data_9KN1
# 
_entry.id   9KN1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KN1         pdb_00009kn1 10.2210/pdb9kn1/pdb 
WWPDB D_1300048019 ?            ?                   
# 
_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       2025-04-23 
_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                        9KN1 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              ahigashiura@hiroshima-u.ac.jp 
_pdbx_contact_author.name_first         Akifumi 
_pdbx_contact_author.name_last          Higashiura 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8448-9349 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Higashiura, A.' 1 0000-0001-8448-9349 
'Yamamoto, A.'   2 0000-0002-2928-2828 
'Ito, H.'        3 0009-0005-3167-4125 
# 
_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            Virology 
_citation.journal_id_ASTM           VIRLAX 
_citation.journal_id_CSD            0922 
_citation.journal_id_ISSN           0042-6822 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            604 
_citation.language                  ? 
_citation.page_first                110411 
_citation.page_last                 110411 
_citation.title                     
'Structural insights into nucleocapsid protein variability: Implications for PJ34 efficacy against SARS-CoV-2.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.virol.2025.110411 
_citation.pdbx_database_id_PubMed   39848104 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yamamoto, A.'   1 ? 
primary 'Ito, H.'        2 ? 
primary 'Sakaguchi, T.'  3 ? 
primary 'Higashiura, A.' 4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Nucleoprotein              13743.378 1   ? ? 'N-terminal domain' ? 
2 polymer     man Nucleoprotein              14100.698 1   ? ? ?                   ? 
3 polymer     man Nucleoprotein              13971.584 1   ? ? ?                   ? 
4 polymer     man Nucleoprotein              13857.481 1   ? ? ?                   ? 
5 non-polymer syn "URIDINE-5'-MONOPHOSPHATE" 324.181   1   ? ? ?                   ? 
6 non-polymer nat 'PHOSPHATE ION'            94.971    1   ? ? ?                   ? 
7 water       nat water                      18.015    263 ? ? ?                   ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'N,Nucleocapsid protein,NC,Protein N' 
2 'N,Nucleocapsid protein,NC,Protein N' 
3 'N,Nucleocapsid protein,NC,Protein N' 
4 'N,Nucleocapsid protein,NC,Protein N' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;TASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKD
GIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
;TASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKD
GIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
A ? 
2 'polypeptide(L)' no no 
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAE
;
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAE
;
B ? 
3 'polypeptide(L)' no no 
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
C ? 
4 'polypeptide(L)' no no 
;NTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANK
DGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
;NTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANK
DGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 "URIDINE-5'-MONOPHOSPHATE" U   
6 'PHOSPHATE ION'            PO4 
7 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ALA n 
1 3   SER n 
1 4   TRP n 
1 5   PHE n 
1 6   THR n 
1 7   ALA n 
1 8   LEU n 
1 9   THR n 
1 10  GLN n 
1 11  HIS n 
1 12  GLY n 
1 13  LYS n 
1 14  GLU n 
1 15  ASP n 
1 16  LEU n 
1 17  LYS n 
1 18  PHE n 
1 19  PRO n 
1 20  ARG n 
1 21  GLY n 
1 22  GLN n 
1 23  GLY n 
1 24  VAL n 
1 25  PRO n 
1 26  ILE n 
1 27  ASN n 
1 28  THR n 
1 29  ASN n 
1 30  SER n 
1 31  SER n 
1 32  PRO n 
1 33  ASP n 
1 34  ASP n 
1 35  GLN n 
1 36  ILE n 
1 37  GLY n 
1 38  TYR n 
1 39  TYR n 
1 40  ARG n 
1 41  ARG n 
1 42  ALA n 
1 43  THR n 
1 44  ARG n 
1 45  ARG n 
1 46  ILE n 
1 47  ARG n 
1 48  GLY n 
1 49  GLY n 
1 50  ASP n 
1 51  GLY n 
1 52  LYS n 
1 53  MET n 
1 54  LYS n 
1 55  ASP n 
1 56  LEU n 
1 57  SER n 
1 58  PRO n 
1 59  ARG n 
1 60  TRP n 
1 61  TYR n 
1 62  PHE n 
1 63  TYR n 
1 64  TYR n 
1 65  LEU n 
1 66  GLY n 
1 67  THR n 
1 68  GLY n 
1 69  PRO n 
1 70  GLU n 
1 71  ALA n 
1 72  GLY n 
1 73  LEU n 
1 74  PRO n 
1 75  TYR n 
1 76  GLY n 
1 77  ALA n 
1 78  ASN n 
1 79  LYS n 
1 80  ASP n 
1 81  GLY n 
1 82  ILE n 
1 83  ILE n 
1 84  TRP n 
1 85  VAL n 
1 86  ALA n 
1 87  THR n 
1 88  GLU n 
1 89  GLY n 
1 90  ALA n 
1 91  LEU n 
1 92  ASN n 
1 93  THR n 
1 94  PRO n 
1 95  LYS n 
1 96  ASP n 
1 97  HIS n 
1 98  ILE n 
1 99  GLY n 
1 100 THR n 
1 101 ARG n 
1 102 ASN n 
1 103 PRO n 
1 104 ALA n 
1 105 ASN n 
1 106 ASN n 
1 107 ALA n 
1 108 ALA n 
1 109 ILE n 
1 110 VAL n 
1 111 LEU n 
1 112 GLN n 
1 113 LEU n 
1 114 PRO n 
1 115 GLN n 
1 116 GLY n 
1 117 THR n 
1 118 THR n 
1 119 LEU n 
1 120 PRO n 
1 121 LYS n 
1 122 GLY n 
1 123 PHE n 
1 124 TYR n 
1 125 ALA n 
2 1   ASN n 
2 2   ASN n 
2 3   THR n 
2 4   ALA n 
2 5   SER n 
2 6   TRP n 
2 7   PHE n 
2 8   THR n 
2 9   ALA n 
2 10  LEU n 
2 11  THR n 
2 12  GLN n 
2 13  HIS n 
2 14  GLY n 
2 15  LYS n 
2 16  GLU n 
2 17  ASP n 
2 18  LEU n 
2 19  LYS n 
2 20  PHE n 
2 21  PRO n 
2 22  ARG n 
2 23  GLY n 
2 24  GLN n 
2 25  GLY n 
2 26  VAL n 
2 27  PRO n 
2 28  ILE n 
2 29  ASN n 
2 30  THR n 
2 31  ASN n 
2 32  SER n 
2 33  SER n 
2 34  PRO n 
2 35  ASP n 
2 36  ASP n 
2 37  GLN n 
2 38  ILE n 
2 39  GLY n 
2 40  TYR n 
2 41  TYR n 
2 42  ARG n 
2 43  ARG n 
2 44  ALA n 
2 45  THR n 
2 46  ARG n 
2 47  ARG n 
2 48  ILE n 
2 49  ARG n 
2 50  GLY n 
2 51  GLY n 
2 52  ASP n 
2 53  GLY n 
2 54  LYS n 
2 55  MET n 
2 56  LYS n 
2 57  ASP n 
2 58  LEU n 
2 59  SER n 
2 60  PRO n 
2 61  ARG n 
2 62  TRP n 
2 63  TYR n 
2 64  PHE n 
2 65  TYR n 
2 66  TYR n 
2 67  LEU n 
2 68  GLY n 
2 69  THR n 
2 70  GLY n 
2 71  PRO n 
2 72  GLU n 
2 73  ALA n 
2 74  GLY n 
2 75  LEU n 
2 76  PRO n 
2 77  TYR n 
2 78  GLY n 
2 79  ALA n 
2 80  ASN n 
2 81  LYS n 
2 82  ASP n 
2 83  GLY n 
2 84  ILE n 
2 85  ILE n 
2 86  TRP n 
2 87  VAL n 
2 88  ALA n 
2 89  THR n 
2 90  GLU n 
2 91  GLY n 
2 92  ALA n 
2 93  LEU n 
2 94  ASN n 
2 95  THR n 
2 96  PRO n 
2 97  LYS n 
2 98  ASP n 
2 99  HIS n 
2 100 ILE n 
2 101 GLY n 
2 102 THR n 
2 103 ARG n 
2 104 ASN n 
2 105 PRO n 
2 106 ALA n 
2 107 ASN n 
2 108 ASN n 
2 109 ALA n 
2 110 ALA n 
2 111 ILE n 
2 112 VAL n 
2 113 LEU n 
2 114 GLN n 
2 115 LEU n 
2 116 PRO n 
2 117 GLN n 
2 118 GLY n 
2 119 THR n 
2 120 THR n 
2 121 LEU n 
2 122 PRO n 
2 123 LYS n 
2 124 GLY n 
2 125 PHE n 
2 126 TYR n 
2 127 ALA n 
2 128 GLU n 
3 1   ASN n 
3 2   ASN n 
3 3   THR n 
3 4   ALA n 
3 5   SER n 
3 6   TRP n 
3 7   PHE n 
3 8   THR n 
3 9   ALA n 
3 10  LEU n 
3 11  THR n 
3 12  GLN n 
3 13  HIS n 
3 14  GLY n 
3 15  LYS n 
3 16  GLU n 
3 17  ASP n 
3 18  LEU n 
3 19  LYS n 
3 20  PHE n 
3 21  PRO n 
3 22  ARG n 
3 23  GLY n 
3 24  GLN n 
3 25  GLY n 
3 26  VAL n 
3 27  PRO n 
3 28  ILE n 
3 29  ASN n 
3 30  THR n 
3 31  ASN n 
3 32  SER n 
3 33  SER n 
3 34  PRO n 
3 35  ASP n 
3 36  ASP n 
3 37  GLN n 
3 38  ILE n 
3 39  GLY n 
3 40  TYR n 
3 41  TYR n 
3 42  ARG n 
3 43  ARG n 
3 44  ALA n 
3 45  THR n 
3 46  ARG n 
3 47  ARG n 
3 48  ILE n 
3 49  ARG n 
3 50  GLY n 
3 51  GLY n 
3 52  ASP n 
3 53  GLY n 
3 54  LYS n 
3 55  MET n 
3 56  LYS n 
3 57  ASP n 
3 58  LEU n 
3 59  SER n 
3 60  PRO n 
3 61  ARG n 
3 62  TRP n 
3 63  TYR n 
3 64  PHE n 
3 65  TYR n 
3 66  TYR n 
3 67  LEU n 
3 68  GLY n 
3 69  THR n 
3 70  GLY n 
3 71  PRO n 
3 72  GLU n 
3 73  ALA n 
3 74  GLY n 
3 75  LEU n 
3 76  PRO n 
3 77  TYR n 
3 78  GLY n 
3 79  ALA n 
3 80  ASN n 
3 81  LYS n 
3 82  ASP n 
3 83  GLY n 
3 84  ILE n 
3 85  ILE n 
3 86  TRP n 
3 87  VAL n 
3 88  ALA n 
3 89  THR n 
3 90  GLU n 
3 91  GLY n 
3 92  ALA n 
3 93  LEU n 
3 94  ASN n 
3 95  THR n 
3 96  PRO n 
3 97  LYS n 
3 98  ASP n 
3 99  HIS n 
3 100 ILE n 
3 101 GLY n 
3 102 THR n 
3 103 ARG n 
3 104 ASN n 
3 105 PRO n 
3 106 ALA n 
3 107 ASN n 
3 108 ASN n 
3 109 ALA n 
3 110 ALA n 
3 111 ILE n 
3 112 VAL n 
3 113 LEU n 
3 114 GLN n 
3 115 LEU n 
3 116 PRO n 
3 117 GLN n 
3 118 GLY n 
3 119 THR n 
3 120 THR n 
3 121 LEU n 
3 122 PRO n 
3 123 LYS n 
3 124 GLY n 
3 125 PHE n 
3 126 TYR n 
3 127 ALA n 
4 1   ASN n 
4 2   THR n 
4 3   ALA n 
4 4   SER n 
4 5   TRP n 
4 6   PHE n 
4 7   THR n 
4 8   ALA n 
4 9   LEU n 
4 10  THR n 
4 11  GLN n 
4 12  HIS n 
4 13  GLY n 
4 14  LYS n 
4 15  GLU n 
4 16  ASP n 
4 17  LEU n 
4 18  LYS n 
4 19  PHE n 
4 20  PRO n 
4 21  ARG n 
4 22  GLY n 
4 23  GLN n 
4 24  GLY n 
4 25  VAL n 
4 26  PRO n 
4 27  ILE n 
4 28  ASN n 
4 29  THR n 
4 30  ASN n 
4 31  SER n 
4 32  SER n 
4 33  PRO n 
4 34  ASP n 
4 35  ASP n 
4 36  GLN n 
4 37  ILE n 
4 38  GLY n 
4 39  TYR n 
4 40  TYR n 
4 41  ARG n 
4 42  ARG n 
4 43  ALA n 
4 44  THR n 
4 45  ARG n 
4 46  ARG n 
4 47  ILE n 
4 48  ARG n 
4 49  GLY n 
4 50  GLY n 
4 51  ASP n 
4 52  GLY n 
4 53  LYS n 
4 54  MET n 
4 55  LYS n 
4 56  ASP n 
4 57  LEU n 
4 58  SER n 
4 59  PRO n 
4 60  ARG n 
4 61  TRP n 
4 62  TYR n 
4 63  PHE n 
4 64  TYR n 
4 65  TYR n 
4 66  LEU n 
4 67  GLY n 
4 68  THR n 
4 69  GLY n 
4 70  PRO n 
4 71  GLU n 
4 72  ALA n 
4 73  GLY n 
4 74  LEU n 
4 75  PRO n 
4 76  TYR n 
4 77  GLY n 
4 78  ALA n 
4 79  ASN n 
4 80  LYS n 
4 81  ASP n 
4 82  GLY n 
4 83  ILE n 
4 84  ILE n 
4 85  TRP n 
4 86  VAL n 
4 87  ALA n 
4 88  THR n 
4 89  GLU n 
4 90  GLY n 
4 91  ALA n 
4 92  LEU n 
4 93  ASN n 
4 94  THR n 
4 95  PRO n 
4 96  LYS n 
4 97  ASP n 
4 98  HIS n 
4 99  ILE n 
4 100 GLY n 
4 101 THR n 
4 102 ARG n 
4 103 ASN n 
4 104 PRO n 
4 105 ALA n 
4 106 ASN n 
4 107 ASN n 
4 108 ALA n 
4 109 ALA n 
4 110 ILE n 
4 111 VAL n 
4 112 LEU n 
4 113 GLN n 
4 114 LEU n 
4 115 PRO n 
4 116 GLN n 
4 117 GLY n 
4 118 THR n 
4 119 THR n 
4 120 LEU n 
4 121 PRO n 
4 122 LYS n 
4 123 GLY n 
4 124 PHE n 
4 125 TYR n 
