.96625 10.67782 1.000 97.36043  ? 93  PRO A C   1 
ATOM   739  O O   . PRO A 1 93  ? 43.18648 -49.14501 9.78003  1.000 99.85040  ? 93  PRO A O   1 
ATOM   740  C CB  . PRO A 1 93  ? 40.79955 -49.58413 11.88816 1.000 91.44363  ? 93  PRO A CB  1 
ATOM   741  C CG  . PRO A 1 93  ? 40.41100 -48.15431 11.67231 1.000 90.22670  ? 93  PRO A CG  1 
ATOM   742  C CD  . PRO A 1 93  ? 41.40219 -47.36107 12.45921 1.000 88.80099  ? 93  PRO A CD  1 
ATOM   743  N N   . GLU A 1 94  ? 43.31973 -51.25253 10.58011 1.000 115.85270 ? 94  GLU A N   1 
ATOM   744  C CA  . GLU A 1 94  ? 44.01388 -51.76144 9.40345  1.000 133.14434 ? 94  GLU A CA  1 
ATOM   745  C C   . GLU A 1 94  ? 43.18710 -51.53115 8.14535  1.000 105.84617 ? 94  GLU A C   1 
ATOM   746  O O   . GLU A 1 94  ? 41.96259 -51.68377 8.14615  1.000 104.37512 ? 94  GLU A O   1 
ATOM   747  C CB  . GLU A 1 94  ? 44.32034 -53.25125 9.56436  1.000 138.90236 ? 94  GLU A CB  1 
ATOM   748  C CG  . GLU A 1 94  ? 45.35741 -53.56476 10.63221 1.000 161.70261 ? 94  GLU A CG  1 
ATOM   749  C CD  . GLU A 1 94  ? 45.82590 -55.00609 10.58033 1.000 167.04665 ? 94  GLU A CD  1 
ATOM   750  O OE1 . GLU A 1 94  ? 45.49312 -55.70415 9.59928  1.000 157.38770 ? 94  GLU A OE1 1 
ATOM   751  O OE2 . GLU A 1 94  ? 46.52674 -55.44074 11.51856 1.000 164.42386 ? 94  GLU A OE2 1 
ATOM   752  N N   . GLY A 1 95  ? 43.86930 -51.16000 7.06565  1.000 109.45281 ? 95  GLY A N   1 
ATOM   753  C CA  . GLY A 1 95  ? 43.20640 -50.78948 5.83622  1.000 113.99862 ? 95  GLY A CA  1 
ATOM   754  C C   . GLY A 1 95  ? 42.73637 -49.35454 5.77638  1.000 110.08709 ? 95  GLY A C   1 
ATOM   755  O O   . GLY A 1 95  ? 42.18019 -48.94526 4.74980  1.000 116.11388 ? 95  GLY A O   1 
ATOM   756  N N   . TYR A 1 96  ? 42.93835 -48.57878 6.83539  1.000 106.54071 ? 96  TYR A N   1 
ATOM   757  C CA  . TYR A 1 96  ? 42.53065 -47.18503 6.88335  1.000 109.55401 ? 96  TYR A CA  1 
ATOM   758  C C   . TYR A 1 96  ? 43.75822 -46.28733 6.92437  1.000 106.73959 ? 96  TYR A C   1 
ATOM   759  O O   . TYR A 1 96  ? 44.85021 -46.70920 7.31539  1.000 110.40405 ? 96  TYR A O   1 
ATOM   760  C CB  . TYR A 1 96  ? 41.61928 -46.92382 8.08979  1.000 100.02006 ? 96  TYR A CB  1 
ATOM   761  C CG  . TYR A 1 96  ? 40.21901 -47.43584 7.85504  1.000 99.41791  ? 96  TYR A CG  1 
ATOM   762  C CD1 . TYR A 1 96  ? 39.95690 -48.79810 7.82518  1.000 100.20593 ? 96  TYR A CD1 1 
ATOM   763  C CD2 . TYR A 1 96  ? 39.16555 -46.56061 7.63266  1.000 98.34791  ? 96  TYR A CD2 1 
ATOM   764  C CE1 . TYR A 1 96  ? 38.68696 -49.27421 7.59090  1.000 99.83346  ? 96  TYR A CE1 1 
ATOM   765  C CE2 . TYR A 1 96  ? 37.89037 -47.02770 7.39554  1.000 98.00451  ? 96  TYR A CE2 1 
ATOM   766  C CZ  . TYR A 1 96  ? 37.65636 -48.38596 7.37712  1.000 98.70386  ? 96  TYR A CZ  1 
ATOM   767  O OH  . TYR A 1 96  ? 36.38658 -48.85886 7.14115  1.000 98.46593  ? 96  TYR A OH  1 
ATOM   768  N N   . GLU A 1 97  ? 43.56559 -45.04629 6.48919  1.000 106.07739 ? 97  GLU A N   1 
ATOM   769  C CA  . GLU A 1 97  ? 44.67102 -44.10437 6.41636  1.000 107.69773 ? 97  GLU A CA  1 
ATOM   770  C C   . GLU A 1 97  ? 45.31975 -43.94972 7.79041  1.000 121.44765 ? 97  GLU A C   1 
ATOM   771  O O   . GLU A 1 97  ? 44.61836 -43.91627 8.80920  1.000 109.36350 ? 97  GLU A O   1 
ATOM   772  C CB  . GLU A 1 97  ? 44.18680 -42.74922 5.90270  1.000 110.17584 ? 97  GLU A CB  1 
ATOM   773  C CG  . GLU A 1 97  ? 43.66751 -42.76807 4.47447  1.000 136.66015 ? 97  GLU A CG  1 
ATOM   774  C CD  . GLU A 1 97  ? 43.27087 -41.38818 3.98592  1.000 141.45149 ? 97  GLU A CD  1 
ATOM   775  O OE1 . GLU A 1 97  ? 43.45108 -40.41468 4.74689  1.000 132.09470 ? 97  GLU A OE1 1 
ATOM   776  O OE2 . GLU A 1 97  ? 42.77936 -41.27553 2.84303  1.000 142.45674 ? 97  GLU A OE2 1 
ATOM   777  N N   . PRO A 1 98  ? 46.64813 -43.85489 7.85582  1.000 124.06732 ? 98  PRO A N   1 
ATOM   778  C CA  . PRO A 1 98  ? 47.33571 -43.91784 9.15399  1.000 104.43715 ? 98  PRO A CA  1 
ATOM   779  C C   . PRO A 1 98  ? 47.03503 -42.70249 10.02034 1.000 104.34891 ? 98  PRO A C   1 
ATOM   780  O O   . PRO A 1 98  ? 47.08080 -41.56053 9.55795  1.000 103.14101 ? 98  PRO A O   1 
ATOM   781  C CB  . PRO A 1 98  ? 48.81789 -43.98025 8.76632  1.000 108.66899 ? 98  PRO A CB  1 
ATOM   782  C CG  . PRO A 1 98  ? 48.87675 -43.35467 7.40930  1.000 113.03718 ? 98  PRO A CG  1 
ATOM   783  C CD  . PRO A 1 98  ? 47.59177 -43.73014 6.73194  1.000 112.41003 ? 98  PRO A CD  1 
ATOM   784  N N   . VAL A 1 99  ? 46.71881 -42.96637 11.28725 1.000 97.28107  ? 99  VAL A N   1 
ATOM   785  C CA  . VAL A 1 99  ? 46.51858 -41.92724 12.29700 1.000 94.86654  ? 99  VAL A CA  1 
ATOM   786  C C   . VAL A 1 99  ? 47.34476 -42.36736 13.50824 1.000 96.60278  ? 99  VAL A C   1 
ATOM   787  O O   . VAL A 1 99  ? 46.88096 -43.14892 14.34126 1.000 99.90892  ? 99  VAL A O   1 
ATOM   788  C CB  . VAL A 1 99  ? 45.04552 -41.73615 12.67215 1.000 95.94276  ? 99  VAL A CB  1 
ATOM   789  C CG1 . VAL A 1 99  ? 44.88475 -40.54777 13.60572 1.000 88.37718  ? 99  VAL A CG1 1 
ATOM   790  C CG2 . VAL A 1 99  ? 44.18619 -41.56181 11.42622 1.000 92.58238  ? 99  VAL A CG2 1 
ATOM   791  N N   . VAL A 1 100 ? 48.57375 -41.86807 13.60312 1.000 95.04058  ? 100 VAL A N   1 
ATOM   792  C CA  A VAL A 1 100 ? 49.51205 -42.27758 14.64395 0.264 97.89044  ? 100 VAL A CA  1 
ATOM   793  C CA  B VAL A 1 100 ? 49.51627 -42.27568 14.64216 0.736 97.84788  ? 100 VAL A CA  1 
ATOM   794  C C   . VAL A 1 100 ? 49.64752 -41.14350 15.65196 1.000 99.69259  ? 100 VAL A C   1 
ATOM   795  O O   . VAL A 1 100 ? 50.06788 -40.03351 15.30068 1.000 96.74416  ? 100 VAL A O   1 
ATOM   796  C CB  A VAL A 1 100 ? 50.87761 -42.66796 14.05497 0.264 99.67223  ? 100 VAL A CB  1 
ATOM   797  C CB  B VAL A 1 100 ? 50.88609 -42.64160 14.05089 0.736 99.32369  ? 100 VAL A CB  1 
ATOM   798  C CG1 A VAL A 1 100 ? 50.80861 -44.05873 13.44313 0.264 102.57924 ? 100 VAL A CG1 1 
ATOM   799  C CG1 B VAL A 1 100 ? 51.84553 -43.05577 15.15668 0.736 98.37086  ? 100 VAL A CG1 1 
ATOM   800  C CG2 A VAL A 1 100 ? 51.32691 -41.65654 13.00838 0.264 102.59412 ? 100 VAL A CG2 1 
ATOM   801  C CG2 B VAL A 1 100 ? 50.74107 -43.74886 13.01665 0.736 101.74485 ? 100 VAL A CG2 1 
ATOM   802  N N   . ASN A 1 101 ? 49.28643 -41.42857 16.90521 1.000 88.82607  ? 101 ASN A N   1 
ATOM   803  C CA  . ASN A 1 101 ? 49.47005 -40.51256 18.03435 1.000 98.29841  ? 101 ASN A CA  1 
ATOM   804  C C   . ASN A 1 101 ? 48.91095 -39.12074 17.74341 1.000 86.68457  ? 101 ASN A C   1 
ATOM   805  O O   . ASN A 1 101 ? 49.57466 -38.10133 17.94389 1.000 87.94413  ? 101 ASN A O   1 
ATOM   806  C CB  . ASN A 1 101 ? 50.94629 -40.43304 18.42684 1.000 89.24508  ? 101 ASN A CB  1 
ATOM   807  C CG  . ASN A 1 101 ? 51.50901 -41.77356 18.85770 1.000 109.02036 ? 101 ASN A CG  1 
ATOM   808  O OD1 . ASN A 1 101 ? 50.80525 -42.59653 19.44206 1.000 99.89564  ? 101 ASN A OD1 1 
ATOM   809  N ND2 . ASN A 1 101 ? 52.78607 -41.99943 18.56961 1.000 131.18357 ? 101 ASN A ND2 1 
ATOM   810  N N   . THR A 1 102 ? 47.66626 -39.08069 17.27399 1.000 85.27720  ? 102 THR A N   1 
ATOM   811  C CA  . THR A 1 102 ? 47.02610 -37.82062 16.92595 1.000 93.87751  ? 102 THR A CA  1 
ATOM   812  C C   . THR A 1 102 ? 45.90314 -37.51858 17.90459 1.000 91.88765  ? 102 THR A C   1 
ATOM   813  O O   . THR A 1 102 ? 44.99393 -38.34624 18.06667 1.000 81.31849  ? 102 THR A O   1 
ATOM   814  C CB  . THR A 1 102 ? 46.48564 -37.86699 15.49868 1.000 95.18240  ? 102 THR A CB  1 
ATOM   815  O OG1 . THR A 1 102 ? 47.57685 -37.98603 14.57559 1.000 111.99840 ? 102 THR A OG1 1 
ATOM   816  C CG2 . THR A 1 102 ? 45.69175 -36.60532 15.18813 1.000 88.25572  ? 102 THR A CG2 1 
ATOM   817  N N   . PRO A 1 103 ? 45.92581 -36.36998 18.58052 1.000 80.53995  ? 103 PRO A N   1 
ATOM   818  C CA  . PRO A 1 103 ? 44.79268 -35.99647 19.43588 1.000 83.52793  ? 103 PRO A CA  1 
ATOM   819  C C   . PRO A 1 103 ? 43.52316 -35.80592 18.61787 1.000 78.88615  ? 103 PRO A C   1 
ATOM   820  O O   . PRO A 1 103 ? 43.55843 -35.35062 17.47202 1.000 93.31259  ? 103 PRO A O   1 
ATOM   821  C CB  . PRO A 1 103 ? 45.24858 -34.67877 20.07744 1.000 77.45389  ? 103 PRO A CB  1 
ATOM   822  C CG  . PRO A 1 103 ? 46.74577 -34.69799 19.97671 1.000 84.07265  ? 103 PRO A CG  1 
ATOM   823  C CD  . PRO A 1 103 ? 47.04913 -35.42464 18.69892 1.000 93.33414  ? 103 PRO A CD  1 
ATOM   824  N N   . ILE A 1 104 ? 42.38890 -36.16270 19.22371 1.000 82.97637  ? 104 ILE A N   1 
ATOM   825  C CA  . ILE A 1 104 ? 41.08795 -36.10133 18.57095 1.000 80.60054  ? 104 ILE A CA  1 
ATOM   826  C C   . ILE A 1 104 ? 40.11638 -35.21807 19.34515 1.000 88.72894  ? 104 ILE A C   1 
ATOM   827  O O   . ILE A 1 104 ? 39.53891 -34.27562 18.79340 1.000 105.64691 ? 104 ILE A O   1 
ATOM   828  C CB  . ILE A 1 104 ? 40.49537 -37.51198 18.37021 1.000 76.61256  ? 104 ILE A CB  1 
ATOM   829  C CG1 . ILE A 1 104 ? 41.36114 -38.33409 17.42555 1.000 94.74026  ? 104 ILE A CG1 1 
ATOM   830  C CG2 . ILE A 1 104 ? 39.06382 -37.41647 17.85616 1.000 99.32811  ? 104 ILE A CG2 1 
ATOM   831  C CD1 . ILE A 1 104 ? 40.73610 -39.65155 17.05098 1.000 125.18350 ? 104 ILE A CD1 1 
ATOM   832  N N   . ALA A 1 105 ? 39.92132 -35.50857 20.62833 1.000 85.30880  ? 105 ALA A N   1 
ATOM   833  C CA  . ALA A 1 105 ? 38.93833 -34.80861 21.43900 1.000 82.96398  ? 105 ALA A CA  1 
ATOM   834  C C   . ALA A 1 105 ? 39.59327 -34.23655 22.68789 1.000 82.76766  ? 105 ALA A C   1 
ATOM   835  O O   . ALA A 1 105 ? 40.63754 -34.70781 23.14793 1.000 68.27390  ? 105 ALA A O   1 
ATOM   836  C CB  . ALA A 1 105 ? 37.77970 -35.73433 21.83958 1.000 69.48090  ? 105 ALA A CB  1 
ATOM   837  N N   . ARG A 1 106 ? 38.95530 -33.20335 23.22955 1.000 82.47077  ? 106 ARG A N   1 
ATOM   838  C CA  . ARG A 1 106 ? 39.37451 -32.56332 24.46710 1.000 63.92048  ? 106 ARG A CA  1 
ATOM   839  C C   . ARG A 1 106 ? 38.17430 -32.48522 25.39698 1.000 82.86933  ? 106 ARG A C   1 
ATOM   840  O O   . ARG A 1 106 ? 37.10005 -32.03055 24.99037 1.000 92.84338  ? 106 ARG A O   1 
ATOM   841  C CB  . ARG A 1 106 ? 39.93482 -31.16201 24.20149 1.000 70.47830  ? 106 ARG A CB  1 
ATOM   842  C CG  . ARG A 1 106 ? 40.34265 -30.40035 25.44812 1.000 87.46905  ? 106 ARG A CG  1 
ATOM   843  C CD  . ARG A 1 106 ? 40.32220 -28.90233 25.19478 1.000 103.40033 ? 106 ARG A CD  1 
ATOM   844  N NE  . ARG A 1 106 ? 40.98489 -28.15109 26.25385 1.000 122.37599 ? 106 ARG A NE  1 
ATOM   845  C CZ  . ARG A 1 106 ? 40.99298 -26.82780 26.33749 1.000 122.22471 ? 106 ARG A CZ  1 
ATOM   846  N NH1 . ARG A 1 106 ? 40.35839 -26.07570 25.45350 1.000 122.98614 ? 106 ARG A NH1 1 
ATOM   847  N NH2 . ARG A 1 106 ? 41.65366 -26.24428 27.33313 1.000 102.32697 ? 106 ARG A NH2 1 
ATOM   848  N N   . ILE A 1 107 ? 38.35174 -32.93188 26.63617 1.000 78.20807  ? 107 ILE A N   1 
ATOM   849  C CA  . ILE A 1 107 ? 37.28425 -32.94576 27.62792 1.000 84.58792  ? 107 ILE A CA  1 
ATOM   850  C C   . ILE A 1 107 ? 37.70749 -32.07653 28.80214 1.000 78.36154  ? 107 ILE A C   1 
ATOM   851  O O   . ILE A 1 107 ? 38.78512 -32.27799 29.37448 1.000 87.62342  ? 107 ILE A O   1 
ATOM   852  C CB  . ILE A 1 107 ? 36.95703 -34.37568 28.09428 1.000 80.04285  ? 107 ILE A CB  1 
ATOM   853  C CG1 . ILE A 1 107 ? 36.64654 -35.27013 26.89189 1.000 66.79131  ? 107 ILE A CG1 1 
ATOM   854  C CG2 . ILE A 1 107 ? 35.78448 -34.36039 29.06366 1.000 71.85150  ? 107 ILE A CG2 1 
ATOM   855  C CD1 . ILE A 1 107 ? 36.30036 -36.69332 27.26469 1.000 77.99723  ? 107 ILE A CD1 1 
ATOM   856  N N   . THR A 1 108 ? 36.86099 -31.11515 29.15773 1.000 85.12644  ? 108 THR A N   1 
ATOM   857  C CA  . THR A 1 108 ? 37.11475 -30.20594 30.26631 1.000 98.08304  ? 108 THR A CA  1 
ATOM   858  C C   . THR A 1 108 ? 36.09221 -30.45394 31.36496 1.000 103.44164 ? 108 THR A C   1 
ATOM   859  O O   . THR A 1 108 ? 34.88302 -30.42150 31.11255 1.000 114.07411 ? 108 THR A O   1 
ATOM   860  C CB  . THR A 1 108 ? 37.05176 -28.74661 29.81040 1.000 106.90505 ? 108 THR A CB  1 
ATOM   861  O OG1 . THR A 1 108 ? 35.72869 -28.44395 29.35034 1.000 107.07540 ? 108 THR A OG1 1 
ATOM   862  C CG2 . THR A 1 108 ? 38.03800 -28.50325 28.68351 1.000 100.90411 ? 108 THR A CG2 1 
ATOM   863  N N   . VAL A 1 109 ? 36.57882 -30.70293 32.57557 1.000 98.51015  ? 109 VAL A N   1 
ATOM   864  C CA  . VAL A 1 109 ? 35.73054 -30.92867 33.73935 1.000 106.01692 ? 109 VAL A CA  1 
ATOM   865  C C   . VAL A 1 109 ? 35.72022 -29.63006 34.53688 1.000 120.74628 ? 109 VAL A C   1 
ATOM   866  O O   . VAL A 1 109 ? 36.68899 -29.30117 35.22699 1.000 129.37071 ? 109 VAL A O   1 
ATOM   867  C CB  . VAL A 1 109 ? 36.22063 -32.10962 34.58069 1.000 99.56399  ? 109 VAL A CB  1 
ATOM   868  C CG1 . VAL A 1 109 ? 35.29854 -32.33188 35.77035 1.000 116.15357 ? 109 VAL A CG1 1 
ATOM   869  C CG2 . VAL A 1 109 ? 36.31241 -33.36440 33.72734 1.000 105.90767 ? 109 VAL A CG2 1 
ATOM   870  N N   . THR A 1 110 ? 34.62228 -28.88472 34.43994 1.000 144.87987 ? 110 THR A N   1 
ATOM   871  C CA  . THR A 1 110 ? 34.46273 -27.61031 35.13214 1.000 158.28815 ? 110 THR A CA  1 
ATOM   872  C C   . THR A 1 110 ? 33.38662 -27.77212 36.19854 1.000 165.38376 ? 110 THR A C   1 
ATOM   873  O O   . THR A 1 110 ? 32.20124 -27.91011 35.87746 1.000 168.66741 ? 110 THR A O   1 
ATOM   874  C CB  . THR A 1 110 ? 34.10146 -26.49448 34.15358 1.000 168.14887 ? 110 THR A CB  1 
ATOM   875  O OG1 . THR A 1 110 ? 32.89882 -26.83943 33.45418 1.000 173.71083 ? 110 THR A OG1 1 
ATOM   876  C CG2 . THR A 1 110 ? 35.22551 -26.28309 33.14969 1.000 160.00993 ? 110 THR A CG2 1 
ATOM   877  N N   . LYS A 1 111 ? 33.80118 -27.75766 37.46218 1.000 169.36448 ? 111 LYS A N   1 
ATOM   878  C CA  . LYS A 1 111 ? 32.87659 -27.85710 38.58195 1.000 167.33550 ? 111 LYS A CA  1 
ATOM   879  C C   . LYS A 1 111 ? 32.39514 -26.46492 38.96868 1.000 157.98789 ? 111 LYS A C   1 
ATOM   880  O O   . LYS A 1 111 ? 33.20455 -25.55076 39.15666 1.000 152.01983 ? 111 LYS A O   1 
ATOM   881  C CB  . LYS A 1 111 ? 33.54319 -28.54718 39.77255 1.000 163.97862 ? 111 LYS A CB  1 
ATOM   882  C CG  . LYS A 1 111 ? 33.99108 -29.97176 39.47949 1.000 169.10652 ? 111 LYS A CG  1 
ATOM   883  C CD  . LYS A 1 111 ? 34.62935 -30.62289 40.69511 1.000 164.08137 ? 111 LYS A CD  1 
ATOM   884  C CE  . LYS A 1 111 ? 35.04689 -32.05461 40.39732 1.000 147.85164 ? 111 LYS A CE  1 
ATOM   885  N NZ  . LYS A 1 111 ? 35.67795 -32.70899 41.57700 1.000 149.67465 ? 111 LYS A NZ  1 
ATOM   886  N N   . ASP A 1 112 ? 31.08085 -26.31050 39.07811 1.000 159.46693 ? 112 ASP A N   1 
ATOM   887  C CA  . ASP A 1 112 ? 30.49986 -25.00929 39.37493 1.000 169.68131 ? 112 ASP A CA  1 
ATOM   888  C C   . ASP A 1 112 ? 30.92473 -24.54981 40.76739 1.000 185.64800 ? 112 ASP A C   1 
ATOM   889  O O   . ASP A 1 112 ? 30.75070 -25.29546 41.74167 1.000 186.70441 ? 112 ASP A O   1 
ATOM   890  C CB  . ASP A 1 112 ? 28.97729 -25.07897 39.27259 1.000 169.07091 ? 112 ASP A CB  1 
ATOM   891  C CG  . ASP A 1 112 ? 28.29917 -23.82365 39.77605 1.000 194.98048 ? 112 ASP A CG  1 
ATOM   892  O OD1 . ASP A 1 112 ? 28.53489 -22.74188 39.19810 1.000 195.50996 ? 112 ASP A OD1 1 
ATOM   893  O OD2 . ASP A 1 112 ? 27.52165 -23.92368 40.74730 1.000 199.41259 ? 112 ASP A OD2 1 
ATOM   894  N N   . PRO A 1 113 ? 31.47983 -23.34198 40.90573 1.000 190.05659 ? 113 PRO A N   1 
ATOM   895  C CA  . PRO A 1 113 ? 32.01512 -22.93273 42.21404 1.000 195.83921 ? 113 PRO A CA  1 
ATOM   896  C C   . PRO A 1 113 ? 30.94776 -22.68402 43.26545 1.000 213.20013 ? 113 PRO A C   1 
ATOM   897  O O   . PRO A 1 113 ? 31.22027 -22.87612 44.45684 1.000 207.64891 ? 113 PRO A O   1 
ATOM   898  C CB  . PRO A 1 113 ? 32.79342 -21.65098 41.88621 1.000 192.75920 ? 113 PRO A CB  1 
ATOM   899  C CG  . PRO A 1 113 ? 32.13268 -21.11832 40.65725 1.000 196.59801 ? 113 PRO A CG  1 
ATOM   900  C CD  . PRO A 1 113 ? 31.70580 -22.32262 39.86661 1.000 177.57331 ? 113 PRO A CD  1 
ATOM   901  N N   . GLU A 1 114 ? 29.74638 -22.26305 42.87393 1.000 233.42988 ? 114 GLU A N   1 
ATOM   902  C CA  . GLU A 1 114 ? 28.68284 -21.97900 43.83882 1.000 245.33100 ? 114 GLU A CA  1 
ATOM   903  C C   . GLU A 1 114 ? 27.88874 -23.24859 44.15835 1.000 251.27673 ? 114 GLU A C   1 
ATOM   904  O O   . GLU A 1 114 ? 26.67112 -23.32369 43.99100 1.000 265.41112 ? 114 GLU A O   1 
ATOM   905  C CB  . GLU A 1 114 ? 27.77916 -20.86434 43.32128 1.000 264.17863 ? 114 GLU A CB  1 
ATOM   906  C CG  . GLU A 1 114 ? 27.33727 -21.02145 41.87649 1.000 265.21782 ? 114 GLU A CG  1 
ATOM   907  C CD  . GLU A 1 114 ? 26.32102 -19.97604 41.46110 1.000 285.81334 ? 114 GLU A CD  1 
ATOM   908  O OE1 . GLU A 1 114 ? 25.95168 -19.13486 42.30732 1.000 293.91799 ? 114 GLU A OE1 1 
ATOM   909  O OE2 . GLU A 1 114 ? 25.89003 -19.99651 40.28897 1.000 290.57027 ? 114 GLU A OE2 1 
ATOM   910  N N   . THR A 1 115 ? 28.61997 -24.25361 44.64001 1.000 238.32120 ? 115 THR A N   1 
ATOM   911  C CA  . THR A 1 115 ? 28.06334 -25.53695 45.07243 1.000 234.37340 ? 115 THR A CA  1 
ATOM   912  C C   . THR A 1 115 ? 27.21196 -26.17246 43.97208 1.000 211.58342 ? 115 THR A C   1 
ATOM   913  O O   . THR A 1 115 ? 26.02999 -26.47286 44.14889 1.000 215.83699 ? 115 THR A O   1 
ATOM   914  C CB  . THR A 1 115 ? 27.25966 -25.38182 46.36798 1.000 241.28034 ? 115 THR A CB  1 
ATOM   915  O OG1 . THR A 1 115 ? 26.08314 -24.60202 46.11909 1.000 253.01605 ? 115 THR A OG1 1 
ATOM   916  C CG2 . THR A 1 115 ? 28.09928 -24.69745 47.43651 1.000 230.87518 ? 115 THR A CG2 1 
ATOM   917  N N   . GLY A 1 116 ? 27.84327 -26.37725 42.81980 1.000 181.58461 ? 116 GLY A N   1 
ATOM   918  C CA  . GLY A 1 116 ? 27.17058 -26.99983 41.69783 1.000 181.12059 ? 116 GLY A CA  1 
ATOM   919  C C   . GLY A 1 116 ? 27.74258 -28.35755 41.34976 1.000 177.34958 ? 116 GLY A C   1 
ATOM   920  O O   . GLY A 1 116 ? 28.84869 -28.70100 41.77786 1.000 168.04579 ? 116 GLY A O   1 
ATOM   921  N N   . LYS A 1 117 ? 26.99977 -29.13887 40.57041 1.000 180.74833 ? 117 LYS A N   1 
ATOM   922  C CA  . LYS A 1 117 ? 27.43875 -30.47279 40.19645 1.000 169.45070 ? 117 LYS A CA  1 
ATOM   923  C C   . LYS A 1 117 ? 28.50325 -30.39383 39.10350 1.000 167.25660 ? 117 LYS A C   1 
ATOM   924  O O   . LYS A 1 117 ? 28.91337 -29.31439 38.66712 1.000 165.50251 ? 117 LYS A O   1 
ATOM   925  C CB  . LYS A 1 117 ? 26.24860 -31.31873 39.74926 1.000 167.85004 ? 117 LYS A CB  1 
ATOM   926  C CG  . LYS A 1 117 ? 25.53630 -30.79354 38.51466 1.000 172.17535 ? 117 LYS A CG  1 
ATOM   927  C CD  . LYS A 1 117 ? 24.38582 -31.70487 38.11905 1.000 172.21927 ? 117 LYS A CD  1 
ATOM   928  C CE  . LYS A 1 117 ? 23.66052 -31.18100 36.89092 1.000 178.00285 ? 117 LYS A CE  1 
ATOM   929  N NZ  . LYS A 1 117 ? 22.52452 -32.06146 36.50157 1.000 179.38965 ? 117 LYS A NZ  1 
ATOM   930  N N   . VAL A 1 118 ? 28.95361 -31.55866 38.65344 1.000 148.68268 ? 118 VAL A N   1 
ATOM   931  C CA  . VAL A 1 118 ? 30.01952 -31.64174 37.66279 1.000 140.35225 ? 118 VAL A CA  1 
ATOM   932  C C   . VAL A 1 118 ? 29.45842 -31.34995 36.27819 1.000 145.20550 ? 118 VAL A C   1 
ATOM   933  O O   . VAL A 1 118 ? 28.35259 -31.78235 35.93023 1.000 147.02691 ? 118 VAL A O   1 
ATOM   934  C CB  . VAL A 1 118 ? 30.69278 -33.02414 37.71664 1.000 137.48069 ? 118 VAL A CB  1 
ATOM   935  C CG1 . VAL A 1 118 ? 31.62262 -33.11104 38.91534 1.000 139.83845 ? 118 VAL A CG1 1 
ATOM   936  C CG2 . VAL A 1 118 ? 29.63905 -34.11942 37.78434 1.000 127.49999 ? 118 VAL A CG2 1 
ATOM   937  N N   . THR A 1 119 ? 30.22621 -30.60883 35.48136 1.000 150.79409 ? 119 THR A N   1 
ATOM   938  C CA  . THR A 1 119 ? 29.85869 -30.27036 34.11279 1.000 136.11621 ? 119 THR A CA  1 
ATOM   939  C C   . THR A 1 119 ? 31.00532 -30.65271 33.19012 1.000 133.88719 ? 119 THR A C   1 
ATOM   940  O O   . THR A 1 119 ? 32.16158 -30.31238 33.45958 1.000 130.19350 ? 119 THR A O   1 
ATOM   941  C CB  . THR A 1 119 ? 29.53898 -28.77754 33.97151 1.000 137.06317 ? 119 THR A CB  1 
ATOM   942  O OG1 . THR A 1 119 ? 28.44589 -28.43707 34.83348 1.000 172.56255 ? 119 THR A OG1 1 
ATOM   943  C CG2 . THR A 1 119 ? 29.16629 -28.44363 32.53417 1.000 134.64357 ? 119 THR A CG2 1 
ATOM   944  N N   . TYR A 1 120 ? 30.68566 -31.35562 32.10716 1.000 126.33264 ? 120 TYR A N   1 
ATOM   945  C CA  . TYR A 1 120 ? 31.68105 -31.85606 31.17108 1.000 89.85060  ? 120 TYR A CA  1 
ATOM   946  C C   . TYR A 1 120 ? 31.43595 -31.26308 29.79237 1.000 91.53108  ? 120 TYR A C   1 
ATOM   947  O O   . TYR A 1 120 ? 30.28813 -31.13132 29.35559 1.000 115.29307 ? 120 TYR A O   1 
ATOM   948  C CB  . TYR A 1 120 ? 31.65012 -33.38316 31.10648 1.000 90.29969  ? 120 TYR A CB  1 
ATOM   949  C CG  . TYR A 1 120 ? 31.72283 -34.02940 32.46866 1.000 89.76737  ? 120 TYR A CG  1 
ATOM   950  C CD1 . TYR A 1 120 ? 32.94579 -34.33101 33.05122 1.000 101.81301 ? 120 TYR A CD1 1 
ATOM   951  C CD2 . TYR A 1 120 ? 30.56782 -34.32280 33.18020 1.000 107.86908 ? 120 TYR A CD2 1 
ATOM   952  C CE1 . TYR A 1 120 ? 33.01629 -34.91455 34.30167 1.000 105.99276 ? 120 TYR A CE1 1 
ATOM   953  C CE2 . TYR A 1 120 ? 30.62795 -34.90352 34.42896 1.000 125.64727 ? 120 TYR A CE2 1 
ATOM   954  C CZ  . TYR A 1 120 ? 31.85395 -35.19823 34.98503 1.000 126.33192 ? 120 TYR A CZ  1 
ATOM   955  O OH  . TYR A 1 120 ? 31.91636 -35.77853 36.22914 1.000 146.66275 ? 120 TYR A OH  1 
ATOM   956  N N   . GLU A 1 121 ? 32.52308 -30.91131 29.11037 1.000 103.47250 ? 121 GLU A N   1 
ATOM   957  C CA  . GLU A 1 121 ? 32.45328 -30.22947 27.82370 1.000 103.35539 ? 121 GLU A CA  1 
ATOM   958  C C   . GLU A 1 121 ? 33.46757 -30.86770 26.88922 1.000 96.28931  ? 121 GLU A C   1 
ATOM   959  O O   . GLU A 1 121 ? 34.65594 -30.93396 27.21579 1.000 107.76553 ? 121 GLU A O   1 
ATOM   960  C CB  . GLU A 1 121 ? 32.72386 -28.73062 27.98947 1.000 118.39990 ? 121 GLU A CB  1 
