data_9LSD
# 
_entry.id   9LSD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9LSD         pdb_00009lsd 10.2210/pdb9lsd/pdb 
WWPDB D_1300056355 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LSD 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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                 3 
_pdbx_contact_author.email              sklunsy@gmail.com 
_pdbx_contact_author.name_first         Shukun 
_pdbx_contact_author.name_last          Luo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2766-3125 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Luo, S.' 1 0000-0002-2766-3125 
'Zhu, C.' 2 0000-0003-4738-2125 
# 
_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                5596 
_citation.page_last                 5601 
_citation.title                     
'A Stereoselective Decarboxylative Aromatase/Cyclase Directs the Biosynthesis of an Axially Chiral Biphenyl Framework in Fasamycin.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c18376 
_citation.pdbx_database_id_PubMed   39910892 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiang, K.' 1 ?                   
primary 'Zhu, C.'   2 ?                   
primary 'Yan, X.'   3 ?                   
primary 'Li, G.'    4 ?                   
primary 'Lin, Z.'   5 0009-0005-2240-449X 
primary 'Deng, Z.'  6 ?                   
primary 'Luo, S.'   7 ?                   
primary 'Qu, X.'    8 0000-0002-3301-8536 
# 
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 'Antibiotic biosynthesis monooxygenase' 13823.254 2   ? ? ? ? 
2 non-polymer syn '2-(2-ETHOXYETHOXY)ETHANOL'             134.174   2   ? ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                         24.305    1   ? ? ? ? 
4 water       nat water                                   18.015    151 ? ? ? ? 
# 
_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       
;GPSGMAEISADNEFATFINLFPTKPRDQQKLVDLIVKAHEELIRHRPGYVSGNVHRSVDGYQVVDYTQWRRREDFEAMVR
DPASAPHFMPIGELTQGKQGAYDVVYTHVTEEAEGAKEGTGDE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPSGMAEISADNEFATFINLFPTKPRDQQKLVDLIVKAHEELIRHRPGYVSGNVHRSVDGYQVVDYTQWRRREDFEAMVR
DPASAPHFMPIGELTQGKQGAYDVVYTHVTEEAEGAKEGTGDE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-(2-ETHOXYETHOXY)ETHANOL' AE3 
3 'MAGNESIUM ION'             MG  
4 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   SER n 
1 4   GLY n 
1 5   MET n 
1 6   ALA n 
1 7   GLU n 
1 8   ILE n 
1 9   SER n 
1 10  ALA n 
1 11  ASP n 
1 12  ASN n 
1 13  GLU n 
1 14  PHE n 
1 15  ALA n 
1 16  THR n 
1 17  PHE n 
1 18  ILE n 
1 19  ASN n 
1 20  LEU n 
1 21  PHE n 
1 22  PRO n 
1 23  THR n 
1 24  LYS n 
1 25  PRO n 
1 26  ARG n 
1 27  ASP n 
1 28  GLN n 
1 29  GLN n 
1 30  LYS n 
1 31  LEU n 
1 32  VAL n 
1 33  ASP n 
1 34  LEU n 
1 35  ILE n 
1 36  VAL n 
1 37  LYS n 
1 38  ALA n 
1 39  HIS n 
1 40  GLU n 
1 41  GLU n 
1 42  LEU n 
1 43  ILE n 
1 44  ARG n 
1 45  HIS n 
1 46  ARG n 
1 47  PRO n 
1 48  GLY n 
1 49  TYR n 
1 50  VAL n 
1 51  SER n 
1 52  GLY n 
1 53  ASN n 
1 54  VAL n 
1 55  HIS n 
1 56  ARG n 
1 57  SER n 
1 58  VAL n 
1 59  ASP n 
1 60  GLY n 
1 61  TYR n 
1 62  GLN n 
1 63  VAL n 
1 64  VAL n 
1 65  ASP n 
1 66  TYR n 
1 67  THR n 
1 68  GLN n 
1 69  TRP n 
1 70  ARG n 
1 71  ARG n 
1 72  ARG n 
1 73  GLU n 
1 74  ASP n 
1 75  PHE n 
1 76  GLU n 
1 77  ALA n 
1 78  MET n 
1 79  VAL n 
1 80  ARG n 
1 81  ASP n 
1 82  PRO n 
1 83  ALA n 
1 84  SER n 
1 85  ALA n 
1 86  PRO n 
1 87  HIS n 
1 88  PHE n 
1 89  MET n 
1 90  PRO n 
1 91  ILE n 
1 92  GLY n 
1 93  GLU n 
1 94  LEU n 
1 95  THR n 
1 96  GLN n 
1 97  GLY n 
1 98  LYS n 
1 99  GLN n 
1 100 GLY n 
1 101 ALA n 
1 102 TYR n 
1 103 ASP n 
1 104 VAL n 
1 105 VAL n 
1 106 TYR n 
1 107 THR n 
1 108 HIS n 
1 109 VAL n 
1 110 THR n 
1 111 GLU n 
1 112 GLU n 
1 113 ALA n 
1 114 GLU n 
1 115 GLY n 
1 116 ALA n 
1 117 LYS n 
1 118 GLU n 
1 119 GLY n 
1 120 THR n 
1 121 GLY n 
1 122 ASP n 
1 123 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   123 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CP970_07265 
_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      'Streptomyces kanamyceticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1967 
_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 
AE3 non-polymer         . '2-(2-ETHOXYETHOXY)ETHANOL' ? 'C6 H14 O3'      134.174 
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  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                       ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'           24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -3  ?   ?   ?   A . n 
A 1 2   PRO 2   -2  ?   ?   ?   A . n 
A 1 3   SER 3   -1  ?   ?   ?   A . n 
A 1 4   GLY 4   0   ?   ?   ?   A . n 
A 1 5   MET 5   1   1   MET MET A . n 
A 1 6   ALA 6   2   2   ALA ALA A . n 
A 1 7   GLU 7   3   3   GLU GLU A . n 
A 1 8   ILE 8   4   4   ILE ILE A . n 
A 1 9   SER 9   5   5   SER SER A . n 
A 1 10  ALA 10  6   6   ALA ALA A . n 
A 1 11  ASP 11  7   7   ASP ASP A . n 
A 1 12  ASN 12  8   8   ASN ASN A . n 
A 1 13  GLU 13  9   9   GLU GLU A . n 
A 1 14  PHE 14  10  10  PHE PHE A . n 
A 1 15  ALA 15  11  11  ALA ALA A . n 
A 1 16  THR 16  12  12  THR THR A . n 
A 1 17  PHE 17  13  13  PHE PHE A . n 
A 1 18  ILE 18  14  14  ILE ILE A . n 
A 1 19  ASN 19  15  15  ASN ASN A . n 
A 1 20  LEU 20  16  16  LEU LEU A . n 
A 1 21  PHE 21  17  17  PHE PHE A . n 
A 1 22  PRO 22  18  18  PRO PRO A . n 
A 1 23  THR 23  19  19  THR THR A . n 
A 1 24  LYS 24  20  20  LYS LYS A . n 
A 1 25  PRO 25  21  21  PRO PRO A . n 
A 1 26  ARG 26  22  22  ARG ARG A . n 
A 1 27  ASP 27  23  23  ASP ASP A . n 
A 1 28  GLN 28  24  24  GLN GLN A . n 
A 1 29  GLN 29  25  25  GLN GLN A . n 
A 1 30  LYS 30  26  26  LYS LYS A . n 
A 1 31  LEU 31  27  27  LEU LEU A . n 
A 1 32  VAL 32  28  28  VAL VAL A . n 
A 1 33  ASP 33  29  29  ASP ASP A . n 
A 1 34  LEU 34  30  30  LEU LEU A . n 
A 1 35  ILE 35  31  31  ILE ILE A . n 
A 1 36  VAL 36  32  32  VAL VAL A . n 
A 1 37  LYS 37  33  33  LYS LYS A . n 
A 1 38  ALA 38  34  34  ALA ALA A . n 
A 1 39  HIS 39  35  35  HIS HIS A . n 
A 1 40  GLU 40  36  36  GLU GLU A . n 
A 1 41  GLU 41  37  37  GLU GLU A . n 
A 1 42  LEU 42  38  38  LEU LEU A . n 
A 1 43  ILE 43  39  39  ILE ILE A . n 
A 1 44  ARG 44  40  40  ARG ARG A . n 
A 1 45  HIS 45  41  41  HIS HIS A . n 
A 1 46  ARG 46  42  42  ARG ARG A . n 
A 1 47  PRO 47  43  43  PRO PRO A . n 
A 1 48  GLY 48  44  44  GLY GLY A . n 
A 1 49  TYR 49  45  45  TYR TYR A . n 
A 1 50  VAL 50  46  46  VAL VAL A . n 
A 1 51  SER 51  47  47  SER SER A . n 
A 1 52  GLY 52  48  48  GLY GLY A . n 
A 1 53  ASN 53  49  49  ASN ASN A . n 
A 1 54  VAL 54  50  50  VAL VAL A . n 
A 1 55  HIS 55  51  51  HIS HIS A . n 
A 1 56  ARG 56  52  52  ARG ARG A . n 
A 1 57  SER 57  53  53  SER SER A . n 
A 1 58  VAL 58  54  54  VAL VAL A . n 
A 1 59  ASP 59  55  55  ASP ASP A . n 
A 1 60  GLY 60  56  56  GLY GLY A . n 
A 1 61  TYR 61  57  57  TYR TYR A . n 
A 1 62  GLN 62  58  58  GLN GLN A . n 
A 1 63  VAL 63  59  59  VAL VAL A . n 
A 1 64  VAL 64  60  60  VAL VAL A . n 
A 1 65  ASP 65  61  61  ASP ASP A . n 
A 1 66  TYR 66  62  62  TYR TYR A . n 
A 1 67  THR 67  63  63  THR THR A . n 
A 1 68  GLN 68  64  64  GLN GLN A . n 
A 1 69  TRP 69  65  65  TRP TRP A . n 
A 1 70  ARG 70  66  66  ARG ARG A . n 
A 1 71  ARG 71  67  67  ARG ARG A . n 
A 1 72  ARG 72  68  68  ARG ARG A . n 
A 1 73  GLU 73  69  69  GLU GLU A . n 
A 1 74  ASP 74  70  70  ASP ASP A . n 
A 1 75  PHE 75  71  71  PHE PHE A . n 
A 1 76  GLU 76  72  72  GLU GLU A . n 
A 1 77  ALA 77  73  73  ALA ALA A . n 
A 1 78  MET 78  74  74  MET MET A . n 
A 1 79  VAL 79  75  75  VAL VAL A . n 
A 1 80  ARG 80  76  76  ARG ARG A . n 
A 1 81  ASP 81  77  77  ASP ASP A . n 
A 1 82  PRO 82  78  78  PRO PRO A . n 
A 1 83  ALA 83  79  79  ALA ALA A . n 
A 1 84  SER 84  80  80  SER SER A . n 
A 1 85  ALA 85  81  81  ALA ALA A . n 
A 1 86  PRO 86  82  82  PRO PRO A . n 
A 1 87  HIS 87  83  83  HIS HIS A . n 
A 1 88  PHE 88  84  84  PHE PHE A . n 
A 1 89  MET 89  85  85  MET MET A . n 
A 1 90  PRO 90  86  86  PRO PRO A . n 
A 1 91  ILE 91  87  87  ILE ILE A . n 
A 1 92  GLY 92  88  88  GLY GLY A . n 
A 1 93  GLU 93  89  89  GLU GLU A . n 
A 1 94  LEU 94  90  90  LEU LEU A . n 
A 1 95  THR 95  91  91  THR THR A . n 
A 1 96  GLN 96  92  92  GLN GLN A . n 
A 1 97  GLY 97  93  93  GLY GLY A . n 
A 1 98  LYS 98  94  94  LYS LYS A . n 
A 1 99  GLN 99  95  95  GLN GLN A . n 
A 1 100 GLY 100 96  96  GLY GLY A . n 
A 1 101 ALA 101 97  97  ALA ALA A . n 
A 1 102 TYR 102 98  98  TYR TYR A . n 
A 1 103 ASP 103 99  99  ASP ASP A . n 
A 1 104 VAL 104 100 100 VAL VAL A . n 
A 1 105 VAL 105 101 101 VAL VAL A . n 
A 1 106 TYR 106 102 102 TYR TYR A . n 
A 1 107 THR 107 103 103 THR THR A . n 
A 1 108 HIS 108 104 104 HIS HIS A . n 
A 1 109 VAL 109 105 105 VAL VAL A . n 
A 1 110 THR 110 106 106 THR THR A . n 
A 1 111 GLU 111 107 107 GLU GLU A . n 
A 1 112 GLU 112 108 ?   ?   ?   A . n 
A 1 113 ALA 113 109 ?   ?   ?   A . n 
A 1 114 GLU 114 110 ?   ?   ?   A . n 
A 1 115 GLY 115 111 ?   ?   ?   A . n 
A 1 116 ALA 116 112 ?   ?   ?   A . n 
A 1 117 LYS 117 113 ?   ?   ?   A . n 
A 1 118 GLU 118 114 ?   ?   ?   A . n 
A 1 119 GLY 119 115 ?   ?   ?   A . n 
A 1 120 THR 120 116 ?   ?   ?   A . n 
A 1 121 GLY 121 117 ?   ?   ?   A . n 
A 1 122 ASP 122 118 ?   ?   ?   A . n 
A 1 123 GLU 123 119 ?   ?   ?   A . n 
B 1 1   GLY 1   -3  ?   ?   ?   B . n 
B 1 2   PRO 2   -2  ?   ?   ?   B . n 
B 1 3   SER 3   -1  ?   ?   ?   B . n 
B 1 4   GLY 4   0   0   GLY GLY B . n 
B 1 5   MET 5   1   1   MET MET B . n 
B 1 6   ALA 6   2   2   ALA ALA B . n 
B 1 7   GLU 7   3   3   GLU GLU B . n 
B 1 8   ILE 8   4   4   ILE ILE B . n 
B 1 9   SER 9   5   5   SER SER B . n 
B 1 10  ALA 10  6   6   ALA ALA B . n 
B 1 11  ASP 11  7   7   ASP ASP B . n 
B 1 12  ASN 12  8   8   ASN ASN B . n 
B 1 13  GLU 13  9   9   GLU GLU B . n 
B 1 14  PHE 14  10  10  PHE PHE B . n 
B 1 15  ALA 15  11  11  ALA ALA B . n 
B 1 16  THR 16  12  12  THR THR B . n 
B 1 17  PHE 17  13  13  PHE PHE B . n 
B 1 18  ILE 18  14  14  ILE ILE B . n 
B 1 19  ASN 19  15  15  ASN ASN B . n 
B 1 20  LEU 20  16  16  LEU LEU B . n 
B 1 21  PHE 21  17  17  PHE PHE B . n 
B 1 22  PRO 22  18  18  PRO PRO B . n 
B 1 23  THR 23  19  19  THR THR B . n 
B 1 24  LYS 24  20  20  LYS LYS B . n 
B 1 25  PRO 25  21  21  PRO PRO B . n 
B 1 26  ARG 26  22  22  ARG ARG B . n 
B 1 27  ASP 27  23  23  ASP ASP B . n 
B 1 28  GLN 28  24  24  GLN GLN B . n 
B 1 29  GLN 29  25  25  GLN GLN B . n 
B 1 30  LYS 30  26  26  LYS LYS B . n 
B 1 31  LEU 31  27  27  LEU LEU B . n 
B 1 32  VAL 32  28  28  VAL VAL B . n 
B 1 33  ASP 33  29  29  ASP ASP B . n 
B 1 34  LEU 34  30  30  LEU LEU B . n 
B 1 35  ILE 35  31  31  ILE ILE B . n 
B 1 36  VAL 36  32  32  VAL VAL B . n 
B 1 37  LYS 37  33  33  LYS LYS B . n 
B 1 38  ALA 38  34  34  ALA ALA B . n 
B 1 39  HIS 39  35  35  HIS HIS B . n 
B 1 40  GLU 40  36  36  GLU GLU B . n 
B 1 41  GLU 41  37  37  GLU GLU B . n 
B 1 42  LEU 42  38  38  LEU LEU B . n 
B 1 43  ILE 43  39  39  ILE ILE B . n 
B 1 44  ARG 44  40  40  ARG ARG B . n 
B 1 45  HIS 45  41  41  HIS HIS B . n 
B 1 46  ARG 46  42  42  ARG ARG B . n 
B 1 47  PRO 47  43  43  PRO PRO B . n 
B 1 48  GLY 48  44  44  GLY GLY B . n 
B 1 49  TYR 49  45  45  TYR TYR B . n 
B 1 50  VAL 50  46  46  VAL VAL B . n 
B 1 51  SER 51  47  47  SER SER B . n 
B 1 52  GLY 52  48  48  GLY GLY B . n 
B 1 53  ASN 53  49  49  ASN ASN B . n 
B 1 54  VAL 54  50  50  VAL VAL B . n 
B 1 55  HIS 55  51  51  HIS HIS B . n 
B 1 56  ARG 56  52  52  ARG ARG B . n 
B 1 57  SER 57  53  53  SER SER B . n 
B 1 58  VAL 58  54  54  VAL VAL B . n 
B 1 59  ASP 59  55  55  ASP ASP B . n 
B 1 60  GLY 60  56  56  GLY GLY B . n 
B 1 61  TYR 61  57  57  TYR TYR B . n 
B 1 62  GLN 62  58  58  GLN GLN B . n 
B 1 63  VAL 63  59  59  VAL VAL B . n 
B 1 64  VAL 64  60  60  VAL VAL B . n 
B 1 65  ASP 65  61  61  ASP ASP B . n 
B 1 66  TYR 66  62  62  TYR TYR B . n 
B 1 67  THR 67  63  63  THR THR B . n 
B 1 68  GLN 68  64  64  GLN GLN B . n 
B 1 69  TRP 69  65  65  TRP TRP B . n 
B 1 70  ARG 70  66  66  ARG ARG B . n 
B 1 71  ARG 71  67  67  ARG ARG B . n 
B 1 72  ARG 72  68  68  ARG ARG B . n 
B 1 73  GLU 73  69  69  GLU GLU B . n 
B 1 74  ASP 74  70  70  ASP ASP B . n 
B 1 75  PHE 75  71  71  PHE PHE B . n 
B 1 76  GLU 76  72  72  GLU GLU B . n 
B 1 77  ALA 77  73  73  ALA ALA B . n 
B 1 78  MET 78  74  74  MET MET B . n 
B 1 79  VAL 79  75  75  VAL VAL B . n 
B 1 80  ARG 80  76  76  ARG ARG B . n 
B 1 81  ASP 81  77  77  ASP ASP B . n 
B 1 82  PRO 82  78  78  PRO PRO B . n 
B 1 83  ALA 83  79  79  ALA ALA B . n 
B 1 84  SER 84  80  80  SER SER B . n 
B 1 85  ALA 85  81  81  ALA ALA B . n 
B 1 86  PRO 86  82  82  PRO PRO B . n 
B 1 87  HIS 87  83  83  HIS HIS B . n 
B 1 88  PHE 88  84  84  PHE PHE B . n 
B 1 89  MET 89  85  85  MET MET B . n 
B 1 90  PRO 90  86  86  PRO PRO B . n 
B 1 91  ILE 91  87  87  ILE ILE B . n 
B 1 92  GLY 92  88  88  GLY GLY B . n 
B 1 93  GLU 93  89  89  GLU GLU B . n 
B 1 94  LEU 94  90  90  LEU LEU B . n 
B 1 95  THR 95  91  91  THR THR B . n 
B 1 96  GLN 96  92  92  GLN GLN B . n 
B 1 97  GLY 97  93  93  GLY GLY B . n 
B 1 98  LYS 98  94  94  LYS LYS B . n 
B 1 99  GLN 99  95  95  GLN GLN B . n 
B 1 100 GLY 100 96  96  GLY GLY B . n 
B 1 101 ALA 101 97  97  ALA ALA B . n 
B 1 102 TYR 102 98  98  TYR TYR B . n 
B 1 103 ASP 103 99  99  ASP ASP B . n 
B 1 104 VAL 104 100 100 VAL VAL B . n 
B 1 105 VAL 105 101 101 VAL VAL B . n 
B 1 106 TYR 106 102 102 TYR TYR B . n 
B 1 107 THR 107 103 103 THR THR B . n 
B 1 108 HIS 108 104 104 HIS HIS B . n 
B 1 109 VAL 109 105 105 VAL VAL B . n 
B 1 110 THR 110 106 106 THR THR B . n 
B 1 111 GLU 111 107 ?   ?   ?   B . n 
B 1 112 GLU 112 108 ?   ?   ?   B . n 
B 1 113 ALA 113 109 ?   ?   ?   B . n 
B 1 114 GLU 114 110 ?   ?   ?   B . n 
B 1 115 GLY 115 111 ?   ?   ?   B . n 
B 1 116 ALA 116 112 ?   ?   ?   B . n 
B 1 117 LYS 117 113 ?   ?   ?   B . n 
B 1 118 GLU 118 114 ?   ?   ?   B . n 
B 1 119 GLY 119 115 ?   ?   ?   B . n 
B 1 120 THR 120 116 ?   ?   ?   B . n 
B 1 121 GLY 121 117 ?   ?   ?   B . n 
B 1 122 ASP 122 118 ?   ?   ?   B . n 
B 1 123 GLU 123 119 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 AE3 1  201 201 AE3 PG9 A . 
D 3 MG  1  202 1   MG  MG  A . 
E 2 AE3 1  201 201 AE3 PG9 B . 
F 4 HOH 1  301 144 HOH HOH A . 
F 4 HOH 2  302 149 HOH HOH A . 
F 4 HOH 3  303 69  HOH HOH A . 
F 4 HOH 4  304 7   HOH HOH A . 
F 4 HOH 5  305 39  HOH HOH A . 
F 4 HOH 6  306 16  HOH HOH A . 
F 4 HOH 7  307 38  HOH HOH A . 
F 4 HOH 8  308 32  HOH HOH A . 
F 4 HOH 9  309 18  HOH HOH A . 
F 4 HOH 10 310 111 HOH HOH A . 
F 4 HOH 11 311 50  HOH HOH A . 
F 4 HOH 12 312 109 HOH HOH A . 
F 4 HOH 13 313 95  HOH HOH A . 
F 4 HOH 14 314 41  HOH HOH A . 
F 4 HOH 15 315 2   HOH HOH A . 
F 4 HOH 16 316 25  HOH HOH A . 
F 4 HOH 17 317 23  HOH HOH A . 
F 4 HOH 18 318 15  HOH HOH A . 
F 4 HOH 19 319 121 HOH HOH A . 
F 4 HOH 20 320 118 HOH HOH A . 
F 4 HOH 21 321 55  HOH HOH A . 
F 4 HOH 22 322 1   HOH HOH A . 
F 4 HOH 23 323 43  HOH HOH A . 
F 4 HOH 24 324 62  HOH HOH A . 
F 4 HOH 25 325 78  HOH HOH A . 
F 4 HOH 26 326 22  HOH HOH A . 
F 4 HOH 27 327 86  HOH HOH A . 
F 4 HOH 28 328 134 HOH HOH A . 
F 4 HOH 29 329 12  HOH HOH A . 
F 4 HOH 30 330 124 HOH HOH A . 
F 4 HOH 31 331 120 HOH HOH A . 
F 4 HOH 32 332 104 HOH HOH A . 
F 4 HOH 33 333 34  HOH HOH A . 
F 4 HOH 34 334 79  HOH HOH A . 
F 4 HOH 35 335 33  HOH HOH A . 
F 4 HOH 36 336 14  HOH HOH A . 
F 4 HOH 37 337 132 HOH HOH A . 
F 4 HOH 38 338 80  HOH HOH A . 
F 4 HOH 39 339 6   HOH HOH A . 
F 4 HOH 40 340 45  HOH HOH A . 
F 4 HOH 41 341 142 HOH HOH A . 
F 4 HOH 42 342 13  HOH HOH A . 
F 4 HOH 43 343 148 HOH HOH A . 
F 4 HOH 44 344 44  HOH HOH A . 
F 4 HOH 45 345 61  HOH HOH A . 
F 4 HOH 46 346 131 HOH HOH A . 
F 4 HOH 47 347 24  HOH HOH A . 
F 4 HOH 48 348 66  HOH HOH A . 
F 4 HOH 49 349 123 HOH HOH A . 
F 4 HOH 50 350 65  HOH HOH A . 
F 4 HOH 51 351 47  HOH HOH A . 
F 4 HOH 52 352 36  HOH HOH A . 
F 4 HOH 53 353 9   HOH HOH A . 
F 4 HOH 54 354 133 HOH HOH A . 
F 4 HOH 55 355 103 HOH HOH A . 
F 4 HOH 56 356 59  HOH HOH A . 
F 4 HOH 57 357 68  HOH HOH A . 
F 4 HOH 58 358 67  HOH HOH A . 
F 4 HOH 59 359 102 HOH HOH A . 
F 4 HOH 60 360 119 HOH HOH A . 
F 4 HOH 61 361 96  HOH HOH A . 
F 4 HOH 62 362 37  HOH HOH A . 
F 4 HOH 63 363 97  HOH HOH A . 
F 4 HOH 64 364 72  HOH HOH A . 
F 4 HOH 65 365 128 HOH HOH A . 
F 4 HOH 66 366 126 HOH HOH A . 
F 4 HOH 67 367 129 HOH HOH A . 
F 4 HOH 68 368 54  HOH HOH A . 
F 4 HOH 69 369 127 HOH HOH A . 
F 4 HOH 70 370 140 HOH HOH A . 
F 4 HOH 71 371 137 HOH HOH A . 
F 4 HOH 72 372 46  HOH HOH A . 
F 4 HOH 73 373 82  HOH HOH A . 
F 4 HOH 74 374 136 HOH HOH A . 
F 4 HOH 75 375 143 HOH HOH A . 
F 4 HOH 76 376 76  HOH HOH A . 
F 4 HOH 77 377 98  HOH HOH A . 
F 4 HOH 78 378 53  HOH HOH A . 
F 4 HOH 79 379 74  HOH HOH A . 
F 4 HOH 80 380 90  HOH HOH A . 
G 4 HOH 1  301 150 HOH HOH B . 
G 4 HOH 2  302 106 HOH HOH B . 
G 4 HOH 3  303 113 HOH HOH B . 
G 4 HOH 4  304 100 HOH HOH B . 
G 4 HOH 5  305 87  HOH HOH B . 
G 4 HOH 6  306 51  HOH HOH B . 
G 4 HOH 7  307 58  HOH HOH B . 
G 4 HOH 8  308 10  HOH HOH B . 
G 4 HOH 9  309 57  HOH HOH B . 
G 4 HOH 10 310 27  HOH HOH B . 
G 4 HOH 11 311 5   HOH HOH B . 
G 4 HOH 12 312 26  HOH HOH B . 
G 4 HOH 13 313 49  HOH HOH B . 
G 4 HOH 14 314 116 HOH HOH B . 
G 4 HOH 15 315 40  HOH HOH B . 
G 4 HOH 16 316 35  HOH HOH B . 
G 4 HOH 17 317 138 HOH HOH B . 
G 4 HOH 18 318 21  HOH HOH B . 
G 4 HOH 19 319 3   HOH HOH B . 
G 4 HOH 20 320 75  HOH HOH B . 
G 4 HOH 21 321 31  HOH HOH B . 
G 4 HOH 22 322 63  HOH HOH B . 
G 4 HOH 23 323 20  HOH HOH B . 
G 4 HOH 24 324 110 HOH HOH B . 
G 4 HOH 25 325 114 HOH HOH B . 
G 4 HOH 26 326 42  HOH HOH B . 
G 4 HOH 27 327 99  HOH HOH B . 
G 4 HOH 28 328 28  HOH HOH B . 
G 4 HOH 29 329 19  HOH HOH B . 
G 4 HOH 30 330 146 HOH HOH B . 
G 4 HOH 31 331 29  HOH HOH B . 
G 4 HOH 32 332 91  HOH HOH B . 
G 4 HOH 33 333 81  HOH HOH B . 
G 4 HOH 34 334 11  HOH HOH B . 
G 4 HOH 35 335 130 HOH HOH B . 
G 4 HOH 36 336 73  HOH HOH B . 
G 4 HOH 37 337 108 HOH HOH B . 
G 4 HOH 38 338 94  HOH HOH B . 
G 4 HOH 39 339 52  HOH HOH B . 
G 4 HOH 40 340 93  HOH HOH B . 
G 4 HOH 41 341 85  HOH HOH B . 
G 4 HOH 42 342 4   HOH HOH B . 
G 4 HOH 43 343 125 HOH HOH B . 
G 4 HOH 44 344 89  HOH HOH B . 
G 4 HOH 45 345 17  HOH HOH B . 
G 4 HOH 46 346 48  HOH HOH B . 
G 4 HOH 47 347 8   HOH HOH B . 
G 4 HOH 48 348 141 HOH HOH B . 
G 4 HOH 49 349 105 HOH HOH B . 
G 4 HOH 50 350 60  HOH HOH B . 
G 4 HOH 51 351 84  HOH HOH B . 
G 4 HOH 52 352 56  HOH HOH B . 
G 4 HOH 53 353 64  HOH HOH B . 
G 4 HOH 54 354 30  HOH HOH B . 
G 4 HOH 55 355 112 HOH HOH B . 
G 4 HOH 56 356 147 HOH HOH B . 
G 4 HOH 57 357 101 HOH HOH B . 
G 4 HOH 58 358 135 HOH HOH B . 
G 4 HOH 59 359 122 HOH HOH B . 
G 4 HOH 60 360 151 HOH HOH B . 
G 4 HOH 61 361 115 HOH HOH B . 
G 4 HOH 62 362 117 HOH HOH B . 
G 4 HOH 63 363 107 HOH HOH B . 
G 4 HOH 64 364 92  HOH HOH B . 
G 4 HOH 65 365 77  HOH HOH B . 
G 4 HOH 66 366 83  HOH HOH B . 
G 4 HOH 67 367 70  HOH HOH B . 
G 4 HOH 68 368 139 HOH HOH B . 
G 4 HOH 69 369 71  HOH HOH B . 
G 4 HOH 70 370 145 HOH HOH B . 
G 4 HOH 71 371 88  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A GLN 25 ? N   B A GLN 29 N   
2 1 Y 0 A GLN 25 ? CA  B A GLN 29 CA  
3 1 Y 0 A GLN 25 ? C   B A GLN 29 C   
4 1 Y 0 A GLN 25 ? O   B A GLN 29 O   
5 1 Y 0 A GLN 25 ? CB  B A GLN 29 CB  
6 1 Y 0 A GLN 25 ? CG  B A GLN 29 CG  
7 1 Y 0 A GLN 25 ? CD  B A GLN 29 CD  
8 1 Y 0 A GLN 25 ? OE1 B A GLN 29 OE1 
9 1 Y 0 A GLN 25 ? NE2 B A GLN 29 NE2 
# 
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 ? ? ? '(1.17.1_3660: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LSD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.669 
_cell.length_a_esd                 ? 
_cell.length_b                     85.669 
_cell.length_b_esd                 ? 
_cell.length_c                     63.359 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9LSD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_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                   9LSD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.33 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '200 mM Magnesium chloride, 100 mM Tris base/ Hydrochloric acid, 30% (v/v) PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 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         2020-10-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979300 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LSD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.01 
_reflns.d_resolution_low                               32.16 
_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                                     17734 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.25 
_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                                0.128 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9890000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.114 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.01 2.13  ? ? ? ? ? ? 2857 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.544               ? ? 1 1 0.8959999999999999 ? ? ? ? 0.489 ? ? ? ? ? ? 
? ? ? 
2.13 2.27  ? ? ? ? ? ? 2658 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.375               ? ? 2 1 0.93               ? ? ? ? 0.335 ? ? ? ? ? ? 
? ? ? 
2.27 2.46  ? ? ? ? ? ? 2505 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.287               ? ? 3 1 0.953              ? ? ? ? 0.259 ? ? ? ? ? ? 
? ? ? 
2.46 2.69  ? ? ? ? ? ? 2322 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.222               ? ? 4 1 0.972              ? ? ? ? 
0.19899999999999998 ? ? ? ? ? ? ? ? ? 
2.69 3.01  ? ? ? ? ? ? 2080 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.16                ? ? 5 1 0.9790000000000001 ? ? ? ? 0.142 ? ? ? ? ? ? 
? ? ? 
3.01 3.47  ? ? ? ? ? ? 1836 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.12300000000000001 ? ? 6 1 0.982              ? ? ? ? 0.11 ? ? ? ? ? ? 
? ? ? 
3.47 4.24  ? ? ? ? ? ? 1577 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.105               ? ? 7 1 0.978              ? ? ? ? 
0.09300000000000001 ? ? ? ? ? ? ? ? ? 
4.24 5.98  ? ? ? ? ? ? 1211 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.10099999999999999 ? ? 8 1 0.9840000000000001 ? ? ? ? 0.09 ? ? ? ? ? ? 
? ? ? 
5.98 32.16 ? ? ? ? ? ? 688  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.085               ? ? 9 1 0.993              ? ? ? ? 0.076 ? ? ? ? ? ? 
? ? ? 
# 
_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                               ? 
_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                                 9LSD 
_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                            2.01 
_refine.ls_d_res_low                             32.01 
_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                     17648 
_refine.ls_number_reflns_R_free                  897 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1879 
_refine.ls_R_factor_R_free                       0.2287 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1857 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 27.51 
_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                            0.26 
_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.pdbx_number_atoms_protein        1735 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         19 
_refine_hist.number_atoms_solvent             151 
_refine_hist.number_atoms_total               1905 
_refine_hist.d_res_high                       2.01 
_refine_hist.d_res_low                        32.01 
# 
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' ? 0.007  ? 1815 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.799  ? 2457 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 32.965 ? 250  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 257  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 327  ? f_plane_restr      ? ? 
# 
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' 2.01 2.14  . . 140 2777 100.00 . . . . 0.2241 . . . . . . . . . . . 0.3308 
'X-RAY DIFFRACTION' 2.14 2.30  . . 132 2798 100.00 . . . . 0.2157 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 2.30 2.53  . . 140 2807 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2771 
'X-RAY DIFFRACTION' 2.53 2.90  . . 167 2757 100.00 . . . . 0.2143 . . . . . . . . . . . 0.2646 
'X-RAY DIFFRACTION' 2.90 3.65  . . 153 2794 99.00  . . . . 0.1780 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 3.65 32.01 . . 165 2818 99.00  . . . . 0.1609 . . . . . . . . . . . 0.1940 
# 
_struct.entry_id                     9LSD 
_struct.title                        'Crystal structure of a polyketide cyclase FasU from Streptomyces kanamyceticus' 
_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        9LSD 
_struct_keywords.text            'polyketide, cyclase, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A5J6G7S2_STRKN 
_struct_ref.pdbx_db_accession          A0A5J6G7S2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAEISADNEFATFINLFPTKPRDQQKLVDLIVKAHEELIRHRPGYVSGNVHRSVDGYQVVDYTQWRRREDFEAMVRDPAS
APHFMPIGELTQGKQGAYDVVYTHVTEEAEGAKEGTGDE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9LSD A 5 ? 123 ? A0A5J6G7S2 1 ? 119 ? 1 119 
2 1 9LSD B 5 ? 123 ? A0A5J6G7S2 1 ? 119 ? 1 119 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9LSD GLY A 1 ? UNP A0A5J6G7S2 ? ? 'expression tag' -3 1 
1 9LSD PRO A 2 ? UNP A0A5J6G7S2 ? ? 'expression tag' -2 2 
1 9LSD SER A 3 ? UNP A0A5J6G7S2 ? ? 'expression tag' -1 3 
1 9LSD GLY A 4 ? UNP A0A5J6G7S2 ? ? 'expression tag' 0  4 
2 9LSD GLY B 1 ? UNP A0A5J6G7S2 ? ? 'expression tag' -3 5 
2 9LSD PRO B 2 ? UNP A0A5J6G7S2 ? ? 'expression tag' -2 6 
2 9LSD SER B 3 ? UNP A0A5J6G7S2 ? ? 'expression tag' -1 7 
2 9LSD GLY B 4 ? UNP A0A5J6G7S2 ? ? 'expression tag' 0  8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3920  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  11150 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 LYS A 24 ? LEU A 42 ? LYS A 20 LEU A 38 1 ? 19 
HELX_P HELX_P2 AA2 ILE A 43 ? ARG A 46 ? ILE A 39 ARG A 42 5 ? 4  
HELX_P HELX_P3 AA3 ARG A 71 ? ASP A 81 ? ARG A 67 ASP A 77 1 ? 11 
HELX_P HELX_P4 AA4 SER A 84 ? GLU A 93 ? SER A 80 GLU A 89 1 ? 10 
HELX_P HELX_P5 AA5 LYS B 24 ? LEU B 42 ? LYS B 20 LEU B 38 1 ? 19 
HELX_P HELX_P6 AA6 ILE B 43 ? ARG B 46 ? ILE B 39 ARG B 42 5 ? 4  
HELX_P HELX_P7 AA7 ARG B 71 ? ASP B 81 ? ARG B 67 ASP B 77 1 ? 11 
HELX_P HELX_P8 AA8 SER B 84 ? THR B 95 ? SER B 80 THR B 91 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? D MG . MG ? ? ? 1_555 F HOH . O ? ? A MG 202 A HOH 301 4_665 ? ? ? ? ? ? ? 2.238 ? ? 
metalc2 metalc ? ? D MG . MG ? ? ? 1_555 F HOH . O ? ? A MG 202 A HOH 341 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc3 metalc ? ? D MG . MG ? ? ? 1_555 F HOH . O ? ? A MG 202 A HOH 375 1_555 ? ? ? ? ? ? ? 1.928 ? ? 
metalc4 metalc ? ? D MG . MG ? ? ? 1_555 G HOH . O ? ? A MG 202 B HOH 330 4_665 ? ? ? ? ? ? ? 2.126 ? ? 
metalc5 metalc ? ? D MG . MG ? ? ? 1_555 G HOH . O ? ? A MG 202 B HOH 348 4_665 ? ? ? ? ? ? ? 1.862 ? ? 
metalc6 metalc ? ? D MG . MG ? ? ? 1_555 G HOH . O ? ? A MG 202 B HOH 370 4_665 ? ? ? ? ? ? ? 1.998 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? F HOH . ? A HOH 301 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? F HOH . ? A HOH 341 ? 1_555 172.5 ? 