4 126 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 125 ? ? ? ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 128 ? ? ? ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 127 ? ? ? ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 126 ? ? ? ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                    ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                   ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                      ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'            ? 'O4 P -3'        94.971  
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 
U   'RNA linking'       y "URIDINE-5'-MONOPHOSPHATE" ? 'C9 H13 N2 O9 P' 324.181 
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   THR 1   49  49  THR THR A . n 
A 1 2   ALA 2   50  50  ALA ALA A . n 
A 1 3   SER 3   51  51  SER SER A . n 
A 1 4   TRP 4   52  52  TRP TRP A . n 
A 1 5   PHE 5   53  53  PHE PHE A . n 
A 1 6   THR 6   54  54  THR THR A . n 
A 1 7   ALA 7   55  55  ALA ALA A . n 
A 1 8   LEU 8   56  56  LEU LEU A . n 
A 1 9   THR 9   57  57  THR THR A . n 
A 1 10  GLN 10  58  58  GLN GLN A . n 
A 1 11  HIS 11  59  59  HIS HIS A . n 
A 1 12  GLY 12  60  60  GLY GLY A . n 
A 1 13  LYS 13  61  61  LYS LYS A . n 
A 1 14  GLU 14  62  62  GLU GLU A . n 
A 1 15  ASP 15  63  63  ASP ASP A . n 
A 1 16  LEU 16  64  64  LEU LEU A . n 
A 1 17  LYS 17  65  65  LYS LYS A . n 
A 1 18  PHE 18  66  66  PHE PHE A . n 
A 1 19  PRO 19  67  67  PRO PRO A . n 
A 1 20  ARG 20  68  68  ARG ARG A . n 
A 1 21  GLY 21  69  69  GLY GLY A . n 
A 1 22  GLN 22  70  70  GLN GLN A . n 
A 1 23  GLY 23  71  71  GLY GLY A . n 
A 1 24  VAL 24  72  72  VAL VAL A . n 
A 1 25  PRO 25  73  73  PRO PRO A . n 
A 1 26  ILE 26  74  74  ILE ILE A . n 
A 1 27  ASN 27  75  75  ASN ASN A . n 
A 1 28  THR 28  76  76  THR THR A . n 
A 1 29  ASN 29  77  77  ASN ASN A . n 
A 1 30  SER 30  78  78  SER SER A . n 
A 1 31  SER 31  79  79  SER SER A . n 
A 1 32  PRO 32  80  80  PRO PRO A . n 
A 1 33  ASP 33  81  81  ASP ASP A . n 
A 1 34  ASP 34  82  82  ASP ASP A . n 
A 1 35  GLN 35  83  83  GLN GLN A . n 
A 1 36  ILE 36  84  84  ILE ILE A . n 
A 1 37  GLY 37  85  85  GLY GLY A . n 
A 1 38  TYR 38  86  86  TYR TYR A . n 
A 1 39  TYR 39  87  87  TYR TYR A . n 
A 1 40  ARG 40  88  88  ARG ARG A . n 
A 1 41  ARG 41  89  89  ARG ARG A . n 
A 1 42  ALA 42  90  90  ALA ALA A . n 
A 1 43  THR 43  91  91  THR THR A . n 
A 1 44  ARG 44  92  92  ARG ARG A . n 
A 1 45  ARG 45  93  93  ARG ARG A . n 
A 1 46  ILE 46  94  94  ILE ILE A . n 
A 1 47  ARG 47  95  95  ARG ARG A . n 
A 1 48  GLY 48  96  96  GLY GLY A . n 
A 1 49  GLY 49  97  97  GLY GLY A . n 
A 1 50  ASP 50  98  98  ASP ASP A . n 
A 1 51  GLY 51  99  99  GLY GLY A . n 
A 1 52  LYS 52  100 100 LYS LYS A . n 
A 1 53  MET 53  101 101 MET MET A . n 
A 1 54  LYS 54  102 102 LYS LYS A . n 
A 1 55  ASP 55  103 103 ASP ASP A . n 
A 1 56  LEU 56  104 104 LEU LEU A . n 
A 1 57  SER 57  105 105 SER SER A . n 
A 1 58  PRO 58  106 106 PRO PRO A . n 
A 1 59  ARG 59  107 107 ARG ARG A . n 
A 1 60  TRP 60  108 108 TRP TRP A . n 
A 1 61  TYR 61  109 109 TYR TYR A . n 
A 1 62  PHE 62  110 110 PHE PHE A . n 
A 1 63  TYR 63  111 111 TYR TYR A . n 
A 1 64  TYR 64  112 112 TYR TYR A . n 
A 1 65  LEU 65  113 113 LEU LEU A . n 
A 1 66  GLY 66  114 114 GLY GLY A . n 
A 1 67  THR 67  115 115 THR THR A . n 
A 1 68  GLY 68  116 116 GLY GLY A . n 
A 1 69  PRO 69  117 117 PRO PRO A . n 
A 1 70  GLU 70  118 118 GLU GLU A . n 
A 1 71  ALA 71  119 119 ALA ALA A . n 
A 1 72  GLY 72  120 120 GLY GLY A . n 
A 1 73  LEU 73  121 121 LEU LEU A . n 
A 1 74  PRO 74  122 122 PRO PRO A . n 
A 1 75  TYR 75  123 123 TYR TYR A . n 
A 1 76  GLY 76  124 124 GLY GLY A . n 
A 1 77  ALA 77  125 125 ALA ALA A . n 
A 1 78  ASN 78  126 126 ASN ASN A . n 
A 1 79  LYS 79  127 127 LYS LYS A . n 
A 1 80  ASP 80  128 128 ASP ASP A . n 
A 1 81  GLY 81  129 129 GLY GLY A . n 
A 1 82  ILE 82  130 130 ILE ILE A . n 
A 1 83  ILE 83  131 131 ILE ILE A . n 
A 1 84  TRP 84  132 132 TRP TRP A . n 
A 1 85  VAL 85  133 133 VAL VAL A . n 
A 1 86  ALA 86  134 134 ALA ALA A . n 
A 1 87  THR 87  135 135 THR THR A . n 
A 1 88  GLU 88  136 136 GLU GLU A . n 
A 1 89  GLY 89  137 137 GLY GLY A . n 
A 1 90  ALA 90  138 138 ALA ALA A . n 
A 1 91  LEU 91  139 139 LEU LEU A . n 
A 1 92  ASN 92  140 140 ASN ASN A . n 
A 1 93  THR 93  141 141 THR THR A . n 
A 1 94  PRO 94  142 142 PRO PRO A . n 
A 1 95  LYS 95  143 143 LYS LYS A . n 
A 1 96  ASP 96  144 144 ASP ASP A . n 
A 1 97  HIS 97  145 145 HIS HIS A . n 
A 1 98  ILE 98  146 146 ILE ILE A . n 
A 1 99  GLY 99  147 147 GLY GLY A . n 
A 1 100 THR 100 148 148 THR THR A . n 
A 1 101 ARG 101 149 149 ARG ARG A . n 
A 1 102 ASN 102 150 150 ASN ASN A . n 
A 1 103 PRO 103 151 151 PRO PRO A . n 
A 1 104 ALA 104 152 152 ALA ALA A . n 
A 1 105 ASN 105 153 153 ASN ASN A . n 
A 1 106 ASN 106 154 154 ASN ASN A . n 
A 1 107 ALA 107 155 155 ALA ALA A . n 
A 1 108 ALA 108 156 156 ALA ALA A . n 
A 1 109 ILE 109 157 157 ILE ILE A . n 
A 1 110 VAL 110 158 158 VAL VAL A . n 
A 1 111 LEU 111 159 159 LEU LEU A . n 
A 1 112 GLN 112 160 160 GLN GLN A . n 
A 1 113 LEU 113 161 161 LEU LEU A . n 
A 1 114 PRO 114 162 162 PRO PRO A . n 
A 1 115 GLN 115 163 163 GLN GLN A . n 
A 1 116 GLY 116 164 164 GLY GLY A . n 
A 1 117 THR 117 165 165 THR THR A . n 
A 1 118 THR 118 166 166 THR THR A . n 
A 1 119 LEU 119 167 167 LEU LEU A . n 
A 1 120 PRO 120 168 168 PRO PRO A . n 
A 1 121 LYS 121 169 169 LYS LYS A . n 
A 1 122 GLY 122 170 170 GLY GLY A . n 
A 1 123 PHE 123 171 171 PHE PHE A . n 
A 1 124 TYR 124 172 172 TYR TYR A . n 
A 1 125 ALA 125 173 173 ALA ALA A . n 
B 2 1   ASN 1   47  47  ASN ASN B . n 
B 2 2   ASN 2   48  48  ASN ASN B . n 
B 2 3   THR 3   49  49  THR THR B . n 
B 2 4   ALA 4   50  50  ALA ALA B . n 
B 2 5   SER 5   51  51  SER SER B . n 
B 2 6   TRP 6   52  52  TRP TRP B . n 
B 2 7   PHE 7   53  53  PHE PHE B . n 
B 2 8   THR 8   54  54  THR THR B . n 
B 2 9   ALA 9   55  55  ALA ALA B . n 
B 2 10  LEU 10  56  56  LEU LEU B . n 
B 2 11  THR 11  57  57  THR THR B . n 
B 2 12  GLN 12  58  58  GLN GLN B . n 
B 2 13  HIS 13  59  59  HIS HIS B . n 
B 2 14  GLY 14  60  60  GLY GLY B . n 
B 2 15  LYS 15  61  61  LYS LYS B . n 
B 2 16  GLU 16  62  62  GLU GLU B . n 
B 2 17  ASP 17  63  63  ASP ASP B . n 
B 2 18  LEU 18  64  64  LEU LEU B . n 
B 2 19  LYS 19  65  65  LYS LYS B . n 
B 2 20  PHE 20  66  66  PHE PHE B . n 
B 2 21  PRO 21  67  67  PRO PRO B . n 
B 2 22  ARG 22  68  68  ARG ARG B . n 
B 2 23  GLY 23  69  69  GLY GLY B . n 
B 2 24  GLN 24  70  70  GLN GLN B . n 
B 2 25  GLY 25  71  71  GLY GLY B . n 
B 2 26  VAL 26  72  72  VAL VAL B . n 
B 2 27  PRO 27  73  73  PRO PRO B . n 
B 2 28  ILE 28  74  74  ILE ILE B . n 
B 2 29  ASN 29  75  75  ASN ASN B . n 
B 2 30  THR 30  76  76  THR THR B . n 
B 2 31  ASN 31  77  77  ASN ASN B . n 
B 2 32  SER 32  78  78  SER SER B . n 
B 2 33  SER 33  79  79  SER SER B . n 
B 2 34  PRO 34  80  80  PRO PRO B . n 
B 2 35  ASP 35  81  81  ASP ASP B . n 
B 2 36  ASP 36  82  82  ASP ASP B . n 
B 2 37  GLN 37  83  83  GLN GLN B . n 
B 2 38  ILE 38  84  84  ILE ILE B . n 
B 2 39  GLY 39  85  85  GLY GLY B . n 
B 2 40  TYR 40  86  86  TYR TYR B . n 
B 2 41  TYR 41  87  87  TYR TYR B . n 
B 2 42  ARG 42  88  88  ARG ARG B . n 
B 2 43  ARG 43  89  89  ARG ARG B . n 
B 2 44  ALA 44  90  90  ALA ALA B . n 
B 2 45  THR 45  91  91  THR THR B . n 
B 2 46  ARG 46  92  92  ARG ARG B . n 
B 2 47  ARG 47  93  93  ARG ARG B . n 
B 2 48  ILE 48  94  94  ILE ILE B . n 
B 2 49  ARG 49  95  95  ARG ARG B . n 
B 2 50  GLY 50  96  96  GLY GLY B . n 
B 2 51  GLY 51  97  97  GLY GLY B . n 
B 2 52  ASP 52  98  98  ASP ASP B . n 
B 2 53  GLY 53  99  99  GLY GLY B . n 
B 2 54  LYS 54  100 100 LYS LYS B . n 
B 2 55  MET 55  101 101 MET MET B . n 
B 2 56  LYS 56  102 102 LYS LYS B . n 
B 2 57  ASP 57  103 103 ASP ASP B . n 
B 2 58  LEU 58  104 104 LEU LEU B . n 
B 2 59  SER 59  105 105 SER SER B . n 
B 2 60  PRO 60  106 106 PRO PRO B . n 
B 2 61  ARG 61  107 107 ARG ARG B . n 
B 2 62  TRP 62  108 108 TRP TRP B . n 
B 2 63  TYR 63  109 109 TYR TYR B . n 
B 2 64  PHE 64  110 110 PHE PHE B . n 
B 2 65  TYR 65  111 111 TYR TYR B . n 
B 2 66  TYR 66  112 112 TYR TYR B . n 
B 2 67  LEU 67  113 113 LEU LEU B . n 
B 2 68  GLY 68  114 114 GLY GLY B . n 
B 2 69  THR 69  115 115 THR THR B . n 
B 2 70  GLY 70  116 116 GLY GLY B . n 
B 2 71  PRO 71  117 117 PRO PRO B . n 
B 2 72  GLU 72  118 118 GLU GLU B . n 
B 2 73  ALA 73  119 119 ALA ALA B . n 
B 2 74  GLY 74  120 120 GLY GLY B . n 
B 2 75  LEU 75  121 121 LEU LEU B . n 
B 2 76  PRO 76  122 122 PRO PRO B . n 
B 2 77  TYR 77  123 123 TYR TYR B . n 
B 2 78  GLY 78  124 124 GLY GLY B . n 
B 2 79  ALA 79  125 125 ALA ALA B . n 
B 2 80  ASN 80  126 126 ASN ASN B . n 
B 2 81  LYS 81  127 127 LYS LYS B . n 
B 2 82  ASP 82  128 128 ASP ASP B . n 
B 2 83  GLY 83  129 129 GLY GLY B . n 
B 2 84  ILE 84  130 130 ILE ILE B . n 
B 2 85  ILE 85  131 131 ILE ILE B . n 
B 2 86  TRP 86  132 132 TRP TRP B . n 
B 2 87  VAL 87  133 133 VAL VAL B . n 
B 2 88  ALA 88  134 134 ALA ALA B . n 
B 2 89  THR 89  135 135 THR THR B . n 
B 2 90  GLU 90  136 136 GLU GLU B . n 
B 2 91  GLY 91  137 137 GLY GLY B . n 
B 2 92  ALA 92  138 138 ALA ALA B . n 
B 2 93  LEU 93  139 139 LEU LEU B . n 
B 2 94  ASN 94  140 140 ASN ASN B . n 
B 2 95  THR 95  141 141 THR THR B . n 
B 2 96  PRO 96  142 142 PRO PRO B . n 
B 2 97  LYS 97  143 143 LYS LYS B . n 
B 2 98  ASP 98  144 144 ASP ASP B . n 
B 2 99  HIS 99  145 145 HIS HIS B . n 
B 2 100 ILE 100 146 146 ILE ILE B . n 
B 2 101 GLY 101 147 147 GLY GLY B . n 
B 2 102 THR 102 148 148 THR THR B . n 
B 2 103 ARG 103 149 149 ARG ARG B . n 
B 2 104 ASN 104 150 150 ASN ASN B . n 
B 2 105 PRO 105 151 151 PRO PRO B . n 
B 2 106 ALA 106 152 152 ALA ALA B . n 
B 2 107 ASN 107 153 153 ASN ASN B . n 
B 2 108 ASN 108 154 154 ASN ASN B . n 
B 2 109 ALA 109 155 155 ALA ALA B . n 
B 2 110 ALA 110 156 156 ALA ALA B . n 
B 2 111 ILE 111 157 157 ILE ILE B . n 
B 2 112 VAL 112 158 158 VAL VAL B . n 
B 2 113 LEU 113 159 159 LEU LEU B . n 
B 2 114 GLN 114 160 160 GLN GLN B . n 
B 2 115 LEU 115 161 161 LEU LEU B . n 
B 2 116 PRO 116 162 162 PRO PRO B . n 
B 2 117 GLN 117 163 163 GLN GLN B . n 
B 2 118 GLY 118 164 164 GLY GLY B . n 
B 2 119 THR 119 165 165 THR THR B . n 
B 2 120 THR 120 166 166 THR THR B . n 
B 2 121 LEU 121 167 167 LEU LEU B . n 
B 2 122 PRO 122 168 168 PRO PRO B . n 
B 2 123 LYS 123 169 169 LYS LYS B . n 
B 2 124 GLY 124 170 170 GLY GLY B . n 