ATOM   961  C CG  . GLU A 1 121 ? 32.29040 -27.87302 26.81814 1.000 147.03364 ? 121 GLU A CG  1 
ATOM   962  C CD  . GLU A 1 121 ? 33.44234 -27.50030 25.90964 1.000 152.64481 ? 121 GLU A CD  1 
ATOM   963  O OE1 . GLU A 1 121 ? 34.58614 -27.91189 26.19671 1.000 137.33603 ? 121 GLU A OE1 1 
ATOM   964  O OE2 . GLU A 1 121 ? 33.20358 -26.79025 24.91058 1.000 163.74958 ? 121 GLU A OE2 1 
ATOM   965  N N   . VAL A 1 122 ? 33.00264 -31.33485 25.73519 1.000 108.90729 ? 122 VAL A N   1 
ATOM   966  C CA  . VAL A 1 122 ? 33.82284 -32.09527 24.79929 1.000 95.98400  ? 122 VAL A CA  1 
ATOM   967  C C   . VAL A 1 122 ? 34.03077 -31.25006 23.55126 1.000 78.05764  ? 122 VAL A C   1 
ATOM   968  O O   . VAL A 1 122 ? 33.07681 -30.95787 22.82132 1.000 95.32579  ? 122 VAL A O   1 
ATOM   969  C CB  . VAL A 1 122 ? 33.18483 -33.44749 24.45492 1.000 85.08314  ? 122 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 122 ? 33.99028 -34.15356 23.37579 1.000 91.71423  ? 122 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 122 ? 33.08427 -34.30996 25.69942 1.000 72.83198  ? 122 VAL A CG2 1 
ATOM   972  N N   . GLU A 1 123 ? 35.27661 -30.86128 23.30395 1.000 98.81314  ? 123 GLU A N   1 
ATOM   973  C CA  . GLU A 1 123 ? 35.66798 -30.15097 22.09645 1.000 82.76192  ? 123 GLU A CA  1 
ATOM   974  C C   . GLU A 1 123 ? 36.46310 -31.07730 21.18639 1.000 80.64336  ? 123 GLU A C   1 
ATOM   975  O O   . GLU A 1 123 ? 36.91028 -32.15476 21.58752 1.000 89.18325  ? 123 GLU A O   1 
ATOM   976  C CB  . GLU A 1 123 ? 36.49574 -28.90449 22.43153 1.000 100.97107 ? 123 GLU A CB  1 
ATOM   977  C CG  . GLU A 1 123 ? 35.73078 -27.81850 23.16157 1.000 126.31850 ? 123 GLU A CG  1 
ATOM   978  C CD  . GLU A 1 123 ? 36.56165 -26.56793 23.36876 1.000 155.03587 ? 123 GLU A CD  1 
ATOM   979  O OE1 . GLU A 1 123 ? 37.63402 -26.45729 22.73775 1.000 149.93062 ? 123 GLU A OE1 1 
ATOM   980  O OE2 . GLU A 1 123 ? 36.14529 -25.69740 24.16210 1.000 166.51290 ? 123 GLU A OE2 1 
ATOM   981  N N   . ALA A 1 124 ? 36.64384 -30.63534 19.94684 1.000 105.15498 ? 124 ALA A N   1 
ATOM   982  C CA  . ALA A 1 124 ? 37.39142 -31.37894 18.94667 1.000 99.09851  ? 124 ALA A CA  1 
ATOM   983  C C   . ALA A 1 124 ? 38.69371 -30.65841 18.62371 1.000 100.10499 ? 124 ALA A C   1 
ATOM   984  O O   . ALA A 1 124 ? 38.77731 -29.42862 18.68935 1.000 114.26444 ? 124 ALA A O   1 
ATOM   985  C CB  . ALA A 1 124 ? 36.56985 -31.56642 17.66846 1.000 84.78384  ? 124 ALA A CB  1 
ATOM   986  N N   . VAL A 1 125 ? 39.71150 -31.43943 18.27600 1.000 119.97192 ? 125 VAL A N   1 
ATOM   987  C CA  . VAL A 1 125 ? 41.00873 -30.89114 17.89478 1.000 129.68108 ? 125 VAL A CA  1 
ATOM   988  C C   . VAL A 1 125 ? 40.96998 -30.54298 16.41255 1.000 133.52240 ? 125 VAL A C   1 
ATOM   989  O O   . VAL A 1 125 ? 40.75508 -31.41558 15.56450 1.000 130.46107 ? 125 VAL A O   1 
ATOM   990  C CB  . VAL A 1 125 ? 42.14169 -31.88045 18.20179 1.000 131.50009 ? 125 VAL A CB  1 
ATOM   991  C CG1 . VAL A 1 125 ? 43.47480 -31.32261 17.72818 1.000 141.89743 ? 125 VAL A CG1 1 
ATOM   992  C CG2 . VAL A 1 125 ? 42.18659 -32.18675 19.69037 1.000 128.25529 ? 125 VAL A CG2 1 
ATOM   993  N N   . LYS A 1 126 ? 41.17423 -29.26407 16.09845 1.000 161.34970 ? 126 LYS A N   1 
ATOM   994  C CA  . LYS A 1 126 ? 41.15010 -28.79223 14.71346 1.000 156.19803 ? 126 LYS A CA  1 
ATOM   995  C C   . LYS A 1 126 ? 42.53401 -28.98046 14.08880 1.000 163.43758 ? 126 LYS A C   1 
ATOM   996  O O   . LYS A 1 126 ? 43.31626 -28.04559 13.90567 1.000 195.95376 ? 126 LYS A O   1 
ATOM   997  C CB  . LYS A 1 126 ? 40.68951 -27.34058 14.65494 1.000 169.84700 ? 126 LYS A CB  1 
ATOM   998  C CG  . LYS A 1 126 ? 40.54181 -26.77292 13.24651 1.000 189.27091 ? 126 LYS A CG  1 
ATOM   999  C CD  . LYS A 1 126 ? 39.53796 -27.55923 12.41764 1.000 187.07944 ? 126 LYS A CD  1 
ATOM   1000 C CE  . LYS A 1 126 ? 39.39727 -26.96397 11.02334 1.000 178.99587 ? 126 LYS A CE  1 
ATOM   1001 N NZ  . LYS A 1 126 ? 38.42101 -27.71297 10.18426 1.000 164.98020 ? 126 LYS A NZ  1 
ATOM   1002 N N   . ASN A 1 127 ? 42.83124 -30.23903 13.77251 1.000 167.26314 ? 127 ASN A N   1 
ATOM   1003 C CA  . ASN A 1 127 ? 44.05666 -30.60967 13.07498 1.000 183.74407 ? 127 ASN A CA  1 
ATOM   1004 C C   . ASN A 1 127 ? 43.69298 -31.53983 11.92980 1.000 198.54799 ? 127 ASN A C   1 
ATOM   1005 O O   . ASN A 1 127 ? 43.08877 -32.59451 12.15263 1.000 194.52832 ? 127 ASN A O   1 
ATOM   1006 C CB  . ASN A 1 127 ? 45.06086 -31.27933 14.01850 1.000 195.44435 ? 127 ASN A CB  1 
ATOM   1007 C CG  . ASN A 1 127 ? 46.26658 -31.84047 13.28483 1.000 213.11020 ? 127 ASN A CG  1 
ATOM   1008 O OD1 . ASN A 1 127 ? 47.10055 -31.09314 12.77238 1.000 210.31795 ? 127 ASN A OD1 1 
ATOM   1009 N ND2 . ASN A 1 127 ? 46.36737 -33.16429 13.23850 1.000 205.63885 ? 127 ASN A ND2 1 
ATOM   1010 N N   . GLY A 1 128 ? 44.05107 -31.14317 10.71080 1.000 185.18760 ? 128 GLY A N   1 
ATOM   1011 C CA  . GLY A 1 128 ? 43.77570 -31.94206 9.53411  1.000 175.50057 ? 128 GLY A CA  1 
ATOM   1012 C C   . GLY A 1 128 ? 44.42635 -33.30695 9.58671  1.000 180.53954 ? 128 GLY A C   1 
ATOM   1013 O O   . GLY A 1 128 ? 45.65099 -33.42679 9.48905  1.000 195.67446 ? 128 GLY A O   1 
ATOM   1014 N N   . ALA A 1 129 ? 43.61204 -34.34480 9.75175  1.000 165.92862 ? 129 ALA A N   1 
ATOM   1015 C CA  . ALA A 1 129 ? 44.11181 -35.70709 9.82796  1.000 142.09071 ? 129 ALA A CA  1 
ATOM   1016 C C   . ALA A 1 129 ? 43.06843 -36.64436 9.24176  1.000 134.04989 ? 129 ALA A C   1 
ATOM   1017 O O   . ALA A 1 129 ? 41.92315 -36.25998 8.99061  1.000 139.18536 ? 129 ALA A O   1 
ATOM   1018 C CB  . ALA A 1 129 ? 44.45454 -36.10248 11.26846 1.000 139.64680 ? 129 ALA A CB  1 
ATOM   1019 N N   . SER A 1 130 ? 43.48431 -37.89278 9.02866  1.000 131.76521 ? 130 SER A N   1 
ATOM   1020 C CA  . SER A 1 130 ? 42.60255 -38.91087 8.47446  1.000 124.47434 ? 130 SER A CA  1 
ATOM   1021 C C   . SER A 1 130 ? 41.45817 -39.27457 9.40936  1.000 115.65535 ? 130 SER A C   1 
ATOM   1022 O O   . SER A 1 130 ? 40.51046 -39.93486 8.97024  1.000 109.50727 ? 130 SER A O   1 
ATOM   1023 C CB  . SER A 1 130 ? 43.41071 -40.16108 8.13325  1.000 124.54905 ? 130 SER A CB  1 
ATOM   1024 O OG  . SER A 1 130 ? 44.46639 -39.84961 7.23998  1.000 132.78723 ? 130 SER A OG  1 
ATOM   1025 N N   . ALA A 1 131 ? 41.52284 -38.86604 10.67470 1.000 119.66180 ? 131 ALA A N   1 
ATOM   1026 C CA  . ALA A 1 131 ? 40.45942 -39.10617 11.63677 1.000 107.28302 ? 131 ALA A CA  1 
ATOM   1027 C C   . ALA A 1 131 ? 40.02330 -37.78546 12.25515 1.000 108.71674 ? 131 ALA A C   1 
ATOM   1028 O O   . ALA A 1 131 ? 40.83204 -36.87189 12.43831 1.000 115.71744 ? 131 ALA A O   1 
ATOM   1029 C CB  . ALA A 1 131 ? 40.90386 -40.08105 12.73246 1.000 104.25519 ? 131 ALA A CB  1 
ATOM   1030 N N   . SER A 1 132 ? 38.73441 -37.68858 12.57492 1.000 102.22839 ? 132 SER A N   1 
ATOM   1031 C CA  . SER A 1 132 ? 38.19931 -36.45114 13.12446 1.000 103.05791 ? 132 SER A CA  1 
ATOM   1032 C C   . SER A 1 132 ? 36.93229 -36.74254 13.91455 1.000 101.56762 ? 132 SER A C   1 
ATOM   1033 O O   . SER A 1 132 ? 36.16147 -37.64405 13.57347 1.000 88.52861  ? 132 SER A O   1 
ATOM   1034 C CB  . SER A 1 132 ? 37.91051 -35.42788 12.02125 1.000 107.58250 ? 132 SER A CB  1 
ATOM   1035 O OG  . SER A 1 132 ? 37.27101 -34.27925 12.54781 1.000 107.79972 ? 132 SER A OG  1 
ATOM   1036 N N   . LEU A 1 133 ? 36.73018 -35.95922 14.97062 1.000 94.54669  ? 133 LEU A N   1 
ATOM   1037 C CA  . LEU A 1 133 ? 35.53191 -36.05440 15.78889 1.000 92.57827  ? 133 LEU A CA  1 
ATOM   1038 C C   . LEU A 1 133 ? 34.35389 -35.39783 15.07775 1.000 101.29046 ? 133 LEU A C   1 
ATOM   1039 O O   . LEU A 1 133 ? 34.52058 -34.47027 14.28067 1.000 96.00523  ? 133 LEU A O   1 
ATOM   1040 C CB  . LEU A 1 133 ? 35.76409 -35.38927 17.14731 1.000 87.97590  ? 133 LEU A CB  1 
ATOM   1041 C CG  . LEU A 1 133 ? 34.74928 -35.62080 18.27056 1.000 86.28578  ? 133 LEU A CG  1 
ATOM   1042 C CD1 . LEU A 1 133 ? 34.80988 -37.05921 18.75749 1.000 84.57500  ? 133 LEU A CD1 1 
ATOM   1043 C CD2 . LEU A 1 133 ? 34.98711 -34.65086 19.42143 1.000 82.98648  ? 133 LEU A CD2 1 
ATOM   1044 N N   . ASP A 1 134 ? 33.15290 -35.88934 15.37333 1.000 112.28780 ? 134 ASP A N   1 
ATOM   1045 C CA  . ASP A 1 134 ? 31.94944 -35.34821 14.76019 1.000 109.32253 ? 134 ASP A CA  1 
ATOM   1046 C C   . ASP A 1 134 ? 31.62781 -33.97469 15.34985 1.000 114.97546 ? 134 ASP A C   1 
ATOM   1047 O O   . ASP A 1 134 ? 32.30078 -33.47802 16.25801 1.000 111.02886 ? 134 ASP A O   1 
ATOM   1048 C CB  . ASP A 1 134 ? 30.78024 -36.31364 14.94201 1.000 105.40108 ? 134 ASP A CB  1 
ATOM   1049 C CG  . ASP A 1 134 ? 30.45772 -36.57208 16.39930 1.000 120.85727 ? 134 ASP A CG  1 
ATOM   1050 O OD1 . ASP A 1 134 ? 31.33879 -36.34802 17.25573 1.000 108.26596 ? 134 ASP A OD1 1 
ATOM   1051 O OD2 . ASP A 1 134 ? 29.32340 -37.00616 16.68835 1.000 103.47373 ? 134 ASP A OD2 1 
ATOM   1052 N N   . GLU A 1 135 ? 30.57911 -33.35220 14.81970 1.000 135.65264 ? 135 GLU A N   1 
ATOM   1053 C CA  . GLU A 1 135 ? 30.14599 -32.02688 15.24402 1.000 149.23860 ? 135 GLU A CA  1 
ATOM   1054 C C   . GLU A 1 135 ? 28.82579 -32.15565 15.99217 1.000 146.63047 ? 135 GLU A C   1 
ATOM   1055 O O   . GLU A 1 135 ? 27.84011 -32.65582 15.43915 1.000 158.29849 ? 135 GLU A O   1 
ATOM   1056 C CB  . GLU A 1 135 ? 30.00723 -31.08921 14.04490 1.000 162.11572 ? 135 GLU A CB  1 
ATOM   1057 C CG  . GLU A 1 135 ? 31.28165 -30.95824 13.22324 1.000 170.63791 ? 135 GLU A CG  1 
ATOM   1058 C CD  . GLU A 1 135 ? 31.15788 -29.94324 12.10424 1.000 201.63085 ? 135 GLU A CD  1 
ATOM   1059 O OE1 . GLU A 1 135 ? 30.13259 -29.23217 12.05416 1.000 205.45863 ? 135 GLU A OE1 1 
ATOM   1060 O OE2 . GLU A 1 135 ? 32.08720 -29.85613 11.27414 1.000 205.39215 ? 135 GLU A OE2 1 
ATOM   1061 N N   . GLN A 1 136 ? 28.81044 -31.69882 17.24318 1.000 133.38791 ? 136 GLN A N   1 
ATOM   1062 C CA  . GLN A 1 136 ? 27.66203 -31.85606 18.12455 1.000 139.42404 ? 136 GLN A CA  1 
ATOM   1063 C C   . GLN A 1 136 ? 27.82971 -30.89159 19.28756 1.000 147.68521 ? 136 GLN A C   1 
ATOM   1064 O O   . GLN A 1 136 ? 28.96402 -30.52143 19.61254 1.000 146.12452 ? 136 GLN A O   1 
ATOM   1065 C CB  . GLN A 1 136 ? 27.55848 -33.30469 18.62987 1.000 127.34323 ? 136 GLN A CB  1 
ATOM   1066 C CG  . GLN A 1 136 ? 26.15948 -33.76298 19.01066 1.000 147.26389 ? 136 GLN A CG  1 
ATOM   1067 C CD  . GLN A 1 136 ? 26.10067 -35.23919 19.34956 1.000 154.05404 ? 136 GLN A CD  1 
ATOM   1068 O OE1 . GLN A 1 136 ? 25.21658 -35.68474 20.08107 1.000 165.85675 ? 136 GLN A OE1 1 
ATOM   1069 N NE2 . GLN A 1 136 ? 27.04104 -36.00824 18.81226 1.000 122.40454 ? 136 GLN A NE2 1 
ATOM   1070 N N   . PRO A 1 137 ? 26.73890 -30.43951 19.90530 1.000 159.57125 ? 137 PRO A N   1 
ATOM   1071 C CA  . PRO A 1 137 ? 26.85348 -29.62496 21.12152 1.000 167.51668 ? 137 PRO A CA  1 
ATOM   1072 C C   . PRO A 1 137 ? 27.73824 -30.30050 22.15342 1.000 176.49781 ? 137 PRO A C   1 
ATOM   1073 O O   . PRO A 1 137 ? 27.61269 -31.50937 22.40092 1.000 173.76493 ? 137 PRO A O   1 
ATOM   1074 C CB  . PRO A 1 137 ? 25.40273 -29.52153 21.60874 1.000 168.47102 ? 137 PRO A CB  1 
ATOM   1075 C CG  . PRO A 1 137 ? 24.60999 -29.55206 20.35083 1.000 164.52298 ? 137 PRO A CG  1 
ATOM   1076 C CD  . PRO A 1 137 ? 25.35606 -30.45683 19.39251 1.000 159.56926 ? 137 PRO A CD  1 
ATOM   1077 N N   . PRO A 1 138 ? 28.65009 -29.55094 22.77527 1.000 183.28189 ? 138 PRO A N   1 
ATOM   1078 C CA  . PRO A 1 138 ? 29.64221 -30.17065 23.66469 1.000 171.56030 ? 138 PRO A CA  1 
ATOM   1079 C C   . PRO A 1 138 ? 29.06486 -30.61658 24.99997 1.000 170.38667 ? 138 PRO A C   1 
ATOM   1080 O O   . PRO A 1 138 ? 29.16786 -29.90711 26.00492 1.000 167.93971 ? 138 PRO A O   1 
ATOM   1081 C CB  . PRO A 1 138 ? 30.68000 -29.05759 23.84744 1.000 160.21506 ? 138 PRO A CB  1 
ATOM   1082 C CG  . PRO A 1 138 ? 29.89999 -27.79644 23.67761 1.000 173.23364 ? 138 PRO A CG  1 
ATOM   1083 C CD  . PRO A 1 138 ? 28.84483 -28.09619 22.64858 1.000 181.38917 ? 138 PRO A CD  1 
ATOM   1084 N N   . SER A 1 139 ? 28.46278 -31.80240 25.02167 1.000 176.72250 ? 139 SER A N   1 
ATOM   1085 C CA  . SER A 1 139 ? 27.93460 -32.37826 26.24908 1.000 174.38944 ? 139 SER A CA  1 
ATOM   1086 C C   . SER A 1 139 ? 28.02369 -33.89442 26.15829 1.000 175.64614 ? 139 SER A C   1 
ATOM   1087 O O   . SER A 1 139 ? 28.07388 -34.46967 25.06776 1.000 173.88217 ? 139 SER A O   1 
ATOM   1088 C CB  . SER A 1 139 ? 26.48956 -31.93576 26.50596 1.000 174.45820 ? 139 SER A CB  1 
ATOM   1089 O OG  . SER A 1 139 ? 25.64106 -32.31731 25.43991 1.000 190.34755 ? 139 SER A OG  1 
ATOM   1090 N N   . LEU A 1 140 ? 28.04378 -34.53850 27.32321 1.000 166.39198 ? 140 LEU A N   1 
ATOM   1091 C CA  A LEU A 1 140 ? 28.14148 -35.99528 27.42104 0.505 161.57761 ? 140 LEU A CA  1 
ATOM   1092 C CA  B LEU A 1 140 ? 28.14464 -35.99527 27.40339 0.495 161.58394 ? 140 LEU A CA  1 
ATOM   1093 C C   . LEU A 1 140 ? 26.78315 -36.67457 27.36389 1.000 171.22234 ? 140 LEU A C   1 
ATOM   1094 O O   . LEU A 1 140 ? 26.55633 -37.67266 28.05379 1.000 174.48626 ? 140 LEU A O   1 
ATOM   1095 C CB  A LEU A 1 140 ? 28.87791 -36.37944 28.70001 0.505 152.46839 ? 140 LEU A CB  1 
ATOM   1096 C CB  B LEU A 1 140 ? 28.91293 -36.38607 28.66111 0.495 152.47018 ? 140 LEU A CB  1 
ATOM   1097 C CG  A LEU A 1 140 ? 30.38674 -36.14480 28.73702 0.505 144.21106 ? 140 LEU A CG  1 
ATOM   1098 C CG  B LEU A 1 140 ? 30.07599 -37.35256 28.43405 0.495 144.69901 ? 140 LEU A CG  1 
ATOM   1099 C CD1 A LEU A 1 140 ? 30.98568 -36.74340 30.00036 0.505 139.45444 ? 140 LEU A CD1 1 
ATOM   1100 C CD1 B LEU A 1 140 ? 30.94632 -36.86359 27.28929 0.495 138.00048 ? 140 LEU A CD1 1 
ATOM   1101 C CD2 A LEU A 1 140 ? 31.04300 -36.73221 27.50133 0.505 137.63586 ? 140 LEU A CD2 1 
ATOM   1102 C CD2 B LEU A 1 140 ? 30.89988 -37.50770 29.69928 0.495 141.95571 ? 140 LEU A CD2 1 
ATOM   1103 N N   . ASP A 1 141 ? 25.85884 -36.15891 26.55342 1.000 198.32350 ? 141 ASP A N   1 
ATOM   1104 C CA  . ASP A 1 141 ? 24.53156 -36.75682 26.46546 1.000 199.06353 ? 141 ASP A CA  1 
ATOM   1105 C C   . ASP A 1 141 ? 24.51770 -37.95027 25.51584 1.000 190.12162 ? 141 ASP A C   1 
ATOM   1106 O O   . ASP A 1 141 ? 23.97249 -39.00874 25.84652 1.000 192.19879 ? 141 ASP A O   1 
ATOM   1107 C CB  . ASP A 1 141 ? 23.51057 -35.70408 26.02603 1.000 214.47531 ? 141 ASP A CB  1 
ATOM   1108 C CG  . ASP A 1 141 ? 23.95675 -34.93514 24.79677 1.000 220.16274 ? 141 ASP A CG  1 
ATOM   1109 O OD1 . ASP A 1 141 ? 25.09717 -35.15517 24.33681 1.000 212.76507 ? 141 ASP A OD1 1 
ATOM   1110 O OD2 . ASP A 1 141 ? 23.16710 -34.11114 24.28980 1.000 225.93111 ? 141 ASP A OD2 1 
ATOM   1111 N N   . LYS A 1 142 ? 25.11559 -37.80232 24.33796 1.000 144.35045 ? 142 LYS A N   1 
ATOM   1112 C CA  . LYS A 1 142 ? 25.09558 -38.83195 23.31060 1.000 113.84600 ? 142 LYS A CA  1 
ATOM   1113 C C   . LYS A 1 142 ? 26.51192 -39.29914 23.00043 1.000 103.96248 ? 142 LYS A C   1 
ATOM   1114 O O   . LYS A 1 142 ? 27.50176 -38.72086 23.45649 1.000 94.92952  ? 142 LYS A O   1 
ATOM   1115 C CB  . LYS A 1 142 ? 24.41503 -38.32179 22.03405 1.000 109.79684 ? 142 LYS A CB  1 
ATOM   1116 C CG  . LYS A 1 142 ? 22.96198 -37.92354 22.22586 1.000 121.26824 ? 142 LYS A CG  1 
ATOM   1117 C CD  . LYS A 1 142 ? 22.33608 -37.47294 20.91746 1.000 120.67612 ? 142 LYS A CD  1 
ATOM   1118 C CE  . LYS A 1 142 ? 20.86363 -37.14607 21.09716 1.000 120.69182 ? 142 LYS A CE  1 
ATOM   1119 N NZ  . LYS A 1 142 ? 20.21515 -36.77791 19.80857 1.000 122.36110 ? 142 LYS A NZ  1 
ATOM   1120 N N   . THR A 1 143 ? 26.59305 -40.36666 22.20967 1.000 110.97023 ? 143 THR A N   1 
ATOM   1121 C CA  . THR A 1 143 ? 27.87489 -40.91425 21.78903 1.000 101.12468 ? 143 THR A CA  1 
ATOM   1122 C C   . THR A 1 143 ? 28.45468 -40.07229 20.65989 1.000 86.27657  ? 143 THR A C   1 
ATOM   1123 O O   . THR A 1 143 ? 27.76782 -39.77923 19.67646 1.000 96.08927  ? 143 THR A O   1 
ATOM   1124 C CB  . THR A 1 143 ? 27.71314 -42.36623 21.33794 1.000 87.43951  ? 143 THR A CB  1 
ATOM   1125 O OG1 . THR A 1 143 ? 27.27232 -43.16597 22.44235 1.000 102.23922 ? 143 THR A OG1 1 
ATOM   1126 C CG2 . THR A 1 143 ? 29.03189 -42.91746 20.81692 1.000 82.45155  ? 143 THR A CG2 1 
ATOM   1127 N N   . ARG A 1 144 ? 29.71862 -39.68405 20.80418 1.000 70.39836  ? 144 ARG A N   1 
ATOM   1128 C CA  . ARG A 1 144 ? 30.39797 -38.85311 19.81856 1.000 96.31743  ? 144 ARG A CA  1 
ATOM   1129 C C   . ARG A 1 144 ? 31.13564 -39.74330 18.82489 1.000 80.18393  ? 144 ARG A C   1 
ATOM   1130 O O   . ARG A 1 144 ? 32.04901 -40.48337 19.20497 1.000 81.12960  ? 144 ARG A O   1 
ATOM   1131 C CB  . ARG A 1 144 ? 31.36784 -37.89269 20.50542 1.000 86.50359  ? 144 ARG A CB  1 
ATOM   1132 C CG  . ARG A 1 144 ? 30.70495 -36.94131 21.48665 1.000 89.01585  ? 144 ARG A CG  1 
ATOM   1133 C CD  . ARG A 1 144 ? 29.82711 -35.93104 20.76820 1.000 87.14672  ? 144 ARG A CD  1 
ATOM   1134 N NE  . ARG A 1 144 ? 30.61178 -35.02238 19.94045 1.000 98.85656  ? 144 ARG A NE  1 
ATOM   1135 C CZ  . ARG A 1 144 ? 31.10871 -33.86751 20.36225 1.000 105.03023 ? 144 ARG A CZ  1 
ATOM   1136 N NH1 . ARG A 1 144 ? 30.91867 -33.44486 21.60115 1.000 103.61311 ? 144 ARG A NH1 1 
ATOM   1137 N NH2 . ARG A 1 144 ? 31.81388 -33.11758 19.52009 1.000 87.50615  ? 144 ARG A NH2 1 
ATOM   1138 N N   . LYS A 1 145 ? 30.74863 -39.66196 17.55644 1.000 93.01316  ? 145 LYS A N   1 
ATOM   1139 C CA  . LYS A 1 145 ? 31.36911 -40.47400 16.52169 1.000 73.57127  ? 145 LYS A CA  1 
ATOM   1140 C C   . LYS A 1 145 ? 32.73600 -39.91967 16.13416 1.000 74.75817  ? 145 LYS A C   1 
ATOM   1141 O O   . LYS A 1 145 ? 33.00441 -38.72034 16.25088 1.000 79.35507  ? 145 LYS A O   1 
ATOM   1142 C CB  . LYS A 1 145 ? 30.46818 -40.54519 15.28858 1.000 97.92581  ? 145 LYS A CB  1 
ATOM   1143 C CG  . LYS A 1 145 ? 29.24442 -41.43172 15.45620 1.000 95.53351  ? 145 LYS A CG  1 
ATOM   1144 C CD  . LYS A 1 145 ? 28.25618 -41.20809 14.32545 1.000 84.60414  ? 145 LYS A CD  1 
ATOM   1145 C CE  . LYS A 1 145 ? 27.52852 -42.49114 13.95457 1.000 92.94765  ? 145 LYS A CE  1 
ATOM   1146 N NZ  . LYS A 1 145 ? 26.81166 -43.10328 15.10536 1.000 92.45389  ? 145 LYS A NZ  1 
ATOM   1147 N N   . ILE A 1 146 ? 33.60765 -40.81671 15.67820 1.000 84.86736  ? 146 ILE A N   1 
ATOM   1148 C CA  . ILE A 1 146 ? 34.92177 -40.46314 15.15209 1.000 77.48369  ? 146 ILE A CA  1 
ATOM   1149 C C   . ILE A 1 146 ? 35.05732 -41.12368 13.78708 1.000 79.08218  ? 146 ILE A C   1 
ATOM   1150 O O   . ILE A 1 146 ? 34.95848 -42.35186 13.67688 1.000 80.68612  ? 146 ILE A O   1 
ATOM   1151 C CB  . ILE A 1 146 ? 36.06215 -40.90239 16.08653 1.000 91.18355  ? 146 ILE A CB  1 
ATOM   1152 C CG1 . ILE A 1 146 ? 35.84542 -40.34620 17.49559 1.000 87.26350  ? 146 ILE A CG1 1 
ATOM   1153 C CG2 . ILE A 1 146 ? 37.40450 -40.44312 15.53998 1.000 74.64670  ? 146 ILE A CG2 1 
ATOM   1154 C CD1 . ILE A 1 146 ? 36.91974 -40.74369 18.48479 1.000 73.39430  ? 146 ILE A CD1 1 
ATOM   1155 N N   . TYR A 1 147 ? 35.27767 -40.31541 12.75383 1.000 93.70662  ? 147 TYR A N   1 
ATOM   1156 C CA  . TYR A 1 147 ? 35.28390 -40.77933 11.37234 1.000 88.03448  ? 147 TYR A CA  1 
ATOM   1157 C C   . TYR A 1 147 ? 36.70401 -41.08165 10.91272 1.000 87.29337  ? 147 TYR A C   1 
ATOM   1158 O O   . TYR A 1 147 ? 37.63166 -40.31862 11.19160 1.000 83.49061  ? 147 TYR A O   1 
ATOM   1159 C CB  . TYR A 1 147 ? 34.65198 -39.73331 10.45220 1.000 85.64064  ? 147 TYR A CB  1 
ATOM   1160 C CG  . TYR A 1 147 ? 33.25399 -39.32947 10.86120 1.000 85.06104  ? 147 TYR A CG  1 
ATOM   1161 C CD1 . TYR A 1 147 ? 32.16639 -40.14280 10.57696 1.000 90.55510  ? 147 TYR A CD1 1 
ATOM   1162 C CD2 . TYR A 1 147 ? 33.02083 -38.13507 11.52896 1.000 100.17516 ? 147 TYR A CD2 1 
ATOM   1163 C CE1 . TYR A 1 147 ? 30.88548 -39.78132 10.94865 1.000 87.48565  ? 147 TYR A CE1 1 
ATOM   1164 C CE2 . TYR A 1 147 ? 31.74230 -37.76418 11.90310 1.000 87.36889  ? 147 TYR A CE2 1 
ATOM   1165 C CZ  . TYR A 1 147 ? 30.67868 -38.59139 11.61082 1.000 101.60475 ? 147 TYR A CZ  1 
ATOM   1166 O OH  . TYR A 1 147 ? 29.40362 -38.22841 11.98108 1.000 95.25289  ? 147 TYR A OH  1 
ATOM   1167 N N   . ASN A 1 148 ? 36.86512 -42.19407 10.19690 1.000 87.84635  ? 148 ASN A N   1 
ATOM   1168 C CA  . ASN A 1 148 ? 38.16378 -42.63126 9.69904  1.000 89.18642  ? 148 ASN A CA  1 
ATOM   1169 C C   . ASN A 1 148 ? 38.09475 -42.83503 8.19251  1.000 101.99799 ? 148 ASN A C   1 
ATOM   1170 O O   . ASN A 1 148 ? 37.16150 -43.46946 7.69037  1.000 95.33839  ? 148 ASN A O   1 
ATOM   1171 C CB  . ASN A 1 148 ? 38.61230 -43.92544 10.38530 1.000 89.30914  ? 148 ASN A CB  1 
ATOM   1172 C CG  . ASN A 1 148 ? 38.96267 -43.71900 11.84359 1.000 99.88147  ? 148 ASN A CG  1 
ATOM   1173 O OD1 . ASN A 1 148 ? 40.11699 -43.44554 12.17406 1.000 87.21035  ? 148 ASN A OD1 1 
ATOM   1174 N N   . LYS A 1 149 ? 39.08728 -42.30770 7.47896  1.000 93.67771  ? 149 LYS A N   1 
ATOM   1175 C CA  . LYS A 1 149 ? 39.14170 -42.40362 6.02494  1.000 97.24063  ? 149 LYS A CA  1 
ATOM   1176 C C   . LYS A 1 149 ? 39.85123 -43.69069 5.62167  1.000 99.69703  ? 149 LYS A C   1 
ATOM   1177 O O   . LYS A 1 149 ? 41.00120 -43.92054 6.01034  1.000 98.82678  ? 149 LYS A O   1 
ATOM   1178 C CB  . LYS A 1 149 ? 39.85245 -41.18907 5.42910  1.000 97.04918  ? 149 LYS A CB  1 
ATOM   1179 C CG  . LYS A 1 149 ? 39.11010 -39.87779 5.62962  1.000 105.23756 ? 149 LYS A CG  1 
ATOM   1180 C CD  . LYS A 1 149 ? 39.86946 -38.70974 5.02106  1.000 95.84145  ? 149 LYS A CD  1 
ATOM   1181 C CE  . LYS A 1 149 ? 39.13392 -37.39743 5.24463  1.000 102.22542 ? 149 LYS A CE  1 
ATOM   1182 N NZ  . LYS A 1 149 ? 39.85421 -36.24138 4.64255  1.000 95.61665  ? 149 LYS A NZ  1 
ATOM   1183 N N   . LYS A 1 150 ? 39.16666 -44.52314 4.84284  1.000 105.00644 ? 150 LYS A N   1 