2  O ? F HOH . ? A HOH 301 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? F HOH . ? A HOH 375 ? 1_555 84.4  ? 
3  O ? F HOH . ? A HOH 341 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? F HOH . ? A HOH 375 ? 1_555 100.4 ? 
4  O ? F HOH . ? A HOH 301 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 330 ? 4_665 89.2  ? 
5  O ? F HOH . ? A HOH 341 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 330 ? 4_665 86.4  ? 
6  O ? F HOH . ? A HOH 375 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 330 ? 4_665 77.3  ? 
7  O ? F HOH . ? A HOH 301 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 348 ? 4_665 86.5  ? 
8  O ? F HOH . ? A HOH 341 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 348 ? 4_665 88.1  ? 
9  O ? F HOH . ? A HOH 375 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 348 ? 4_665 169.6 ? 
10 O ? G HOH . ? B HOH 330 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 348 ? 4_665 97.5  ? 
11 O ? F HOH . ? A HOH 301 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 370 ? 4_665 89.3  ? 
12 O ? F HOH . ? A HOH 341 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 370 ? 4_665 95.1  ? 
13 O ? F HOH . ? A HOH 375 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 370 ? 4_665 103.2 ? 
14 O ? G HOH . ? B HOH 330 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 370 ? 4_665 178.3 ? 
15 O ? G HOH . ? B HOH 348 ? 4_665 MG ? D MG . ? A MG 202 ? 1_555 O ? G HOH . ? B HOH 370 ? 4_665 81.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? 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 ALA A 6   ? ILE A 8   ? ALA A 2  ILE A 4   
AA1 2 ALA B 6   ? ILE B 8   ? ALA B 2  ILE B 4   
AA2 1 ALA A 15  ? PRO A 22  ? ALA A 11 PRO A 18  
AA2 2 GLN A 62  ? TRP A 69  ? GLN A 58 TRP A 65  
AA2 3 TYR A 49  ? SER A 57  ? TYR A 45 SER A 53  
AA2 4 ALA B 101 ? VAL B 109 ? ALA B 97 VAL B 105 
AA2 5 ALA B 15  ? PRO B 22  ? ALA B 11 PRO B 18  
AA2 6 GLN B 62  ? TRP B 69  ? GLN B 58 TRP B 65  
AA2 7 TYR B 49  ? SER B 57  ? TYR B 45 SER B 53  
AA2 8 ALA A 101 ? VAL A 109 ? ALA A 97 VAL A 105 
AA2 9 ALA A 15  ? PRO A 22  ? ALA A 11 PRO A 18  
# 
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 ALA A 6   ? N ALA A 2  O ILE B 8   ? O ILE B 4  
AA2 1 2 N PHE A 21  ? N PHE A 17 O VAL A 63  ? O VAL A 59 
AA2 2 3 O VAL A 64  ? O VAL A 60 N HIS A 55  ? N HIS A 51 
AA2 3 4 N ARG A 56  ? N ARG A 52 O ASP B 103 ? O ASP B 99 
AA2 4 5 O TYR B 102 ? O TYR B 98 N THR B 16  ? N THR B 12 
AA2 5 6 N ALA B 15  ? N ALA B 11 O TRP B 69  ? O TRP B 65 
AA2 6 7 O VAL B 64  ? O VAL B 60 N HIS B 55  ? N HIS B 51 
AA2 7 8 O ARG B 56  ? O ARG B 52 N ASP A 103 ? N ASP A 99 
AA2 8 9 O TYR A 102 ? O TYR A 98 N THR A 16  ? N THR A 12 
# 
_pdbx_entry_details.entry_id                   9LSD 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 19 ? ? -152.18 -159.28 
2 1 LEU A 38 ? ? -133.48 -57.97  
3 1 LEU B 38 ? ? -135.61 -55.32  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -3  ? A GLY 1   
2  1 Y 1 A PRO -2  ? A PRO 2   
3  1 Y 1 A SER -1  ? A SER 3   
4  1 Y 1 A GLY 0   ? A GLY 4   
5  1 Y 1 A GLU 108 ? A GLU 112 
6  1 Y 1 A ALA 109 ? A ALA 113 
7  1 Y 1 A GLU 110 ? A GLU 114 
8  1 Y 1 A GLY 111 ? A GLY 115 
9  1 Y 1 A ALA 112 ? A ALA 116 
10 1 Y 1 A LYS 113 ? A LYS 117 
11 1 Y 1 A GLU 114 ? A GLU 118 
12 1 Y 1 A GLY 115 ? A GLY 119 
13 1 Y 1 A THR 116 ? A THR 120 
14 1 Y 1 A GLY 117 ? A GLY 121 
15 1 Y 1 A ASP 118 ? A ASP 122 
16 1 Y 1 A GLU 119 ? A GLU 123 
17 1 Y 1 B GLY -3  ? B GLY 1   
18 1 Y 1 B PRO -2  ? B PRO 2   
19 1 Y 1 B SER -1  ? B SER 3   
20 1 Y 1 B GLU 107 ? B GLU 111 
21 1 Y 1 B GLU 108 ? B GLU 112 
22 1 Y 1 B ALA 109 ? B ALA 113 
23 1 Y 1 B GLU 110 ? B GLU 114 
24 1 Y 1 B GLY 111 ? B GLY 115 
25 1 Y 1 B ALA 112 ? B ALA 116 
26 1 Y 1 B LYS 113 ? B LYS 117 
27 1 Y 1 B GLU 114 ? B GLU 118 
28 1 Y 1 B GLY 115 ? B GLY 119 
29 1 Y 1 B THR 116 ? B THR 120 
30 1 Y 1 B GLY 117 ? B GLY 121 
31 1 Y 1 B ASP 118 ? B ASP 122 
32 1 Y 1 B GLU 119 ? B GLU 123 
# 
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 
AE3 C1   C  N N 1   
AE3 C2   C  N N 2   
AE3 O2   O  N N 3   
AE3 C3   C  N N 4   
AE3 C4   C  N N 5   
AE3 O3   O  N N 6   
AE3 C5   C  N N 7   
AE3 C6   C  N N 8   
AE3 O4   O  N N 9   
AE3 H1C1 H  N N 10  
AE3 H1C2 H  N N 11  
AE3 H1C3 H  N N 12  
AE3 H2C1 H  N N 13  
AE3 H2C2 H  N N 14  
AE3 H3C1 H  N N 15  
AE3 H3C2 H  N N 16  
AE3 H4C1 H  N N 17  
AE3 H4C2 H  N N 18  
AE3 H5C1 H  N N 19  
AE3 H5C2 H  N N 20  
AE3 H6C1 H  N N 21  
AE3 H6C2 H  N N 22  
AE3 H4   H  N N 23  
ALA N    N  N N 24  
ALA CA   C  N S 25  
ALA C    C  N N 26  
ALA O    O  N N 27  
ALA CB   C  N N 28  
ALA OXT  O  N N 29  
ALA H    H  N N 30  
ALA H2   H  N N 31  
ALA HA   H  N N 32  
ALA HB1  H  N N 33  
ALA HB2  H  N N 34  
ALA HB3  H  N N 35  
ALA HXT  H  N N 36  
ARG N    N  N N 37  
ARG CA   C  N S 38  
ARG C    C  N N 39  
ARG O    O  N N 40  
ARG CB   C  N N 41  
ARG CG   C  N N 42  
ARG CD   C  N N 43  
ARG NE   N  N N 44  
ARG CZ   C  N N 45  
ARG NH1  N  N N 46  
ARG NH2  N  N N 47  
ARG OXT  O  N N 48  
ARG H    H  N N 49  
ARG H2   H  N N 50  
ARG HA   H  N N 51  
ARG HB2  H  N N 52  
ARG HB3  H  N N 53  
ARG HG2  H  N N 54  
ARG HG3  H  N N 55  
ARG HD2  H  N N 56  
ARG HD3  H  N N 57  
ARG HE   H  N N 58  
ARG HH11 H  N N 59  
ARG HH12 H  N N 60  
ARG HH21 H  N N 61  
ARG HH22 H  N N 62  
ARG HXT  H  N N 63  
ASN N    N  N N 64  
ASN CA   C  N S 65  
ASN C    C  N N 66  
ASN O    O  N N 67  
ASN CB   C  N N 68  
ASN CG   C  N N 69  
ASN OD1  O  N N 70  
ASN ND2  N  N N 71  
ASN OXT  O  N N 72  
ASN H    H  N N 73  
ASN H2   H  N N 74  
ASN HA   H  N N 75  
ASN HB2  H  N N 76  
ASN HB3  H  N N 77  
ASN HD21 H  N N 78  
ASN HD22 H  N N 79  
ASN HXT  H  N N 80  
ASP N    N  N N 81  
ASP CA   C  N S 82  
ASP C    C  N N 83  
ASP O    O  N N 84  
ASP CB   C  N N 85  
ASP CG   C  N N 86  
ASP OD1  O  N N 87  
ASP OD2  O  N N 88  
ASP OXT  O  N N 89  
ASP H    H  N N 90  
ASP H2   H  N N 91  
ASP HA   H  N N 92  
ASP HB2  H  N N 93  
ASP HB3  H  N N 94  
ASP HD2  H  N N 95  
ASP HXT  H  N N 96  
GLN N    N  N N 97  
GLN CA   C  N S 98  
GLN C    C  N N 99  
GLN O    O  N N 100 
GLN CB   C  N N 101 
GLN CG   C  N N 102 
GLN CD   C  N N 103 
GLN OE1  O  N N 104 
GLN NE2  N  N N 105 
GLN OXT  O  N N 106 
GLN H    H  N N 107 
GLN H2   H  N N 108 
GLN HA   H  N N 109 
GLN HB2  H  N N 110 
GLN HB3  H  N N 111 
GLN HG2  H  N N 112 
GLN HG3  H  N N 113 
GLN HE21 H  N N 114 
GLN HE22 H  N N 115 
GLN HXT  H  N N 116 
GLU N    N  N N 117 
GLU CA   C  N S 118 
GLU C    C  N N 119 
GLU O    O  N N 120 
GLU CB   C  N N 121 
GLU CG   C  N N 122 
GLU CD   C  N N 123 
GLU OE1  O  N N 124 
GLU OE2  O  N N 125 
GLU OXT  O  N N 126 
GLU H    H  N N 127 
GLU H2   H  N N 128 
GLU HA   H  N N 129 
GLU HB2  H  N N 130 
GLU HB3  H  N N 131 
GLU HG2  H  N N 132 
GLU HG3  H  N N 133 
GLU HE2  H  N N 134 
GLU HXT  H  N N 135 
GLY N    N  N N 136 
GLY CA   C  N N 137 
GLY C    C  N N 138 
GLY O    O  N N 139 
GLY OXT  O  N N 140 
GLY H    H  N N 141 
GLY H2   H  N N 142 
GLY HA2  H  N N 143 
GLY HA3  H  N N 144 
GLY HXT  H  N N 145 
HIS N    N  N N 146 
HIS CA   C  N S 147 
HIS C    C  N N 148 
HIS O    O  N N 149 
HIS CB   C  N N 150 
HIS CG   C  Y N 151 
HIS ND1  N  Y N 152 
HIS CD2  C  Y N 153 
HIS CE1  C  Y N 154 
HIS NE2  N  Y N 155 
HIS OXT  O  N N 156 
HIS H    H  N N 157 
HIS H2   H  N N 158 
HIS HA   H  N N 159 
HIS HB2  H  N N 160 
HIS HB3  H  N N 161 
HIS HD1  H  N N 162 
HIS HD2  H  N N 163 
HIS HE1  H  N N 164 
HIS HE2  H  N N 165 
HIS HXT  H  N N 166 
HOH O    O  N N 167 
HOH H1   H  N N 168 
HOH H2   H  N N 169 
ILE N    N  N N 170 
ILE CA   C  N S 171 
ILE C    C  N N 172 
ILE O    O  N N 173 
ILE CB   C  N S 174 
ILE CG1  C  N N 175 
ILE CG2  C  N N 176 
ILE CD1  C  N N 177 
ILE OXT  O  N N 178 
ILE H    H  N N 179 
ILE H2   H  N N 180 
ILE HA   H  N N 181 
ILE HB   H  N N 182 
ILE HG12 H  N N 183 
ILE HG13 H  N N 184 
ILE HG21 H  N N 185 
ILE HG22 H  N N 186 
ILE HG23 H  N N 187 
ILE HD11 H  N N 188 
ILE HD12 H  N N 189 
ILE HD13 H  N N 190 
ILE HXT  H  N N 191 
LEU N    N  N N 192 
LEU CA   C  N S 193 
LEU C    C  N N 194 
LEU O    O  N N 195 
LEU CB   C  N N 196 
LEU CG   C  N N 197 
LEU CD1  C  N N 198 
LEU CD2  C  N N 199 
LEU OXT  O  N N 200 
LEU H    H  N N 201 
LEU H2   H  N N 202 
LEU HA   H  N N 203 
LEU HB2  H  N N 204 
LEU HB3  H  N N 205 
LEU HG   H  N N 206 
LEU HD11 H  N N 207 
LEU HD12 H  N N 208 
LEU HD13 H  N N 209 
LEU HD21 H  N N 210 
LEU HD22 H  N N 211 
LEU HD23 H  N N 212 
LEU HXT  H  N N 213 
LYS N    N  N N 214 
LYS CA   C  N S 215 
LYS C    C  N N 216 
LYS O    O  N N 217 
LYS CB   C  N N 218 
LYS CG   C  N N 219 
LYS CD   C  N N 220 
LYS CE   C  N N 221 
LYS NZ   N  N N 222 
LYS OXT  O  N N 223 
LYS H    H  N N 224 
LYS H2   H  N N 225 
LYS HA   H  N N 226 
LYS HB2  H  N N 227 
LYS HB3  H  N N 228 
LYS HG2  H  N N 229 
LYS HG3  H  N N 230 
LYS HD2  H  N N 231 
LYS HD3  H  N N 232 
LYS HE2  H  N N 233 
LYS HE3  H  N N 234 
LYS HZ1  H  N N 235 
LYS HZ2  H  N N 236 
LYS HZ3  H  N N 237 
LYS HXT  H  N N 238 
MET N    N  N N 239 
MET CA   C  N S 240 
MET C    C  N N 241 
MET O    O  N N 242 
MET CB   C  N N 243 
MET CG   C  N N 244 
MET SD   S  N N 245 
MET CE   C  N N 246 
MET OXT  O  N N 247 
MET H    H  N N 248 
MET H2   H  N N 249 
MET HA   H  N N 250 
MET HB2  H  N N 251 
MET HB3  H  N N 252 
MET HG2  H  N N 253 
MET HG3  H  N N 254 
MET HE1  H  N N 255 
MET HE2  H  N N 256 
MET HE3  H  N N 257 
MET HXT  H  N N 258 
MG  MG   MG N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
# 
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 
AE3 C1  C2   sing N N 1   
AE3 C1  H1C1 sing N N 2   
AE3 C1  H1C2 sing N N 3   
AE3 C1  H1C3 sing N N 4   
AE3 C2  O2   sing N N 5   
AE3 C2  H2C1 sing N N 6   
AE3 C2  H2C2 sing N N 7   
AE3 O2  C3   sing N N 8   
AE3 C3  C4   sing N N 9   
AE3 C3  H3C1 sing N N 10  
AE3 C3  H3C2 sing N N 11  
AE3 C4  O3   sing N N 12  
AE3 C4  H4C1 sing N N 13  
AE3 C4  H4C2 sing N N 14  
AE3 O3  C5   sing N N 15  
AE3 C5  C6   sing N N 16  
AE3 C5  H5C1 sing N N 17  
AE3 C5  H5C2 sing N N 18  
AE3 C6  O4   sing N N 19  
AE3 C6  H6C1 sing N N 20  
AE3 C6  H6C2 sing N N 21  
AE3 O4  H4   sing N N 22  
ALA N   CA   sing N N 23  
ALA N   H    sing N N 24  
ALA N   H2   sing N N 25  
ALA CA  C    sing N N 26  
ALA CA  CB   sing N N 27  
ALA CA  HA   sing N N 28  
ALA C   O    doub N N 29  
ALA C   OXT  sing N N 30  
ALA CB  HB1  sing N N 31  
ALA CB  HB2  sing N N 32  
ALA CB  HB3  sing N N 33  
ALA OXT HXT  sing N N 34  
ARG N   CA   sing N N 35  
ARG N   H    sing N N 36  
ARG N   H2   sing N N 37  
ARG CA  C    sing N N 38  
ARG CA  CB   sing N N 39  
ARG CA  HA   sing N N 40  
ARG C   O    doub N N 41  
ARG C   OXT  sing N N 42  
ARG CB  CG   sing N N 43  
ARG CB  HB2  sing N N 44  
ARG CB  HB3  sing N N 45  
ARG CG  CD   sing N N 46  
ARG CG  HG2  sing N N 47  
ARG CG  HG3  sing N N 48  
ARG CD  NE   sing N N 49  
ARG CD  HD2  sing N N 50  
ARG CD  HD3  sing N N 51  
ARG NE  CZ   sing N N 52  
ARG NE  HE   sing N N 53  
ARG CZ  NH1  sing N N 54  
ARG CZ  NH2  doub N N 55  
ARG NH1 HH11 sing N N 56  
ARG NH1 HH12 sing N N 57  
ARG NH2 HH21 sing N N 58  
ARG NH2 HH22 sing N N 59  
ARG OXT HXT  sing N N 60  
ASN N   CA   sing N N 61  
ASN N   H    sing N N 62  
ASN N   H2   sing N N 63  
ASN CA  C    sing N N 64  
ASN CA  CB   sing N N 65  
ASN CA  HA   sing N N 66  
ASN C   O    doub N N 67  
ASN C   OXT  sing N N 68  
ASN CB  CG   sing N N 69  
ASN CB  HB2  sing N N 70  
ASN CB  HB3  sing N N 71  
ASN CG  OD1  doub N N 72  
ASN CG  ND2  sing N N 73  
ASN ND2 HD21 sing N N 74  
ASN ND2 HD22 sing N N 75  
ASN OXT HXT  sing N N 76  
ASP N   CA   sing N N 77  
ASP N   H    sing N N 78  
ASP N   H2   sing N N 79  
ASP CA  C    sing N N 80  
ASP CA  CB   sing N N 81  
ASP CA  HA   sing N N 82  
ASP C   O    doub N N 83  
ASP C   OXT  sing N N 84  
ASP CB  CG   sing N N 85  
ASP CB  HB2  sing N N 86  
ASP CB  HB3  sing N N 87  
ASP CG  OD1  doub N N 88  
ASP CG  OD2  sing N N 89  
ASP OD2 HD2  sing N N 90  
ASP OXT HXT  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_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          ? 
# 
_atom_sites.entry_id                    9LSD 
_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]   0.011673 
_atom_sites.fract_transf_matrix[1][2]   0.006739 
_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]   0.013479 
_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]   0.015783 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 5   ? 32.217 36.144 5.181   1.00 43.97 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 5   ? 30.978 35.428 4.877   1.00 47.79 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 5   ? 31.235 34.041 4.293   1.00 48.92 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 5   ? 32.296 33.787 3.722   1.00 47.06 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 5   ? 30.131 36.244 3.918   1.00 50.12 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 5   ? 29.352 37.331 4.620   1.00 51.57 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 5   ? 29.053 38.733 3.545   1.00 82.20 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 5   ? 28.585 37.905 2.025   1.00 59.57 ? 1   MET A CE  1 
ATOM   9    N  N   . ALA A 1 6   ? 30.267 33.138 4.451   1.00 41.78 ? 2   ALA A N   1 
ATOM   10   C  CA  . ALA A 1 6   ? 30.436 31.786 3.936   1.00 35.68 ? 2   ALA A CA  1 
ATOM   11   C  C   . ALA A 1 6   ? 30.566 31.816 2.415   1.00 35.61 ? 2   ALA A C   1 
ATOM   12   O  O   . ALA A 1 6   ? 29.762 32.447 1.724   1.00 33.93 ? 2   ALA A O   1 
ATOM   13   C  CB  . ALA A 1 6   ? 29.260 30.910 4.368   1.00 33.65 ? 2   ALA A CB  1 
ATOM   14   N  N   . GLU A 1 7   ? 31.598 31.153 1.900   1.00 36.92 ? 3   GLU A N   1 
ATOM   15   C  CA  . GLU A 1 7   ? 31.897 31.124 0.475   1.00 39.83 ? 3   GLU A CA  1 
ATOM   16   C  C   . GLU A 1 7   ? 31.805 29.701 -0.052  1.00 40.70 ? 3   GLU A C   1 
ATOM   17   O  O   . GLU A 1 7   ? 32.257 28.754 0.603   1.00 35.56 ? 3   GLU A O   1 
ATOM   18   C  CB  . GLU A 1 7   ? 33.299 31.680 0.187   1.00 35.00 ? 3   GLU A CB  1 
ATOM   19   C  CG  . GLU A 1 7   ? 33.591 32.995 0.874   1.00 45.63 ? 3   GLU A CG  1 
ATOM   20   C  CD  . GLU A 1 7   ? 35.059 33.370 0.804   1.00 56.73 ? 3   GLU A CD  1 
ATOM   21   O  OE1 . GLU A 1 7   ? 35.386 34.400 0.179   1.00 58.10 ? 3   GLU A OE1 1 
ATOM   22   O  OE2 . GLU A 1 7   ? 35.886 32.624 1.365   1.00 54.52 ? 3   GLU A OE2 1 
ATOM   23   N  N   . ILE A 1 8   ? 31.246 29.559 -1.250  1.00 30.45 ? 4   ILE A N   1 
ATOM   24   C  CA  . ILE A 1 8   ? 31.174 28.278 -1.944  1.00 34.45 ? 4   ILE A CA  1 
ATOM   25   C  C   . ILE A 1 8   ? 32.371 28.194 -2.882  1.00 43.35 ? 4   ILE A C   1 
ATOM   26   O  O   . ILE A 1 8   ? 32.523 29.027 -3.784  1.00 45.64 ? 4   ILE A O   1 
ATOM   27   C  CB  . ILE A 1 8   ? 29.850 28.127 -2.709  1.00 30.02 ? 4   ILE A CB  1 
ATOM   28   C  CG1 . ILE A 1 8   ? 28.677 28.297 -1.757  1.00 29.70 ? 4   ILE A CG1 1 
ATOM   29   C  CG2 . ILE A 1 8   ? 29.783 26.792 -3.426  1.00 34.17 ? 4   ILE A CG2 1 
ATOM   30   C  CD1 . ILE A 1 8   ? 27.342 28.279 -2.442  1.00 36.13 ? 4   ILE A CD1 1 
ATOM   31   N  N   . SER A 1 9   ? 33.231 27.203 -2.662  1.00 41.69 ? 5   SER A N   1 
ATOM   32   C  CA  . SER A 1 9   ? 34.467 27.046 -3.419  1.00 41.73 ? 5   SER A CA  1 
ATOM   33   C  C   . SER A 1 9   ? 34.495 25.686 -4.092  1.00 44.08 ? 5   SER A C   1 
ATOM   34   O  O   . SER A 1 9   ? 34.311 24.661 -3.426  1.00 42.07 ? 5   SER A O   1 
ATOM   35   C  CB  . SER A 1 9   ? 35.696 27.177 -2.516  1.00 50.12 ? 5   SER A CB  1 
ATOM   36   O  OG  . SER A 1 9   ? 36.854 26.723 -3.195  1.00 48.84 ? 5   SER A OG  1 
ATOM   37   N  N   . ALA A 1 10  ? 34.762 25.675 -5.401  1.00 43.51 ? 6   ALA A N   1 
ATOM   38   C  CA  . ALA A 1 10  ? 34.995 24.404 -6.069  1.00 41.19 ? 6   ALA A CA  1 
ATOM   39   C  C   . ALA A 1 10  ? 36.331 23.790 -5.692  1.00 44.81 ? 6   ALA A C   1 
ATOM   40   O  O   . ALA A 1 10  ? 36.635 22.690 -6.165  1.00 40.87 ? 6   ALA A O   1 
ATOM   41   C  CB  . ALA A 1 10  ? 34.913 24.562 -7.589  1.00 38.06 ? 6   ALA A CB  1 
ATOM   42   N  N   . ASP A 1 11  ? 37.134 24.457 -4.857  1.00 42.79 ? 7   ASP A N   1 
ATOM   43   C  CA  . ASP A 1 11  ? 38.337 23.819 -4.337  1.00 50.47 ? 7   ASP A CA  1 
ATOM   44   C  C   . ASP A 1 11  ? 38.046 22.864 -3.188  1.00 53.05 ? 7   ASP A C   1 
ATOM   45   O  O   . ASP A 1 11  ? 38.905 22.034 -2.858  1.00 43.61 ? 7   ASP A O   1 
ATOM   46   C  CB  . ASP A 1 11  ? 39.354 24.873 -3.895  1.00 50.63 ? 7   ASP A CB  1 
ATOM   47   C  CG  . ASP A 1 11  ? 39.940 25.637 -5.067  1.00 73.81 ? 7   ASP A CG  1 
ATOM   48   O  OD1 . ASP A 1 11  ? 39.897 25.103 -6.198  1.00 74.21 ? 7   ASP A OD1 1 
ATOM   49   O  OD2 . ASP A 1 11  ? 40.450 26.761 -4.860  1.00 74.69 ? 7   ASP A OD2 1 
ATOM   50   N  N   . ASN A 1 12  ? 36.856 22.955 -2.591  1.00 44.59 ? 8   ASN A N   1 
ATOM   51   C  CA  . ASN A 1 12  ? 36.446 22.079 -1.501  1.00 38.76 ? 8   ASN A CA  1 
ATOM   52   C  C   . ASN A 1 12  ? 37.464 22.094 -0.369  1.00 47.08 ? 8   ASN A C   1 
ATOM   53   O  O   . ASN A 1 12  ? 37.824 21.051 0.190   1.00 38.16 ? 8   ASN A O   1 
ATOM   54   C  CB  . ASN A 1 12  ? 36.203 20.661 -2.008  1.00 36.85 ? 8   ASN A CB  1 
ATOM   55   C  CG  . ASN A 1 12  ? 34.910 20.544 -2.784  1.00 38.85 ? 8   ASN A CG  1 
ATOM   56   O  OD1 . ASN A 1 12  ? 33.834 20.486 -2.195  1.00 33.04 ? 8   ASN A OD1 1 
ATOM   57   N  ND2 . ASN A 1 12  ? 35.008 20.512 -4.114  1.00 31.63 ? 8   ASN A ND2 1 
ATOM   58   N  N   . GLU A 1 13  ? 37.941 23.299 -0.042  1.00 37.76 ? 9   GLU A N   1 
ATOM   59   C  CA  . GLU A 1 13  ? 38.817 23.475 1.110   1.00 40.06 ? 9   GLU A CA  1 
ATOM   60   C  C   . GLU A 1 13  ? 38.204 22.876 2.372   1.00 48.53 ? 9   GLU A C   1 
ATOM   61   O  O   . GLU A 1 13  ? 38.909 22.295 3.209   1.00 44.31 ? 9   GLU A O   1 
ATOM   62   C  CB  . GLU A 1 13  ? 39.097 24.965 1.311   1.00 51.06 ? 9   GLU A CB  1 
ATOM   63   C  CG  . GLU A 1 13  ? 40.279 25.265 2.206   1.00 63.58 ? 9   GLU A CG  1 
ATOM   64   C  CD  . GLU A 1 13  ? 40.400 26.744 2.532   1.00 66.86 ? 9   GLU A CD  1 
ATOM   65   O  OE1 . GLU A 1 13  ? 41.094 27.079 3.519   1.00 67.49 ? 9   GLU A OE1 1 
ATOM   66   O  OE2 . GLU A 1 13  ? 39.802 27.567 1.802   1.00 68.20 ? 9   GLU A OE2 1 
ATOM   67   N  N   . PHE A 1 14  ? 36.890 23.015 2.520   1.00 36.25 ? 10  PHE A N   1 
ATOM   68   C  CA  . PHE A 1 14  ? 36.127 22.549 3.665   1.00 37.55 ? 10  PHE A CA  1 
ATOM   69   C  C   . PHE A 1 14  ? 35.209 21.406 3.256   1.00 31.79 ? 10  PHE A C   1 
ATOM   70   O  O   . PHE A 1 14  ? 34.896 21.225 2.079   1.00 39.03 ? 10  PHE A O   1 
ATOM   71   C  CB  . PHE A 1 14  ? 35.290 23.691 4.251   1.00 31.73 ? 10  PHE A CB  1 
ATOM   72   C  CG  . PHE A 1 14  ? 36.093 24.913 4.589   1.00 39.64 ? 10  PHE A CG  1 
ATOM   73   C  CD1 . PHE A 1 14  ? 37.131 24.842 5.505   1.00 42.87 ? 10  PHE A CD1 1 
ATOM   74   C  CD2 . PHE A 1 14  ? 35.823 26.125 3.978   1.00 43.27 ? 10  PHE A CD2 1 
ATOM   75   C  CE1 . PHE A 1 14  ? 37.876 25.958 5.823   1.00 40.22 ? 10  PHE A CE1 1 
ATOM   76   C  CE2 . PHE A 1 14  ? 36.566 27.248 4.283   1.00 49.65 ? 10  PHE A CE2 1 
ATOM   77   C  CZ  . PHE A 1 14  ? 37.598 27.164 5.207   1.00 48.21 ? 10  PHE A CZ  1 
ATOM   78   N  N   . ALA A 1 15  ? 34.771 20.639 4.248   1.00 28.73 ? 11  ALA A N   1 
ATOM   79   C  CA  . ALA A 1 15  ? 33.676 19.705 4.039   1.00 28.94 ? 11  ALA A CA  1 
ATOM   80   C  C   . ALA A 1 15  ? 32.349 20.449 4.043   1.00 29.02 ? 11  ALA A C   1 
ATOM   81   O  O   . ALA A 1 15  ? 32.166 21.436 4.764   1.00 29.82 ? 11  ALA A O   1 
ATOM   82   C  CB  . ALA A 1 15  ? 33.665 18.628 5.118   1.00 24.85 ? 11  ALA A CB  1 
ATOM   83   N  N   . THR A 1 16  ? 31.408 19.949 3.248   1.00 24.21 ? 12  THR A N   1 
ATOM   84   C  CA  . THR A 1 16  ? 30.110 20.582 3.082   1.00 26.05 ? 12  THR A CA  1 
ATOM   85   C  C   . THR A 1 16  ? 29.019 19.578 3.409   1.00 29.02 ? 12  THR A C   1 
ATOM   86   O  O   . THR A 1 16  ? 28.967 18.492 2.819   1.00 29.45 ? 12  THR A O   1 
ATOM   87   C  CB  . THR A 1 16  ? 29.935 21.113 1.659   1.00 25.87 ? 12  THR A CB  1 
ATOM   88   O  OG1 . THR A 1 16  ? 31.018 22.002 1.352   1.00 28.11 ? 12  THR A OG1 1 
ATOM   89   C  CG2 . THR A 1 16  ? 28.585 21.851 1.519   1.00 28.57 ? 12  THR A CG2 1 
ATOM   90   N  N   . PHE A 1 17  ? 28.150 19.940 4.337   1.00 25.64 ? 13  PHE A N   1 
ATOM   91   C  CA  . PHE A 1 17  ? 26.944 19.176 4.604   1.00 31.23 ? 13  PHE A CA  1 
ATOM   92   C  C   . PHE A 1 17  ? 25.740 19.997 4.185   1.00 33.87 ? 13  PHE A C   1 
ATOM   93   O  O   . PHE A 1 17  ? 25.685 21.205 4.435   1.00 29.74 ? 13  PHE A O   1 
ATOM   94   C  CB  . PHE A 1 17  ? 26.830 18.808 6.075   1.00 23.18 ? 13  PHE A CB  1 
ATOM   95   C  CG  . PHE A 1 17  ? 27.817 17.785 6.508   1.00 28.27 ? 13  PHE A CG  1 
ATOM   96   C  CD1 . PHE A 1 17  ? 27.451 16.455 6.614   1.00 27.71 ? 13  PHE A CD1 1 
ATOM   97   C  CD2 . PHE A 1 17  ? 29.122 18.144 6.800   1.00 26.43 ? 13  PHE A CD2 1 
ATOM   98   C  CE1 . PHE A 1 17  ? 28.371 15.497 7.020   1.00 28.00 ? 13  PHE A CE1 1 
ATOM   99   C  CE2 . PHE A 1 17  ? 30.047 17.193 7.199   1.00 29.03 ? 13  PHE A CE2 1 
ATOM   100  C  CZ  . PHE A 1 17  ? 29.675 15.872 7.315   1.00 28.38 ? 13  PHE A CZ  1 
ATOM   101  N  N   . ILE A 1 18  ? 24.790 19.340 3.536   1.00 29.36 ? 14  ILE A N   1 
ATOM   102  C  CA  . ILE A 1 18  ? 23.510 19.933 3.206   1.00 23.81 ? 14  ILE A CA  1 
ATOM   103  C  C   . ILE A 1 18  ? 22.479 19.056 3.883   1.00 33.89 ? 14  ILE A C   1 
ATOM   104  O  O   . ILE A 1 18  ? 22.119 17.986 3.381   1.00 32.04 ? 14  ILE A O   1 
ATOM   105  C  CB  . ILE A 1 18  ? 23.277 20.031 1.701   1.00 29.74 ? 14  ILE A CB  1 
ATOM   106  C  CG1 . ILE A 1 18  ? 24.449 20.762 1.039   1.00 23.31 ? 14  ILE A CG1 1 
ATOM   107  C  CG2 . ILE A 1 18  ? 21.965 20.751 1.434   1.00 30.66 ? 14  ILE A CG2 1 
ATOM   108  C  CD1 . ILE A 1 18  ? 24.338 20.819 -0.463  1.00 24.87 ? 14  ILE A CD1 1 
ATOM   109  N  N   . ASN A 1 19  ? 22.018 19.494 5.040   1.00 27.80 ? 15  ASN A N   1 
ATOM   110  C  CA  . ASN A 1 19  ? 21.090 18.721 5.840   1.00 27.49 ? 15  ASN A CA  1 
ATOM   111  C  C   . ASN A 1 19  ? 19.671 19.189 5.564   1.00 28.58 ? 15  ASN A C   1 
ATOM   112  O  O   . ASN A 1 19  ? 19.378 20.390 5.629   1.00 21.58 ? 15  ASN A O   1 
ATOM   113  C  CB  . ASN A 1 19  ? 21.497 18.834 7.308   1.00 23.46 ? 15  ASN A CB  1 
ATOM   114  C  CG  . ASN A 1 19  ? 22.918 18.322 7.510   1.00 38.91 ? 15  ASN A CG  1 
ATOM   115  O  OD1 . ASN A 1 19  ? 23.403 17.544 6.679   1.00 35.32 ? 15  ASN A OD1 1 
ATOM   116  N  ND2 . ASN A 1 19  ? 23.605 18.777 8.556   1.00 36.79 ? 15  ASN A ND2 1 
ATOM   117  N  N   . LEU A 1 20  ? 18.810 18.235 5.216   1.00 23.01 ? 16  LEU A N   1 
ATOM   118  C  CA  . LEU A 1 20  ? 17.459 18.494 4.734   1.00 29.67 ? 16  LEU A CA  1 
ATOM   119  C  C   . LEU A 1 20  ? 16.464 18.058 5.796   1.00 33.48 ? 16  LEU A C   1 
ATOM   120  O  O   . LEU A 1 20  ? 16.429 16.882 6.167   1.00 34.79 ? 16  LEU A O   1 
ATOM   121  C  CB  . LEU A 1 20  ? 17.176 17.737 3.441   1.00 32.35 ? 16  LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 20  ? 18.222 17.819 2.337   1.00 41.46 ? 16  LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 20  ? 18.123 16.601 1.426   1.00 39.37 ? 16  LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 20  ? 18.059 19.113 1.570   1.00 37.19 ? 16  LEU A CD2 1 
ATOM   125  N  N   . PHE A 1 21  ? 15.638 18.991 6.250   1.00 24.25 ? 17  PHE A N   1 
ATOM   126  C  CA  . PHE A 1 21  ? 14.684 18.746 7.331   1.00 29.21 ? 17  PHE A CA  1 
ATOM   127  C  C   . PHE A 1 21  ? 13.277 18.952 6.788   1.00 34.37 ? 17  PHE A C   1 
ATOM   128  O  O   . PHE A 1 21  ? 12.760 20.080 6.786   1.00 34.23 ? 17  PHE A O   1 
ATOM   129  C  CB  . PHE A 1 21  ? 14.952 19.660 8.526   1.00 24.85 ? 17  PHE A CB  1 
ATOM   130  C  CG  . PHE A 1 21  ? 16.337 19.533 9.112   1.00 25.79 ? 17  PHE A CG  1 
ATOM   131  C  CD1 . PHE A 1 21  ? 16.657 18.473 9.950   1.00 35.73 ? 17  PHE A CD1 1 
ATOM   132  C  CD2 . PHE A 1 21  ? 17.301 20.495 8.861   1.00 26.44 ? 17  PHE A CD2 1 
ATOM   133  C  CE1 . PHE A 1 21  ? 17.923 18.361 10.503  1.00 30.24 ? 17  PHE A CE1 1 
ATOM   134  C  CE2 . PHE A 1 21  ? 18.563 20.396 9.401   1.00 27.36 ? 17  PHE A CE2 1 
ATOM   135  C  CZ  . PHE A 1 21  ? 18.879 19.316 10.227  1.00 37.65 ? 17  PHE A CZ  1 
ATOM   136  N  N   . PRO A 1 22  ? 12.632 17.900 6.295   1.00 39.27 ? 18  PRO A N   1 
ATOM   137  C  CA  . PRO A 1 22  ? 11.242 18.036 5.856   1.00 28.31 ? 18  PRO A CA  1 
ATOM   138  C  C   . PRO A 1 22  ? 10.322 18.299 7.035   1.00 29.04 ? 18  PRO A C   1 
ATOM   139  O  O   . PRO A 1 22  ? 10.495 17.750 8.125   1.00 26.61 ? 18  PRO A O   1 
ATOM   140  C  CB  . PRO A 1 22  ? 10.941 16.682 5.206   1.00 34.96 ? 18  PRO A CB  1 
ATOM   141  C  CG  . PRO A 1 22  ? 12.291 16.122 4.872   1.00 40.96 ? 18  PRO A CG  1 
ATOM   142  C  CD  . PRO A 1 22  ? 13.176 16.570 5.983   1.00 33.75 ? 18  PRO A CD  1 
ATOM   143  N  N   . THR A 1 23  ? 9.337  19.155 6.813   1.00 26.66 ? 19  THR A N   1 
ATOM   144  C  CA  . THR A 1 23  ? 8.468  19.571 7.901   1.00 24.97 ? 19  THR A CA  1 
ATOM   145  C  C   . THR A 1 23  ? 7.120  19.932 7.290   1.00 27.81 ? 19  THR A C   1 
ATOM   146  O  O   . THR A 1 23  ? 6.795  19.507 6.177   1.00 27.20 ? 19  THR A O   1 
ATOM   147  C  CB  . THR A 1 23  ? 9.133  20.710 8.696   1.00 27.43 ? 19  THR A CB  1 
ATOM   148  O  OG1 . THR A 1 23  ? 8.330  21.058 9.840   1.00 28.92 ? 19  THR A OG1 1 
ATOM   149  C  CG2 . THR A 1 23  ? 9.374  21.947 7.809   1.00 27.28 ? 19  THR A CG2 1 
ATOM   150  N  N   . LYS A 1 24  ? 6.335  20.716 8.005   1.00 26.26 ? 20  LYS A N   1 
ATOM   151  C  CA  . LYS A 1 24  ? 5.076  21.182 7.457   1.00 25.98 ? 20  LYS A CA  1 
ATOM   152  C  C   . LYS A 1 24  ? 4.819  22.571 8.007   1.00 27.47 ? 20  LYS A C   1 