B 2 125 PHE 125 171 171 PHE PHE B . n 
B 2 126 TYR 126 172 172 TYR TYR B . n 
B 2 127 ALA 127 173 173 ALA ALA B . n 
B 2 128 GLU 128 174 174 GLU GLU B . n 
C 3 1   ASN 1   47  47  ASN ASN C . n 
C 3 2   ASN 2   48  48  ASN ASN C . n 
C 3 3   THR 3   49  49  THR THR C . n 
C 3 4   ALA 4   50  50  ALA ALA C . n 
C 3 5   SER 5   51  51  SER SER C . n 
C 3 6   TRP 6   52  52  TRP TRP C . n 
C 3 7   PHE 7   53  53  PHE PHE C . n 
C 3 8   THR 8   54  54  THR THR C . n 
C 3 9   ALA 9   55  55  ALA ALA C . n 
C 3 10  LEU 10  56  56  LEU LEU C . n 
C 3 11  THR 11  57  57  THR THR C . n 
C 3 12  GLN 12  58  58  GLN GLN C . n 
C 3 13  HIS 13  59  59  HIS HIS C . n 
C 3 14  GLY 14  60  60  GLY GLY C . n 
C 3 15  LYS 15  61  61  LYS LYS C . n 
C 3 16  GLU 16  62  62  GLU GLU C . n 
C 3 17  ASP 17  63  63  ASP ASP C . n 
C 3 18  LEU 18  64  64  LEU LEU C . n 
C 3 19  LYS 19  65  65  LYS LYS C . n 
C 3 20  PHE 20  66  66  PHE PHE C . n 
C 3 21  PRO 21  67  67  PRO PRO C . n 
C 3 22  ARG 22  68  68  ARG ARG C . n 
C 3 23  GLY 23  69  69  GLY GLY C . n 
C 3 24  GLN 24  70  70  GLN GLN C . n 
C 3 25  GLY 25  71  71  GLY GLY C . n 
C 3 26  VAL 26  72  72  VAL VAL C . n 
C 3 27  PRO 27  73  73  PRO PRO C . n 
C 3 28  ILE 28  74  74  ILE ILE C . n 
C 3 29  ASN 29  75  75  ASN ASN C . n 
C 3 30  THR 30  76  76  THR THR C . n 
C 3 31  ASN 31  77  77  ASN ASN C . n 
C 3 32  SER 32  78  78  SER SER C . n 
C 3 33  SER 33  79  79  SER SER C . n 
C 3 34  PRO 34  80  80  PRO PRO C . n 
C 3 35  ASP 35  81  81  ASP ASP C . n 
C 3 36  ASP 36  82  82  ASP ASP C . n 
C 3 37  GLN 37  83  83  GLN GLN C . n 
C 3 38  ILE 38  84  84  ILE ILE C . n 
C 3 39  GLY 39  85  85  GLY GLY C . n 
C 3 40  TYR 40  86  86  TYR TYR C . n 
C 3 41  TYR 41  87  87  TYR TYR C . n 
C 3 42  ARG 42  88  88  ARG ARG C . n 
C 3 43  ARG 43  89  89  ARG ARG C . n 
C 3 44  ALA 44  90  90  ALA ALA C . n 
C 3 45  THR 45  91  91  THR THR C . n 
C 3 46  ARG 46  92  92  ARG ARG C . n 
C 3 47  ARG 47  93  93  ARG ARG C . n 
C 3 48  ILE 48  94  94  ILE ILE C . n 
C 3 49  ARG 49  95  95  ARG ARG C . n 
C 3 50  GLY 50  96  96  GLY GLY C . n 
C 3 51  GLY 51  97  97  GLY GLY C . n 
C 3 52  ASP 52  98  98  ASP ASP C . n 
C 3 53  GLY 53  99  99  GLY GLY C . n 
C 3 54  LYS 54  100 100 LYS LYS C . n 
C 3 55  MET 55  101 101 MET MET C . n 
C 3 56  LYS 56  102 102 LYS LYS C . n 
C 3 57  ASP 57  103 103 ASP ASP C . n 
C 3 58  LEU 58  104 104 LEU LEU C . n 
C 3 59  SER 59  105 105 SER SER C . n 
C 3 60  PRO 60  106 106 PRO PRO C . n 
C 3 61  ARG 61  107 107 ARG ARG C . n 
C 3 62  TRP 62  108 108 TRP TRP C . n 
C 3 63  TYR 63  109 109 TYR TYR C . n 
C 3 64  PHE 64  110 110 PHE PHE C . n 
C 3 65  TYR 65  111 111 TYR TYR C . n 
C 3 66  TYR 66  112 112 TYR TYR C . n 
C 3 67  LEU 67  113 113 LEU LEU C . n 
C 3 68  GLY 68  114 114 GLY GLY C . n 
C 3 69  THR 69  115 115 THR THR C . n 
C 3 70  GLY 70  116 116 GLY GLY C . n 
C 3 71  PRO 71  117 117 PRO PRO C . n 
C 3 72  GLU 72  118 118 GLU GLU C . n 
C 3 73  ALA 73  119 119 ALA ALA C . n 
C 3 74  GLY 74  120 120 GLY GLY C . n 
C 3 75  LEU 75  121 121 LEU LEU C . n 
C 3 76  PRO 76  122 122 PRO PRO C . n 
C 3 77  TYR 77  123 123 TYR TYR C . n 
C 3 78  GLY 78  124 124 GLY GLY C . n 
C 3 79  ALA 79  125 125 ALA ALA C . n 
C 3 80  ASN 80  126 126 ASN ASN C . n 
C 3 81  LYS 81  127 127 LYS LYS C . n 
C 3 82  ASP 82  128 128 ASP ASP C . n 
C 3 83  GLY 83  129 129 GLY GLY C . n 
C 3 84  ILE 84  130 130 ILE ILE C . n 
C 3 85  ILE 85  131 131 ILE ILE C . n 
C 3 86  TRP 86  132 132 TRP TRP C . n 
C 3 87  VAL 87  133 133 VAL VAL C . n 
C 3 88  ALA 88  134 134 ALA ALA C . n 
C 3 89  THR 89  135 135 THR THR C . n 
C 3 90  GLU 90  136 136 GLU GLU C . n 
C 3 91  GLY 91  137 137 GLY GLY C . n 
C 3 92  ALA 92  138 138 ALA ALA C . n 
C 3 93  LEU 93  139 139 LEU LEU C . n 
C 3 94  ASN 94  140 140 ASN ASN C . n 
C 3 95  THR 95  141 141 THR THR C . n 
C 3 96  PRO 96  142 142 PRO PRO C . n 
C 3 97  LYS 97  143 143 LYS LYS C . n 
C 3 98  ASP 98  144 144 ASP ASP C . n 
C 3 99  HIS 99  145 145 HIS HIS C . n 
C 3 100 ILE 100 146 146 ILE ILE C . n 
C 3 101 GLY 101 147 147 GLY GLY C . n 
C 3 102 THR 102 148 148 THR THR C . n 
C 3 103 ARG 103 149 149 ARG ARG C . n 
C 3 104 ASN 104 150 150 ASN ASN C . n 
C 3 105 PRO 105 151 151 PRO PRO C . n 
C 3 106 ALA 106 152 152 ALA ALA C . n 
C 3 107 ASN 107 153 153 ASN ASN C . n 
C 3 108 ASN 108 154 154 ASN ASN C . n 
C 3 109 ALA 109 155 155 ALA ALA C . n 
C 3 110 ALA 110 156 156 ALA ALA C . n 
C 3 111 ILE 111 157 157 ILE ILE C . n 
C 3 112 VAL 112 158 158 VAL VAL C . n 
C 3 113 LEU 113 159 159 LEU LEU C . n 
C 3 114 GLN 114 160 160 GLN GLN C . n 
C 3 115 LEU 115 161 161 LEU LEU C . n 
C 3 116 PRO 116 162 162 PRO PRO C . n 
C 3 117 GLN 117 163 163 GLN GLN C . n 
C 3 118 GLY 118 164 164 GLY GLY C . n 
C 3 119 THR 119 165 165 THR THR C . n 
C 3 120 THR 120 166 166 THR THR C . n 
C 3 121 LEU 121 167 167 LEU LEU C . n 
C 3 122 PRO 122 168 168 PRO PRO C . n 
C 3 123 LYS 123 169 169 LYS LYS C . n 
C 3 124 GLY 124 170 170 GLY GLY C . n 
C 3 125 PHE 125 171 171 PHE PHE C . n 
C 3 126 TYR 126 172 172 TYR TYR C . n 
C 3 127 ALA 127 173 173 ALA ALA C . n 
D 4 1   ASN 1   48  48  ASN ASN D . n 
D 4 2   THR 2   49  49  THR THR D . n 
D 4 3   ALA 3   50  50  ALA ALA D . n 
D 4 4   SER 4   51  51  SER SER D . n 
D 4 5   TRP 5   52  52  TRP TRP D . n 
D 4 6   PHE 6   53  53  PHE PHE D . n 
D 4 7   THR 7   54  54  THR THR D . n 
D 4 8   ALA 8   55  55  ALA ALA D . n 
D 4 9   LEU 9   56  56  LEU LEU D . n 
D 4 10  THR 10  57  57  THR THR D . n 
D 4 11  GLN 11  58  58  GLN GLN D . n 
D 4 12  HIS 12  59  59  HIS HIS D . n 
D 4 13  GLY 13  60  60  GLY GLY D . n 
D 4 14  LYS 14  61  61  LYS LYS D . n 
D 4 15  GLU 15  62  62  GLU GLU D . n 
D 4 16  ASP 16  63  63  ASP ASP D . n 
D 4 17  LEU 17  64  64  LEU LEU D . n 
D 4 18  LYS 18  65  65  LYS LYS D . n 
D 4 19  PHE 19  66  66  PHE PHE D . n 
D 4 20  PRO 20  67  67  PRO PRO D . n 
D 4 21  ARG 21  68  68  ARG ARG D . n 
D 4 22  GLY 22  69  69  GLY GLY D . n 
D 4 23  GLN 23  70  70  GLN GLN D . n 
D 4 24  GLY 24  71  71  GLY GLY D . n 
D 4 25  VAL 25  72  72  VAL VAL D . n 
D 4 26  PRO 26  73  73  PRO PRO D . n 
D 4 27  ILE 27  74  74  ILE ILE D . n 
D 4 28  ASN 28  75  75  ASN ASN D . n 
D 4 29  THR 29  76  76  THR THR D . n 
D 4 30  ASN 30  77  77  ASN ASN D . n 
D 4 31  SER 31  78  78  SER SER D . n 
D 4 32  SER 32  79  79  SER SER D . n 
D 4 33  PRO 33  80  80  PRO PRO D . n 
D 4 34  ASP 34  81  81  ASP ASP D . n 
D 4 35  ASP 35  82  82  ASP ASP D . n 
D 4 36  GLN 36  83  83  GLN GLN D . n 
D 4 37  ILE 37  84  84  ILE ILE D . n 
D 4 38  GLY 38  85  85  GLY GLY D . n 
D 4 39  TYR 39  86  86  TYR TYR D . n 
D 4 40  TYR 40  87  87  TYR TYR D . n 
D 4 41  ARG 41  88  88  ARG ARG D . n 
D 4 42  ARG 42  89  89  ARG ARG D . n 
D 4 43  ALA 43  90  90  ALA ALA D . n 
D 4 44  THR 44  91  91  THR THR D . n 
D 4 45  ARG 45  92  92  ARG ARG D . n 
D 4 46  ARG 46  93  93  ARG ARG D . n 
D 4 47  ILE 47  94  94  ILE ILE D . n 
D 4 48  ARG 48  95  95  ARG ARG D . n 
D 4 49  GLY 49  96  96  GLY GLY D . n 
D 4 50  GLY 50  97  97  GLY GLY D . n 
D 4 51  ASP 51  98  98  ASP ASP D . n 
D 4 52  GLY 52  99  99  GLY GLY D . n 
D 4 53  LYS 53  100 100 LYS LYS D . n 
D 4 54  MET 54  101 101 MET MET D . n 
D 4 55  LYS 55  102 102 LYS LYS D . n 
D 4 56  ASP 56  103 103 ASP ASP D . n 
D 4 57  LEU 57  104 104 LEU LEU D . n 
D 4 58  SER 58  105 105 SER SER D . n 
D 4 59  PRO 59  106 106 PRO PRO D . n 
D 4 60  ARG 60  107 107 ARG ARG D . n 
D 4 61  TRP 61  108 108 TRP TRP D . n 
D 4 62  TYR 62  109 109 TYR TYR D . n 
D 4 63  PHE 63  110 110 PHE PHE D . n 
D 4 64  TYR 64  111 111 TYR TYR D . n 
D 4 65  TYR 65  112 112 TYR TYR D . n 
D 4 66  LEU 66  113 113 LEU LEU D . n 
D 4 67  GLY 67  114 114 GLY GLY D . n 
D 4 68  THR 68  115 115 THR THR D . n 
D 4 69  GLY 69  116 116 GLY GLY D . n 
D 4 70  PRO 70  117 117 PRO PRO D . n 
D 4 71  GLU 71  118 118 GLU GLU D . n 
D 4 72  ALA 72  119 119 ALA ALA D . n 
D 4 73  GLY 73  120 120 GLY GLY D . n 
D 4 74  LEU 74  121 121 LEU LEU D . n 
D 4 75  PRO 75  122 122 PRO PRO D . n 
D 4 76  TYR 76  123 123 TYR TYR D . n 
D 4 77  GLY 77  124 124 GLY GLY D . n 
D 4 78  ALA 78  125 125 ALA ALA D . n 
D 4 79  ASN 79  126 126 ASN ASN D . n 
D 4 80  LYS 80  127 127 LYS LYS D . n 
D 4 81  ASP 81  128 128 ASP ASP D . n 
D 4 82  GLY 82  129 129 GLY GLY D . n 
D 4 83  ILE 83  130 130 ILE ILE D . n 
D 4 84  ILE 84  131 131 ILE ILE D . n 
D 4 85  TRP 85  132 132 TRP TRP D . n 
D 4 86  VAL 86  133 133 VAL VAL D . n 
D 4 87  ALA 87  134 134 ALA ALA D . n 
D 4 88  THR 88  135 135 THR THR D . n 
D 4 89  GLU 89  136 136 GLU GLU D . n 
D 4 90  GLY 90  137 137 GLY GLY D . n 
D 4 91  ALA 91  138 138 ALA ALA D . n 
D 4 92  LEU 92  139 139 LEU LEU D . n 
D 4 93  ASN 93  140 140 ASN ASN D . n 
D 4 94  THR 94  141 141 THR THR D . n 
D 4 95  PRO 95  142 142 PRO PRO D . n 
D 4 96  LYS 96  143 143 LYS LYS D . n 
D 4 97  ASP 97  144 144 ASP ASP D . n 
D 4 98  HIS 98  145 145 HIS HIS D . n 
D 4 99  ILE 99  146 146 ILE ILE D . n 
D 4 100 GLY 100 147 147 GLY GLY D . n 
D 4 101 THR 101 148 148 THR THR D . n 
D 4 102 ARG 102 149 149 ARG ARG D . n 
D 4 103 ASN 103 150 150 ASN ASN D . n 
D 4 104 PRO 104 151 151 PRO PRO D . n 
D 4 105 ALA 105 152 152 ALA ALA D . n 
D 4 106 ASN 106 153 153 ASN ASN D . n 
D 4 107 ASN 107 154 154 ASN ASN D . n 
D 4 108 ALA 108 155 155 ALA ALA D . n 
D 4 109 ALA 109 156 156 ALA ALA D . n 
D 4 110 ILE 110 157 157 ILE ILE D . n 
D 4 111 VAL 111 158 158 VAL VAL D . n 
D 4 112 LEU 112 159 159 LEU LEU D . n 
D 4 113 GLN 113 160 160 GLN GLN D . n 
D 4 114 LEU 114 161 161 LEU LEU D . n 
D 4 115 PRO 115 162 162 PRO PRO D . n 
D 4 116 GLN 116 163 163 GLN GLN D . n 
D 4 117 GLY 117 164 164 GLY GLY D . n 
D 4 118 THR 118 165 165 THR THR D . n 
D 4 119 THR 119 166 166 THR THR D . n 
D 4 120 LEU 120 167 167 LEU LEU D . n 
D 4 121 PRO 121 168 168 PRO PRO D . n 
D 4 122 LYS 122 169 169 LYS LYS D . n 
D 4 123 GLY 123 170 170 GLY GLY D . n 
D 4 124 PHE 124 171 171 PHE PHE D . n 
D 4 125 TYR 125 172 172 TYR TYR D . n 
D 4 126 ALA 126 173 173 ALA ALA D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   U 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 5 U   1  201 201 U   U   A . 