ATOM   1184 C CA  . LYS A 1 150 ? 39.74480 -45.77213 4.37356  1.000 106.54709 ? 150 LYS A CA  1 
ATOM   1185 C C   . LYS A 1 150 ? 40.70178 -45.51461 3.21642  1.000 108.19856 ? 150 LYS A C   1 
ATOM   1186 O O   . LYS A 1 150 ? 40.49811 -44.61144 2.40108  1.000 108.87541 ? 150 LYS A O   1 
ATOM   1187 C CB  . LYS A 1 150 ? 38.64494 -46.74548 3.94385  1.000 109.47629 ? 150 LYS A CB  1 
ATOM   1188 C CG  . LYS A 1 150 ? 39.12126 -48.17556 3.72754  1.000 122.49608 ? 150 LYS A CG  1 
ATOM   1189 C CD  . LYS A 1 150 ? 37.97757 -49.07746 3.28721  1.000 116.41185 ? 150 LYS A CD  1 
ATOM   1190 C CE  . LYS A 1 150 ? 38.44121 -50.51370 3.09361  1.000 133.02376 ? 150 LYS A CE  1 
ATOM   1191 N NZ  . LYS A 1 150 ? 37.32653 -51.39738 2.64861  1.000 146.90492 ? 150 LYS A NZ  1 
ATOM   1192 N N   . ALA A 1 151 ? 41.76147 -46.31666 3.15945  1.000 109.40189 ? 151 ALA A N   1 
ATOM   1193 C CA  . ALA A 1 151 ? 42.77321 -46.20455 2.11467  1.000 122.34708 ? 151 ALA A CA  1 
ATOM   1194 C C   . ALA A 1 151 ? 42.30714 -46.99285 0.89551  1.000 116.19727 ? 151 ALA A C   1 
ATOM   1195 O O   . ALA A 1 151 ? 42.22966 -48.22539 0.93492  1.000 118.62740 ? 151 ALA A O   1 
ATOM   1196 C CB  . ALA A 1 151 ? 44.12354 -46.70971 2.61536  1.000 110.96920 ? 151 ALA A CB  1 
ATOM   1197 N N   . VAL A 1 152 ? 41.99690 -46.28383 -0.18433 1.000 120.01195 ? 152 VAL A N   1 
ATOM   1198 C CA  . VAL A 1 152 ? 41.53435 -46.92002 -1.41249 1.000 122.59263 ? 152 VAL A CA  1 
ATOM   1199 C C   . VAL A 1 152 ? 42.72431 -47.54745 -2.12556 1.000 125.13626 ? 152 VAL A C   1 
ATOM   1200 O O   . VAL A 1 152 ? 43.78307 -46.92288 -2.26167 1.000 123.74286 ? 152 VAL A O   1 
ATOM   1201 C CB  . VAL A 1 152 ? 40.81771 -45.90293 -2.31454 1.000 123.68707 ? 152 VAL A CB  1 
ATOM   1202 C CG1 . VAL A 1 152 ? 40.10978 -46.61490 -3.46054 1.000 128.90545 ? 152 VAL A CG1 1 
ATOM   1203 C CG2 . VAL A 1 152 ? 39.83747 -45.07091 -1.50310 1.000 120.63647 ? 152 VAL A CG2 1 
ATOM   1204 N N   . LYS A 1 153 ? 42.55440 -48.78519 -2.58078 1.000 138.20283 ? 153 LYS A N   1 
ATOM   1205 C CA  . LYS A 1 153 ? 43.59292 -49.50511 -3.30373 1.000 156.79488 ? 153 LYS A CA  1 
ATOM   1206 C C   . LYS A 1 153 ? 43.36792 -49.38227 -4.80494 1.000 149.49319 ? 153 LYS A C   1 
ATOM   1207 O O   . LYS A 1 153 ? 42.22551 -49.38763 -5.27393 1.000 148.10622 ? 153 LYS A O   1 
ATOM   1208 C CB  . LYS A 1 153 ? 43.62110 -50.98094 -2.89971 1.000 172.48213 ? 153 LYS A CB  1 
ATOM   1209 C CG  . LYS A 1 153 ? 44.09584 -51.23106 -1.47667 1.000 183.17352 ? 153 LYS A CG  1 
ATOM   1210 C CD  . LYS A 1 153 ? 45.53953 -50.78978 -1.28888 1.000 189.88913 ? 153 LYS A CD  1 
ATOM   1211 C CE  . LYS A 1 153 ? 46.04147 -51.11453 0.10959  1.000 202.06730 ? 153 LYS A CE  1 
ATOM   1212 N NZ  . LYS A 1 153 ? 46.05452 -52.58066 0.37093  1.000 212.49103 ? 153 LYS A NZ  1 
ATOM   1213 N N   . LEU A 1 154 ? 44.46708 -49.27366 -5.54896 1.000 137.49300 ? 154 LEU A N   1 
ATOM   1214 C CA  . LEU A 1 154 ? 44.43685 -49.14002 -7.00539 1.000 141.42193 ? 154 LEU A CA  1 
ATOM   1215 C C   . LEU A 1 154 ? 43.55854 -47.97404 -7.45268 1.000 140.80270 ? 154 LEU A C   1 
ATOM   1216 O O   . LEU A 1 154 ? 43.99430 -47.11456 -8.21832 1.000 140.98469 ? 154 LEU A O   1 
ATOM   1217 C CB  . LEU A 1 154 ? 43.95470 -50.43947 -7.65665 1.000 146.83651 ? 154 LEU A CB  1 
ATOM   1218 C CG  . LEU A 1 154 ? 43.87565 -50.43001 -9.18510 1.000 152.84901 ? 154 LEU A CG  1 
ATOM   1219 C CD1 . LEU A 1 154 ? 45.23516 -50.12009 -9.79519 1.000 151.56676 ? 154 LEU A CD1 1 
ATOM   1220 C CD2 . LEU A 1 154 ? 43.34151 -51.75509 -9.70597 1.000 157.15704 ? 154 LEU A CD2 1 
HETATM 1221 S S   . SO4 B 2 .   ? 49.52156 -19.60238 37.94800 0.652 86.06754  ? 201 SO4 A S   1 
HETATM 1222 O O1  . SO4 B 2 .   ? 50.58635 -19.45840 36.95993 0.652 81.37102  ? 201 SO4 A O1  1 
HETATM 1223 O O2  . SO4 B 2 .   ? 48.45196 -18.65525 37.65004 0.652 89.85905  ? 201 SO4 A O2  1 
HETATM 1224 O O3  . SO4 B 2 .   ? 48.98894 -20.96092 37.90164 0.652 66.55693  ? 201 SO4 A O3  1 
HETATM 1225 O O4  . SO4 B 2 .   ? 50.05557 -19.33268 39.27967 0.652 99.27266  ? 201 SO4 A O4  1 
HETATM 1226 S S   . SO4 C 2 .   ? 41.06881 -22.94436 25.22808 0.658 124.66323 ? 202 SO4 A S   1 
HETATM 1227 O O1  . SO4 C 2 .   ? 41.80416 -24.00952 24.55199 0.658 98.94203  ? 202 SO4 A O1  1 
HETATM 1228 O O2  . SO4 C 2 .   ? 40.07199 -22.38699 24.31870 0.658 115.90810 ? 202 SO4 A O2  1 
HETATM 1229 O O3  . SO4 C 2 .   ? 40.39995 -23.48438 26.40840 0.658 108.96798 ? 202 SO4 A O3  1 
HETATM 1230 O O4  . SO4 C 2 .   ? 41.99850 -21.89430 25.63355 0.658 120.99394 ? 202 SO4 A O4  1 
HETATM 1231 S S   . SO4 D 2 .   ? 43.46792 -35.96628 42.01257 0.709 121.85590 ? 203 SO4 A S   1 
HETATM 1232 O O1  . SO4 D 2 .   ? 42.16983 -35.82603 42.66591 0.709 118.35107 ? 203 SO4 A O1  1 
HETATM 1233 O O2  . SO4 D 2 .   ? 43.36984 -35.48897 40.63713 0.709 119.89994 ? 203 SO4 A O2  1 
HETATM 1234 O O3  . SO4 D 2 .   ? 44.46280 -35.17622 42.73217 0.709 111.10243 ? 203 SO4 A O3  1 
HETATM 1235 O O4  . SO4 D 2 .   ? 43.86587 -37.37134 42.00969 0.709 98.28391  ? 203 SO4 A O4  1 
HETATM 1236 S S   . SO4 E 2 .   ? 43.04430 -41.73872 33.98958 0.752 129.98200 ? 204 SO4 A S   1 
HETATM 1237 O O1  . SO4 E 2 .   ? 43.08656 -41.00856 32.72561 0.752 76.73128  ? 204 SO4 A O1  1 
HETATM 1238 O O2  . SO4 E 2 .   ? 41.87329 -41.31870 34.75392 0.752 111.29182 ? 204 SO4 A O2  1 
HETATM 1239 O O3  . SO4 E 2 .   ? 42.96184 -43.17138 33.72172 0.752 116.26794 ? 204 SO4 A O3  1 
HETATM 1240 O O4  . SO4 E 2 .   ? 44.25400 -41.45837 34.75761 0.752 94.47545  ? 204 SO4 A O4  1 
HETATM 1241 S S   . SO4 F 2 .   ? 51.18576 -33.44272 42.88029 0.453 115.26105 ? 205 SO4 A S   1 
HETATM 1242 O O1  . SO4 F 2 .   ? 51.87061 -33.95817 41.69864 0.453 98.47930  ? 205 SO4 A O1  1 
HETATM 1243 O O2  . SO4 F 2 .   ? 51.40701 -34.35031 44.00261 0.453 71.99536  ? 205 SO4 A O2  1 
HETATM 1244 O O3  . SO4 F 2 .   ? 51.71089 -32.12159 43.21154 0.453 95.97673  ? 205 SO4 A O3  1 
HETATM 1245 O O4  . SO4 F 2 .   ? 49.75650 -33.33824 42.60322 0.453 85.70481  ? 205 SO4 A O4  1 
HETATM 1246 S S   . SO4 G 2 .   ? 52.71197 -14.55770 37.86868 0.611 120.64417 ? 206 SO4 A S   1 
HETATM 1247 O O1  . SO4 G 2 .   ? 54.02136 -13.95467 38.10118 0.611 96.53512  ? 206 SO4 A O1  1 
HETATM 1248 O O2  . SO4 G 2 .   ? 52.67997 -15.15240 36.53579 0.611 116.31293 ? 206 SO4 A O2  1 
HETATM 1249 O O3  . SO4 G 2 .   ? 52.46774 -15.59378 38.86815 0.611 95.16336  ? 206 SO4 A O3  1 
HETATM 1250 O O4  . SO4 G 2 .   ? 51.67862 -13.53093 37.96821 0.611 111.67245 ? 206 SO4 A O4  1 
HETATM 1251 O O   . HOH H 3 .   ? 31.28399 -39.45235 0.11572  1.000 107.55308 ? 301 HOH A O   1 
HETATM 1252 O O   . HOH H 3 .   ? 52.27723 -18.31948 35.97097 1.000 90.77583  ? 302 HOH A O   1 
HETATM 1253 O O   . HOH H 3 .   ? 52.81713 -32.96479 45.13078 1.000 90.11250  ? 303 HOH A O   1 
HETATM 1254 O O   . HOH H 3 .   ? 47.654   -32.497   42.365   1.000 107.61214 ? 304 HOH A O   1 
HETATM 1255 O O   . HOH H 3 .   ? 29.96821 -34.24266 23.78177 1.000 117.28722 ? 305 HOH A O   1 
HETATM 1256 O O   . HOH H 3 .   ? 32.55286 -27.92208 31.43795 1.000 120.77488 ? 306 HOH A O   1 
HETATM 1257 O O   . HOH H 3 .   ? 40.20980 -42.31653 1.98989  1.000 104.51159 ? 307 HOH A O   1 
HETATM 1258 O O   . HOH H 3 .   ? 43.166   -45.507   34.059   1.000 109.02243 ? 308 HOH A O   1 
HETATM 1259 O O   . HOH H 3 .   ? 42.29656 -33.59733 41.61330 1.000 96.33553  ? 309 HOH A O   1 
HETATM 1260 O O   . HOH H 3 .   ? 50.733   -16.989   39.729   1.000 101.55124 ? 310 HOH A O   1 
HETATM 1261 O O   . HOH H 3 .   ? 45.10571 -51.12677 14.15449 1.000 110.78158 ? 311 HOH A O   1 
HETATM 1262 O O   . HOH H 3 .   ? 52.817   -30.007   43.662   1.000 96.93016  ? 312 HOH A O   1 
HETATM 1263 O O   . HOH H 3 .   ? 39.63476 -21.61707 27.76807 1.000 100.64897 ? 313 HOH A O   1 
HETATM 1264 O O   . HOH H 3 .   ? 34.60126 -51.67643 21.34961 1.000 69.71070  ? 314 HOH A O   1 
HETATM 1265 O O   . HOH H 3 .   ? 46.32652 -39.34301 10.27250 1.000 95.21652  ? 315 HOH A O   1 
HETATM 1266 O O   . HOH H 3 .   ? 41.94307 -18.78924 32.61458 1.000 108.45412 ? 316 HOH A O   1 
HETATM 1267 O O   . HOH H 3 .   ? 39.01920 -25.91424 38.77580 1.000 108.99218 ? 317 HOH A O   1 
HETATM 1268 O O   . HOH H 3 .   ? 28.14250 -48.74424 34.38536 0.50  119.54081 ? 318 HOH A O   1 
HETATM 1269 O O   . HOH H 3 .   ? 42.34874 -27.03949 20.98343 1.000 115.90014 ? 319 HOH A O   1 
HETATM 1270 O O   . HOH H 3 .   ? 56.28500 -32.49616 30.66782 0.33  87.90831  ? 320 HOH A O   1 
HETATM 1271 O O   . HOH H 3 .   ? 28.14293 -44.58525 11.62851 1.000 76.87883  ? 321 HOH A O   1 
HETATM 1272 O O   . HOH H 3 .   ? 55.801   -30.392   27.488   1.000 113.20027 ? 322 HOH A O   1 
HETATM 1273 O O   . HOH H 3 .   ? 50.34586 -35.92512 42.35000 0.50  96.93576  ? 323 HOH A O   1 
HETATM 1274 O O   . HOH H 3 .   ? 49.59248 -30.67311 12.87883 1.000 135.03704 ? 324 HOH A O   1 
HETATM 1275 O O   . HOH H 3 .   ? 44.25536 -25.22837 32.14976 1.000 93.29107  ? 325 HOH A O   1 
HETATM 1276 O O   . HOH H 3 .   ? 36.97370 -29.66165 25.90554 1.000 102.88820 ? 326 HOH A O   1 
HETATM 1277 O O   . HOH H 3 .   ? 29.57278 -38.83664 24.97234 1.000 103.04031 ? 327 HOH A O   1 
HETATM 1278 O O   . HOH H 3 .   ? 53.911   -32.463   41.198   1.000 105.37653 ? 328 HOH A O   1 
HETATM 1279 O O   . HOH H 3 .   ? 57.043   -29.933   20.160   1.000 133.56463 ? 329 HOH A O   1 
HETATM 1280 O O   . HOH H 3 .   ? 54.973   -27.322   36.816   1.000 77.71430  ? 330 HOH A O   1 
HETATM 1281 O O   . HOH H 3 .   ? 36.67471 -44.05567 4.31051  1.000 102.81555 ? 331 HOH A O   1 
HETATM 1282 O O   . HOH H 3 .   ? 26.22870 -40.99540 17.97689 1.000 87.76256  ? 332 HOH A O   1 
HETATM 1283 O O   . HOH H 3 .   ? 32.83557 -47.76465 35.38599 1.000 124.60913 ? 333 HOH A O   1 
HETATM 1284 O O   . HOH H 3 .   ? 52.254   -46.244   30.967   1.000 82.52898  ? 334 HOH A O   1 
HETATM 1285 O O   . HOH H 3 .   ? 43.01503 -27.19837 18.10165 1.000 114.20689 ? 335 HOH A O   1 
HETATM 1286 O O   . HOH H 3 .   ? 25.46407 -33.03607 22.35679 1.000 163.73350 ? 336 HOH A O   1 
HETATM 1287 O O   . HOH H 3 .   ? 43.37129 -39.95190 42.35000 0.50  124.68920 ? 337 HOH A O   1 
HETATM 1288 O O   . HOH H 3 .   ? 35.07643 -47.49599 3.19326  1.000 94.93835  ? 338 HOH A O   1 
HETATM 1289 O O   . HOH H 3 .   ? 47.07386 -40.41873 7.15241  1.000 98.59122  ? 339 HOH A O   1 
HETATM 1290 O O   . HOH H 3 .   ? 31.17802 -52.03438 25.61029 1.000 118.91300 ? 340 HOH A O   1 
HETATM 1291 O O   . HOH H 3 .   ? 36.39815 -49.26744 25.91593 1.000 78.61812  ? 341 HOH A O   1 
HETATM 1292 O O   . HOH H 3 .   ? 52.56252 -41.13379 23.40903 1.000 114.20329 ? 342 HOH A O   1 
HETATM 1293 O O   . HOH H 3 .   ? 28.34431 -41.63182 31.53257 1.000 130.94879 ? 343 HOH A O   1 
HETATM 1294 O O   . HOH H 3 .   ? 48.93323 -28.97725 19.59662 1.000 139.40356 ? 344 HOH A O   1 
HETATM 1295 O O   . HOH H 3 .   ? 54.90995 -40.36398 18.14835 1.000 123.50144 ? 345 HOH A O   1 
HETATM 1296 O O   . HOH H 3 .   ? 19.55023 -39.25735 18.86214 1.000 88.11416  ? 346 HOH A O   1 
HETATM 1297 O O   . HOH H 3 .   ? 48.419   -49.874   27.162   1.000 105.73983 ? 347 HOH A O   1 
HETATM 1298 O O   . HOH H 3 .   ? 37.98456 -32.17576 38.81910 1.000 110.97356 ? 348 HOH A O   1 
HETATM 1299 O O   . HOH H 3 .   ? 44.95636 -21.30858 32.53293 1.000 92.74987  ? 349 HOH A O   1 
HETATM 1300 O O   . HOH H 3 .   ? 38.35220 -29.92703 37.38619 1.000 92.57091  ? 350 HOH A O   1 
HETATM 1301 O O   . HOH H 3 .   ? 39.21505 -44.15550 31.00117 1.000 107.99401 ? 351 HOH A O   1 
HETATM 1302 O O   . HOH H 3 .   ? 43.44795 -36.30547 45.13257 1.000 98.37008  ? 352 HOH A O   1 
HETATM 1303 O O   . HOH H 3 .   ? 44.317   -40.584   38.941   1.000 101.78551 ? 353 HOH A O   1 
HETATM 1304 O O   . HOH H 3 .   ? 27.76417 -42.70819 6.62875  1.000 95.97688  ? 354 HOH A O   1 
HETATM 1305 O O   . HOH H 3 .   ? 33.98691 -26.20446 29.65097 1.000 123.70341 ? 355 HOH A O   1 
HETATM 1306 O O   . HOH H 3 .   ? 32.50737 -53.16662 23.82320 1.000 99.58444  ? 356 HOH A O   1 
HETATM 1307 O O   . HOH H 3 .   ? 45.08278 -15.04699 32.99153 1.000 92.89772  ? 357 HOH A O   1 
HETATM 1308 O O   . HOH H 3 .   ? 38.61434 -23.20286 29.30724 1.000 107.13199 ? 358 HOH A O   1 
HETATM 1309 O O   . HOH H 3 .   ? 39.78782 -50.59100 28.36487 1.000 112.96550 ? 359 HOH A O   1 
HETATM 1310 O O   . HOH H 3 .   ? 39.29707 -34.47151 15.88987 1.000 93.28825  ? 360 HOH A O   1 
HETATM 1311 O O   . HOH H 3 .   ? 47.80639 -45.66012 11.91828 1.000 90.34153  ? 361 HOH A O   1 
HETATM 1312 O O   . HOH H 3 .   ? 38.45396 -22.39131 32.16511 1.000 95.80188  ? 362 HOH A O   1 
HETATM 1313 O O   . HOH H 3 .   ? 50.82853 -44.37522 22.89423 1.000 97.74373  ? 363 HOH A O   1 
HETATM 1314 O O   . HOH H 3 .   ? 32.64308 -55.97719 19.70462 1.000 86.61144  ? 364 HOH A O   1 
HETATM 1315 O O   . HOH H 3 .   ? 53.86952 -30.88202 19.00059 1.000 113.53445 ? 365 HOH A O   1 
HETATM 1316 O O   . HOH H 3 .   ? 48.25104 -37.12778 11.74319 1.000 93.69657  ? 366 HOH A O   1 
HETATM 1317 O O   . HOH H 3 .   ? 49.17725 -39.46908 11.83158 1.000 92.38060  ? 367 HOH A O   1 
HETATM 1318 O O   . HOH H 3 .   ? 51.39213 -46.06337 16.70775 1.000 131.97463 ? 368 HOH A O   1 
HETATM 1319 O O   . HOH H 3 .   ? 29.93834 -40.00984 38.25470 1.000 107.28419 ? 369 HOH A O   1 
HETATM 1320 O O   . HOH H 3 .   ? 17.73859 -38.08713 21.02189 1.000 109.88903 ? 370 HOH A O   1 
HETATM 1321 O O   . HOH H 3 .   ? 41.034   -45.367   32.795   1.000 107.83721 ? 371 HOH A O   1 
HETATM 1322 O O   . HOH H 3 .   ? 23.79129 -41.61488 21.97675 1.000 108.00114 ? 372 HOH A O   1 
HETATM 1323 O O   . HOH H 3 .   ? 56.28500 -32.49616 33.08468 0.33  83.81566  ? 373 HOH A O   1 
HETATM 1324 O O   . HOH H 3 .   ? 46.95242 -47.53274 -4.95796 1.000 96.49536  ? 374 HOH A O   1 
HETATM 1325 O O   . HOH H 3 .   ? 35.33705 -48.60435 30.31209 1.000 95.01920  ? 375 HOH A O   1 
HETATM 1326 O O   . HOH H 3 .   ? 52.33142 -37.92997 14.83652 1.000 107.10152 ? 376 HOH A O   1 
HETATM 1327 O O   . HOH H 3 .   ? 41.65548 -53.46978 24.42569 1.000 86.68710  ? 377 HOH A O   1 
HETATM 1328 O O   . HOH H 3 .   ? 34.670   -57.402   19.086   1.000 84.66380  ? 378 HOH A O   1 
HETATM 1329 O O   . HOH H 3 .   ? 45.25546 -28.32725 16.64239 1.000 125.03323 ? 379 HOH A O   1 
HETATM 1330 O O   . HOH H 3 .   ? 28.42802 -42.12416 33.94264 1.000 106.07890 ? 380 HOH A O   1 
HETATM 1331 O O   . HOH H 3 .   ? 37.87220 -49.15221 29.30966 1.000 97.54189  ? 381 HOH A O   1 
HETATM 1332 O O   . HOH H 3 .   ? 40.52612 -27.80435 22.13917 1.000 109.41942 ? 382 HOH A O   1 
HETATM 1333 O O   . HOH H 3 .   ? 56.28500 -32.49616 19.74405 0.33  130.41520 ? 383 HOH A O   1 
HETATM 1334 O O   . HOH H 3 .   ? 42.76283 -53.73000 12.66637 1.000 84.16925  ? 384 HOH A O   1 
HETATM 1335 O O   . HOH H 3 .   ? 29.87630 -37.42961 38.24595 1.000 127.70783 ? 385 HOH A O   1 
HETATM 1336 O O   . HOH H 3 .   ? 43.08217 -47.76755 32.23117 1.000 91.45865  ? 386 HOH A O   1 
HETATM 1337 O O   . HOH H 3 .   ? 47.19008 -51.28600 7.28696  1.000 98.95464  ? 387 HOH A O   1 
HETATM 1338 O O   . HOH H 3 .   ? 48.418   -18.721   44.520   1.000 102.49626 ? 388 HOH A O   1 
HETATM 1339 O O   . HOH H 3 .   ? 27.39328 -41.35052 36.73749 1.000 109.34041 ? 389 HOH A O   1 
HETATM 1340 O O   . HOH H 3 .   ? 51.21205 -35.27649 17.08328 1.000 100.34172 ? 390 HOH A O   1 
HETATM 1341 O O   . HOH H 3 .   ? 37.31736 -51.63710 24.32212 1.000 95.06331  ? 391 HOH A O   1 
HETATM 1342 O O   . HOH H 3 .   ? 53.121   -52.373   15.067   1.000 119.14501 ? 392 HOH A O   1 
HETATM 1343 O O   . HOH H 3 .   ? 56.28500 -32.49616 26.64788 0.33  77.81451  ? 393 HOH A O   1 
HETATM 1344 O O   . HOH H 3 .   ? 29.04292 -34.71397 11.86655 1.000 99.81657  ? 394 HOH A O   1 
HETATM 1345 O O   . HOH H 3 .   ? 54.169   -39.780   16.011   1.000 101.31519 ? 395 HOH A O   1 
HETATM 1346 O O   . HOH H 3 .   ? 40.612   -47.830   31.476   1.000 111.89486 ? 396 HOH A O   1 
HETATM 1347 O O   . HOH H 3 .   ? 35.31708 -54.00186 22.93331 1.000 99.18241  ? 397 HOH A O   1 
HETATM 1348 O O   . HOH H 3 .   ? 37.93393 -47.83242 32.03179 1.000 90.51432  ? 398 HOH A O   1 
HETATM 1349 O O   . HOH H 3 .   ? 53.94894 -34.24190 17.56510 1.000 112.10023 ? 399 HOH A O   1 
HETATM 1350 O O   . HOH H 3 .   ? 55.454   -33.661   38.319   1.000 88.39763  ? 400 HOH A O   1 
HETATM 1351 O O   . HOH H 3 .   ? 53.539   -36.334   16.626   1.000 118.84002 ? 401 HOH A O   1 
HETATM 1352 O O   . HOH H 3 .   ? 29.480   -35.508   8.990    1.000 96.83739  ? 402 HOH A O   1 
HETATM 1353 O O   . HOH H 3 .   ? 35.52581 -26.56355 19.21433 1.000 117.60957 ? 403 HOH A O   1 
HETATM 1354 O O   . HOH H 3 .   ? 40.63804 -52.21870 -7.91573 1.000 91.28816  ? 404 HOH A O   1 
HETATM 1355 O O   . HOH H 3 .   ? 37.17846 -51.03365 27.21605 1.000 111.84461 ? 405 HOH A O   1 
HETATM 1356 O O   . HOH H 3 .   ? 33.00624 -27.49149 20.27006 1.000 103.48837 ? 406 HOH A O   1 
HETATM 1357 O O   . HOH H 3 .   ? 51.25732 -29.75657 18.38539 1.000 112.82076 ? 407 HOH A O   1 
HETATM 1358 O O   . HOH H 3 .   ? 51.34681 -48.62999 18.85603 1.000 116.35627 ? 408 HOH A O   1 
HETATM 1359 O O   . HOH H 3 .   ? 35.09581 -56.28596 22.00567 1.000 105.19609 ? 409 HOH A O   1 
HETATM 1360 O O   . HOH H 3 .   ? 56.28500 -32.49616 42.35000 0.16  66.33179  ? 410 HOH A O   1 
HETATM 1361 O O   . HOH H 3 .   ? 49.33204 -33.37286 16.84288 1.000 100.82282 ? 411 HOH A O   1 
HETATM 1362 O O   . HOH H 3 .   ? 27.25635 -24.80438 50.65885 1.000 147.67591 ? 412 HOH A O   1 
HETATM 1363 O O   . HOH H 3 .   ? 26.24875 -27.09483 50.38554 1.000 129.67572 ? 413 HOH A O   1 
HETATM 1364 O O   . HOH H 3 .   ? 44.77183 -57.39541 27.45776 1.000 103.69140 ? 414 HOH A O   1 
HETATM 1365 O O   . HOH H 3 .   ? 44.42814 -23.50765 20.28735 1.000 88.22381  ? 415 HOH A O   1 
HETATM 1366 O O   . HOH H 3 .   ? 56.285   -32.496   36.269   0.33  88.96500  ? 416 HOH A O   1 
HETATM 1367 O O   . HOH H 3 .   ? 53.88816 -39.98986 11.70703 1.000 111.09465 ? 417 HOH A O   1 
HETATM 1368 O O   . HOH H 3 .   ? 42.59836 -11.99649 36.31810 1.000 103.78237 ? 418 HOH A O   1 
HETATM 1369 O O   . HOH H 3 .   ? 23.15793 -21.22181 49.06520 1.000 104.78977 ? 419 HOH A O   1 
HETATM 1370 O O   . HOH H 3 .   ? 49.19224 -33.85138 4.91275  1.000 104.87854 ? 420 HOH A O   1 
HETATM 1371 O O   . HOH H 3 .   ? 56.28500 -32.49616 16.32156 0.33  107.33095 ? 421 HOH A O   1 
HETATM 1372 O O   . HOH H 3 .   ? 28.24951 -23.24738 52.20919 1.000 120.37044 ? 422 HOH A O   1 
HETATM 1373 O O   . HOH H 3 .   ? 51.38364 -34.99899 3.08535  1.000 92.80487  ? 423 HOH A 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   . PRO A 6   ? 1.55981 2.91500 0.87466 -0.37551 0.04748  -0.26367 6   PRO A N   
2    C CA  . PRO A 6   ? 1.58566 3.02544 1.04621 -0.34664 -0.03768 -0.28382 6   PRO A CA  
3    C C   . PRO A 6   ? 1.51743 2.96491 1.06132 -0.37200 -0.03415 -0.25248 6   PRO A C   
4    O O   . PRO A 6   ? 1.29093 2.69555 0.79077 -0.33313 -0.07747 -0.21530 6   PRO A O   
5    C CB  . PRO A 6   ? 1.38558 2.93304 1.02373 -0.36493 -0.04404 -0.34631 6   PRO A CB  
6    C CG  . PRO A 6   ? 1.62810 3.15783 1.17482 -0.39332 0.01416  -0.36538 6   PRO A CG  
7    C CD  . PRO A 6   ? 1.85972 3.25147 1.17989 -0.37792 0.05624  -0.31161 6   PRO A CD  
8    N N   . VAL A 7   ? 1.53771 3.03802 1.20118 -0.43166 0.01364  -0.26938 7   VAL A N   
9    C CA  . VAL A 7   ? 1.41658 2.91912 1.19335 -0.44335 0.01139  -0.24408 7   VAL A CA  
10   C C   . VAL A 7   ? 1.43369 2.81379 1.09105 -0.44576 0.05209  -0.17844 7   VAL A C   
11   O O   . VAL A 7   ? 1.27799 2.62698 0.97152 -0.42436 0.02395  -0.14215 7   VAL A O   
12   C CB  . VAL A 7   ? 0.96348 2.53549 0.88815 -0.49208 0.05376  -0.27930 7   VAL A CB  
13   C CG1 . VAL A 7   ? 0.95269 2.42967 0.94895 -0.45319 0.04834  -0.24585 7   VAL A CG1 
14   C CG2 . VAL A 7   ? 1.09998 2.66290 1.08255 -0.45149 0.05386  -0.31777 7   VAL A CG2 
15   N N   . GLU A 8   ? 1.36999 2.67435 0.88806 -0.47132 0.12516  -0.16185 8   GLU A N   
16   C CA  . GLU A 8   ? 1.50511 2.68509 0.91248 -0.47663 0.17907  -0.10006 8   GLU A CA  
17   C C   . GLU A 8   ? 1.59756 2.68721 0.83114 -0.41150 0.14263  -0.05107 8   GLU A C   
18   O O   . GLU A 8   ? 1.65484 2.66243 0.84380 -0.39314 0.14363  0.00346  8   GLU A O   
19   C CB  . GLU A 8   ? 1.75503 2.85259 1.13754 -0.51847 0.27190  -0.10287 8   GLU A CB  
20   C CG  . GLU A 8   ? 1.81067 2.76159 1.09346 -0.51822 0.33622  -0.04301 8   GLU A CG  
21   C CD  . GLU A 8   ? 2.18143 3.01646 1.25113 -0.47460 0.36670  -0.00040 8   GLU A CD  
22   O OE1 . GLU A 8   ? 2.14973 2.94847 1.17197 -0.48165 0.41807  -0.01738 8   GLU A OE1 
23   O OE2 . GLU A 8   ? 2.24464 3.02074 1.19141 -0.42613 0.33642  0.05105  8   GLU A OE2 
24   N N   . ALA A 9   ? 1.66797 2.77078 0.79838 -0.37164 0.10867  -0.07200 9   ALA A N   
25   C CA  . ALA A 9   ? 1.83066 2.86758 0.80897 -0.29407 0.05047  -0.03744 9   ALA A CA  
26   C C   . ALA A 9   ? 1.62431 2.70513 0.72390 -0.25664 -0.04242 -0.03522 9   ALA A C   
27   O O   . ALA A 9   ? 1.82164 2.82404 0.83366 -0.20880 -0.07135 0.01367  9   ALA A O   
28   C CB  . ALA A 9   ? 1.84258 2.89020 0.73979 -0.24674 0.01379  -0.07667 9   ALA A CB  
29   N N   . ALA A 10  ? 1.42334 2.62462 0.72798 -0.27605 -0.08411 -0.08655 10  ALA A N   
30   C CA  . ALA A 10  ? 1.30096 2.53771 0.74654 -0.25006 -0.15074 -0.08209 10  ALA A CA  
31   C C   . ALA A 10  ? 1.27196 2.43750 0.73853 -0.27620 -0.10561 -0.02569 10  ALA A C   
32   O O   . ALA A 10  ? 1.27657 2.40352 0.75386 -0.23967 -0.14685 0.00901  10  ALA A O   
33   C CB  . ALA A 10  ? 1.10443 2.47280 0.76263 -0.26692 -0.18312 -0.14444 10  ALA A CB  
34   N N   . LYS A 11  ? 1.24383 2.39397 0.72423 -0.33840 -0.02204 -0.02158 11  LYS A N   