ATOM   153  O  O   . LYS A 1 24  ? 5.369  22.935 9.055   1.00 27.65 ? 20  LYS A O   1 
ATOM   154  C  CB  . LYS A 1 24  ? 3.933  20.211 7.786   1.00 32.29 ? 20  LYS A CB  1 
ATOM   155  C  CG  . LYS A 1 24  ? 3.625  20.042 9.255   1.00 38.38 ? 20  LYS A CG  1 
ATOM   156  C  CD  . LYS A 1 24  ? 2.540  18.971 9.414   1.00 42.24 ? 20  LYS A CD  1 
ATOM   157  C  CE  . LYS A 1 24  ? 2.788  18.095 10.628  1.00 52.80 ? 20  LYS A CE  1 
ATOM   158  N  NZ  . LYS A 1 24  ? 2.392  16.682 10.360  1.00 60.89 ? 20  LYS A NZ  1 
ATOM   159  N  N   . PRO A 1 25  ? 4.016  23.385 7.315   1.00 31.78 ? 21  PRO A N   1 
ATOM   160  C  CA  . PRO A 1 25  ? 3.925  24.804 7.698   1.00 27.33 ? 21  PRO A CA  1 
ATOM   161  C  C   . PRO A 1 25  ? 3.685  25.041 9.177   1.00 27.81 ? 21  PRO A C   1 
ATOM   162  O  O   . PRO A 1 25  ? 4.294  25.951 9.754   1.00 27.84 ? 21  PRO A O   1 
ATOM   163  C  CB  . PRO A 1 25  ? 2.759  25.310 6.840   1.00 30.74 ? 21  PRO A CB  1 
ATOM   164  C  CG  . PRO A 1 25  ? 2.845  24.456 5.591   1.00 24.50 ? 21  PRO A CG  1 
ATOM   165  C  CD  . PRO A 1 25  ? 3.258  23.092 6.077   1.00 25.81 ? 21  PRO A CD  1 
ATOM   166  N  N   . ARG A 1 26  ? 2.839  24.242 9.829   1.00 30.02 ? 22  ARG A N   1 
ATOM   167  C  CA  . ARG A 1 26  ? 2.562  24.584 11.216  1.00 37.62 ? 22  ARG A CA  1 
ATOM   168  C  C   . ARG A 1 26  ? 3.764  24.339 12.119  1.00 28.92 ? 22  ARG A C   1 
ATOM   169  O  O   . ARG A 1 26  ? 3.856  24.971 13.173  1.00 32.66 ? 22  ARG A O   1 
ATOM   170  C  CB  . ARG A 1 26  ? 1.343  23.827 11.733  1.00 38.64 ? 22  ARG A CB  1 
ATOM   171  C  CG  . ARG A 1 26  ? 1.460  22.323 11.773  1.00 38.68 ? 22  ARG A CG  1 
ATOM   172  C  CD  . ARG A 1 26  ? 0.206  21.752 12.426  1.00 49.04 ? 22  ARG A CD  1 
ATOM   173  N  NE  . ARG A 1 26  ? 0.110  20.305 12.302  1.00 45.87 ? 22  ARG A NE  1 
ATOM   174  C  CZ  . ARG A 1 26  ? -0.488 19.681 11.293  1.00 56.90 ? 22  ARG A CZ  1 
ATOM   175  N  NH1 . ARG A 1 26  ? -0.530 18.353 11.262  1.00 62.81 ? 22  ARG A NH1 1 
ATOM   176  N  NH2 . ARG A 1 26  ? -1.045 20.381 10.314  1.00 51.60 ? 22  ARG A NH2 1 
ATOM   177  N  N   . ASP A 1 27  ? 4.696  23.466 11.719  1.00 27.22 ? 23  ASP A N   1 
ATOM   178  C  CA  . ASP A 1 27  ? 5.881  23.163 12.524  1.00 30.04 ? 23  ASP A CA  1 
ATOM   179  C  C   . ASP A 1 27  ? 7.125  23.946 12.117  1.00 33.47 ? 23  ASP A C   1 
ATOM   180  O  O   . ASP A 1 27  ? 8.116  23.915 12.854  1.00 27.49 ? 23  ASP A O   1 
ATOM   181  C  CB  . ASP A 1 27  ? 6.240  21.671 12.436  1.00 32.33 ? 23  ASP A CB  1 
ATOM   182  C  CG  . ASP A 1 27  ? 5.240  20.763 13.149  1.00 39.44 ? 23  ASP A CG  1 
ATOM   183  O  OD1 . ASP A 1 27  ? 5.132  19.586 12.748  1.00 33.46 ? 23  ASP A OD1 1 
ATOM   184  O  OD2 . ASP A 1 27  ? 4.562  21.220 14.087  1.00 37.42 ? 23  ASP A OD2 1 
ATOM   185  N  N   . GLN A 1 28  ? 7.121  24.622 10.962  1.00 29.02 ? 24  GLN A N   1 
ATOM   186  C  CA  . GLN A 1 28  ? 8.396  25.025 10.364  1.00 27.41 ? 24  GLN A CA  1 
ATOM   187  C  C   . GLN A 1 28  ? 9.117  26.072 11.199  1.00 31.14 ? 24  GLN A C   1 
ATOM   188  O  O   . GLN A 1 28  ? 10.331 25.976 11.398  1.00 30.14 ? 24  GLN A O   1 
ATOM   189  C  CB  . GLN A 1 28  ? 8.194  25.534 8.938   1.00 30.54 ? 24  GLN A CB  1 
ATOM   190  C  CG  . GLN A 1 28  ? 9.507  25.902 8.213   1.00 23.44 ? 24  GLN A CG  1 
ATOM   191  C  CD  . GLN A 1 28  ? 9.260  26.712 6.936   1.00 26.41 ? 24  GLN A CD  1 
ATOM   192  O  OE1 . GLN A 1 28  ? 8.543  27.708 6.950   1.00 26.98 ? 24  GLN A OE1 1 
ATOM   193  N  NE2 . GLN A 1 28  ? 9.861  26.281 5.830   1.00 23.05 ? 24  GLN A NE2 1 
ATOM   194  N  N   A GLN A 1 29  ? 8.401  27.081 11.708  0.53 28.18 ? 25  GLN A N   1 
ATOM   195  N  N   B GLN A 1 29  ? 8.389  27.073 11.708  0.00 28.41 ? 25  GLN A N   1 
ATOM   196  N  N   D GLN A 1 29  ? 8.386  27.083 11.680  0.47 28.36 ? 25  GLN A N   1 
ATOM   197  C  CA  A GLN A 1 29  ? 9.085  28.130 12.460  0.53 28.23 ? 25  GLN A CA  1 
ATOM   198  C  CA  B GLN A 1 29  ? 9.029  28.139 12.474  0.00 28.24 ? 25  GLN A CA  1 
ATOM   199  C  CA  D GLN A 1 29  ? 8.994  28.138 12.483  0.47 28.25 ? 25  GLN A CA  1 
ATOM   200  C  C   A GLN A 1 29  ? 9.627  27.605 13.787  0.53 29.73 ? 25  GLN A C   1 
ATOM   201  C  C   B GLN A 1 29  ? 9.609  27.615 13.784  0.00 29.79 ? 25  GLN A C   1 
ATOM   202  C  C   D GLN A 1 29  ? 9.625  27.570 13.748  0.47 29.88 ? 25  GLN A C   1 
ATOM   203  O  O   A GLN A 1 29  ? 10.727 27.985 14.203  0.53 29.90 ? 25  GLN A O   1 
ATOM   204  O  O   B GLN A 1 29  ? 10.704 28.021 14.191  0.00 29.84 ? 25  GLN A O   1 
ATOM   205  O  O   D GLN A 1 29  ? 10.772 27.885 14.081  0.47 29.83 ? 25  GLN A O   1 
ATOM   206  C  CB  A GLN A 1 29  ? 8.162  29.332 12.680  0.53 29.18 ? 25  GLN A CB  1 
ATOM   207  C  CB  B GLN A 1 29  ? 8.031  29.266 12.741  0.00 29.17 ? 25  GLN A CB  1 
ATOM   208  C  CB  D GLN A 1 29  ? 7.942  29.193 12.827  0.47 29.18 ? 25  GLN A CB  1 
ATOM   209  C  CG  A GLN A 1 29  ? 8.902  30.679 12.757  0.53 30.54 ? 25  GLN A CG  1 
ATOM   210  C  CG  B GLN A 1 29  ? 8.676  30.632 12.901  0.00 29.87 ? 25  GLN A CG  1 
ATOM   211  C  CG  D GLN A 1 29  ? 8.450  30.344 13.669  0.47 28.90 ? 25  GLN A CG  1 
ATOM   212  C  CD  A GLN A 1 29  ? 9.606  31.068 11.451  0.53 31.19 ? 25  GLN A CD  1 
ATOM   213  C  CD  B GLN A 1 29  ? 9.475  31.044 11.681  0.00 30.37 ? 25  GLN A CD  1 
ATOM   214  C  CD  D GLN A 1 29  ? 7.430  31.453 13.794  0.47 28.85 ? 25  GLN A CD  1 
ATOM   215  O  OE1 A GLN A 1 29  ? 10.832 30.981 11.343  0.53 28.01 ? 25  GLN A OE1 1 
ATOM   216  O  OE1 B GLN A 1 29  ? 10.705 30.993 11.684  0.00 28.76 ? 25  GLN A OE1 1 
ATOM   217  O  OE1 D GLN A 1 29  ? 6.911  31.715 14.878  0.47 23.71 ? 25  GLN A OE1 1 
ATOM   218  N  NE2 A GLN A 1 29  ? 8.827  31.511 10.459  0.53 30.10 ? 25  GLN A NE2 1 
ATOM   219  N  NE2 B GLN A 1 29  ? 8.778  31.456 10.628  0.00 29.98 ? 25  GLN A NE2 1 
ATOM   220  N  NE2 D GLN A 1 29  ? 7.132  32.108 12.681  0.47 23.84 ? 25  GLN A NE2 1 
ATOM   221  N  N   . LYS A 1 30  ? 8.882  26.724 14.463  1.00 28.09 ? 26  LYS A N   1 
ATOM   222  C  CA  . LYS A 1 30  ? 9.429  26.062 15.650  1.00 33.88 ? 26  LYS A CA  1 
ATOM   223  C  C   . LYS A 1 30  ? 10.704 25.284 15.321  1.00 30.38 ? 26  LYS A C   1 
ATOM   224  O  O   . LYS A 1 30  ? 11.681 25.304 16.085  1.00 30.92 ? 26  LYS A O   1 
ATOM   225  C  CB  . LYS A 1 30  ? 8.378  25.117 16.234  1.00 32.64 ? 26  LYS A CB  1 
ATOM   226  C  CG  . LYS A 1 30  ? 8.782  24.402 17.515  1.00 36.49 ? 26  LYS A CG  1 
ATOM   227  C  CD  . LYS A 1 30  ? 9.464  25.351 18.491  1.00 50.58 ? 26  LYS A CD  1 
ATOM   228  C  CE  . LYS A 1 30  ? 8.471  26.341 19.097  1.00 57.74 ? 26  LYS A CE  1 
ATOM   229  N  NZ  . LYS A 1 30  ? 9.170  27.541 19.625  1.00 62.21 ? 26  LYS A NZ  1 
ATOM   230  N  N   . LEU A 1 31  ? 10.712 24.587 14.188  1.00 30.44 ? 27  LEU A N   1 
ATOM   231  C  CA  . LEU A 1 31  ? 11.896 23.832 13.793  1.00 25.96 ? 27  LEU A CA  1 
ATOM   232  C  C   . LEU A 1 31  ? 13.061 24.767 13.511  1.00 25.20 ? 27  LEU A C   1 
ATOM   233  O  O   . LEU A 1 31  ? 14.168 24.565 14.021  1.00 28.52 ? 27  LEU A O   1 
ATOM   234  C  CB  . LEU A 1 31  ? 11.569 22.973 12.571  1.00 28.04 ? 27  LEU A CB  1 
ATOM   235  C  CG  . LEU A 1 31  ? 12.702 22.195 11.910  1.00 32.01 ? 27  LEU A CG  1 
ATOM   236  C  CD1 . LEU A 1 31  ? 13.346 21.229 12.903  1.00 29.76 ? 27  LEU A CD1 1 
ATOM   237  C  CD2 . LEU A 1 31  ? 12.176 21.465 10.664  1.00 26.64 ? 27  LEU A CD2 1 
ATOM   238  N  N   . VAL A 1 32  ? 12.818 25.815 12.706  1.00 26.44 ? 28  VAL A N   1 
ATOM   239  C  CA  . VAL A 1 32  ? 13.839 26.827 12.446  1.00 22.17 ? 28  VAL A CA  1 
ATOM   240  C  C   . VAL A 1 32  ? 14.405 27.348 13.761  1.00 32.14 ? 28  VAL A C   1 
ATOM   241  O  O   . VAL A 1 32  ? 15.623 27.436 13.938  1.00 26.22 ? 28  VAL A O   1 
ATOM   242  C  CB  . VAL A 1 32  ? 13.271 27.990 11.599  1.00 23.22 ? 28  VAL A CB  1 
ATOM   243  C  CG1 . VAL A 1 32  ? 14.249 29.173 11.588  1.00 22.08 ? 28  VAL A CG1 1 
ATOM   244  C  CG2 . VAL A 1 32  ? 12.990 27.562 10.165  1.00 18.93 ? 28  VAL A CG2 1 
ATOM   245  N  N   . ASP A 1 33  ? 13.526 27.727 14.694  1.00 30.11 ? 29  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 33  ? 13.994 28.304 15.956  1.00 32.36 ? 29  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 33  ? 14.885 27.321 16.716  1.00 26.82 ? 29  ASP A C   1 
ATOM   248  O  O   . ASP A 1 33  ? 15.919 27.707 17.268  1.00 29.87 ? 29  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 33  ? 12.803 28.724 16.825  1.00 28.69 ? 29  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 33  ? 12.061 29.949 16.282  1.00 36.46 ? 29  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 33  ? 12.613 30.703 15.447  1.00 33.89 ? 29  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 33  ? 10.916 30.169 16.732  1.00 39.52 ? 29  ASP A OD2 1 
ATOM   253  N  N   . LEU A 1 34  ? 14.513 26.043 16.725  1.00 22.74 ? 30  LEU A N   1 
ATOM   254  C  CA  . LEU A 1 34  ? 15.328 25.052 17.423  1.00 30.33 ? 30  LEU A CA  1 
ATOM   255  C  C   . LEU A 1 34  ? 16.662 24.810 16.721  1.00 32.08 ? 30  LEU A C   1 
ATOM   256  O  O   . LEU A 1 34  ? 17.666 24.529 17.382  1.00 29.76 ? 30  LEU A O   1 
ATOM   257  C  CB  . LEU A 1 34  ? 14.561 23.738 17.544  1.00 23.75 ? 30  LEU A CB  1 
ATOM   258  C  CG  . LEU A 1 34  ? 13.394 23.633 18.530  1.00 29.29 ? 30  LEU A CG  1 
ATOM   259  C  CD1 . LEU A 1 34  ? 12.665 22.347 18.275  1.00 26.68 ? 30  LEU A CD1 1 
ATOM   260  C  CD2 . LEU A 1 34  ? 13.911 23.655 19.954  1.00 33.75 ? 30  LEU A CD2 1 
ATOM   261  N  N   . ILE A 1 35  ? 16.693 24.897 15.392  1.00 24.04 ? 31  ILE A N   1 
ATOM   262  C  CA  . ILE A 1 35  ? 17.945 24.698 14.664  1.00 23.76 ? 31  ILE A CA  1 
ATOM   263  C  C   . ILE A 1 35  ? 18.889 25.876 14.887  1.00 26.05 ? 31  ILE A C   1 
ATOM   264  O  O   . ILE A 1 35  ? 20.075 25.694 15.170  1.00 27.59 ? 31  ILE A O   1 
ATOM   265  C  CB  . ILE A 1 35  ? 17.660 24.460 13.166  1.00 22.15 ? 31  ILE A CB  1 
ATOM   266  C  CG1 . ILE A 1 35  ? 17.155 23.020 12.949  1.00 19.61 ? 31  ILE A CG1 1 
ATOM   267  C  CG2 . ILE A 1 35  ? 18.914 24.658 12.351  1.00 23.82 ? 31  ILE A CG2 1 
ATOM   268  C  CD1 . ILE A 1 35  ? 16.443 22.777 11.595  1.00 23.75 ? 31  ILE A CD1 1 
ATOM   269  N  N   . VAL A 1 36  ? 18.371 27.104 14.798  1.00 25.61 ? 32  VAL A N   1 
ATOM   270  C  CA  . VAL A 1 36  ? 19.200 28.287 15.032  1.00 23.58 ? 32  VAL A CA  1 
ATOM   271  C  C   . VAL A 1 36  ? 19.709 28.318 16.468  1.00 28.11 ? 32  VAL A C   1 
ATOM   272  O  O   . VAL A 1 36  ? 20.871 28.659 16.721  1.00 27.70 ? 32  VAL A O   1 
ATOM   273  C  CB  . VAL A 1 36  ? 18.401 29.559 14.699  1.00 29.55 ? 32  VAL A CB  1 
ATOM   274  C  CG1 . VAL A 1 36  ? 19.111 30.782 15.234  1.00 26.70 ? 32  VAL A CG1 1 
ATOM   275  C  CG2 . VAL A 1 36  ? 18.179 29.666 13.209  1.00 27.37 ? 32  VAL A CG2 1 
ATOM   276  N  N   . LYS A 1 37  ? 18.848 27.972 17.433  1.00 27.10 ? 33  LYS A N   1 
ATOM   277  C  CA  . LYS A 1 37  ? 19.288 27.930 18.828  1.00 32.79 ? 33  LYS A CA  1 
ATOM   278  C  C   . LYS A 1 37  ? 20.438 26.943 19.006  1.00 31.29 ? 33  LYS A C   1 
ATOM   279  O  O   . LYS A 1 37  ? 21.447 27.259 19.646  1.00 34.25 ? 33  LYS A O   1 
ATOM   280  C  CB  . LYS A 1 37  ? 18.105 27.576 19.734  1.00 35.72 ? 33  LYS A CB  1 
ATOM   281  C  CG  . LYS A 1 37  ? 18.452 27.276 21.202  1.00 37.03 ? 33  LYS A CG  1 
ATOM   282  C  CD  . LYS A 1 37  ? 17.217 26.760 21.948  1.00 36.72 ? 33  LYS A CD  1 
ATOM   283  C  CE  . LYS A 1 37  ? 17.467 26.607 23.455  1.00 46.32 ? 33  LYS A CE  1 
ATOM   284  N  NZ  . LYS A 1 37  ? 17.710 27.918 24.121  1.00 45.98 ? 33  LYS A NZ  1 
ATOM   285  N  N   . ALA A 1 38  ? 20.312 25.741 18.419  1.00 28.06 ? 34  ALA A N   1 
ATOM   286  C  CA  . ALA A 1 38  ? 21.396 24.763 18.487  1.00 29.71 ? 34  ALA A CA  1 
ATOM   287  C  C   . ALA A 1 38  ? 22.672 25.315 17.866  1.00 25.84 ? 34  ALA A C   1 
ATOM   288  O  O   . ALA A 1 38  ? 23.765 25.137 18.413  1.00 24.68 ? 34  ALA A O   1 
ATOM   289  C  CB  . ALA A 1 38  ? 20.981 23.462 17.791  1.00 25.50 ? 34  ALA A CB  1 
ATOM   290  N  N   . HIS A 1 39  ? 22.552 26.016 16.735  1.00 20.75 ? 35  HIS A N   1 
ATOM   291  C  CA  . HIS A 1 39  ? 23.724 26.610 16.104  1.00 18.07 ? 35  HIS A CA  1 
ATOM   292  C  C   . HIS A 1 39  ? 24.418 27.602 17.031  1.00 30.23 ? 35  HIS A C   1 
ATOM   293  O  O   . HIS A 1 39  ? 25.643 27.561 17.199  1.00 25.54 ? 35  HIS A O   1 
ATOM   294  C  CB  . HIS A 1 39  ? 23.332 27.286 14.790  1.00 19.57 ? 35  HIS A CB  1 
ATOM   295  C  CG  . HIS A 1 39  ? 23.603 26.442 13.584  1.00 27.54 ? 35  HIS A CG  1 
ATOM   296  N  ND1 . HIS A 1 39  ? 24.874 26.235 13.095  1.00 23.81 ? 35  HIS A ND1 1 
ATOM   297  C  CD2 . HIS A 1 39  ? 22.770 25.732 12.783  1.00 26.96 ? 35  HIS A CD2 1 
ATOM   298  C  CE1 . HIS A 1 39  ? 24.815 25.433 12.044  1.00 24.94 ? 35  HIS A CE1 1 
ATOM   299  N  NE2 . HIS A 1 39  ? 23.550 25.112 11.836  1.00 24.20 ? 35  HIS A NE2 1 
ATOM   300  N  N   . GLU A 1 40  ? 23.655 28.513 17.636  1.00 24.53 ? 36  GLU A N   1 
ATOM   301  C  CA  . GLU A 1 40  ? 24.274 29.555 18.445  1.00 24.07 ? 36  GLU A CA  1 
ATOM   302  C  C   . GLU A 1 40  ? 24.826 28.993 19.749  1.00 22.16 ? 36  GLU A C   1 
ATOM   303  O  O   . GLU A 1 40  ? 25.927 29.366 20.173  1.00 30.57 ? 36  GLU A O   1 
ATOM   304  C  CB  . GLU A 1 40  ? 23.260 30.668 18.714  1.00 31.15 ? 36  GLU A CB  1 
ATOM   305  C  CG  . GLU A 1 40  ? 22.848 31.430 17.446  1.00 30.99 ? 36  GLU A CG  1 
ATOM   306  C  CD  . GLU A 1 40  ? 21.914 32.594 17.737  1.00 27.75 ? 36  GLU A CD  1 
ATOM   307  O  OE1 . GLU A 1 40  ? 21.214 32.549 18.767  1.00 29.86 ? 36  GLU A OE1 1 
ATOM   308  O  OE2 . GLU A 1 40  ? 21.871 33.543 16.930  1.00 28.31 ? 36  GLU A OE2 1 
ATOM   309  N  N   . GLU A 1 41  ? 24.093 28.069 20.371  1.00 23.71 ? 37  GLU A N   1 
ATOM   310  C  CA  . GLU A 1 41  ? 24.446 27.531 21.675  1.00 26.24 ? 37  GLU A CA  1 
ATOM   311  C  C   . GLU A 1 41  ? 25.381 26.338 21.607  1.00 33.85 ? 37  GLU A C   1 
ATOM   312  O  O   . GLU A 1 41  ? 26.065 26.064 22.593  1.00 29.61 ? 37  GLU A O   1 
ATOM   313  C  CB  . GLU A 1 41  ? 23.184 27.113 22.434  1.00 27.83 ? 37  GLU A CB  1 
ATOM   314  C  CG  . GLU A 1 41  ? 22.256 28.277 22.786  1.00 36.69 ? 37  GLU A CG  1 
ATOM   315  C  CD  . GLU A 1 41  ? 21.089 27.850 23.661  1.00 37.73 ? 37  GLU A CD  1 
ATOM   316  O  OE1 . GLU A 1 41  ? 20.199 28.679 23.940  1.00 52.32 ? 37  GLU A OE1 1 
ATOM   317  O  OE2 . GLU A 1 41  ? 21.056 26.679 24.066  1.00 39.11 ? 37  GLU A OE2 1 
ATOM   318  N  N   . LEU A 1 42  ? 25.436 25.617 20.485  1.00 26.79 ? 38  LEU A N   1 
ATOM   319  C  CA  . LEU A 1 42  ? 26.226 24.392 20.461  1.00 26.43 ? 38  LEU A CA  1 
ATOM   320  C  C   . LEU A 1 42  ? 27.123 24.261 19.234  1.00 26.61 ? 38  LEU A C   1 
ATOM   321  O  O   . LEU A 1 42  ? 28.346 24.145 19.363  1.00 25.08 ? 38  LEU A O   1 
ATOM   322  C  CB  . LEU A 1 42  ? 25.307 23.184 20.541  1.00 25.48 ? 38  LEU A CB  1 
ATOM   323  C  CG  . LEU A 1 42  ? 26.083 21.861 20.534  1.00 32.58 ? 38  LEU A CG  1 
ATOM   324  C  CD1 . LEU A 1 42  ? 26.475 21.468 21.949  1.00 40.27 ? 38  LEU A CD1 1 
ATOM   325  C  CD2 . LEU A 1 42  ? 25.256 20.794 19.907  1.00 28.90 ? 38  LEU A CD2 1 
ATOM   326  N  N   . ILE A 1 43  ? 26.532 24.294 18.039  1.00 23.18 ? 39  ILE A N   1 
ATOM   327  C  CA  . ILE A 1 43  ? 27.263 23.882 16.836  1.00 21.87 ? 39  ILE A CA  1 
ATOM   328  C  C   . ILE A 1 43  ? 28.460 24.781 16.593  1.00 20.66 ? 39  ILE A C   1 
ATOM   329  O  O   . ILE A 1 43  ? 29.571 24.304 16.348  1.00 26.95 ? 39  ILE A O   1 
ATOM   330  C  CB  . ILE A 1 43  ? 26.326 23.861 15.616  1.00 22.82 ? 39  ILE A CB  1 
ATOM   331  C  CG1 . ILE A 1 43  ? 25.160 22.912 15.890  1.00 21.02 ? 39  ILE A CG1 1 
ATOM   332  C  CG2 . ILE A 1 43  ? 27.130 23.493 14.353  1.00 18.55 ? 39  ILE A CG2 1 
ATOM   333  C  CD1 . ILE A 1 43  ? 24.065 22.930 14.787  1.00 21.28 ? 39  ILE A CD1 1 
ATOM   334  N  N   . ARG A 1 44  ? 28.263 26.099 16.673  1.00 22.82 ? 40  ARG A N   1 
ATOM   335  C  CA  . ARG A 1 44  ? 29.342 27.006 16.319  1.00 21.80 ? 40  ARG A CA  1 
ATOM   336  C  C   . ARG A 1 44  ? 30.538 26.914 17.254  1.00 25.38 ? 40  ARG A C   1 
ATOM   337  O  O   . ARG A 1 44  ? 31.604 27.447 16.910  1.00 23.21 ? 40  ARG A O   1 
ATOM   338  C  CB  . ARG A 1 44  ? 28.839 28.450 16.249  1.00 22.59 ? 40  ARG A CB  1 
ATOM   339  C  CG  . ARG A 1 44  ? 28.264 29.012 17.532  1.00 22.99 ? 40  ARG A CG  1 
ATOM   340  C  CD  . ARG A 1 44  ? 28.052 30.506 17.383  1.00 24.41 ? 40  ARG A CD  1 
ATOM   341  N  NE  . ARG A 1 44  ? 27.538 31.143 18.593  1.00 28.60 ? 40  ARG A NE  1 
ATOM   342  C  CZ  . ARG A 1 44  ? 27.354 32.460 18.708  1.00 29.00 ? 40  ARG A CZ  1 
ATOM   343  N  NH1 . ARG A 1 44  ? 26.885 32.974 19.833  1.00 24.45 ? 40  ARG A NH1 1 
ATOM   344  N  NH2 . ARG A 1 44  ? 27.623 33.262 17.689  1.00 27.89 ? 40  ARG A NH2 1 
ATOM   345  N  N   . HIS A 1 45  ? 30.409 26.244 18.400  1.00 25.66 ? 41  HIS A N   1 
ATOM   346  C  CA  . HIS A 1 45  ? 31.531 26.103 19.321  1.00 27.41 ? 41  HIS A CA  1 
ATOM   347  C  C   . HIS A 1 45  ? 32.239 24.768 19.184  1.00 29.90 ? 41  HIS A C   1 
ATOM   348  O  O   . HIS A 1 45  ? 33.186 24.518 19.932  1.00 27.57 ? 41  HIS A O   1 
ATOM   349  C  CB  . HIS A 1 45  ? 31.070 26.280 20.778  1.00 23.81 ? 41  HIS A CB  1 
ATOM   350  C  CG  . HIS A 1 45  ? 30.303 27.539 21.010  1.00 29.04 ? 41  HIS A CG  1 
ATOM   351  N  ND1 . HIS A 1 45  ? 30.859 28.788 20.845  1.00 33.96 ? 41  HIS A ND1 1 
ATOM   352  C  CD2 . HIS A 1 45  ? 29.007 27.744 21.340  1.00 27.53 ? 41  HIS A CD2 1 
ATOM   353  C  CE1 . HIS A 1 45  ? 29.946 29.710 21.094  1.00 33.37 ? 41  HIS A CE1 1 
ATOM   354  N  NE2 . HIS A 1 45  ? 28.815 29.104 21.403  1.00 32.82 ? 41  HIS A NE2 1 
ATOM   355  N  N   . ARG A 1 46  ? 31.802 23.909 18.257  1.00 27.97 ? 42  ARG A N   1 
ATOM   356  C  CA  . ARG A 1 46  ? 32.419 22.603 18.074  1.00 28.95 ? 42  ARG A CA  1 
ATOM   357  C  C   . ARG A 1 46  ? 33.788 22.732 17.405  1.00 25.64 ? 42  ARG A C   1 
ATOM   358  O  O   . ARG A 1 46  ? 33.998 23.604 16.559  1.00 27.07 ? 42  ARG A O   1 
ATOM   359  C  CB  . ARG A 1 46  ? 31.524 21.700 17.217  1.00 26.15 ? 42  ARG A CB  1 
ATOM   360  C  CG  . ARG A 1 46  ? 30.259 21.240 17.894  1.00 24.94 ? 42  ARG A CG  1 
ATOM   361  C  CD  . ARG A 1 46  ? 30.554 20.253 19.015  1.00 32.01 ? 42  ARG A CD  1 
ATOM   362  N  NE  . ARG A 1 46  ? 31.554 19.271 18.604  1.00 32.18 ? 42  ARG A NE  1 
ATOM   363  C  CZ  . ARG A 1 46  ? 31.745 18.096 19.191  1.00 33.48 ? 42  ARG A CZ  1 
ATOM   364  N  NH1 . ARG A 1 46  ? 32.695 17.293 18.736  1.00 36.39 ? 42  ARG A NH1 1 
ATOM   365  N  NH2 . ARG A 1 46  ? 31.011 17.729 20.238  1.00 32.95 ? 42  ARG A NH2 1 
ATOM   366  N  N   . PRO A 1 47  ? 34.732 21.862 17.760  1.00 26.93 ? 43  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 47  ? 35.991 21.791 17.008  1.00 26.02 ? 43  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 47  ? 35.721 21.523 15.535  1.00 28.85 ? 43  PRO A C   1 
ATOM   369  O  O   . PRO A 1 47  ? 34.892 20.684 15.192  1.00 26.90 ? 43  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 47  ? 36.726 20.612 17.660  1.00 27.30 ? 43  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 47  ? 36.127 20.507 19.031  1.00 34.85 ? 43  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 47  ? 34.692 20.906 18.885  1.00 25.24 ? 43  PRO A CD  1 
ATOM   373  N  N   . GLY A 1 48  ? 36.428 22.246 14.660  1.00 25.95 ? 44  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 48  ? 36.298 22.042 13.229  1.00 26.70 ? 44  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 48  ? 35.151 22.772 12.562  1.00 26.03 ? 44  GLY A C   1 
ATOM   376  O  O   . GLY A 1 48  ? 35.060 22.749 11.330  1.00 27.85 ? 44  GLY A O   1 
ATOM   377  N  N   . TYR A 1 49  ? 34.270 23.412 13.323  1.00 25.08 ? 45  TYR A N   1 
ATOM   378  C  CA  . TYR A 1 49  ? 33.172 24.170 12.730  1.00 22.38 ? 45  TYR A CA  1 
ATOM   379  C  C   . TYR A 1 49  ? 33.693 25.323 11.878  1.00 25.00 ? 45  TYR A C   1 
ATOM   380  O  O   . TYR A 1 49  ? 34.574 26.071 12.303  1.00 26.99 ? 45  TYR A O   1 
ATOM   381  C  CB  . TYR A 1 49  ? 32.262 24.699 13.830  1.00 24.10 ? 45  TYR A CB  1 
ATOM   382  C  CG  . TYR A 1 49  ? 31.330 25.829 13.399  1.00 25.05 ? 45  TYR A CG  1 
ATOM   383  C  CD1 . TYR A 1 49  ? 30.087 25.560 12.849  1.00 20.53 ? 45  TYR A CD1 1 
ATOM   384  C  CD2 . TYR A 1 49  ? 31.707 27.160 13.550  1.00 30.54 ? 45  TYR A CD2 1 
ATOM   385  C  CE1 . TYR A 1 49  ? 29.224 26.592 12.475  1.00 23.32 ? 45  TYR A CE1 1 
ATOM   386  C  CE2 . TYR A 1 49  ? 30.865 28.204 13.165  1.00 27.20 ? 45  TYR A CE2 1 
ATOM   387  C  CZ  . TYR A 1 49  ? 29.615 27.912 12.642  1.00 26.18 ? 45  TYR A CZ  1 
ATOM   388  O  OH  . TYR A 1 49  ? 28.771 28.946 12.271  1.00 25.11 ? 45  TYR A OH  1 
ATOM   389  N  N   . VAL A 1 50  ? 33.139 25.481 10.675  1.00 26.93 ? 46  VAL A N   1 
ATOM   390  C  CA  . VAL A 1 50  ? 33.481 26.601 9.792   1.00 28.66 ? 46  VAL A CA  1 
ATOM   391  C  C   . VAL A 1 50  ? 32.295 27.554 9.612   1.00 30.82 ? 46  VAL A C   1 
ATOM   392  O  O   . VAL A 1 50  ? 32.412 28.748 9.878   1.00 32.61 ? 46  VAL A O   1 
ATOM   393  C  CB  . VAL A 1 50  ? 34.024 26.106 8.432   1.00 30.84 ? 46  VAL A CB  1 
ATOM   394  C  CG1 . VAL A 1 50  ? 34.200 27.277 7.479   1.00 28.42 ? 46  VAL A CG1 1 
ATOM   395  C  CG2 . VAL A 1 50  ? 35.363 25.373 8.633   1.00 24.31 ? 46  VAL A CG2 1 
ATOM   396  N  N   . SER A 1 51  ? 31.140 27.045 9.166   1.00 24.36 ? 47  SER A N   1 
ATOM   397  C  CA  . SER A 1 51  ? 29.994 27.943 9.022   1.00 25.93 ? 47  SER A CA  1 
ATOM   398  C  C   . SER A 1 51  ? 28.677 27.197 9.171   1.00 28.08 ? 47  SER A C   1 
ATOM   399  O  O   . SER A 1 51  ? 28.598 25.983 8.973   1.00 28.54 ? 47  SER A O   1 
ATOM   400  C  CB  . SER A 1 51  ? 29.991 28.679 7.676   1.00 27.25 ? 47  SER A CB  1 
ATOM   401  O  OG  . SER A 1 51  ? 29.841 27.787 6.580   1.00 30.15 ? 47  SER A OG  1 
ATOM   402  N  N   . GLY A 1 52  ? 27.645 27.949 9.537   1.00 24.00 ? 48  GLY A N   1 
ATOM   403  C  CA  . GLY A 1 52  ? 26.282 27.437 9.536   1.00 25.24 ? 48  GLY A CA  1 
ATOM   404  C  C   . GLY A 1 52  ? 25.376 28.412 8.811   1.00 27.14 ? 48  GLY A C   1 
ATOM   405  O  O   . GLY A 1 52  ? 25.508 29.620 8.967   1.00 25.07 ? 48  GLY A O   1 
ATOM   406  N  N   . ASN A 1 53  ? 24.469 27.870 7.989   1.00 22.61 ? 49  ASN A N   1 
ATOM   407  C  CA  . ASN A 1 53  ? 23.619 28.704 7.118   1.00 22.93 ? 49  ASN A CA  1 
ATOM   408  C  C   . ASN A 1 53  ? 22.243 28.049 7.019   1.00 29.53 ? 49  ASN A C   1 
ATOM   409  O  O   . ASN A 1 53  ? 22.069 27.102 6.241   1.00 26.31 ? 49  ASN A O   1 
ATOM   410  C  CB  . ASN A 1 53  ? 24.242 28.858 5.733   1.00 19.41 ? 49  ASN A CB  1 
ATOM   411  C  CG  . ASN A 1 53  ? 25.691 29.326 5.787   1.00 30.08 ? 49  ASN A CG  1 
ATOM   412  O  OD1 . ASN A 1 53  ? 25.963 30.526 5.698   1.00 29.29 ? 49  ASN A OD1 1 
ATOM   413  N  ND2 . ASN A 1 53  ? 26.631 28.381 5.924   1.00 25.30 ? 49  ASN A ND2 1 
ATOM   414  N  N   . VAL A 1 54  ? 21.272 28.562 7.777   1.00 20.32 ? 50  VAL A N   1 
ATOM   415  C  CA  . VAL A 1 54  ? 19.947 27.950 7.881   1.00 17.61 ? 50  VAL A CA  1 
ATOM   416  C  C   . VAL A 1 54  ? 18.990 28.630 6.909   1.00 21.34 ? 50  VAL A C   1 
ATOM   417  O  O   . VAL A 1 54  ? 18.861 29.861 6.908   1.00 21.46 ? 50  VAL A O   1 
ATOM   418  C  CB  . VAL A 1 54  ? 19.411 28.016 9.320   1.00 23.79 ? 50  VAL A CB  1 
ATOM   419  C  CG1 . VAL A 1 54  ? 18.020 27.382 9.410   1.00 21.71 ? 50  VAL A CG1 1 
ATOM   420  C  CG2 . VAL A 1 54  ? 20.420 27.325 10.296  1.00 17.88 ? 50  VAL A CG2 1 
ATOM   421  N  N   . HIS A 1 55  ? 18.294 27.820 6.106   1.00 23.51 ? 51  HIS A N   1 
ATOM   422  C  CA  . HIS A 1 55  ? 17.382 28.290 5.066   1.00 23.03 ? 51  HIS A CA  1 
ATOM   423  C  C   . HIS A 1 55  ? 15.976 27.786 5.350   1.00 25.16 ? 51  HIS A C   1 
ATOM   424  O  O   . HIS A 1 55  ? 15.782 26.598 5.624   1.00 25.50 ? 51  HIS A O   1 
ATOM   425  C  CB  . HIS A 1 55  ? 17.812 27.793 3.675   1.00 25.71 ? 51  HIS A CB  1 
ATOM   426  C  CG  . HIS A 1 55  ? 19.202 28.194 3.280   1.00 25.35 ? 51  HIS A CG  1 
ATOM   427  N  ND1 . HIS A 1 55  ? 20.328 27.658 3.865   1.00 26.61 ? 51  HIS A ND1 1 
ATOM   428  C  CD2 . HIS A 1 55  ? 19.644 29.048 2.324   1.00 27.52 ? 51  HIS A CD2 1 
ATOM   429  C  CE1 . HIS A 1 55  ? 21.406 28.185 3.310   1.00 27.02 ? 51  HIS A CE1 1 
ATOM   430  N  NE2 . HIS A 1 55  ? 21.018 29.024 2.363   1.00 28.62 ? 51  HIS A NE2 1 
ATOM   431  N  N   . ARG A 1 56  ? 14.993 28.672 5.229   1.00 18.83 ? 52  ARG A N   1 
ATOM   432  C  CA  . ARG A 1 56  ? 13.600 28.341 5.495   1.00 22.35 ? 52  ARG A CA  1 
ATOM   433  C  C   . ARG A 1 56  ? 12.852 28.401 4.169   1.00 25.65 ? 52  ARG A C   1 
ATOM   434  O  O   . ARG A 1 56  ? 12.816 29.457 3.532   1.00 22.27 ? 52  ARG A O   1 
ATOM   435  C  CB  . ARG A 1 56  ? 13.030 29.326 6.518   1.00 29.83 ? 52  ARG A CB  1 
ATOM   436  C  CG  . ARG A 1 56  ? 11.543 29.199 6.849   1.00 25.16 ? 52  ARG A CG  1 
ATOM   437  C  CD  . ARG A 1 56  ? 11.091 30.400 7.677   1.00 30.31 ? 52  ARG A CD  1 
ATOM   438  N  NE  . ARG A 1 56  ? 11.123 31.633 6.891   1.00 23.36 ? 52  ARG A NE  1 
ATOM   439  C  CZ  . ARG A 1 56  ? 11.258 32.848 7.403   1.00 31.09 ? 52  ARG A CZ  1 
ATOM   440  N  NH1 . ARG A 1 56  ? 11.376 33.003 8.719   1.00 29.97 ? 52  ARG A NH1 1 
ATOM   441  N  NH2 . ARG A 1 56  ? 11.284 33.911 6.591   1.00 28.19 ? 52  ARG A NH2 1 
ATOM   442  N  N   . SER A 1 57  ? 12.300 27.272 3.728   1.00 25.85 ? 53  SER A N   1 
ATOM   443  C  CA  . SER A 1 57  ? 11.601 27.277 2.448   1.00 25.92 ? 53  SER A CA  1 
ATOM   444  C  C   . SER A 1 57  ? 10.402 28.202 2.539   1.00 27.46 ? 53  SER A C   1 
ATOM   445  O  O   . SER A 1 57  ? 9.709  28.236 3.556   1.00 23.21 ? 53  SER A O   1 
ATOM   446  C  CB  . SER A 1 57  ? 11.148 25.867 2.043   1.00 22.56 ? 53  SER A CB  1 