F 6 PO4 1  201 201 PO4 PO4 B . 
G 7 HOH 1  301 46  HOH HOH A . 
G 7 HOH 2  302 19  HOH HOH A . 
G 7 HOH 3  303 206 HOH HOH A . 
G 7 HOH 4  304 35  HOH HOH A . 
G 7 HOH 5  305 22  HOH HOH A . 
G 7 HOH 6  306 65  HOH HOH A . 
G 7 HOH 7  307 11  HOH HOH A . 
G 7 HOH 8  308 216 HOH HOH A . 
G 7 HOH 9  309 169 HOH HOH A . 
G 7 HOH 10 310 31  HOH HOH A . 
G 7 HOH 11 311 93  HOH HOH A . 
G 7 HOH 12 312 52  HOH HOH A . 
G 7 HOH 13 313 188 HOH HOH A . 
G 7 HOH 14 314 164 HOH HOH A . 
G 7 HOH 15 315 160 HOH HOH A . 
G 7 HOH 16 316 17  HOH HOH A . 
G 7 HOH 17 317 245 HOH HOH A . 
G 7 HOH 18 318 21  HOH HOH A . 
G 7 HOH 19 319 72  HOH HOH A . 
G 7 HOH 20 320 137 HOH HOH A . 
G 7 HOH 21 321 3   HOH HOH A . 
G 7 HOH 22 322 78  HOH HOH A . 
G 7 HOH 23 323 190 HOH HOH A . 
G 7 HOH 24 324 14  HOH HOH A . 
G 7 HOH 25 325 70  HOH HOH A . 
G 7 HOH 26 326 57  HOH HOH A . 
G 7 HOH 27 327 126 HOH HOH A . 
G 7 HOH 28 328 181 HOH HOH A . 
G 7 HOH 29 329 138 HOH HOH A . 
G 7 HOH 30 330 254 HOH HOH A . 
G 7 HOH 31 331 4   HOH HOH A . 
G 7 HOH 32 332 119 HOH HOH A . 
G 7 HOH 33 333 15  HOH HOH A . 
G 7 HOH 34 334 50  HOH HOH A . 
G 7 HOH 35 335 209 HOH HOH A . 
G 7 HOH 36 336 54  HOH HOH A . 
G 7 HOH 37 337 151 HOH HOH A . 
G 7 HOH 38 338 67  HOH HOH A . 
G 7 HOH 39 339 205 HOH HOH A . 
G 7 HOH 40 340 179 HOH HOH A . 
G 7 HOH 41 341 55  HOH HOH A . 
G 7 HOH 42 342 139 HOH HOH A . 
G 7 HOH 43 343 33  HOH HOH A . 
G 7 HOH 44 344 110 HOH HOH A . 
G 7 HOH 45 345 103 HOH HOH A . 
G 7 HOH 46 346 85  HOH HOH A . 
G 7 HOH 47 347 39  HOH HOH A . 
G 7 HOH 48 348 75  HOH HOH A . 
G 7 HOH 49 349 66  HOH HOH A . 
G 7 HOH 50 350 29  HOH HOH A . 
G 7 HOH 51 351 271 HOH HOH A . 
G 7 HOH 52 352 38  HOH HOH A . 
G 7 HOH 53 353 79  HOH HOH A . 
G 7 HOH 54 354 236 HOH HOH A . 
G 7 HOH 55 355 176 HOH HOH A . 
G 7 HOH 56 356 157 HOH HOH A . 
G 7 HOH 57 357 43  HOH HOH A . 
G 7 HOH 58 358 211 HOH HOH A . 
G 7 HOH 59 359 123 HOH HOH A . 
G 7 HOH 60 360 53  HOH HOH A . 
G 7 HOH 61 361 101 HOH HOH A . 
G 7 HOH 62 362 122 HOH HOH A . 
G 7 HOH 63 363 149 HOH HOH A . 
G 7 HOH 64 364 7   HOH HOH A . 
G 7 HOH 65 365 233 HOH HOH A . 
G 7 HOH 66 366 165 HOH HOH A . 
G 7 HOH 67 367 247 HOH HOH A . 
G 7 HOH 68 368 87  HOH HOH A . 
G 7 HOH 69 369 96  HOH HOH A . 
G 7 HOH 70 370 186 HOH HOH A . 
G 7 HOH 71 371 248 HOH HOH A . 
G 7 HOH 72 372 229 HOH HOH A . 
G 7 HOH 73 373 153 HOH HOH A . 
G 7 HOH 74 374 155 HOH HOH A . 
G 7 HOH 75 375 144 HOH HOH A . 
G 7 HOH 76 376 100 HOH HOH A . 
G 7 HOH 77 377 220 HOH HOH A . 
G 7 HOH 78 378 120 HOH HOH A . 
G 7 HOH 79 379 235 HOH HOH A . 
G 7 HOH 80 380 28  HOH HOH A . 
G 7 HOH 81 381 121 HOH HOH A . 
G 7 HOH 82 382 232 HOH HOH A . 
G 7 HOH 83 383 175 HOH HOH A . 
G 7 HOH 84 384 135 HOH HOH A . 
G 7 HOH 85 385 161 HOH HOH A . 
H 7 HOH 1  301 18  HOH HOH B . 
H 7 HOH 2  302 180 HOH HOH B . 
H 7 HOH 3  303 128 HOH HOH B . 
H 7 HOH 4  304 131 HOH HOH B . 
H 7 HOH 5  305 88  HOH HOH B . 
H 7 HOH 6  306 166 HOH HOH B . 
H 7 HOH 7  307 45  HOH HOH B . 
H 7 HOH 8  308 32  HOH HOH B . 
H 7 HOH 9  309 91  HOH HOH B . 
H 7 HOH 10 310 261 HOH HOH B . 
H 7 HOH 11 311 106 HOH HOH B . 
H 7 HOH 12 312 64  HOH HOH B . 
H 7 HOH 13 313 152 HOH HOH B . 
H 7 HOH 14 314 200 HOH HOH B . 
H 7 HOH 15 315 224 HOH HOH B . 
H 7 HOH 16 316 198 HOH HOH B . 
H 7 HOH 17 317 250 HOH HOH B . 
H 7 HOH 18 318 130 HOH HOH B . 
H 7 HOH 19 319 196 HOH HOH B . 
H 7 HOH 20 320 24  HOH HOH B . 
H 7 HOH 21 321 74  HOH HOH B . 
H 7 HOH 22 322 195 HOH HOH B . 
H 7 HOH 23 323 133 HOH HOH B . 
H 7 HOH 24 324 94  HOH HOH B . 
H 7 HOH 25 325 1   HOH HOH B . 
H 7 HOH 26 326 140 HOH HOH B . 
H 7 HOH 27 327 60  HOH HOH B . 
H 7 HOH 28 328 10  HOH HOH B . 
H 7 HOH 29 329 48  HOH HOH B . 
H 7 HOH 30 330 27  HOH HOH B . 
H 7 HOH 31 331 41  HOH HOH B . 
H 7 HOH 32 332 257 HOH HOH B . 
H 7 HOH 33 333 251 HOH HOH B . 
H 7 HOH 34 334 40  HOH HOH B . 
H 7 HOH 35 335 26  HOH HOH B . 
H 7 HOH 36 336 265 HOH HOH B . 
H 7 HOH 37 337 73  HOH HOH B . 
H 7 HOH 38 338 90  HOH HOH B . 
H 7 HOH 39 339 218 HOH HOH B . 
H 7 HOH 40 340 12  HOH HOH B . 
H 7 HOH 41 341 62  HOH HOH B . 
H 7 HOH 42 342 219 HOH HOH B . 
H 7 HOH 43 343 95  HOH HOH B . 
H 7 HOH 44 344 244 HOH HOH B . 
H 7 HOH 45 345 263 HOH HOH B . 
H 7 HOH 46 346 49  HOH HOH B . 
H 7 HOH 47 347 210 HOH HOH B . 
H 7 HOH 48 348 83  HOH HOH B . 
H 7 HOH 49 349 30  HOH HOH B . 
H 7 HOH 50 350 116 HOH HOH B . 
H 7 HOH 51 351 77  HOH HOH B . 
H 7 HOH 52 352 129 HOH HOH B . 
H 7 HOH 53 353 146 HOH HOH B . 
H 7 HOH 54 354 168 HOH HOH B . 
H 7 HOH 55 355 242 HOH HOH B . 
H 7 HOH 56 356 134 HOH HOH B . 
H 7 HOH 57 357 225 HOH HOH B . 
H 7 HOH 58 358 69  HOH HOH B . 
H 7 HOH 59 359 76  HOH HOH B . 
H 7 HOH 60 360 171 HOH HOH B . 
H 7 HOH 61 361 237 HOH HOH B . 
H 7 HOH 62 362 124 HOH HOH B . 
H 7 HOH 63 363 187 HOH HOH B . 
H 7 HOH 64 364 202 HOH HOH B . 
H 7 HOH 65 365 246 HOH HOH B . 
H 7 HOH 66 366 16  HOH HOH B . 
H 7 HOH 67 367 222 HOH HOH B . 
H 7 HOH 68 368 267 HOH HOH B . 
H 7 HOH 69 369 207 HOH HOH B . 
H 7 HOH 70 370 253 HOH HOH B . 
H 7 HOH 71 371 174 HOH HOH B . 
H 7 HOH 72 372 192 HOH HOH B . 
H 7 HOH 73 373 266 HOH HOH B . 
H 7 HOH 74 374 259 HOH HOH B . 
H 7 HOH 75 375 142 HOH HOH B . 
H 7 HOH 76 376 243 HOH HOH B . 
H 7 HOH 77 377 241 HOH HOH B . 
H 7 HOH 78 378 264 HOH HOH B . 
I 7 HOH 1  201 172 HOH HOH C . 
I 7 HOH 2  202 71  HOH HOH C . 
I 7 HOH 3  203 255 HOH HOH C . 
I 7 HOH 4  204 84  HOH HOH C . 
I 7 HOH 5  205 272 HOH HOH C . 
I 7 HOH 6  206 5   HOH HOH C . 
I 7 HOH 7  207 34  HOH HOH C . 
I 7 HOH 8  208 8   HOH HOH C . 
I 7 HOH 9  209 252 HOH HOH C . 
I 7 HOH 10 210 184 HOH HOH C . 
I 7 HOH 11 211 80  HOH HOH C . 
I 7 HOH 12 212 99  HOH HOH C . 
I 7 HOH 13 213 68  HOH HOH C . 
I 7 HOH 14 214 104 HOH HOH C . 
I 7 HOH 15 215 56  HOH HOH C . 
I 7 HOH 16 216 223 HOH HOH C . 
I 7 HOH 17 217 113 HOH HOH C . 
I 7 HOH 18 218 59  HOH HOH C . 
I 7 HOH 19 219 117 HOH HOH C . 
I 7 HOH 20 220 9   HOH HOH C . 
I 7 HOH 21 221 158 HOH HOH C . 
I 7 HOH 22 222 199 HOH HOH C . 
I 7 HOH 23 223 44  HOH HOH C . 
I 7 HOH 24 224 61  HOH HOH C . 
I 7 HOH 25 225 115 HOH HOH C . 
I 7 HOH 26 226 213 HOH HOH C . 
I 7 HOH 27 227 143 HOH HOH C . 
I 7 HOH 28 228 203 HOH HOH C . 
I 7 HOH 29 229 258 HOH HOH C . 
I 7 HOH 30 230 163 HOH HOH C . 
I 7 HOH 31 231 262 HOH HOH C . 
I 7 HOH 32 232 191 HOH HOH C . 
I 7 HOH 33 233 98  HOH HOH C . 
I 7 HOH 34 234 240 HOH HOH C . 
I 7 HOH 35 235 162 HOH HOH C . 
I 7 HOH 36 236 228 HOH HOH C . 
I 7 HOH 37 237 97  HOH HOH C . 
I 7 HOH 38 238 92  HOH HOH C . 
I 7 HOH 39 239 217 HOH HOH C . 
I 7 HOH 40 240 112 HOH HOH C . 
I 7 HOH 41 241 89  HOH HOH C . 
I 7 HOH 42 242 270 HOH HOH C . 
J 7 HOH 1  201 214 HOH HOH D . 
J 7 HOH 2  202 25  HOH HOH D . 
J 7 HOH 3  203 118 HOH HOH D . 
J 7 HOH 4  204 141 HOH HOH D . 
J 7 HOH 5  205 204 HOH HOH D . 
J 7 HOH 6  206 125 HOH HOH D . 
J 7 HOH 7  207 20  HOH HOH D . 
J 7 HOH 8  208 13  HOH HOH D . 
J 7 HOH 9  209 42  HOH HOH D . 
J 7 HOH 10 210 51  HOH HOH D . 
J 7 HOH 11 211 173 HOH HOH D . 
J 7 HOH 12 212 159 HOH HOH D . 
J 7 HOH 13 213 201 HOH HOH D . 