35   C CA  . LYS A 11  ? 1.21936 2.30721 0.72668 -0.36458 0.02210  0.02158  11  LYS A CA  
36   C C   . LYS A 11  ? 1.40530 2.35742 0.73735 -0.34042 0.04924  0.08783  11  LYS A C   
37   O O   . LYS A 11  ? 1.39937 2.29710 0.74661 -0.32899 0.04326  0.13040  11  LYS A O   
38   C CB  . LYS A 11  ? 1.15474 2.26745 0.72745 -0.43344 0.10070  -0.00445 11  LYS A CB  
39   C CG  . LYS A 11  ? 1.08868 2.17158 0.73811 -0.46006 0.13336  0.01733  11  LYS A CG  
40   C CD  . LYS A 11  ? 1.21631 2.32567 0.92524 -0.52349 0.20776  -0.02001 11  LYS A CD  
41   C CE  . LYS A 11  ? 0.95802 2.17616 0.77265 -0.53377 0.18515  -0.08562 11  LYS A CE  
42   N NZ  . LYS A 11  ? 0.93084 2.09535 0.80156 -0.55558 0.21712  -0.13014 11  LYS A NZ  
43   N N   . ALA A 12  ? 1.58086 2.47145 0.74003 -0.32814 0.08296  0.09949  12  ALA A N   
44   C CA  . ALA A 12  ? 1.78246 2.53183 0.75653 -0.29693 0.11814  0.16784  12  ALA A CA  
45   C C   . ALA A 12  ? 1.82841 2.55495 0.75831 -0.21978 0.02579  0.19608  12  ALA A C   
46   O O   . ALA A 12  ? 1.91127 2.54003 0.77425 -0.19882 0.03839  0.25551  12  ALA A O   
47   C CB  . ALA A 12  ? 1.97434 2.66005 0.76317 -0.29056 0.17810  0.17396  12  ALA A CB  
48   N N   . GLU A 13  ? 1.77785 2.59514 0.75439 -0.17619 -0.06715 0.14962  13  GLU A N   
49   C CA  . GLU A 13  ? 1.80619 2.61816 0.77592 -0.10277 -0.16226 0.16185  13  GLU A CA  
50   C C   . GLU A 13  ? 1.63968 2.48136 0.78984 -0.11614 -0.18900 0.17099  13  GLU A C   
51   O O   . GLU A 13  ? 1.68224 2.47773 0.81502 -0.06793 -0.23642 0.20468  13  GLU A O   
52   C CB  . GLU A 13  ? 1.79374 2.70372 0.79074 -0.05473 -0.25291 0.09585  13  GLU A CB  
53   C CG  . GLU A 13  ? 1.97602 2.86256 0.79001 -0.03451 -0.23195 0.08050  13  GLU A CG  
54   C CD  . GLU A 13  ? 2.21722 2.95426 0.77924 0.01911  -0.20295 0.14802  13  GLU A CD  
55   O OE1 . GLU A 13  ? 2.28965 2.97655 0.81128 0.08459  -0.26657 0.17427  13  GLU A OE1 
56   O OE2 . GLU A 13  ? 2.35140 3.00033 0.77436 -0.00289 -0.11015 0.17303  13  GLU A OE2 
57   N N   . ALA A 14  ? 1.47804 2.39266 0.79580 -0.17599 -0.15810 0.14188  14  ALA A N   
58   C CA  . ALA A 14  ? 1.30745 2.24988 0.79094 -0.18279 -0.17901 0.14886  14  ALA A CA  
59   C C   . ALA A 14  ? 1.33891 2.18471 0.78627 -0.21007 -0.11627 0.20710  14  ALA A C   
60   O O   . ALA A 14  ? 1.44037 2.27119 0.96726 -0.19503 -0.14058 0.23103  14  ALA A O   
61   C CB  . ALA A 14  ? 1.11662 2.17341 0.78341 -0.22210 -0.17405 0.09426  14  ALA A CB  
62   N N   . ILE A 15  ? 1.37938 1.50592 0.99429 0.06384  -0.05316 0.08270  15  ILE A N   
63   C CA  . ILE A 15  ? 1.31045 1.40122 0.90929 0.04119  -0.04679 0.09233  15  ILE A CA  
64   C C   . ILE A 15  ? 1.40964 1.44615 0.97979 0.06376  -0.06244 0.08372  15  ILE A C   
65   O O   . ILE A 15  ? 1.61996 1.62382 1.14614 0.09192  -0.07194 0.08857  15  ILE A O   
66   C CB  . ILE A 15  ? 1.35637 1.43999 0.92909 0.01741  -0.02652 0.11660  15  ILE A CB  
67   C CG1 . ILE A 15  ? 1.40823 1.55041 1.02038 -0.00506 -0.01656 0.11660  15  ILE A CG1 
68   C CG2 . ILE A 15  ? 1.33179 1.36570 0.88103 -0.00240 -0.01772 0.12432  15  ILE A CG2 
69   C CD1 . ILE A 15  ? 1.61426 1.76418 1.21736 -0.02936 0.00508  0.12929  15  ILE A CD1 
70   N N   . ALA A 16  ? 1.48288 1.50696 1.07393 0.05445  -0.06701 0.06896  16  ALA A N   
71   C CA  . ALA A 16  ? 1.58800 1.56381 1.16048 0.07727  -0.08523 0.05468  16  ALA A CA  
72   C C   . ALA A 16  ? 1.66191 1.57553 1.18277 0.06451  -0.07640 0.07896  16  ALA A C   
73   O O   . ALA A 16  ? 1.61780 1.52951 1.12130 0.03669  -0.05326 0.10349  16  ALA A O   
74   C CB  . ALA A 16  ? 1.57510 1.56798 1.19910 0.07187  -0.09121 0.02206  16  ALA A CB  
75   N N   . ALA A 17  ? 1.88110 1.74202 1.37993 0.08510  -0.09369 0.06787  17  ALA A N   
76   C CA  . ALA A 17  ? 1.89557 1.68260 1.33940 0.07601  -0.08453 0.08902  17  ALA A CA  
77   C C   . ALA A 17  ? 1.95566 1.75146 1.43852 0.03801  -0.07198 0.08328  17  ALA A C   
78   O O   . ALA A 17  ? 2.02112 1.84185 1.55148 0.03983  -0.08511 0.05503  17  ALA A O   
79   C CB  . ALA A 17  ? 1.87861 1.59494 1.27021 0.12348  -0.11351 0.07969  17  ALA A CB  
80   N N   . GLY A 18  ? 1.59606 1.37280 1.06102 0.00271  -0.04450 0.10574  18  GLY A N   
81   C CA  . GLY A 18  ? 1.41249 1.19879 0.91231 -0.03383 -0.03198 0.09919  18  GLY A CA  
82   C C   . GLY A 18  ? 1.18926 1.03860 0.72667 -0.07110 -0.01069 0.10378  18  GLY A C   
83   O O   . GLY A 18  ? 1.13895 1.02881 0.68158 -0.06911 -0.00618 0.11087  18  GLY A O   
84   N N   . LYS A 19  ? 1.31346 1.17128 0.87851 -0.10289 -0.00018 0.09588  19  LYS A N   
85   C CA  . LYS A 19  ? 1.19836 1.11931 0.80348 -0.13347 0.01255  0.09142  19  LYS A CA  
86   C C   . LYS A 19  ? 1.06964 1.05148 0.70365 -0.12027 -0.00286 0.08192  19  LYS A C   
87   O O   . LYS A 19  ? 1.05443 1.03587 0.69705 -0.10244 -0.01857 0.06870  19  LYS A O   
88   C CB  . LYS A 19  ? 1.30383 1.22642 0.93607 -0.16208 0.01826  0.07665  19  LYS A CB  
89   C CG  . LYS A 19  ? 1.52593 1.38439 1.13311 -0.18019 0.03881  0.08368  19  LYS A CG  
90   C CD  . LYS A 19  ? 1.77654 1.63642 1.41483 -0.20339 0.03966  0.06433  19  LYS A CD  
91   C CE  . LYS A 19  ? 1.75765 1.69663 1.44566 -0.22449 0.03811  0.04605  19  LYS A CE  
92   N NZ  . LYS A 19  ? 1.66885 1.61231 1.38406 -0.24295 0.03514  0.02440  19  LYS A NZ  
93   N N   . GLY A 20  ? 0.96882 1.00028 0.61845 -0.12946 0.00388  0.08554  20  GLY A N   
94   C CA  . GLY A 20  ? 0.84439 0.92111 0.51070 -0.11423 -0.00874 0.07977  20  GLY A CA  
95   C C   . GLY A 20  ? 0.81902 0.95055 0.50776 -0.12747 -0.00554 0.07707  20  GLY A C   
96   O O   . GLY A 20  ? 0.83626 0.98045 0.53486 -0.14792 0.00827  0.07719  20  GLY A O   
97   N N   . LYS A 21  ? 0.78562 0.94678 0.48219 -0.11459 -0.01760 0.07090  21  LYS A N   
98   C CA  A LYS A 21  ? 0.94588 1.15640 0.65836 -0.11678 -0.02284 0.06537  21  LYS A CA  
99   C CA  B LYS A 21  ? 0.90983 1.12034 0.62232 -0.11680 -0.02276 0.06545  21  LYS A CA  
100  C C   . LYS A 21  ? 0.77083 0.99410 0.47569 -0.09222 -0.03120 0.06897  21  LYS A C   
101  O O   . LYS A 21  ? 0.88326 1.08064 0.57602 -0.07997 -0.03254 0.06749  21  LYS A O   
102  C CB  A LYS A 21  ? 0.93379 1.15610 0.65330 -0.12854 -0.03146 0.04929  21  LYS A CB  
103  C CB  B LYS A 21  ? 0.97902 1.20126 0.69897 -0.12908 -0.03110 0.04933  21  LYS A CB  
104  C CG  A LYS A 21  ? 1.02675 1.24657 0.76387 -0.15554 -0.02239 0.03966  21  LYS A CG  
105  C CG  B LYS A 21  ? 0.96156 1.23529 0.69741 -0.12654 -0.04286 0.03747  21  LYS A CG  
106  C CD  A LYS A 21  ? 1.01748 1.24851 0.75827 -0.16236 -0.03452 0.02081  21  LYS A CD  
107  C CD  B LYS A 21  ? 0.84750 1.12753 0.58121 -0.13240 -0.05575 0.01914  21  LYS A CD  
108  C CE  A LYS A 21  ? 0.93682 1.21026 0.67689 -0.14634 -0.05338 0.01088  21  LYS A CE  
109  C CE  B LYS A 21  ? 1.24510 1.58042 0.99885 -0.12581 -0.07314 -0.00020 21  LYS A CE  
110  N NZ  A LYS A 21  ? 1.31708 1.59020 1.04238 -0.14527 -0.06863 -0.00622 21  LYS A NZ  
111  N NZ  B LYS A 21  ? 1.24084 1.58049 0.98315 -0.12411 -0.09137 -0.02042 21  LYS A NZ  
112  N N   . LEU A 22  ? 0.73435 0.99835 0.45095 -0.08614 -0.03483 0.06940  22  LEU A N   
113  C CA  . LEU A 22  ? 0.88294 1.15780 0.59262 -0.06283 -0.04185 0.07243  22  LEU A CA  
114  C C   . LEU A 22  ? 0.90565 1.18214 0.60041 -0.05467 -0.05516 0.06394  22  LEU A C   
115  O O   . LEU A 22  ? 0.76872 1.07354 0.47211 -0.05877 -0.06665 0.05340  22  LEU A O   
116  C CB  . LEU A 22  ? 0.72887 1.04377 0.45634 -0.05708 -0.04014 0.07572  22  LEU A CB  
117  C CG  . LEU A 22  ? 0.76150 1.08710 0.48429 -0.03219 -0.04715 0.07803  22  LEU A CG  
118  C CD1 . LEU A 22  ? 0.68353 0.97606 0.39394 -0.02033 -0.04000 0.08332  22  LEU A CD1 
119  C CD2 . LEU A 22  ? 0.73596 1.10869 0.48205 -0.02757 -0.04727 0.07656  22  LEU A CD2 
120  N N   . LEU A 23  ? 0.78961 1.03241 0.45920 -0.04207 -0.05257 0.06535  23  LEU A N   
121  C CA  . LEU A 23  ? 0.87295 1.09486 0.50720 -0.03220 -0.06006 0.06077  23  LEU A CA  
122  C C   . LEU A 23  ? 0.88188 1.10228 0.49870 -0.00833 -0.06348 0.06556  23  LEU A C   
123  O O   . LEU A 23  ? 1.00460 1.22820 0.59706 0.00676  -0.08009 0.06302  23  LEU A O   
124  C CB  . LEU A 23  ? 0.77935 0.94953 0.38860 -0.04097 -0.04619 0.05545  23  LEU A CB  
125  C CG  . LEU A 23  ? 0.95036 1.11526 0.57122 -0.06278 -0.04496 0.04806  23  LEU A CG  
126  C CD1 . LEU A 23  ? 0.83401 0.95111 0.43388 -0.07087 -0.02984 0.03785  23  LEU A CD1 
127  C CD2 . LEU A 23  ? 0.79737 0.98746 0.41621 -0.06791 -0.06189 0.04183  23  LEU A CD2 
128  N N   . ARG A 24  ? 0.77984 0.99439 0.40775 -0.00159 -0.05028 0.06974  24  ARG A N   
129  C CA  . ARG A 24  ? 0.82906 1.03596 0.44162 0.01958  -0.04940 0.07286  24  ARG A CA  
130  C C   . ARG A 24  ? 0.78266 1.01717 0.43154 0.02524  -0.04217 0.07457  24  ARG A C   
131  O O   . ARG A 24  ? 0.74865 0.98146 0.41765 0.01691  -0.03240 0.07116  24  ARG A O   
132  C CB  . ARG A 24  ? 0.80022 0.94197 0.36791 0.02202  -0.03133 0.06959  24  ARG A CB  
133  C CG  . ARG A 24  ? 1.48884 1.59084 0.99852 0.02511  -0.03925 0.07010  24  ARG A CG  
134  C CD  . ARG A 24  ? 1.60630 1.63519 1.07020 0.01615  -0.01066 0.06466  24  ARG A CD  
135  N NE  . ARG A 24  ? 1.67046 1.65573 1.10496 0.02902  0.00920  0.06651  24  ARG A NE  
136  C CZ  . ARG A 24  ? 1.73795 1.64949 1.12513 0.02107  0.04213  0.06014  24  ARG A CZ  
137  N NH1 . ARG A 24  ? 1.67187 1.54797 1.03617 0.00096  0.05786  0.05076  24  ARG A NH1 
138  N NH2 . ARG A 24  ? 1.81848 1.68826 1.18101 0.03143  0.06359  0.06100  24  ARG A NH2 
139  N N   . GLU A 25  ? 0.86540 1.12417 0.52002 0.04282  -0.04965 0.07749  25  GLU A N   
140  C CA  . GLU A 25  ? 0.78014 1.06211 0.46295 0.05219  -0.04260 0.07717  25  GLU A CA  
141  C C   . GLU A 25  ? 0.77571 1.02896 0.43951 0.06969  -0.03474 0.07493  25  GLU A C   
142  O O   . GLU A 25  ? 0.84958 1.09901 0.49091 0.08498  -0.04707 0.07851  25  GLU A O   
143  C CB  . GLU A 25  ? 0.76621 1.10611 0.47874 0.05473  -0.05410 0.07973  25  GLU A CB  
144  C CG  . GLU A 25  ? 1.15895 1.52018 0.88679 0.03429  -0.05440 0.08130  25  GLU A CG  
145  C CD  . GLU A 25  ? 1.27467 1.68797 1.03141 0.03266  -0.05568 0.07973  25  GLU A CD  
146  O OE1 . GLU A 25  ? 1.31368 1.74798 1.08219 0.04821  -0.05572 0.07871  25  GLU A OE1 
147  O OE2 . GLU A 25  ? 1.34182 1.77450 1.11150 0.01377  -0.05330 0.07667  25  GLU A OE2 
148  N N   . GLU A 26  ? 0.69679 0.92821 0.37017 0.06900  -0.01446 0.06545  26  GLU A N   
149  C CA  . GLU A 26  ? 0.88629 1.08485 0.54593 0.08101  0.00159  0.05969  26  GLU A CA  
150  C C   . GLU A 26  ? 0.84335 1.07334 0.54884 0.08792  0.01042  0.04683  26  GLU A C   
151  O O   . GLU A 26  ? 0.67787 0.93812 0.41467 0.08381  0.00689  0.03996  26  GLU A O   
152  C CB  . GLU A 26  ? 0.76546 0.89435 0.38944 0.06940  0.02744  0.05073  26  GLU A CB  
153  C CG  . GLU A 26  ? 1.27164 1.36245 0.84229 0.06308  0.02012  0.06089  26  GLU A CG  
154  C CD  . GLU A 26  ? 1.51054 1.52691 1.04079 0.04892  0.05240  0.05046  26  GLU A CD  
155  O OE1 . GLU A 26  ? 1.32846 1.32383 0.87703 0.04312  0.08282  0.03267  26  GLU A OE1 
156  O OE2 . GLU A 26  ? 1.68642 1.66615 1.16845 0.04235  0.04964  0.05622  26  GLU A OE2 
157  N N   . TRP A 27  ? 0.73297 0.95019 0.43703 0.10114  0.02113  0.04226  27  TRP A N   
158  C CA  . TRP A 27  ? 0.86807 1.11539 0.61707 0.10957  0.03026  0.02527  27  TRP A CA  
159  C C   . TRP A 27  ? 0.88969 1.08914 0.62860 0.11314  0.05831  0.01218  27  TRP A C   
160  O O   . TRP A 27  ? 1.01956 1.16613 0.70749 0.11729  0.06385  0.02479  27  TRP A O   
161  C CB  . TRP A 27  ? 0.65308 0.96084 0.42573 0.12415  0.00939  0.03408  27  TRP A CB  
162  C CG  . TRP A 27  ? 0.65463 0.96004 0.40208 0.13573  -0.00453 0.04896  27  TRP A CG  
163  C CD1 . TRP A 27  ? 0.74695 1.03111 0.48288 0.15241  0.00025  0.04769  27  TRP A CD1 
164  C CD2 . TRP A 27  ? 0.76114 1.08606 0.49382 0.13437  -0.02757 0.06234  27  TRP A CD2 
165  N NE1 . TRP A 27  ? 0.80750 1.09677 0.51954 0.16599  -0.02326 0.05954  27  TRP A NE1 
166  C CE2 . TRP A 27  ? 0.84066 1.15988 0.55517 0.15451  -0.04059 0.06580  27  TRP A CE2 
167  C CE3 . TRP A 27  ? 0.68088 1.02702 0.41641 0.11868  -0.03804 0.06805  27  TRP A CE3 
168  C CZ2 . TRP A 27  ? 0.70185 1.04460 0.40767 0.16138  -0.06704 0.06956  27  TRP A CZ2 
169  C CZ3 . TRP A 27  ? 0.65837 1.02682 0.38748 0.12043  -0.05861 0.07252  27  TRP A CZ3 
170  C CH2 . TRP A 27  ? 0.70279 1.07376 0.42041 0.14256  -0.07455 0.07077  27  TRP A CH2 
171  N N   . SER A 28  ? 0.79534 1.58396 0.63754 0.03737  -0.22400 0.02804  28  SER A N   
172  C CA  . SER A 28  ? 0.71222 1.51924 0.55450 0.06200  -0.22731 0.01612  28  SER A CA  
173  C C   . SER A 28  ? 0.72265 1.59903 0.62614 0.07479  -0.20079 -0.03626 28  SER A C   
174  O O   . SER A 28  ? 0.71775 1.66921 0.66549 0.07202  -0.19212 -0.06080 28  SER A O   
175  C CB  . SER A 28  ? 0.96084 1.70702 0.75251 0.02819  -0.21197 0.01059  28  SER A CB  
176  O OG  . SER A 28  ? 0.85317 1.65040 0.63372 -0.01498 -0.18847 -0.02401 28  SER A OG  
177  N N   . GLU A 29  ? 0.88484 1.70227 0.80097 0.08495  -0.17570 -0.05869 29  GLU A N   
178  C CA  A GLU A 29  ? 0.85558 1.69255 0.83872 0.09264  -0.13634 -0.11808 29  GLU A CA  
179  C CA  B GLU A 29  ? 0.86459 1.70069 0.84756 0.09277  -0.13630 -0.11800 29  GLU A CA  
180  C C   . GLU A 29  ? 0.79319 1.68569 0.74705 0.03491  -0.10094 -0.16078 29  GLU A C   
181  O O   . GLU A 29  ? 0.77316 1.65514 0.65121 -0.00542 -0.10712 -0.14232 29  GLU A O   
182  C CB  A GLU A 29  ? 0.87720 1.61582 0.88063 0.12566  -0.13085 -0.12236 29  GLU A CB  
183  C CB  B GLU A 29  ? 0.88700 1.62365 0.88866 0.12542  -0.13121 -0.12136 29  GLU A CB  
184  C CG  A GLU A 29  ? 0.86285 1.54022 0.78653 0.09529  -0.12477 -0.10736 29  GLU A CG  
185  C CG  B GLU A 29  ? 0.99448 1.73537 1.07930 0.14849  -0.10121 -0.18385 29  GLU A CG  
186  C CD  A GLU A 29  ? 1.02568 1.60727 0.95880 0.11604  -0.11829 -0.11537 29  GLU A CD  
187  C CD  B GLU A 29  ? 1.14721 1.77468 1.23180 0.17118  -0.10335 -0.18385 29  GLU A CD  
188  O OE1 A GLU A 29  ? 1.27515 1.82868 1.28065 0.15776  -0.12392 -0.13257 29  GLU A OE1 
189  O OE1 B GLU A 29  ? 1.25880 1.81873 1.26667 0.15399  -0.11688 -0.14181 29  GLU A OE1 
190  O OE2 A GLU A 29  ? 1.11543 1.64873 0.98222 0.08932  -0.11155 -0.10564 29  GLU A OE2 
191  O OE2 B GLU A 29  ? 1.02937 1.63692 1.18979 0.20435  -0.09463 -0.22877 29  GLU A OE2 
192  N N   . GLU A 30  ? 0.81941 1.77638 0.83698 0.02929  -0.06588 -0.22155 30  GLU A N   
193  C CA  . GLU A 30  ? 0.83567 1.84561 0.82943 -0.03096 -0.02771 -0.26715 30  GLU A CA  
194  C C   . GLU A 30  ? 0.84727 1.77515 0.81401 -0.03399 -0.00491 -0.27648 30  GLU A C   
195  O O   . GLU A 30  ? 0.90126 1.77035 0.91749 0.00922  0.00560  -0.29555 30  GLU A O   
196  C CB  . GLU A 30  ? 0.83107 1.94159 0.90647 -0.03773 0.00718  -0.33865 30  GLU A CB  
197  C CG  . GLU A 30  ? 0.80862 2.02884 0.88413 -0.06870 -0.00659 -0.33856 30  GLU A CG  
198  C CD  . GLU A 30  ? 0.91363 2.25322 1.06923 -0.08501 0.03264  -0.42034 30  GLU A CD  
199  O OE1 . GLU A 30  ? 1.05964 2.39142 1.27970 -0.06351 0.06857  -0.47896 30  GLU A OE1 
200  O OE2 . GLU A 30  ? 0.85025 2.29491 1.00357 -0.12163 0.02629  -0.42936 30  GLU A OE2 
201  N N   . LYS A 31  ? 0.83069 1.74995 0.71661 -0.08549 -0.00261 -0.26191 31  LYS A N   
202  C CA  . LYS A 31  ? 0.92197 1.77207 0.77008 -0.09717 0.01931  -0.26853 31  LYS A CA  
203  C C   . LYS A 31  ? 0.86902 1.77353 0.71270 -0.15439 0.06507  -0.32222 31  LYS A C   
204  O O   . LYS A 31  ? 0.84602 1.83193 0.67113 -0.20647 0.06595  -0.33299 31  LYS A O   
205  C CB  . LYS A 31  ? 0.83429 1.63556 0.59700 -0.11142 -0.01293 -0.21624 31  LYS A CB  
206  C CG  . LYS A 31  ? 1.19139 1.95464 0.95085 -0.06659 -0.05926 -0.16361 31  LYS A CG  
207  C CD  . LYS A 31  ? 1.40996 2.14606 1.09209 -0.08450 -0.09002 -0.12583 31  LYS A CD  
208  C CE  . LYS A 31  ? 1.28935 2.00311 0.96848 -0.04696 -0.13546 -0.07803 31  LYS A CE  
209  N NZ  . LYS A 31  ? 1.32249 1.95794 0.98127 -0.05690 -0.14710 -0.04722 31  LYS A NZ  
210  N N   . THR A 32  ? 1.02341 1.88070 0.87880 -0.15015 0.10048  -0.35457 32  THR A N   
211  C CA  . THR A 32  ? 0.92807 1.83173 0.78403 -0.20294 0.14922  -0.40968 32  THR A CA  
212  C C   . THR A 32  ? 0.93389 1.77741 0.70839 -0.23796 0.15871  -0.39152 32  THR A C   
213  O O   . THR A 32  ? 0.96182 1.71558 0.71950 -0.20639 0.15583  -0.37436 32  THR A O   
214  C CB  . THR A 32  ? 0.97764 1.88412 0.92351 -0.16916 0.18508  -0.47364 32  THR A CB  
215  O OG1 . THR A 32  ? 0.97194 1.93898 1.00049 -0.13065 0.17199  -0.49311 32  THR A OG1 
216  C CG2 . THR A 32  ? 0.99318 1.96330 0.94374 -0.22905 0.23863  -0.53679 32  THR A CG2 
217  N N   . THR A 33  ? 0.96910 1.85708 0.69656 -0.30570 0.16454  -0.39139 33  THR A N   
218  C CA  . THR A 33  ? 0.94396 1.75558 0.63504 -0.33065 0.15902  -0.35566 33  THR A CA  
219  C C   . THR A 33  ? 0.95979 1.73724 0.65739 -0.33568 0.20769  -0.39768 33  THR A C   
220  O O   . THR A 33  ? 1.01459 1.83976 0.76209 -0.34931 0.24530  -0.45257 33  THR A O   
221  C CB  . THR A 33  ? 1.00326 1.83555 0.70439 -0.38732 0.13902  -0.32646 33  THR A CB  
222  O OG1 . THR A 33  ? 0.95405 1.85629 0.69669 -0.43406 0.17026  -0.37256 33  THR A OG1 
223  C CG2 . THR A 33  ? 0.94824 1.79739 0.64783 -0.37888 0.09284  -0.28207 33  THR A CG2 
224  N N   . GLY A 34  ? 0.97469 1.66919 0.62657 -0.32471 0.20485  -0.37225 34  GLY A N   
225  C CA  . GLY A 34  ? 1.05074 1.69738 0.69730 -0.33340 0.24425  -0.40042 34  GLY A CA  
226  C C   . GLY A 34  ? 1.00843 1.64751 0.65930 -0.38579 0.24526  -0.38386 34  GLY A C   
227  O O   . GLY A 34  ? 0.99794 1.67690 0.66470 -0.42011 0.22080  -0.36262 34  GLY A O   
228  N N   . GLU A 35  ? 1.06609 1.65102 0.70111 -0.39351 0.27207  -0.39531 35  GLU A N   
229  C CA  . GLU A 35  ? 1.08771 1.66586 0.72910 -0.44174 0.27365  -0.38505 35  GLU A CA  
230  C C   . GLU A 35  ? 1.16940 1.72920 0.79344 -0.45206 0.23045  -0.33126 35  GLU A C   
231  O O   . GLU A 35  ? 0.96268 1.53886 0.60382 -0.49607 0.22157  -0.32381 35  GLU A O   
232  C CB  . GLU A 35  ? 1.15257 1.67210 0.77604 -0.44308 0.30788  -0.40437 35  GLU A CB  
233  C CG  . GLU A 35  ? 1.19843 1.73738 0.85744 -0.43596 0.35440  -0.46928 35  GLU A CG  
234  C CD  . GLU A 35  ? 1.33185 1.95318 1.05069 -0.47791 0.36567  -0.50333 35  GLU A CD  
235  O OE1 . GLU A 35  ? 1.48977 2.12717 1.20696 -0.52763 0.34582  -0.47961 35  GLU A OE1 
236  O OE2 . GLU A 35  ? 1.77016 2.44263 1.54158 -0.46216 0.39161  -0.55919 35  GLU A OE2 
237  N N   . ASP A 36  ? 0.96965 1.49873 0.56578 -0.41323 0.20333  -0.29881 36  ASP A N   
238  C CA  . ASP A 36  ? 0.91544 1.43594 0.51190 -0.41412 0.16414  -0.25709 36  ASP A CA  
239  C C   . ASP A 36  ? 0.87357 1.44587 0.49599 -0.42430 0.13605  -0.24231 36  ASP A C   
240  O O   . ASP A 36  ? 0.84523 1.41131 0.47474 -0.42547 0.10740  -0.21181 36  ASP A O   
241  C CB  . ASP A 36  ? 0.93366 1.40673 0.49738 -0.37059 0.14586  -0.23283 36  ASP A CB  
242  C CG  . ASP A 36  ? 1.21207 1.68950 0.75736 -0.33403 0.14085  -0.23682 36  ASP A CG  
243  O OD1 . ASP A 36  ? 1.01385 1.53949 0.57926 -0.33559 0.14494  -0.25444 36  ASP A OD1 
244  O OD2 . ASP A 36  ? 1.23893 1.67629 0.75020 -0.30667 0.13122  -0.22333 36  ASP A OD2 
245  N N   . GLY A 37  ? 0.88323 1.50678 0.52155 -0.43053 0.14571  -0.26512 37  GLY A N   
246  C CA  . GLY A 37  ? 0.85126 1.52442 0.51010 -0.44367 0.12022  -0.24901 37  GLY A CA  
247  C C   . GLY A 37  ? 0.91666 1.56876 0.56279 -0.39668 0.08215  -0.21392 37  GLY A C   
248  O O   . GLY A 37  ? 0.80141 1.47402 0.45956 -0.40149 0.05744  -0.19202 37  GLY A O   
249  N N   . LEU A 38  ? 1.21227 1.53768 0.59935 -0.56287 -0.11854 0.02780  38  LEU A N   
250  C CA  . LEU A 38  ? 1.26774 1.54500 0.59227 -0.57862 -0.10288 0.03048  38  LEU A CA  
251  C C   . LEU A 38  ? 1.31110 1.56487 0.57433 -0.57937 -0.13233 0.04395  38  LEU A C   
252  O O   . LEU A 38  ? 1.32637 1.57437 0.57410 -0.57106 -0.15498 0.05617  38  LEU A O   
253  C CB  . LEU A 38  ? 1.32255 1.54487 0.61671 -0.58864 -0.06760 0.03168  38  LEU A CB  
254  C CG  . LEU A 38  ? 1.35892 1.59745 0.70871 -0.59168 -0.03395 0.01660  38  LEU A CG  
255  C CD1 . LEU A 38  ? 1.44818 1.62778 0.76467 -0.60183 0.00016  0.02251  38  LEU A CD1 
256  C CD2 . LEU A 38  ? 1.25607 1.52273 0.62505 -0.59599 -0.02230 0.00428  38  LEU A CD2 
257  N N   . LEU A 39  ? 1.33268 1.57335 0.56238 -0.58896 -0.13198 0.04026  39  LEU A N   
258  C CA  A LEU A 39  ? 1.37760 1.59295 0.55758 -0.58716 -0.15642 0.04819  39  LEU A CA  
259  C CA  B LEU A 39  ? 1.37790 1.59302 0.55757 -0.58719 -0.15636 0.04824  39  LEU A CA  
260  C C   . LEU A 39  ? 1.44241 1.60750 0.55843 -0.60055 -0.13491 0.04224  39  LEU A C   
261  O O   . LEU A 39  ? 1.42912 1.60208 0.55569 -0.60952 -0.12247 0.02960  39  LEU A O   
262  C CB  A LEU A 39  ? 1.32495 1.58268 0.56392 -0.57283 -0.18059 0.04745  39  LEU A CB  
263  C CB  B LEU A 39  ? 1.32523 1.58277 0.56397 -0.57261 -0.18084 0.04769  39  LEU A CB  
264  C CG  A LEU A 39  ? 1.35972 1.59667 0.57778 -0.56169 -0.20509 0.05374  39  LEU A CG  
265  C CG  B LEU A 39  ? 1.39953 1.65157 0.63783 -0.55355 -0.21125 0.05956  39  LEU A CG  
266  C CD1 A LEU A 39  ? 1.36347 1.60073 0.58442 -0.54290 -0.22639 0.06826  39  LEU A CD1 
267  C CD1 B LEU A 39  ? 1.41053 1.61486 0.58581 -0.55758 -0.21500 0.05773  39  LEU A CD1 
268  C CD2 A LEU A 39  ? 1.31884 1.58985 0.58582 -0.55731 -0.21791 0.04937  39  LEU A CD2 
269  C CD2 B LEU A 39  ? 1.40168 1.65153 0.63718 -0.54220 -0.22033 0.07173  39  LEU A CD2 
270  N N   . GLU A 40  ? 1.51384 1.62839 0.56418 -0.59969 -0.12924 0.05199  40  GLU A N   
271  C CA  . GLU A 40  ? 1.58265 1.64798 0.56918 -0.60606 -0.10838 0.04788  40  GLU A CA  