ATOM   447  O  OG  . SER A 1 57  ? 10.000 25.431 2.776   1.00 25.28 ? 53  SER A OG  1 
ATOM   448  N  N   . VAL A 1 58  ? 10.149 28.951 1.463   1.00 26.92 ? 54  VAL A N   1 
ATOM   449  C  CA  . VAL A 1 58  ? 9.066  29.927 1.533   1.00 22.84 ? 54  VAL A CA  1 
ATOM   450  C  C   . VAL A 1 58  ? 7.717  29.233 1.627   1.00 25.47 ? 54  VAL A C   1 
ATOM   451  O  O   . VAL A 1 58  ? 6.768  29.801 2.173   1.00 27.59 ? 54  VAL A O   1 
ATOM   452  C  CB  . VAL A 1 58  ? 9.127  30.907 0.345   1.00 23.02 ? 54  VAL A CB  1 
ATOM   453  C  CG1 . VAL A 1 58  ? 10.513 31.530 0.226   1.00 24.05 ? 54  VAL A CG1 1 
ATOM   454  C  CG2 . VAL A 1 58  ? 8.795  30.200 -0.945  1.00 25.89 ? 54  VAL A CG2 1 
ATOM   455  N  N   . ASP A 1 59  ? 7.608  27.996 1.141   1.00 23.14 ? 55  ASP A N   1 
ATOM   456  C  CA  . ASP A 1 59  ? 6.316  27.313 1.128   1.00 30.33 ? 55  ASP A CA  1 
ATOM   457  C  C   . ASP A 1 59  ? 6.002  26.616 2.442   1.00 28.24 ? 55  ASP A C   1 
ATOM   458  O  O   . ASP A 1 59  ? 4.925  26.016 2.562   1.00 24.75 ? 55  ASP A O   1 
ATOM   459  C  CB  . ASP A 1 59  ? 6.240  26.305 -0.032  1.00 28.65 ? 55  ASP A CB  1 
ATOM   460  C  CG  . ASP A 1 59  ? 7.173  25.119 0.147   1.00 29.93 ? 55  ASP A CG  1 
ATOM   461  O  OD1 . ASP A 1 59  ? 7.856  25.023 1.187   1.00 26.19 ? 55  ASP A OD1 1 
ATOM   462  O  OD2 . ASP A 1 59  ? 7.214  24.264 -0.759  1.00 26.98 ? 55  ASP A OD2 1 
ATOM   463  N  N   . GLY A 1 60  ? 6.906  26.689 3.420   1.00 25.35 ? 56  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 60  ? 6.685  26.133 4.734   1.00 27.68 ? 56  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 60  ? 7.002  24.659 4.897   1.00 25.58 ? 56  GLY A C   1 
ATOM   466  O  O   . GLY A 1 60  ? 6.805  24.125 5.997   1.00 28.47 ? 56  GLY A O   1 
ATOM   467  N  N   . TYR A 1 61  ? 7.485  23.976 3.863   1.00 23.59 ? 57  TYR A N   1 
ATOM   468  C  CA  . TYR A 1 61  ? 7.604  22.522 3.938   1.00 24.13 ? 57  TYR A CA  1 
ATOM   469  C  C   . TYR A 1 61  ? 9.026  22.010 4.142   1.00 29.35 ? 57  TYR A C   1 
ATOM   470  O  O   . TYR A 1 61  ? 9.214  20.789 4.178   1.00 30.56 ? 57  TYR A O   1 
ATOM   471  C  CB  . TYR A 1 61  ? 7.007  21.877 2.677   1.00 32.24 ? 57  TYR A CB  1 
ATOM   472  C  CG  . TYR A 1 61  ? 5.498  21.766 2.756   1.00 30.22 ? 57  TYR A CG  1 
ATOM   473  C  CD1 . TYR A 1 61  ? 4.900  20.695 3.403   1.00 32.24 ? 57  TYR A CD1 1 
ATOM   474  C  CD2 . TYR A 1 61  ? 4.679  22.761 2.239   1.00 30.01 ? 57  TYR A CD2 1 
ATOM   475  C  CE1 . TYR A 1 61  ? 3.531  20.595 3.505   1.00 32.91 ? 57  TYR A CE1 1 
ATOM   476  C  CE2 . TYR A 1 61  ? 3.283  22.676 2.340   1.00 29.58 ? 57  TYR A CE2 1 
ATOM   477  C  CZ  . TYR A 1 61  ? 2.724  21.576 2.969   1.00 36.04 ? 57  TYR A CZ  1 
ATOM   478  O  OH  . TYR A 1 61  ? 1.358  21.450 3.088   1.00 38.12 ? 57  TYR A OH  1 
ATOM   479  N  N   . GLN A 1 62  ? 10.029 22.881 4.287   1.00 29.61 ? 58  GLN A N   1 
ATOM   480  C  CA  . GLN A 1 62  ? 11.384 22.357 4.435   1.00 26.36 ? 58  GLN A CA  1 
ATOM   481  C  C   . GLN A 1 62  ? 12.297 23.387 5.107   1.00 26.86 ? 58  GLN A C   1 
ATOM   482  O  O   . GLN A 1 62  ? 12.086 24.598 4.991   1.00 23.85 ? 58  GLN A O   1 
ATOM   483  C  CB  . GLN A 1 62  ? 11.941 21.929 3.068   1.00 27.91 ? 58  GLN A CB  1 
ATOM   484  C  CG  . GLN A 1 62  ? 13.301 21.249 3.089   1.00 36.11 ? 58  GLN A CG  1 
ATOM   485  C  CD  . GLN A 1 62  ? 13.297 19.953 2.307   1.00 44.36 ? 58  GLN A CD  1 
ATOM   486  O  OE1 . GLN A 1 62  ? 12.382 19.693 1.526   1.00 54.25 ? 58  GLN A OE1 1 
ATOM   487  N  NE2 . GLN A 1 62  ? 14.303 19.119 2.533   1.00 45.36 ? 58  GLN A NE2 1 
ATOM   488  N  N   . VAL A 1 63  ? 13.296 22.879 5.835   1.00 21.65 ? 59  VAL A N   1 
ATOM   489  C  CA  . VAL A 1 63  ? 14.416 23.666 6.343   1.00 18.61 ? 59  VAL A CA  1 
ATOM   490  C  C   . VAL A 1 63  ? 15.686 22.988 5.867   1.00 19.54 ? 59  VAL A C   1 
ATOM   491  O  O   . VAL A 1 63  ? 15.800 21.758 5.930   1.00 26.73 ? 59  VAL A O   1 
ATOM   492  C  CB  . VAL A 1 63  ? 14.430 23.783 7.882   1.00 22.81 ? 59  VAL A CB  1 
ATOM   493  C  CG1 . VAL A 1 63  ? 15.576 24.706 8.328   1.00 15.78 ? 59  VAL A CG1 1 
ATOM   494  C  CG2 . VAL A 1 63  ? 13.087 24.276 8.422   1.00 23.50 ? 59  VAL A CG2 1 
ATOM   495  N  N   . VAL A 1 64  ? 16.625 23.777 5.371   1.00 23.48 ? 60  VAL A N   1 
ATOM   496  C  CA  . VAL A 1 64  ? 17.887 23.265 4.858   1.00 17.96 ? 60  VAL A CA  1 
ATOM   497  C  C   . VAL A 1 64  ? 19.014 23.967 5.602   1.00 24.96 ? 60  VAL A C   1 
ATOM   498  O  O   . VAL A 1 64  ? 19.060 25.204 5.667   1.00 22.45 ? 60  VAL A O   1 
ATOM   499  C  CB  . VAL A 1 64  ? 18.008 23.477 3.338   1.00 26.29 ? 60  VAL A CB  1 
ATOM   500  C  CG1 . VAL A 1 64  ? 19.376 23.046 2.857   1.00 21.09 ? 60  VAL A CG1 1 
ATOM   501  C  CG2 . VAL A 1 64  ? 16.913 22.708 2.610   1.00 21.23 ? 60  VAL A CG2 1 
ATOM   502  N  N   . ASP A 1 65  ? 19.919 23.182 6.152   1.00 25.93 ? 61  ASP A N   1 
ATOM   503  C  CA  . ASP A 1 65  ? 21.106 23.710 6.807   1.00 21.79 ? 61  ASP A CA  1 
ATOM   504  C  C   . ASP A 1 65  ? 22.312 23.377 5.940   1.00 23.43 ? 61  ASP A C   1 
ATOM   505  O  O   . ASP A 1 65  ? 22.648 22.204 5.751   1.00 28.85 ? 61  ASP A O   1 
ATOM   506  C  CB  . ASP A 1 65  ? 21.269 23.139 8.209   1.00 21.72 ? 61  ASP A CB  1 
ATOM   507  C  CG  . ASP A 1 65  ? 22.443 23.757 8.948   1.00 33.17 ? 61  ASP A CG  1 
ATOM   508  O  OD1 . ASP A 1 65  ? 22.955 24.811 8.498   1.00 32.69 ? 61  ASP A OD1 1 
ATOM   509  O  OD2 . ASP A 1 65  ? 22.861 23.185 9.967   1.00 34.68 ? 61  ASP A OD2 1 
ATOM   510  N  N   . TYR A 1 66  ? 22.939 24.413 5.407   1.00 23.28 ? 62  TYR A N   1 
ATOM   511  C  CA  . TYR A 1 66  ? 24.174 24.312 4.650   1.00 21.21 ? 62  TYR A CA  1 
ATOM   512  C  C   . TYR A 1 66  ? 25.292 24.648 5.628   1.00 26.76 ? 62  TYR A C   1 
ATOM   513  O  O   . TYR A 1 66  ? 25.424 25.799 6.054   1.00 26.39 ? 62  TYR A O   1 
ATOM   514  C  CB  . TYR A 1 66  ? 24.129 25.280 3.476   1.00 23.53 ? 62  TYR A CB  1 
ATOM   515  C  CG  . TYR A 1 66  ? 25.200 25.134 2.431   1.00 28.32 ? 62  TYR A CG  1 
ATOM   516  C  CD1 . TYR A 1 66  ? 24.927 24.547 1.209   1.00 27.79 ? 62  TYR A CD1 1 
ATOM   517  C  CD2 . TYR A 1 66  ? 26.467 25.635 2.644   1.00 28.24 ? 62  TYR A CD2 1 
ATOM   518  C  CE1 . TYR A 1 66  ? 25.891 24.439 0.245   1.00 28.73 ? 62  TYR A CE1 1 
ATOM   519  C  CE2 . TYR A 1 66  ? 27.442 25.532 1.688   1.00 30.04 ? 62  TYR A CE2 1 
ATOM   520  C  CZ  . TYR A 1 66  ? 27.150 24.935 0.486   1.00 30.84 ? 62  TYR A CZ  1 
ATOM   521  O  OH  . TYR A 1 66  ? 28.128 24.839 -0.470  1.00 30.03 ? 62  TYR A OH  1 
ATOM   522  N  N   . THR A 1 67  ? 26.054 23.645 6.040   1.00 28.13 ? 63  THR A N   1 
ATOM   523  C  CA  . THR A 1 67  ? 27.074 23.869 7.053   1.00 20.79 ? 63  THR A CA  1 
ATOM   524  C  C   . THR A 1 67  ? 28.424 23.347 6.578   1.00 27.51 ? 63  THR A C   1 
ATOM   525  O  O   . THR A 1 67  ? 28.504 22.309 5.902   1.00 27.18 ? 63  THR A O   1 
ATOM   526  C  CB  . THR A 1 67  ? 26.643 23.228 8.392   1.00 28.92 ? 63  THR A CB  1 
ATOM   527  O  OG1 . THR A 1 67  ? 27.713 23.295 9.328   1.00 37.80 ? 63  THR A OG1 1 
ATOM   528  C  CG2 . THR A 1 67  ? 26.185 21.780 8.205   1.00 29.96 ? 63  THR A CG2 1 
ATOM   529  N  N   . GLN A 1 68  ? 29.485 24.101 6.893   1.00 25.23 ? 64  GLN A N   1 
ATOM   530  C  CA  . GLN A 1 68  ? 30.841 23.806 6.443   1.00 24.74 ? 64  GLN A CA  1 
ATOM   531  C  C   . GLN A 1 68  ? 31.737 23.454 7.628   1.00 29.10 ? 64  GLN A C   1 
ATOM   532  O  O   . GLN A 1 68  ? 31.606 24.031 8.715   1.00 24.71 ? 64  GLN A O   1 
ATOM   533  C  CB  . GLN A 1 68  ? 31.454 24.992 5.691   1.00 26.94 ? 64  GLN A CB  1 
ATOM   534  C  CG  . GLN A 1 68  ? 30.765 25.347 4.369   1.00 24.33 ? 64  GLN A CG  1 
ATOM   535  C  CD  . GLN A 1 68  ? 31.266 26.664 3.800   1.00 29.01 ? 64  GLN A CD  1 
ATOM   536  O  OE1 . GLN A 1 68  ? 31.518 27.626 4.534   1.00 26.23 ? 64  GLN A OE1 1 
ATOM   537  N  NE2 . GLN A 1 68  ? 31.434 26.706 2.487   1.00 24.57 ? 64  GLN A NE2 1 
ATOM   538  N  N   . TRP A 1 69  ? 32.661 22.519 7.404   1.00 29.32 ? 65  TRP A N   1 
ATOM   539  C  CA  . TRP A 1 69  ? 33.487 21.957 8.466   1.00 25.75 ? 65  TRP A CA  1 
ATOM   540  C  C   . TRP A 1 69  ? 34.913 21.778 7.962   1.00 28.58 ? 65  TRP A C   1 
ATOM   541  O  O   . TRP A 1 69  ? 35.150 21.663 6.759   1.00 28.09 ? 65  TRP A O   1 
ATOM   542  C  CB  . TRP A 1 69  ? 32.900 20.614 8.957   1.00 25.10 ? 65  TRP A CB  1 
ATOM   543  C  CG  . TRP A 1 69  ? 31.589 20.831 9.656   1.00 27.33 ? 65  TRP A CG  1 
ATOM   544  C  CD1 . TRP A 1 69  ? 30.375 21.009 9.072   1.00 27.74 ? 65  TRP A CD1 1 
ATOM   545  C  CD2 . TRP A 1 69  ? 31.378 20.949 11.070  1.00 21.82 ? 65  TRP A CD2 1 
ATOM   546  N  NE1 . TRP A 1 69  ? 29.415 21.226 10.036  1.00 27.71 ? 65  TRP A NE1 1 
ATOM   547  C  CE2 . TRP A 1 69  ? 30.008 21.189 11.270  1.00 27.88 ? 65  TRP A CE2 1 
ATOM   548  C  CE3 . TRP A 1 69  ? 32.218 20.866 12.186  1.00 20.96 ? 65  TRP A CE3 1 
ATOM   549  C  CZ2 . TRP A 1 69  ? 29.454 21.364 12.549  1.00 22.18 ? 65  TRP A CZ2 1 
ATOM   550  C  CZ3 . TRP A 1 69  ? 31.678 21.045 13.437  1.00 26.97 ? 65  TRP A CZ3 1 
ATOM   551  C  CH2 . TRP A 1 69  ? 30.302 21.278 13.613  1.00 27.29 ? 65  TRP A CH2 1 
ATOM   552  N  N   . ARG A 1 70  ? 35.864 21.782 8.898   1.00 21.60 ? 66  ARG A N   1 
ATOM   553  C  CA  . ARG A 1 70  ? 37.246 21.426 8.577   1.00 27.12 ? 66  ARG A CA  1 
ATOM   554  C  C   . ARG A 1 70  ? 37.335 20.056 7.918   1.00 30.17 ? 66  ARG A C   1 
ATOM   555  O  O   . ARG A 1 70  ? 37.906 19.907 6.828   1.00 26.32 ? 66  ARG A O   1 
ATOM   556  C  CB  . ARG A 1 70  ? 38.080 21.459 9.856   1.00 31.57 ? 66  ARG A CB  1 
ATOM   557  C  CG  . ARG A 1 70  ? 39.478 20.917 9.730   1.00 50.05 ? 66  ARG A CG  1 
ATOM   558  C  CD  . ARG A 1 70  ? 40.187 20.933 11.092  1.00 48.46 ? 66  ARG A CD  1 
ATOM   559  N  NE  . ARG A 1 70  ? 39.504 20.109 12.094  1.00 32.89 ? 66  ARG A NE  1 
ATOM   560  C  CZ  . ARG A 1 70  ? 39.678 20.246 13.405  1.00 52.37 ? 66  ARG A CZ  1 
ATOM   561  N  NH1 . ARG A 1 70  ? 40.511 21.174 13.872  1.00 49.44 ? 66  ARG A NH1 1 
ATOM   562  N  NH2 . ARG A 1 70  ? 39.029 19.453 14.251  1.00 38.95 ? 66  ARG A NH2 1 
ATOM   563  N  N   . ARG A 1 71  ? 36.783 19.042 8.574   1.00 29.01 ? 67  ARG A N   1 
ATOM   564  C  CA  . ARG A 1 71  ? 36.690 17.694 8.032   1.00 28.18 ? 67  ARG A CA  1 
ATOM   565  C  C   . ARG A 1 71  ? 35.305 17.144 8.321   1.00 32.30 ? 67  ARG A C   1 
ATOM   566  O  O   . ARG A 1 71  ? 34.680 17.510 9.320   1.00 24.25 ? 67  ARG A O   1 
ATOM   567  C  CB  . ARG A 1 71  ? 37.726 16.740 8.648   1.00 28.92 ? 67  ARG A CB  1 
ATOM   568  C  CG  . ARG A 1 71  ? 39.163 17.191 8.533   1.00 39.94 ? 67  ARG A CG  1 
ATOM   569  C  CD  . ARG A 1 71  ? 40.050 16.325 9.436   1.00 45.55 ? 67  ARG A CD  1 
ATOM   570  N  NE  . ARG A 1 71  ? 39.558 16.345 10.810  1.00 49.88 ? 67  ARG A NE  1 
ATOM   571  C  CZ  . ARG A 1 71  ? 39.490 15.281 11.607  1.00 52.37 ? 67  ARG A CZ  1 
ATOM   572  N  NH1 . ARG A 1 71  ? 39.901 14.092 11.173  1.00 44.75 ? 67  ARG A NH1 1 
ATOM   573  N  NH2 . ARG A 1 71  ? 39.007 15.405 12.842  1.00 45.05 ? 67  ARG A NH2 1 
ATOM   574  N  N   . ARG A 1 72  ? 34.834 16.253 7.439   1.00 29.68 ? 68  ARG A N   1 
ATOM   575  C  CA  . ARG A 1 72  ? 33.586 15.534 7.688   1.00 25.90 ? 68  ARG A CA  1 
ATOM   576  C  C   . ARG A 1 72  ? 33.560 14.937 9.089   1.00 23.91 ? 68  ARG A C   1 
ATOM   577  O  O   . ARG A 1 72  ? 32.523 14.959 9.763   1.00 27.63 ? 68  ARG A O   1 
ATOM   578  C  CB  . ARG A 1 72  ? 33.395 14.435 6.633   1.00 29.68 ? 68  ARG A CB  1 
ATOM   579  C  CG  . ARG A 1 72  ? 32.969 14.961 5.244   1.00 35.29 ? 68  ARG A CG  1 
ATOM   580  C  CD  . ARG A 1 72  ? 33.128 13.881 4.157   1.00 36.43 ? 68  ARG A CD  1 
ATOM   581  N  NE  . ARG A 1 72  ? 32.192 12.765 4.329   1.00 35.02 ? 68  ARG A NE  1 
ATOM   582  C  CZ  . ARG A 1 72  ? 32.255 11.628 3.643   1.00 34.10 ? 68  ARG A CZ  1 
ATOM   583  N  NH1 . ARG A 1 72  ? 33.217 11.452 2.743   1.00 28.59 ? 68  ARG A NH1 1 
ATOM   584  N  NH2 . ARG A 1 72  ? 31.356 10.669 3.855   1.00 25.54 ? 68  ARG A NH2 1 
ATOM   585  N  N   . GLU A 1 73  ? 34.704 14.425 9.551   1.00 22.29 ? 69  GLU A N   1 
ATOM   586  C  CA  . GLU A 1 73  ? 34.790 13.812 10.873  1.00 30.23 ? 69  GLU A CA  1 
ATOM   587  C  C   . GLU A 1 73  ? 34.374 14.766 11.992  1.00 31.52 ? 69  GLU A C   1 
ATOM   588  O  O   . GLU A 1 73  ? 33.874 14.315 13.032  1.00 27.35 ? 69  GLU A O   1 
ATOM   589  C  CB  . GLU A 1 73  ? 36.216 13.324 11.124  1.00 27.75 ? 69  GLU A CB  1 
ATOM   590  C  CG  . GLU A 1 73  ? 36.632 12.105 10.316  1.00 33.51 ? 69  GLU A CG  1 
ATOM   591  C  CD  . GLU A 1 73  ? 36.853 12.396 8.834   1.00 41.85 ? 69  GLU A CD  1 
ATOM   592  O  OE1 . GLU A 1 73  ? 37.176 13.548 8.480   1.00 36.33 ? 69  GLU A OE1 1 
ATOM   593  O  OE2 . GLU A 1 73  ? 36.718 11.459 8.020   1.00 43.59 ? 69  GLU A OE2 1 
ATOM   594  N  N   . ASP A 1 74  ? 34.603 16.074 11.819  1.00 31.17 ? 70  ASP A N   1 
ATOM   595  C  CA  . ASP A 1 74  ? 34.273 17.028 12.877  1.00 24.51 ? 70  ASP A CA  1 
ATOM   596  C  C   . ASP A 1 74  ? 32.767 17.128 13.078  1.00 22.78 ? 70  ASP A C   1 
ATOM   597  O  O   . ASP A 1 74  ? 32.290 17.221 14.214  1.00 24.24 ? 70  ASP A O   1 
ATOM   598  C  CB  . ASP A 1 74  ? 34.850 18.401 12.550  1.00 26.51 ? 70  ASP A CB  1 
ATOM   599  C  CG  . ASP A 1 74  ? 36.359 18.395 12.437  1.00 34.41 ? 70  ASP A CG  1 
ATOM   600  O  OD1 . ASP A 1 74  ? 37.009 17.632 13.171  1.00 33.20 ? 70  ASP A OD1 1 
ATOM   601  O  OD2 . ASP A 1 74  ? 36.901 19.181 11.632  1.00 35.98 ? 70  ASP A OD2 1 
ATOM   602  N  N   . PHE A 1 75  ? 32.005 17.145 11.983  1.00 23.61 ? 71  PHE A N   1 
ATOM   603  C  CA  . PHE A 1 75  ? 30.551 17.138 12.084  1.00 24.27 ? 71  PHE A CA  1 
ATOM   604  C  C   . PHE A 1 75  ? 30.066 15.842 12.711  1.00 28.69 ? 71  PHE A C   1 
ATOM   605  O  O   . PHE A 1 75  ? 29.200 15.843 13.597  1.00 22.13 ? 71  PHE A O   1 
ATOM   606  C  CB  . PHE A 1 75  ? 29.936 17.326 10.700  1.00 22.91 ? 71  PHE A CB  1 
ATOM   607  C  CG  . PHE A 1 75  ? 28.442 17.183 10.672  1.00 26.43 ? 71  PHE A CG  1 
ATOM   608  C  CD1 . PHE A 1 75  ? 27.622 18.296 10.807  1.00 24.43 ? 71  PHE A CD1 1 
ATOM   609  C  CD2 . PHE A 1 75  ? 27.848 15.940 10.476  1.00 29.82 ? 71  PHE A CD2 1 
ATOM   610  C  CE1 . PHE A 1 75  ? 26.238 18.165 10.768  1.00 27.91 ? 71  PHE A CE1 1 
ATOM   611  C  CE2 . PHE A 1 75  ? 26.467 15.808 10.441  1.00 28.09 ? 71  PHE A CE2 1 
ATOM   612  C  CZ  . PHE A 1 75  ? 25.665 16.925 10.582  1.00 23.53 ? 71  PHE A CZ  1 
ATOM   613  N  N   . GLU A 1 76  ? 30.618 14.716 12.252  1.00 25.97 ? 72  GLU A N   1 
ATOM   614  C  CA  . GLU A 1 76  ? 30.178 13.414 12.741  1.00 27.04 ? 72  GLU A CA  1 
ATOM   615  C  C   . GLU A 1 76  ? 30.431 13.274 14.230  1.00 23.62 ? 72  GLU A C   1 
ATOM   616  O  O   . GLU A 1 76  ? 29.617 12.690 14.957  1.00 29.07 ? 72  GLU A O   1 
ATOM   617  C  CB  . GLU A 1 76  ? 30.894 12.304 11.957  1.00 22.21 ? 72  GLU A CB  1 
ATOM   618  C  CG  . GLU A 1 76  ? 30.403 12.257 10.517  1.00 23.45 ? 72  GLU A CG  1 
ATOM   619  C  CD  . GLU A 1 76  ? 31.203 11.332 9.619   1.00 23.31 ? 72  GLU A CD  1 
ATOM   620  O  OE1 . GLU A 1 76  ? 32.393 11.084 9.905   1.00 26.11 ? 72  GLU A OE1 1 
ATOM   621  O  OE2 . GLU A 1 76  ? 30.607 10.851 8.633   1.00 27.36 ? 72  GLU A OE2 1 
ATOM   622  N  N   . ALA A 1 77  ? 31.572 13.785 14.690  1.00 21.66 ? 73  ALA A N   1 
ATOM   623  C  CA  . ALA A 1 77  ? 31.886 13.769 16.116  1.00 26.30 ? 73  ALA A CA  1 
ATOM   624  C  C   . ALA A 1 77  ? 30.831 14.511 16.925  1.00 25.54 ? 73  ALA A C   1 
ATOM   625  O  O   . ALA A 1 77  ? 30.452 14.067 18.011  1.00 26.54 ? 73  ALA A O   1 
ATOM   626  C  CB  . ALA A 1 77  ? 33.254 14.396 16.349  1.00 24.10 ? 73  ALA A CB  1 
ATOM   627  N  N   . MET A 1 78  ? 30.365 15.658 16.424  1.00 24.18 ? 74  MET A N   1 
ATOM   628  C  CA  . MET A 1 78  ? 29.319 16.394 17.130  1.00 26.01 ? 74  MET A CA  1 
ATOM   629  C  C   . MET A 1 78  ? 28.034 15.577 17.211  1.00 25.74 ? 74  MET A C   1 
ATOM   630  O  O   . MET A 1 78  ? 27.392 15.523 18.260  1.00 24.67 ? 74  MET A O   1 
ATOM   631  C  CB  . MET A 1 78  ? 29.051 17.732 16.434  1.00 25.15 ? 74  MET A CB  1 
ATOM   632  C  CG  . MET A 1 78  ? 27.773 18.429 16.929  1.00 27.35 ? 74  MET A CG  1 
ATOM   633  S  SD  . MET A 1 78  ? 27.382 19.857 15.914  1.00 26.79 ? 74  MET A SD  1 
ATOM   634  C  CE  . MET A 1 78  ? 27.007 19.038 14.369  1.00 23.02 ? 74  MET A CE  1 
ATOM   635  N  N   . VAL A 1 79  ? 27.641 14.934 16.107  1.00 24.37 ? 75  VAL A N   1 
ATOM   636  C  CA  . VAL A 1 79  ? 26.418 14.136 16.105  1.00 24.64 ? 75  VAL A CA  1 
ATOM   637  C  C   . VAL A 1 79  ? 26.512 12.979 17.106  1.00 25.74 ? 75  VAL A C   1 
ATOM   638  O  O   . VAL A 1 79  ? 25.523 12.626 17.757  1.00 26.72 ? 75  VAL A O   1 
ATOM   639  C  CB  . VAL A 1 79  ? 26.118 13.641 14.673  1.00 29.01 ? 75  VAL A CB  1 
ATOM   640  C  CG1 . VAL A 1 79  ? 25.029 12.589 14.681  1.00 33.27 ? 75  VAL A CG1 1 
ATOM   641  C  CG2 . VAL A 1 79  ? 25.708 14.833 13.773  1.00 24.93 ? 75  VAL A CG2 1 
ATOM   642  N  N   . ARG A 1 80  ? 27.694 12.366 17.232  1.00 24.79 ? 76  ARG A N   1 
ATOM   643  C  CA  . ARG A 1 80  ? 27.913 11.243 18.141  1.00 30.29 ? 76  ARG A CA  1 
ATOM   644  C  C   . ARG A 1 80  ? 28.054 11.650 19.604  1.00 27.88 ? 76  ARG A C   1 
ATOM   645  O  O   . ARG A 1 80  ? 28.003 10.777 20.474  1.00 32.06 ? 76  ARG A O   1 
ATOM   646  C  CB  . ARG A 1 80  ? 29.179 10.472 17.748  1.00 26.25 ? 76  ARG A CB  1 
ATOM   647  C  CG  . ARG A 1 80  ? 29.093 9.746  16.408  1.00 30.45 ? 76  ARG A CG  1 
ATOM   648  C  CD  . ARG A 1 80  ? 30.231 8.730  16.304  1.00 32.70 ? 76  ARG A CD  1 
ATOM   649  N  NE  . ARG A 1 80  ? 31.539 9.344  16.508  1.00 31.26 ? 76  ARG A NE  1 
ATOM   650  C  CZ  . ARG A 1 80  ? 32.309 9.788  15.520  1.00 33.55 ? 76  ARG A CZ  1 
ATOM   651  N  NH1 . ARG A 1 80  ? 33.492 10.333 15.781  1.00 30.48 ? 76  ARG A NH1 1 
ATOM   652  N  NH2 . ARG A 1 80  ? 31.896 9.679  14.263  1.00 29.60 ? 76  ARG A NH2 1 
ATOM   653  N  N   . ASP A 1 81  ? 28.290 12.924 19.886  1.00 26.08 ? 77  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 81  ? 28.540 13.384 21.244  1.00 28.40 ? 77  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 81  ? 27.244 13.395 22.047  1.00 30.97 ? 77  ASP A C   1 
ATOM   656  O  O   . ASP A 1 81  ? 26.292 14.066 21.643  1.00 33.70 ? 77  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 81  ? 29.126 14.790 21.207  1.00 30.88 ? 77  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 81  ? 29.758 15.189 22.518  1.00 29.20 ? 77  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 81  ? 29.238 14.827 23.590  1.00 27.98 ? 77  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 81  ? 30.792 15.848 22.469  1.00 31.53 ? 77  ASP A OD2 1 
ATOM   661  N  N   . PRO A 1 82  ? 27.169 12.706 23.195  1.00 32.88 ? 78  PRO A N   1 
ATOM   662  C  CA  . PRO A 1 82  ? 25.937 12.787 24.001  1.00 27.71 ? 78  PRO A CA  1 
ATOM   663  C  C   . PRO A 1 82  ? 25.621 14.201 24.479  1.00 25.64 ? 78  PRO A C   1 
ATOM   664  O  O   . PRO A 1 82  ? 24.450 14.506 24.731  1.00 31.41 ? 78  PRO A O   1 
ATOM   665  C  CB  . PRO A 1 82  ? 26.211 11.830 25.177  1.00 33.29 ? 78  PRO A CB  1 
ATOM   666  C  CG  . PRO A 1 82  ? 27.677 11.770 25.293  1.00 27.69 ? 78  PRO A CG  1 
ATOM   667  C  CD  . PRO A 1 82  ? 28.209 11.900 23.864  1.00 28.84 ? 78  PRO A CD  1 
ATOM   668  N  N   . ALA A 1 83  ? 26.616 15.084 24.561  1.00 25.20 ? 79  ALA A N   1 
ATOM   669  C  CA  . ALA A 1 83  ? 26.367 16.471 24.927  1.00 31.79 ? 79  ALA A CA  1 
ATOM   670  C  C   . ALA A 1 83  ? 25.505 17.211 23.907  1.00 34.53 ? 79  ALA A C   1 
ATOM   671  O  O   . ALA A 1 83  ? 24.966 18.271 24.230  1.00 30.44 ? 79  ALA A O   1 
ATOM   672  C  CB  . ALA A 1 83  ? 27.692 17.207 25.110  1.00 30.15 ? 79  ALA A CB  1 
ATOM   673  N  N   . SER A 1 84  ? 25.356 16.691 22.689  1.00 33.51 ? 80  SER A N   1 
ATOM   674  C  CA  . SER A 1 84  ? 24.486 17.342 21.714  1.00 31.49 ? 80  SER A CA  1 
ATOM   675  C  C   . SER A 1 84  ? 23.019 16.993 21.874  1.00 32.05 ? 80  SER A C   1 
ATOM   676  O  O   . SER A 1 84  ? 22.175 17.660 21.265  1.00 31.07 ? 80  SER A O   1 
ATOM   677  C  CB  . SER A 1 84  ? 24.908 16.986 20.289  1.00 26.16 ? 80  SER A CB  1 
ATOM   678  O  OG  . SER A 1 84  ? 26.309 17.079 20.138  1.00 24.97 ? 80  SER A OG  1 
ATOM   679  N  N   . ALA A 1 85  ? 22.698 15.961 22.647  1.00 25.69 ? 81  ALA A N   1 
ATOM   680  C  CA  . ALA A 1 85  ? 21.330 15.457 22.671  1.00 30.63 ? 81  ALA A CA  1 
ATOM   681  C  C   . ALA A 1 85  ? 20.302 16.469 23.166  1.00 30.32 ? 81  ALA A C   1 
ATOM   682  O  O   . ALA A 1 85  ? 19.193 16.493 22.604  1.00 35.81 ? 81  ALA A O   1 
ATOM   683  C  CB  . ALA A 1 85  ? 21.262 14.172 23.508  1.00 37.75 ? 81  ALA A CB  1 
ATOM   684  N  N   . PRO A 1 86  ? 20.557 17.283 24.198  1.00 35.18 ? 82  PRO A N   1 
ATOM   685  C  CA  . PRO A 1 86  ? 19.536 18.274 24.584  1.00 36.05 ? 82  PRO A CA  1 
ATOM   686  C  C   . PRO A 1 86  ? 19.175 19.225 23.458  1.00 37.01 ? 82  PRO A C   1 
ATOM   687  O  O   . PRO A 1 86  ? 18.017 19.643 23.360  1.00 37.95 ? 82  PRO A O   1 
ATOM   688  C  CB  . PRO A 1 86  ? 20.185 19.019 25.758  1.00 32.87 ? 82  PRO A CB  1 
ATOM   689  C  CG  . PRO A 1 86  ? 21.145 18.022 26.340  1.00 39.57 ? 82  PRO A CG  1 
ATOM   690  C  CD  . PRO A 1 86  ? 21.666 17.234 25.172  1.00 38.26 ? 82  PRO A CD  1 
ATOM   691  N  N   . HIS A 1 87  ? 20.127 19.572 22.597  1.00 33.54 ? 83  HIS A N   1 
ATOM   692  C  CA  . HIS A 1 87  ? 19.820 20.474 21.495  1.00 31.37 ? 83  HIS A CA  1 
ATOM   693  C  C   . HIS A 1 87  ? 19.182 19.747 20.324  1.00 36.77 ? 83  HIS A C   1 
ATOM   694  O  O   . HIS A 1 87  ? 18.310 20.309 19.649  1.00 40.34 ? 83  HIS A O   1 
ATOM   695  C  CB  . HIS A 1 87  ? 21.087 21.166 21.010  1.00 28.22 ? 83  HIS A CB  1 
ATOM   696  C  CG  . HIS A 1 87  ? 21.784 21.977 22.057  1.00 36.80 ? 83  HIS A CG  1 
ATOM   697  N  ND1 . HIS A 1 87  ? 22.763 21.452 22.874  1.00 44.88 ? 83  HIS A ND1 1 
ATOM   698  C  CD2 . HIS A 1 87  ? 21.667 23.282 22.398  1.00 37.59 ? 83  HIS A CD2 1 
ATOM   699  C  CE1 . HIS A 1 87  ? 23.215 22.399 23.676  1.00 40.99 ? 83  HIS A CE1 1 
ATOM   700  N  NE2 . HIS A 1 87  ? 22.572 23.520 23.402  1.00 36.81 ? 83  HIS A NE2 1 
ATOM   701  N  N   . PHE A 1 88  ? 19.600 18.508 20.068  1.00 30.57 ? 84  PHE A N   1 
ATOM   702  C  CA  . PHE A 1 88  ? 19.183 17.810 18.864  1.00 29.09 ? 84  PHE A CA  1 
ATOM   703  C  C   . PHE A 1 88  ? 17.908 16.996 19.052  1.00 38.49 ? 84  PHE A C   1 
ATOM   704  O  O   . PHE A 1 88  ? 17.147 16.850 18.090  1.00 29.92 ? 84  PHE A O   1 
ATOM   705  C  CB  . PHE A 1 88  ? 20.310 16.908 18.361  1.00 31.75 ? 84  PHE A CB  1 
ATOM   706  C  CG  . PHE A 1 88  ? 21.505 17.659 17.819  1.00 30.02 ? 84  PHE A CG  1 
ATOM   707  C  CD1 . PHE A 1 88  ? 22.638 16.969 17.401  1.00 27.56 ? 84  PHE A CD1 1 
ATOM   708  C  CD2 . PHE A 1 88  ? 21.493 19.040 17.722  1.00 24.75 ? 84  PHE A CD2 1 
ATOM   709  C  CE1 . PHE A 1 88  ? 23.742 17.648 16.892  1.00 27.23 ? 84  PHE A CE1 1 
ATOM   710  C  CE2 . PHE A 1 88  ? 22.589 19.735 17.236  1.00 32.05 ? 84  PHE A CE2 1 
ATOM   711  C  CZ  . PHE A 1 88  ? 23.723 19.039 16.815  1.00 29.02 ? 84  PHE A CZ  1 
ATOM   712  N  N   . MET A 1 89  ? 17.649 16.476 20.264  1.00 35.73 ? 85  MET A N   1 
ATOM   713  C  CA  . MET A 1 89  ? 16.420 15.716 20.510  1.00 41.14 ? 85  MET A CA  1 
ATOM   714  C  C   . MET A 1 89  ? 15.143 16.484 20.188  1.00 30.18 ? 85  MET A C   1 
ATOM   715  O  O   . MET A 1 89  ? 14.249 15.897 19.558  1.00 36.39 ? 85  MET A O   1 
ATOM   716  C  CB  . MET A 1 89  ? 16.370 15.234 21.967  1.00 43.46 ? 85  MET A CB  1 
ATOM   717  C  CG  . MET A 1 89  ? 17.124 13.967 22.258  1.00 51.68 ? 85  MET A CG  1 
ATOM   718  S  SD  . MET A 1 89  ? 16.954 13.530 24.004  1.00 70.71 ? 85  MET A SD  1 
ATOM   719  C  CE  . MET A 1 89  ? 15.188 13.745 24.216  1.00 45.72 ? 85  MET A CE  1 
ATOM   720  N  N   . PRO A 1 90  ? 14.959 17.740 20.614  1.00 33.34 ? 86  PRO A N   1 
ATOM   721  C  CA  . PRO A 1 90  ? 13.735 18.461 20.222  1.00 35.01 ? 86  PRO A CA  1 
ATOM   722  C  C   . PRO A 1 90  ? 13.581 18.622 18.720  1.00 42.04 ? 86  PRO A C   1 
ATOM   723  O  O   . PRO A 1 90  ? 12.451 18.729 18.227  1.00 45.26 ? 86  PRO A O   1 
ATOM   724  C  CB  . PRO A 1 90  ? 13.895 19.825 20.903  1.00 35.61 ? 86  PRO A CB  1 
ATOM   725  C  CG  . PRO A 1 90  ? 14.917 19.628 21.957  1.00 43.72 ? 86  PRO A CG  1 
ATOM   726  C  CD  . PRO A 1 90  ? 15.834 18.583 21.445  1.00 35.75 ? 86  PRO A CD  1 
ATOM   727  N  N   . ILE A 1 91  ? 14.685 18.659 17.975  1.00 33.66 ? 87  ILE A N   1 
ATOM   728  C  CA  . ILE A 1 91  ? 14.598 18.765 16.524  1.00 36.93 ? 87  ILE A CA  1 
ATOM   729  C  C   . ILE A 1 91  ? 14.058 17.468 15.940  1.00 40.21 ? 87  ILE A C   1 
ATOM   730  O  O   . ILE A 1 91  ? 13.130 17.467 15.118  1.00 34.39 ? 87  ILE A O   1 
ATOM   731  C  CB  . ILE A 1 91  ? 15.977 19.127 15.939  1.00 34.65 ? 87  ILE A CB  1 
ATOM   732  C  CG1 . ILE A 1 91  ? 16.327 20.566 16.304  1.00 27.61 ? 87  ILE A CG1 1 
ATOM   733  C  CG2 . ILE A 1 91  ? 15.977 18.930 14.435  1.00 35.55 ? 87  ILE A CG2 1 
ATOM   734  C  CD1 . ILE A 1 91  ? 17.790 20.920 16.122  1.00 32.60 ? 87  ILE A CD1 1 
ATOM   735  N  N   . GLY A 1 92  ? 14.613 16.336 16.381  1.00 37.69 ? 88  GLY A N   1 
ATOM   736  C  CA  . GLY A 1 92  ? 14.116 15.043 15.947  1.00 34.91 ? 88  GLY A CA  1 
ATOM   737  C  C   . GLY A 1 92  ? 12.657 14.806 16.269  1.00 34.55 ? 88  GLY A C   1 
ATOM   738  O  O   . GLY A 1 92  ? 12.013 13.981 15.612  1.00 43.11 ? 88  GLY A O   1 
ATOM   739  N  N   . GLU A 1 93  ? 12.111 15.519 17.254  1.00 39.72 ? 89  GLU A N   1 
ATOM   740  C  CA  . GLU A 1 93  ? 10.686 15.407 17.538  1.00 42.48 ? 89  GLU A CA  1 
ATOM   741  C  C   . GLU A 1 93  ? 9.831  16.023 16.444  1.00 47.65 ? 89  GLU A C   1 