J 7 HOH 14 214 81  HOH HOH D . 
J 7 HOH 15 215 23  HOH HOH D . 
J 7 HOH 16 216 147 HOH HOH D . 
J 7 HOH 17 217 114 HOH HOH D . 
J 7 HOH 18 218 107 HOH HOH D . 
J 7 HOH 19 219 154 HOH HOH D . 
J 7 HOH 20 220 82  HOH HOH D . 
J 7 HOH 21 221 6   HOH HOH D . 
J 7 HOH 22 222 256 HOH HOH D . 
J 7 HOH 23 223 183 HOH HOH D . 
J 7 HOH 24 224 212 HOH HOH D . 
J 7 HOH 25 225 238 HOH HOH D . 
J 7 HOH 26 226 47  HOH HOH D . 
J 7 HOH 27 227 185 HOH HOH D . 
J 7 HOH 28 228 102 HOH HOH D . 
J 7 HOH 29 229 268 HOH HOH D . 
J 7 HOH 30 230 182 HOH HOH D . 
J 7 HOH 31 231 156 HOH HOH D . 
J 7 HOH 32 232 108 HOH HOH D . 
J 7 HOH 33 233 269 HOH HOH D . 
J 7 HOH 34 234 178 HOH HOH D . 
J 7 HOH 35 235 63  HOH HOH D . 
J 7 HOH 36 236 234 HOH HOH D . 
J 7 HOH 37 237 37  HOH HOH D . 
J 7 HOH 38 238 221 HOH HOH D . 
J 7 HOH 39 239 2   HOH HOH D . 
J 7 HOH 40 240 150 HOH HOH D . 
J 7 HOH 41 241 189 HOH HOH D . 
J 7 HOH 42 242 36  HOH HOH D . 
J 7 HOH 43 243 145 HOH HOH D . 
J 7 HOH 44 244 215 HOH HOH D . 
J 7 HOH 45 245 193 HOH HOH D . 
J 7 HOH 46 246 132 HOH HOH D . 
J 7 HOH 47 247 58  HOH HOH D . 
J 7 HOH 48 248 111 HOH HOH D . 
J 7 HOH 49 249 136 HOH HOH D . 
J 7 HOH 50 250 109 HOH HOH D . 
J 7 HOH 51 251 105 HOH HOH D . 
J 7 HOH 52 252 177 HOH HOH D . 
J 7 HOH 53 253 194 HOH HOH D . 
J 7 HOH 54 254 86  HOH HOH D . 
J 7 HOH 55 255 170 HOH HOH D . 
J 7 HOH 56 256 197 HOH HOH D . 
J 7 HOH 57 257 167 HOH HOH D . 
J 7 HOH 58 258 226 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KN1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.753 
_cell.length_a_esd                 ? 
_cell.length_b                     92.659 
_cell.length_b_esd                 ? 
_cell.length_c                     97.412 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9KN1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9KN1 
_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             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.11 
_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              8.0 
_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    '30% PEG3350, 100 mM Tris-HCl pH8.0, 5 mM UMP' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-15 
_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   0.9 
_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                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          40.60 
_reflns.entry_id                                       9KN1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.12 
_reflns.d_resolution_low                               48.71 
_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                                     30878 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.155 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.12 
_reflns_shell.d_res_low                                     2.18 
_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                             2480 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.439 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_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               ? 
# 
_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                                 9KN1 
_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                            2.12 
_refine.ls_d_res_low                             48.71 
_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                     30735 
_refine.ls_number_reflns_R_free                  1449 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 4.71 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2275 
_refine.ls_R_factor_R_free                       0.2928 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2243 
_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                          1.33 
_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             1.10 
_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                 32.98 
_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                            0.39 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.12 
_refine_hist.d_res_low                        48.71 
_refine_hist.number_atoms_solvent             263 
_refine_hist.number_atoms_total               4226 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3937 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.881  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.560 ? 1492 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 567  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 733  ? 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' 2.12 2.20  . . 151 2801 97.00  . . . . 0.3352 . . . . . . . . . . . 0.3863 
'X-RAY DIFFRACTION' 2.20 2.28  . . 141 2881 99.00  . . . . 0.3224 . . . . . . . . . . . 0.3613 
'X-RAY DIFFRACTION' 2.28 2.39  . . 145 2883 100.00 . . . . 0.3195 . . . . . . . . . . . 0.3934 
'X-RAY DIFFRACTION' 2.39 2.51  . . 156 2888 100.00 . . . . 0.3052 . . . . . . . . . . . 0.3823 
'X-RAY DIFFRACTION' 2.51 2.67  . . 168 2907 100.00 . . . . 0.2916 . . . . . . . . . . . 0.3900 
'X-RAY DIFFRACTION' 2.67 2.88  . . 144 2904 100.00 . . . . 0.2887 . . . . . . . . . . . 0.3489 
'X-RAY DIFFRACTION' 2.88 3.17  . . 138 2920 100.00 . . . . 0.2492 . . . . . . . . . . . 0.2747 
'X-RAY DIFFRACTION' 3.17 3.62  . . 127 2976 100.00 . . . . 0.2199 . . . . . . . . . . . 0.3403 
'X-RAY DIFFRACTION' 3.62 4.57  . . 139 2994 100.00 . . . . 0.1759 . . . . . . . . . . . 0.2805 
'X-RAY DIFFRACTION' 4.57 48.71 . . 140 3132 100.00 . . . . 0.1717 . . . . . . . . . . . 0.1883 
# 
_struct.entry_id                     9KN1 
_struct.title                        
'Crystal structure of SARS-CoV-2 nucleocapsid phosphoprotein N-terminal domain(N-NTD) in complex with UMP' 
_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        9KN1 
_struct_keywords.text            'SARS-CoV-2, nucleocapsid, nucleic acid binding protein, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
I N N 7 ? 
J N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP NCAP_SARS2 P0DTC9 ? 1 
;TASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKD
GIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
49 
2 UNP NCAP_SARS2 P0DTC9 ? 2 
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAE
;
47 
3 UNP NCAP_SARS2 P0DTC9 ? 3 
;NNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN
KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
47 
4 UNP NCAP_SARS2 P0DTC9 ? 4 
;NTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANK
DGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYA
;
48 
# 
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 9KN1 A 1 ? 125 ? P0DTC9 49 ? 173 ? 49 173 
2 2 9KN1 B 1 ? 128 ? P0DTC9 47 ? 174 ? 47 174 
3 3 9KN1 C 1 ? 127 ? P0DTC9 47 ? 173 ? 47 173 
4 4 9KN1 D 1 ? 126 ? P0DTC9 48 ? 173 ? 48 173 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
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)' 0    ? 
1 MORE         0    ? 
1 'SSA (A^2)'  7620 ? 
2 'ABSA (A^2)' 170  ? 
2 MORE         -5   ? 
2 'SSA (A^2)'  7840 ? 
3 'ABSA (A^2)' 0    ? 
3 MORE         0    ? 
3 'SSA (A^2)'  7820 ? 
4 'ABSA (A^2)' 0    ? 
4 MORE         0    ? 
4 'SSA (A^2)'  7560 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,G 
2 1 B,F,H 
3 1 C,I   
4 1 D,J   
# 
_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 SER A 31 ? ASP A 34 ? SER A 79  ASP A 82  5 ? 4 
HELX_P HELX_P2 AA2 SER B 33 ? ASP B 36 ? SER B 79  ASP B 82  5 ? 4 
HELX_P HELX_P3 AA3 SER C 33 ? ASP C 36 ? SER C 79  ASP C 82  5 ? 4 
HELX_P HELX_P4 AA4 SER D 32 ? ASP D 35 ? SER D 79  ASP D 82  5 ? 4 
HELX_P HELX_P5 AA5 THR D 68 ? ALA D 72 ? THR D 115 ALA D 119 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? 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 ILE A 82  ? ALA A 86  ? ILE A 130 ALA A 134 
AA1 2 ILE A 36  ? ALA A 42  ? ILE A 84  ALA A 90  
AA1 3 ARG A 59  ? TYR A 64  ? ARG A 107 TYR A 112 
AA1 4 LEU A 8   ? GLN A 10  ? LEU A 56  GLN A 58  
AA1 5 PHE A 123 ? TYR A 124 ? PHE A 171 TYR A 172 
AA2 1 ARG A 45  ? ARG A 47  ? ARG A 93  ARG A 95  
AA2 2 MET A 53  ? ASP A 55  ? MET A 101 ASP A 103 
AA3 1 LEU B 10  ? THR B 11  ? LEU B 56  THR B 57  
AA3 2 ARG B 61  ? TYR B 66  ? ARG B 107 TYR B 112 
AA3 3 ILE B 38  ? ALA B 44  ? ILE B 84  ALA B 90  
AA3 4 ILE B 84  ? ALA B 88  ? ILE B 130 ALA B 134 
AA4 1 ARG B 47  ? ARG B 49  ? ARG B 93  ARG B 95  
AA4 2 MET B 55  ? ASP B 57  ? MET B 101 ASP B 103 
AA5 1 LEU C 10  ? THR C 11  ? LEU C 56  THR C 57  
AA5 2 ARG C 61  ? TYR C 66  ? ARG C 107 TYR C 112 
AA5 3 ILE C 38  ? ALA C 44  ? ILE C 84  ALA C 90  
AA5 4 ILE C 84  ? ALA C 88  ? ILE C 130 ALA C 134 
AA6 1 ARG C 47  ? ARG C 49  ? ARG C 93  ARG C 95  
AA6 2 MET C 55  ? ASP C 57  ? MET C 101 ASP C 103 
AA7 1 ILE D 83  ? ALA D 87  ? ILE D 130 ALA D 134 
AA7 2 ILE D 37  ? ALA D 43  ? ILE D 84  ALA D 90  
AA7 3 ARG D 60  ? TYR D 65  ? ARG D 107 TYR D 112 
AA7 4 LEU D 9   ? GLN D 11  ? LEU D 56  GLN D 58  
AA7 5 PHE D 124 ? TYR D 125 ? PHE D 171 TYR D 172 
AA8 1 ARG D 46  ? ARG D 48  ? ARG D 93  ARG D 95  
AA8 2 MET D 54  ? ASP D 56  ? MET D 101 ASP D 103 
# 
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 O VAL A 85 ? O VAL A 133 N GLY A 37  ? N GLY A 85  
AA1 2 3 N ALA A 42 ? N ALA A 90  O ARG A 59  ? O ARG A 107 
AA1 3 4 O TRP A 60 ? O TRP A 108 N LEU A 8   ? N LEU A 56  
AA1 4 5 N THR A 9  ? N THR A 57  O TYR A 124 ? O TYR A 172 
AA2 1 2 N ILE A 46 ? N ILE A 94  O LYS A 54  ? O LYS A 102 
AA3 1 2 N LEU B 10 ? N LEU B 56  O TRP B 62  ? O TRP B 108 
AA3 2 3 O ARG B 61 ? O ARG B 107 N ALA B 44  ? N ALA B 90  
AA3 3 4 N GLY B 39 ? N GLY B 85  O VAL B 87  ? O VAL B 133 
AA4 1 2 N ILE B 48 ? N ILE B 94  O LYS B 56  ? O LYS B 102 
AA5 1 2 N LEU C 10 ? N LEU C 56  O TRP C 62  ? O TRP C 108 
AA5 2 3 O TYR C 63 ? O TYR C 109 N ARG C 42  ? N ARG C 88  
AA5 3 4 N GLY C 39 ? N GLY C 85  O VAL C 87  ? O VAL C 133 
AA6 1 2 N ILE C 48 ? N ILE C 94  O LYS C 56  ? O LYS C 102 
AA7 1 2 O VAL D 86 ? O VAL D 133 N GLY D 38  ? N GLY D 85  
AA7 2 3 N TYR D 39 ? N TYR D 86  O TYR D 64  ? O TYR D 111 
AA7 3 4 O TRP D 61 ? O TRP D 108 N LEU D 9   ? N LEU D 56  
AA7 4 5 N THR D 10 ? N THR D 57  O TYR D 125 ? O TYR D 172 
AA8 1 2 N ILE D 47 ? N ILE D 94  O LYS D 55  ? O LYS D 102 
# 
_pdbx_entry_details.entry_id                   9KN1 
_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     Y 
_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 LYS A 143 ? ? -99.15 57.42   
2 1 ASN C 140 ? ? -97.06 34.30   
3 1 PRO C 168 ? ? -67.47 -174.15 
4 1 ASN D 77  ? ? -93.59 31.23   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
GLN N      N N N 74  
GLN CA     C N S 75  
GLN C      C N N 76  
GLN O      O N N 77  
GLN CB     C N N 78  
GLN CG     C N N 79  
GLN CD     C N N 80  
GLN OE1    O N N 81  
GLN NE2    N N N 82  
GLN OXT    O N N 83  
GLN H      H N N 84  
GLN H2     H N N 85  
GLN HA     H N N 86  