272  C C   . GLU A 40  ? 1.62166 1.67150 0.58086 -0.59240 -0.13607 0.04810  40  GLU A C   
273  O O   . GLU A 40  ? 1.64998 1.68840 0.58780 -0.57828 -0.15410 0.06117  40  GLU A O   
274  C CB  . GLU A 40  ? 1.64056 1.66122 0.57394 -0.61035 -0.07795 0.06043  40  GLU A CB  
275  C CG  . GLU A 40  ? 1.72193 1.75450 0.71840 -0.61326 -0.04440 0.05722  40  GLU A CG  
276  C CD  . GLU A 40  ? 2.04643 2.10600 1.09738 -0.60446 -0.05667 0.06469  40  GLU A CD  
277  O OE1 . GLU A 40  ? 2.11788 2.19196 1.16210 -0.59592 -0.09195 0.07292  40  GLU A OE1 
278  O OE2 . GLU A 40  ? 2.14016 2.20709 1.24188 -0.60560 -0.03152 0.06111  40  GLU A OE2 
279  N N   . ILE A 41  ? 1.62547 1.67592 0.58497 -0.59662 -0.13899 0.03274  41  ILE A N   
280  C CA  . ILE A 41  ? 1.73339 1.77092 0.66665 -0.58595 -0.16433 0.02775  41  ILE A CA  
281  C C   . ILE A 41  ? 1.92344 1.91425 0.78580 -0.58868 -0.14448 0.01864  41  ILE A C   
282  O O   . ILE A 41  ? 1.74195 1.72453 0.60088 -0.60230 -0.11872 0.00697  41  ILE A O   
283  C CB  . ILE A 41  ? 2.02138 2.09742 1.01225 -0.58781 -0.18709 0.01673  41  ILE A CB  
284  C CG1 . ILE A 41  ? 1.86280 1.94878 0.87462 -0.60597 -0.16517 0.00183  41  ILE A CG1 
285  C CG2 . ILE A 41  ? 1.65418 1.77641 0.71291 -0.57785 -0.20718 0.02879  41  ILE A CG2 
286  C CD1 . ILE A 41  ? 1.91022 2.02909 0.97220 -0.60938 -0.18506 -0.00784 41  ILE A CD1 
287  N N   . ASP A 42  ? 1.81019 1.77234 0.61586 -0.57297 -0.15507 0.02439  42  ASP A N   
288  C CA  A ASP A 42  ? 2.02837 1.94867 0.76220 -0.56855 -0.13893 0.01697  42  ASP A CA  
289  C CA  B ASP A 42  ? 2.03006 1.95031 0.76381 -0.56852 -0.13892 0.01703  42  ASP A CA  
290  C C   . ASP A 42  ? 1.91499 1.83930 0.63956 -0.56285 -0.16730 -0.00288 42  ASP A C   
291  O O   . ASP A 42  ? 2.05636 1.99057 0.77817 -0.54756 -0.19846 -0.00062 42  ASP A O   
292  C CB  A ASP A 42  ? 2.09974 1.98822 0.77279 -0.55153 -0.12981 0.03690  42  ASP A CB  
293  C CB  B ASP A 42  ? 2.09856 1.98736 0.77205 -0.55144 -0.13012 0.03708  42  ASP A CB  
294  C CG  A ASP A 42  ? 2.21734 2.09489 0.89505 -0.55979 -0.09708 0.05553  42  ASP A CG  
295  C CG  B ASP A 42  ? 2.12908 1.97567 0.73760 -0.54879 -0.09504 0.03727  42  ASP A CG  
296  O OD1 A ASP A 42  ? 2.21973 2.12013 0.95106 -0.57727 -0.08561 0.05133  42  ASP A OD1 
297  O OD1 B ASP A 42  ? 2.17332 2.00951 0.79085 -0.56205 -0.05952 0.04194  42  ASP A OD1 
298  O OD2 A ASP A 42  ? 2.06670 1.91418 0.69521 -0.54806 -0.08182 0.07461  42  ASP A OD2 
299  O OD2 B ASP A 42  ? 2.25590 2.08218 0.80604 -0.53136 -0.10231 0.03268  42  ASP A OD2 
300  N N   . LEU A 43  ? 1.92178 1.83890 0.64301 -0.57515 -0.15618 -0.02334 43  LEU A N   
301  C CA  . LEU A 43  ? 2.18965 2.10745 0.90052 -0.57227 -0.18171 -0.04578 43  LEU A CA  
302  C C   . LEU A 43  ? 2.04831 1.93406 0.67881 -0.55094 -0.18652 -0.04916 43  LEU A C   
303  O O   . LEU A 43  ? 2.11414 1.97489 0.69581 -0.53945 -0.16493 -0.03252 43  LEU A O   
304  C CB  . LEU A 43  ? 1.94644 1.86233 0.67294 -0.59163 -0.16604 -0.06722 43  LEU A CB  
305  C CG  . LEU A 43  ? 1.85383 1.79970 0.64897 -0.61073 -0.14995 -0.06231 43  LEU A CG  
306  C CD1 . LEU A 43  ? 1.94238 1.88242 0.74369 -0.62792 -0.13088 -0.08343 43  LEU A CD1 
307  C CD2 . LEU A 43  ? 1.78619 1.77772 0.65213 -0.61063 -0.18061 -0.05506 43  LEU A CD2 
308  N N   . GLU A 44  ? 2.31732 2.20613 0.93517 -0.54426 -0.21523 -0.07107 44  GLU A N   
309  C CA  . GLU A 44  ? 2.56800 2.43340 1.10918 -0.52034 -0.22299 -0.07772 44  GLU A CA  
310  C C   . GLU A 44  ? 2.74697 2.57553 1.22661 -0.51817 -0.18723 -0.08259 44  GLU A C   
311  O O   . GLU A 44  ? 2.89850 2.70562 1.30941 -0.49497 -0.17937 -0.07519 44  GLU A O   
312  C CB  . GLU A 44  ? 2.40948 2.28866 0.95423 -0.51471 -0.26191 -0.10570 44  GLU A CB  
313  C CG  . GLU A 44  ? 2.61256 2.47911 1.08310 -0.48468 -0.27729 -0.11251 44  GLU A CG  
314  C CD  . GLU A 44  ? 2.66017 2.53510 1.12627 -0.48067 -0.31072 -0.14872 44  GLU A CD  
315  O OE1 . GLU A 44  ? 2.67311 2.55911 1.19370 -0.50332 -0.31952 -0.16776 44  GLU A OE1 
316  O OE2 . GLU A 44  ? 2.66170 2.53365 1.07053 -0.45404 -0.32814 -0.15877 44  GLU A OE2 
317  N N   . THR A 45  ? 2.89030 2.71296 1.39388 -0.53979 -0.16352 -0.09335 45  THR A N   
318  C CA  . THR A 45  ? 2.92597 2.71482 1.37799 -0.53771 -0.12656 -0.09768 45  THR A CA  
319  C C   . THR A 45  ? 2.81357 2.58594 1.25031 -0.53463 -0.08824 -0.06753 45  THR A C   
320  O O   . THR A 45  ? 2.89198 2.63545 1.28234 -0.52761 -0.05516 -0.06547 45  THR A O   
321  C CB  . THR A 45  ? 2.88417 2.67356 1.37085 -0.56149 -0.11273 -0.11937 45  THR A CB  
322  O OG1 . THR A 45  ? 2.64628 2.45681 1.19935 -0.58228 -0.09702 -0.10507 45  THR A OG1 
323  C CG2 . THR A 45  ? 2.81909 2.62430 1.32923 -0.56743 -0.15010 -0.14915 45  THR A CG2 
324  N N   . GLY A 46  ? 2.52925 2.31943 1.00598 -0.53900 -0.09137 -0.04459 46  GLY A N   
325  C CA  . GLY A 46  ? 2.37726 2.15274 0.84657 -0.53798 -0.05716 -0.01712 46  GLY A CA  
326  C C   . GLY A 46  ? 2.24046 2.02828 0.77019 -0.56234 -0.03145 -0.01362 46  GLY A C   
327  O O   . GLY A 46  ? 2.18560 1.96767 0.72381 -0.56425 -0.00732 0.00819  46  GLY A O   
328  N N   . LYS A 47  ? 2.25450 2.06063 0.82724 -0.58015 -0.03534 -0.03456 47  LYS A N   
329  C CA  A LYS A 47  ? 2.21990 2.04415 0.85074 -0.60029 -0.01082 -0.03257 47  LYS A CA  
330  C CA  B LYS A 47  ? 2.21971 2.04434 0.85109 -0.60048 -0.01122 -0.03300 47  LYS A CA  
331  C C   . LYS A 47  ? 2.06955 1.93187 0.76105 -0.60637 -0.03050 -0.02017 47  LYS A C   
332  O O   . LYS A 47  ? 1.99064 1.87272 0.69685 -0.59995 -0.06807 -0.02002 47  LYS A O   
333  C CB  A LYS A 47  ? 2.16089 1.99507 0.81750 -0.61522 -0.00775 -0.05731 47  LYS A CB  
334  C CB  B LYS A 47  ? 2.15968 1.99505 0.81724 -0.61526 -0.01015 -0.05809 47  LYS A CB  
335  C CG  A LYS A 47  ? 2.24631 2.04370 0.84689 -0.60952 0.01439  -0.07161 47  LYS A CG  
336  C CG  B LYS A 47  ? 2.14523 1.99954 0.85641 -0.63267 0.02063  -0.05837 47  LYS A CG  
337  C CD  A LYS A 47  ? 2.18214 1.95615 0.76679 -0.60720 0.06203  -0.05752 47  LYS A CD  
338  C CD  B LYS A 47  ? 2.14563 1.96842 0.82795 -0.63021 0.06706  -0.05361 47  LYS A CD  
339  C CE  A LYS A 47  ? 2.10626 1.90343 0.75605 -0.62599 0.08825  -0.05902 47  LYS A CE  
340  C CE  B LYS A 47  ? 2.19369 2.04021 0.93609 -0.64508 0.09723  -0.05568 47  LYS A CE  
341  N NZ  A LYS A 47  ? 2.13257 1.90818 0.77514 -0.62267 0.13510  -0.04721 47  LYS A NZ  
342  N NZ  B LYS A 47  ? 2.20878 2.07867 0.98494 -0.65762 0.08820  -0.07643 47  LYS A NZ  
343  N N   . LYS A 48  ? 1.55001 1.90862 0.98357 -0.35723 -0.03186 0.03768  48  LYS A N   
344  C CA  . LYS A 48  ? 1.61600 1.98445 1.06530 -0.38307 -0.02580 0.03089  48  LYS A CA  
345  C C   . LYS A 48  ? 1.39496 1.80729 0.89647 -0.41924 -0.02845 0.02958  48  LYS A C   
346  O O   . LYS A 48  ? 1.38683 1.81566 0.90749 -0.43854 -0.02717 0.03331  48  LYS A O   
347  C CB  . LYS A 48  ? 1.48003 1.82149 0.90337 -0.39421 -0.01162 0.03227  48  LYS A CB  
348  C CG  . LYS A 48  ? 1.85236 2.13839 1.21090 -0.35756 -0.00353 0.03619  48  LYS A CG  
349  C CD  . LYS A 48  ? 1.92063 2.17556 1.25113 -0.37528 0.01360  0.03896  48  LYS A CD  
350  C CE  . LYS A 48  ? 2.26979 2.46314 1.52598 -0.33995 0.02634  0.04699  48  LYS A CE  
351  N NZ  . LYS A 48  ? 2.25933 2.42137 1.48164 -0.37224 0.04530  0.05138  48  LYS A NZ  
352  N N   . ALA A 49  ? 1.22553 1.65648 0.74471 -0.42595 -0.03120 0.02429  49  ALA A N   
353  C CA  . ALA A 49  ? 1.33874 1.80202 0.89493 -0.45866 -0.02959 0.02414  49  ALA A CA  
354  C C   . ALA A 49  ? 1.03679 1.50064 0.59242 -0.47627 -0.02094 0.01713  49  ALA A C   
355  O O   . ALA A 49  ? 1.12568 1.57934 0.66198 -0.46199 -0.01849 0.01038  49  ALA A O   
356  C CB  . ALA A 49  ? 1.22620 1.70883 0.79644 -0.45792 -0.03547 0.02398  49  ALA A CB  
357  N N   . THR A 50  ? 1.13917 1.61309 0.71038 -0.50286 -0.01749 0.01740  50  THR A N   
358  C CA  . THR A 50  ? 1.26139 1.72884 0.82491 -0.51806 -0.01071 0.01002  50  THR A CA  
359  C C   . THR A 50  ? 1.14947 1.64192 0.73333 -0.53678 -0.00925 0.00763  50  THR A C   
360  O O   . THR A 50  ? 1.00659 1.51626 0.60984 -0.54989 -0.01190 0.01301  50  THR A O   
361  C CB  . THR A 50  ? 1.27814 1.73623 0.83639 -0.53383 -0.00817 0.00994  50  THR A CB  
362  O OG1 . THR A 50  ? 1.66388 2.14977 1.24929 -0.54908 -0.01155 0.01441  50  THR A OG1 
363  C CG2 . THR A 50  ? 1.46414 1.89468 0.99501 -0.51622 -0.00712 0.01354  50  THR A CG2 
364  N N   . PHE A 51  ? 1.25774 1.74806 0.82934 -0.53412 -0.00452 -0.00037 51  PHE A N   
365  C CA  . PHE A 51  ? 0.84575 1.35574 0.42675 -0.54920 -0.00155 -0.00402 51  PHE A CA  
366  C C   . PHE A 51  ? 0.97523 1.46671 0.53240 -0.55149 0.00417  -0.01299 51  PHE A C   
367  O O   . PHE A 51  ? 0.89998 1.36247 0.42972 -0.53827 0.00657  -0.01724 51  PHE A O   
368  C CB  . PHE A 51  ? 0.84127 1.37490 0.42818 -0.54144 -0.00089 -0.00646 51  PHE A CB  
369  C CG  . PHE A 51  ? 1.03381 1.58195 0.63857 -0.54101 -0.00660 0.00186  51  PHE A CG  
370  C CD1 . PHE A 51  ? 1.11366 1.65104 0.71110 -0.51842 -0.01127 0.00393  51  PHE A CD1 
371  C CD2 . PHE A 51  ? 0.84506 1.40988 0.46462 -0.56069 -0.00794 0.00743  51  PHE A CD2 
372  C CE1 . PHE A 51  ? 0.81092 1.35635 0.41801 -0.51501 -0.01757 0.01076  51  PHE A CE1 
373  C CE2 . PHE A 51  ? 1.06977 1.63912 0.69690 -0.56019 -0.01320 0.01546  51  PHE A CE2 
374  C CZ  . PHE A 51  ? 1.03890 1.59977 0.66092 -0.53697 -0.01815 0.01682  51  PHE A CZ  
375  N N   . GLN A 52  ? 1.02525 1.52675 0.58457 -0.56587 0.00629  -0.01576 52  GLN A N   
376  C CA  . GLN A 52  ? 0.91082 1.39252 0.44265 -0.56631 0.01105  -0.02477 52  GLN A CA  
377  C C   . GLN A 52  ? 1.10402 1.60165 0.62955 -0.56560 0.01446  -0.03014 52  GLN A C   
378  O O   . GLN A 52  ? 0.94141 1.45564 0.48007 -0.57862 0.01259  -0.02586 52  GLN A O   
379  C CB  . GLN A 52  ? 0.91527 1.38645 0.44601 -0.58380 0.01002  -0.02363 52  GLN A CB  
380  C CG  . GLN A 52  ? 0.95662 1.39773 0.45205 -0.58380 0.01378  -0.03350 52  GLN A CG  
381  C CD  . GLN A 52  ? 0.96286 1.40132 0.45802 -0.60327 0.01296  -0.03371 52  GLN A CD  
382  O OE1 . GLN A 52  ? 1.23625 1.69823 0.75073 -0.61184 0.01058  -0.02892 52  GLN A OE1 
383  N NE2 . GLN A 52  ? 1.00353 1.41942 0.46924 -0.62064 0.01593  -0.03983 52  GLN A NE2 
384  N N   . LYS A 53  ? 1.03565 1.52460 0.53400 -0.54749 0.01976  -0.03963 53  LYS A N   
385  C CA  . LYS A 53  ? 0.97364 1.47818 0.45863 -0.54243 0.02510  -0.04619 53  LYS A CA  
386  C C   . LYS A 53  ? 1.03609 1.51530 0.49158 -0.54488 0.02601  -0.05219 53  LYS A C   
387  O O   . LYS A 53  ? 1.04153 1.48868 0.46579 -0.53614 0.02646  -0.05965 53  LYS A O   
388  C CB  . LYS A 53  ? 0.99799 1.51355 0.46285 -0.52059 0.03129  -0.05522 53  LYS A CB  
389  C CG  . LYS A 53  ? 1.08234 1.62012 0.52674 -0.51479 0.03998  -0.06376 53  LYS A CG  
390  C CD  . LYS A 53  ? 1.01440 1.61005 0.48368 -0.52190 0.04468  -0.06330 53  LYS A CD  
391  C CE  . LYS A 53  ? 1.06787 1.67914 0.56213 -0.54785 0.04179  -0.05363 53  LYS A CE  
392  N NZ  . LYS A 53  ? 1.06880 1.66550 0.53513 -0.54837 0.04716  -0.05526 53  LYS A NZ  
393  N N   . VAL A 54  ? 1.01103 1.50074 0.46899 -0.55683 0.02525  -0.04970 54  VAL A N   
394  C CA  . VAL A 54  ? 1.09719 1.56347 0.52437 -0.55640 0.02400  -0.05577 54  VAL A CA  
395  C C   . VAL A 54  ? 1.07953 1.55409 0.48252 -0.54813 0.02919  -0.05907 54  VAL A C   
396  O O   . VAL A 54  ? 1.06755 1.56903 0.48473 -0.55253 0.03344  -0.05370 54  VAL A O   
397  C CB  . VAL A 54  ? 1.09379 1.55624 0.53617 -0.57444 0.01680  -0.04950 54  VAL A CB  
398  C CG1 . VAL A 54  ? 1.00743 1.46315 0.46852 -0.58285 0.01471  -0.04601 54  VAL A CG1 
399  C CG2 . VAL A 54  ? 1.24676 1.73054 0.71106 -0.58480 0.01431  -0.03914 54  VAL A CG2 
400  N N   . ASP A 55  ? 1.39378 1.84248 0.75481 -0.53593 0.02860  -0.06856 55  ASP A N   
401  C CA  . ASP A 55  ? 1.17069 1.61927 0.49680 -0.52383 0.03425  -0.07156 55  ASP A CA  
402  C C   . ASP A 55  ? 1.16601 1.61805 0.49825 -0.53852 0.02988  -0.06221 55  ASP A C   
403  O O   . ASP A 55  ? 1.15443 1.59552 0.49564 -0.54809 0.01962  -0.06029 55  ASP A O   
404  C CB  . ASP A 55  ? 1.23045 1.64337 0.50279 -0.50193 0.03113  -0.08608 55  ASP A CB  
405  C CG  . ASP A 55  ? 1.46196 1.87107 0.68705 -0.48080 0.03970  -0.08997 55  ASP A CG  
406  O OD1 . ASP A 55  ? 1.29916 1.70894 0.51518 -0.48642 0.03971  -0.08330 55  ASP A OD1 
407  O OD2 . ASP A 55  ? 1.32777 1.73087 0.51746 -0.45697 0.04732  -0.09973 55  ASP A OD2 
408  N N   . ALA A 56  ? 1.18239 1.64825 0.50448 -0.53883 0.03850  -0.05650 56  ALA A N   
409  C CA  . ALA A 56  ? 1.33840 1.79812 0.65609 -0.55088 0.03433  -0.04668 56  ALA A CA  
410  C C   . ALA A 56  ? 1.29993 1.72504 0.56979 -0.53636 0.02721  -0.05158 56  ALA A C   
411  O O   . ALA A 56  ? 1.25439 1.66635 0.51607 -0.54120 0.01945  -0.04508 56  ALA A O   
412  C CB  . ALA A 56  ? 1.20867 1.68502 0.51675 -0.55623 0.04718  -0.03945 56  ALA A CB  
413  N N   . GLU A 57  ? 1.33535 1.74215 0.56733 -0.51470 0.02748  -0.06443 57  GLU A N   
414  C CA  A GLU A 57  ? 1.56043 1.93369 0.74160 -0.49599 0.01671  -0.07330 57  GLU A CA  
415  C CA  B GLU A 57  ? 1.55638 1.92966 0.73762 -0.49603 0.01670  -0.07328 57  GLU A CA  
416  C C   . GLU A 57  ? 1.52533 1.88791 0.71584 -0.49613 0.00079  -0.08591 57  GLU A C   
417  O O   . GLU A 57  ? 1.48400 1.84087 0.67803 -0.49983 -0.01313 -0.08741 57  GLU A O   
418  C CB  A GLU A 57  ? 1.44122 1.79569 0.55869 -0.46693 0.02672  -0.08058 57  GLU A CB  
419  C CB  B GLU A 57  ? 1.45031 1.80487 0.56789 -0.46702 0.02676  -0.08050 57  GLU A CB  
420  C CG  A GLU A 57  ? 1.64417 2.00283 0.73672 -0.46569 0.04456  -0.06723 57  GLU A CG  
421  C CG  B GLU A 57  ? 1.72171 2.03731 0.77796 -0.44024 0.01169  -0.09428 57  GLU A CG  
422  C CD  A GLU A 57  ? 1.71546 2.05080 0.73390 -0.43189 0.05651  -0.07287 57  GLU A CD  
423  C CD  B GLU A 57  ? 1.77431 2.07333 0.80806 -0.43832 0.00286  -0.08772 57  GLU A CD  
424  O OE1 A GLU A 57  ? 1.81932 2.13935 0.81057 -0.40856 0.05056  -0.08882 57  GLU A OE1 
425  O OE1 B GLU A 57  ? 1.79331 2.10174 0.83822 -0.45279 0.01423  -0.07079 57  GLU A OE1 
426  O OE2 A GLU A 57  ? 1.69518 2.02333 0.67688 -0.42727 0.07234  -0.06113 57  GLU A OE2 
427  O OE2 B GLU A 57  ? 1.79669 2.07079 0.79755 -0.42038 -0.01772 -0.10135 57  GLU A OE2 
428  N N   . THR A 58  ? 1.47927 1.83782 0.66974 -0.49113 0.00232  -0.09589 58  THR A N   
429  C CA  . THR A 58  ? 1.36462 1.70782 0.55754 -0.49482 -0.01215 -0.10862 58  THR A CA  
430  C C   . THR A 58  ? 1.26440 1.62955 0.51618 -0.52303 -0.01197 -0.09871 58  THR A C   
431  O O   . THR A 58  ? 1.50850 1.86838 0.76689 -0.53207 -0.02301 -0.10576 58  THR A O   
432  C CB  . THR A 58  ? 1.36759 1.68700 0.52798 -0.47772 -0.01217 -0.12352 58  THR A CB  
433  O OG1 . THR A 58  ? 1.45116 1.78638 0.64192 -0.48508 0.00085  -0.11565 58  THR A OG1 
434  C CG2 . THR A 58  ? 1.43582 1.73624 0.53411 -0.44454 -0.00888 -0.13209 58  THR A CG2 
435  N N   . GLY A 59  ? 1.34944 1.74002 0.64146 -0.53585 -0.00042 -0.08390 59  GLY A N   
436  C CA  . GLY A 59  ? 1.15804 1.56584 0.49847 -0.55691 0.00034  -0.07481 59  GLY A CA  
437  C C   . GLY A 59  ? 1.17742 1.57214 0.51951 -0.55905 0.00277  -0.08031 59  GLY A C   
438  O O   . GLY A 59  ? 1.15051 1.55432 0.52486 -0.57476 0.00429  -0.07284 59  GLY A O   
439  N N   . LYS A 60  ? 1.20284 1.57231 0.50348 -0.54179 0.00289  -0.09341 60  LYS A N   
440  C CA  . LYS A 60  ? 1.25980 1.61014 0.54554 -0.54901 0.00433  -0.10045 60  LYS A CA  
441  C C   . LYS A 60  ? 1.18242 1.54929 0.49730 -0.54811 0.01361  -0.08990 60  LYS A C   
442  O O   . LYS A 60  ? 1.16442 1.55352 0.49085 -0.53365 0.01990  -0.08500 60  LYS A O   
443  C CB  . LYS A 60  ? 1.29564 1.61442 0.52114 -0.52713 0.00137  -0.11843 60  LYS A CB  
444  C CG  . LYS A 60  ? 1.40231 1.68874 0.59716 -0.52890 0.00125  -0.12785 60  LYS A CG  
445  C CD  . LYS A 60  ? 1.40265 1.66250 0.53724 -0.49520 -0.00004 -0.14456 60  LYS A CD  
446  C CE  . LYS A 60  ? 1.68169 1.90339 0.77823 -0.48940 -0.00056 -0.15396 60  LYS A CE  
447  N NZ  . LYS A 60  ? 1.78740 1.98649 0.82250 -0.44800 -0.00149 -0.17088 60  LYS A NZ  
448  N N   . PRO A 61  ? 1.17356 1.53035 0.49703 -0.56408 0.01424  -0.08701 61  PRO A N   
449  C CA  . PRO A 61  ? 1.19722 1.56285 0.53768 -0.55544 0.01985  -0.08004 61  PRO A CA  
450  C C   . PRO A 61  ? 1.19011 1.54309 0.49065 -0.52692 0.02394  -0.09067 61  PRO A C   
451  O O   . PRO A 61  ? 1.37079 1.69025 0.62029 -0.51782 0.02139  -0.10466 61  PRO A O   
452  C CB  . PRO A 61  ? 1.15244 1.49632 0.49034 -0.57748 0.01919  -0.07718 61  PRO A CB  
453  C CG  . PRO A 61  ? 1.18818 1.53369 0.53106 -0.60557 0.01526  -0.07791 61  PRO A CG  
454  C CD  . PRO A 61  ? 1.19263 1.53136 0.50819 -0.59282 0.01020  -0.08980 61  PRO A CD  
455  N N   . LEU A 62  ? 1.16203 1.54367 0.48323 -0.51153 0.02930  -0.08567 62  LEU A N   
456  C CA  . LEU A 62  ? 1.19854 1.58622 0.48804 -0.48203 0.03544  -0.09565 62  LEU A CA  
457  C C   . LEU A 62  ? 1.20733 1.58588 0.48504 -0.46510 0.03634  -0.09726 62  LEU A C   
458  O O   . LEU A 62  ? 1.35336 1.75001 0.66826 -0.47229 0.03521  -0.08687 62  LEU A O   
459  C CB  . LEU A 62  ? 1.17122 1.61022 0.48876 -0.47994 0.04265  -0.09127 62  LEU A CB  
460  C CG  . LEU A 62  ? 1.39188 1.83422 0.71289 -0.49187 0.04175  -0.08817 62  LEU A CG  
461  C CD1 . LEU A 62  ? 1.21754 1.70527 0.55736 -0.49377 0.05070  -0.08294 62  LEU A CD1 
462  C CD2 . LEU A 62  ? 1.23604 1.64128 0.50021 -0.47707 0.03961  -0.10178 62  LEU A CD2 
463  N N   . ALA A 63  ? 1.27400 1.61997 0.49268 -0.43788 0.03675  -0.11159 63  ALA A N   
464  C CA  . ALA A 63  ? 1.38373 1.71594 0.57442 -0.41029 0.03678  -0.11680 63  ALA A CA  
465  C C   . ALA A 63  ? 1.43573 1.81335 0.62051 -0.38028 0.04410  -0.12649 63  ALA A C   
466  O O   . ALA A 63  ? 1.42802 1.83235 0.61098 -0.37772 0.05070  -0.13148 63  ALA A O   
467  C CB  . ALA A 63  ? 1.38215 1.63989 0.49943 -0.39783 0.03072  -0.12853 63  ALA A CB  
468  N N   . GLY A 64  ? 1.31797 1.70676 0.49681 -0.35744 0.04350  -0.13006 64  GLY A N   
469  C CA  . GLY A 64  ? 1.33175 1.77547 0.50806 -0.33172 0.05063  -0.14243 64  GLY A CA  
470  C C   . GLY A 64  ? 1.28664 1.81801 0.53617 -0.35477 0.05682  -0.13447 64  GLY A C   
471  O O   . GLY A 64  ? 1.44694 2.04392 0.70487 -0.34075 0.06422  -0.14643 64  GLY A O   
472  N N   . ALA A 65  ? 1.22152 1.76048 0.52304 -0.39050 0.05351  -0.11687 65  ALA A N   
473  C CA  . ALA A 65  ? 1.13976 1.75232 0.50331 -0.41463 0.05586  -0.10986 65  ALA A CA  
474  C C   . ALA A 65  ? 1.12628 1.75032 0.49929 -0.40125 0.04768  -0.11138 65  ALA A C   
475  O O   . ALA A 65  ? 1.15858 1.72168 0.51081 -0.39086 0.03867  -0.10554 65  ALA A O   
476  C CB  . ALA A 65  ? 1.09004 1.69560 0.49394 -0.45177 0.05245  -0.09258 65  ALA A CB  
477  N N   . VAL A 66  ? 0.76555 1.51143 0.57615 -0.20432 -0.03991 -0.17485 66  VAL A N   
478  C CA  . VAL A 66  ? 0.85378 1.58769 0.69611 -0.18172 -0.04644 -0.18026 66  VAL A CA  
479  C C   . VAL A 66  ? 0.89960 1.58928 0.68544 -0.17650 -0.04181 -0.13738 66  VAL A C   
480  O O   . VAL A 66  ? 0.84654 1.51764 0.58362 -0.20236 -0.02278 -0.13274 66  VAL A O   
481  C CB  . VAL A 66  ? 0.80904 1.57184 0.70676 -0.19316 -0.03211 -0.24332 66  VAL A CB  
482  C CG1 . VAL A 66  ? 0.63572 1.37976 0.57212 -0.16483 -0.04749 -0.24831 66  VAL A CG1 
483  C CG2 . VAL A 66  ? 0.82069 1.61598 0.77862 -0.19508 -0.03460 -0.28563 66  VAL A CG2 
484  N N   . PHE A 67  ? 0.75135 1.41683 0.54548 -0.14483 -0.05879 -0.10582 67  PHE A N   
485  C CA  . PHE A 67  ? 0.78517 1.40604 0.53941 -0.13368 -0.05527 -0.06736 67  PHE A CA  
486  C C   . PHE A 67  ? 0.75451 1.36377 0.54463 -0.11475 -0.05633 -0.07532 67  PHE A C   
487  O O   . PHE A 67  ? 0.91890 1.53632 0.76646 -0.10120 -0.06812 -0.09685 67  PHE A O   
488  C CB  . PHE A 67  ? 0.71442 1.30660 0.45324 -0.11033 -0.07178 -0.01971 67  PHE A CB  
489  C CG  . PHE A 67  ? 0.78558 1.36812 0.48595 -0.12250 -0.07580 -0.00610 67  PHE A CG  
490  C CD1 . PHE A 67  ? 0.76997 1.38720 0.49017 -0.12796 -0.08375 -0.01903 67  PHE A CD1 
491  C CD2 . PHE A 67  ? 0.70743 1.23941 0.34830 -0.12781 -0.07538 0.01925  67  PHE A CD2 
492  C CE1 . PHE A 67  ? 0.83002 1.43736 0.51178 -0.13833 -0.09108 -0.00720 67  PHE A CE1 
493  C CE2 . PHE A 67  ? 0.90201 1.41514 0.49922 -0.13722 -0.08680 0.03207  67  PHE A CE2 
494  C CZ  . PHE A 67  ? 1.06593 1.61924 0.68398 -0.14233 -0.09476 0.01885  67  PHE A CZ  
495  N N   . ARG A 68  ? 0.79801 1.37545 0.55420 -0.11317 -0.04560 -0.05589 68  ARG A N   
496  C CA  . ARG A 68  ? 0.75445 1.30966 0.54007 -0.09304 -0.04611 -0.05511 68  ARG A CA  
497  C C   . ARG A 68  ? 0.81370 1.32954 0.55408 -0.08249 -0.04304 -0.01214 68  ARG A C   
498  O O   . ARG A 68  ? 0.74342 1.23742 0.43115 -0.09860 -0.03266 0.00180  68  ARG A O   
499  C CB  . ARG A 68  ? 0.72254 1.29347 0.53499 -0.10802 -0.03012 -0.10364 68  ARG A CB  
500  C CG  . ARG A 68  ? 0.94557 1.49132 0.77855 -0.08910 -0.03111 -0.10224 68  ARG A CG  
501  C CD  . ARG A 68  ? 0.92463 1.49745 0.80843 -0.09661 -0.02497 -0.16179 68  ARG A CD  
502  N NE  . ARG A 68  ? 0.92704 1.50929 0.87636 -0.07561 -0.05381 -0.18863 68  ARG A NE  
503  C CZ  . ARG A 68  ? 0.78717 1.39989 0.79797 -0.07598 -0.05994 -0.24968 68  ARG A CZ  
504  N NH1 . ARG A 68  ? 0.97035 1.61941 0.99094 -0.10068 -0.03312 -0.29635 68  ARG A NH1 
505  N NH2 . ARG A 68  ? 0.99714 1.60225 1.06113 -0.05261 -0.09504 -0.26785 68  ARG A NH2 
506  N N   . LEU A 69  ? 0.86310 1.36005 0.62583 -0.05669 -0.05297 0.00771  69  LEU A N   
507  C CA  . LEU A 69  ? 0.66919 1.13384 0.40282 -0.04283 -0.05143 0.04277  69  LEU A CA  
508  C C   . LEU A 69  ? 0.70541 1.14972 0.44585 -0.04061 -0.03874 0.03346  69  LEU A C   
509  O O   . LEU A 69  ? 0.79740 1.24365 0.57726 -0.03068 -0.04504 0.01861  69  LEU A O   