ATOM   742  O  O   . GLU A 1 93  ? 8.650  15.683 16.331  1.00 48.74 ? 89  GLU A O   1 
ATOM   743  C  CB  . GLU A 1 93  ? 10.356 16.068 18.872  1.00 39.79 ? 89  GLU A CB  1 
ATOM   744  C  CG  . GLU A 1 93  ? 10.703 15.187 20.064  1.00 50.00 ? 89  GLU A CG  1 
ATOM   745  C  CD  . GLU A 1 93  ? 10.051 15.655 21.345  1.00 69.80 ? 89  GLU A CD  1 
ATOM   746  O  OE1 . GLU A 1 93  ? 10.190 16.857 21.684  1.00 63.18 ? 89  GLU A OE1 1 
ATOM   747  O  OE2 . GLU A 1 93  ? 9.391  14.816 22.003  1.00 78.46 ? 89  GLU A OE2 1 
ATOM   748  N  N   . LEU A 1 94  ? 10.394 16.921 15.643  1.00 41.86 ? 90  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 94  ? 9.642  17.591 14.593  1.00 41.90 ? 90  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 94  ? 9.921  17.037 13.217  1.00 38.81 ? 90  LEU A C   1 
ATOM   751  O  O   . LEU A 1 94  ? 9.064  17.138 12.336  1.00 47.63 ? 90  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 94  ? 9.958  19.088 14.581  1.00 37.92 ? 90  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 94  ? 9.467  19.854 15.798  1.00 33.27 ? 90  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 94  ? 9.832  21.301 15.652  1.00 33.28 ? 90  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 94  ? 7.977  19.680 15.971  1.00 34.97 ? 90  LEU A CD2 1 
ATOM   756  N  N   . THR A 1 95  ? 11.091 16.445 13.010  1.00 38.41 ? 91  THR A N   1 
ATOM   757  C  CA  . THR A 1 95  ? 11.520 16.122 11.666  1.00 35.40 ? 91  THR A CA  1 
ATOM   758  C  C   . THR A 1 95  ? 12.457 14.923 11.699  1.00 41.42 ? 91  THR A C   1 
ATOM   759  O  O   . THR A 1 95  ? 13.208 14.721 12.659  1.00 40.68 ? 91  THR A O   1 
ATOM   760  C  CB  . THR A 1 95  ? 12.221 17.329 11.035  1.00 36.92 ? 91  THR A CB  1 
ATOM   761  O  OG1 . THR A 1 95  ? 12.655 17.009 9.714   1.00 29.78 ? 91  THR A OG1 1 
ATOM   762  C  CG2 . THR A 1 95  ? 13.433 17.732 11.874  1.00 35.39 ? 91  THR A CG2 1 
ATOM   763  N  N   . GLN A 1 96  ? 12.405 14.133 10.635  1.00 40.07 ? 92  GLN A N   1 
ATOM   764  C  CA  . GLN A 1 96  ? 13.399 13.096 10.374  1.00 51.17 ? 92  GLN A CA  1 
ATOM   765  C  C   . GLN A 1 96  ? 14.386 13.697 9.378   1.00 38.53 ? 92  GLN A C   1 
ATOM   766  O  O   . GLN A 1 96  ? 14.160 13.695 8.167   1.00 44.55 ? 92  GLN A O   1 
ATOM   767  C  CB  . GLN A 1 96  ? 12.742 11.822 9.853   1.00 58.21 ? 92  GLN A CB  1 
ATOM   768  C  CG  . GLN A 1 96  ? 11.674 11.256 10.789  1.00 70.69 ? 92  GLN A CG  1 
ATOM   769  C  CD  . GLN A 1 96  ? 10.945 10.064 10.196  1.00 77.61 ? 92  GLN A CD  1 
ATOM   770  O  OE1 . GLN A 1 96  ? 11.364 8.920  10.373  1.00 86.96 ? 92  GLN A OE1 1 
ATOM   771  N  NE2 . GLN A 1 96  ? 9.844  10.326 9.495   1.00 78.41 ? 92  GLN A NE2 1 
ATOM   772  N  N   . GLY A 1 97  ? 15.476 14.249 9.903   1.00 39.78 ? 93  GLY A N   1 
ATOM   773  C  CA  . GLY A 1 97  ? 16.446 14.899 9.044   1.00 42.80 ? 93  GLY A CA  1 
ATOM   774  C  C   . GLY A 1 97  ? 17.182 13.900 8.169   1.00 45.67 ? 93  GLY A C   1 
ATOM   775  O  O   . GLY A 1 97  ? 17.525 12.795 8.593   1.00 54.75 ? 93  GLY A O   1 
ATOM   776  N  N   . LYS A 1 98  ? 17.432 14.302 6.930   1.00 37.90 ? 94  LYS A N   1 
ATOM   777  C  CA  . LYS A 1 98  ? 18.271 13.538 6.014   1.00 43.32 ? 94  LYS A CA  1 
ATOM   778  C  C   . LYS A 1 98  ? 19.549 14.344 5.823   1.00 42.02 ? 94  LYS A C   1 
ATOM   779  O  O   . LYS A 1 98  ? 19.544 15.373 5.142   1.00 36.37 ? 94  LYS A O   1 
ATOM   780  C  CB  . LYS A 1 98  ? 17.562 13.272 4.687   1.00 45.31 ? 94  LYS A CB  1 
ATOM   781  C  CG  . LYS A 1 98  ? 18.494 12.801 3.574   1.00 61.26 ? 94  LYS A CG  1 
ATOM   782  C  CD  . LYS A 1 98  ? 18.065 11.441 3.028   1.00 70.84 ? 94  LYS A CD  1 
ATOM   783  C  CE  . LYS A 1 98  ? 19.119 10.815 2.117   1.00 68.47 ? 94  LYS A CE  1 
ATOM   784  N  NZ  . LYS A 1 98  ? 18.500 9.984  1.043   1.00 64.80 ? 94  LYS A NZ  1 
ATOM   785  N  N   . GLN A 1 99  ? 20.633 13.897 6.445   1.00 31.99 ? 95  GLN A N   1 
ATOM   786  C  CA  . GLN A 1 99  ? 21.885 14.629 6.408   1.00 40.38 ? 95  GLN A CA  1 
ATOM   787  C  C   . GLN A 1 99  ? 22.874 13.919 5.499   1.00 37.31 ? 95  GLN A C   1 
ATOM   788  O  O   . GLN A 1 99  ? 22.821 12.703 5.323   1.00 36.23 ? 95  GLN A O   1 
ATOM   789  C  CB  . GLN A 1 99  ? 22.482 14.763 7.803   1.00 37.68 ? 95  GLN A CB  1 
ATOM   790  C  CG  . GLN A 1 99  ? 23.136 13.508 8.263   1.00 48.64 ? 95  GLN A CG  1 
ATOM   791  C  CD  . GLN A 1 99  ? 23.498 13.537 9.722   1.00 58.21 ? 95  GLN A CD  1 
ATOM   792  O  OE1 . GLN A 1 99  ? 24.516 12.969 10.113  1.00 50.28 ? 95  GLN A OE1 1 
ATOM   793  N  NE2 . GLN A 1 99  ? 22.661 14.185 10.546  1.00 51.16 ? 95  GLN A NE2 1 
ATOM   794  N  N   . GLY A 1 100 ? 23.790 14.684 4.931   1.00 37.22 ? 96  GLY A N   1 
ATOM   795  C  CA  . GLY A 1 100 ? 24.804 14.062 4.115   1.00 36.88 ? 96  GLY A CA  1 
ATOM   796  C  C   . GLY A 1 100 ? 25.877 15.031 3.692   1.00 30.55 ? 96  GLY A C   1 
ATOM   797  O  O   . GLY A 1 100 ? 25.616 16.230 3.594   1.00 27.25 ? 96  GLY A O   1 
ATOM   798  N  N   . ALA A 1 101 ? 27.075 14.517 3.429   1.00 29.99 ? 97  ALA A N   1 
ATOM   799  C  CA  . ALA A 1 101 ? 28.183 15.317 2.937   1.00 24.57 ? 97  ALA A CA  1 
ATOM   800  C  C   . ALA A 1 101 ? 28.114 15.435 1.420   1.00 27.67 ? 97  ALA A C   1 
ATOM   801  O  O   . ALA A 1 101 ? 27.590 14.553 0.727   1.00 27.50 ? 97  ALA A O   1 
ATOM   802  C  CB  . ALA A 1 101 ? 29.516 14.709 3.353   1.00 25.02 ? 97  ALA A CB  1 
ATOM   803  N  N   . TYR A 1 102 ? 28.637 16.551 0.909   1.00 24.84 ? 98  TYR A N   1 
ATOM   804  C  CA  . TYR A 1 102 ? 28.586 16.886 -0.507  1.00 27.27 ? 98  TYR A CA  1 
ATOM   805  C  C   . TYR A 1 102 ? 29.951 17.351 -0.983  1.00 27.84 ? 98  TYR A C   1 
ATOM   806  O  O   . TYR A 1 102 ? 30.755 17.860 -0.197  1.00 26.36 ? 98  TYR A O   1 
ATOM   807  C  CB  . TYR A 1 102 ? 27.548 17.986 -0.777  1.00 24.27 ? 98  TYR A CB  1 
ATOM   808  C  CG  . TYR A 1 102 ? 26.116 17.473 -0.733  1.00 24.13 ? 98  TYR A CG  1 
ATOM   809  C  CD1 . TYR A 1 102 ? 25.405 17.247 -1.905  1.00 27.27 ? 98  TYR A CD1 1 
ATOM   810  C  CD2 . TYR A 1 102 ? 25.485 17.204 0.484   1.00 26.62 ? 98  TYR A CD2 1 
ATOM   811  C  CE1 . TYR A 1 102 ? 24.099 16.776 -1.871  1.00 29.57 ? 98  TYR A CE1 1 
ATOM   812  C  CE2 . TYR A 1 102 ? 24.170 16.715 0.526   1.00 26.46 ? 98  TYR A CE2 1 
ATOM   813  C  CZ  . TYR A 1 102 ? 23.489 16.513 -0.658  1.00 23.26 ? 98  TYR A CZ  1 
ATOM   814  O  OH  . TYR A 1 102 ? 22.190 16.039 -0.632  1.00 28.69 ? 98  TYR A OH  1 
ATOM   815  N  N   . ASP A 1 103 ? 30.203 17.178 -2.282  1.00 29.16 ? 99  ASP A N   1 
ATOM   816  C  CA  . ASP A 1 103 ? 31.326 17.813 -2.968  1.00 26.72 ? 99  ASP A CA  1 
ATOM   817  C  C   . ASP A 1 103 ? 30.791 18.949 -3.824  1.00 28.52 ? 99  ASP A C   1 
ATOM   818  O  O   . ASP A 1 103 ? 29.858 18.738 -4.607  1.00 27.08 ? 99  ASP A O   1 
ATOM   819  C  CB  . ASP A 1 103 ? 32.068 16.840 -3.888  1.00 23.58 ? 99  ASP A CB  1 
ATOM   820  C  CG  . ASP A 1 103 ? 32.834 15.775 -3.132  1.00 32.36 ? 99  ASP A CG  1 
ATOM   821  O  OD1 . ASP A 1 103 ? 33.465 16.095 -2.110  1.00 33.73 ? 99  ASP A OD1 1 
ATOM   822  O  OD2 . ASP A 1 103 ? 32.813 14.620 -3.591  1.00 33.54 ? 99  ASP A OD2 1 
ATOM   823  N  N   . VAL A 1 104 ? 31.395 20.132 -3.696  1.00 22.83 ? 100 VAL A N   1 
ATOM   824  C  CA  . VAL A 1 104 ? 31.132 21.239 -4.620  1.00 25.50 ? 100 VAL A CA  1 
ATOM   825  C  C   . VAL A 1 104 ? 31.824 20.918 -5.937  1.00 25.01 ? 100 VAL A C   1 
ATOM   826  O  O   . VAL A 1 104 ? 33.052 20.857 -5.994  1.00 29.50 ? 100 VAL A O   1 
ATOM   827  C  CB  . VAL A 1 104 ? 31.627 22.574 -4.059  1.00 26.05 ? 100 VAL A CB  1 
ATOM   828  C  CG1 . VAL A 1 104 ? 31.298 23.715 -5.048  1.00 28.25 ? 100 VAL A CG1 1 
ATOM   829  C  CG2 . VAL A 1 104 ? 31.005 22.834 -2.729  1.00 25.46 ? 100 VAL A CG2 1 
ATOM   830  N  N   . VAL A 1 105 ? 31.050 20.684 -6.990  1.00 24.82 ? 101 VAL A N   1 
ATOM   831  C  CA  . VAL A 1 105 ? 31.619 20.296 -8.272  1.00 27.17 ? 101 VAL A CA  1 
ATOM   832  C  C   . VAL A 1 105 ? 31.565 21.414 -9.305  1.00 35.06 ? 101 VAL A C   1 
ATOM   833  O  O   . VAL A 1 105 ? 32.293 21.338 -10.305 1.00 33.30 ? 101 VAL A O   1 
ATOM   834  C  CB  . VAL A 1 105 ? 30.950 19.022 -8.827  1.00 31.22 ? 101 VAL A CB  1 
ATOM   835  C  CG1 . VAL A 1 105 ? 30.942 17.900 -7.767  1.00 28.22 ? 101 VAL A CG1 1 
ATOM   836  C  CG2 . VAL A 1 105 ? 29.557 19.323 -9.282  1.00 32.79 ? 101 VAL A CG2 1 
ATOM   837  N  N   . TYR A 1 106 ? 30.736 22.440 -9.105  1.00 33.43 ? 102 TYR A N   1 
ATOM   838  C  CA  . TYR A 1 106 ? 30.677 23.593 -10.000 1.00 31.06 ? 102 TYR A CA  1 
ATOM   839  C  C   . TYR A 1 106 ? 30.233 24.803 -9.203  1.00 22.43 ? 102 TYR A C   1 
ATOM   840  O  O   . TYR A 1 106 ? 29.291 24.712 -8.412  1.00 29.23 ? 102 TYR A O   1 
ATOM   841  C  CB  . TYR A 1 106 ? 29.703 23.370 -11.165 1.00 26.40 ? 102 TYR A CB  1 
ATOM   842  C  CG  . TYR A 1 106 ? 29.391 24.611 -12.001 1.00 34.99 ? 102 TYR A CG  1 
ATOM   843  C  CD1 . TYR A 1 106 ? 28.353 25.477 -11.642 1.00 35.45 ? 102 TYR A CD1 1 
ATOM   844  C  CD2 . TYR A 1 106 ? 30.105 24.896 -13.172 1.00 37.44 ? 102 TYR A CD2 1 
ATOM   845  C  CE1 . TYR A 1 106 ? 28.056 26.607 -12.411 1.00 31.12 ? 102 TYR A CE1 1 
ATOM   846  C  CE2 . TYR A 1 106 ? 29.808 26.029 -13.954 1.00 28.88 ? 102 TYR A CE2 1 
ATOM   847  C  CZ  . TYR A 1 106 ? 28.773 26.870 -13.562 1.00 30.73 ? 102 TYR A CZ  1 
ATOM   848  O  OH  . TYR A 1 106 ? 28.465 27.987 -14.312 1.00 30.82 ? 102 TYR A OH  1 
ATOM   849  N  N   . THR A 1 107 ? 30.906 25.931 -9.423  1.00 23.88 ? 103 THR A N   1 
ATOM   850  C  CA  . THR A 1 107 ? 30.484 27.202 -8.861  1.00 28.83 ? 103 THR A CA  1 
ATOM   851  C  C   . THR A 1 107 ? 30.795 28.307 -9.861  1.00 38.60 ? 103 THR A C   1 
ATOM   852  O  O   . THR A 1 107 ? 31.839 28.293 -10.518 1.00 34.52 ? 103 THR A O   1 
ATOM   853  C  CB  . THR A 1 107 ? 31.150 27.479 -7.503  1.00 24.84 ? 103 THR A CB  1 
ATOM   854  O  OG1 . THR A 1 107 ? 30.659 28.717 -6.967  1.00 40.11 ? 103 THR A OG1 1 
ATOM   855  C  CG2 . THR A 1 107 ? 32.659 27.540 -7.635  1.00 36.09 ? 103 THR A CG2 1 
ATOM   856  N  N   . HIS A 1 108 ? 29.860 29.238 -10.001 1.00 27.68 ? 104 HIS A N   1 
ATOM   857  C  CA  . HIS A 1 108 ? 30.066 30.419 -10.820 1.00 26.34 ? 104 HIS A CA  1 
ATOM   858  C  C   . HIS A 1 108 ? 29.294 31.561 -10.180 1.00 34.52 ? 104 HIS A C   1 
ATOM   859  O  O   . HIS A 1 108 ? 28.258 31.337 -9.552  1.00 31.01 ? 104 HIS A O   1 
ATOM   860  C  CB  . HIS A 1 108 ? 29.612 30.185 -12.263 1.00 31.16 ? 104 HIS A CB  1 
ATOM   861  C  CG  . HIS A 1 108 ? 29.644 31.419 -13.108 1.00 40.04 ? 104 HIS A CG  1 
ATOM   862  N  ND1 . HIS A 1 108 ? 28.555 32.253 -13.245 1.00 29.09 ? 104 HIS A ND1 1 
ATOM   863  C  CD2 . HIS A 1 108 ? 30.638 31.968 -13.847 1.00 36.86 ? 104 HIS A CD2 1 
ATOM   864  C  CE1 . HIS A 1 108 ? 28.879 33.266 -14.031 1.00 39.79 ? 104 HIS A CE1 1 
ATOM   865  N  NE2 . HIS A 1 108 ? 30.135 33.113 -14.416 1.00 34.44 ? 104 HIS A NE2 1 
ATOM   866  N  N   . VAL A 1 109 ? 29.807 32.783 -10.328 1.00 28.92 ? 105 VAL A N   1 
ATOM   867  C  CA  . VAL A 1 109 ? 29.166 33.967 -9.765  1.00 34.32 ? 105 VAL A CA  1 
ATOM   868  C  C   . VAL A 1 109 ? 29.402 35.145 -10.710 1.00 41.36 ? 105 VAL A C   1 
ATOM   869  O  O   . VAL A 1 109 ? 30.438 35.229 -11.372 1.00 35.90 ? 105 VAL A O   1 
ATOM   870  C  CB  . VAL A 1 109 ? 29.686 34.265 -8.336  1.00 31.76 ? 105 VAL A CB  1 
ATOM   871  C  CG1 . VAL A 1 109 ? 31.172 34.594 -8.370  1.00 41.73 ? 105 VAL A CG1 1 
ATOM   872  C  CG2 . VAL A 1 109 ? 28.918 35.434 -7.718  1.00 33.35 ? 105 VAL A CG2 1 
ATOM   873  N  N   . THR A 1 110 ? 28.420 36.046 -10.787 1.00 39.60 ? 106 THR A N   1 
ATOM   874  C  CA  . THR A 1 110 ? 28.562 37.279 -11.558 1.00 48.69 ? 106 THR A CA  1 
ATOM   875  C  C   . THR A 1 110 ? 29.545 38.224 -10.871 1.00 45.44 ? 106 THR A C   1 
ATOM   876  O  O   . THR A 1 110 ? 29.656 38.256 -9.642  1.00 48.27 ? 106 THR A O   1 
ATOM   877  C  CB  . THR A 1 110 ? 27.200 37.972 -11.718 1.00 41.16 ? 106 THR A CB  1 
ATOM   878  O  OG1 . THR A 1 110 ? 26.275 37.073 -12.334 1.00 52.33 ? 106 THR A OG1 1 
ATOM   879  C  CG2 . THR A 1 110 ? 27.313 39.194 -12.605 1.00 47.09 ? 106 THR A CG2 1 
ATOM   880  N  N   . GLU A 1 111 ? 30.262 39.009 -11.673 1.00 63.20 ? 107 GLU A N   1 
ATOM   881  C  CA  . GLU A 1 111 ? 31.161 40.019 -11.113 1.00 60.20 ? 107 GLU A CA  1 
ATOM   882  C  C   . GLU A 1 111 ? 30.547 41.412 -11.175 1.00 57.34 ? 107 GLU A C   1 
ATOM   883  O  O   . GLU A 1 111 ? 31.107 42.367 -10.631 1.00 74.37 ? 107 GLU A O   1 
ATOM   884  C  CB  . GLU A 1 111 ? 32.511 40.009 -11.841 1.00 67.27 ? 107 GLU A CB  1 
ATOM   885  C  CG  . GLU A 1 111 ? 33.123 38.614 -12.022 1.00 72.67 ? 107 GLU A CG  1 
ATOM   886  C  CD  . GLU A 1 111 ? 33.287 37.827 -10.719 1.00 78.25 ? 107 GLU A CD  1 
ATOM   887  O  OE1 . GLU A 1 111 ? 33.547 36.605 -10.808 1.00 72.11 ? 107 GLU A OE1 1 
ATOM   888  O  OE2 . GLU A 1 111 ? 33.196 38.418 -9.615  1.00 79.91 ? 107 GLU A OE2 1 
ATOM   889  N  N   . GLY B 1 4   ? 35.106 37.258 -5.037  1.00 48.52 ? 0   GLY B N   1 
ATOM   890  C  CA  . GLY B 1 4   ? 35.231 36.466 -6.249  1.00 50.70 ? 0   GLY B CA  1 
ATOM   891  C  C   . GLY B 1 4   ? 34.439 35.163 -6.268  1.00 52.52 ? 0   GLY B C   1 
ATOM   892  O  O   . GLY B 1 4   ? 34.469 34.440 -7.259  1.00 55.29 ? 0   GLY B O   1 
ATOM   893  N  N   . MET B 1 5   ? 33.719 34.865 -5.183  1.00 46.45 ? 1   MET B N   1 
ATOM   894  C  CA  . MET B 1 5   ? 33.007 33.601 -5.032  1.00 41.76 ? 1   MET B CA  1 
ATOM   895  C  C   . MET B 1 5   ? 31.578 33.849 -4.563  1.00 41.80 ? 1   MET B C   1 
ATOM   896  O  O   . MET B 1 5   ? 31.258 34.909 -4.017  1.00 36.47 ? 1   MET B O   1 
ATOM   897  C  CB  . MET B 1 5   ? 33.722 32.683 -4.033  1.00 43.88 ? 1   MET B CB  1 
ATOM   898  C  CG  . MET B 1 5   ? 35.067 32.152 -4.521  1.00 52.74 ? 1   MET B CG  1 
ATOM   899  S  SD  . MET B 1 5   ? 36.247 32.143 -3.165  1.00 88.23 ? 1   MET B SD  1 
ATOM   900  C  CE  . MET B 1 5   ? 35.830 30.602 -2.357  1.00 65.10 ? 1   MET B CE  1 
ATOM   901  N  N   . ALA B 1 6   ? 30.712 32.855 -4.774  1.00 34.62 ? 2   ALA B N   1 
ATOM   902  C  CA  . ALA B 1 6   ? 29.353 32.959 -4.261  1.00 36.92 ? 2   ALA B CA  1 
ATOM   903  C  C   . ALA B 1 6   ? 29.381 32.993 -2.738  1.00 33.40 ? 2   ALA B C   1 
ATOM   904  O  O   . ALA B 1 6   ? 30.130 32.248 -2.101  1.00 42.97 ? 2   ALA B O   1 
ATOM   905  C  CB  . ALA B 1 6   ? 28.493 31.793 -4.752  1.00 33.74 ? 2   ALA B CB  1 
ATOM   906  N  N   . GLU B 1 7   ? 28.569 33.873 -2.156  1.00 33.17 ? 3   GLU B N   1 
ATOM   907  C  CA  . GLU B 1 7   ? 28.560 34.112 -0.720  1.00 39.90 ? 3   GLU B CA  1 
ATOM   908  C  C   . GLU B 1 7   ? 27.151 33.943 -0.173  1.00 39.48 ? 3   GLU B C   1 
ATOM   909  O  O   . GLU B 1 7   ? 26.180 34.379 -0.800  1.00 37.80 ? 3   GLU B O   1 
ATOM   910  C  CB  . GLU B 1 7   ? 29.101 35.518 -0.404  1.00 40.19 ? 3   GLU B CB  1 
ATOM   911  C  CG  . GLU B 1 7   ? 30.493 35.752 -1.005  1.00 47.63 ? 3   GLU B CG  1 
ATOM   912  C  CD  . GLU B 1 7   ? 31.101 37.092 -0.634  1.00 47.55 ? 3   GLU B CD  1 
ATOM   913  O  OE1 . GLU B 1 7   ? 32.347 37.186 -0.585  1.00 55.53 ? 3   GLU B OE1 1 
ATOM   914  O  OE2 . GLU B 1 7   ? 30.334 38.047 -0.397  1.00 41.99 ? 3   GLU B OE2 1 
ATOM   915  N  N   . ILE B 1 8   ? 27.036 33.289 0.983   1.00 33.16 ? 4   ILE B N   1 
ATOM   916  C  CA  . ILE B 1 8   ? 25.752 33.105 1.658   1.00 32.81 ? 4   ILE B CA  1 
ATOM   917  C  C   . ILE B 1 8   ? 25.645 34.138 2.768   1.00 40.38 ? 4   ILE B C   1 
ATOM   918  O  O   . ILE B 1 8   ? 26.484 34.165 3.674   1.00 45.76 ? 4   ILE B O   1 
ATOM   919  C  CB  . ILE B 1 8   ? 25.599 31.689 2.237   1.00 31.92 ? 4   ILE B CB  1 
ATOM   920  C  CG1 . ILE B 1 8   ? 25.897 30.616 1.198   1.00 33.67 ? 4   ILE B CG1 1 
ATOM   921  C  CG2 . ILE B 1 8   ? 24.195 31.509 2.780   1.00 35.96 ? 4   ILE B CG2 1 
ATOM   922  C  CD1 . ILE B 1 8   ? 25.555 29.187 1.677   1.00 35.60 ? 4   ILE B CD1 1 
ATOM   923  N  N   . SER B 1 9   ? 24.612 34.977 2.722   1.00 41.91 ? 5   SER B N   1 
ATOM   924  C  CA  . SER B 1 9   ? 24.382 35.929 3.803   1.00 48.53 ? 5   SER B CA  1 
ATOM   925  C  C   . SER B 1 9   ? 22.893 36.165 3.999   1.00 45.04 ? 5   SER B C   1 
ATOM   926  O  O   . SER B 1 9   ? 22.127 36.227 3.030   1.00 51.33 ? 5   SER B O   1 
ATOM   927  C  CB  . SER B 1 9   ? 25.072 37.272 3.549   1.00 56.73 ? 5   SER B CB  1 
ATOM   928  O  OG  . SER B 1 9   ? 26.464 37.102 3.485   1.00 65.29 ? 5   SER B OG  1 
ATOM   929  N  N   . ALA B 1 10  ? 22.508 36.354 5.262   1.00 51.35 ? 6   ALA B N   1 
ATOM   930  C  CA  . ALA B 1 10  ? 21.118 36.461 5.689   1.00 48.82 ? 6   ALA B CA  1 
ATOM   931  C  C   . ALA B 1 10  ? 20.511 37.839 5.450   1.00 61.24 ? 6   ALA B C   1 
ATOM   932  O  O   . ALA B 1 10  ? 19.393 38.092 5.918   1.00 62.34 ? 6   ALA B O   1 
ATOM   933  C  CB  . ALA B 1 10  ? 20.998 36.095 7.172   1.00 38.79 ? 6   ALA B CB  1 
ATOM   934  N  N   . ASP B 1 11  ? 21.201 38.741 4.751   1.00 57.39 ? 7   ASP B N   1 
ATOM   935  C  CA  . ASP B 1 11  ? 20.530 39.984 4.393   1.00 74.48 ? 7   ASP B CA  1 
ATOM   936  C  C   . ASP B 1 11  ? 19.444 39.760 3.349   1.00 71.24 ? 7   ASP B C   1 
ATOM   937  O  O   . ASP B 1 11  ? 18.582 40.630 3.173   1.00 64.91 ? 7   ASP B O   1 
ATOM   938  C  CB  . ASP B 1 11  ? 21.555 41.010 3.911   1.00 59.79 ? 7   ASP B CB  1 
ATOM   939  C  CG  . ASP B 1 11  ? 22.615 41.303 4.964   1.00 82.80 ? 7   ASP B CG  1 
ATOM   940  O  OD1 . ASP B 1 11  ? 23.289 42.354 4.877   1.00 91.06 ? 7   ASP B OD1 1 
ATOM   941  O  OD2 . ASP B 1 11  ? 22.774 40.475 5.886   1.00 76.44 ? 7   ASP B OD2 1 
ATOM   942  N  N   . ASN B 1 12  ? 19.455 38.597 2.690   1.00 64.04 ? 8   ASN B N   1 
ATOM   943  C  CA  . ASN B 1 12  ? 18.483 38.228 1.662   1.00 55.80 ? 8   ASN B CA  1 
ATOM   944  C  C   . ASN B 1 12  ? 18.370 39.302 0.590   1.00 59.01 ? 8   ASN B C   1 
ATOM   945  O  O   . ASN B 1 12  ? 17.300 39.530 0.016   1.00 58.99 ? 8   ASN B O   1 
ATOM   946  C  CB  . ASN B 1 12  ? 17.129 37.898 2.281   1.00 61.60 ? 8   ASN B CB  1 
ATOM   947  C  CG  . ASN B 1 12  ? 17.149 36.565 2.996   1.00 52.42 ? 8   ASN B CG  1 
ATOM   948  O  OD1 . ASN B 1 12  ? 17.171 35.500 2.360   1.00 37.49 ? 8   ASN B OD1 1 
ATOM   949  N  ND2 . ASN B 1 12  ? 17.181 36.613 4.326   1.00 50.87 ? 8   ASN B ND2 1 
ATOM   950  N  N   . GLU B 1 13  ? 19.500 39.962 0.333   1.00 51.50 ? 9   GLU B N   1 
ATOM   951  C  CA  . GLU B 1 13  ? 19.653 40.798 -0.848  1.00 47.53 ? 9   GLU B CA  1 
ATOM   952  C  C   . GLU B 1 13  ? 19.200 40.061 -2.107  1.00 43.96 ? 9   GLU B C   1 
ATOM   953  O  O   . GLU B 1 13  ? 18.607 40.658 -3.011  1.00 46.97 ? 9   GLU B O   1 
ATOM   954  C  CB  . GLU B 1 13  ? 21.120 41.211 -0.939  1.00 49.56 ? 9   GLU B CB  1 
ATOM   955  C  CG  . GLU B 1 13  ? 21.467 42.261 -1.950  1.00 58.79 ? 9   GLU B CG  1 
ATOM   956  C  CD  . GLU B 1 13  ? 22.969 42.466 -2.032  1.00 65.92 ? 9   GLU B CD  1 
ATOM   957  O  OE1 . GLU B 1 13  ? 23.419 43.625 -2.175  1.00 85.87 ? 9   GLU B OE1 1 
ATOM   958  O  OE2 . GLU B 1 13  ? 23.706 41.462 -1.947  1.00 77.25 ? 9   GLU B OE2 1 
ATOM   959  N  N   . PHE B 1 14  ? 19.459 38.758 -2.168  1.00 40.46 ? 10  PHE B N   1 
ATOM   960  C  CA  . PHE B 1 14  ? 19.171 37.900 -3.306  1.00 40.35 ? 10  PHE B CA  1 
ATOM   961  C  C   . PHE B 1 14  ? 18.063 36.918 -2.962  1.00 35.50 ? 10  PHE B C   1 
ATOM   962  O  O   . PHE B 1 14  ? 17.819 36.618 -1.790  1.00 34.41 ? 10  PHE B O   1 
ATOM   963  C  CB  . PHE B 1 14  ? 20.408 37.094 -3.717  1.00 30.87 ? 10  PHE B CB  1 
ATOM   964  C  CG  . PHE B 1 14  ? 21.619 37.927 -3.946  1.00 39.00 ? 10  PHE B CG  1 
ATOM   965  C  CD1 . PHE B 1 14  ? 21.537 39.100 -4.673  1.00 42.97 ? 10  PHE B CD1 1 
ATOM   966  C  CD2 . PHE B 1 14  ? 22.844 37.544 -3.426  1.00 42.67 ? 10  PHE B CD2 1 
ATOM   967  C  CE1 . PHE B 1 14  ? 22.664 39.885 -4.880  1.00 49.30 ? 10  PHE B CE1 1 
ATOM   968  C  CE2 . PHE B 1 14  ? 23.966 38.319 -3.625  1.00 39.57 ? 10  PHE B CE2 1 
ATOM   969  C  CZ  . PHE B 1 14  ? 23.876 39.493 -4.355  1.00 42.51 ? 10  PHE B CZ  1 
ATOM   970  N  N   . ALA B 1 15  ? 17.416 36.391 -4.006  1.00 26.13 ? 11  ALA B N   1 
ATOM   971  C  CA  . ALA B 1 15  ? 16.572 35.211 -3.860  1.00 28.90 ? 11  ALA B CA  1 
ATOM   972  C  C   . ALA B 1 15  ? 17.440 33.974 -4.008  1.00 30.44 ? 11  ALA B C   1 
ATOM   973  O  O   . ALA B 1 15  ? 18.393 33.958 -4.792  1.00 27.31 ? 11  ALA B O   1 
ATOM   974  C  CB  . ALA B 1 15  ? 15.443 35.175 -4.890  1.00 26.30 ? 11  ALA B CB  1 
ATOM   975  N  N   . THR B 1 16  ? 17.103 32.940 -3.254  1.00 22.28 ? 12  THR B N   1 
ATOM   976  C  CA  . THR B 1 16  ? 17.883 31.720 -3.185  1.00 21.28 ? 12  THR B CA  1 
ATOM   977  C  C   . THR B 1 16  ? 16.981 30.551 -3.534  1.00 24.62 ? 12  THR B C   1 
ATOM   978  O  O   . THR B 1 16  ? 15.913 30.390 -2.936  1.00 25.85 ? 12  THR B O   1 
ATOM   979  C  CB  . THR B 1 16  ? 18.463 31.558 -1.776  1.00 29.95 ? 12  THR B CB  1 
ATOM   980  O  OG1 . THR B 1 16  ? 19.243 32.712 -1.461  1.00 28.08 ? 12  THR B OG1 1 
ATOM   981  C  CG2 . THR B 1 16  ? 19.323 30.304 -1.665  1.00 19.58 ? 12  THR B CG2 1 
ATOM   982  N  N   . PHE B 1 17  ? 17.387 29.759 -4.517  1.00 23.71 ? 13  PHE B N   1 
ATOM   983  C  CA  . PHE B 1 17  ? 16.720 28.502 -4.814  1.00 19.98 ? 13  PHE B CA  1 
ATOM   984  C  C   . PHE B 1 17  ? 17.643 27.348 -4.454  1.00 29.77 ? 13  PHE B C   1 
ATOM   985  O  O   . PHE B 1 17  ? 18.853 27.397 -4.707  1.00 25.41 ? 13  PHE B O   1 
ATOM   986  C  CB  . PHE B 1 17  ? 16.321 28.402 -6.282  1.00 26.19 ? 13  PHE B CB  1 
ATOM   987  C  CG  . PHE B 1 17  ? 15.165 29.285 -6.652  1.00 25.17 ? 13  PHE B CG  1 
ATOM   988  C  CD1 . PHE B 1 17  ? 13.903 28.747 -6.869  1.00 29.28 ? 13  PHE B CD1 1 
ATOM   989  C  CD2 . PHE B 1 17  ? 15.340 30.648 -6.781  1.00 26.19 ? 13  PHE B CD2 1 
ATOM   990  C  CE1 . PHE B 1 17  ? 12.833 29.568 -7.212  1.00 26.33 ? 13  PHE B CE1 1 
ATOM   991  C  CE2 . PHE B 1 17  ? 14.279 31.473 -7.115  1.00 29.98 ? 13  PHE B CE2 1 
ATOM   992  C  CZ  . PHE B 1 17  ? 13.030 30.936 -7.338  1.00 21.22 ? 13  PHE B CZ  1 
ATOM   993  N  N   . ILE B 1 18  ? 17.075 26.323 -3.846  1.00 27.83 ? 14  ILE B N   1 
ATOM   994  C  CA  . ILE B 1 18  ? 17.798 25.100 -3.533  1.00 25.49 ? 14  ILE B CA  1 
ATOM   995  C  C   . ILE B 1 18  ? 17.025 24.002 -4.233  1.00 29.37 ? 14  ILE B C   1 
ATOM   996  O  O   . ILE B 1 18  ? 15.940 23.621 -3.786  1.00 31.56 ? 14  ILE B O   1 
ATOM   997  C  CB  . ILE B 1 18  ? 17.910 24.841 -2.027  1.00 28.23 ? 14  ILE B CB  1 
ATOM   998  C  CG1 . ILE B 1 18  ? 18.386 26.099 -1.296  1.00 26.17 ? 14  ILE B CG1 1 
ATOM   999  C  CG2 . ILE B 1 18  ? 18.875 23.678 -1.768  1.00 25.42 ? 14  ILE B CG2 1 
ATOM   1000 C  CD1 . ILE B 1 18  ? 18.568 25.917 0.219   1.00 21.32 ? 14  ILE B CD1 1 
ATOM   1001 N  N   . ASN B 1 19  ? 17.547 23.515 -5.350  1.00 26.52 ? 15  ASN B N   1 
ATOM   1002 C  CA  . ASN B 1 19  ? 16.846 22.509 -6.130  1.00 26.85 ? 15  ASN B CA  1 
ATOM   1003 C  C   . ASN B 1 19  ? 17.461 21.151 -5.829  1.00 34.31 ? 15  ASN B C   1 
ATOM   1004 O  O   . ASN B 1 19  ? 18.674 20.963 -5.981  1.00 30.29 ? 15  ASN B O   1 
ATOM   1005 C  CB  . ASN B 1 19  ? 16.894 22.857 -7.619  1.00 29.06 ? 15  ASN B CB  1 
ATOM   1006 C  CG  . ASN B 1 19  ? 16.381 24.270 -7.888  1.00 43.37 ? 15  ASN B CG  1 
ATOM   1007 O  OD1 . ASN B 1 19  ? 15.641 24.854 -7.074  1.00 35.97 ? 15  ASN B OD1 1 
ATOM   1008 N  ND2 . ASN B 1 19  ? 16.770 24.826 -9.025  1.00 51.17 ? 15  ASN B ND2 1 
ATOM   1009 N  N   . LEU B 1 20  ? 16.632 20.224 -5.359  1.00 31.35 ? 16  LEU B N   1 
ATOM   1010 C  CA  . LEU B 1 20  ? 17.086 18.908 -4.907  1.00 37.27 ? 16  LEU B CA  1 
ATOM   1011 C  C   . LEU B 1 20  ? 16.736 17.887 -5.975  1.00 42.49 ? 16  LEU B C   1 
ATOM   1012 O  O   . LEU B 1 20  ? 15.554 17.628 -6.220  1.00 46.31 ? 16  LEU B O   1 
ATOM   1013 C  CB  . LEU B 1 20  ? 16.439 18.523 -3.578  1.00 36.31 ? 16  LEU B CB  1 
ATOM   1014 C  CG  . LEU B 1 20  ? 16.406 19.589 -2.487  1.00 38.42 ? 16  LEU B CG  1 
ATOM   1015 C  CD1 . LEU B 1 20  ? 15.479 19.172 -1.362  1.00 43.38 ? 16  LEU B CD1 1 
ATOM   1016 C  CD2 . LEU B 1 20  ? 17.795 19.820 -1.952  1.00 39.33 ? 16  LEU B CD2 1 
ATOM   1017 N  N   . PHE B 1 21  ? 17.756 17.289 -6.595  1.00 41.56 ? 17  PHE B N   1 
ATOM   1018 C  CA  . PHE B 1 21  ? 17.555 16.287 -7.640  1.00 42.76 ? 17  PHE B CA  1 
ATOM   1019 C  C   . PHE B 1 21  ? 17.939 14.913 -7.099  1.00 47.21 ? 17  PHE B C   1 
ATOM   1020 O  O   . PHE B 1 21  ? 19.106 14.502 -7.201  1.00 41.20 ? 17  PHE B O   1 
ATOM   1021 C  CB  . PHE B 1 21  ? 18.375 16.618 -8.893  1.00 37.27 ? 17  PHE B CB  1 
ATOM   1022 C  CG  . PHE B 1 21  ? 18.076 17.965 -9.488  1.00 43.02 ? 17  PHE B CG  1 
ATOM   1023 C  CD1 . PHE B 1 21  ? 17.020 18.130 -10.371 1.00 47.55 ? 17  PHE B CD1 1 
ATOM   1024 C  CD2 . PHE B 1 21  ? 18.864 19.058 -9.186  1.00 27.30 ? 17  PHE B CD2 1 
ATOM   1025 C  CE1 . PHE B 1 21  ? 16.751 19.364 -10.923 1.00 48.58 ? 17  PHE B CE1 1 
ATOM   1026 C  CE2 . PHE B 1 21  ? 18.605 20.294 -9.736  1.00 35.84 ? 17  PHE B CE2 1 
ATOM   1027 C  CZ  . PHE B 1 21  ? 17.542 20.448 -10.605 1.00 45.60 ? 17  PHE B CZ  1 
ATOM   1028 N  N   . PRO B 1 22  ? 17.003 14.165 -6.519  1.00 48.69 ? 18  PRO B N   1 
ATOM   1029 C  CA  . PRO B 1 22  ? 17.335 12.816 -6.046  1.00 40.74 ? 18  PRO B CA  1 
ATOM   1030 C  C   . PRO B 1 22  ? 17.706 11.938 -7.222  1.00 37.39 ? 18  PRO B C   1 
ATOM   1031 O  O   . PRO B 1 22  ? 17.146 12.069 -8.309  1.00 39.83 ? 18  PRO B O   1 
ATOM   1032 C  CB  . PRO B 1 22  ? 16.038 12.340 -5.382  1.00 42.49 ? 18  PRO B CB  1 
ATOM   1033 C  CG  . PRO B 1 22  ? 15.185 13.588 -5.244  1.00 42.65 ? 18  PRO B CG  1 
ATOM   1034 C  CD  . PRO B 1 22  ? 15.570 14.453 -6.389  1.00 42.83 ? 18  PRO B CD  1 
ATOM   1035 N  N   . THR B 1 23  ? 18.668 11.047 -7.013  1.00 37.93 ? 19  THR B N   1 
ATOM   1036 C  CA  . THR B 1 23  ? 19.138 10.225 -8.121  1.00 37.26 ? 19  THR B CA  1 