GLN HB2    H N N 87  
GLN HB3    H N N 88  
GLN HG2    H N N 89  
GLN HG3    H N N 90  
GLN HE21   H N N 91  
GLN HE22   H N N 92  
GLN HXT    H N N 93  
GLU N      N N N 94  
GLU CA     C N S 95  
GLU C      C N N 96  
GLU O      O N N 97  
GLU CB     C N N 98  
GLU CG     C N N 99  
GLU CD     C N N 100 
GLU OE1    O N N 101 
GLU OE2    O N N 102 
GLU OXT    O N N 103 
GLU H      H N N 104 
GLU H2     H N N 105 
GLU HA     H N N 106 
GLU HB2    H N N 107 
GLU HB3    H N N 108 
GLU HG2    H N N 109 
GLU HG3    H N N 110 
GLU HE2    H N N 111 
GLU HXT    H N N 112 
GLY N      N N N 113 
GLY CA     C N N 114 
GLY C      C N N 115 
GLY O      O N N 116 
GLY OXT    O N N 117 
GLY H      H N N 118 
GLY H2     H N N 119 
GLY HA2    H N N 120 
GLY HA3    H N N 121 
GLY HXT    H N N 122 
HIS N      N N N 123 
HIS CA     C N S 124 
HIS C      C N N 125 
HIS O      O N N 126 
HIS CB     C N N 127 
HIS CG     C Y N 128 
HIS ND1    N Y N 129 
HIS CD2    C Y N 130 
HIS CE1    C Y N 131 
HIS NE2    N Y N 132 
HIS OXT    O N N 133 
HIS H      H N N 134 
HIS H2     H N N 135 
HIS HA     H N N 136 
HIS HB2    H N N 137 
HIS HB3    H N N 138 
HIS HD1    H N N 139 
HIS HD2    H N N 140 
HIS HE1    H N N 141 
HIS HE2    H N N 142 
HIS HXT    H N N 143 
HOH O      O N N 144 
HOH H1     H N N 145 
HOH H2     H N N 146 
ILE N      N N N 147 
ILE CA     C N S 148 
ILE C      C N N 149 
ILE O      O N N 150 
ILE CB     C N S 151 
ILE CG1    C N N 152 
ILE CG2    C N N 153 
ILE CD1    C N N 154 
ILE OXT    O N N 155 
ILE H      H N N 156 
ILE H2     H N N 157 
ILE HA     H N N 158 
ILE HB     H N N 159 
ILE HG12   H N N 160 
ILE HG13   H N N 161 
ILE HG21   H N N 162 
ILE HG22   H N N 163 
ILE HG23   H N N 164 
ILE HD11   H N N 165 
ILE HD12   H N N 166 
ILE HD13   H N N 167 
ILE HXT    H N N 168 
LEU N      N N N 169 
LEU CA     C N S 170 
LEU C      C N N 171 
LEU O      O N N 172 
LEU CB     C N N 173 
LEU CG     C N N 174 
LEU CD1    C N N 175 
LEU CD2    C N N 176 
LEU OXT    O N N 177 
LEU H      H N N 178 
LEU H2     H N N 179 
LEU HA     H N N 180 
LEU HB2    H N N 181 
LEU HB3    H N N 182 
LEU HG     H N N 183 
LEU HD11   H N N 184 
LEU HD12   H N N 185 
LEU HD13   H N N 186 
LEU HD21   H N N 187 
LEU HD22   H N N 188 
LEU HD23   H N N 189 
LEU HXT    H N N 190 
LYS N      N N N 191 
LYS CA     C N S 192 
LYS C      C N N 193 
LYS O      O N N 194 
LYS CB     C N N 195 
LYS CG     C N N 196 
LYS CD     C N N 197 
LYS CE     C N N 198 
LYS NZ     N N N 199 
LYS OXT    O N N 200 
LYS H      H N N 201 
LYS H2     H N N 202 
LYS HA     H N N 203 
LYS HB2    H N N 204 
LYS HB3    H N N 205 
LYS HG2    H N N 206 
LYS HG3    H N N 207 
LYS HD2    H N N 208 
LYS HD3    H N N 209 
LYS HE2    H N N 210 
LYS HE3    H N N 211 
LYS HZ1    H N N 212 
LYS HZ2    H N N 213 
LYS HZ3    H N N 214 
LYS HXT    H N N 215 
MET N      N N N 216 
MET CA     C N S 217 
MET C      C N N 218 
MET O      O N N 219 
MET CB     C N N 220 
MET CG     C N N 221 
MET SD     S N N 222 
MET CE     C N N 223 
MET OXT    O N N 224 
MET H      H N N 225 
MET H2     H N N 226 
MET HA     H N N 227 
MET HB2    H N N 228 
MET HB3    H N N 229 
MET HG2    H N N 230 
MET HG3    H N N 231 
MET HE1    H N N 232 
MET HE2    H N N 233 
MET HE3    H N N 234 
MET HXT    H N N 235 
PHE N      N N N 236 
PHE CA     C N S 237 
PHE C      C N N 238 
PHE O      O N N 239 
PHE CB     C N N 240 
PHE CG     C Y N 241 
PHE CD1    C Y N 242 
PHE CD2    C Y N 243 
PHE CE1    C Y N 244 
PHE CE2    C Y N 245 
PHE CZ     C Y N 246 
PHE OXT    O N N 247 
PHE H      H N N 248 
PHE H2     H N N 249 
PHE HA     H N N 250 
PHE HB2    H N N 251 
PHE HB3    H N N 252 
PHE HD1    H N N 253 
PHE HD2    H N N 254 
PHE HE1    H N N 255 
PHE HE2    H N N 256 
PHE HZ     H N N 257 
PHE HXT    H N N 258 
PO4 P      P N N 259 
PO4 O1     O N N 260 
PO4 O2     O N N 261 
PO4 O3     O N N 262 
PO4 O4     O N N 263 
PRO N      N N N 264 
PRO CA     C N S 265 
PRO C      C N N 266 
PRO O      O N N 267 
PRO CB     C N N 268 
PRO CG     C N N 269 
PRO CD     C N N 270 
PRO OXT    O N N 271 
PRO H      H N N 272 
PRO HA     H N N 273 
PRO HB2    H N N 274 
PRO HB3    H N N 275 
PRO HG2    H N N 276 
PRO HG3    H N N 277 
PRO HD2    H N N 278 
PRO HD3    H N N 279 
PRO HXT    H N N 280 
SER N      N N N 281 
SER CA     C N S 282 
SER C      C N N 283 
SER O      O N N 284 
SER CB     C N N 285 
SER OG     O N N 286 
SER OXT    O N N 287 
SER H      H N N 288 
SER H2     H N N 289 
SER HA     H N N 290 
SER HB2    H N N 291 
SER HB3    H N N 292 
SER HG     H N N 293 
SER HXT    H N N 294 
THR N      N N N 295 
THR CA     C N S 296 
THR C      C N N 297 
THR O      O N N 298 
THR CB     C N R 299 
THR OG1    O N N 300 
THR CG2    C N N 301 
THR OXT    O N N 302 
THR H      H N N 303 
THR H2     H N N 304 
THR HA     H N N 305 
THR HB     H N N 306 
THR HG1    H N N 307 
THR HG21   H N N 308 
THR HG22   H N N 309 
THR HG23   H N N 310 
THR HXT    H N N 311 
TRP N      N N N 312 
TRP CA     C N S 313 
TRP C      C N N 314 
TRP O      O N N 315 
TRP CB     C N N 316 
TRP CG     C Y N 317 
TRP CD1    C Y N 318 
TRP CD2    C Y N 319 
TRP NE1    N Y N 320 
TRP CE2    C Y N 321 
TRP CE3    C Y N 322 
TRP CZ2    C Y N 323 
TRP CZ3    C Y N 324 
TRP CH2    C Y N 325 
TRP OXT    O N N 326 
TRP H      H N N 327 
TRP H2     H N N 328 
TRP HA     H N N 329 
TRP HB2    H N N 330 
TRP HB3    H N N 331 
TRP HD1    H N N 332 
TRP HE1    H N N 333 
TRP HE3    H N N 334 
TRP HZ2    H N N 335 
TRP HZ3    H N N 336 
TRP HH2    H N N 337 
TRP HXT    H N N 338 
TYR N      N N N 339 
TYR CA     C N S 340 
TYR C      C N N 341 
TYR O      O N N 342 
TYR CB     C N N 343 
TYR CG     C Y N 344 
TYR CD1    C Y N 345 
TYR CD2    C Y N 346 
TYR CE1    C Y N 347 
TYR CE2    C Y N 348 
TYR CZ     C Y N 349 
TYR OH     O N N 350 
TYR OXT    O N N 351 
TYR H      H N N 352 
TYR H2     H N N 353 
TYR HA     H N N 354 
TYR HB2    H N N 355 
TYR HB3    H N N 356 
TYR HD1    H N N 357 
TYR HD2    H N N 358 
TYR HE1    H N N 359 
TYR HE2    H N N 360 
TYR HH     H N N 361 
TYR HXT    H N N 362 
U   OP3    O N N 363 
U   P      P N N 364 
U   OP1    O N N 365 
U   OP2    O N N 366 
U   "O5'"  O N N 367 
U   "C5'"  C N N 368 
U   "C4'"  C N R 369 
U   "O4'"  O N N 370 
U   "C3'"  C N S 371 
U   "O3'"  O N N 372 
U   "C2'"  C N R 373 
U   "O2'"  O N N 374 
U   "C1'"  C N R 375 
U   N1     N N N 376 
U   C2     C N N 377 
U   O2     O N N 378 
U   N3     N N N 379 
U   C4     C N N 380 
U   O4     O N N 381 
U   C5     C N N 382 
U   C6     C N N 383 
U   HOP3   H N N 384 
U   HOP2   H N N 385 
U   "H5'"  H N N 386 
U   "H5''" H N N 387 
U   "H4'"  H N N 388 
U   "H3'"  H N N 389 
U   "HO3'" H N N 390 
U   "H2'"  H N N 391 
U   "HO2'" H N N 392 
U   "H1'"  H N N 393 
U   H3     H N N 394 
U   H5     H N N 395 
U   H6     H N N 396 
VAL N      N N N 397 
VAL CA     C N S 398 
VAL C      C N N 399 
VAL O      O N N 400 
VAL CB     C N N 401 
VAL CG1    C N N 402 
VAL CG2    C N N 403 
VAL OXT    O N N 404 
VAL H      H N N 405 
VAL H2     H N N 406 
VAL HA     H N N 407 
VAL HB     H N N 408 
VAL HG11   H N N 409 
VAL HG12   H N N 410 
VAL HG13   H N N 411 
VAL HG21   H N N 412 
VAL HG22   H N N 413 
VAL HG23   H N N 414 
VAL HXT    H N N 415 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
GLN N     CA     sing N N 70  
GLN N     H      sing N N 71  
GLN N     H2     sing N N 72  
GLN CA    C      sing N N 73  
GLN CA    CB     sing N N 74  
GLN CA    HA     sing N N 75  
GLN C     O      doub N N 76  
GLN C     OXT    sing N N 77  
GLN CB    CG     sing N N 78  
GLN CB    HB2    sing N N 79  
GLN CB    HB3    sing N N 80  
GLN CG    CD     sing N N 81  
GLN CG    HG2    sing N N 82  
GLN CG    HG3    sing N N 83  
GLN CD    OE1    doub N N 84  
GLN CD    NE2    sing N N 85  
GLN NE2   HE21   sing N N 86  
GLN NE2   HE22   sing N N 87  
GLN OXT   HXT    sing N N 88  
GLU N     CA     sing N N 89  
GLU N     H      sing N N 90  
GLU N     H2     sing N N 91  
GLU CA    C      sing N N 92  
GLU CA    CB     sing N N 93  
GLU CA    HA     sing N N 94  
GLU C     O      doub N N 95  
GLU C     OXT    sing N N 96  
GLU CB    CG     sing N N 97  
GLU CB    HB2    sing N N 98  
GLU CB    HB3    sing N N 99  
GLU CG    CD     sing N N 100 
GLU CG    HG2    sing N N 101 
GLU CG    HG3    sing N N 102 
GLU CD    OE1    doub N N 103 
GLU CD    OE2    sing N N 104 
GLU OE2   HE2    sing N N 105 
GLU OXT   HXT    sing N N 106 
GLY N     CA     sing N N 107 
GLY N     H      sing N N 108 
GLY N     H2     sing N N 109 
GLY CA    C      sing N N 110 
GLY CA    HA2    sing N N 111 
GLY CA    HA3    sing N N 112 
GLY C     O      doub N N 113 
GLY C     OXT    sing N N 114 
GLY OXT   HXT    sing N N 115 
HIS N     CA     sing N N 116 
HIS N     H      sing N N 117 
HIS N     H2     sing N N 118 
HIS CA    C      sing N N 119 
HIS CA    CB     sing N N 120 
HIS CA    HA     sing N N 121 
HIS C     O      doub N N 122 
HIS C     OXT    sing N N 123 
HIS CB    CG     sing N N 124 
HIS CB    HB2    sing N N 125 
HIS CB    HB3    sing N N 126 
HIS CG    ND1    sing Y N 127 
HIS CG    CD2    doub Y N 128 
HIS ND1   CE1    doub Y N 129 
HIS ND1   HD1    sing N N 130 
HIS CD2   NE2    sing Y N 131 
HIS CD2   HD2    sing N N 132 
HIS CE1   NE2    sing Y N 133 
HIS CE1   HE1    sing N N 134 
HIS NE2   HE2    sing N N 135 
HIS OXT   HXT    sing N N 136 
HOH O     H1     sing N N 137 
HOH O     H2     sing N N 138 
ILE N     CA     sing N N 139 
ILE N     H      sing N N 140 
ILE N     H2     sing N N 141 
ILE CA    C      sing N N 142 
ILE CA    CB     sing N N 143 
ILE CA    HA     sing N N 144 
ILE C     O      doub N N 145 
ILE C     OXT    sing N N 146 
ILE CB    CG1    sing N N 147 
ILE CB    CG2    sing N N 148 
ILE CB    HB     sing N N 149 
ILE CG1   CD1    sing N N 150 
ILE CG1   HG12   sing N N 151 
ILE CG1   HG13   sing N N 152 
ILE CG2   HG21   sing N N 153 
ILE CG2   HG22   sing N N 154 
ILE CG2   HG23   sing N N 155 
ILE CD1   HD11   sing N N 156 
ILE CD1   HD12   sing N N 157 
ILE CD1   HD13   sing N N 158 
ILE OXT   HXT    sing N N 159 
LEU N     CA     sing N N 160 
LEU N     H      sing N N 161 
LEU N     H2     sing N N 162 
LEU CA    C      sing N N 163 
LEU CA    CB     sing N N 164 
LEU CA    HA     sing N N 165 
LEU C     O      doub N N 166 
LEU C     OXT    sing N N 167 
LEU CB    CG     sing N N 168 
LEU CB    HB2    sing N N 169 
LEU CB    HB3    sing N N 170 
LEU CG    CD1    sing N N 171 
LEU CG    CD2    sing N N 172 
LEU CG    HG     sing N N 173 
LEU CD1   HD11   sing N N 174 
LEU CD1   HD12   sing N N 175 
LEU CD1   HD13   sing N N 176 
LEU CD2   HD21   sing N N 177 
LEU CD2   HD22   sing N N 178 
LEU CD2   HD23   sing N N 179 
LEU OXT   HXT    sing N N 180 
LYS N     CA     sing N N 181 
LYS N     H      sing N N 182 
LYS N     H2     sing N N 183 