510  C CB  . LEU A 69  ? 0.72844 1.19242 0.48429 -0.02085 -0.06645 0.06560  69  LEU A CB  
511  C CG  . LEU A 69  ? 0.86672 1.29911 0.61133 -0.00425 -0.06529 0.09256  69  LEU A CG  
512  C CD1 . LEU A 69  ? 0.74689 1.15671 0.45489 -0.00659 -0.06968 0.10613  69  LEU A CD1 
513  C CD2 . LEU A 69  ? 0.85765 1.30329 0.63313 0.01046  -0.07406 0.10156  69  LEU A CD2 
514  N N   . TYR A 70  ? 0.78840 1.20788 0.48585 -0.05114 -0.02369 0.04219  70  TYR A N   
515  C CA  . TYR A 70  ? 0.62225 1.02292 0.32249 -0.05097 -0.00926 0.03351  70  TYR A CA  
516  C C   . TYR A 70  ? 0.85310 1.22142 0.53994 -0.02980 -0.01275 0.06806  70  TYR A C   
517  O O   . TYR A 70  ? 0.78957 1.13341 0.45053 -0.02326 -0.02009 0.09412  70  TYR A O   
518  C CB  . TYR A 70  ? 0.65085 1.04375 0.31088 -0.08353 0.01456  0.01439  70  TYR A CB  
519  C CG  . TYR A 70  ? 0.94001 1.37537 0.62504 -0.10829 0.02448  -0.03440 70  TYR A CG  
520  C CD1 . TYR A 70  ? 0.79469 1.25073 0.46124 -0.12739 0.02266  -0.04077 70  TYR A CD1 
521  C CD2 . TYR A 70  ? 0.58251 1.04134 0.31435 -0.11213 0.03419  -0.07945 70  TYR A CD2 
522  C CE1 . TYR A 70  ? 0.75408 1.25539 0.45005 -0.15160 0.03383  -0.09260 70  TYR A CE1 
523  C CE2 . TYR A 70  ? 0.84920 1.35456 0.61681 -0.13267 0.04194  -0.13402 70  TYR A CE2 
524  C CZ  . TYR A 70  ? 0.80762 1.33521 0.55794 -0.15341 0.04357  -0.14132 70  TYR A CZ  
525  O OH  . TYR A 70  ? 1.03919 1.61924 0.83124 -0.17539 0.05332  -0.20237 70  TYR A OH  
526  N N   . ARG A 71  ? 0.80990 1.17192 0.52345 -0.01792 -0.00995 0.06281  71  ARG A N   
527  C CA  . ARG A 71  ? 0.65918 0.99759 0.36843 -0.00008 -0.00993 0.08723  71  ARG A CA  
528  C C   . ARG A 71  ? 0.67009 0.98575 0.36661 -0.00675 0.00839  0.07838  71  ARG A C   
529  O O   . ARG A 71  ? 0.69109 1.01847 0.41050 -0.01326 0.01395  0.05024  71  ARG A O   
530  C CB  . ARG A 71  ? 0.83767 1.18733 0.58231 0.01469  -0.02199 0.09003  71  ARG A CB  
531  C CG  . ARG A 71  ? 1.03459 1.36945 0.77968 0.02824  -0.01801 0.10729  71  ARG A CG  
532  C CD  . ARG A 71  ? 1.04094 1.38484 0.80795 0.03116  -0.02666 0.10765  71  ARG A CD  
533  N NE  . ARG A 71  ? 1.18333 1.51993 0.95189 0.03793  -0.01819 0.11665  71  ARG A NE  
534  C CZ  . ARG A 71  ? 1.26099 1.58108 1.02700 0.03581  -0.01147 0.11141  71  ARG A CZ  
535  N NH1 . ARG A 71  ? 1.29514 1.60360 1.06041 0.03061  -0.01601 0.09665  71  ARG A NH1 
536  N NH2 . ARG A 71  ? 1.24332 1.56224 1.01163 0.03935  -0.00132 0.11655  71  ARG A NH2 
537  N N   . PHE A 72  ? 0.67114 0.95329 0.33393 -0.00394 0.01475  0.09942  72  PHE A N   
538  C CA  . PHE A 72  ? 0.70352 0.95815 0.34815 -0.01274 0.03384  0.09315  72  PHE A CA  
539  C C   . PHE A 72  ? 0.91734 1.15288 0.57119 0.00941  0.03199  0.11134  72  PHE A C   
540  O O   . PHE A 72  ? 0.99336 1.21964 0.64376 0.02631  0.01849  0.13306  72  PHE A O   
541  C CB  . PHE A 72  ? 0.74269 0.96117 0.32573 -0.03784 0.04503  0.09873  72  PHE A CB  
542  C CG  . PHE A 72  ? 0.91930 1.15847 0.49141 -0.06775 0.05346  0.07335  72  PHE A CG  
543  C CD1 . PHE A 72  ? 0.69384 0.95478 0.27778 -0.09240 0.07613  0.03371  72  PHE A CD1 
544  C CD2 . PHE A 72  ? 0.93164 1.17109 0.48939 -0.07144 0.03905  0.08265  72  PHE A CD2 
545  C CE1 . PHE A 72  ? 0.87401 1.16027 0.46023 -0.12092 0.08573  0.00144  72  PHE A CE1 
546  C CE2 . PHE A 72  ? 0.84859 1.10965 0.40100 -0.10084 0.04899  0.05508  72  PHE A CE2 
547  C CZ  . PHE A 72  ? 0.82281 1.10899 0.39139 -0.12624 0.07315  0.01322  72  PHE A CZ  
548  N N   . LEU A 73  ? 0.84495 1.07882 0.51472 0.00938  0.04459  0.09754  73  LEU A N   
549  C CA  . LEU A 73  ? 0.73995 0.95742 0.41736 0.02503  0.04827  0.10826  73  LEU A CA  
550  C C   . LEU A 73  ? 0.85193 1.03064 0.49787 0.01336  0.06682  0.10583  73  LEU A C   
551  O O   . LEU A 73  ? 0.68657 0.86928 0.33009 -0.00538 0.08273  0.08240  73  LEU A O   
552  C CB  . LEU A 73  ? 0.81310 1.05348 0.52499 0.03104  0.04688  0.09601  73  LEU A CB  
553  C CG  . LEU A 73  ? 0.96572 1.22877 0.69908 0.04139  0.03163  0.10538  73  LEU A CG  
554  C CD1 . LEU A 73  ? 1.18275 1.45097 0.92931 0.03973  0.03041  0.09684  73  LEU A CD1 
555  C CD2 . LEU A 73  ? 0.96074 1.22171 0.69672 0.05577  0.02936  0.12189  73  LEU A CD2 
556  N N   . PHE A 74  ? 0.74081 0.88161 0.36542 0.02434  0.06301  0.12626  74  PHE A N   
557  C CA  . PHE A 74  ? 0.90108 0.99046 0.48693 0.01235  0.07754  0.12833  74  PHE A CA  
558  C C   . PHE A 74  ? 1.05860 1.13557 0.66798 0.03332  0.07963  0.13102  74  PHE A C   
559  O O   . PHE A 74  ? 1.02846 1.12171 0.66959 0.05852  0.06436  0.13873  74  PHE A O   
560  C CB  . PHE A 74  ? 0.79130 0.82495 0.31573 0.00383  0.06536  0.15107  74  PHE A CB  
561  C CG  . PHE A 74  ? 1.10707 1.15161 0.60043 -0.02193 0.06522  0.14746  74  PHE A CG  
562  C CD1 . PHE A 74  ? 1.45302 1.50372 0.92494 -0.05931 0.09144  0.12231  74  PHE A CD1 
563  C CD2 . PHE A 74  ? 1.32140 1.37463 0.80991 -0.01076 0.03999  0.16383  74  PHE A CD2 
564  C CE1 . PHE A 74  ? 1.52947 1.59598 0.97783 -0.08601 0.09421  0.11166  74  PHE A CE1 
565  C CE2 . PHE A 74  ? 1.38045 1.44562 0.83928 -0.03694 0.04120  0.15809  74  PHE A CE2 
566  C CZ  . PHE A 74  ? 1.17887 1.24925 0.62069 -0.07423 0.06909  0.13037  74  PHE A CZ  
567  N N   . GLU A 75  ? 1.02393 1.07670 0.62075 0.02032  0.10060  0.11945  75  GLU A N   
568  C CA  . GLU A 75  ? 1.07545 1.10234 0.68335 0.03601  0.10428  0.12143  75  GLU A CA  
569  C C   . GLU A 75  ? 1.16800 1.11842 0.72322 0.03512  0.09424  0.14177  75  GLU A C   
570  O O   . GLU A 75  ? 1.20273 1.10892 0.70164 0.00473  0.10725  0.14272  75  GLU A O   
571  C CB  . GLU A 75  ? 0.86755 0.90434 0.48723 0.02204  0.13020  0.09768  75  GLU A CB  
572  C CG  . GLU A 75  ? 1.15194 1.16126 0.78189 0.03454  0.13751  0.09593  75  GLU A CG  
573  C CD  . GLU A 75  ? 1.43816 1.45663 1.07543 0.01789  0.16343  0.07108  75  GLU A CD  
574  O OE1 . GLU A 75  ? 1.37165 1.42308 1.01353 0.00070  0.17184  0.05280  75  GLU A OE1 
575  O OE2 . GLU A 75  ? 1.36846 1.36281 1.01126 0.02347  0.17324  0.06616  75  GLU A OE2 
576  N N   . GLU A 76  ? 1.13244 1.06483 0.70393 0.06625  0.06935  0.15510  76  GLU A N   
577  C CA  A GLU A 76  ? 1.12930 0.97832 0.64985 0.07276  0.04609  0.17696  76  GLU A CA  
578  C CA  B GLU A 76  ? 1.12758 0.97691 0.64859 0.07310  0.04584  0.17699  76  GLU A CA  
579  C C   . GLU A 76  ? 1.31260 1.12058 0.84661 0.08820  0.04828  0.17067  76  GLU A C   
580  O O   . GLU A 76  ? 1.36221 1.21636 0.96441 0.11375  0.04954  0.15328  76  GLU A O   
581  C CB  A GLU A 76  ? 1.21302 1.06607 0.74594 0.10204  0.00642  0.19218  76  GLU A CB  
582  C CB  B GLU A 76  ? 1.22745 1.08334 0.76374 0.10316  0.00648  0.19142  76  GLU A CB  
583  C CG  A GLU A 76  ? 1.30672 1.18149 0.81066 0.08421  0.00020  0.20213  76  GLU A CG  
584  C CG  B GLU A 76  ? 1.51877 1.28182 1.00447 0.11795  -0.03090 0.21444  76  GLU A CG  
585  C CD  A GLU A 76  ? 1.53547 1.37196 1.01156 0.10344  -0.04362 0.22453  76  GLU A CD  
586  C CD  B GLU A 76  ? 1.62895 1.41117 1.15281 0.15758  -0.07436 0.21890  76  GLU A CD  
587  O OE1 A GLU A 76  ? 1.69311 1.46288 1.15210 0.12549  -0.07211 0.23602  76  GLU A OE1 
588  O OE1 B GLU A 76  ? 1.27929 1.14933 0.88188 0.17587  -0.06925 0.19847  76  GLU A OE1 
589  O OE2 A GLU A 76  ? 1.45987 1.33054 0.93186 0.09790  -0.05308 0.22908  76  GLU A OE2 
590  O OE2 B GLU A 76  ? 1.57084 1.27806 1.04260 0.16815  -0.11503 0.24133  76  GLU A OE2 
591  N N   . ASN A 77  ? 1.31820 1.03775 0.78357 0.06819  0.05042  0.18252  77  ASN A N   
592  C CA  . ASN A 77  ? 1.41765 1.07787 0.88307 0.08021  0.04889  0.17888  77  ASN A CA  
593  C C   . ASN A 77  ? 1.39193 1.11066 0.91817 0.08009  0.08355  0.14824  77  ASN A C   
594  O O   . ASN A 77  ? 1.58401 1.27799 1.13632 0.09822  0.08221  0.13768  77  ASN A O   
595  C CB  . ASN A 77  ? 1.59339 1.22253 1.08844 0.12787  0.00244  0.18676  77  ASN A CB  
596  C CG  . ASN A 77  ? 1.83314 1.39080 1.25983 0.13048  -0.04048 0.21883  77  ASN A CG  
597  O OD1 . ASN A 77  ? 1.79456 1.38295 1.25770 0.16270  -0.07467 0.22164  77  ASN A OD1 
598  N ND2 . ASN A 77  ? 2.08361 1.54478 1.40618 0.09253  -0.03855 0.24139  77  ASN A ND2 
599  N N   . GLY A 78  ? 1.46128 1.25384 1.00948 0.06027  0.11142  0.13206  78  GLY A N   
600  C CA  . GLY A 78  ? 1.29438 1.14131 0.89405 0.06009  0.13804  0.10455  78  GLY A CA  
601  C C   . GLY A 78  ? 1.26616 1.16158 0.93599 0.09373  0.12794  0.09241  78  GLY A C   
602  O O   . GLY A 78  ? 1.47236 1.38925 1.17623 0.09560  0.14629  0.07065  78  GLY A O   
603  N N   . GLU A 79  ? 1.04233 0.95921 0.73512 0.11717  0.10088  0.10179  79  GLU A N   
604  C CA  . GLU A 79  ? 1.13560 1.10651 0.89856 0.14444  0.09352  0.08304  79  GLU A CA  
605  C C   . GLU A 79  ? 1.24798 1.28462 1.03821 0.14882  0.08353  0.08398  79  GLU A C   
606  O O   . GLU A 79  ? 1.01061 1.10994 0.85093 0.15214  0.09334  0.06246  79  GLU A O   
607  C CB  . GLU A 79  ? 1.27343 1.19619 1.05517 0.17828  0.06412  0.08183  79  GLU A CB  
608  C CG  . GLU A 79  ? 1.84311 1.69202 1.60157 0.17701  0.07002  0.07907  79  GLU A CG  
609  C CD  . GLU A 79  ? 2.12143 1.90892 1.89459 0.21467  0.02968  0.07953  79  GLU A CD  
610  O OE1 . GLU A 79  ? 2.08120 1.90140 1.89930 0.24482  -0.00041 0.07364  79  GLU A OE1 
611  O OE2 . GLU A 79  ? 2.34525 2.04970 2.08607 0.21458  0.02532  0.08354  79  GLU A OE2 
612  N N   . PHE A 80  ? 0.88925 0.89288 1.02435 0.24243  0.26718  0.18311  80  PHE A N   
613  C CA  . PHE A 80  ? 0.90701 0.95747 1.02719 0.22922  0.24781  0.18683  80  PHE A CA  
614  C C   . PHE A 80  ? 0.84930 0.88725 0.93186 0.20473  0.22857  0.16632  80  PHE A C   
615  O O   . PHE A 80  ? 0.99229 0.99809 1.06656 0.20244  0.23230  0.15507  80  PHE A O   
616  C CB  . PHE A 80  ? 0.81607 0.92274 0.95149 0.23900  0.24153  0.22502  80  PHE A CB  
617  C CG  . PHE A 80  ? 0.86769 0.98494 1.04763 0.26821  0.25937  0.24810  80  PHE A CG  
618  C CD1 . PHE A 80  ? 1.09586 1.23373 1.29858 0.27508  0.26567  0.24327  80  PHE A CD1 
619  C CD2 . PHE A 80  ? 1.13155 1.23682 1.32965 0.28651  0.26832  0.27335  80  PHE A CD2 
620  C CE1 . PHE A 80  ? 1.01397 1.15193 1.24729 0.28990  0.27244  0.25588  80  PHE A CE1 
621  C CE2 . PHE A 80  ? 1.20180 1.30520 1.42873 0.30081  0.27468  0.28862  80  PHE A CE2 
622  C CZ  . PHE A 80  ? 1.11739 1.23710 1.36301 0.30296  0.27651  0.27827  80  PHE A CZ  
623  N N   . VAL A 81  ? 1.01258 1.07709 1.07368 0.18591  0.20802  0.16020  81  VAL A N   
624  C CA  . VAL A 81  ? 0.96915 1.02907 0.99725 0.16324  0.18671  0.14267  81  VAL A CA  
625  C C   . VAL A 81  ? 1.00933 1.12531 1.02809 0.15509  0.17266  0.16687  81  VAL A C   
626  O O   . VAL A 81  ? 1.12151 1.27454 1.13850 0.14941  0.16385  0.17741  81  VAL A O   
627  C CB  . VAL A 81  ? 0.89057 0.92562 0.89646 0.14452  0.17128  0.11328  81  VAL A CB  
628  C CG1 . VAL A 81  ? 1.12164 1.15564 1.09740 0.12307  0.14681  0.09726  81  VAL A CG1 
629  C CG2 . VAL A 81  ? 1.02154 1.00143 1.03379 0.14940  0.18302  0.08917  81  VAL A CG2 
630  N N   . ALA A 82  ? 0.91142 1.03623 0.92276 0.15180  0.17096  0.17502  82  ALA A N   
631  C CA  . ALA A 82  ? 0.89868 1.07671 0.89818 0.14098  0.15802  0.19820  82  ALA A CA  
632  C C   . ALA A 82  ? 0.82878 1.00691 0.79407 0.11418  0.13752  0.17357  82  ALA A C   
633  O O   . ALA A 82  ? 0.79403 0.93370 0.74899 0.10723  0.13617  0.14365  82  ALA A O   
634  C CB  . ALA A 82  ? 0.96348 1.15433 0.97160 0.14896  0.16761  0.22384  82  ALA A CB  
635  N N   . GLU A 83  ? 0.99847 1.22056 0.94830 0.09939  0.12145  0.18520  83  GLU A N   
636  C CA  . GLU A 83  ? 1.05890 1.28443 0.97576 0.07296  0.10102  0.16432  83  GLU A CA  
637  C C   . GLU A 83  ? 0.94445 1.22075 0.84974 0.06108  0.09630  0.18675  83  GLU A C   
638  O O   . GLU A 83  ? 1.08919 1.41604 0.99704 0.05991  0.09187  0.21686  83  GLU A O   
639  C CB  . GLU A 83  ? 0.95346 1.18397 0.85502 0.05973  0.08489  0.15678  83  GLU A CB  
640  C CG  . GLU A 83  ? 1.06668 1.28662 0.93384 0.03299  0.06213  0.13127  83  GLU A CG  
641  C CD  . GLU A 83  ? 1.50541 1.72802 1.35349 0.01709  0.04533  0.12726  83  GLU A CD  
642  O OE1 . GLU A 83  ? 1.68889 1.93361 1.55096 0.02519  0.05280  0.14567  83  GLU A OE1 
643  O OE2 . GLU A 83  ? 1.57415 1.77643 1.39361 -0.00436 0.02469  0.10477  83  GLU A OE2 
644  N N   . ARG A 84  ? 0.93342 1.19936 0.82649 0.05070  0.09737  0.17126  84  ARG A N   
645  C CA  . ARG A 84  ? 0.82903 1.14042 0.70821 0.03584  0.09522  0.19047  84  ARG A CA  
646  C C   . ARG A 84  ? 0.89448 1.20741 0.74296 0.00781  0.08035  0.15970  84  ARG A C   
647  O O   . ARG A 84  ? 0.89025 1.16265 0.73591 0.00434  0.08088  0.12201  84  ARG A O   
648  C CB  . ARG A 84  ? 0.89194 1.19461 0.78281 0.04486  0.11277  0.20058  84  ARG A CB  
649  C CG  . ARG A 84  ? 1.11371 1.39711 1.03695 0.07465  0.12893  0.22253  84  ARG A CG  
650  C CD  . ARG A 84  ? 1.23226 1.56137 1.16896 0.08414  0.13031  0.27210  84  ARG A CD  
651  N NE  . ARG A 84  ? 1.14278 1.45211 1.11475 0.11481  0.14434  0.29007  84  ARG A NE  
652  C CZ  . ARG A 84  ? 1.36514 1.69882 1.35914 0.13118  0.14829  0.33146  84  ARG A CZ  
653  N NH1 . ARG A 84  ? 1.35951 1.73953 1.34233 0.11897  0.13819  0.36299  84  ARG A NH1 
654  N NH2 . ARG A 84  ? 1.44051 1.75062 1.46920 0.16006  0.16192  0.34129  84  ARG A NH2 
655  N N   . TYR A 85  ? 0.92580 1.28591 0.75350 -0.01184 0.06699  0.17453  85  TYR A N   
656  C CA  . TYR A 85  ? 0.83651 1.20310 0.63390 -0.04047 0.05344  0.14771  85  TYR A CA  
657  C C   . TYR A 85  ? 0.85741 1.26222 0.64160 -0.05786 0.05952  0.15774  85  TYR A C   
658  O O   . TYR A 85  ? 0.94670 1.38915 0.73754 -0.05330 0.06616  0.19752  85  TYR A O   
659  C CB  . TYR A 85  ? 0.86715 1.26126 0.64412 -0.05687 0.03469  0.15525  85  TYR A CB  
660  C CG  . TYR A 85  ? 0.80570 1.16186 0.58524 -0.04973 0.02523  0.14035  85  TYR A CG  
661  C CD1 . TYR A 85  ? 0.99854 1.36070 0.79946 -0.03028 0.03133  0.16410  85  TYR A CD1 
662  C CD2 . TYR A 85  ? 0.92577 1.24049 0.68599 -0.06414 0.00934  0.10231  85  TYR A CD2 
663  C CE1 . TYR A 85  ? 0.92202 1.25207 0.72105 -0.02880 0.02328  0.15009  85  TYR A CE1 
664  C CE2 . TYR A 85  ? 0.96263 1.24103 0.72033 -0.06167 -0.00182 0.09131  85  TYR A CE2 
665  C CZ  . TYR A 85  ? 1.08705 1.37460 0.86208 -0.04580 0.00584  0.11527  85  TYR A CZ  
666  O OH  . TYR A 85  ? 1.30201 1.55564 1.07066 -0.04801 -0.00454 0.10379  85  TYR A OH  
667  N N   . VAL A 86  ? 0.80461 1.19956 0.57044 -0.07890 0.05648  0.12071  86  VAL A N   
668  C CA  . VAL A 86  ? 0.65874 1.09185 0.40625 -0.10280 0.06232  0.12316  86  VAL A CA  
669  C C   . VAL A 86  ? 0.78162 1.22600 0.50045 -0.13282 0.04880  0.09244  86  VAL A C   
670  O O   . VAL A 86  ? 0.77375 1.17617 0.49398 -0.13388 0.04348  0.04737  86  VAL A O   
671  C CB  . VAL A 86  ? 0.76242 1.17208 0.52153 -0.09873 0.08062  0.10291  86  VAL A CB  
672  C CG1 . VAL A 86  ? 0.88157 1.33318 0.61628 -0.13036 0.08629  0.10060  86  VAL A CG1 
673  C CG2 . VAL A 86  ? 0.76732 1.16470 0.55159 -0.07148 0.09427  0.13556  86  VAL A CG2 
674  N N   . LEU A 87  ? 0.93897 1.43054 0.64204 -0.15445 0.04070  0.11385  87  LEU A N   
675  C CA  . LEU A 87  ? 0.74812 1.24817 0.43079 -0.18374 0.02890  0.08530  87  LEU A CA  
676  C C   . LEU A 87  ? 0.86134 1.37562 0.53338 -0.20585 0.04106  0.06146  87  LEU A C   
677  O O   . LEU A 87  ? 0.85213 1.39059 0.53261 -0.20853 0.04897  0.08617  87  LEU A O   
678  C CB  . LEU A 87  ? 0.87965 1.41134 0.57091 -0.19306 0.01376  0.11299  87  LEU A CB  
679  C CG  . LEU A 87  ? 0.84401 1.38657 0.51806 -0.22429 0.00329  0.08889  87  LEU A CG  
680  C CD1 . LEU A 87  ? 0.76043 1.26038 0.41773 -0.22664 -0.00607 0.05270  87  LEU A CD1 
681  C CD2 . LEU A 87  ? 0.79604 1.37631 0.48307 -0.23279 -0.00801 0.11908  87  LEU A CD2 
682  N N   . VAL A 88  ? 0.76394 1.26055 0.41898 -0.22188 0.04109  0.01060  88  VAL A N   
683  C CA  . VAL A 88  ? 0.84774 1.35599 0.49702 -0.24368 0.05469  -0.02352 88  VAL A CA  
684  C C   . VAL A 88  ? 0.96235 1.47964 0.60007 -0.27201 0.04374  -0.05098 88  VAL A C   
685  O O   . VAL A 88  ? 0.99451 1.48241 0.62706 -0.27031 0.02884  -0.07252 88  VAL A O   
686  C CB  . VAL A 88  ? 0.95515 1.41732 0.62640 -0.22659 0.06584  -0.06944 88  VAL A CB  
687  C CG1 . VAL A 88  ? 0.78144 1.26087 0.44719 -0.25239 0.08044  -0.11330 88  VAL A CG1 
688  C CG2 . VAL A 88  ? 0.76445 1.20934 0.46098 -0.19708 0.07778  -0.04089 88  VAL A CG2 
689  N N   . GLU A 89  ? 1.07130 1.62568 0.70637 -0.29863 0.05039  -0.04944 89  GLU A N   
690  C CA  . GLU A 89  ? 0.81813 1.38405 0.44484 -0.32831 0.04589  -0.07810 89  GLU A CA  
691  C C   . GLU A 89  ? 0.77047 1.31812 0.40289 -0.33631 0.05976  -0.13903 89  GLU A C   
692  O O   . GLU A 89  ? 0.84068 1.40811 0.47811 -0.34641 0.07687  -0.14846 89  GLU A O   
693  C CB  . GLU A 89  ? 0.84003 1.45703 0.46356 -0.35477 0.04471  -0.04712 89  GLU A CB  
694  C CG  . GLU A 89  ? 0.96669 1.59944 0.58161 -0.38844 0.04387  -0.07551 89  GLU A CG  
695  C CD  . GLU A 89  ? 1.12889 1.80907 0.74096 -0.41183 0.03524  -0.03897 89  GLU A CD  
696  O OE1 . GLU A 89  ? 0.82812 1.52668 0.44814 -0.39866 0.02764  0.00730  89  GLU A OE1 
697  O OE2 . GLU A 89  ? 1.16965 1.86725 0.77408 -0.44211 0.03606  -0.05790 89  GLU A OE2 
698  N N   . VAL A 90  ? 0.95145 1.45700 0.59011 -0.32951 0.05067  -0.18012 90  VAL A N   
699  C CA  . VAL A 90  ? 1.00497 1.48329 0.66757 -0.32649 0.06040  -0.23932 90  VAL A CA  
700  C C   . VAL A 90  ? 0.91554 1.42629 0.57930 -0.35878 0.07231  -0.26127 90  VAL A C   
701  O O   . VAL A 90  ? 1.17522 1.69883 0.85725 -0.36690 0.09064  -0.29187 90  VAL A O   
702  C CB  . VAL A 90  ? 0.91042 1.32158 0.59089 -0.30034 0.04137  -0.26897 90  VAL A CB  
703  C CG1 . VAL A 90  ? 0.90100 1.28079 0.62085 -0.28960 0.04837  -0.32388 90  VAL A CG1 
704  C CG2 . VAL A 90  ? 0.86065 1.24242 0.54064 -0.27230 0.03087  -0.24961 90  VAL A CG2 
705  N N   . ARG A 91  ? 1.08513 1.61103 0.73122 -0.37876 0.06346  -0.24642 91  ARG A N   
706  C CA  A ARG A 91  ? 1.04508 1.60197 0.68971 -0.41151 0.07517  -0.26692 91  ARG A CA  
707  C CA  B ARG A 91  ? 1.04645 1.60382 0.69107 -0.41162 0.07532  -0.26668 91  ARG A CA  
708  C C   . ARG A 91  ? 1.10895 1.70905 0.72845 -0.43907 0.06819  -0.22308 91  ARG A C   
709  O O   . ARG A 91  ? 1.03228 1.61688 0.64110 -0.43021 0.05084  -0.19745 91  ARG A O   
710  C CB  A ARG A 91  ? 1.12233 1.63278 0.78381 -0.40170 0.07074  -0.31424 91  ARG A CB  
711  C CB  B ARG A 91  ? 1.11816 1.62955 0.78040 -0.40187 0.07155  -0.31506 91  ARG A CB  
712  C CG  A ARG A 91  ? 1.26261 1.73673 0.96376 -0.37619 0.07774  -0.36121 91  ARG A CG  
713  C CG  B ARG A 91  ? 1.16268 1.70461 0.81995 -0.43511 0.08358  -0.33430 91  ARG A CG  
714  C CD  A ARG A 91  ? 1.40647 1.82721 1.12798 -0.35930 0.06539  -0.39843 91  ARG A CD  
715  C CD  B ARG A 91  ? 1.30964 1.80176 0.99063 -0.41845 0.07959  -0.38320 91  ARG A CD  
716  N NE  A ARG A 91  ? 1.33442 1.78183 1.04505 -0.38909 0.07422  -0.41206 91  ARG A NE  
717  N NE  B ARG A 91  ? 1.61502 2.13197 1.28484 -0.44935 0.08847  -0.39737 91  ARG A NE  
718  C CZ  A ARG A 91  ? 1.51296 1.92189 1.23671 -0.38048 0.06545  -0.44366 91  ARG A CZ  
719  C CZ  B ARG A 91  ? 1.64937 2.13744 1.33951 -0.44263 0.08956  -0.44079 91  ARG A CZ  
720  N NH1 A ARG A 91  ? 1.38144 1.72178 1.13036 -0.34316 0.04460  -0.46228 91  ARG A NH1 
721  N NH1 B ARG A 91  ? 1.77631 2.20975 1.50275 -0.40546 0.08011  -0.47257 91  ARG A NH1 
722  N NH2 A ARG A 91  ? 1.77092 2.20964 1.48167 -0.41079 0.07628  -0.45493 91  ARG A NH2 
723  N NH2 B ARG A 91  ? 1.27977 1.79464 0.95538 -0.47380 0.09909  -0.45092 91  ARG A NH2 
724  N N   A SER A 92  ? 1.29933 1.85137 0.59722 -0.22340 0.05127  -0.17659 92  SER A N   
725  N N   B SER A 92  ? 1.29953 1.85161 0.59727 -0.22331 0.05142  -0.17677 92  SER A N   
726  C CA  A SER A 92  ? 1.20107 1.73988 0.48565 -0.25013 0.04824  -0.16194 92  SER A CA  
727  C CA  B SER A 92  ? 1.20146 1.74155 0.48611 -0.25080 0.04842  -0.16191 92  SER A CA  
728  C C   A SER A 92  ? 1.24386 1.74937 0.49485 -0.23418 0.06465  -0.18377 92  SER A C   
729  C C   B SER A 92  ? 1.24459 1.75211 0.49561 -0.23553 0.06491  -0.18362 92  SER A C   
730  O O   A SER A 92  ? 1.27134 1.77995 0.50956 -0.21270 0.08064  -0.20880 92  SER A O   
731  O O   B SER A 92  ? 1.27297 1.78614 0.51128 -0.21578 0.08127  -0.20854 92  SER A O   
732  C CB  A SER A 92  ? 1.21252 1.81206 0.50421 -0.30062 0.04790  -0.14413 92  SER A CB  
733  C CB  B SER A 92  ? 1.21241 1.81426 0.50476 -0.30104 0.04811  -0.14421 92  SER A CB  
734  O OG  A SER A 92  ? 1.25269 1.89431 0.53088 -0.30966 0.06879  -0.16341 92  SER A OG  
735  O OG  B SER A 92  ? 1.33459 1.92452 0.62360 -0.33028 0.03589  -0.12173 92  SER A OG  
736  N N   . PRO A 93  ? 1.25173 1.72462 0.48875 -0.24386 0.06057  -0.17589 93  PRO A N   
737  C CA  . PRO A 93  ? 1.29537 1.73759 0.49958 -0.23176 0.07559  -0.19622 93  PRO A CA  
738  C C   . PRO A 93  ? 1.33841 1.83072 0.53012 -0.25564 0.09223  -0.20934 93  PRO A C   
739  O O   . PRO A 93  ? 1.34764 1.89507 0.55115 -0.29368 0.09001  -0.19560 93  PRO A O   
740  C CB  . PRO A 93  ? 1.28814 1.69838 0.48793 -0.24636 0.06504  -0.18144 93  PRO A CB  
741  C CG  . PRO A 93  ? 1.25240 1.69468 0.48112 -0.27899 0.04683  -0.15287 93  PRO A CG  
742  C CD  . PRO A 93  ? 1.22120 1.68001 0.47282 -0.26317 0.04137  -0.15007 93  PRO A CD  
743  N N   . GLU A 94  ? 1.58855 2.05955 0.75378 -0.23290 0.10900  -0.23638 94  GLU A N   
744  C CA  . GLU A 94  ? 1.79637 2.31386 0.94864 -0.25046 0.12686  -0.25471 94  GLU A CA  
745  C C   . GLU A 94  ? 1.44392 1.98942 0.58833 -0.29572 0.12449  -0.24136 94  GLU A C   
746  O O   . GLU A 94  ? 1.43981 1.94993 0.57604 -0.30246 0.11520  -0.23071 94  GLU A O   