ATOM   1037 C  C   . THR B 1 23  ? 19.577 8.867  -7.583  1.00 36.54 ? 19  THR B C   1 
ATOM   1038 O  O   . THR B 1 23  ? 19.320 8.522  -6.427  1.00 43.62 ? 19  THR B O   1 
ATOM   1039 C  CB  . THR B 1 23  ? 20.259 10.944 -8.883  1.00 34.50 ? 19  THR B CB  1 
ATOM   1040 O  OG1 . THR B 1 23  ? 20.547 10.231 -10.090 1.00 42.35 ? 19  THR B OG1 1 
ATOM   1041 C  CG2 . THR B 1 23  ? 21.514 11.035 -8.035  1.00 31.51 ? 19  THR B CG2 1 
ATOM   1042 N  N   . LYS B 1 24  ? 20.211 8.083  -8.445  1.00 38.42 ? 20  LYS B N   1 
ATOM   1043 C  CA  . LYS B 1 24  ? 20.815 6.804  -8.118  1.00 46.42 ? 20  LYS B CA  1 
ATOM   1044 C  C   . LYS B 1 24  ? 22.294 6.849  -8.477  1.00 33.73 ? 20  LYS B C   1 
ATOM   1045 O  O   . LYS B 1 24  ? 22.670 7.490  -9.461  1.00 37.92 ? 20  LYS B O   1 
ATOM   1046 C  CB  . LYS B 1 24  ? 20.144 5.648  -8.872  1.00 41.70 ? 20  LYS B CB  1 
ATOM   1047 C  CG  . LYS B 1 24  ? 18.645 5.556  -8.683  1.00 47.05 ? 20  LYS B CG  1 
ATOM   1048 C  CD  . LYS B 1 24  ? 18.039 4.452  -9.545  1.00 51.78 ? 20  LYS B CD  1 
ATOM   1049 C  CE  . LYS B 1 24  ? 18.619 4.460  -10.950 1.00 58.58 ? 20  LYS B CE  1 
ATOM   1050 N  NZ  . LYS B 1 24  ? 17.562 4.484  -12.001 1.00 58.86 ? 20  LYS B NZ  1 
ATOM   1051 N  N   . PRO B 1 25  ? 23.152 6.176  -7.706  1.00 33.20 ? 21  PRO B N   1 
ATOM   1052 C  CA  . PRO B 1 25  ? 24.602 6.289  -7.944  1.00 39.33 ? 21  PRO B CA  1 
ATOM   1053 C  C   . PRO B 1 25  ? 25.020 6.102  -9.396  1.00 40.87 ? 21  PRO B C   1 
ATOM   1054 O  O   . PRO B 1 25  ? 25.911 6.814  -9.867  1.00 35.64 ? 21  PRO B O   1 
ATOM   1055 C  CB  . PRO B 1 25  ? 25.173 5.187  -7.036  1.00 38.39 ? 21  PRO B CB  1 
ATOM   1056 C  CG  . PRO B 1 25  ? 24.216 5.127  -5.905  1.00 39.44 ? 21  PRO B CG  1 
ATOM   1057 C  CD  . PRO B 1 25  ? 22.857 5.327  -6.540  1.00 34.16 ? 21  PRO B CD  1 
ATOM   1058 N  N   . ARG B 1 26  ? 24.391 5.184  -10.132 1.00 39.40 ? 22  ARG B N   1 
ATOM   1059 C  CA  . ARG B 1 26  ? 24.818 4.960  -11.506 1.00 32.64 ? 22  ARG B CA  1 
ATOM   1060 C  C   . ARG B 1 26  ? 24.401 6.089  -12.443 1.00 41.15 ? 22  ARG B C   1 
ATOM   1061 O  O   . ARG B 1 26  ? 24.995 6.227  -13.519 1.00 37.16 ? 22  ARG B O   1 
ATOM   1062 C  CB  . ARG B 1 26  ? 24.264 3.631  -12.018 1.00 48.67 ? 22  ARG B CB  1 
ATOM   1063 C  CG  . ARG B 1 26  ? 22.757 3.605  -12.166 1.00 46.70 ? 22  ARG B CG  1 
ATOM   1064 C  CD  . ARG B 1 26  ? 22.323 2.388  -12.962 1.00 56.48 ? 22  ARG B CD  1 
ATOM   1065 N  NE  . ARG B 1 26  ? 20.881 2.190  -12.890 1.00 59.94 ? 22  ARG B NE  1 
ATOM   1066 C  CZ  . ARG B 1 26  ? 20.268 1.469  -11.955 1.00 68.83 ? 22  ARG B CZ  1 
ATOM   1067 N  NH1 . ARG B 1 26  ? 20.970 0.862  -11.007 1.00 59.42 ? 22  ARG B NH1 1 
ATOM   1068 N  NH2 . ARG B 1 26  ? 18.947 1.351  -11.971 1.00 74.46 ? 22  ARG B NH2 1 
ATOM   1069 N  N   . ASP B 1 27  ? 23.395 6.890  -12.069 1.00 38.40 ? 23  ASP B N   1 
ATOM   1070 C  CA  . ASP B 1 27  ? 22.974 8.043  -12.867 1.00 40.84 ? 23  ASP B CA  1 
ATOM   1071 C  C   . ASP B 1 27  ? 23.609 9.359  -12.434 1.00 43.36 ? 23  ASP B C   1 
ATOM   1072 O  O   . ASP B 1 27  ? 23.518 10.339 -13.180 1.00 36.25 ? 23  ASP B O   1 
ATOM   1073 C  CB  . ASP B 1 27  ? 21.457 8.242  -12.792 1.00 37.76 ? 23  ASP B CB  1 
ATOM   1074 C  CG  . ASP B 1 27  ? 20.680 7.168  -13.498 1.00 44.13 ? 23  ASP B CG  1 
ATOM   1075 O  OD1 . ASP B 1 27  ? 21.216 6.549  -14.441 1.00 39.90 ? 23  ASP B OD1 1 
ATOM   1076 O  OD2 . ASP B 1 27  ? 19.519 6.962  -13.101 1.00 40.72 ? 23  ASP B OD2 1 
ATOM   1077 N  N   . GLN B 1 28  ? 24.230 9.409  -11.254 1.00 35.19 ? 24  GLN B N   1 
ATOM   1078 C  CA  . GLN B 1 28  ? 24.487 10.692 -10.599 1.00 35.20 ? 24  GLN B CA  1 
ATOM   1079 C  C   . GLN B 1 28  ? 25.435 11.575 -11.401 1.00 34.77 ? 24  GLN B C   1 
ATOM   1080 O  O   . GLN B 1 28  ? 25.202 12.781 -11.523 1.00 34.34 ? 24  GLN B O   1 
ATOM   1081 C  CB  . GLN B 1 28  ? 25.041 10.466 -9.197  1.00 29.37 ? 24  GLN B CB  1 
ATOM   1082 C  CG  . GLN B 1 28  ? 25.104 11.729 -8.359  1.00 32.12 ? 24  GLN B CG  1 
ATOM   1083 C  CD  . GLN B 1 28  ? 26.018 11.583 -7.175  1.00 27.81 ? 24  GLN B CD  1 
ATOM   1084 O  OE1 . GLN B 1 28  ? 27.106 11.030 -7.287  1.00 30.22 ? 24  GLN B OE1 1 
ATOM   1085 N  NE2 . GLN B 1 28  ? 25.592 12.092 -6.031  1.00 28.77 ? 24  GLN B NE2 1 
ATOM   1086 N  N   . GLN B 1 29  ? 26.519 11.009 -11.941 1.00 35.13 ? 25  GLN B N   1 
ATOM   1087 C  CA  . GLN B 1 29  ? 27.484 11.849 -12.648 1.00 37.29 ? 25  GLN B CA  1 
ATOM   1088 C  C   . GLN B 1 29  ? 26.923 12.337 -13.974 1.00 37.21 ? 25  GLN B C   1 
ATOM   1089 O  O   . GLN B 1 29  ? 27.219 13.458 -14.402 1.00 40.73 ? 25  GLN B O   1 
ATOM   1090 C  CB  . GLN B 1 29  ? 28.800 11.105 -12.872 1.00 41.73 ? 25  GLN B CB  1 
ATOM   1091 C  CG  . GLN B 1 29  ? 29.941 11.999 -13.386 1.00 36.92 ? 25  GLN B CG  1 
ATOM   1092 C  CD  . GLN B 1 29  ? 30.230 13.212 -12.477 1.00 46.96 ? 25  GLN B CD  1 
ATOM   1093 O  OE1 . GLN B 1 29  ? 30.375 13.079 -11.260 1.00 41.79 ? 25  GLN B OE1 1 
ATOM   1094 N  NE2 . GLN B 1 29  ? 30.338 14.394 -13.083 1.00 39.89 ? 25  GLN B NE2 1 
ATOM   1095 N  N   . LYS B 1 30  ? 26.135 11.501 -14.651 1.00 36.53 ? 26  LYS B N   1 
ATOM   1096 C  CA  . LYS B 1 30  ? 25.447 11.966 -15.848 1.00 41.85 ? 26  LYS B CA  1 
ATOM   1097 C  C   . LYS B 1 30  ? 24.555 13.156 -15.519 1.00 40.64 ? 26  LYS B C   1 
ATOM   1098 O  O   . LYS B 1 30  ? 24.544 14.155 -16.245 1.00 37.77 ? 26  LYS B O   1 
ATOM   1099 C  CB  . LYS B 1 30  ? 24.629 10.831 -16.466 1.00 41.87 ? 26  LYS B CB  1 
ATOM   1100 C  CG  . LYS B 1 30  ? 23.801 11.251 -17.680 1.00 48.33 ? 26  LYS B CG  1 
ATOM   1101 C  CD  . LYS B 1 30  ? 24.663 11.414 -18.925 1.00 59.88 ? 26  LYS B CD  1 
ATOM   1102 C  CE  . LYS B 1 30  ? 24.488 12.782 -19.580 1.00 56.64 ? 26  LYS B CE  1 
ATOM   1103 N  NZ  . LYS B 1 30  ? 25.178 13.859 -18.806 1.00 43.55 ? 26  LYS B NZ  1 
ATOM   1104 N  N   . LEU B 1 31  ? 23.829 13.078 -14.403 1.00 39.37 ? 27  LEU B N   1 
ATOM   1105 C  CA  . LEU B 1 31  ? 22.968 14.181 -13.992 1.00 36.46 ? 27  LEU B CA  1 
ATOM   1106 C  C   . LEU B 1 31  ? 23.782 15.432 -13.689 1.00 34.66 ? 27  LEU B C   1 
ATOM   1107 O  O   . LEU B 1 31  ? 23.393 16.538 -14.080 1.00 39.05 ? 27  LEU B O   1 
ATOM   1108 C  CB  . LEU B 1 31  ? 22.135 13.760 -12.782 1.00 33.30 ? 27  LEU B CB  1 
ATOM   1109 C  CG  . LEU B 1 31  ? 21.187 14.810 -12.196 1.00 43.20 ? 27  LEU B CG  1 
ATOM   1110 C  CD1 . LEU B 1 31  ? 20.285 15.414 -13.263 1.00 30.75 ? 27  LEU B CD1 1 
ATOM   1111 C  CD2 . LEU B 1 31  ? 20.362 14.172 -11.112 1.00 35.14 ? 27  LEU B CD2 1 
ATOM   1112 N  N   . VAL B 1 32  ? 24.919 15.274 -12.999 1.00 34.48 ? 28  VAL B N   1 
ATOM   1113 C  CA  . VAL B 1 32  ? 25.800 16.402 -12.709 1.00 33.48 ? 28  VAL B CA  1 
ATOM   1114 C  C   . VAL B 1 32  ? 26.261 17.062 -14.001 1.00 36.26 ? 28  VAL B C   1 
ATOM   1115 O  O   . VAL B 1 32  ? 26.178 18.285 -14.161 1.00 30.49 ? 28  VAL B O   1 
ATOM   1116 C  CB  . VAL B 1 32  ? 27.006 15.944 -11.867 1.00 35.97 ? 28  VAL B CB  1 
ATOM   1117 C  CG1 . VAL B 1 32  ? 28.039 17.047 -11.801 1.00 32.34 ? 28  VAL B CG1 1 
ATOM   1118 C  CG2 . VAL B 1 32  ? 26.571 15.539 -10.469 1.00 30.97 ? 28  VAL B CG2 1 
ATOM   1119 N  N   . ASP B 1 33  ? 26.771 16.261 -14.937 1.00 35.67 ? 29  ASP B N   1 
ATOM   1120 C  CA  . ASP B 1 33  ? 27.258 16.816 -16.197 1.00 33.78 ? 29  ASP B CA  1 
ATOM   1121 C  C   . ASP B 1 33  ? 26.175 17.624 -16.914 1.00 30.47 ? 29  ASP B C   1 
ATOM   1122 O  O   . ASP B 1 33  ? 26.445 18.717 -17.419 1.00 32.94 ? 29  ASP B O   1 
ATOM   1123 C  CB  . ASP B 1 33  ? 27.779 15.693 -17.088 1.00 38.12 ? 29  ASP B CB  1 
ATOM   1124 C  CG  . ASP B 1 33  ? 28.987 14.986 -16.492 1.00 42.96 ? 29  ASP B CG  1 
ATOM   1125 O  OD1 . ASP B 1 33  ? 29.626 15.548 -15.578 1.00 40.99 ? 29  ASP B OD1 1 
ATOM   1126 O  OD2 . ASP B 1 33  ? 29.293 13.860 -16.934 1.00 51.39 ? 29  ASP B OD2 1 
ATOM   1127 N  N   . LEU B 1 34  ? 24.941 17.111 -16.951 1.00 30.55 ? 30  LEU B N   1 
ATOM   1128 C  CA  . LEU B 1 34  ? 23.855 17.837 -17.614 1.00 32.15 ? 30  LEU B CA  1 
ATOM   1129 C  C   . LEU B 1 34  ? 23.577 19.167 -16.931 1.00 39.20 ? 30  LEU B C   1 
ATOM   1130 O  O   . LEU B 1 34  ? 23.325 20.181 -17.595 1.00 31.83 ? 30  LEU B O   1 
ATOM   1131 C  CB  . LEU B 1 34  ? 22.588 16.992 -17.624 1.00 32.04 ? 30  LEU B CB  1 
ATOM   1132 C  CG  . LEU B 1 34  ? 22.604 15.791 -18.565 1.00 41.72 ? 30  LEU B CG  1 
ATOM   1133 C  CD1 . LEU B 1 34  ? 21.473 14.868 -18.193 1.00 43.89 ? 30  LEU B CD1 1 
ATOM   1134 C  CD2 . LEU B 1 34  ? 22.467 16.247 -20.014 1.00 39.57 ? 30  LEU B CD2 1 
ATOM   1135 N  N   . ILE B 1 35  ? 23.604 19.179 -15.601 1.00 33.03 ? 31  ILE B N   1 
ATOM   1136 C  CA  . ILE B 1 35  ? 23.285 20.398 -14.873 1.00 32.68 ? 31  ILE B CA  1 
ATOM   1137 C  C   . ILE B 1 35  ? 24.381 21.432 -15.070 1.00 36.71 ? 31  ILE B C   1 
ATOM   1138 O  O   . ILE B 1 35  ? 24.102 22.614 -15.302 1.00 32.34 ? 31  ILE B O   1 
ATOM   1139 C  CB  . ILE B 1 35  ? 23.046 20.064 -13.390 1.00 28.11 ? 31  ILE B CB  1 
ATOM   1140 C  CG1 . ILE B 1 35  ? 21.775 19.208 -13.264 1.00 27.32 ? 31  ILE B CG1 1 
ATOM   1141 C  CG2 . ILE B 1 35  ? 22.930 21.324 -12.575 1.00 29.86 ? 31  ILE B CG2 1 
ATOM   1142 C  CD1 . ILE B 1 35  ? 21.528 18.652 -11.865 1.00 28.96 ? 31  ILE B CD1 1 
ATOM   1143 N  N   . VAL B 1 36  ? 25.646 21.001 -15.019 1.00 38.63 ? 32  VAL B N   1 
ATOM   1144 C  CA  . VAL B 1 36  ? 26.758 21.918 -15.263 1.00 30.92 ? 32  VAL B CA  1 
ATOM   1145 C  C   . VAL B 1 36  ? 26.712 22.465 -16.693 1.00 32.04 ? 32  VAL B C   1 
ATOM   1146 O  O   . VAL B 1 36  ? 26.983 23.648 -16.928 1.00 30.47 ? 32  VAL B O   1 
ATOM   1147 C  CB  . VAL B 1 36  ? 28.095 21.218 -14.956 1.00 31.97 ? 32  VAL B CB  1 
ATOM   1148 C  CG1 . VAL B 1 36  ? 29.275 22.110 -15.336 1.00 32.67 ? 32  VAL B CG1 1 
ATOM   1149 C  CG2 . VAL B 1 36  ? 28.152 20.843 -13.478 1.00 30.10 ? 32  VAL B CG2 1 
ATOM   1150 N  N   . LYS B 1 37  ? 26.367 21.621 -17.666 1.00 31.59 ? 33  LYS B N   1 
ATOM   1151 C  CA  . LYS B 1 37  ? 26.201 22.101 -19.038 1.00 36.04 ? 33  LYS B CA  1 
ATOM   1152 C  C   . LYS B 1 37  ? 25.126 23.185 -19.116 1.00 35.94 ? 33  LYS B C   1 
ATOM   1153 O  O   . LYS B 1 37  ? 25.324 24.233 -19.743 1.00 33.80 ? 33  LYS B O   1 
ATOM   1154 C  CB  . LYS B 1 37  ? 25.853 20.928 -19.961 1.00 34.68 ? 33  LYS B CB  1 
ATOM   1155 C  CG  . LYS B 1 37  ? 25.810 21.266 -21.441 1.00 37.33 ? 33  LYS B CG  1 
ATOM   1156 C  CD  . LYS B 1 37  ? 25.903 19.996 -22.298 1.00 43.39 ? 33  LYS B CD  1 
ATOM   1157 C  CE  . LYS B 1 37  ? 24.559 19.629 -22.930 1.00 52.69 ? 33  LYS B CE  1 
ATOM   1158 N  NZ  . LYS B 1 37  ? 24.448 20.054 -24.361 1.00 54.48 ? 33  LYS B NZ  1 
ATOM   1159 N  N   . ALA B 1 38  ? 23.975 22.943 -18.486 1.00 36.10 ? 34  ALA B N   1 
ATOM   1160 C  CA  . ALA B 1 38  ? 22.920 23.951 -18.449 1.00 31.83 ? 34  ALA B CA  1 
ATOM   1161 C  C   . ALA B 1 38  ? 23.433 25.250 -17.845 1.00 29.75 ? 34  ALA B C   1 
ATOM   1162 O  O   . ALA B 1 38  ? 23.190 26.338 -18.377 1.00 31.27 ? 34  ALA B O   1 
ATOM   1163 C  CB  . ALA B 1 38  ? 21.720 23.423 -17.660 1.00 30.72 ? 34  ALA B CB  1 
ATOM   1164 N  N   . HIS B 1 39  ? 24.174 25.156 -16.739 1.00 26.83 ? 35  HIS B N   1 
ATOM   1165 C  CA  . HIS B 1 39  ? 24.706 26.372 -16.133 1.00 26.78 ? 35  HIS B CA  1 
ATOM   1166 C  C   . HIS B 1 39  ? 25.682 27.067 -17.061 1.00 32.42 ? 35  HIS B C   1 
ATOM   1167 O  O   . HIS B 1 39  ? 25.651 28.296 -17.200 1.00 33.90 ? 35  HIS B O   1 
ATOM   1168 C  CB  . HIS B 1 39  ? 25.386 26.062 -14.810 1.00 22.78 ? 35  HIS B CB  1 
ATOM   1169 C  CG  . HIS B 1 39  ? 24.443 26.049 -13.656 1.00 28.95 ? 35  HIS B CG  1 
ATOM   1170 N  ND1 . HIS B 1 39  ? 23.994 27.203 -13.055 1.00 32.16 ? 35  HIS B ND1 1 
ATOM   1171 C  CD2 . HIS B 1 39  ? 23.826 25.025 -13.020 1.00 33.06 ? 35  HIS B CD2 1 
ATOM   1172 C  CE1 . HIS B 1 39  ? 23.162 26.890 -12.078 1.00 33.50 ? 35  HIS B CE1 1 
ATOM   1173 N  NE2 . HIS B 1 39  ? 23.031 25.576 -12.046 1.00 29.18 ? 35  HIS B NE2 1 
ATOM   1174 N  N   . GLU B 1 40  ? 26.563 26.301 -17.698 1.00 35.51 ? 36  GLU B N   1 
ATOM   1175 C  CA  . GLU B 1 40  ? 27.572 26.915 -18.550 1.00 36.24 ? 36  GLU B CA  1 
ATOM   1176 C  C   . GLU B 1 40  ? 26.944 27.545 -19.777 1.00 25.21 ? 36  GLU B C   1 
ATOM   1177 O  O   . GLU B 1 40  ? 27.384 28.604 -20.229 1.00 35.51 ? 36  GLU B O   1 
ATOM   1178 C  CB  . GLU B 1 40  ? 28.617 25.878 -18.951 1.00 34.44 ? 36  GLU B CB  1 
ATOM   1179 C  CG  . GLU B 1 40  ? 29.660 25.674 -17.870 1.00 31.82 ? 36  GLU B CG  1 
ATOM   1180 C  CD  . GLU B 1 40  ? 30.585 24.515 -18.159 1.00 42.78 ? 36  GLU B CD  1 
ATOM   1181 O  OE1 . GLU B 1 40  ? 31.615 24.392 -17.457 1.00 53.37 ? 36  GLU B OE1 1 
ATOM   1182 O  OE2 . GLU B 1 40  ? 30.286 23.734 -19.085 1.00 38.63 ? 36  GLU B OE2 1 
ATOM   1183 N  N   . GLU B 1 41  ? 25.900 26.929 -20.314 1.00 27.83 ? 37  GLU B N   1 
ATOM   1184 C  CA  . GLU B 1 41  ? 25.387 27.335 -21.613 1.00 38.41 ? 37  GLU B CA  1 
ATOM   1185 C  C   . GLU B 1 41  ? 24.119 28.168 -21.548 1.00 40.59 ? 37  GLU B C   1 
ATOM   1186 O  O   . GLU B 1 41  ? 23.791 28.832 -22.533 1.00 39.77 ? 37  GLU B O   1 
ATOM   1187 C  CB  . GLU B 1 41  ? 25.114 26.103 -22.479 1.00 38.59 ? 37  GLU B CB  1 
ATOM   1188 C  CG  . GLU B 1 41  ? 26.384 25.425 -22.952 1.00 41.46 ? 37  GLU B CG  1 
ATOM   1189 C  CD  . GLU B 1 41  ? 26.116 24.078 -23.573 1.00 39.23 ? 37  GLU B CD  1 
ATOM   1190 O  OE1 . GLU B 1 41  ? 24.931 23.709 -23.704 1.00 46.31 ? 37  GLU B OE1 1 
ATOM   1191 O  OE2 . GLU B 1 41  ? 27.095 23.381 -23.911 1.00 49.65 ? 37  GLU B OE2 1 
ATOM   1192 N  N   . LEU B 1 42  ? 23.393 28.144 -20.438 1.00 30.07 ? 38  LEU B N   1 
ATOM   1193 C  CA  . LEU B 1 42  ? 22.097 28.806 -20.410 1.00 30.77 ? 38  LEU B CA  1 
ATOM   1194 C  C   . LEU B 1 42  ? 21.913 29.613 -19.133 1.00 38.66 ? 38  LEU B C   1 
ATOM   1195 O  O   . LEU B 1 42  ? 21.649 30.819 -19.189 1.00 33.79 ? 38  LEU B O   1 
ATOM   1196 C  CB  . LEU B 1 42  ? 20.977 27.774 -20.550 1.00 33.26 ? 38  LEU B CB  1 
ATOM   1197 C  CG  . LEU B 1 42  ? 19.526 28.215 -20.319 1.00 39.00 ? 38  LEU B CG  1 
ATOM   1198 C  CD1 . LEU B 1 42  ? 19.011 29.050 -21.469 1.00 41.18 ? 38  LEU B CD1 1 
ATOM   1199 C  CD2 . LEU B 1 42  ? 18.629 27.014 -20.106 1.00 42.23 ? 38  LEU B CD2 1 
ATOM   1200 N  N   . ILE B 1 43  ? 22.065 28.960 -17.979 1.00 30.49 ? 39  ILE B N   1 
ATOM   1201 C  CA  . ILE B 1 43  ? 21.590 29.550 -16.728 1.00 26.82 ? 39  ILE B CA  1 
ATOM   1202 C  C   . ILE B 1 43  ? 22.378 30.806 -16.386 1.00 30.71 ? 39  ILE B C   1 
ATOM   1203 O  O   . ILE B 1 43  ? 21.799 31.846 -16.046 1.00 31.47 ? 39  ILE B O   1 
ATOM   1204 C  CB  . ILE B 1 43  ? 21.642 28.518 -15.590 1.00 27.42 ? 39  ILE B CB  1 
ATOM   1205 C  CG1 . ILE B 1 43  ? 20.715 27.330 -15.904 1.00 23.93 ? 39  ILE B CG1 1 
ATOM   1206 C  CG2 . ILE B 1 43  ? 21.261 29.173 -14.279 1.00 24.28 ? 39  ILE B CG2 1 
ATOM   1207 C  CD1 . ILE B 1 43  ? 20.767 26.213 -14.855 1.00 27.76 ? 39  ILE B CD1 1 
ATOM   1208 N  N   . ARG B 1 44  ? 23.707 30.743 -16.480 1.00 24.71 ? 40  ARG B N   1 
ATOM   1209 C  CA  . ARG B 1 44  ? 24.506 31.902 -16.104 1.00 25.91 ? 40  ARG B CA  1 
ATOM   1210 C  C   . ARG B 1 44  ? 24.203 33.136 -16.947 1.00 26.82 ? 40  ARG B C   1 
ATOM   1211 O  O   . ARG B 1 44  ? 24.631 34.235 -16.574 1.00 29.83 ? 40  ARG B O   1 
ATOM   1212 C  CB  . ARG B 1 44  ? 26.008 31.590 -16.213 1.00 33.07 ? 40  ARG B CB  1 
ATOM   1213 C  CG  . ARG B 1 44  ? 26.531 31.581 -17.652 1.00 32.18 ? 40  ARG B CG  1 
ATOM   1214 C  CD  . ARG B 1 44  ? 28.068 31.532 -17.711 1.00 39.90 ? 40  ARG B CD  1 
ATOM   1215 N  NE  . ARG B 1 44  ? 28.575 30.304 -17.109 1.00 37.83 ? 40  ARG B NE  1 
ATOM   1216 C  CZ  . ARG B 1 44  ? 29.863 30.028 -16.905 1.00 41.57 ? 40  ARG B CZ  1 
ATOM   1217 N  NH1 . ARG B 1 44  ? 30.803 30.892 -17.263 1.00 39.14 ? 40  ARG B NH1 1 
ATOM   1218 N  NH2 . ARG B 1 44  ? 30.208 28.881 -16.335 1.00 32.71 ? 40  ARG B NH2 1 
ATOM   1219 N  N   . HIS B 1 45  ? 23.506 32.995 -18.069 1.00 27.11 ? 41  HIS B N   1 
ATOM   1220 C  CA  . HIS B 1 45  ? 23.287 34.131 -18.952 1.00 35.31 ? 41  HIS B CA  1 
ATOM   1221 C  C   . HIS B 1 45  ? 21.905 34.739 -18.795 1.00 36.67 ? 41  HIS B C   1 
ATOM   1222 O  O   . HIS B 1 45  ? 21.576 35.682 -19.517 1.00 31.64 ? 41  HIS B O   1 
ATOM   1223 C  CB  . HIS B 1 45  ? 23.519 33.720 -20.410 1.00 37.21 ? 41  HIS B CB  1 
ATOM   1224 C  CG  . HIS B 1 45  ? 24.895 33.183 -20.658 1.00 41.13 ? 41  HIS B CG  1 
ATOM   1225 N  ND1 . HIS B 1 45  ? 25.124 31.895 -21.092 1.00 42.30 ? 41  HIS B ND1 1 
ATOM   1226 C  CD2 . HIS B 1 45  ? 26.114 33.747 -20.489 1.00 30.03 ? 41  HIS B CD2 1 
ATOM   1227 C  CE1 . HIS B 1 45  ? 26.425 31.691 -21.191 1.00 34.22 ? 41  HIS B CE1 1 
ATOM   1228 N  NE2 . HIS B 1 45  ? 27.048 32.801 -20.834 1.00 48.54 ? 41  HIS B NE2 1 
ATOM   1229 N  N   . ARG B 1 46  ? 21.100 34.226 -17.867 1.00 32.26 ? 42  ARG B N   1 
ATOM   1230 C  CA  . ARG B 1 46  ? 19.744 34.721 -17.677 1.00 29.55 ? 42  ARG B CA  1 
ATOM   1231 C  C   . ARG B 1 46  ? 19.763 36.083 -16.991 1.00 24.32 ? 42  ARG B C   1 
ATOM   1232 O  O   . ARG B 1 46  ? 20.629 36.358 -16.157 1.00 23.83 ? 42  ARG B O   1 
ATOM   1233 C  CB  . ARG B 1 46  ? 18.920 33.736 -16.842 1.00 28.20 ? 42  ARG B CB  1 
ATOM   1234 C  CG  . ARG B 1 46  ? 18.601 32.430 -17.533 1.00 28.48 ? 42  ARG B CG  1 
ATOM   1235 C  CD  . ARG B 1 46  ? 17.607 32.626 -18.675 1.00 34.87 ? 42  ARG B CD  1 
ATOM   1236 N  NE  . ARG B 1 46  ? 16.534 33.557 -18.312 1.00 38.25 ? 42  ARG B NE  1 
ATOM   1237 C  CZ  . ARG B 1 46  ? 15.397 33.710 -18.990 1.00 38.69 ? 42  ARG B CZ  1 
ATOM   1238 N  NH1 . ARG B 1 46  ? 15.162 32.992 -20.088 1.00 35.29 ? 42  ARG B NH1 1 
ATOM   1239 N  NH2 . ARG B 1 46  ? 14.496 34.593 -18.575 1.00 31.77 ? 42  ARG B NH2 1 
ATOM   1240 N  N   . PRO B 1 47  ? 18.830 36.965 -17.339 1.00 27.16 ? 43  PRO B N   1 
ATOM   1241 C  CA  . PRO B 1 47  ? 18.724 38.231 -16.607 1.00 23.26 ? 43  PRO B CA  1 
ATOM   1242 C  C   . PRO B 1 47  ? 18.489 37.968 -15.125 1.00 23.13 ? 43  PRO B C   1 
ATOM   1243 O  O   . PRO B 1 47  ? 17.722 37.082 -14.749 1.00 29.66 ? 43  PRO B O   1 
ATOM   1244 C  CB  . PRO B 1 47  ? 17.515 38.924 -17.260 1.00 25.54 ? 43  PRO B CB  1 
ATOM   1245 C  CG  . PRO B 1 47  ? 17.406 38.295 -18.617 1.00 34.80 ? 43  PRO B CG  1 
ATOM   1246 C  CD  . PRO B 1 47  ? 17.834 36.857 -18.425 1.00 24.48 ? 43  PRO B CD  1 
ATOM   1247 N  N   . GLY B 1 48  ? 19.175 38.732 -14.284 1.00 24.97 ? 44  GLY B N   1 
ATOM   1248 C  CA  . GLY B 1 48  ? 19.013 38.584 -12.855 1.00 24.09 ? 44  GLY B CA  1 
ATOM   1249 C  C   . GLY B 1 48  ? 19.749 37.420 -12.224 1.00 28.05 ? 44  GLY B C   1 
ATOM   1250 O  O   . GLY B 1 48  ? 19.704 37.284 -10.995 1.00 23.57 ? 44  GLY B O   1 
ATOM   1251 N  N   . TYR B 1 49  ? 20.409 36.573 -13.013 1.00 27.48 ? 45  TYR B N   1 
ATOM   1252 C  CA  . TYR B 1 49  ? 21.255 35.524 -12.455 1.00 27.79 ? 45  TYR B CA  1 
ATOM   1253 C  C   . TYR B 1 49  ? 22.315 36.131 -11.552 1.00 30.41 ? 45  TYR B C   1 
ATOM   1254 O  O   . TYR B 1 49  ? 22.903 37.164 -11.873 1.00 27.52 ? 45  TYR B O   1 
ATOM   1255 C  CB  . TYR B 1 49  ? 21.915 34.729 -13.586 1.00 23.70 ? 45  TYR B CB  1 
ATOM   1256 C  CG  . TYR B 1 49  ? 23.097 33.843 -13.177 1.00 28.20 ? 45  TYR B CG  1 
ATOM   1257 C  CD1 . TYR B 1 49  ? 22.898 32.557 -12.695 1.00 28.54 ? 45  TYR B CD1 1 
ATOM   1258 C  CD2 . TYR B 1 49  ? 24.406 34.291 -13.310 1.00 30.86 ? 45  TYR B CD2 1 
ATOM   1259 C  CE1 . TYR B 1 49  ? 23.977 31.740 -12.341 1.00 26.00 ? 45  TYR B CE1 1 
ATOM   1260 C  CE2 . TYR B 1 49  ? 25.494 33.485 -12.958 1.00 28.45 ? 45  TYR B CE2 1 
ATOM   1261 C  CZ  . TYR B 1 49  ? 25.268 32.216 -12.474 1.00 33.34 ? 45  TYR B CZ  1 
ATOM   1262 O  OH  . TYR B 1 49  ? 26.333 31.422 -12.143 1.00 29.66 ? 45  TYR B OH  1 
ATOM   1263 N  N   . VAL B 1 50  ? 22.573 35.492 -10.405 1.00 26.63 ? 46  VAL B N   1 
ATOM   1264 C  CA  . VAL B 1 50  ? 23.667 35.898 -9.535  1.00 24.79 ? 46  VAL B CA  1 
ATOM   1265 C  C   . VAL B 1 50  ? 24.703 34.786 -9.362  1.00 30.22 ? 46  VAL B C   1 
ATOM   1266 O  O   . VAL B 1 50  ? 25.899 35.013 -9.554  1.00 27.79 ? 46  VAL B O   1 
ATOM   1267 C  CB  . VAL B 1 50  ? 23.164 36.404 -8.170  1.00 28.36 ? 46  VAL B CB  1 
ATOM   1268 C  CG1 . VAL B 1 50  ? 24.339 36.585 -7.234  1.00 28.51 ? 46  VAL B CG1 1 
ATOM   1269 C  CG2 . VAL B 1 50  ? 22.453 37.741 -8.345  1.00 29.59 ? 46  VAL B CG2 1 
ATOM   1270 N  N   . SER B 1 51  ? 24.266 33.580 -8.998  1.00 26.16 ? 47  SER B N   1 
ATOM   1271 C  CA  . SER B 1 51  ? 25.249 32.497 -8.912  1.00 28.19 ? 47  SER B CA  1 
ATOM   1272 C  C   . SER B 1 51  ? 24.595 31.143 -9.122  1.00 32.84 ? 47  SER B C   1 
ATOM   1273 O  O   . SER B 1 51  ? 23.374 30.987 -9.017  1.00 24.47 ? 47  SER B O   1 
ATOM   1274 C  CB  . SER B 1 51  ? 25.997 32.502 -7.577  1.00 29.92 ? 47  SER B CB  1 
ATOM   1275 O  OG  . SER B 1 51  ? 25.146 32.124 -6.510  1.00 27.12 ? 47  SER B OG  1 
ATOM   1276 N  N   . GLY B 1 52  ? 25.438 30.166 -9.449  1.00 23.78 ? 48  GLY B N   1 
ATOM   1277 C  CA  . GLY B 1 52  ? 25.025 28.778 -9.552  1.00 31.01 ? 48  GLY B CA  1 
ATOM   1278 C  C   . GLY B 1 52  ? 26.087 27.885 -8.945  1.00 31.41 ? 48  GLY B C   1 
ATOM   1279 O  O   . GLY B 1 52  ? 27.283 28.122 -9.167  1.00 28.81 ? 48  GLY B O   1 
ATOM   1280 N  N   . ASN B 1 53  ? 25.674 26.881 -8.162  1.00 30.52 ? 49  ASN B N   1 
ATOM   1281 C  CA  . ASN B 1 53  ? 26.604 26.081 -7.356  1.00 28.66 ? 49  ASN B CA  1 
ATOM   1282 C  C   . ASN B 1 53  ? 26.074 24.660 -7.254  1.00 27.84 ? 49  ASN B C   1 
ATOM   1283 O  O   . ASN B 1 53  ? 25.094 24.421 -6.548  1.00 28.27 ? 49  ASN B O   1 
ATOM   1284 C  CB  . ASN B 1 53  ? 26.780 26.670 -5.967  1.00 24.80 ? 49  ASN B CB  1 
ATOM   1285 C  CG  . ASN B 1 53  ? 26.968 28.150 -5.989  1.00 33.33 ? 49  ASN B CG  1 
ATOM   1286 O  OD1 . ASN B 1 53  ? 28.096 28.636 -5.985  1.00 33.26 ? 49  ASN B OD1 1 
ATOM   1287 N  ND2 . ASN B 1 53  ? 25.860 28.891 -6.020  1.00 34.72 ? 49  ASN B ND2 1 
ATOM   1288 N  N   . VAL B 1 54  ? 26.739 23.722 -7.918  1.00 26.34 ? 50  VAL B N   1 
ATOM   1289 C  CA  . VAL B 1 54  ? 26.247 22.358 -8.056  1.00 28.30 ? 50  VAL B CA  1 
ATOM   1290 C  C   . VAL B 1 54  ? 26.984 21.451 -7.078  1.00 31.66 ? 50  VAL B C   1 
ATOM   1291 O  O   . VAL B 1 54  ? 28.221 21.427 -7.047  1.00 29.58 ? 50  VAL B O   1 
ATOM   1292 C  CB  . VAL B 1 54  ? 26.402 21.872 -9.504  1.00 34.75 ? 50  VAL B CB  1 
ATOM   1293 C  CG1 . VAL B 1 54  ? 25.912 20.431 -9.651  1.00 28.31 ? 50  VAL B CG1 1 
ATOM   1294 C  CG2 . VAL B 1 54  ? 25.654 22.828 -10.436 1.00 30.56 ? 50  VAL B CG2 1 
ATOM   1295 N  N   . HIS B 1 55  ? 26.226 20.716 -6.270  1.00 26.54 ? 51  HIS B N   1 
ATOM   1296 C  CA  . HIS B 1 55  ? 26.772 19.870 -5.218  1.00 24.85 ? 51  HIS B CA  1 
ATOM   1297 C  C   . HIS B 1 55  ? 26.381 18.426 -5.489  1.00 30.31 ? 51  HIS B C   1 
ATOM   1298 O  O   . HIS B 1 55  ? 25.217 18.138 -5.789  1.00 30.22 ? 51  HIS B O   1 
ATOM   1299 C  CB  . HIS B 1 55  ? 26.249 20.279 -3.834  1.00 27.35 ? 51  HIS B CB  1 
ATOM   1300 C  CG  . HIS B 1 55  ? 26.568 21.690 -3.443  1.00 31.70 ? 51  HIS B CG  1 
ATOM   1301 N  ND1 . HIS B 1 55  ? 25.995 22.788 -4.056  1.00 28.77 ? 51  HIS B ND1 1 
ATOM   1302 C  CD2 . HIS B 1 55  ? 27.372 22.179 -2.470  1.00 27.71 ? 51  HIS B CD2 1 
ATOM   1303 C  CE1 . HIS B 1 55  ? 26.454 23.891 -3.494  1.00 29.05 ? 51  HIS B CE1 1 
ATOM   1304 N  NE2 . HIS B 1 55  ? 27.287 23.550 -2.524  1.00 28.87 ? 51  HIS B NE2 1 
ATOM   1305 N  N   . ARG B 1 56  ? 27.351 17.523 -5.352  1.00 29.44 ? 52  ARG B N   1 
ATOM   1306 C  CA  . ARG B 1 56  ? 27.174 16.097 -5.602  1.00 26.61 ? 52  ARG B CA  1 
ATOM   1307 C  C   . ARG B 1 56  ? 27.276 15.356 -4.271  1.00 25.58 ? 52  ARG B C   1 
ATOM   1308 O  O   . ARG B 1 56  ? 28.306 15.432 -3.602  1.00 25.85 ? 52  ARG B O   1 
ATOM   1309 C  CB  . ARG B 1 56  ? 28.237 15.616 -6.596  1.00 32.22 ? 52  ARG B CB  1 
ATOM   1310 C  CG  . ARG B 1 56  ? 28.211 14.128 -6.945  1.00 34.01 ? 52  ARG B CG  1 
ATOM   1311 C  CD  . ARG B 1 56  ? 29.451 13.717 -7.747  1.00 31.19 ? 52  ARG B CD  1 
ATOM   1312 N  NE  . ARG B 1 56  ? 30.681 13.936 -6.988  1.00 30.26 ? 52  ARG B NE  1 
ATOM   1313 C  CZ  . ARG B 1 56  ? 31.852 14.263 -7.524  1.00 34.78 ? 52  ARG B CZ  1 
ATOM   1314 N  NH1 . ARG B 1 56  ? 31.974 14.395 -8.845  1.00 27.51 ? 52  ARG B NH1 1 
ATOM   1315 N  NH2 . ARG B 1 56  ? 32.905 14.453 -6.737  1.00 31.53 ? 52  ARG B NH2 1 
ATOM   1316 N  N   . SER B 1 57  ? 26.210 14.658 -3.872  1.00 25.05 ? 53  SER B N   1 
ATOM   1317 C  CA  . SER B 1 57  ? 26.261 13.930 -2.609  1.00 31.02 ? 53  SER B CA  1 
ATOM   1318 C  C   . SER B 1 57  ? 27.318 12.833 -2.696  1.00 29.08 ? 53  SER B C   1 
ATOM   1319 O  O   . SER B 1 57  ? 27.424 12.127 -3.698  1.00 29.38 ? 53  SER B O   1 
ATOM   1320 C  CB  . SER B 1 57  ? 24.890 13.329 -2.267  1.00 30.85 ? 53  SER B CB  1 
ATOM   1321 O  OG  . SER B 1 57  ? 24.571 12.231 -3.100  1.00 32.50 ? 53  SER B OG  1 
ATOM   1322 N  N   . VAL B 1 58  ? 28.136 12.712 -1.650  1.00 31.28 ? 54  VAL B N   1 
ATOM   1323 C  CA  . VAL B 1 58  ? 29.214 11.725 -1.685  1.00 26.17 ? 54  VAL B CA  1 
ATOM   1324 C  C   . VAL B 1 58  ? 28.692 10.301 -1.773  1.00 29.46 ? 54  VAL B C   1 
ATOM   1325 O  O   . VAL B 1 58  ? 29.416 9.420  -2.243  1.00 30.21 ? 54  VAL B O   1 
ATOM   1326 C  CB  . VAL B 1 58  ? 30.129 11.862 -0.460  1.00 23.67 ? 54  VAL B CB  1 
ATOM   1327 C  CG1 . VAL B 1 58  ? 30.749 13.251 -0.415  1.00 25.21 ? 54  VAL B CG1 1 
ATOM   1328 C  CG2 . VAL B 1 58  ? 29.360 11.528 0.786   1.00 22.46 ? 54  VAL B CG2 1 
ATOM   1329 N  N   . ASP B 1 59  ? 27.443 10.050 -1.343  1.00 27.66 ? 55  ASP B N   1 
ATOM   1330 C  CA  . ASP B 1 59  ? 26.859 8.709  -1.379  1.00 32.84 ? 55  ASP B CA  1 
ATOM   1331 C  C   . ASP B 1 59  ? 26.229 8.352  -2.724  1.00 35.93 ? 55  ASP B C   1 