LYS CA    C      sing N N 184 
LYS CA    CB     sing N N 185 
LYS CA    HA     sing N N 186 
LYS C     O      doub N N 187 
LYS C     OXT    sing N N 188 
LYS CB    CG     sing N N 189 
LYS CB    HB2    sing N N 190 
LYS CB    HB3    sing N N 191 
LYS CG    CD     sing N N 192 
LYS CG    HG2    sing N N 193 
LYS CG    HG3    sing N N 194 
LYS CD    CE     sing N N 195 
LYS CD    HD2    sing N N 196 
LYS CD    HD3    sing N N 197 
LYS CE    NZ     sing N N 198 
LYS CE    HE2    sing N N 199 
LYS CE    HE3    sing N N 200 
LYS NZ    HZ1    sing N N 201 
LYS NZ    HZ2    sing N N 202 
LYS NZ    HZ3    sing N N 203 
LYS OXT   HXT    sing N N 204 
MET N     CA     sing N N 205 
MET N     H      sing N N 206 
MET N     H2     sing N N 207 
MET CA    C      sing N N 208 
MET CA    CB     sing N N 209 
MET CA    HA     sing N N 210 
MET C     O      doub N N 211 
MET C     OXT    sing N N 212 
MET CB    CG     sing N N 213 
MET CB    HB2    sing N N 214 
MET CB    HB3    sing N N 215 
MET CG    SD     sing N N 216 
MET CG    HG2    sing N N 217 
MET CG    HG3    sing N N 218 
MET SD    CE     sing N N 219 
MET CE    HE1    sing N N 220 
MET CE    HE2    sing N N 221 
MET CE    HE3    sing N N 222 
MET OXT   HXT    sing N N 223 
PHE N     CA     sing N N 224 
PHE N     H      sing N N 225 
PHE N     H2     sing N N 226 
PHE CA    C      sing N N 227 
PHE CA    CB     sing N N 228 
PHE CA    HA     sing N N 229 
PHE C     O      doub N N 230 
PHE C     OXT    sing N N 231 
PHE CB    CG     sing N N 232 
PHE CB    HB2    sing N N 233 
PHE CB    HB3    sing N N 234 
PHE CG    CD1    doub Y N 235 
PHE CG    CD2    sing Y N 236 
PHE CD1   CE1    sing Y N 237 
PHE CD1   HD1    sing N N 238 
PHE CD2   CE2    doub Y N 239 
PHE CD2   HD2    sing N N 240 
PHE CE1   CZ     doub Y N 241 
PHE CE1   HE1    sing N N 242 
PHE CE2   CZ     sing Y N 243 
PHE CE2   HE2    sing N N 244 
PHE CZ    HZ     sing N N 245 
PHE OXT   HXT    sing N N 246 
PO4 P     O1     doub N N 247 
PO4 P     O2     sing N N 248 
PO4 P     O3     sing N N 249 
PO4 P     O4     sing N N 250 
PRO N     CA     sing N N 251 
PRO N     CD     sing N N 252 
PRO N     H      sing N N 253 
PRO CA    C      sing N N 254 
PRO CA    CB     sing N N 255 
PRO CA    HA     sing N N 256 
PRO C     O      doub N N 257 
PRO C     OXT    sing N N 258 
PRO CB    CG     sing N N 259 
PRO CB    HB2    sing N N 260 
PRO CB    HB3    sing N N 261 
PRO CG    CD     sing N N 262 
PRO CG    HG2    sing N N 263 
PRO CG    HG3    sing N N 264 
PRO CD    HD2    sing N N 265 
PRO CD    HD3    sing N N 266 
PRO OXT   HXT    sing N N 267 
SER N     CA     sing N N 268 
SER N     H      sing N N 269 
SER N     H2     sing N N 270 
SER CA    C      sing N N 271 
SER CA    CB     sing N N 272 
SER CA    HA     sing N N 273 
SER C     O      doub N N 274 
SER C     OXT    sing N N 275 
SER CB    OG     sing N N 276 
SER CB    HB2    sing N N 277 
SER CB    HB3    sing N N 278 
SER OG    HG     sing N N 279 
SER OXT   HXT    sing N N 280 
THR N     CA     sing N N 281 
THR N     H      sing N N 282 
THR N     H2     sing N N 283 
THR CA    C      sing N N 284 
THR CA    CB     sing N N 285 
THR CA    HA     sing N N 286 
THR C     O      doub N N 287 
THR C     OXT    sing N N 288 
THR CB    OG1    sing N N 289 
THR CB    CG2    sing N N 290 
THR CB    HB     sing N N 291 
THR OG1   HG1    sing N N 292 
THR CG2   HG21   sing N N 293 
THR CG2   HG22   sing N N 294 
THR CG2   HG23   sing N N 295 
THR OXT   HXT    sing N N 296 
TRP N     CA     sing N N 297 
TRP N     H      sing N N 298 
TRP N     H2     sing N N 299 
TRP CA    C      sing N N 300 
TRP CA    CB     sing N N 301 
TRP CA    HA     sing N N 302 
TRP C     O      doub N N 303 
TRP C     OXT    sing N N 304 
TRP CB    CG     sing N N 305 
TRP CB    HB2    sing N N 306 
TRP CB    HB3    sing N N 307 
TRP CG    CD1    doub Y N 308 
TRP CG    CD2    sing Y N 309 
TRP CD1   NE1    sing Y N 310 
TRP CD1   HD1    sing N N 311 
TRP CD2   CE2    doub Y N 312 
TRP CD2   CE3    sing Y N 313 
TRP NE1   CE2    sing Y N 314 
TRP NE1   HE1    sing N N 315 
TRP CE2   CZ2    sing Y N 316 
TRP CE3   CZ3    doub Y N 317 
TRP CE3   HE3    sing N N 318 
TRP CZ2   CH2    doub Y N 319 
TRP CZ2   HZ2    sing N N 320 
TRP CZ3   CH2    sing Y N 321 
TRP CZ3   HZ3    sing N N 322 
TRP CH2   HH2    sing N N 323 
TRP OXT   HXT    sing N N 324 
TYR N     CA     sing N N 325 
TYR N     H      sing N N 326 
TYR N     H2     sing N N 327 
TYR CA    C      sing N N 328 
TYR CA    CB     sing N N 329 
TYR CA    HA     sing N N 330 
TYR C     O      doub N N 331 
TYR C     OXT    sing N N 332 
TYR CB    CG     sing N N 333 
TYR CB    HB2    sing N N 334 
TYR CB    HB3    sing N N 335 
TYR CG    CD1    doub Y N 336 
TYR CG    CD2    sing Y N 337 
TYR CD1   CE1    sing Y N 338 
TYR CD1   HD1    sing N N 339 
TYR CD2   CE2    doub Y N 340 
TYR CD2   HD2    sing N N 341 
TYR CE1   CZ     doub Y N 342 
TYR CE1   HE1    sing N N 343 
TYR CE2   CZ     sing Y N 344 
TYR CE2   HE2    sing N N 345 
TYR CZ    OH     sing N N 346 
TYR OH    HH     sing N N 347 
TYR OXT   HXT    sing N N 348 
U   OP3   P      sing N N 349 
U   OP3   HOP3   sing N N 350 
U   P     OP1    doub N N 351 
U   P     OP2    sing N N 352 
U   P     "O5'"  sing N N 353 
U   OP2   HOP2   sing N N 354 
U   "O5'" "C5'"  sing N N 355 
U   "C5'" "C4'"  sing N N 356 
U   "C5'" "H5'"  sing N N 357 
U   "C5'" "H5''" sing N N 358 
U   "C4'" "O4'"  sing N N 359 
U   "C4'" "C3'"  sing N N 360 
U   "C4'" "H4'"  sing N N 361 
U   "O4'" "C1'"  sing N N 362 
U   "C3'" "O3'"  sing N N 363 
U   "C3'" "C2'"  sing N N 364 
U   "C3'" "H3'"  sing N N 365 
U   "O3'" "HO3'" sing N N 366 
U   "C2'" "O2'"  sing N N 367 
U   "C2'" "C1'"  sing N N 368 
U   "C2'" "H2'"  sing N N 369 
U   "O2'" "HO2'" sing N N 370 
U   "C1'" N1     sing N N 371 
U   "C1'" "H1'"  sing N N 372 
U   N1    C2     sing N N 373 
U   N1    C6     sing N N 374 
U   C2    O2     doub N N 375 
U   C2    N3     sing N N 376 
U   N3    C4     sing N N 377 
U   N3    H3     sing N N 378 
U   C4    O4     doub N N 379 
U   C4    C5     sing N N 380 
U   C5    C6     doub N N 381 
U   C5    H5     sing N N 382 
U   C6    H6     sing N N 383 
VAL N     CA     sing N N 384 
VAL N     H      sing N N 385 
VAL N     H2     sing N N 386 
VAL CA    C      sing N N 387 
VAL CA    CB     sing N N 388 
VAL CA    HA     sing N N 389 
VAL C     O      doub N N 390 
VAL C     OXT    sing N N 391 
VAL CB    CG1    sing N N 392 
VAL CB    CG2    sing N N 393 
VAL CB    HB     sing N N 394 
VAL CG1   HG11   sing N N 395 
VAL CG1   HG12   sing N N 396 
VAL CG1   HG13   sing N N 397 
VAL CG2   HG21   sing N N 398 
VAL CG2   HG22   sing N N 399 
VAL CG2   HG23   sing N N 400 
VAL OXT   HXT    sing N N 401 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6M3M 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9KN1 
_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]   0.017020 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010792 
_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]   0.010266 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . THR A 1 1   ? 11.256  -9.180  -27.283 1.00 45.23  ? 49  THR A N     1 
ATOM   2    C CA    . THR A 1 1   ? 10.953  -8.018  -26.441 1.00 43.05  ? 49  THR A CA    1 
ATOM   3    C C     . THR A 1 1   ? 11.333  -8.272  -24.980 1.00 48.02  ? 49  THR A C     1 
ATOM   4    O O     . THR A 1 1   ? 11.223  -9.402  -24.486 1.00 56.75  ? 49  THR A O     1 
ATOM   5    C CB    . THR A 1 1   ? 9.461   -7.635  -26.482 1.00 47.54  ? 49  THR A CB    1 
ATOM   6    O OG1   . THR A 1 1   ? 8.717   -8.558  -25.671 1.00 55.18  ? 49  THR A OG1   1 
ATOM   7    C CG2   . THR A 1 1   ? 8.916   -7.644  -27.923 1.00 51.87  ? 49  THR A CG2   1 
ATOM   8    N N     . ALA A 1 2   ? 11.743  -7.212  -24.283 1.00 37.82  ? 50  ALA A N     1 
ATOM   9    C CA    . ALA A 1 2   ? 12.244  -7.330  -22.923 1.00 32.14  ? 50  ALA A CA    1 
ATOM   10   C C     . ALA A 1 2   ? 11.949  -6.046  -22.154 1.00 30.60  ? 50  ALA A C     1 
ATOM   11   O O     . ALA A 1 2   ? 11.497  -5.041  -22.713 1.00 30.37  ? 50  ALA A O     1 
ATOM   12   C CB    . ALA A 1 2   ? 13.752  -7.616  -22.929 1.00 37.14  ? 50  ALA A CB    1 
ATOM   13   N N     . SER A 1 3   ? 12.233  -6.085  -20.859 1.00 28.20  ? 51  SER A N     1 
ATOM   14   C CA    . SER A 1 3   ? 12.139  -4.890  -20.033 1.00 28.11  ? 51  SER A CA    1 
ATOM   15   C C     . SER A 1 3   ? 13.111  -3.816  -20.506 1.00 30.76  ? 51  SER A C     1 
ATOM   16   O O     . SER A 1 3   ? 14.203  -4.103  -20.999 1.00 28.27  ? 51  SER A O     1 
ATOM   17   C CB    . SER A 1 3   ? 12.438  -5.220  -18.573 1.00 29.38  ? 51  SER A CB    1 
ATOM   18   O OG    . SER A 1 3   ? 12.759  -4.038  -17.851 1.00 27.52  ? 51  SER A OG    1 
ATOM   19   N N     . TRP A 1 4   ? 12.712  -2.561  -20.323 1.00 28.24  ? 52  TRP A N     1 
ATOM   20   C CA    . TRP A 1 4   ? 13.601  -1.452  -20.614 1.00 30.62  ? 52  TRP A CA    1 
ATOM   21   C C     . TRP A 1 4   ? 14.745  -1.318  -19.610 1.00 32.04  ? 52  TRP A C     1 
ATOM   22   O O     . TRP A 1 4   ? 15.661  -0.531  -19.849 1.00 29.88  ? 52  TRP A O     1 
ATOM   23   C CB    . TRP A 1 4   ? 12.805  -0.150  -20.672 1.00 26.56  ? 52  TRP A CB    1 
ATOM   24   C CG    . TRP A 1 4   ? 12.266  0.122   -22.022 1.00 28.21  ? 52  TRP A CG    1 
ATOM   25   C CD1   . TRP A 1 4   ? 10.963  0.121   -22.397 1.00 28.73  ? 52  TRP A CD1   1 
ATOM   26   C CD2   . TRP A 1 4   ? 13.022  0.417   -23.203 1.00 37.57  ? 52  TRP A CD2   1 
ATOM   27   N NE1   . TRP A 1 4   ? 10.849  0.408   -23.736 1.00 31.59  ? 52  TRP A NE1   1 
ATOM   28   C CE2   . TRP A 1 4   ? 12.102  0.597   -24.255 1.00 35.43  ? 52  TRP A CE2   1 
ATOM   29   C CE3   . TRP A 1 4   ? 14.388  0.554   -23.473 1.00 32.65  ? 52  TRP A CE3   1 
ATOM   30   C CZ2   . TRP A 1 4   ? 12.504  0.909   -25.555 1.00 36.56  ? 52  TRP A CZ2   1 
ATOM   31   C CZ3   . TRP A 1 4   ? 14.785  0.847   -24.765 1.00 33.07  ? 52  TRP A CZ3   1 
ATOM   32   C CH2   . TRP A 1 4   ? 13.849  1.036   -25.786 1.00 36.13  ? 52  TRP A CH2   1 
ATOM   33   N N     . PHE A 1 5   ? 14.723  -2.052  -18.506 1.00 30.69  ? 53  PHE A N     1 
ATOM   34   C CA    . PHE A 1 5   ? 15.660  -1.832  -17.419 1.00 27.32  ? 53  PHE A CA    1 
ATOM   35   C C     . PHE A 1 5   ? 16.267  -3.157  -16.977 1.00 32.03  ? 53  PHE A C     1 
ATOM   36   O O     . PHE A 1 5   ? 15.714  -4.243  -17.214 1.00 26.29  ? 53  PHE A O     1 
ATOM   37   C CB    . PHE A 1 5   ? 14.969  -1.133  -16.231 1.00 25.99  ? 53  PHE A CB    1 
ATOM   38   C CG    . PHE A 1 5   ? 14.196  0.121   -16.620 1.00 31.56  ? 53  PHE A CG    1 
ATOM   39   C CD1   . PHE A 1 5   ? 12.854  0.048   -16.987 1.00 28.63  ? 53  PHE A CD1   1 
ATOM   40   C CD2   . PHE A 1 5   ? 14.809  1.367   -16.614 1.00 29.21  ? 53  PHE A CD2   1 