747  C CB  . GLU A 94  ? 1.89181 2.37093 1.01492 -0.21637 0.14313  -0.28627 94  GLU A CB  
748  C CG  . GLU A 94  ? 2.18693 2.64409 1.31295 -0.17371 0.14759  -0.30332 94  GLU A CG  
749  C CD  . GLU A 94  ? 2.27452 2.70181 1.37068 -0.14505 0.16484  -0.33593 94  GLU A CD  
750  O OE1 . GLU A 94  ? 2.15587 2.59180 1.23234 -0.16062 0.17514  -0.34755 94  GLU A OE1 
751  O OE2 . GLU A 94  ? 2.25400 2.64785 1.34551 -0.10761 0.16752  -0.35052 94  GLU A OE2 
752  N N   . GLY A 95  ? 1.46743 2.07794 0.61333 -0.32770 0.13301  -0.24255 95  GLY A N   
753  C CA  . GLY A 95  ? 1.51789 2.15970 0.65383 -0.37386 0.12914  -0.22723 95  GLY A CA  
754  C C   . GLY A 95  ? 1.45525 2.11536 0.61220 -0.40560 0.10852  -0.19087 95  GLY A C   
755  O O   . GLY A 95  ? 1.52682 2.21139 0.67359 -0.44569 0.10249  -0.17469 95  GLY A O   
756  N N   . TYR A 96  ? 1.40547 2.05306 0.58953 -0.38880 0.09654  -0.17770 96  TYR A N   
757  C CA  . TYR A 96  ? 1.43174 2.09294 0.63787 -0.41576 0.07562  -0.14364 96  TYR A CA  
758  C C   . TYR A 96  ? 1.37251 2.08422 0.59888 -0.42478 0.07747  -0.13788 96  TYR A C   
759  O O   . TYR A 96  ? 1.41302 2.13831 0.64353 -0.39950 0.09222  -0.16107 96  TYR A O   
760  C CB  . TYR A 96  ? 1.32424 1.92930 0.54677 -0.39153 0.05803  -0.13191 96  TYR A CB  
761  C CG  . TYR A 96  ? 1.33459 1.90093 0.54191 -0.39787 0.05188  -0.12853 96  TYR A CG  
762  C CD1 . TYR A 96  ? 1.36351 1.89815 0.54571 -0.37702 0.06613  -0.15370 96  TYR A CD1 
763  C CD2 . TYR A 96  ? 1.31894 1.88110 0.53673 -0.42560 0.03155  -0.10074 96  TYR A CD2 
764  C CE1 . TYR A 96  ? 1.37392 1.87639 0.54291 -0.38460 0.06120  -0.15193 96  TYR A CE1 
765  C CE2 . TYR A 96  ? 1.32927 1.85992 0.53454 -0.43236 0.02625  -0.09954 96  TYR A CE2 
766  C CZ  . TYR A 96  ? 1.35557 1.85781 0.53692 -0.41243 0.04158  -0.12552 96  TYR A CZ  
767  O OH  . TYR A 96  ? 1.36623 1.83918 0.53584 -0.42045 0.03677  -0.12546 96  TYR A OH  
768  N N   . GLU A 97  ? 1.35095 2.09030 0.58920 -0.46221 0.06188  -0.10669 97  GLU A N   
769  C CA  . GLU A 97  ? 1.34578 2.14366 0.60259 -0.48275 0.06292  -0.09818 97  GLU A CA  
770  C C   . GLU A 97  ? 1.51342 2.30346 0.79758 -0.44627 0.06153  -0.10927 97  GLU A C   
771  O O   . GLU A 97  ? 1.37624 2.10883 0.67025 -0.41563 0.04777  -0.10436 97  GLU A O   
772  C CB  . GLU A 97  ? 1.36469 2.19108 0.63042 -0.53420 0.04140  -0.05860 97  GLU A CB  
773  C CG  . GLU A 97  ? 1.70453 2.54714 0.94079 -0.57534 0.04084  -0.04560 97  GLU A CG  
774  C CD  . GLU A 97  ? 1.75459 2.62266 0.99726 -0.62696 0.01696  -0.00369 97  GLU A CD  
775  O OE1 . GLU A 97  ? 1.62363 2.49975 0.89561 -0.63204 0.00176  0.01496  97  GLU A OE1 
776  O OE2 . GLU A 97  ? 1.77240 2.65096 0.98934 -0.66241 0.01204  0.01132  97  GLU A OE2 
777  N N   . PRO A 98  ? 1.52269 2.37183 0.81947 -0.44859 0.07548  -0.12589 98  PRO A N   
778  C CA  . PRO A 98  ? 1.26902 2.11052 0.58859 -0.40752 0.07601  -0.14365 98  PRO A CA  
779  C C   . PRO A 98  ? 1.25854 2.09916 0.60709 -0.41360 0.05226  -0.11818 98  PRO A C   
780  O O   . PRO A 98  ? 1.22246 2.11229 0.58414 -0.46052 0.04123  -0.09090 98  PRO A O   
781  C CB  . PRO A 98  ? 1.29226 2.21509 0.62158 -0.41952 0.09665  -0.16706 98  PRO A CB  
782  C CG  . PRO A 98  ? 1.33054 2.31406 0.65030 -0.48060 0.09944  -0.14753 98  PRO A CG  
783  C CD  . PRO A 98  ? 1.35089 2.27922 0.64096 -0.48842 0.09219  -0.13202 98  PRO A CD  
784  N N   . VAL A 99  ? 1.18641 1.96757 0.54226 -0.36625 0.04349  -0.12636 99  VAL A N   
785  C CA  . VAL A 99  ? 1.14797 1.92434 0.53219 -0.36189 0.02158  -0.10914 99  VAL A CA  
786  C C   . VAL A 99  ? 1.16972 1.93563 0.56512 -0.31213 0.02601  -0.13804 99  VAL A C   
787  O O   . VAL A 99  ? 1.24143 1.93211 0.62254 -0.26645 0.02424  -0.15017 99  VAL A O   
788  C CB  . VAL A 99  ? 1.18658 1.89182 0.56699 -0.35383 0.00198  -0.08824 99  VAL A CB  
789  C CG1 . VAL A 99  ? 1.07950 1.78730 0.49113 -0.35435 -0.02155 -0.06983 99  VAL A CG1 
790  C CG2 . VAL A 99  ? 1.14790 1.85670 0.51311 -0.39649 -0.00122 -0.06564 99  VAL A CG2 
791  N N   . VAL A 100 ? 1.11609 1.95885 0.53617 -0.32237 0.03127  -0.14909 100 VAL A N   
792  C CA  A VAL A 100 ? 1.14589 1.99319 0.58031 -0.27697 0.03569  -0.18060 100 VAL A CA  
793  C CA  B VAL A 100 ? 1.14521 1.99286 0.57971 -0.27707 0.03573  -0.18063 100 VAL A CA  
794  C C   . VAL A 100 ? 1.15058 2.01811 0.61917 -0.27291 0.01351  -0.17055 100 VAL A C   
795  O O   . VAL A 100 ? 1.08039 2.02215 0.57330 -0.31461 0.00723  -0.15453 100 VAL A O   
796  C CB  A VAL A 100 ? 1.13939 2.06568 0.58202 -0.28476 0.05916  -0.20980 100 VAL A CB  
797  C CB  B VAL A 100 ? 1.13422 2.06216 0.57747 -0.28560 0.05900  -0.20946 100 VAL A CB  
798  C CG1 A VAL A 100 ? 1.20107 2.08709 0.60938 -0.26759 0.07933  -0.22940 100 VAL A CG1 
799  C CG1 B VAL A 100 ? 1.11339 2.04779 0.57647 -0.23568 0.06082  -0.24419 100 VAL A CG1 
800  C CG2 A VAL A 100 ? 1.14002 2.16083 0.59727 -0.34866 0.06312  -0.19198 100 VAL A CG2 
801  C CG2 B VAL A 100 ? 1.18303 2.09050 0.59230 -0.28984 0.07962  -0.22017 100 VAL A CG2 
802  N N   . ASN A 101 ? 1.03589 1.83513 0.50397 -0.22426 0.00085  -0.17894 101 ASN A N   
803  C CA  . ASN A 101 ? 1.14145 1.95144 0.64200 -0.20836 -0.02146 -0.17705 101 ASN A CA  
804  C C   . ASN A 101 ? 0.97902 1.81532 0.49928 -0.25301 -0.04196 -0.14068 101 ASN A C   
805  O O   . ASN A 101 ? 0.96212 1.86343 0.51593 -0.27071 -0.05383 -0.13628 101 ASN A O   
806  C CB  . ASN A 101 ? 0.99072 1.87818 0.52201 -0.19278 -0.01538 -0.20848 101 ASN A CB  
807  C CG  . ASN A 101 ? 1.25724 2.11170 0.77333 -0.14378 0.00012  -0.24379 101 ASN A CG  
808  O OD1 . ASN A 101 ? 1.18323 1.94274 0.66961 -0.10998 -0.00206 -0.24369 101 ASN A OD1 
809  N ND2 . ASN A 101 ? 1.50498 2.43786 1.04155 -0.14195 0.01570  -0.27379 101 ASN A ND2 
810  N N   . THR A 102 ? 0.98530 1.76874 0.48610 -0.27092 -0.04801 -0.11436 102 THR A N   
811  C CA  . THR A 102 ? 1.08417 1.88123 0.60152 -0.31345 -0.06912 -0.07681 102 THR A CA  
812  C C   . THR A 102 ? 1.08222 1.80274 0.60636 -0.28535 -0.09278 -0.06720 102 THR A C   
813  O O   . THR A 102 ? 0.97994 1.63056 0.47923 -0.26105 -0.08791 -0.07275 102 THR A O   
814  C CB  . THR A 102 ? 1.10454 1.91195 0.60000 -0.36169 -0.05997 -0.05355 102 THR A CB  
815  O OG1 . THR A 102 ? 1.29242 2.17864 0.78436 -0.39351 -0.03945 -0.06144 102 THR A OG1 
816  C CG2 . THR A 102 ? 1.01250 1.81833 0.52248 -0.40261 -0.08515 -0.01145 102 THR A CG2 
817  N N   . PRO A 103 ? 0.92377 1.65395 0.48244 -0.28710 -0.11901 -0.05445 103 PRO A N   
818  C CA  . PRO A 103 ? 0.98176 1.64131 0.55061 -0.26351 -0.14250 -0.04581 103 PRO A CA  
819  C C   . PRO A 103 ? 0.93719 1.56619 0.49393 -0.29372 -0.14699 -0.01768 103 PRO A C   
820  O O   . PRO A 103 ? 1.10759 1.77635 0.66151 -0.34315 -0.14505 0.00765  103 PRO A O   
821  C CB  . PRO A 103 ? 0.87985 1.56700 0.49605 -0.26677 -0.17133 -0.03677 103 PRO A CB  
822  C CG  . PRO A 103 ? 0.93374 1.69862 0.56202 -0.27228 -0.15992 -0.05401 103 PRO A CG  
823  C CD  . PRO A 103 ? 1.04928 1.85389 0.64310 -0.30503 -0.12909 -0.05271 103 PRO A CD  
824  N N   . ILE A 104 ? 1.01478 1.57411 0.56383 -0.26469 -0.15336 -0.02253 104 ILE A N   
825  C CA  . ILE A 104 ? 0.99784 1.52650 0.53810 -0.28571 -0.15764 -0.00248 104 ILE A CA  
826  C C   . ILE A 104 ? 1.10379 1.59382 0.67368 -0.27353 -0.18601 0.00754  104 ILE A C   
827  O O   . ILE A 104 ? 1.31001 1.80592 0.89817 -0.30550 -0.20378 0.03564  104 ILE A O   
828  C CB  . ILE A 104 ? 0.97418 1.46004 0.47671 -0.26598 -0.13521 -0.02012 104 ILE A CB  
829  C CG1 . ILE A 104 ? 1.20022 1.72221 0.67727 -0.28040 -0.10928 -0.02958 104 ILE A CG1 
830  C CG2 . ILE A 104 ? 1.27291 1.72861 0.77249 -0.28330 -0.14278 -0.00329 104 ILE A CG2 
831  C CD1 . ILE A 104 ? 1.61185 2.08999 1.05457 -0.26538 -0.09065 -0.04328 104 ILE A CD1 
832  N N   . ALA A 105 ? 1.07318 1.52064 0.64753 -0.22717 -0.19140 -0.01522 105 ALA A N   
833  C CA  . ALA A 105 ? 1.04692 1.45606 0.64927 -0.21028 -0.21611 -0.01293 105 ALA A CA  
834  C C   . ALA A 105 ? 1.03566 1.44088 0.66825 -0.17895 -0.23474 -0.02802 105 ALA A C   
835  O O   . ALA A 105 ? 0.85167 1.26884 0.47359 -0.16039 -0.22495 -0.04545 105 ALA A O   
836  C CB  . ALA A 105 ? 0.90275 1.25703 0.48018 -0.18606 -0.20639 -0.02630 105 ALA A CB  
837  N N   . ARG A 106 ? 1.02386 1.41186 0.69780 -0.17227 -0.26279 -0.02294 106 ARG A N   
838  C CA  . ARG A 106 ? 0.78090 1.15650 0.49129 -0.14106 -0.28566 -0.03884 106 ARG A CA  
839  C C   . ARG A 106 ? 1.03504 1.35807 0.75554 -0.11332 -0.29916 -0.05073 106 ARG A C   
840  O O   . ARG A 106 ? 1.15551 1.47897 0.89314 -0.12840 -0.30643 -0.03927 106 ARG A O   
841  C CB  . ARG A 106 ? 0.83289 1.24627 0.59870 -0.16110 -0.31028 -0.02364 106 ARG A CB  
842  C CG  . ARG A 106 ? 1.03642 1.43586 0.85114 -0.12834 -0.33740 -0.04258 106 ARG A CG  
843  C CD  . ARG A 106 ? 1.20928 1.63068 1.08878 -0.14399 -0.36337 -0.02948 106 ARG A CD  
844  N NE  . ARG A 106 ? 1.43232 1.85165 1.36576 -0.11503 -0.38784 -0.05096 106 ARG A NE  
845  C CZ  . ARG A 106 ? 1.40233 1.84074 1.40091 -0.11666 -0.40864 -0.05165 106 ARG A CZ  
846  N NH1 . ARG A 106 ? 1.40341 1.85385 1.41565 -0.15029 -0.41044 -0.02366 106 ARG A NH1 
847  N NH2 . ARG A 106 ? 1.13273 1.57466 1.18056 -0.08810 -0.42833 -0.07715 106 ARG A NH2 
848  N N   . ILE A 107 ? 0.99229 1.28019 0.69907 -0.08321 -0.30045 -0.06897 107 ILE A N   
849  C CA  . ILE A 107 ? 1.08657 1.33277 0.79461 -0.06681 -0.31002 -0.07700 107 ILE A CA  
850  C C   . ILE A 107 ? 0.99909 1.23185 0.74644 -0.05662 -0.33710 -0.07968 107 ILE A C   
851  O O   . ILE A 107 ? 1.11494 1.35803 0.85632 -0.05357 -0.32934 -0.08144 107 ILE A O   
852  C CB  . ILE A 107 ? 1.06215 1.27152 0.70760 -0.05728 -0.28047 -0.08500 107 ILE A CB  
853  C CG1 . ILE A 107 ? 0.90180 1.12345 0.51252 -0.07099 -0.25430 -0.08046 107 ILE A CG1 
854  C CG2 . ILE A 107 ? 0.97107 1.14301 0.61595 -0.05104 -0.28710 -0.08863 107 ILE A CG2 
855  C CD1 . ILE A 107 ? 1.07498 1.25831 0.63025 -0.05907 -0.22582 -0.09051 107 ILE A CD1 
856  N N   . THR A 108 ? 1.07102 1.29472 0.86868 -0.05382 -0.35670 -0.07851 108 THR A N   
857  C CA  . THR A 108 ? 1.22253 1.44019 1.06399 -0.06308 -0.37075 -0.06488 108 THR A CA  
858  C C   . THR A 108 ? 1.29114 1.51729 1.12189 -0.07354 -0.35372 -0.05987 108 THR A C   
859  O O   . THR A 108 ? 1.43448 1.63405 1.26577 -0.08049 -0.35630 -0.05521 108 THR A O   
860  C CB  . THR A 108 ? 1.30083 1.53835 1.22273 -0.04199 -0.39609 -0.08214 108 THR A CB  
861  O OG1 . THR A 108 ? 1.27299 1.57530 1.22008 -0.02983 -0.38134 -0.10556 108 THR A OG1 
862  C CG2 . THR A 108 ? 1.19768 1.50511 1.13110 -0.04856 -0.39445 -0.08738 108 THR A CG2 
863  N N   . VAL A 109 ? 1.21820 1.47863 1.04611 -0.05135 -0.33982 -0.07956 109 VAL A N   
864  C CA  . VAL A 109 ? 1.31306 1.57329 1.14181 -0.02527 -0.32247 -0.10128 109 VAL A CA  
865  C C   . VAL A 109 ? 1.46883 1.75674 1.36223 -0.01255 -0.33762 -0.10835 109 VAL A C   
866  O O   . VAL A 109 ? 1.56659 1.86704 1.48187 0.01422  -0.33827 -0.12434 109 VAL A O   
867  C CB  . VAL A 109 ? 1.24881 1.49751 1.03666 0.01405  -0.29271 -0.12805 109 VAL A CB  
868  C CG1 . VAL A 109 ? 1.46345 1.70011 1.24975 0.04136  -0.28056 -0.14878 109 VAL A CG1 
869  C CG2 . VAL A 109 ? 1.35764 1.58198 1.08439 0.00225  -0.27444 -0.12200 109 VAL A CG2 
870  N N   . THR A 110 ? 1.76136 2.05762 1.68580 -0.02882 -0.34928 -0.09977 110 THR A N   
871  C CA  . THR A 110 ? 1.90522 2.21850 1.89051 -0.01388 -0.36353 -0.11057 110 THR A CA  
872  C C   . THR A 110 ? 2.00280 2.29289 1.98814 0.01373  -0.35554 -0.13725 110 THR A C   
873  O O   . THR A 110 ? 2.04787 2.33302 2.02770 -0.00264 -0.35482 -0.13136 110 THR A O   
874  C CB  . THR A 110 ? 2.00344 2.35477 2.03069 -0.04746 -0.38093 -0.08628 110 THR A CB  
875  O OG1 . THR A 110 ? 2.07732 2.43570 2.08720 -0.06990 -0.37545 -0.07670 110 THR A OG1 
876  C CG2 . THR A 110 ? 1.88648 2.27772 1.91545 -0.07208 -0.38341 -0.06416 110 THR A CG2 
877  N N   . LYS A 111 ? 2.05442 2.33474 2.04592 0.05504  -0.34949 -0.16751 111 LYS A N   
878  C CA  . LYS A 111 ? 2.03344 2.29850 2.02605 0.08291  -0.34207 -0.19477 111 LYS A CA  
879  C C   . LYS A 111 ? 1.89306 2.16186 1.94790 0.08758  -0.36308 -0.20445 111 LYS A C   
880  O O   . LYS A 111 ? 1.80285 2.07824 1.89497 0.09555  -0.37736 -0.20864 111 LYS A O   
881  C CB  . LYS A 111 ? 2.00271 2.25973 1.96800 0.12612  -0.32484 -0.22251 111 LYS A CB  
882  C CG  . LYS A 111 ? 2.09105 2.33926 1.99497 0.12709  -0.30246 -0.21561 111 LYS A CG  
883  C CD  . LYS A 111 ? 2.03699 2.27952 1.91783 0.17267  -0.28705 -0.24003 111 LYS A CD  
884  C CE  . LYS A 111 ? 1.85504 2.08494 1.67771 0.17477  -0.26499 -0.23162 111 LYS A CE  
885  N NZ  . LYS A 111 ? 1.88665 2.11097 1.68933 0.22004  -0.25306 -0.24996 111 LYS A NZ  
886  N N   . ASP A 112 ? 2.12976 2.14935 1.77991 0.52672  0.19341  -0.67584 112 ASP A N   
887  C CA  . ASP A 112 ? 2.24321 2.19286 2.01105 0.56204  0.26381  -0.73122 112 ASP A CA  
888  C C   . ASP A 112 ? 2.49286 2.40414 2.15677 0.53895  0.31780  -0.85180 112 ASP A C   
889  O O   . ASP A 112 ? 2.52862 2.48510 2.08021 0.50572  0.33515  -0.85300 112 ASP A O   
890  C CB  . ASP A 112 ? 2.17582 2.17226 2.07584 0.61299  0.31181  -0.68318 112 ASP A CB  
891  C CG  . ASP A 112 ? 2.48231 2.41436 2.51170 0.65166  0.39816  -0.75162 112 ASP A CG  
892  O OD1 . ASP A 112 ? 2.47982 2.32732 2.62135 0.66303  0.39551  -0.75304 112 ASP A OD1 
893  O OD2 . ASP A 112 ? 2.52977 2.49395 2.55304 0.66908  0.47247  -0.80446 112 ASP A OD2 
894  N N   . PRO A 113 ? 2.57051 2.38103 2.26974 0.52422  0.33932  -0.90724 113 PRO A N   
895  C CA  . PRO A 113 ? 2.70226 2.45826 2.28048 0.47057  0.37404  -0.96909 113 PRO A CA  
896  C C   . PRO A 113 ? 2.92262 2.67473 2.50328 0.48989  0.46137  -1.00536 113 PRO A C   
897  O O   . PRO A 113 ? 2.90488 2.64484 2.34000 0.44790  0.47657  -1.03729 113 PRO A O   
898  C CB  . PRO A 113 ? 2.67955 2.33100 2.31342 0.46255  0.37131  -1.00795 113 PRO A CB  
899  C CG  . PRO A 113 ? 2.66815 2.30281 2.49887 0.52462  0.37545  -0.97622 113 PRO A CG  
900  C CD  . PRO A 113 ? 2.39042 2.12495 2.23161 0.55163  0.32480  -0.90274 113 PRO A CD  
901  N N   . GLU A 114 ? 3.12080 2.88102 2.86744 0.55297  0.51527  -0.99595 114 GLU A N   
902  C CA  . GLU A 114 ? 3.26536 3.02487 3.03124 0.57464  0.60047  -1.02932 114 GLU A CA  
903  C C   . GLU A 114 ? 3.32547 3.18335 3.03854 0.57734  0.61235  -0.98852 114 GLU A C   
904  O O   . GLU A 114 ? 3.44736 3.34978 3.28727 0.62663  0.65953  -0.96398 114 GLU A O   
905  C CB  . GLU A 114 ? 3.44188 3.16299 3.43271 0.63586  0.65017  -1.03060 114 GLU A CB  
906  C CG  . GLU A 114 ? 3.38305 3.13712 3.55690 0.68448  0.61347  -0.95112 114 GLU A CG  
907  C CD  . GLU A 114 ? 3.57833 3.29519 3.98608 0.73991  0.65796  -0.93004 114 GLU A CD  
908  O OE1 . GLU A 114 ? 3.68847 3.36205 4.11702 0.74074  0.72125  -0.98912 114 GLU A OE1 
909  O OE2 . GLU A 114 ? 3.57755 3.31072 4.15207 0.77909  0.62309  -0.84817 114 GLU A OE2 
910  N N   . THR A 115 ? 3.21093 3.10180 2.74239 0.51936  0.56425  -0.97456 115 THR A N   
911  C CA  . THR A 115 ? 3.15905 3.13473 2.61134 0.50439  0.56502  -0.93261 115 THR A CA  
912  C C   . THR A 115 ? 2.79271 2.86394 2.38256 0.55624  0.54805  -0.86312 115 THR A C   
913  O O   . THR A 115 ? 2.80684 2.92766 2.46633 0.58762  0.60214  -0.84508 115 THR A O   
914  C CB  . THR A 115 ? 3.27309 3.22697 2.66749 0.50465  0.64897  -0.97474 115 THR A CB  
915  O OG1 . THR A 115 ? 3.36146 3.31525 2.93674 0.57170  0.72092  -0.98936 115 THR A OG1 
916  C CG2 . THR A 115 ? 3.21509 3.08409 2.47302 0.46458  0.65246  -1.04210 115 THR A CG2 
917  N N   . GLY A 116 ? 2.39391 2.48857 2.01691 0.56799  0.46788  -0.81893 116 GLY A N   
918  C CA  . GLY A 116 ? 2.32529 2.50471 2.05176 0.62373  0.43401  -0.73916 116 GLY A CA  
919  C C   . GLY A 116 ? 2.29566 2.54520 1.89761 0.59065  0.35323  -0.67127 116 GLY A C   
920  O O   . GLY A 116 ? 2.23124 2.45680 1.69693 0.52686  0.30842  -0.68400 116 GLY A O   
921  N N   . LYS A 117 ? 2.29123 2.61101 1.96537 0.60832  0.32650  -0.57211 117 LYS A N   
922  C CA  . LYS A 117 ? 2.15895 2.54576 1.73364 0.57688  0.25710  -0.50497 117 LYS A CA  
923  C C   . LYS A 117 ? 2.14354 2.49191 1.71953 0.55037  0.17616  -0.46379 117 LYS A C   
924  O O   . LYS A 117 ? 2.12509 2.39464 1.76862 0.55476  0.17213  -0.48543 117 LYS A O   
925  C CB  . LYS A 117 ? 2.08333 2.55747 1.73674 0.60068  0.26166  -0.41966 117 LYS A CB  
926  C CG  . LYS A 117 ? 2.07803 2.54529 1.91856 0.63318  0.24503  -0.34449 117 LYS A CG  
927  C CD  . LYS A 117 ? 2.02352 2.58549 1.93454 0.65069  0.24433  -0.26215 117 LYS A CD  
928  C CE  . LYS A 117 ? 2.03572 2.59528 2.13229 0.67882  0.21847  -0.18117 117 LYS A CE  
929  N NZ  . LYS A 117 ? 1.99620 2.65276 2.16703 0.69274  0.21415  -0.10189 117 LYS A NZ  
930  N N   . VAL A 118 ? 1.91406 2.31674 1.41847 0.52033  0.11543  -0.40513 118 VAL A N   
931  C CA  . VAL A 118 ? 1.82230 2.19537 1.31508 0.48699  0.04430  -0.37130 118 VAL A CA  
932  C C   . VAL A 118 ? 1.84013 2.20707 1.46995 0.50167  0.02078  -0.28763 118 VAL A C   
933  O O   . VAL A 118 ? 1.81892 2.24497 1.52247 0.52485  0.03046  -0.22512 118 VAL A O   
934  C CB  . VAL A 118 ? 1.80412 2.23752 1.18200 0.44824  -0.00546 -0.34345 118 VAL A CB  
935  C CG1 . VAL A 118 ? 1.87045 2.26019 1.18259 0.39075  -0.00774 -0.38651 118 VAL A CG1 
936  C CG2 . VAL A 118 ? 1.64519 2.16975 1.02948 0.46203  0.00795  -0.28446 118 VAL A CG2 
937  N N   . THR A 119 ? 1.92391 2.21929 1.58629 0.48433  -0.01231 -0.28448 119 THR A N   
938  C CA  . THR A 119 ? 1.70667 1.98515 1.47998 0.48683  -0.04394 -0.20232 119 THR A CA  
939  C C   . THR A 119 ? 1.70436 1.96363 1.41911 0.43363  -0.10560 -0.17455 119 THR A C   
940  O O   . THR A 119 ? 1.69636 1.90217 1.34823 0.40760  -0.11516 -0.23449 119 THR A O   
941  C CB  . THR A 119 ? 1.70599 1.90152 1.60027 0.51918  -0.01410 -0.22141 119 THR A CB  
942  O OG1 . THR A 119 ? 2.12596 2.34075 2.08988 0.56833  0.05207  -0.25281 119 THR A OG1 
943  C CG2 . THR A 119 ? 1.64525 1.82301 1.64758 0.51687  -0.05621 -0.12490 119 THR A CG2 
944  N N   . TYR A 120 ? 1.58620 1.88972 1.32414 0.41414  -0.14463 -0.08749 120 TYR A N   
945  C CA  . TYR A 120 ? 1.14551 1.43900 0.82940 0.35817  -0.19514 -0.05964 120 TYR A CA  
946  C C   . TYR A 120 ? 1.15396 1.40750 0.91631 0.34350  -0.22439 0.01317  120 TYR A C   
947  O O   . TYR A 120 ? 1.41665 1.69767 1.26630 0.36927  -0.22450 0.07741  120 TYR A O   
948  C CB  . TYR A 120 ? 1.14323 1.52561 0.76213 0.33333  -0.21506 -0.02615 120 TYR A CB  
949  C CG  . TYR A 120 ? 1.14654 1.57418 0.69003 0.34861  -0.18962 -0.08165 120 TYR A CG  
950  C CD1 . TYR A 120 ? 1.32801 1.71911 0.82131 0.30480  -0.18918 -0.13221 120 TYR A CD1 
951  C CD2 . TYR A 120 ? 1.34976 1.83482 0.91396 0.38838  -0.15263 -0.07404 120 TYR A CD2 
952  C CE1 . TYR A 120 ? 1.38375 1.78695 0.85655 0.29504  -0.16039 -0.16028 120 TYR A CE1 
953  C CE2 . TYR A 120 ? 1.58985 2.11236 1.07180 0.39607  -0.12856 -0.12145 120 TYR A CE2 
954  C CZ  . TYR A 120 ? 1.62384 2.08981 1.08638 0.33805  -0.13197 -0.15656 120 TYR A CZ  
955  O OH  . TYR A 120 ? 1.88804 2.35720 1.32728 0.31943  -0.10888 -0.17690 120 TYR A OH  
956  N N   . GLU A 121 ? 1.33665 1.52635 1.06849 0.29891  -0.25078 0.00507  121 GLU A N   
957  C CA  . GLU A 121 ? 1.33430 1.47013 1.12261 0.27584  -0.27892 0.06978  121 GLU A CA  
958  C C   . GLU A 121 ? 1.27187 1.40200 0.98469 0.20465  -0.31377 0.08677  121 GLU A C   
959  O O   . GLU A 121 ? 1.44705 1.54774 1.09980 0.17795  -0.31125 0.02218  121 GLU A O   
960  C CB  . GLU A 121 ? 1.53846 1.57285 1.38735 0.29710  -0.26029 0.03184  121 GLU A CB  
961  C CG  . GLU A 121 ? 1.89099 1.87029 1.82533 0.29001  -0.28541 0.11141  121 GLU A CG  
962  C CD  . GLU A 121 ? 2.00278 1.90641 1.89061 0.22839  -0.31169 0.11497  121 GLU A CD  
963  O OE1 . GLU A 121 ? 1.83961 1.73702 1.64151 0.19380  -0.30854 0.05152  121 GLU A OE1 
964  O OE2 . GLU A 121 ? 2.14335 1.99373 2.08466 0.21293  -0.33596 0.18324  121 GLU A OE2 
965  N N   . VAL A 122 ? 1.41976 1.57914 1.13908 0.17093  -0.34486 0.17082  122 VAL A N   
966  C CA  . VAL A 122 ? 1.27850 1.44299 0.92547 0.09777  -0.36986 0.18806  122 VAL A CA  
967  C C   . VAL A 122 ? 1.07171 1.15993 0.73420 0.05482  -0.39410 0.23892  122 VAL A C   
968  O O   . VAL A 122 ? 1.27107 1.36313 0.98774 0.05961  -0.40576 0.31122  122 VAL A O   
969  C CB  . VAL A 122 ? 1.13327 1.31367 0.78584 0.08870  -0.33459 0.18486  122 VAL A CB  
970  C CG1 . VAL A 122 ? 1.22731 1.39150 0.86591 0.03738  -0.30478 0.16781  122 VAL A CG1 
971  C CG2 . VAL A 122 ? 0.97247 1.17229 0.62252 0.08877  -0.31377 0.14837  122 VAL A CG2 
972  N N   . GLU A 123 ? 1.37129 1.38951 0.99365 0.01254  -0.39100 0.19373  123 GLU A N   
973  C CA  . GLU A 123 ? 1.19588 1.13657 0.81214 -0.04195 -0.41029 0.23652  123 GLU A CA  
974  C C   . GLU A 123 ? 1.18049 1.14018 0.74341 -0.11648 -0.39199 0.22586  123 GLU A C   
975  O O   . GLU A 123 ? 1.26902 1.28599 0.83355 -0.11174 -0.34897 0.16846  123 GLU A O   
976  C CB  . GLU A 123 ? 1.45179 1.29166 1.09299 -0.03258 -0.39306 0.17923  123 GLU A CB  
977  C CG  . GLU A 123 ? 1.75310 1.55949 1.48695 0.04193  -0.37883 0.17446  123 GLU A CG  
978  C CD  . GLU A 123 ? 2.14367 1.84336 1.90363 0.04273  -0.36128 0.11996  123 GLU A CD  
979  O OE1 . GLU A 123 ? 2.11279 1.76032 1.82357 -0.01876 -0.36628 0.10442  123 GLU A OE1 
980  O OE2 . GLU A 123 ? 2.27544 1.94247 2.10882 0.10236  -0.33815 0.08899  123 GLU A OE2 
981  N N   . ALA A 124 ? 1.51358 1.41859 1.06324 -0.17529 -0.40335 0.27196  124 ALA A N   
982  C CA  . ALA A 124 ? 1.44309 1.35152 0.97068 -0.24568 -0.36869 0.25341  124 ALA A CA  
983  C C   . ALA A 124 ? 1.50919 1.32247 0.97187 -0.30688 -0.38527 0.23140  124 ALA A C   