ATOM   1332 O  O   . ASP B 1 59  ? 25.768 7.219  -2.899  1.00 31.86 ? 55  ASP B O   1 
ATOM   1333 C  CB  . ASP B 1 59  ? 25.820 8.552  -0.253  1.00 32.31 ? 55  ASP B CB  1 
ATOM   1334 C  CG  . ASP B 1 59  ? 24.570 9.401  -0.464  1.00 40.89 ? 55  ASP B CG  1 
ATOM   1335 O  OD1 . ASP B 1 59  ? 24.438 10.071 -1.510  1.00 35.13 ? 55  ASP B OD1 1 
ATOM   1336 O  OD2 . ASP B 1 59  ? 23.697 9.401  0.436   1.00 38.38 ? 55  ASP B OD2 1 
ATOM   1337 N  N   . GLY B 1 60  ? 26.170 9.284  -3.668  1.00 29.75 ? 56  GLY B N   1 
ATOM   1338 C  CA  . GLY B 1 60  ? 25.677 8.988  -4.993  1.00 28.23 ? 56  GLY B CA  1 
ATOM   1339 C  C   . GLY B 1 60  ? 24.183 9.149  -5.227  1.00 28.87 ? 56  GLY B C   1 
ATOM   1340 O  O   . GLY B 1 60  ? 23.739 8.953  -6.364  1.00 34.10 ? 56  GLY B O   1 
ATOM   1341 N  N   . TYR B 1 61  ? 23.391 9.509  -4.216  1.00 29.27 ? 57  TYR B N   1 
ATOM   1342 C  CA  . TYR B 1 61  ? 21.931 9.513  -4.365  1.00 33.46 ? 57  TYR B CA  1 
ATOM   1343 C  C   . TYR B 1 61  ? 21.308 10.897 -4.535  1.00 39.03 ? 57  TYR B C   1 
ATOM   1344 O  O   . TYR B 1 61  ? 20.088 10.983 -4.692  1.00 35.68 ? 57  TYR B O   1 
ATOM   1345 C  CB  . TYR B 1 61  ? 21.260 8.818  -3.170  1.00 41.94 ? 57  TYR B CB  1 
ATOM   1346 C  CG  . TYR B 1 61  ? 21.362 7.317  -3.232  1.00 45.25 ? 57  TYR B CG  1 
ATOM   1347 C  CD1 . TYR B 1 61  ? 20.455 6.566  -3.975  1.00 45.52 ? 57  TYR B CD1 1 
ATOM   1348 C  CD2 . TYR B 1 61  ? 22.387 6.649  -2.574  1.00 39.85 ? 57  TYR B CD2 1 
ATOM   1349 C  CE1 . TYR B 1 61  ? 20.559 5.182  -4.045  1.00 43.98 ? 57  TYR B CE1 1 
ATOM   1350 C  CE2 . TYR B 1 61  ? 22.503 5.267  -2.645  1.00 43.77 ? 57  TYR B CE2 1 
ATOM   1351 C  CZ  . TYR B 1 61  ? 21.586 4.539  -3.377  1.00 44.06 ? 57  TYR B CZ  1 
ATOM   1352 O  OH  . TYR B 1 61  ? 21.706 3.167  -3.440  1.00 46.31 ? 57  TYR B OH  1 
ATOM   1353 N  N   . GLN B 1 62  ? 22.089 11.973 -4.522  1.00 37.23 ? 58  GLN B N   1 
ATOM   1354 C  CA  . GLN B 1 62  ? 21.491 13.302 -4.564  1.00 31.15 ? 58  GLN B CA  1 
ATOM   1355 C  C   . GLN B 1 62  ? 22.421 14.295 -5.257  1.00 37.30 ? 58  GLN B C   1 
ATOM   1356 O  O   . GLN B 1 62  ? 23.643 14.237 -5.092  1.00 30.40 ? 58  GLN B O   1 
ATOM   1357 C  CB  . GLN B 1 62  ? 21.161 13.782 -3.146  1.00 29.56 ? 58  GLN B CB  1 
ATOM   1358 C  CG  . GLN B 1 62  ? 20.324 15.059 -3.089  1.00 41.47 ? 58  GLN B CG  1 
ATOM   1359 C  CD  . GLN B 1 62  ? 18.894 14.799 -2.632  1.00 52.98 ? 58  GLN B CD  1 
ATOM   1360 O  OE1 . GLN B 1 62  ? 18.561 13.702 -2.184  1.00 54.60 ? 58  GLN B OE1 1 
ATOM   1361 N  NE2 . GLN B 1 62  ? 18.043 15.807 -2.755  1.00 45.21 ? 58  GLN B NE2 1 
ATOM   1362 N  N   . VAL B 1 63  ? 21.834 15.193 -6.049  1.00 33.67 ? 59  VAL B N   1 
ATOM   1363 C  CA  . VAL B 1 63  ? 22.517 16.380 -6.556  1.00 29.63 ? 59  VAL B CA  1 
ATOM   1364 C  C   . VAL B 1 63  ? 21.720 17.593 -6.099  1.00 30.38 ? 59  VAL B C   1 
ATOM   1365 O  O   . VAL B 1 63  ? 20.484 17.575 -6.120  1.00 30.61 ? 59  VAL B O   1 
ATOM   1366 C  CB  . VAL B 1 63  ? 22.662 16.353 -8.092  1.00 35.65 ? 59  VAL B CB  1 
ATOM   1367 C  CG1 . VAL B 1 63  ? 23.448 17.562 -8.598  1.00 28.05 ? 59  VAL B CG1 1 
ATOM   1368 C  CG2 . VAL B 1 63  ? 23.329 15.074 -8.534  1.00 28.32 ? 59  VAL B CG2 1 
ATOM   1369 N  N   . VAL B 1 64  ? 22.418 18.628 -5.645  1.00 29.05 ? 60  VAL B N   1 
ATOM   1370 C  CA  . VAL B 1 64  ? 21.772 19.835 -5.134  1.00 27.58 ? 60  VAL B CA  1 
ATOM   1371 C  C   . VAL B 1 64  ? 22.330 21.029 -5.901  1.00 29.81 ? 60  VAL B C   1 
ATOM   1372 O  O   . VAL B 1 64  ? 23.548 21.243 -5.920  1.00 30.15 ? 60  VAL B O   1 
ATOM   1373 C  CB  . VAL B 1 64  ? 21.988 19.999 -3.623  1.00 26.12 ? 60  VAL B CB  1 
ATOM   1374 C  CG1 . VAL B 1 64  ? 21.433 21.322 -3.142  1.00 27.41 ? 60  VAL B CG1 1 
ATOM   1375 C  CG2 . VAL B 1 64  ? 21.341 18.854 -2.865  1.00 33.48 ? 60  VAL B CG2 1 
ATOM   1376 N  N   . ASP B 1 65  ? 21.446 21.798 -6.533  1.00 27.96 ? 61  ASP B N   1 
ATOM   1377 C  CA  . ASP B 1 65  ? 21.813 23.047 -7.201  1.00 27.02 ? 61  ASP B CA  1 
ATOM   1378 C  C   . ASP B 1 65  ? 21.379 24.207 -6.317  1.00 29.42 ? 61  ASP B C   1 
ATOM   1379 O  O   . ASP B 1 65  ? 20.183 24.438 -6.124  1.00 31.07 ? 61  ASP B O   1 
ATOM   1380 C  CB  . ASP B 1 65  ? 21.179 23.161 -8.588  1.00 34.66 ? 61  ASP B CB  1 
ATOM   1381 C  CG  . ASP B 1 65  ? 21.700 24.375 -9.381  1.00 34.41 ? 61  ASP B CG  1 
ATOM   1382 O  OD1 . ASP B 1 65  ? 22.700 25.000 -8.960  1.00 38.71 ? 61  ASP B OD1 1 
ATOM   1383 O  OD2 . ASP B 1 65  ? 21.111 24.698 -10.430 1.00 47.16 ? 61  ASP B OD2 1 
ATOM   1384 N  N   . TYR B 1 66  ? 22.359 24.920 -5.777  1.00 26.69 ? 62  TYR B N   1 
ATOM   1385 C  CA  . TYR B 1 66  ? 22.147 26.112 -4.972  1.00 25.90 ? 62  TYR B CA  1 
ATOM   1386 C  C   . TYR B 1 66  ? 22.370 27.309 -5.887  1.00 32.74 ? 62  TYR B C   1 
ATOM   1387 O  O   . TYR B 1 66  ? 23.490 27.528 -6.353  1.00 24.10 ? 62  TYR B O   1 
ATOM   1388 C  CB  . TYR B 1 66  ? 23.127 26.124 -3.806  1.00 23.50 ? 62  TYR B CB  1 
ATOM   1389 C  CG  . TYR B 1 66  ? 22.910 27.192 -2.757  1.00 25.10 ? 62  TYR B CG  1 
ATOM   1390 C  CD1 . TYR B 1 66  ? 22.298 26.876 -1.553  1.00 28.85 ? 62  TYR B CD1 1 
ATOM   1391 C  CD2 . TYR B 1 66  ? 23.366 28.499 -2.942  1.00 26.13 ? 62  TYR B CD2 1 
ATOM   1392 C  CE1 . TYR B 1 66  ? 22.113 27.828 -0.563  1.00 24.53 ? 62  TYR B CE1 1 
ATOM   1393 C  CE2 . TYR B 1 66  ? 23.167 29.480 -1.954  1.00 24.21 ? 62  TYR B CE2 1 
ATOM   1394 C  CZ  . TYR B 1 66  ? 22.545 29.123 -0.764  1.00 23.29 ? 62  TYR B CZ  1 
ATOM   1395 O  OH  . TYR B 1 66  ? 22.354 30.050 0.240   1.00 27.79 ? 62  TYR B OH  1 
ATOM   1396 N  N   . THR B 1 67  ? 21.320 28.089 -6.145  1.00 27.69 ? 63  THR B N   1 
ATOM   1397 C  CA  . THR B 1 67  ? 21.425 29.170 -7.116  1.00 22.30 ? 63  THR B CA  1 
ATOM   1398 C  C   . THR B 1 67  ? 20.849 30.464 -6.548  1.00 26.34 ? 63  THR B C   1 
ATOM   1399 O  O   . THR B 1 67  ? 19.858 30.441 -5.816  1.00 28.08 ? 63  THR B O   1 
ATOM   1400 C  CB  . THR B 1 67  ? 20.728 28.733 -8.434  1.00 27.88 ? 63  THR B CB  1 
ATOM   1401 O  OG1 . THR B 1 67  ? 21.164 29.551 -9.517  1.00 39.78 ? 63  THR B OG1 1 
ATOM   1402 C  CG2 . THR B 1 67  ? 19.231 28.763 -8.316  1.00 23.82 ? 63  THR B CG2 1 
ATOM   1403 N  N   . GLN B 1 68  ? 21.502 31.597 -6.846  1.00 21.51 ? 64  GLN B N   1 
ATOM   1404 C  CA  . GLN B 1 68  ? 21.083 32.895 -6.342  1.00 20.80 ? 64  GLN B CA  1 
ATOM   1405 C  C   . GLN B 1 68  ? 20.674 33.796 -7.502  1.00 27.48 ? 64  GLN B C   1 
ATOM   1406 O  O   . GLN B 1 68  ? 21.212 33.703 -8.609  1.00 25.43 ? 64  GLN B O   1 
ATOM   1407 C  CB  . GLN B 1 68  ? 22.180 33.576 -5.532  1.00 25.24 ? 64  GLN B CB  1 
ATOM   1408 C  CG  . GLN B 1 68  ? 22.660 32.792 -4.335  1.00 29.49 ? 64  GLN B CG  1 
ATOM   1409 C  CD  . GLN B 1 68  ? 23.889 33.423 -3.727  1.00 33.03 ? 64  GLN B CD  1 
ATOM   1410 O  OE1 . GLN B 1 68  ? 24.835 33.746 -4.441  1.00 28.07 ? 64  GLN B OE1 1 
ATOM   1411 N  NE2 . GLN B 1 68  ? 23.868 33.637 -2.409  1.00 24.02 ? 64  GLN B NE2 1 
ATOM   1412 N  N   . TRP B 1 69  ? 19.708 34.661 -7.233  1.00 25.58 ? 65  TRP B N   1 
ATOM   1413 C  CA  . TRP B 1 69  ? 19.047 35.454 -8.261  1.00 24.50 ? 65  TRP B CA  1 
ATOM   1414 C  C   . TRP B 1 69  ? 18.665 36.781 -7.635  1.00 26.92 ? 65  TRP B C   1 
ATOM   1415 O  O   . TRP B 1 69  ? 18.498 36.890 -6.415  1.00 28.31 ? 65  TRP B O   1 
ATOM   1416 C  CB  . TRP B 1 69  ? 17.785 34.749 -8.814  1.00 24.47 ? 65  TRP B CB  1 
ATOM   1417 C  CG  . TRP B 1 69  ? 18.068 33.468 -9.480  1.00 25.51 ? 65  TRP B CG  1 
ATOM   1418 C  CD1 . TRP B 1 69  ? 18.250 32.254 -8.879  1.00 26.58 ? 65  TRP B CD1 1 
ATOM   1419 C  CD2 . TRP B 1 69  ? 18.216 33.250 -10.887 1.00 25.20 ? 65  TRP B CD2 1 
ATOM   1420 N  NE1 . TRP B 1 69  ? 18.503 31.296 -9.830  1.00 30.29 ? 65  TRP B NE1 1 
ATOM   1421 C  CE2 . TRP B 1 69  ? 18.499 31.881 -11.068 1.00 24.72 ? 65  TRP B CE2 1 
ATOM   1422 C  CE3 . TRP B 1 69  ? 18.146 34.082 -12.014 1.00 24.28 ? 65  TRP B CE3 1 
ATOM   1423 C  CZ2 . TRP B 1 69  ? 18.695 31.317 -12.328 1.00 20.44 ? 65  TRP B CZ2 1 
ATOM   1424 C  CZ3 . TRP B 1 69  ? 18.353 33.519 -13.272 1.00 21.53 ? 65  TRP B CZ3 1 
ATOM   1425 C  CH2 . TRP B 1 69  ? 18.641 32.157 -13.415 1.00 22.61 ? 65  TRP B CH2 1 
ATOM   1426 N  N   . ARG B 1 70  ? 18.502 37.794 -8.480  1.00 24.37 ? 66  ARG B N   1 
ATOM   1427 C  CA  . ARG B 1 70  ? 18.097 39.092 -7.956  1.00 28.46 ? 66  ARG B CA  1 
ATOM   1428 C  C   . ARG B 1 70  ? 16.666 39.046 -7.423  1.00 25.87 ? 66  ARG B C   1 
ATOM   1429 O  O   . ARG B 1 70  ? 16.354 39.665 -6.400  1.00 32.52 ? 66  ARG B O   1 
ATOM   1430 C  CB  . ARG B 1 70  ? 18.248 40.157 -9.044  1.00 35.15 ? 66  ARG B CB  1 
ATOM   1431 C  CG  . ARG B 1 70  ? 19.690 40.314 -9.530  1.00 30.71 ? 66  ARG B CG  1 
ATOM   1432 C  CD  . ARG B 1 70  ? 20.114 41.756 -9.480  1.00 42.50 ? 66  ARG B CD  1 
ATOM   1433 N  NE  . ARG B 1 70  ? 21.376 41.983 -10.172 1.00 41.56 ? 66  ARG B NE  1 
ATOM   1434 C  CZ  . ARG B 1 70  ? 22.501 42.343 -9.564  1.00 57.53 ? 66  ARG B CZ  1 
ATOM   1435 N  NH1 . ARG B 1 70  ? 23.611 42.546 -10.270 1.00 55.42 ? 66  ARG B NH1 1 
ATOM   1436 N  NH2 . ARG B 1 70  ? 22.517 42.497 -8.244  1.00 59.32 ? 66  ARG B NH2 1 
ATOM   1437 N  N   . ARG B 1 71  ? 15.783 38.329 -8.104  1.00 26.10 ? 67  ARG B N   1 
ATOM   1438 C  CA  . ARG B 1 71  ? 14.436 38.135 -7.582  1.00 27.14 ? 67  ARG B CA  1 
ATOM   1439 C  C   . ARG B 1 71  ? 13.981 36.746 -7.988  1.00 26.98 ? 67  ARG B C   1 
ATOM   1440 O  O   . ARG B 1 71  ? 14.471 36.179 -8.966  1.00 23.23 ? 67  ARG B O   1 
ATOM   1441 C  CB  . ARG B 1 71  ? 13.471 39.219 -8.091  1.00 31.80 ? 67  ARG B CB  1 
ATOM   1442 C  CG  . ARG B 1 71  ? 13.391 39.293 -9.597  1.00 35.61 ? 67  ARG B CG  1 
ATOM   1443 C  CD  . ARG B 1 71  ? 12.446 40.392 -10.081 1.00 36.69 ? 67  ARG B CD  1 
ATOM   1444 N  NE  . ARG B 1 71  ? 12.494 40.539 -11.540 1.00 36.93 ? 67  ARG B NE  1 
ATOM   1445 C  CZ  . ARG B 1 71  ? 11.524 41.096 -12.258 1.00 52.00 ? 67  ARG B CZ  1 
ATOM   1446 N  NH1 . ARG B 1 71  ? 11.639 41.213 -13.581 1.00 44.07 ? 67  ARG B NH1 1 
ATOM   1447 N  NH2 . ARG B 1 71  ? 10.429 41.532 -11.643 1.00 46.87 ? 67  ARG B NH2 1 
ATOM   1448 N  N   . ARG B 1 72  ? 13.040 36.189 -7.217  1.00 23.73 ? 68  ARG B N   1 
ATOM   1449 C  CA  . ARG B 1 72  ? 12.528 34.863 -7.538  1.00 26.42 ? 68  ARG B CA  1 
ATOM   1450 C  C   . ARG B 1 72  ? 11.985 34.804 -8.948  1.00 22.84 ? 68  ARG B C   1 
ATOM   1451 O  O   . ARG B 1 72  ? 12.027 33.745 -9.580  1.00 24.07 ? 68  ARG B O   1 
ATOM   1452 C  CB  . ARG B 1 72  ? 11.419 34.461 -6.569  1.00 27.61 ? 68  ARG B CB  1 
ATOM   1453 C  CG  . ARG B 1 72  ? 11.904 34.107 -5.182  1.00 35.34 ? 68  ARG B CG  1 
ATOM   1454 C  CD  . ARG B 1 72  ? 10.757 34.151 -4.191  1.00 37.69 ? 68  ARG B CD  1 
ATOM   1455 N  NE  . ARG B 1 72  ? 9.773  33.087 -4.394  1.00 32.82 ? 68  ARG B NE  1 
ATOM   1456 C  CZ  . ARG B 1 72  ? 8.623  33.021 -3.725  1.00 30.24 ? 68  ARG B CZ  1 
ATOM   1457 N  NH1 . ARG B 1 72  ? 8.331  33.955 -2.837  1.00 25.65 ? 68  ARG B NH1 1 
ATOM   1458 N  NH2 . ARG B 1 72  ? 7.777  32.030 -3.938  1.00 24.76 ? 68  ARG B NH2 1 
ATOM   1459 N  N   . GLU B 1 73  ? 11.446 35.923 -9.443  1.00 22.49 ? 69  GLU B N   1 
ATOM   1460 C  CA  . GLU B 1 73  ? 10.846 35.943 -10.771 1.00 26.79 ? 69  GLU B CA  1 
ATOM   1461 C  C   . GLU B 1 73  ? 11.869 35.668 -11.861 1.00 26.05 ? 69  GLU B C   1 
ATOM   1462 O  O   . GLU B 1 73  ? 11.499 35.213 -12.947 1.00 24.16 ? 69  GLU B O   1 
ATOM   1463 C  CB  . GLU B 1 73  ? 10.177 37.304 -11.020 1.00 23.61 ? 69  GLU B CB  1 
ATOM   1464 C  CG  . GLU B 1 73  ? 8.845  37.464 -10.264 1.00 30.14 ? 69  GLU B CG  1 
ATOM   1465 C  CD  . GLU B 1 73  ? 9.025  37.862 -8.806  1.00 32.66 ? 69  GLU B CD  1 
ATOM   1466 O  OE1 . GLU B 1 73  ? 10.172 38.120 -8.395  1.00 30.74 ? 69  GLU B OE1 1 
ATOM   1467 O  OE2 . GLU B 1 73  ? 8.014  37.932 -8.071  1.00 34.75 ? 69  GLU B OE2 1 
ATOM   1468 N  N   . ASP B 1 74  ? 13.143 35.947 -11.602 1.00 21.69 ? 70  ASP B N   1 
ATOM   1469 C  CA  . ASP B 1 74  ? 14.143 35.720 -12.636 1.00 26.25 ? 70  ASP B CA  1 
ATOM   1470 C  C   . ASP B 1 74  ? 14.347 34.229 -12.873 1.00 25.36 ? 70  ASP B C   1 
ATOM   1471 O  O   . ASP B 1 74  ? 14.429 33.787 -14.022 1.00 25.68 ? 70  ASP B O   1 
ATOM   1472 C  CB  . ASP B 1 74  ? 15.445 36.406 -12.250 1.00 24.63 ? 70  ASP B CB  1 
ATOM   1473 C  CG  . ASP B 1 74  ? 15.292 37.890 -12.138 1.00 29.83 ? 70  ASP B CG  1 
ATOM   1474 O  OD1 . ASP B 1 74  ? 14.459 38.461 -12.868 1.00 23.74 ? 70  ASP B OD1 1 
ATOM   1475 O  OD2 . ASP B 1 74  ? 16.000 38.492 -11.319 1.00 25.30 ? 70  ASP B OD2 1 
ATOM   1476 N  N   . PHE B 1 75  ? 14.402 33.438 -11.800 1.00 22.68 ? 71  PHE B N   1 
ATOM   1477 C  CA  . PHE B 1 75  ? 14.478 31.986 -11.952 1.00 21.11 ? 71  PHE B CA  1 
ATOM   1478 C  C   . PHE B 1 75  ? 13.221 31.440 -12.613 1.00 27.27 ? 71  PHE B C   1 
ATOM   1479 O  O   . PHE B 1 75  ? 13.297 30.587 -13.509 1.00 23.62 ? 71  PHE B O   1 
ATOM   1480 C  CB  . PHE B 1 75  ? 14.689 31.326 -10.589 1.00 21.34 ? 71  PHE B CB  1 
ATOM   1481 C  CG  . PHE B 1 75  ? 14.656 29.823 -10.631 1.00 27.45 ? 71  PHE B CG  1 
ATOM   1482 C  CD1 . PHE B 1 75  ? 15.827 29.104 -10.747 1.00 24.62 ? 71  PHE B CD1 1 
ATOM   1483 C  CD2 . PHE B 1 75  ? 13.451 29.124 -10.537 1.00 30.21 ? 71  PHE B CD2 1 
ATOM   1484 C  CE1 . PHE B 1 75  ? 15.808 27.723 -10.789 1.00 29.69 ? 71  PHE B CE1 1 
ATOM   1485 C  CE2 . PHE B 1 75  ? 13.428 27.741 -10.582 1.00 28.75 ? 71  PHE B CE2 1 
ATOM   1486 C  CZ  . PHE B 1 75  ? 14.613 27.043 -10.710 1.00 26.46 ? 71  PHE B CZ  1 
ATOM   1487 N  N   . GLU B 1 76  ? 12.051 31.924 -12.182 1.00 25.70 ? 72  GLU B N   1 
ATOM   1488 C  CA  . GLU B 1 76  ? 10.791 31.413 -12.715 1.00 25.99 ? 72  GLU B CA  1 
ATOM   1489 C  C   . GLU B 1 76  ? 10.650 31.719 -14.202 1.00 25.09 ? 72  GLU B C   1 
ATOM   1490 O  O   . GLU B 1 76  ? 10.204 30.863 -14.978 1.00 29.70 ? 72  GLU B O   1 
ATOM   1491 C  CB  . GLU B 1 76  ? 9.621  32.001 -11.918 1.00 27.09 ? 72  GLU B CB  1 
ATOM   1492 C  CG  . GLU B 1 76  ? 9.521  31.421 -10.495 1.00 28.72 ? 72  GLU B CG  1 
ATOM   1493 C  CD  . GLU B 1 76  ? 8.542  32.152 -9.590  1.00 31.73 ? 72  GLU B CD  1 
ATOM   1494 O  OE1 . GLU B 1 76  ? 8.138  33.299 -9.904  1.00 26.58 ? 72  GLU B OE1 1 
ATOM   1495 O  OE2 . GLU B 1 76  ? 8.191  31.573 -8.541  1.00 27.26 ? 72  GLU B OE2 1 
ATOM   1496 N  N   . ALA B 1 77  ? 11.012 32.940 -14.614 1.00 25.71 ? 73  ALA B N   1 
ATOM   1497 C  CA  . ALA B 1 77  ? 11.004 33.282 -16.038 1.00 24.90 ? 73  ALA B CA  1 
ATOM   1498 C  C   . ALA B 1 77  ? 11.836 32.289 -16.837 1.00 25.02 ? 73  ALA B C   1 
ATOM   1499 O  O   . ALA B 1 77  ? 11.411 31.812 -17.898 1.00 26.21 ? 73  ALA B O   1 
ATOM   1500 C  CB  . ALA B 1 77  ? 11.529 34.706 -16.239 1.00 21.33 ? 73  ALA B CB  1 
ATOM   1501 N  N   . MET B 1 78  ? 13.010 31.920 -16.309 1.00 28.52 ? 74  MET B N   1 
ATOM   1502 C  CA  . MET B 1 78  ? 13.865 30.967 -17.003 1.00 27.44 ? 74  MET B CA  1 
ATOM   1503 C  C   . MET B 1 78  ? 13.179 29.619 -17.157 1.00 27.49 ? 74  MET B C   1 
ATOM   1504 O  O   . MET B 1 78  ? 13.250 28.989 -18.218 1.00 28.90 ? 74  MET B O   1 
ATOM   1505 C  CB  . MET B 1 78  ? 15.186 30.812 -16.249 1.00 25.61 ? 74  MET B CB  1 
ATOM   1506 C  CG  . MET B 1 78  ? 16.048 29.670 -16.790 1.00 28.82 ? 74  MET B CG  1 
ATOM   1507 S  SD  . MET B 1 78  ? 17.516 29.314 -15.809 1.00 31.18 ? 74  MET B SD  1 
ATOM   1508 C  CE  . MET B 1 78  ? 16.797 28.763 -14.264 1.00 25.86 ? 74  MET B CE  1 
ATOM   1509 N  N   . VAL B 1 79  ? 12.512 29.153 -16.103 1.00 28.06 ? 75  VAL B N   1 
ATOM   1510 C  CA  . VAL B 1 79  ? 11.864 27.850 -16.167 1.00 24.29 ? 75  VAL B CA  1 
ATOM   1511 C  C   . VAL B 1 79  ? 10.697 27.869 -17.161 1.00 31.43 ? 75  VAL B C   1 
ATOM   1512 O  O   . VAL B 1 79  ? 10.455 26.875 -17.856 1.00 27.76 ? 75  VAL B O   1 
ATOM   1513 C  CB  . VAL B 1 79  ? 11.439 27.413 -14.751 1.00 24.93 ? 75  VAL B CB  1 
ATOM   1514 C  CG1 . VAL B 1 79  ? 10.392 26.311 -14.810 1.00 33.99 ? 75  VAL B CG1 1 
ATOM   1515 C  CG2 . VAL B 1 79  ? 12.678 26.933 -13.948 1.00 26.16 ? 75  VAL B CG2 1 
ATOM   1516 N  N   . ARG B 1 80  ? 9.989  29.002 -17.274 1.00 26.60 ? 76  ARG B N   1 
ATOM   1517 C  CA  . ARG B 1 80  ? 8.860  29.147 -18.198 1.00 27.18 ? 76  ARG B CA  1 
ATOM   1518 C  C   . ARG B 1 80  ? 9.289  29.346 -19.649 1.00 33.41 ? 76  ARG B C   1 
ATOM   1519 O  O   . ARG B 1 80  ? 8.454  29.212 -20.547 1.00 36.78 ? 76  ARG B O   1 
ATOM   1520 C  CB  . ARG B 1 80  ? 7.994  30.347 -17.793 1.00 27.99 ? 76  ARG B CB  1 
ATOM   1521 C  CG  . ARG B 1 80  ? 7.145  30.125 -16.558 1.00 32.36 ? 76  ARG B CG  1 
ATOM   1522 C  CD  . ARG B 1 80  ? 6.019  31.159 -16.458 1.00 29.30 ? 76  ARG B CD  1 
ATOM   1523 N  NE  . ARG B 1 80  ? 6.510  32.532 -16.584 1.00 26.77 ? 76  ARG B NE  1 
ATOM   1524 C  CZ  . ARG B 1 80  ? 6.962  33.255 -15.562 1.00 29.30 ? 76  ARG B CZ  1 
ATOM   1525 N  NH1 . ARG B 1 80  ? 7.386  34.500 -15.756 1.00 31.52 ? 76  ARG B NH1 1 
ATOM   1526 N  NH2 . ARG B 1 80  ? 7.017  32.725 -14.342 1.00 29.28 ? 76  ARG B NH2 1 
ATOM   1527 N  N   . ASP B 1 81  ? 10.541 29.704 -19.890 1.00 30.94 ? 77  ASP B N   1 
ATOM   1528 C  CA  . ASP B 1 81  ? 11.023 30.016 -21.235 1.00 28.71 ? 77  ASP B CA  1 
ATOM   1529 C  C   . ASP B 1 81  ? 11.180 28.748 -22.066 1.00 36.45 ? 77  ASP B C   1 
ATOM   1530 O  O   . ASP B 1 81  ? 11.917 27.831 -21.655 1.00 29.96 ? 77  ASP B O   1 
ATOM   1531 C  CB  . ASP B 1 81  ? 12.356 30.748 -21.135 1.00 33.72 ? 77  ASP B CB  1 
ATOM   1532 C  CG  . ASP B 1 81  ? 12.755 31.435 -22.429 1.00 36.74 ? 77  ASP B CG  1 
ATOM   1533 O  OD1 . ASP B 1 81  ? 12.431 30.931 -23.527 1.00 35.74 ? 77  ASP B OD1 1 
ATOM   1534 O  OD2 . ASP B 1 81  ? 13.394 32.494 -22.339 1.00 36.71 ? 77  ASP B OD2 1 
ATOM   1535 N  N   . PRO B 1 82  ? 10.535 28.647 -23.235 1.00 31.83 ? 78  PRO B N   1 
ATOM   1536 C  CA  . PRO B 1 82  ? 10.679 27.419 -24.036 1.00 33.94 ? 78  PRO B CA  1 
ATOM   1537 C  C   . PRO B 1 82  ? 12.102 27.190 -24.527 1.00 29.96 ? 78  PRO B C   1 
ATOM   1538 O  O   . PRO B 1 82  ? 12.460 26.042 -24.821 1.00 34.70 ? 78  PRO B O   1 
ATOM   1539 C  CB  . PRO B 1 82  ? 9.689  27.629 -25.194 1.00 36.87 ? 78  PRO B CB  1 
ATOM   1540 C  CG  . PRO B 1 82  ? 9.437  29.071 -25.236 1.00 28.82 ? 78  PRO B CG  1 
ATOM   1541 C  CD  . PRO B 1 82  ? 9.592  29.599 -23.851 1.00 31.93 ? 78  PRO B CD  1 
ATOM   1542 N  N   . ALA B 1 83  ? 12.929 28.243 -24.588 1.00 34.54 ? 79  ALA B N   1 
ATOM   1543 C  CA  . ALA B 1 83  ? 14.342 28.097 -24.917 1.00 32.59 ? 79  ALA B CA  1 
ATOM   1544 C  C   . ALA B 1 83  ? 15.092 27.241 -23.907 1.00 39.87 ? 79  ALA B C   1 
ATOM   1545 O  O   . ALA B 1 83  ? 16.178 26.740 -24.215 1.00 39.74 ? 79  ALA B O   1 
ATOM   1546 C  CB  . ALA B 1 83  ? 15.004 29.472 -25.004 1.00 33.72 ? 79  ALA B CB  1 
ATOM   1547 N  N   . SER B 1 84  ? 14.557 27.084 -22.704 1.00 35.45 ? 80  SER B N   1 
ATOM   1548 C  CA  . SER B 1 84  ? 15.246 26.327 -21.673 1.00 34.92 ? 80  SER B CA  1 
ATOM   1549 C  C   . SER B 1 84  ? 15.088 24.831 -21.864 1.00 39.52 ? 80  SER B C   1 
ATOM   1550 O  O   . SER B 1 84  ? 15.876 24.058 -21.304 1.00 35.43 ? 80  SER B O   1 
ATOM   1551 C  CB  . SER B 1 84  ? 14.706 26.740 -20.307 1.00 30.79 ? 80  SER B CB  1 
ATOM   1552 O  OG  . SER B 1 84  ? 15.055 28.093 -20.040 1.00 30.97 ? 80  SER B OG  1 
ATOM   1553 N  N   . ALA B 1 85  ? 14.100 24.420 -22.662 1.00 31.26 ? 81  ALA B N   1 
ATOM   1554 C  CA  . ALA B 1 85  ? 13.755 23.008 -22.766 1.00 32.15 ? 81  ALA B CA  1 
ATOM   1555 C  C   . ALA B 1 85  ? 14.884 22.135 -23.298 1.00 40.36 ? 81  ALA B C   1 
ATOM   1556 O  O   . ALA B 1 85  ? 15.072 21.038 -22.747 1.00 40.71 ? 81  ALA B O   1 
ATOM   1557 C  CB  . ALA B 1 85  ? 12.490 22.849 -23.621 1.00 36.48 ? 81  ALA B CB  1 
ATOM   1558 N  N   . PRO B 1 86  ? 15.648 22.516 -24.333 1.00 41.52 ? 82  PRO B N   1 
ATOM   1559 C  CA  . PRO B 1 86  ? 16.750 21.637 -24.764 1.00 40.58 ? 82  PRO B CA  1 
ATOM   1560 C  C   . PRO B 1 86  ? 17.684 21.249 -23.634 1.00 43.34 ? 82  PRO B C   1 
ATOM   1561 O  O   . PRO B 1 86  ? 18.188 20.118 -23.628 1.00 43.43 ? 82  PRO B O   1 
ATOM   1562 C  CB  . PRO B 1 86  ? 17.474 22.475 -25.826 1.00 36.22 ? 82  PRO B CB  1 
ATOM   1563 C  CG  . PRO B 1 86  ? 16.416 23.357 -26.375 1.00 43.85 ? 82  PRO B CG  1 
ATOM   1564 C  CD  . PRO B 1 86  ? 15.524 23.695 -25.211 1.00 40.18 ? 82  PRO B CD  1 
ATOM   1565 N  N   . HIS B 1 87  ? 17.903 22.140 -22.658 1.00 33.30 ? 83  HIS B N   1 
ATOM   1566 C  CA  . HIS B 1 87  ? 18.821 21.872 -21.558 1.00 36.75 ? 83  HIS B CA  1 
ATOM   1567 C  C   . HIS B 1 87  ? 18.160 21.165 -20.381 1.00 37.85 ? 83  HIS B C   1 
ATOM   1568 O  O   . HIS B 1 87  ? 18.791 20.315 -19.738 1.00 39.51 ? 83  HIS B O   1 
ATOM   1569 C  CB  . HIS B 1 87  ? 19.454 23.172 -21.075 1.00 35.28 ? 83  HIS B CB  1 
ATOM   1570 C  CG  . HIS B 1 87  ? 20.543 23.678 -21.967 1.00 41.86 ? 83  HIS B CG  1 
ATOM   1571 N  ND1 . HIS B 1 87  ? 20.332 24.647 -22.924 1.00 42.67 ? 83  HIS B ND1 1 
ATOM   1572 C  CD2 . HIS B 1 87  ? 21.854 23.348 -22.047 1.00 41.56 ? 83  HIS B CD2 1 
ATOM   1573 C  CE1 . HIS B 1 87  ? 21.468 24.898 -23.550 1.00 48.04 ? 83  HIS B CE1 1 
ATOM   1574 N  NE2 . HIS B 1 87  ? 22.407 24.123 -23.037 1.00 44.07 ? 83  HIS B NE2 1 
ATOM   1575 N  N   . PHE B 1 88  ? 16.903 21.486 -20.079 1.00 37.00 ? 84  PHE B N   1 
ATOM   1576 C  CA  . PHE B 1 88  ? 16.258 20.929 -18.899 1.00 36.40 ? 84  PHE B CA  1 
ATOM   1577 C  C   . PHE B 1 88  ? 15.575 19.596 -19.175 1.00 42.66 ? 84  PHE B C   1 
ATOM   1578 O  O   . PHE B 1 88  ? 15.428 18.788 -18.253 1.00 46.10 ? 84  PHE B O   1 
ATOM   1579 C  CB  . PHE B 1 88  ? 15.242 21.931 -18.332 1.00 40.75 ? 84  PHE B CB  1 
ATOM   1580 C  CG  . PHE B 1 88  ? 15.863 23.212 -17.806 1.00 35.75 ? 84  PHE B CG  1 
ATOM   1581 C  CD1 . PHE B 1 88  ? 17.235 23.343 -17.683 1.00 34.10 ? 84  PHE B CD1 1 
ATOM   1582 C  CD2 . PHE B 1 88  ? 15.063 24.276 -17.413 1.00 32.65 ? 84  PHE B CD2 1 
ATOM   1583 C  CE1 . PHE B 1 88  ? 17.794 24.511 -17.186 1.00 31.06 ? 84  PHE B CE1 1 
ATOM   1584 C  CE2 . PHE B 1 88  ? 15.622 25.444 -16.911 1.00 27.32 ? 84  PHE B CE2 1 
ATOM   1585 C  CZ  . PHE B 1 88  ? 16.982 25.558 -16.801 1.00 31.15 ? 84  PHE B CZ  1 
ATOM   1586 N  N   . MET B 1 89  ? 15.166 19.352 -20.423 1.00 43.22 ? 85  MET B N   1 
ATOM   1587 C  CA  . MET B 1 89  ? 14.460 18.117 -20.770 1.00 45.17 ? 85  MET B CA  1 
ATOM   1588 C  C   . MET B 1 89  ? 15.248 16.860 -20.436 1.00 41.96 ? 85  MET B C   1 
ATOM   1589 O  O   . MET B 1 89  ? 14.677 15.956 -19.799 1.00 46.34 ? 85  MET B O   1 
ATOM   1590 C  CB  . MET B 1 89  ? 14.093 18.129 -22.257 1.00 40.21 ? 85  MET B CB  1 
ATOM   1591 C  CG  . MET B 1 89  ? 12.764 18.742 -22.588 1.00 54.72 ? 85  MET B CG  1 
ATOM   1592 S  SD  . MET B 1 89  ? 12.238 18.219 -24.226 1.00 69.18 ? 85  MET B SD  1 
ATOM   1593 C  CE  . MET B 1 89  ? 13.819 17.953 -25.034 1.00 63.78 ? 85  MET B CE  1 
ATOM   1594 N  N   . PRO B 1 90  ? 16.519 16.713 -20.828 1.00 44.80 ? 86  PRO B N   1 
ATOM   1595 C  CA  . PRO B 1 90  ? 17.258 15.518 -20.405 1.00 47.57 ? 86  PRO B CA  1 
ATOM   1596 C  C   . PRO B 1 90  ? 17.400 15.397 -18.900 1.00 49.90 ? 86  PRO B C   1 
ATOM   1597 O  O   . PRO B 1 90  ? 17.542 14.279 -18.394 1.00 50.31 ? 86  PRO B O   1 
ATOM   1598 C  CB  . PRO B 1 90  ? 18.620 15.689 -21.091 1.00 50.24 ? 86  PRO B CB  1 
ATOM   1599 C  CG  . PRO B 1 90  ? 18.731 17.121 -21.375 1.00 47.48 ? 86  PRO B CG  1 
ATOM   1600 C  CD  . PRO B 1 90  ? 17.352 17.567 -21.694 1.00 44.49 ? 86  PRO B CD  1 
ATOM   1601 N  N   . ILE B 1 91  ? 17.376 16.513 -18.167 1.00 41.57 ? 87  ILE B N   1 
ATOM   1602 C  CA  . ILE B 1 91  ? 17.482 16.442 -16.716 1.00 43.31 ? 87  ILE B CA  1 
ATOM   1603 C  C   . ILE B 1 91  ? 16.243 15.786 -16.127 1.00 46.33 ? 87  ILE B C   1 
ATOM   1604 O  O   . ILE B 1 91  ? 16.338 14.924 -15.243 1.00 48.30 ? 87  ILE B O   1 
ATOM   1605 C  CB  . ILE B 1 91  ? 17.705 17.843 -16.123 1.00 34.80 ? 87  ILE B CB  1 
ATOM   1606 C  CG1 . ILE B 1 91  ? 19.089 18.359 -16.480 1.00 37.25 ? 87  ILE B CG1 1 
ATOM   1607 C  CG2 . ILE B 1 91  ? 17.480 17.820 -14.621 1.00 34.86 ? 87  ILE B CG2 1 
ATOM   1608 C  CD1 . ILE B 1 91  ? 19.313 19.784 -16.034 1.00 39.84 ? 87  ILE B CD1 1 
ATOM   1609 N  N   . GLY B 1 92  ? 15.060 16.197 -16.592 1.00 50.63 ? 88  GLY B N   1 
ATOM   1610 C  CA  . GLY B 1 92  ? 13.826 15.546 -16.178 1.00 40.20 ? 88  GLY B CA  1 
ATOM   1611 C  C   . GLY B 1 92  ? 13.742 14.095 -16.607 1.00 46.04 ? 88  GLY B C   1 
ATOM   1612 O  O   . GLY B 1 92  ? 12.948 13.333 -16.049 1.00 44.75 ? 88  GLY B O   1 
ATOM   1613 N  N   . GLU B 1 93  ? 14.545 13.697 -17.594 1.00 45.66 ? 89  GLU B N   1 
ATOM   1614 C  CA  . GLU B 1 93  ? 14.617 12.292 -17.965 1.00 53.21 ? 89  GLU B CA  1 
ATOM   1615 C  C   . GLU B 1 93  ? 15.313 11.473 -16.889 1.00 56.00 ? 89  GLU B C   1 
ATOM   1616 O  O   . GLU B 1 93  ? 15.057 10.267 -16.768 1.00 49.03 ? 89  GLU B O   1 
ATOM   1617 C  CB  . GLU B 1 93  ? 15.346 12.146 -19.299 1.00 53.29 ? 89  GLU B CB  1 
ATOM   1618 C  CG  . GLU B 1 93  ? 14.438 12.250 -20.513 1.00 60.42 ? 89  GLU B CG  1 
ATOM   1619 C  CD  . GLU B 1 93  ? 15.181 12.017 -21.816 1.00 79.39 ? 89  GLU B CD  1 
ATOM   1620 O  OE1 . GLU B 1 93  ? 14.516 11.864 -22.864 1.00 86.64 ? 89  GLU B OE1 1 
ATOM   1621 O  OE2 . GLU B 1 93  ? 16.433 11.998 -21.794 1.00 76.67 ? 89  GLU B OE2 1 
ATOM   1622 N  N   . LEU B 1 94  ? 16.184 12.109 -16.102 1.00 44.21 ? 90  LEU B N   1 
ATOM   1623 C  CA  . LEU B 1 94  ? 16.978 11.430 -15.087 1.00 40.33 ? 90  LEU B CA  1 
ATOM   1624 C  C   . LEU B 1 94  ? 16.435 11.591 -13.682 1.00 43.65 ? 90  LEU B C   1 
ATOM   1625 O  O   . LEU B 1 94  ? 16.711 10.745 -12.828 1.00 51.55 ? 90  LEU B O   1 
ATOM   1626 C  CB  . LEU B 1 94  ? 18.418 11.948 -15.098 1.00 46.54 ? 90  LEU B CB  1 
ATOM   1627 C  CG  . LEU B 1 94  ? 19.311 11.386 -16.191 1.00 43.08 ? 90  LEU B CG  1 