984  O O   . ALA A 124 ? 1.72279 1.44916 1.16958 -0.30367 -0.42240 0.25234  124 ALA A O   
985  C CB  . ALA A 124 ? 1.24743 1.17364 0.80033 -0.27995 -0.36643 0.31173  124 ALA A CB  
986  N N   . VAL A 125 ? 1.57824 2.07125 0.90890 -0.73890 -0.42399 0.17189  125 VAL A N   
987  C CA  . VAL A 125 ? 1.66034 2.28847 0.97847 -0.86745 -0.40066 0.16464  125 VAL A CA  
988  C C   . VAL A 125 ? 1.77208 2.31876 0.98240 -0.96379 -0.38691 0.19968  125 VAL A C   
989  O O   . VAL A 125 ? 1.72008 2.30370 0.93314 -0.92535 -0.36463 0.21122  125 VAL A O   
990  C CB  . VAL A 125 ? 1.54976 2.46126 0.98538 -0.83470 -0.36021 0.12814  125 VAL A CB  
991  C CG1 . VAL A 125 ? 1.63666 2.69024 1.06456 -0.96745 -0.32884 0.11510  125 VAL A CG1 
992  C CG2 . VAL A 125 ? 1.45652 2.43193 0.98467 -0.73620 -0.37472 0.09375  125 VAL A CG2 
993  N N   . LYS A 126 ? 2.19718 2.62560 1.30777 -1.08551 -0.39706 0.21638  126 LYS A N   
994  C CA  . LYS A 126 ? 2.20814 2.53304 1.19364 -1.18563 -0.38484 0.25088  126 LYS A CA  
995  C C   . LYS A 126 ? 2.21942 2.76154 1.22893 -1.28328 -0.33432 0.23363  126 LYS A C   
996  O O   . LYS A 126 ? 2.64712 3.19096 1.60727 -1.40073 -0.31576 0.22988  126 LYS A O   
997  C CB  . LYS A 126 ? 2.50626 2.58595 1.36120 -1.26325 -0.41350 0.27883  126 LYS A CB  
998  C CG  . LYS A 126 ? 2.85339 2.78446 1.55359 -1.35939 -0.40447 0.31791  126 LYS A CG  
999  C CD  . LYS A 126 ? 2.86069 2.70346 1.54401 -1.27421 -0.41154 0.33842  126 LYS A CD  
1000 C CE  . LYS A 126 ? 2.85286 2.54559 1.40258 -1.35529 -0.40443 0.36431  126 LYS A CE  
1001 N NZ  . LYS A 126 ? 2.69209 2.31254 1.26386 -1.24177 -0.40324 0.36791  126 LYS A NZ  
1002 N N   . ASN A 127 ? 2.17836 2.90581 1.27107 -1.22135 -0.30482 0.22085  127 ASN A N   
1003 C CA  . ASN A 127 ? 2.30364 3.24786 1.42994 -1.29665 -0.25272 0.20447  127 ASN A CA  
1004 C C   . ASN A 127 ? 2.49545 3.45323 1.59524 -1.25679 -0.23143 0.22790  127 ASN A C   
1005 O O   . ASN A 127 ? 2.41104 3.39656 1.58359 -1.12280 -0.23133 0.22631  127 ASN A O   
1006 C CB  . ASN A 127 ? 2.31362 3.52047 1.59190 -1.24558 -0.22618 0.15598  127 ASN A CB  
1007 C CG  . ASN A 127 ? 2.44572 3.88146 1.77004 -1.29518 -0.16739 0.13693  127 ASN A CG  
1008 O OD1 . ASN A 127 ? 2.42263 3.87335 1.69515 -1.40842 -0.13928 0.13066  127 ASN A OD1 
1009 N ND2 . ASN A 127 ? 2.26546 3.86625 1.68163 -1.19727 -0.14460 0.12562  127 ASN A ND2 
1010 N N   . GLY A 128 ? 2.36866 3.28530 1.38233 -1.35511 -0.19741 0.25104  128 GLY A N   
1011 C CA  . GLY A 128 ? 2.25016 3.16606 1.25201 -1.31184 -0.16682 0.27236  128 GLY A CA  
1012 C C   . GLY A 128 ? 2.17812 3.35887 1.32268 -1.23797 -0.12797 0.24288  128 GLY A C   
1013 O O   . GLY A 128 ? 2.28271 3.66642 1.48561 -1.29999 -0.09261 0.21403  128 GLY A O   
1014 N N   . ALA A 129 ? 1.97382 3.14533 1.18538 -1.09664 -0.13504 0.24328  129 ALA A N   
1015 C CA  . ALA A 129 ? 1.55102 2.94970 0.89809 -1.01034 -0.09872 0.21665  129 ALA A CA  
1016 C C   . ALA A 129 ? 1.47411 2.77788 0.84130 -0.89103 -0.09521 0.23049  129 ALA A C   
1017 O O   . ALA A 129 ? 1.64086 2.71871 0.92883 -0.86331 -0.12508 0.25460  129 ALA A O   
1018 C CB  . ALA A 129 ? 1.43589 2.98671 0.88334 -0.94683 -0.10749 0.18281  129 ALA A CB  
1019 N N   . SER A 130 ? 1.34944 2.82939 0.82764 -0.81818 -0.05988 0.20988  130 SER A N   
1020 C CA  . SER A 130 ? 1.26719 2.68529 0.77699 -0.70645 -0.04942 0.21569  130 SER A CA  
1021 C C   . SER A 130 ? 1.18485 2.49685 0.71267 -0.59136 -0.07290 0.21420  130 SER A C   
1022 O O   . SER A 130 ? 1.13743 2.35406 0.66929 -0.50671 -0.06932 0.21873  130 SER A O   
1023 C CB  . SER A 130 ? 1.15902 2.78576 0.78752 -0.65525 -0.01344 0.18896  130 SER A CB  
1024 O OG  . SER A 130 ? 1.24366 2.94950 0.85215 -0.75129 0.00043  0.18348  130 SER A OG  
1025 N N   . ALA A 131 ? 1.22778 2.55026 0.76856 -0.58437 -0.09776 0.20310  131 ALA A N   
1026 C CA  . ALA A 131 ? 1.10519 2.30826 0.66282 -0.47683 -0.12558 0.19711  131 ALA A CA  
1027 C C   . ALA A 131 ? 1.20983 2.23853 0.68238 -0.53098 -0.17980 0.20808  131 ALA A C   
1028 O O   . ALA A 131 ? 1.29510 2.36788 0.73376 -0.63729 -0.19001 0.20844  131 ALA A O   
1029 C CB  . ALA A 131 ? 0.96756 2.34539 0.64827 -0.38322 -0.10289 0.16565  131 ALA A CB  
1030 N N   . SER A 132 ? 1.20428 2.03356 0.64637 -0.45820 -0.21336 0.21330  132 SER A N   
1031 C CA  . SER A 132 ? 1.30175 1.94514 0.66884 -0.49926 -0.26565 0.22306  132 SER A CA  
1032 C C   . SER A 132 ? 1.32361 1.82232 0.71318 -0.38089 -0.29224 0.21142  132 SER A C   
1033 O O   . SER A 132 ? 1.16139 1.62532 0.57698 -0.28985 -0.27649 0.20549  132 SER A O   
1034 C CB  . SER A 132 ? 1.45570 1.93189 0.70005 -0.59474 -0.28157 0.25381  132 SER A CB  
1035 O OG  . SER A 132 ? 1.54619 1.82612 0.72358 -0.62124 -0.32946 0.26260  132 SER A OG  
1036 N N   . LEU A 133 ? 1.26547 1.68101 0.64586 -0.38593 -0.33016 0.20496  133 LEU A N   
1037 C CA  . LEU A 133 ? 1.28342 1.55276 0.68137 -0.28406 -0.35511 0.19109  133 LEU A CA  
1038 C C   . LEU A 133 ? 1.49253 1.54072 0.81533 -0.28999 -0.37630 0.20664  133 LEU A C   
1039 O O   . LEU A 133 ? 1.48060 1.44828 0.71888 -0.38834 -0.38856 0.23112  133 LEU A O   
1040 C CB  . LEU A 133 ? 1.21989 1.48371 0.63908 -0.29008 -0.38406 0.17703  133 LEU A CB  
1041 C CG  . LEU A 133 ? 1.21623 1.38409 0.67815 -0.17743 -0.39790 0.15427  133 LEU A CG  
1042 C CD1 . LEU A 133 ? 1.13019 1.40919 0.67408 -0.06475 -0.36777 0.12894  133 LEU A CD1 
1043 C CD2 . LEU A 133 ? 1.18433 1.32233 0.64644 -0.21006 -0.42930 0.14648  133 LEU A CD2 
1044 N N   . ASP A 134 ? 1.23079 1.90361 1.13203 -0.17062 -0.33600 0.36707  134 ASP A N   
1045 C CA  . ASP A 134 ? 1.21738 1.82512 1.11125 -0.16652 -0.36942 0.43207  134 ASP A CA  
1046 C C   . ASP A 134 ? 1.29061 1.82040 1.25754 -0.17009 -0.37454 0.45596  134 ASP A C   
1047 O O   . ASP A 134 ? 1.22465 1.75174 1.24220 -0.17774 -0.34780 0.42386  134 ASP A O   
1048 C CB  . ASP A 134 ? 1.16577 1.77737 1.06162 -0.12253 -0.40149 0.42138  134 ASP A CB  
1049 C CG  . ASP A 134 ? 1.34085 1.94823 1.30295 -0.09469 -0.39718 0.36842  134 ASP A CG  
1050 O OD1 . ASP A 134 ? 1.16925 1.78359 1.16077 -0.10358 -0.37048 0.32979  134 ASP A OD1 
1051 O OD2 . ASP A 134 ? 1.11747 1.71651 1.09755 -0.07013 -0.42015 0.36313  134 ASP A OD2 
1052 N N   . GLU A 135 ? 1.57217 2.03407 1.54794 -0.16174 -0.41602 0.50956  135 GLU A N   
1053 C CA  . GLU A 135 ? 1.74780 2.12466 1.79793 -0.15744 -0.43652 0.53114  135 GLU A CA  
1054 C C   . GLU A 135 ? 1.68567 2.05632 1.82931 -0.10274 -0.46268 0.50189  135 GLU A C   
1055 O O   . GLU A 135 ? 1.83432 2.21130 1.96901 -0.07910 -0.49823 0.51819  135 GLU A O   
1056 C CB  . GLU A 135 ? 1.95930 2.24913 1.95124 -0.19273 -0.47711 0.61081  135 GLU A CB  
1057 C CG  . GLU A 135 ? 2.09746 2.40300 1.98301 -0.26481 -0.44430 0.63723  135 GLU A CG  
1058 C CD  . GLU A 135 ? 2.55336 2.74952 2.35817 -0.31683 -0.48846 0.72136  135 GLU A CD  
1059 O OE1 . GLU A 135 ? 2.62168 2.71660 2.46821 -0.28757 -0.55347 0.75790  135 GLU A OE1 
1060 O OE2 . GLU A 135 ? 2.63210 2.84206 2.32981 -0.39052 -0.46168 0.74701  135 GLU A OE2 
1061 N N   . GLN A 136 ? 1.48984 1.85480 1.72349 -0.08768 -0.44285 0.45385  136 GLN A N   
1062 C CA  . GLN A 136 ? 1.52961 1.91152 1.85635 -0.04721 -0.45184 0.40609  136 GLN A CA  
1063 C C   . GLN A 136 ? 1.61327 1.96542 2.03268 -0.04433 -0.43179 0.36568  136 GLN A C   
1064 O O   . GLN A 136 ? 1.60536 1.94424 2.00246 -0.07313 -0.40135 0.36328  136 GLN A O   
1065 C CB  . GLN A 136 ? 1.36355 1.82251 1.65240 -0.04193 -0.42835 0.35862  136 GLN A CB  
1066 C CG  . GLN A 136 ? 1.58625 2.07645 1.93265 -0.01399 -0.44514 0.32518  136 GLN A CG  
1067 C CD  . GLN A 136 ? 1.67674 2.22289 1.95372 -0.02165 -0.43093 0.29105  136 GLN A CD  
1068 O OE1 . GLN A 136 ? 1.80381 2.38169 2.11630 -0.01811 -0.42628 0.24523  136 GLN A OE1 
1069 N NE2 . GLN A 136 ? 1.30559 1.86362 1.48160 -0.03607 -0.42633 0.30862  136 GLN A NE2 
1070 N N   . PRO A 137 ? 1.72900 2.07580 2.25818 -0.01146 -0.44802 0.32828  137 PRO A N   
1071 C CA  . PRO A 137 ? 1.80513 2.13511 2.42463 -0.00878 -0.42332 0.27509  137 PRO A CA  
1072 C C   . PRO A 137 ? 1.91930 2.29279 2.49403 -0.03669 -0.36745 0.22853  137 PRO A C   
1073 O O   . PRO A 137 ? 1.88372 2.31395 2.40461 -0.04256 -0.35221 0.20304  137 PRO A O   
1074 C CB  . PRO A 137 ? 1.76699 2.12934 2.50480 0.02964  -0.44061 0.22052  137 PRO A CB  
1075 C CG  . PRO A 137 ? 1.72423 2.06794 2.45895 0.05462  -0.50125 0.27256  137 PRO A CG  
1076 C CD  . PRO A 137 ? 1.70791 2.05936 2.29563 0.02535  -0.49675 0.33315  137 PRO A CD  
1077 N N   . PRO A 138 ? 2.01175 2.35011 2.60201 -0.05605 -0.34361 0.21710  138 PRO A N   
1078 C CA  . PRO A 138 ? 1.87019 2.23882 2.40950 -0.08350 -0.30186 0.17849  138 PRO A CA  
1079 C C   . PRO A 138 ? 1.83416 2.23447 2.40529 -0.08441 -0.27755 0.10388  138 PRO A C   
1080 O O   . PRO A 138 ? 1.79057 2.17053 2.41984 -0.09198 -0.25621 0.06120  138 PRO A O   
1081 C CB  . PRO A 138 ? 1.73751 2.05406 2.29587 -0.10477 -0.28977 0.19161  138 PRO A CB  
1082 C CG  . PRO A 138 ? 1.89311 2.14642 2.54256 -0.08285 -0.31989 0.20596  138 PRO A CG  
1083 C CD  . PRO A 138 ? 1.99478 2.25330 2.64389 -0.05522 -0.36268 0.24166  138 PRO A CD  
1084 N N   . SER A 139 ? 1.91494 2.36190 2.43781 -0.08449 -0.28030 0.08683  139 SER A N   
1085 C CA  . SER A 139 ? 1.87713 2.35150 2.39737 -0.10400 -0.25667 0.01870  139 SER A CA  
1086 C C   . SER A 139 ? 1.92399 2.42188 2.32788 -0.12091 -0.26619 0.01919  139 SER A C   
1087 O O   . SER A 139 ? 1.91378 2.42373 2.26922 -0.10562 -0.29158 0.06468  139 SER A O   
1088 C CB  . SER A 139 ? 1.83168 2.33859 2.45835 -0.08755 -0.25512 -0.02151 139 SER A CB  
1089 O OG  . SER A 139 ? 2.02106 2.55599 2.65529 -0.06145 -0.28786 0.01202  139 SER A OG  
1090 N N   . LEU A 140 ? 1.82557 2.32054 2.17603 -0.15669 -0.25005 -0.03273 140 LEU A N   
1091 C CA  A LEU A 140 ? 1.80647 2.29941 2.03334 -0.17911 -0.26964 -0.03767 140 LEU A CA  
1092 C CA  B LEU A 140 ? 1.80645 2.29957 2.03344 -0.17860 -0.26995 -0.03692 140 LEU A CA  
1093 C C   . LEU A 140 ? 1.91912 2.45114 2.13541 -0.19080 -0.27305 -0.05401 140 LEU A C   
1094 O O   . LEU A 140 ? 1.99631 2.51602 2.11735 -0.23332 -0.27716 -0.08406 140 LEU A O   
1095 C CB  A LEU A 140 ? 1.73130 2.17872 1.88308 -0.22083 -0.26400 -0.08017 140 LEU A CB  
1096 C CB  B LEU A 140 ? 1.73163 2.17887 1.88267 -0.21951 -0.26502 -0.07831 140 LEU A CB  
1097 C CG  A LEU A 140 ? 1.64359 2.05708 1.77869 -0.21250 -0.27326 -0.06910 140 LEU A CG  
1098 C CG  B LEU A 140 ? 1.67849 2.09291 1.72650 -0.21705 -0.30310 -0.06337 140 LEU A CG  
1099 C CD1 A LEU A 140 ? 1.63193 1.99003 1.67666 -0.25397 -0.28498 -0.11228 140 LEU A CD1 
1100 C CD1 B LEU A 140 ? 1.57070 2.00822 1.66447 -0.17710 -0.30795 -0.01979 140 LEU A CD1 
1101 C CD2 A LEU A 140 ? 1.56631 1.99781 1.66542 -0.18124 -0.30386 -0.02623 140 LEU A CD2 
1102 C CD2 B LEU A 140 ? 1.68264 2.03890 1.67213 -0.25239 -0.30846 -0.10392 140 LEU A CD2 
1103 N N   . ASP A 141 ? 2.21770 2.79178 2.52591 -0.15811 -0.27684 -0.03556 141 ASP A N   
1104 C CA  . ASP A 141 ? 2.20715 2.83303 2.52333 -0.16848 -0.27984 -0.05722 141 ASP A CA  
1105 C C   . ASP A 141 ? 2.12744 2.75314 2.34317 -0.16210 -0.31701 -0.01350 141 ASP A C   
1106 O O   . ASP A 141 ? 2.17693 2.81249 2.31325 -0.19824 -0.32263 -0.03557 141 ASP A O   
1107 C CB  . ASP A 141 ? 2.33552 3.00719 2.80637 -0.13039 -0.27915 -0.06514 141 ASP A CB  
1108 C CG  . ASP A 141 ? 2.40447 3.04358 2.91712 -0.07975 -0.31154 0.00392  141 ASP A CG  
1109 O OD1 . ASP A 141 ? 2.35223 2.94974 2.78213 -0.07970 -0.32106 0.05054  141 ASP A OD1 
1110 O OD2 . ASP A 141 ? 2.43464 3.08867 3.06104 -0.04371 -0.33088 0.00776  141 ASP A OD2 
1111 N N   . LYS A 142 ? 1.55430 2.16630 1.76406 -0.12324 -0.34246 0.04630  142 LYS A N   
1112 C CA  . LYS A 142 ? 1.19429 1.81168 1.31966 -0.11216 -0.37709 0.08564  142 LYS A CA  
1113 C C   . LYS A 142 ? 1.10937 1.69262 1.14811 -0.10782 -0.39062 0.10697  142 LYS A C   
1114 O O   . LYS A 142 ? 0.99735 1.55728 1.05225 -0.11058 -0.37418 0.09808  142 LYS A O   
1115 C CB  . LYS A 142 ? 1.11257 1.75541 1.30380 -0.07418 -0.39876 0.13214  142 LYS A CB  
1116 C CG  . LYS A 142 ? 1.20740 1.89660 1.50364 -0.06850 -0.39679 0.10215  142 LYS A CG  
1117 C CD  . LYS A 142 ? 1.17820 1.87639 1.53055 -0.02781 -0.43537 0.15148  142 LYS A CD  
1118 C CE  . LYS A 142 ? 1.11860 1.87441 1.59273 -0.01539 -0.44224 0.10972  142 LYS A CE  
1119 N NZ  . LYS A 142 ? 1.12421 1.87765 1.64730 0.02609  -0.49500 0.15835  142 LYS A NZ  
1120 N N   . THR A 143 ? 1.22524 1.81243 1.17870 -0.10019 -0.42218 0.12833  143 THR A N   
1121 C CA  . THR A 143 ? 1.12833 1.70154 1.01241 -0.09013 -0.43925 0.13564  143 THR A CA  
1122 C C   . THR A 143 ? 0.91803 1.51425 0.84584 -0.06794 -0.42958 0.17918  143 THR A C   
1123 O O   . THR A 143 ? 1.02950 1.64292 0.97853 -0.05493 -0.43791 0.22059  143 THR A O   
1124 C CB  . THR A 143 ? 1.00510 1.51809 0.79911 -0.07313 -0.44683 0.11706  143 THR A CB  
1125 O OG1 . THR A 143 ? 1.22793 1.68694 0.96975 -0.09657 -0.44735 0.07603  143 THR A OG1 
1126 C CG2 . THR A 143 ? 0.96719 1.44345 0.72215 -0.04571 -0.44801 0.10062  143 THR A CG2 
1127 N N   . ARG A 144 ? 0.66579 1.39976 0.60927 -0.42672 -0.09539 0.15361  144 ARG A N   
1128 C CA  . ARG A 144 ? 0.99690 1.75729 0.90544 -0.44303 -0.09064 0.16097  144 ARG A CA  
1129 C C   . ARG A 144 ? 0.79659 1.57848 0.67155 -0.47144 -0.08706 0.14906  144 ARG A C   
1130 O O   . ARG A 144 ? 0.80287 1.59331 0.68638 -0.46712 -0.06862 0.14029  144 ARG A O   
1131 C CB  . ARG A 144 ? 0.86815 1.63101 0.78758 -0.42078 -0.07241 0.16298  144 ARG A CB  
1132 C CG  . ARG A 144 ? 0.89896 1.63674 0.84649 -0.39710 -0.07476 0.16955  144 ARG A CG  
1133 C CD  . ARG A 144 ? 0.87755 1.62275 0.81088 -0.41043 -0.08757 0.18777  144 ARG A CD  
1134 N NE  . ARG A 144 ? 1.02651 1.79497 0.93463 -0.42411 -0.08040 0.19273  144 ARG A NE  
1135 C CZ  . ARG A 144 ? 1.10343 1.86156 1.02568 -0.41139 -0.06718 0.19026  144 ARG A CZ  
1136 N NH1 . ARG A 144 ? 1.08412 1.81441 1.03830 -0.38777 -0.06109 0.18394  144 ARG A NH1 
1137 N NH2 . ARG A 144 ? 0.88356 1.65164 0.78964 -0.42240 -0.05502 0.19143  144 ARG A NH2 
1138 N N   . LYS A 145 ? 0.97097 1.75823 0.80488 -0.49582 -0.10518 0.14692  145 LYS A N   
1139 C CA  . LYS A 145 ? 0.74878 1.52387 0.52272 -0.51012 -0.10448 0.12797  145 LYS A CA  
1140 C C   . LYS A 145 ? 0.77473 1.54688 0.51886 -0.49544 -0.06969 0.13434  145 LYS A C   
1141 O O   . LYS A 145 ? 0.82072 1.61664 0.57777 -0.49253 -0.06057 0.15167  145 LYS A O   
1142 C CB  . LYS A 145 ? 1.08382 1.83711 0.79980 -0.52052 -0.13416 0.11878  145 LYS A CB  
1143 C CG  . LYS A 145 ? 1.05427 1.78624 0.78932 -0.52800 -0.15336 0.10415  145 LYS A CG  
1144 C CD  . LYS A 145 ? 0.93142 1.65414 0.62901 -0.53014 -0.17614 0.10055  145 LYS A CD  
1145 C CE  . LYS A 145 ? 1.05381 1.75032 0.72745 -0.54972 -0.18935 0.07043  145 LYS A CE  
1146 N NZ  . LYS A 145 ? 1.03055 1.72019 0.76208 -0.54985 -0.19056 0.06744  145 LYS A NZ  
1147 N N   . ILE A 146 ? 0.92708 1.66766 0.62983 -0.48684 -0.04689 0.11967  146 ILE A N   
1148 C CA  . ILE A 146 ? 0.84777 1.58382 0.51243 -0.47302 -0.01432 0.12291  146 ILE A CA  
1149 C C   . ILE A 146 ? 0.91312 1.59645 0.49519 -0.47191 -0.01541 0.10535  146 ILE A C   
1150 O O   . ILE A 146 ? 0.95143 1.59957 0.51470 -0.47321 -0.01273 0.08664  146 ILE A O   
1151 C CB  . ILE A 146 ? 1.00030 1.75821 0.70605 -0.45510 0.02022  0.12377  146 ILE A CB  
1152 C CG1 . ILE A 146 ? 0.90794 1.70464 0.70304 -0.44713 0.01076  0.13035  146 ILE A CG1 
1153 C CG2 . ILE A 146 ? 0.80142 1.54379 0.49103 -0.42974 0.04392  0.11976  146 ILE A CG2 
1154 C CD1 . ILE A 146 ? 0.71476 1.52098 0.55290 -0.41358 0.03148  0.12542  146 ILE A CD1 
1155 N N   . TYR A 147 ? 1.11785 1.79326 0.64931 -0.46995 -0.01629 0.11094  147 TYR A N   
1156 C CA  . TYR A 147 ? 1.08685 1.71881 0.53925 -0.47044 -0.02179 0.09478  147 TYR A CA  
1157 C C   . TYR A 147 ? 1.09642 1.70086 0.51946 -0.44925 0.01502  0.08846  147 TYR A C   
1158 O O   . TYR A 147 ? 1.03161 1.65045 0.49020 -0.43057 0.03638  0.09974  147 TYR A O   
1159 C CB  . TYR A 147 ? 1.06186 1.69486 0.49723 -0.46836 -0.04420 0.10473  147 TYR A CB  
1160 C CG  . TYR A 147 ? 1.03208 1.69540 0.50445 -0.48126 -0.07918 0.11474  147 TYR A CG  
1161 C CD1 . TYR A 147 ? 1.10801 1.76692 0.56576 -0.49843 -0.10963 0.09746  147 TYR A CD1 
1162 C CD2 . TYR A 147 ? 1.19541 1.88979 0.72100 -0.47572 -0.07896 0.13956  147 TYR A CD2 
1163 C CE1 . TYR A 147 ? 1.04438 1.73223 0.54745 -0.50463 -0.13897 0.10702  147 TYR A CE1 
1164 C CE2 . TYR A 147 ? 1.01237 1.73306 0.57419 -0.48274 -0.10814 0.15092  147 TYR A CE2 
1165 C CZ  . TYR A 147 ? 1.19588 1.91424 0.75039 -0.49448 -0.13805 0.13543  147 TYR A CZ  
1166 O OH  . TYR A 147 ? 1.09225 1.83552 0.69140 -0.49557 -0.16217 0.14702  147 TYR A OH  
1167 N N   . ASN A 148 ? 1.13905 1.70155 0.49715 -0.45254 0.02223  0.06773  148 ASN A N   
1168 C CA  . ASN A 148 ? 1.17751 1.70915 0.50202 -0.42998 0.05741  0.06151  148 ASN A CA  
1169 C C   . ASN A 148 ? 1.38124 1.86906 0.62516 -0.43283 0.04999  0.04510  148 ASN A C   
1170 O O   . ASN A 148 ? 1.31818 1.78543 0.51881 -0.45629 0.02824  0.02542  148 ASN A O   
1171 C CB  . ASN A 148 ? 1.18398 1.70085 0.50851 -0.42462 0.08637  0.05324  148 ASN A CB  
1172 C CG  . ASN A 148 ? 1.27211 1.83946 0.68347 -0.41168 0.09967  0.07165  148 ASN A CG  
1173 O OD1 . ASN A 148 ? 1.09422 1.67823 0.54114 -0.38235 0.12390  0.08111  148 ASN A OD1 
1174 N N   . LYS A 149 ? 1.28575 1.76131 0.51226 -0.40969 0.06776  0.05098  149 LYS A N   
1175 C CA  . LYS A 149 ? 1.36728 1.80605 0.52137 -0.40785 0.06320  0.03821  149 LYS A CA  
1176 C C   . LYS A 149 ? 1.43317 1.82375 0.53111 -0.40186 0.09151  0.01742  149 LYS A C   
1177 O O   . LYS A 149 ? 1.41830 1.80511 0.53155 -0.37698 0.12510  0.02480  149 LYS A O   
1178 C CB  . LYS A 149 ? 1.36097 1.80647 0.51999 -0.38578 0.07067  0.05561  149 LYS A CB  
1179 C CG  . LYS A 149 ? 1.43990 1.91991 0.63874 -0.39055 0.04894  0.07583  149 LYS A CG  
1180 C CD  . LYS A 149 ? 1.32369 1.79939 0.51845 -0.36996 0.06404  0.09120  149 LYS A CD  
1181 C CE  . LYS A 149 ? 1.38479 1.88641 0.61290 -0.37297 0.05026  0.11279  149 LYS A CE  
1182 N NZ  . LYS A 149 ? 1.30880 1.79788 0.52631 -0.35451 0.07009  0.12715  149 LYS A NZ  
1183 N N   . LYS A 150 ? 1.53363 1.88803 0.56810 -0.42376 0.07960  -0.00930 150 LYS A N   
1184 C CA  . LYS A 150 ? 1.59376 1.88999 0.56456 -0.42172 0.11054  -0.03315 150 LYS A CA  
1185 C C   . LYS A 150 ? 1.63660 1.91000 0.56445 -0.39715 0.12536  -0.03222 150 LYS A C   
1186 O O   . LYS A 150 ? 1.64181 1.93228 0.56268 -0.39443 0.10306  -0.02496 150 LYS A O   
1187 C CB  . LYS A 150 ? 1.66049 1.92109 0.57801 -0.45995 0.09475  -0.06890 150 LYS A CB  
1188 C CG  . LYS A 150 ? 1.86826 2.05337 0.73266 -0.45973 0.13458  -0.09677 150 LYS A CG  
1189 C CD  . LYS A 150 ? 1.81595 1.96106 0.64612 -0.49877 0.11846  -0.13678 150 LYS A CD  
1190 C CE  . LYS A 150 ? 2.07249 2.12816 0.85365 -0.49764 0.16540  -0.16568 150 LYS A CE  
1191 N NZ  . LYS A 150 ? 2.27438 2.28872 1.01862 -0.54317 0.15402  -0.21035 150 LYS A NZ  
1192 N N   . ALA A 151 ? 1.67401 1.90914 0.57363 -0.37586 0.16586  -0.03713 151 ALA A N   
1193 C CA  . ALA A 151 ? 1.85963 2.07110 0.71790 -0.34982 0.18374  -0.03623 151 ALA A CA  
1194 C C   . ALA A 151 ? 1.82731 1.98611 0.60155 -0.37064 0.17948  -0.07014 151 ALA A C   
1195 O O   . ALA A 151 ? 1.89031 1.99572 0.62127 -0.38305 0.20326  -0.09546 151 ALA A O   
1196 C CB  . ALA A 151 ? 1.71497 1.91575 0.58560 -0.31301 0.22898  -0.02353 151 ALA A CB  
1197 N N   . VAL A 152 ? 1.87890 2.05073 0.63028 -0.37413 0.15268  -0.07133 152 VAL A N   
1198 C CA  . VAL A 152 ? 1.94822 2.08333 0.62641 -0.39401 0.14477  -0.10376 152 VAL A CA  
1199 C C   . VAL A 152 ? 2.01476 2.09985 0.64000 -0.36941 0.18315  -0.11208 152 VAL A C   
1200 O O   . VAL A 152 ? 1.98703 2.08641 0.62822 -0.33396 0.19749  -0.08723 152 VAL A O   
1201 C CB  . VAL A 152 ? 1.94838 2.12564 0.62553 -0.39943 0.10466  -0.09673 152 VAL A CB  
1202 C CG1 . VAL A 152 ? 2.04339 2.19876 0.65566 -0.42627 0.09105  -0.13310 152 VAL A CG1 
1203 C CG2 . VAL A 152 ? 1.86989 2.10252 0.61122 -0.41147 0.07200  -0.07745 152 VAL A CG2 
1204 N N   . LYS A 153 ? 2.22134 2.24562 0.78412 -0.38877 0.20187  -0.14822 153 LYS A N   
1205 C CA  . LYS A 153 ? 2.49369 2.46310 1.00070 -0.36697 0.24082  -0.15928 153 LYS A CA  
1206 C C   . LYS A 153 ? 2.42140 2.38564 0.87302 -0.37701 0.22227  -0.17908 153 LYS A C   
1207 O O   . LYS A 153 ? 2.40416 2.38249 0.84072 -0.41253 0.18968  -0.20133 153 LYS A O   
1208 C CB  . LYS A 153 ? 2.73078 2.62332 1.19943 -0.37915 0.28291  -0.18735 153 LYS A CB  
1209 C CG  . LYS A 153 ? 2.84873 2.74357 1.36746 -0.35713 0.31283  -0.16333 153 LYS A CG  
1210 C CD  . LYS A 153 ? 2.91303 2.83764 1.46426 -0.30272 0.33711  -0.12573 153 LYS A CD  
1211 C CE  . LYS A 153 ? 3.04434 2.98310 1.65020 -0.27670 0.36818  -0.10064 153 LYS A CE  
1212 N NZ  . LYS A 153 ? 3.21830 3.07403 1.78136 -0.27709 0.41667  -0.12097 153 LYS A NZ  
1213 N N   . LEU A 154 ? 2.28241 2.23408 0.70762 -0.34401 0.24297  -0.16971 154 LEU A N   
1214 C CA  . LEU A 154 ? 2.35070 2.29977 0.72291 -0.34673 0.23002  -0.18495 154 LEU A CA  
1215 C C   . LEU A 154 ? 2.31369 2.32766 0.70852 -0.35684 0.18138  -0.17230 154 LEU A C   
1216 O O   . LEU A 154 ? 2.30882 2.34892 0.69903 -0.33266 0.17272  -0.15297 154 LEU A O   
1217 C CB  . LEU A 154 ? 2.46302 2.34958 0.76652 -0.38085 0.24396  -0.23381 154 LEU A CB  
1218 C CG  . LEU A 154 ? 2.55804 2.44482 0.80471 -0.38746 0.23167  -0.25438 154 LEU A CG  
1219 C CD1 . LEU A 154 ? 2.54903 2.43015 0.77966 -0.34203 0.25464  -0.23296 154 LEU A CD1 
1220 C CD2 . LEU A 154 ? 2.65413 2.47804 0.83908 -0.42775 0.24831  -0.30689 154 LEU A CD2 
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