ATOM   1628 C  CD1 . LEU B 1 94  ? 20.759 11.701 -15.901 1.00 43.81 ? 90  LEU B CD1 1 
ATOM   1629 C  CD2 . LEU B 1 94  ? 19.088 9.883  -16.330 1.00 41.27 ? 90  LEU B CD2 1 
ATOM   1630 N  N   . THR B 1 95  ? 15.691 12.654 -13.400 1.00 42.73 ? 91  THR B N   1 
ATOM   1631 C  CA  . THR B 1 95  ? 15.294 12.898 -12.025 1.00 38.23 ? 91  THR B CA  1 
ATOM   1632 C  C   . THR B 1 95  ? 14.005 13.705 -11.999 1.00 48.67 ? 91  THR B C   1 
ATOM   1633 O  O   . THR B 1 95  ? 13.685 14.429 -12.944 1.00 46.26 ? 91  THR B O   1 
ATOM   1634 C  CB  . THR B 1 95  ? 16.409 13.631 -11.259 1.00 45.06 ? 91  THR B CB  1 
ATOM   1635 O  OG1 . THR B 1 95  ? 15.951 14.008 -9.957  1.00 43.01 ? 91  THR B OG1 1 
ATOM   1636 C  CG2 . THR B 1 95  ? 16.844 14.873 -12.008 1.00 48.80 ? 91  THR B CG2 1 
ATOM   1637 N  N   . GLN B 1 96  ? 13.265 13.560 -10.910 1.00 49.99 ? 92  GLN B N   1 
ATOM   1638 C  CA  . GLN B 1 96  ? 12.100 14.396 -10.639 1.00 58.64 ? 92  GLN B CA  1 
ATOM   1639 C  C   . GLN B 1 96  ? 12.587 15.489 -9.699  1.00 45.85 ? 92  GLN B C   1 
ATOM   1640 O  O   . GLN B 1 96  ? 12.534 15.354 -8.477  1.00 50.72 ? 92  GLN B O   1 
ATOM   1641 C  CB  . GLN B 1 96  ? 10.960 13.586 -10.038 1.00 62.94 ? 92  GLN B CB  1 
ATOM   1642 C  CG  . GLN B 1 96  ? 9.576  14.073 -10.440 1.00 70.60 ? 92  GLN B CG  1 
ATOM   1643 C  CD  . GLN B 1 96  ? 8.515  12.988 -10.337 1.00 84.47 ? 92  GLN B CD  1 
ATOM   1644 O  OE1 . GLN B 1 96  ? 8.822  11.791 -10.336 1.00 76.28 ? 92  GLN B OE1 1 
ATOM   1645 N  NE2 . GLN B 1 96  ? 7.253  13.405 -10.246 1.00 84.89 ? 92  GLN B NE2 1 
ATOM   1646 N  N   . GLY B 1 97  ? 13.086 16.572 -10.284 1.00 50.34 ? 93  GLY B N   1 
ATOM   1647 C  CA  . GLY B 1 97  ? 13.683 17.625 -9.485  1.00 47.72 ? 93  GLY B CA  1 
ATOM   1648 C  C   . GLY B 1 97  ? 12.658 18.308 -8.600  1.00 46.16 ? 93  GLY B C   1 
ATOM   1649 O  O   . GLY B 1 97  ? 11.506 18.507 -8.985  1.00 51.53 ? 93  GLY B O   1 
ATOM   1650 N  N   . LYS B 1 98  ? 13.090 18.673 -7.398  1.00 44.99 ? 94  LYS B N   1 
ATOM   1651 C  CA  . LYS B 1 98  ? 12.257 19.358 -6.418  1.00 42.29 ? 94  LYS B CA  1 
ATOM   1652 C  C   . LYS B 1 98  ? 12.822 20.758 -6.206  1.00 41.92 ? 94  LYS B C   1 
ATOM   1653 O  O   . LYS B 1 98  ? 13.799 20.936 -5.473  1.00 41.30 ? 94  LYS B O   1 
ATOM   1654 C  CB  . LYS B 1 98  ? 12.210 18.583 -5.110  1.00 41.23 ? 94  LYS B CB  1 
ATOM   1655 C  CG  . LYS B 1 98  ? 11.522 19.360 -3.991  1.00 51.46 ? 94  LYS B CG  1 
ATOM   1656 C  CD  . LYS B 1 98  ? 10.777 18.440 -3.039  1.00 62.93 ? 94  LYS B CD  1 
ATOM   1657 C  CE  . LYS B 1 98  ? 11.595 18.161 -1.789  1.00 58.28 ? 94  LYS B CE  1 
ATOM   1658 N  NZ  . LYS B 1 98  ? 11.788 19.392 -0.972  1.00 58.55 ? 94  LYS B NZ  1 
ATOM   1659 N  N   . GLN B 1 99  ? 12.193 21.748 -6.832  1.00 41.19 ? 95  GLN B N   1 
ATOM   1660 C  CA  . GLN B 1 99  ? 12.677 23.123 -6.830  1.00 38.85 ? 95  GLN B CA  1 
ATOM   1661 C  C   . GLN B 1 99  ? 11.965 23.945 -5.761  1.00 39.15 ? 95  GLN B C   1 
ATOM   1662 O  O   . GLN B 1 99  ? 10.769 23.764 -5.523  1.00 35.18 ? 95  GLN B O   1 
ATOM   1663 C  CB  . GLN B 1 99  ? 12.467 23.762 -8.204  1.00 41.76 ? 95  GLN B CB  1 
ATOM   1664 C  CG  . GLN B 1 99  ? 12.406 25.284 -8.192  1.00 51.14 ? 95  GLN B CG  1 
ATOM   1665 C  CD  . GLN B 1 99  ? 11.057 25.823 -8.624  1.00 53.43 ? 95  GLN B CD  1 
ATOM   1666 O  OE1 . GLN B 1 99  ? 10.609 25.550 -9.744  1.00 46.63 ? 95  GLN B OE1 1 
ATOM   1667 N  NE2 . GLN B 1 99  ? 10.393 26.589 -7.738  1.00 47.20 ? 95  GLN B NE2 1 
ATOM   1668 N  N   . GLY B 1 100 ? 12.701 24.862 -5.125  1.00 33.66 ? 96  GLY B N   1 
ATOM   1669 C  CA  . GLY B 1 100 ? 12.071 25.772 -4.184  1.00 35.93 ? 96  GLY B CA  1 
ATOM   1670 C  C   . GLY B 1 100 ? 12.907 26.963 -3.758  1.00 30.36 ? 96  GLY B C   1 
ATOM   1671 O  O   . GLY B 1 100 ? 14.129 26.847 -3.622  1.00 27.92 ? 96  GLY B O   1 
ATOM   1672 N  N   . ALA B 1 101 ? 12.252 28.106 -3.544  1.00 25.77 ? 97  ALA B N   1 
ATOM   1673 C  CA  . ALA B 1 101 ? 12.894 29.300 -3.010  1.00 28.13 ? 97  ALA B CA  1 
ATOM   1674 C  C   . ALA B 1 101 ? 12.943 29.273 -1.485  1.00 26.37 ? 97  ALA B C   1 
ATOM   1675 O  O   . ALA B 1 101 ? 12.053 28.736 -0.818  1.00 24.97 ? 97  ALA B O   1 
ATOM   1676 C  CB  . ALA B 1 101 ? 12.161 30.560 -3.463  1.00 24.96 ? 97  ALA B CB  1 
ATOM   1677 N  N   . TYR B 1 102 ? 13.991 29.889 -0.936  1.00 22.59 ? 98  TYR B N   1 
ATOM   1678 C  CA  . TYR B 1 102 ? 14.282 29.866 0.488   1.00 22.24 ? 98  TYR B CA  1 
ATOM   1679 C  C   . TYR B 1 102 ? 14.607 31.274 0.964   1.00 26.98 ? 98  TYR B C   1 
ATOM   1680 O  O   . TYR B 1 102 ? 15.141 32.089 0.212   1.00 27.63 ? 98  TYR B O   1 
ATOM   1681 C  CB  . TYR B 1 102 ? 15.466 28.929 0.787   1.00 19.49 ? 98  TYR B CB  1 
ATOM   1682 C  CG  . TYR B 1 102 ? 15.093 27.459 0.692   1.00 25.91 ? 98  TYR B CG  1 
ATOM   1683 C  CD1 . TYR B 1 102 ? 14.891 26.693 1.839   1.00 23.52 ? 98  TYR B CD1 1 
ATOM   1684 C  CD2 . TYR B 1 102 ? 14.935 26.845 -0.545  1.00 22.81 ? 98  TYR B CD2 1 
ATOM   1685 C  CE1 . TYR B 1 102 ? 14.542 25.349 1.755   1.00 22.96 ? 98  TYR B CE1 1 
ATOM   1686 C  CE2 . TYR B 1 102 ? 14.580 25.501 -0.641  1.00 26.32 ? 98  TYR B CE2 1 
ATOM   1687 C  CZ  . TYR B 1 102 ? 14.387 24.764 0.515   1.00 20.76 ? 98  TYR B CZ  1 
ATOM   1688 O  OH  . TYR B 1 102 ? 14.033 23.446 0.403   1.00 25.85 ? 98  TYR B OH  1 
ATOM   1689 N  N   . ASP B 1 103 ? 14.283 31.561 2.225   1.00 23.42 ? 99  ASP B N   1 
ATOM   1690 C  CA  . ASP B 1 103 ? 14.886 32.695 2.915   1.00 24.38 ? 99  ASP B CA  1 
ATOM   1691 C  C   . ASP B 1 103 ? 16.089 32.207 3.695   1.00 23.71 ? 99  ASP B C   1 
ATOM   1692 O  O   . ASP B 1 103 ? 16.015 31.175 4.357   1.00 24.42 ? 99  ASP B O   1 
ATOM   1693 C  CB  . ASP B 1 103 ? 13.920 33.354 3.905   1.00 24.22 ? 99  ASP B CB  1 
ATOM   1694 C  CG  . ASP B 1 103 ? 12.705 33.930 3.238   1.00 32.80 ? 99  ASP B CG  1 
ATOM   1695 O  OD1 . ASP B 1 103 ? 12.838 34.450 2.113   1.00 31.44 ? 99  ASP B OD1 1 
ATOM   1696 O  OD2 . ASP B 1 103 ? 11.626 33.858 3.855   1.00 32.00 ? 99  ASP B OD2 1 
ATOM   1697 N  N   . VAL B 1 104 ? 17.175 32.976 3.652   1.00 24.55 ? 100 VAL B N   1 
ATOM   1698 C  CA  . VAL B 1 104 ? 18.334 32.729 4.505   1.00 24.93 ? 100 VAL B CA  1 
ATOM   1699 C  C   . VAL B 1 104 ? 18.055 33.409 5.840   1.00 32.18 ? 100 VAL B C   1 
ATOM   1700 O  O   . VAL B 1 104 ? 18.074 34.635 5.935   1.00 30.62 ? 100 VAL B O   1 
ATOM   1701 C  CB  . VAL B 1 104 ? 19.631 33.258 3.880   1.00 26.64 ? 100 VAL B CB  1 
ATOM   1702 C  CG1 . VAL B 1 104 ? 20.804 32.982 4.804   1.00 30.27 ? 100 VAL B CG1 1 
ATOM   1703 C  CG2 . VAL B 1 104 ? 19.877 32.643 2.521   1.00 27.41 ? 100 VAL B CG2 1 
ATOM   1704 N  N   . VAL B 1 105 ? 17.780 32.619 6.875   1.00 25.09 ? 101 VAL B N   1 
ATOM   1705 C  CA  . VAL B 1 105 ? 17.357 33.193 8.144   1.00 23.40 ? 101 VAL B CA  1 
ATOM   1706 C  C   . VAL B 1 105 ? 18.470 33.228 9.178   1.00 30.88 ? 101 VAL B C   1 
ATOM   1707 O  O   . VAL B 1 105 ? 18.298 33.871 10.227  1.00 27.45 ? 101 VAL B O   1 
ATOM   1708 C  CB  . VAL B 1 105 ? 16.143 32.437 8.717   1.00 28.00 ? 101 VAL B CB  1 
ATOM   1709 C  CG1 . VAL B 1 105 ? 14.970 32.492 7.735   1.00 28.28 ? 101 VAL B CG1 1 
ATOM   1710 C  CG2 . VAL B 1 105 ? 16.532 30.998 9.011   1.00 32.64 ? 101 VAL B CG2 1 
ATOM   1711 N  N   . TYR B 1 106 ? 19.592 32.550 8.936   1.00 23.78 ? 102 TYR B N   1 
ATOM   1712 C  CA  . TYR B 1 106 ? 20.713 32.565 9.879   1.00 21.12 ? 102 TYR B CA  1 
ATOM   1713 C  C   . TYR B 1 106 ? 21.965 32.204 9.114   1.00 26.36 ? 102 TYR B C   1 
ATOM   1714 O  O   . TYR B 1 106 ? 21.973 31.213 8.380   1.00 23.46 ? 102 TYR B O   1 
ATOM   1715 C  CB  . TYR B 1 106 ? 20.529 31.572 11.032  1.00 21.67 ? 102 TYR B CB  1 
ATOM   1716 C  CG  . TYR B 1 106 ? 21.763 31.357 11.937  1.00 24.62 ? 102 TYR B CG  1 
ATOM   1717 C  CD1 . TYR B 1 106 ? 21.989 32.178 13.048  1.00 26.05 ? 102 TYR B CD1 1 
ATOM   1718 C  CD2 . TYR B 1 106 ? 22.670 30.329 11.697  1.00 23.12 ? 102 TYR B CD2 1 
ATOM   1719 C  CE1 . TYR B 1 106 ? 23.083 31.991 13.883  1.00 24.63 ? 102 TYR B CE1 1 
ATOM   1720 C  CE2 . TYR B 1 106 ? 23.789 30.132 12.533  1.00 22.23 ? 102 TYR B CE2 1 
ATOM   1721 C  CZ  . TYR B 1 106 ? 23.979 30.970 13.628  1.00 28.65 ? 102 TYR B CZ  1 
ATOM   1722 O  OH  . TYR B 1 106 ? 25.059 30.792 14.476  1.00 25.14 ? 102 TYR B OH  1 
ATOM   1723 N  N   . THR B 1 107 ? 23.017 32.988 9.306   1.00 26.55 ? 103 THR B N   1 
ATOM   1724 C  CA  . THR B 1 107 ? 24.306 32.686 8.713   1.00 21.96 ? 103 THR B CA  1 
ATOM   1725 C  C   . THR B 1 107 ? 25.381 33.128 9.698   1.00 32.75 ? 103 THR B C   1 
ATOM   1726 O  O   . THR B 1 107 ? 25.297 34.215 10.269  1.00 29.08 ? 103 THR B O   1 
ATOM   1727 C  CB  . THR B 1 107 ? 24.471 33.371 7.349   1.00 30.33 ? 103 THR B CB  1 
ATOM   1728 O  OG1 . THR B 1 107 ? 25.774 33.086 6.830   1.00 45.17 ? 103 THR B OG1 1 
ATOM   1729 C  CG2 . THR B 1 107 ? 24.333 34.856 7.477   1.00 26.59 ? 103 THR B CG2 1 
ATOM   1730 N  N   . HIS B 1 108 ? 26.349 32.256 9.940   1.00 25.25 ? 104 HIS B N   1 
ATOM   1731 C  CA  . HIS B 1 108 ? 27.444 32.539 10.851  1.00 24.32 ? 104 HIS B CA  1 
ATOM   1732 C  C   . HIS B 1 108 ? 28.681 31.883 10.277  1.00 26.15 ? 104 HIS B C   1 
ATOM   1733 O  O   . HIS B 1 108 ? 28.603 30.778 9.734   1.00 21.44 ? 104 HIS B O   1 
ATOM   1734 C  CB  . HIS B 1 108 ? 27.171 32.012 12.272  1.00 22.41 ? 104 HIS B CB  1 
ATOM   1735 C  CG  . HIS B 1 108 ? 28.326 32.191 13.208  1.00 29.88 ? 104 HIS B CG  1 
ATOM   1736 N  ND1 . HIS B 1 108 ? 29.301 31.230 13.385  1.00 23.94 ? 104 HIS B ND1 1 
ATOM   1737 C  CD2 . HIS B 1 108 ? 28.673 33.231 14.006  1.00 29.29 ? 104 HIS B CD2 1 
ATOM   1738 C  CE1 . HIS B 1 108 ? 30.205 31.676 14.241  1.00 24.50 ? 104 HIS B CE1 1 
ATOM   1739 N  NE2 . HIS B 1 108 ? 29.837 32.881 14.645  1.00 29.80 ? 104 HIS B NE2 1 
ATOM   1740 N  N   . VAL B 1 109 ? 29.808 32.582 10.363  1.00 25.36 ? 105 VAL B N   1 
ATOM   1741 C  CA  . VAL B 1 109 ? 31.100 32.047 9.962   1.00 30.44 ? 105 VAL B CA  1 
ATOM   1742 C  C   . VAL B 1 109 ? 32.062 32.242 11.115  1.00 36.75 ? 105 VAL B C   1 
ATOM   1743 O  O   . VAL B 1 109 ? 31.990 33.241 11.836  1.00 35.33 ? 105 VAL B O   1 
ATOM   1744 C  CB  . VAL B 1 109 ? 31.660 32.729 8.694   1.00 40.59 ? 105 VAL B CB  1 
ATOM   1745 C  CG1 . VAL B 1 109 ? 32.775 31.877 8.063   1.00 37.01 ? 105 VAL B CG1 1 
ATOM   1746 C  CG2 . VAL B 1 109 ? 30.560 32.995 7.702   1.00 41.90 ? 105 VAL B CG2 1 
ATOM   1747 N  N   . THR B 1 110 ? 32.962 31.293 11.292  1.00 36.40 ? 106 THR B N   1 
ATOM   1748 C  CA  . THR B 1 110 ? 34.048 31.510 12.219  1.00 36.29 ? 106 THR B CA  1 
ATOM   1749 C  C   . THR B 1 110 ? 35.068 32.439 11.534  1.00 29.21 ? 106 THR B C   1 
ATOM   1750 O  O   . THR B 1 110 ? 35.842 33.131 12.203  1.00 60.23 ? 106 THR B O   1 
ATOM   1751 C  CB  . THR B 1 110 ? 34.688 30.193 12.620  1.00 40.46 ? 106 THR B CB  1 
ATOM   1752 O  OG1 . THR B 1 110 ? 35.345 30.341 13.882  1.00 54.34 ? 106 THR B OG1 1 
ATOM   1753 C  CG2 . THR B 1 110 ? 35.696 29.779 11.558  1.00 35.14 ? 106 THR B CG2 1 
HETATM 1754 C  C1  . AE3 C 2 .   ? 17.011 13.392 12.798  1.00 49.81 ? 201 AE3 A C1  1 
HETATM 1755 C  C2  . AE3 C 2 .   ? 17.623 14.738 12.643  1.00 49.95 ? 201 AE3 A C2  1 
HETATM 1756 O  O2  . AE3 C 2 .   ? 18.153 15.151 13.854  1.00 54.06 ? 201 AE3 A O2  1 
HETATM 1757 C  C3  . AE3 C 2 .   ? 18.522 16.563 13.877  1.00 40.00 ? 201 AE3 A C3  1 
HETATM 1758 C  C4  . AE3 C 2 .   ? 20.045 16.707 14.239  1.00 45.50 ? 201 AE3 A C4  1 
HETATM 1759 O  O3  . AE3 C 2 .   ? 20.800 17.008 12.991  1.00 52.68 ? 201 AE3 A O3  1 
HETATM 1760 C  C5  . AE3 C 2 .   ? 22.159 17.183 13.163  1.00 43.70 ? 201 AE3 A C5  1 
HETATM 1761 C  C6  . AE3 C 2 .   ? 22.689 18.080 12.068  1.00 37.41 ? 201 AE3 A C6  1 
HETATM 1762 O  O4  . AE3 C 2 .   ? 22.518 19.509 12.514  1.00 41.40 ? 201 AE3 A O4  1 
HETATM 1763 MG MG  . MG  D 3 .   ? 18.666 35.555 15.883  1.00 34.89 ? 202 MG  A MG  1 
HETATM 1764 C  C1  . AE3 E 2 .   ? 12.154 18.182 -13.794 1.00 56.08 ? 201 AE3 B C1  1 
HETATM 1765 C  C2  . AE3 E 2 .   ? 12.916 19.314 -13.199 1.00 53.16 ? 201 AE3 B C2  1 
HETATM 1766 O  O2  . AE3 E 2 .   ? 14.140 19.424 -13.830 1.00 56.15 ? 201 AE3 B O2  1 
HETATM 1767 C  C3  . AE3 E 2 .   ? 14.314 20.700 -14.504 1.00 49.12 ? 201 AE3 B C3  1 
HETATM 1768 C  C4  . AE3 E 2 .   ? 15.366 21.562 -13.716 1.00 46.01 ? 201 AE3 B C4  1 
HETATM 1769 O  O3  . AE3 E 2 .   ? 14.827 22.933 -13.493 1.00 50.79 ? 201 AE3 B O3  1 
HETATM 1770 C  C5  . AE3 E 2 .   ? 15.793 23.916 -13.532 1.00 50.86 ? 201 AE3 B C5  1 
HETATM 1771 C  C6  . AE3 E 2 .   ? 16.666 23.754 -12.317 1.00 42.35 ? 201 AE3 B C6  1 
HETATM 1772 O  O4  . AE3 E 2 .   ? 17.992 24.383 -12.607 1.00 48.13 ? 201 AE3 B O4  1 
HETATM 1773 O  O   . HOH F 4 .   ? 25.570 37.353 -14.614 1.00 36.96 ? 301 HOH A O   1 
HETATM 1774 O  O   . HOH F 4 .   ? 22.879 20.771 10.376  1.00 37.68 ? 302 HOH A O   1 
HETATM 1775 O  O   . HOH F 4 .   ? 26.440 11.859 11.214  1.00 35.52 ? 303 HOH A O   1 
HETATM 1776 O  O   . HOH F 4 .   ? 5.353  27.418 11.553  1.00 31.18 ? 304 HOH A O   1 
HETATM 1777 O  O   . HOH F 4 .   ? 30.853 14.776 25.597  1.00 47.36 ? 305 HOH A O   1 
HETATM 1778 O  O   . HOH F 4 .   ? 2.749  25.990 1.181   1.00 30.20 ? 306 HOH A O   1 
HETATM 1779 O  O   . HOH F 4 .   ? 21.382 15.677 1.789   1.00 45.72 ? 307 HOH A O   1 
HETATM 1780 O  O   . HOH F 4 .   ? 32.967 20.629 0.349   1.00 30.65 ? 308 HOH A O   1 
HETATM 1781 O  O   . HOH F 4 .   ? 34.265 26.214 16.872  1.00 27.89 ? 309 HOH A O   1 
HETATM 1782 O  O   . HOH F 4 .   ? 34.669 28.082 1.457   1.00 41.51 ? 310 HOH A O   1 
HETATM 1783 O  O   . HOH F 4 .   ? 7.574  18.262 3.973   1.00 42.22 ? 311 HOH A O   1 
HETATM 1784 O  O   . HOH F 4 .   ? 35.120 11.880 14.375  1.00 40.81 ? 312 HOH A O   1 
HETATM 1785 O  O   . HOH F 4 .   ? 11.200 36.515 7.085   1.00 48.83 ? 313 HOH A O   1 
HETATM 1786 O  O   . HOH F 4 .   ? 32.031 17.354 2.072   1.00 26.09 ? 314 HOH A O   1 
HETATM 1787 O  O   . HOH F 4 .   ? 33.610 10.434 12.173  1.00 27.76 ? 315 HOH A O   1 
HETATM 1788 O  O   . HOH F 4 .   ? 33.265 29.487 3.789   1.00 30.70 ? 316 HOH A O   1 
HETATM 1789 O  O   . HOH F 4 .   ? 26.457 28.471 13.500  1.00 24.02 ? 317 HOH A O   1 
HETATM 1790 O  O   . HOH F 4 .   ? 24.267 12.777 20.490  1.00 32.23 ? 318 HOH A O   1 
HETATM 1791 O  O   . HOH F 4 .   ? 33.259 25.329 -0.769  1.00 38.09 ? 319 HOH A O   1 
HETATM 1792 O  O   . HOH F 4 .   ? 39.742 21.650 5.967   1.00 40.74 ? 320 HOH A O   1 
HETATM 1793 O  O   . HOH F 4 .   ? 32.449 29.750 15.832  1.00 39.40 ? 321 HOH A O   1 
HETATM 1794 O  O   . HOH F 4 .   ? 30.759 24.580 0.647   1.00 23.95 ? 322 HOH A O   1 
HETATM 1795 O  O   . HOH F 4 .   ? 4.118  29.482 2.524   1.00 29.17 ? 323 HOH A O   1 
HETATM 1796 O  O   . HOH F 4 .   ? 32.608 9.861  18.930  1.00 37.72 ? 324 HOH A O   1 
HETATM 1797 O  O   . HOH F 4 .   ? 7.170  18.874 11.117  1.00 34.97 ? 325 HOH A O   1 
HETATM 1798 O  O   . HOH F 4 .   ? 33.251 18.556 16.364  1.00 32.27 ? 326 HOH A O   1 
HETATM 1799 O  O   . HOH F 4 .   ? 37.846 18.254 4.682   1.00 41.07 ? 327 HOH A O   1 
HETATM 1800 O  O   . HOH F 4 .   ? 36.703 16.730 15.725  1.00 41.27 ? 328 HOH A O   1 
HETATM 1801 O  O   . HOH F 4 .   ? 32.048 12.724 19.768  1.00 32.42 ? 329 HOH A O   1 
HETATM 1802 O  O   . HOH F 4 .   ? 16.199 18.880 25.265  1.00 46.27 ? 330 HOH A O   1 
HETATM 1803 O  O   . HOH F 4 .   ? 26.207 27.791 24.723  1.00 44.36 ? 331 HOH A O   1 
HETATM 1804 O  O   . HOH F 4 .   ? 2.104  19.268 13.880  1.00 52.47 ? 332 HOH A O   1 
HETATM 1805 O  O   . HOH F 4 .   ? 17.877 23.023 19.779  1.00 33.85 ? 333 HOH A O   1 
HETATM 1806 O  O   . HOH F 4 .   ? 28.560 18.497 21.250  1.00 36.71 ? 334 HOH A O   1 
HETATM 1807 O  O   . HOH F 4 .   ? 27.878 10.252 8.902   1.00 33.71 ? 335 HOH A O   1 
HETATM 1808 O  O   . HOH F 4 .   ? 30.033 12.252 6.052   1.00 28.31 ? 336 HOH A O   1 
HETATM 1809 O  O   . HOH F 4 .   ? 29.696 22.775 21.447  1.00 36.56 ? 337 HOH A O   1 
HETATM 1810 O  O   . HOH F 4 .   ? 34.843 33.304 4.895   1.00 45.40 ? 338 HOH A O   1 
HETATM 1811 O  O   . HOH F 4 .   ? 27.094 31.166 22.419  1.00 23.74 ? 339 HOH A O   1 
HETATM 1812 O  O   . HOH F 4 .   ? 5.939  26.720 14.095  1.00 29.75 ? 340 HOH A O   1 
HETATM 1813 O  O   . HOH F 4 .   ? 20.115 34.569 14.888  1.00 31.34 ? 341 HOH A O   1 
HETATM 1814 O  O   . HOH F 4 .   ? 34.416 13.565 -1.095  1.00 28.81 ? 342 HOH A O   1 
HETATM 1815 O  O   . HOH F 4 .   ? 18.321 32.666 18.691  1.00 40.82 ? 343 HOH A O   1 
HETATM 1816 O  O   . HOH F 4 .   ? 34.425 17.924 -0.066  1.00 39.06 ? 344 HOH A O   1 
HETATM 1817 O  O   . HOH F 4 .   ? 25.828 12.233 0.943   1.00 36.67 ? 345 HOH A O   1 
HETATM 1818 O  O   . HOH F 4 .   ? 35.558 16.846 18.262  1.00 48.49 ? 346 HOH A O   1 
HETATM 1819 O  O   . HOH F 4 .   ? 22.904 13.794 17.085  1.00 38.74 ? 347 HOH A O   1 
HETATM 1820 O  O   . HOH F 4 .   ? 28.922 8.012  19.999  1.00 30.70 ? 348 HOH A O   1 
HETATM 1821 O  O   . HOH F 4 .   ? 13.685 16.431 1.463   1.00 51.11 ? 349 HOH A O   1 
HETATM 1822 O  O   . HOH F 4 .   ? 27.533 12.133 5.145   1.00 33.07 ? 350 HOH A O   1 
HETATM 1823 O  O   . HOH F 4 .   ? 36.321 8.743  9.201   1.00 37.92 ? 351 HOH A O   1 
HETATM 1824 O  O   . HOH F 4 .   ? 16.165 30.581 18.062  1.00 36.81 ? 352 HOH A O   1 
HETATM 1825 O  O   . HOH F 4 .   ? 36.459 15.912 4.949   1.00 30.62 ? 353 HOH A O   1 
HETATM 1826 O  O   . HOH F 4 .   ? 20.379 11.518 8.313   1.00 49.99 ? 354 HOH A O   1 
HETATM 1827 O  O   . HOH F 4 .   ? 36.970 18.540 1.677   1.00 49.51 ? 355 HOH A O   1 
HETATM 1828 O  O   . HOH F 4 .   ? 25.822 11.987 7.536   1.00 42.85 ? 356 HOH A O   1 
HETATM 1829 O  O   . HOH F 4 .   ? 0.612  22.572 8.576   1.00 27.16 ? 357 HOH A O   1 
HETATM 1830 O  O   . HOH F 4 .   ? 21.633 12.260 12.774  1.00 42.13 ? 358 HOH A O   1 
HETATM 1831 O  O   . HOH F 4 .   ? 34.764 23.152 -10.908 1.00 46.11 ? 359 HOH A O   1 
HETATM 1832 O  O   . HOH F 4 .   ? 35.498 25.182 0.582   1.00 42.47 ? 360 HOH A O   1 
HETATM 1833 O  O   . HOH F 4 .   ? 9.587  18.382 2.173   1.00 42.14 ? 361 HOH A O   1 
HETATM 1834 O  O   . HOH F 4 .   ? 33.524 25.483 -11.171 1.00 38.80 ? 362 HOH A O   1 
HETATM 1835 O  O   . HOH F 4 .   ? 33.281 14.799 20.630  1.00 35.34 ? 363 HOH A O   1 
HETATM 1836 O  O   . HOH F 4 .   ? -1.865 23.283 9.260   1.00 38.11 ? 364 HOH A O   1 
HETATM 1837 O  O   . HOH F 4 .   ? 15.489 32.105 15.536  1.00 47.65 ? 365 HOH A O   1 
HETATM 1838 O  O   . HOH F 4 .   ? 33.043 28.412 -13.497 1.00 45.52 ? 366 HOH A O   1 
HETATM 1839 O  O   . HOH F 4 .   ? 32.965 32.569 -10.896 1.00 43.73 ? 367 HOH A O   1 
HETATM 1840 O  O   . HOH F 4 .   ? 10.587 23.549 -1.235  1.00 42.74 ? 368 HOH A O   1 
HETATM 1841 O  O   . HOH F 4 .   ? 36.888 13.885 15.426  1.00 49.82 ? 369 HOH A O   1 
HETATM 1842 O  O   . HOH F 4 .   ? 29.491 30.869 24.565  1.00 44.69 ? 370 HOH A O   1 
HETATM 1843 O  O   . HOH F 4 .   ? 22.768 9.809  9.347   1.00 43.82 ? 371 HOH A O   1 
HETATM 1844 O  O   . HOH F 4 .   ? 21.615 13.702 19.909  1.00 40.22 ? 372 HOH A O   1 
HETATM 1845 O  O   . HOH F 4 .   ? 35.533 27.227 18.954  1.00 42.45 ? 373 HOH A O   1 
HETATM 1846 O  O   . HOH F 4 .   ? 34.045 30.822 -12.547 1.00 47.92 ? 374 HOH A O   1 
HETATM 1847 O  O   . HOH F 4 .   ? 17.872 34.103 16.873  1.00 36.68 ? 375 HOH A O   1 
HETATM 1848 O  O   . HOH F 4 .   ? 25.514 30.466 24.105  1.00 43.24 ? 376 HOH A O   1 
HETATM 1849 O  O   . HOH F 4 .   ? 29.343 20.359 22.926  1.00 43.80 ? 377 HOH A O   1 
HETATM 1850 O  O   . HOH F 4 .   ? 26.796 10.406 3.059   1.00 37.39 ? 378 HOH A O   1 
HETATM 1851 O  O   . HOH F 4 .   ? 35.315 30.617 5.299   1.00 44.31 ? 379 HOH A O   1 
HETATM 1852 O  O   . HOH F 4 .   ? 34.865 16.354 2.235   1.00 41.77 ? 380 HOH A O   1 
HETATM 1853 O  O   . HOH G 4 .   ? 18.845 25.184 -10.705 1.00 39.41 ? 301 HOH B O   1 
HETATM 1854 O  O   . HOH G 4 .   ? 28.032 12.315 -18.438 1.00 50.95 ? 302 HOH B O   1 
HETATM 1855 O  O   . HOH G 4 .   ? 17.621 9.073  -4.638  1.00 42.86 ? 303 HOH B O   1 
HETATM 1856 O  O   . HOH G 4 .   ? 28.094 34.269 5.660   1.00 39.09 ? 304 HOH B O   1 
HETATM 1857 O  O   . HOH G 4 .   ? 14.550 36.183 1.296   1.00 47.12 ? 305 HOH B O   1 
HETATM 1858 O  O   . HOH G 4 .   ? 6.720  27.973 -21.987 1.00 38.06 ? 306 HOH B O   1 
HETATM 1859 O  O   . HOH G 4 .   ? 17.452 18.228 -25.235 1.00 47.01 ? 307 HOH B O   1 
HETATM 1860 O  O   . HOH G 4 .   ? 30.429 13.574 -4.433  1.00 31.79 ? 308 HOH B O   1 
HETATM 1861 O  O   . HOH G 4 .   ? 8.759  36.076 -14.201 1.00 35.54 ? 309 HOH B O   1 
HETATM 1862 O  O   . HOH G 4 .   ? 17.725 34.423 -0.187  1.00 35.12 ? 310 HOH B O   1 
HETATM 1863 O  O   . HOH G 4 .   ? 26.244 29.228 -13.591 1.00 31.78 ? 311 HOH B O   1 
HETATM 1864 O  O   . HOH G 4 .   ? 10.785 31.383 4.207   1.00 29.44 ? 312 HOH B O   1 
HETATM 1865 O  O   . HOH G 4 .   ? 25.701 4.992  -1.478  1.00 28.17 ? 313 HOH B O   1 
HETATM 1866 O  O   . HOH G 4 .   ? 26.931 36.259 9.892   1.00 44.66 ? 314 HOH B O   1 
HETATM 1867 O  O   . HOH G 4 .   ? 18.703 9.321  -11.825 1.00 41.74 ? 315 HOH B O   1 
HETATM 1868 O  O   . HOH G 4 .   ? 16.000 30.355 -21.060 1.00 34.24 ? 316 HOH B O   1 
HETATM 1869 O  O   . HOH G 4 .   ? 10.183 40.163 -6.663  1.00 38.78 ? 317 HOH B O   1 
HETATM 1870 O  O   . HOH G 4 .   ? 9.656  31.222 -6.318  1.00 31.45 ? 318 HOH B O   1 
HETATM 1871 O  O   . HOH G 4 .   ? 7.364  34.664 -12.081 1.00 23.13 ? 319 HOH B O   1 
HETATM 1872 O  O   . HOH G 4 .   ? 9.462  27.482 -11.213 1.00 37.26 ? 320 HOH B O   1 
HETATM 1873 O  O   . HOH G 4 .   ? 29.316 6.822  -2.912  1.00 34.11 ? 321 HOH B O   1 
HETATM 1874 O  O   . HOH G 4 .   ? 21.519 38.312 -18.910 1.00 37.74 ? 322 HOH B O   1 
HETATM 1875 O  O   . HOH G 4 .   ? 5.555  37.350 -9.035  1.00 30.96 ? 323 HOH B O   1 
HETATM 1876 O  O   . HOH G 4 .   ? 7.164  33.723 -18.927 1.00 36.20 ? 324 HOH B O   1 
HETATM 1877 O  O   . HOH G 4 .   ? 18.003 33.625 12.924  1.00 46.25 ? 325 HOH B O   1 
HETATM 1878 O  O   . HOH G 4 .   ? 7.692  28.891 -8.601  1.00 37.94 ? 326 HOH B O   1 
HETATM 1879 O  O   . HOH G 4 .   ? 13.977 22.430 -2.305  1.00 40.21 ? 327 HOH B O   1 
HETATM 1880 O  O   . HOH G 4 .   ? 10.425 35.420 1.251   1.00 27.07 ? 328 HOH B O   1 
HETATM 1881 O  O   . HOH G 4 .   ? 21.911 32.656 -0.761  1.00 27.23 ? 329 HOH B O   1 
HETATM 1882 O  O   . HOH G 4 .   ? 22.910 38.782 -14.089 1.00 37.10 ? 330 HOH B O   1 
HETATM 1883 O  O   . HOH G 4 .   ? 26.944 35.456 -4.038  1.00 40.57 ? 331 HOH B O   1 
HETATM 1884 O  O   . HOH G 4 .   ? 13.204 38.481 -15.323 1.00 37.75 ? 332 HOH B O   1 
HETATM 1885 O  O   . HOH G 4 .   ? 12.383 32.055 -26.053 1.00 42.03 ? 333 HOH B O   1 
HETATM 1886 O  O   . HOH G 4 .   ? 9.981  26.907 -1.031  1.00 27.92 ? 334 HOH B O   1 
HETATM 1887 O  O   . HOH G 4 .   ? 30.802 37.637 -4.317  1.00 45.45 ? 335 HOH B O   1 
HETATM 1888 O  O   . HOH G 4 .   ? 14.802 39.352 -4.108  1.00 42.00 ? 336 HOH B O   1 
HETATM 1889 O  O   . HOH G 4 .   ? 26.967 35.379 -15.567 1.00 37.73 ? 337 HOH B O   1 
HETATM 1890 O  O   . HOH G 4 .   ? 29.138 19.021 -18.096 1.00 36.98 ? 338 HOH B O   1 
HETATM 1891 O  O   . HOH G 4 .   ? 10.836 25.600 -20.328 1.00 33.91 ? 339 HOH B O   1 
HETATM 1892 O  O   . HOH G 4 .   ? 18.225 41.779 -5.577  1.00 40.93 ? 340 HOH B O   1 
HETATM 1893 O  O   . HOH G 4 .   ? 26.487 8.591  -13.978 1.00 40.04 ? 341 HOH B O   1 
HETATM 1894 O  O   . HOH G 4 .   ? 15.698 35.333 -16.072 1.00 27.98 ? 342 HOH B O   1 
HETATM 1895 O  O   . HOH G 4 .   ? 31.978 13.125 -16.226 1.00 53.10 ? 343 HOH B O   1 
HETATM 1896 O  O   . HOH G 4 .   ? 9.784  33.265 -19.775 1.00 34.02 ? 344 HOH B O   1 
HETATM 1897 O  O   . HOH G 4 .   ? 14.376 33.498 -2.188  1.00 24.72 ? 345 HOH B O   1 
HETATM 1898 O  O   . HOH G 4 .   ? 21.716 20.355 -19.992 1.00 35.56 ? 346 HOH B O   1 
HETATM 1899 O  O   . HOH G 4 .   ? 12.504 37.686 -4.782  1.00 24.12 ? 347 HOH B O   1 
HETATM 1900 O  O   . HOH G 4 .   ? 23.471 37.050 -16.478 1.00 28.91 ? 348 HOH B O   1 
HETATM 1901 O  O   . HOH G 4 .   ? 22.878 12.182 0.987   1.00 42.52 ? 349 HOH B O   1 
HETATM 1902 O  O   . HOH G 4 .   ? 11.740 24.223 -17.500 1.00 35.84 ? 350 HOH B O   1 
HETATM 1903 O  O   . HOH G 4 .   ? 22.602 34.706 0.494   1.00 42.15 ? 351 HOH B O   1 
HETATM 1904 O  O   . HOH G 4 .   ? 5.584  30.035 -20.296 1.00 40.64 ? 352 HOH B O   1 
HETATM 1905 O  O   . HOH G 4 .   ? 19.949 32.337 -21.156 1.00 40.96 ? 353 HOH B O   1 
HETATM 1906 O  O   . HOH G 4 .   ? 22.463 35.683 10.551  1.00 30.76 ? 354 HOH B O   1 
HETATM 1907 O  O   . HOH G 4 .   ? 33.315 36.755 2.257   1.00 55.13 ? 355 HOH B O   1 
HETATM 1908 O  O   . HOH G 4 .   ? 7.387  36.516 -18.123 1.00 43.76 ? 356 HOH B O   1 
HETATM 1909 O  O   . HOH G 4 .   ? 29.240 35.579 10.969  1.00 31.59 ? 357 HOH B O   1 
HETATM 1910 O  O   . HOH G 4 .   ? 16.913 35.237 -21.358 1.00 51.66 ? 358 HOH B O   1 
HETATM 1911 O  O   . HOH G 4 .   ? 31.771 16.991 -12.114 1.00 46.65 ? 359 HOH B O   1 
HETATM 1912 O  O   . HOH G 4 .   ? 9.634  28.463 -5.234  1.00 35.17 ? 360 HOH B O   1 
HETATM 1913 O  O   . HOH G 4 .   ? 11.954 35.064 -20.513 1.00 50.17 ? 361 HOH B O   1 
HETATM 1914 O  O   . HOH G 4 .   ? 25.784 20.028 -27.305 1.00 58.61 ? 362 HOH B O   1 
HETATM 1915 O  O   . HOH G 4 .   ? 17.658 40.672 7.072   1.00 57.85 ? 363 HOH B O   1 
HETATM 1916 O  O   . HOH G 4 .   ? 30.554 32.439 -20.232 1.00 45.34 ? 364 HOH B O   1 
HETATM 1917 O  O   . HOH G 4 .   ? 10.435 34.225 -22.726 1.00 46.94 ? 365 HOH B O   1 
HETATM 1918 O  O   . HOH G 4 .   ? 12.143 23.401 -19.975 1.00 35.90 ? 366 HOH B O   1 
HETATM 1919 O  O   . HOH G 4 .   ? 24.826 2.440  -2.004  1.00 43.81 ? 367 HOH B O   1 
HETATM 1920 O  O   . HOH G 4 .   ? 10.468 42.433 -8.136  1.00 49.14 ? 368 HOH B O   1 
HETATM 1921 O  O   . HOH G 4 .   ? 32.169 9.781  -12.554 1.00 40.99 ? 369 HOH B O   1 
HETATM 1922 O  O   . HOH G 4 .   ? 25.374 38.450 -17.379 1.00 40.21 ? 370 HOH B O   1 
HETATM 1923 O  O   . HOH G 4 .   ? 13.354 35.955 -2.176  1.00 37.80 ? 371 HOH B O   1 
# 