ATOM   41   C CE1   . PHE A 1 5   ? 12.136  1.202   -17.350 1.00 27.48  ? 53  PHE A CE1   1 
ATOM   42   C CE2   . PHE A 1 5   ? 14.118  2.515   -16.973 1.00 28.79  ? 53  PHE A CE2   1 
ATOM   43   C CZ    . PHE A 1 5   ? 12.758  2.440   -17.337 1.00 28.56  ? 53  PHE A CZ    1 
ATOM   44   N N     . THR A 1 6   ? 17.442  -3.053  -16.353 1.00 31.51  ? 54  THR A N     1 
ATOM   45   C CA    . THR A 1 6   ? 18.074  -4.209  -15.739 1.00 32.79  ? 54  THR A CA    1 
ATOM   46   C C     . THR A 1 6   ? 17.317  -4.589  -14.462 1.00 33.23  ? 54  THR A C     1 
ATOM   47   O O     . THR A 1 6   ? 16.545  -3.804  -13.918 1.00 34.04  ? 54  THR A O     1 
ATOM   48   C CB    . THR A 1 6   ? 19.549  -3.916  -15.432 1.00 34.08  ? 54  THR A CB    1 
ATOM   49   O OG1   . THR A 1 6   ? 19.650  -2.740  -14.619 1.00 31.53  ? 54  THR A OG1   1 
ATOM   50   C CG2   . THR A 1 6   ? 20.327  -3.669  -16.719 1.00 30.68  ? 54  THR A CG2   1 
ATOM   51   N N     . ALA A 1 7   ? 17.591  -5.788  -13.955 1.00 31.67  ? 55  ALA A N     1 
ATOM   52   C CA    . ALA A 1 7   ? 16.785  -6.421  -12.928 1.00 33.64  ? 55  ALA A CA    1 
ATOM   53   C C     . ALA A 1 7   ? 17.137  -5.943  -11.521 1.00 37.70  ? 55  ALA A C     1 
ATOM   54   O O     . ALA A 1 7   ? 18.133  -5.251  -11.285 1.00 40.80  ? 55  ALA A O     1 
ATOM   55   C CB    . ALA A 1 7   ? 16.956  -7.933  -13.001 1.00 37.88  ? 55  ALA A CB    1 
ATOM   56   N N     . LEU A 1 8   ? 16.284  -6.317  -10.572 1.00 32.78  ? 56  LEU A N     1 
ATOM   57   C CA    . LEU A 1 8   ? 16.634  -6.357  -9.159  1.00 37.14  ? 56  LEU A CA    1 
ATOM   58   C C     . LEU A 1 8   ? 16.742  -7.814  -8.750  1.00 41.50  ? 56  LEU A C     1 
ATOM   59   O O     . LEU A 1 8   ? 15.927  -8.639  -9.176  1.00 42.23  ? 56  LEU A O     1 
ATOM   60   C CB    . LEU A 1 8   ? 15.589  -5.675  -8.288  1.00 35.21  ? 56  LEU A CB    1 
ATOM   61   C CG    . LEU A 1 8   ? 15.481  -4.168  -8.419  1.00 33.93  ? 56  LEU A CG    1 
ATOM   62   C CD1   . LEU A 1 8   ? 14.166  -3.759  -7.781  1.00 33.88  ? 56  LEU A CD1   1 
ATOM   63   C CD2   . LEU A 1 8   ? 16.666  -3.528  -7.719  1.00 35.99  ? 56  LEU A CD2   1 
ATOM   64   N N     . THR A 1 9   ? 17.734  -8.143  -7.933  1.00 34.99  ? 57  THR A N     1 
ATOM   65   C CA    . THR A 1 9   ? 17.908  -9.526  -7.515  1.00 39.39  ? 57  THR A CA    1 
ATOM   66   C C     . THR A 1 9   ? 17.437  -9.713  -6.078  1.00 41.41  ? 57  THR A C     1 
ATOM   67   O O     . THR A 1 9   ? 17.747  -8.904  -5.197  1.00 42.69  ? 57  THR A O     1 
ATOM   68   C CB    . THR A 1 9   ? 19.369  -9.967  -7.675  1.00 43.51  ? 57  THR A CB    1 
ATOM   69   O OG1   . THR A 1 9   ? 19.747  -9.889  -9.065  1.00 41.78  ? 57  THR A OG1   1 
ATOM   70   C CG2   . THR A 1 9   ? 19.539  -11.395 -7.207  1.00 39.30  ? 57  THR A CG2   1 
ATOM   71   N N     . GLN A 1 10  ? 16.686  -10.786 -5.849  1.00 41.03  ? 58  GLN A N     1 
ATOM   72   C CA    . GLN A 1 10  ? 16.131  -11.095 -4.534  1.00 46.25  ? 58  GLN A CA    1 
ATOM   73   C C     . GLN A 1 10  ? 17.027  -12.099 -3.807  1.00 47.49  ? 58  GLN A C     1 
ATOM   74   O O     . GLN A 1 10  ? 17.175  -13.248 -4.247  1.00 42.25  ? 58  GLN A O     1 
ATOM   75   C CB    . GLN A 1 10  ? 14.711  -11.647 -4.673  1.00 42.27  ? 58  GLN A CB    1 
ATOM   76   C CG    . GLN A 1 10  ? 14.041  -12.061 -3.368  1.00 43.84  ? 58  GLN A CG    1 
ATOM   77   C CD    . GLN A 1 10  ? 12.755  -12.842 -3.610  1.00 48.22  ? 58  GLN A CD    1 
ATOM   78   O OE1   . GLN A 1 10  ? 12.063  -12.615 -4.599  1.00 47.54  ? 58  GLN A OE1   1 
ATOM   79   N NE2   . GLN A 1 10  ? 12.437  -13.775 -2.713  1.00 48.44  ? 58  GLN A NE2   1 
ATOM   80   N N     . HIS A 1 11  ? 17.609  -11.675 -2.686  1.00 50.11  ? 59  HIS A N     1 
ATOM   81   C CA    . HIS A 1 11  ? 18.403  -12.583 -1.864  1.00 51.18  ? 59  HIS A CA    1 
ATOM   82   C C     . HIS A 1 11  ? 17.631  -13.148 -0.683  1.00 58.80  ? 59  HIS A C     1 
ATOM   83   O O     . HIS A 1 11  ? 17.917  -14.267 -0.245  1.00 63.47  ? 59  HIS A O     1 
ATOM   84   C CB    . HIS A 1 11  ? 19.670  -11.878 -1.381  1.00 50.61  ? 59  HIS A CB    1 
ATOM   85   C CG    . HIS A 1 11  ? 20.611  -11.537 -2.495  1.00 52.10  ? 59  HIS A CG    1 
ATOM   86   N ND1   . HIS A 1 11  ? 20.895  -10.240 -2.862  1.00 52.31  ? 59  HIS A ND1   1 
ATOM   87   C CD2   . HIS A 1 11  ? 21.296  -12.329 -3.359  1.00 53.56  ? 59  HIS A CD2   1 
ATOM   88   C CE1   . HIS A 1 11  ? 21.729  -10.244 -3.888  1.00 52.10  ? 59  HIS A CE1   1 
ATOM   89   N NE2   . HIS A 1 11  ? 21.983  -11.499 -4.214  1.00 51.09  ? 59  HIS A NE2   1 
ATOM   90   N N     . GLY A 1 12  ? 16.638  -12.427 -0.184  1.00 54.17  ? 60  GLY A N     1 
ATOM   91   C CA    . GLY A 1 12  ? 15.795  -12.926 0.875   1.00 55.14  ? 60  GLY A CA    1 
ATOM   92   C C     . GLY A 1 12  ? 14.701  -13.827 0.344   1.00 57.93  ? 60  GLY A C     1 
ATOM   93   O O     . GLY A 1 12  ? 14.731  -14.302 -0.796  1.00 53.92  ? 60  GLY A O     1 
ATOM   94   N N     . LYS A 1 13  ? 13.706  -14.050 1.197   1.00 57.25  ? 61  LYS A N     1 
ATOM   95   C CA    . LYS A 1 13  ? 12.658  -15.023 0.950   1.00 59.26  ? 61  LYS A CA    1 
ATOM   96   C C     . LYS A 1 13  ? 11.296  -14.374 0.775   1.00 57.44  ? 61  LYS A C     1 
ATOM   97   O O     . LYS A 1 13  ? 10.292  -15.082 0.625   1.00 56.04  ? 61  LYS A O     1 
ATOM   98   C CB    . LYS A 1 13  ? 12.610  -16.050 2.093   1.00 64.03  ? 61  LYS A CB    1 
ATOM   99   C CG    . LYS A 1 13  ? 13.907  -16.860 2.280   1.00 64.14  ? 61  LYS A CG    1 
ATOM   100  C CD    . LYS A 1 13  ? 14.946  -16.100 3.109   1.00 60.09  ? 61  LYS A CD    1 
ATOM   101  C CE    . LYS A 1 13  ? 16.302  -16.772 3.072   1.00 68.79  ? 61  LYS A CE    1 
ATOM   102  N NZ    . LYS A 1 13  ? 17.363  -15.909 3.685   1.00 75.02  ? 61  LYS A NZ    1 
ATOM   103  N N     . GLU A 1 14  ? 11.236  -13.052 0.775   1.00 56.46  ? 62  GLU A N     1 
ATOM   104  C CA    . GLU A 1 14  ? 9.986   -12.341 0.586   1.00 53.37  ? 62  GLU A CA    1 
ATOM   105  C C     . GLU A 1 14  ? 9.923   -11.767 -0.826  1.00 50.43  ? 62  GLU A C     1 
ATOM   106  O O     . GLU A 1 14  ? 10.948  -11.525 -1.468  1.00 47.52  ? 62  GLU A O     1 
ATOM   107  C CB    . GLU A 1 14  ? 9.845   -11.224 1.620   1.00 50.62  ? 62  GLU A CB    1 
ATOM   108  C CG    . GLU A 1 14  ? 10.487  -9.902  1.205   1.00 58.47  ? 62  GLU A CG    1 
ATOM   109  C CD    . GLU A 1 14  ? 12.019  -9.893  1.303   1.00 59.69  ? 62  GLU A CD    1 
ATOM   110  O OE1   . GLU A 1 14  ? 12.670  -10.857 0.830   1.00 54.80  ? 62  GLU A OE1   1 
ATOM   111  O OE2   . GLU A 1 14  ? 12.563  -8.906  1.858   1.00 56.83  ? 62  GLU A OE2   1 
ATOM   112  N N     . ASP A 1 15  ? 8.703   -11.562 -1.303  1.00 48.51  ? 63  ASP A N     1 
ATOM   113  C CA    . ASP A 1 15  ? 8.504   -10.929 -2.589  1.00 42.64  ? 63  ASP A CA    1 
ATOM   114  C C     . ASP A 1 15  ? 8.850   -9.444  -2.523  1.00 43.79  ? 63  ASP A C     1 
ATOM   115  O O     . ASP A 1 15  ? 8.832   -8.813  -1.465  1.00 45.67  ? 63  ASP A O     1 
ATOM   116  C CB    . ASP A 1 15  ? 7.061   -11.116 -3.053  1.00 43.38  ? 63  ASP A CB    1 
ATOM   117  C CG    . ASP A 1 15  ? 6.757   -12.556 -3.393  1.00 54.69  ? 63  ASP A CG    1 
ATOM   118  O OD1   . ASP A 1 15  ? 7.725   -13.267 -3.772  1.00 55.47  ? 63  ASP A OD1   1 
ATOM   119  O OD2   . ASP A 1 15  ? 5.571   -12.982 -3.266  1.00 50.29  ? 63  ASP A OD2   1 
ATOM   120  N N     . LEU A 1 16  ? 9.163   -8.891  -3.689  1.00 40.45  ? 64  LEU A N     1 
ATOM   121  C CA    . LEU A 1 16  ? 9.417   -7.465  -3.814  1.00 39.15  ? 64  LEU A CA    1 
ATOM   122  C C     . LEU A 1 16  ? 8.180   -6.649  -3.468  1.00 43.93  ? 64  LEU A C     1 
ATOM   123  O O     . LEU A 1 16  ? 7.044   -7.040  -3.773  1.00 42.35  ? 64  LEU A O     1 
ATOM   124  C CB    . LEU A 1 16  ? 9.864   -7.168  -5.236  1.00 37.68  ? 64  LEU A CB    1 
ATOM   125  C CG    . LEU A 1 16  ? 10.174  -5.749  -5.640  1.00 36.19  ? 64  LEU A CG    1 
ATOM   126  C CD1   . LEU A 1 16  ? 11.308  -5.179  -4.807  1.00 42.02  ? 64  LEU A CD1   1 
ATOM   127  C CD2   . LEU A 1 16  ? 10.572  -5.820  -7.097  1.00 37.60  ? 64  LEU A CD2   1 
ATOM   128  N N     . LYS A 1 17  ? 8.402   -5.507  -2.824  1.00 38.39  ? 65  LYS A N     1 
ATOM   129  C CA    . LYS A 1 17  ? 7.313   -4.578  -2.578  1.00 43.60  ? 65  LYS A CA    1 
ATOM   130  C C     . LYS A 1 17  ? 7.905   -3.232  -2.206  1.00 45.83  ? 65  LYS A C     1 
ATOM   131  O O     . LYS A 1 17  ? 8.951   -3.163  -1.558  1.00 48.88  ? 65  LYS A O     1 
ATOM   132  C CB    . LYS A 1 17  ? 6.370   -5.080  -1.478  1.00 49.21  ? 65  LYS A CB    1 
ATOM   133  C CG    . LYS A 1 17  ? 6.982   -5.118  -0.093  1.00 51.23  ? 65  LYS A CG    1 
ATOM   134  C CD    . LYS A 1 17  ? 6.031   -5.778  0.903   1.00 55.36  ? 65  LYS A CD    1 
ATOM   135  C CE    . LYS A 1 17  ? 4.562   -5.385  0.665   1.00 62.69  ? 65  LYS A CE    1 
ATOM   136  N NZ    . LYS A 1 17  ? 4.245   -3.949  0.961   1.00 60.30  ? 65  LYS A NZ    1 
ATOM   137  N N     . PHE A 1 18  ? 7.234   -2.173  -2.630  1.00 40.34  ? 66  PHE A N     1 
ATOM   138  C CA    . PHE A 1 18  ? 7.737   -0.833  -2.439  1.00 39.82  ? 66  PHE A CA    1 
ATOM   139  C C     . PHE A 1 18  ? 6.741   -0.002  -1.651  1.00 48.16  ? 66  PHE A C     1 
ATOM   140  O O     . PHE A 1 18  ? 5.530   -0.233  -1.737  1.00 46.78  ? 66  PHE A O     1 
ATOM   141  C CB    . PHE A 1 18  ? 7.986   -0.145  -3.780  1.00 39.63  ? 66  PHE A CB    1 
ATOM   142  C CG    . PHE A 1 18  ? 9.310   -0.477  -4.405  1.00 38.60  ? 66  PHE A CG    1 
ATOM   143  C CD1   . PHE A 1 18  ? 10.445  0.258   -4.079  1.00 39.35  ? 66  PHE A CD1   1 
ATOM   144  C CD2   . PHE A 1 18  ? 9.408   -1.493  -5.338  1.00 30.95  ? 66  PHE A CD2   1 
ATOM   145  C CE1   . PHE A 1 18  ? 11.651  -0.024  -4.664  1.00 33.45  ? 66  PHE A CE1   1 
ATOM   146  C CE2   . PHE A 1 18  ? 10.610  -1.791  -5.929  1.00 33.62  ? 66  PHE A CE2   1 
ATOM   147  C CZ    . PHE A 1 18  ? 11.741  -1.059  -5.586  1.00 34.98  ? 66  PHE A CZ    1 
ATOM   148  N N     . PRO A 1 19  ? 7.217   0.977   -0.882  1.00 50.60  ? 67  PRO A N     1 
ATOM   149  C CA    . PRO A 1 19  ? 6.290   1.926   -0.263  1.00 49.74  ? 67  PRO A CA    1 
ATOM   150  C C     . PRO A 1 19  ? 5.463   2.620   -1.333  1.00 50.81  ? 67  PRO A C     1 
ATOM   151  O O     . PRO A 1 19  ? 5.933   2.868   -2.444  1.00 46.88  ? 67  PRO A O     1 
ATOM   152  C CB    . PRO A 1 19  ? 7.215   2.906   0.464   1.00 49.68  ? 67  PRO A CB    1 
ATOM   153  C CG    . PRO A 1 19  ? 8.456   2.125   0.728   1.00 57.05  ? 67  PRO A CG    1 
ATOM   154  C CD    . PRO A 1 19  ? 8.608   1.190   -0.445  1.00 51.17  ? 67  PRO A CD    1 
ATOM   155  N N     . ARG A 1 20  ? 4.207   2.882   -1.005  1.00 53.22  ? 68  ARG A N     1 
ATOM   156  C CA    . ARG A 1 20  ? 3.325   3.604   -1.907  1.00 53.78  ? 68  ARG A CA    1 
ATOM   157  C C     . ARG A 1 20  ? 3.977   4.898   -2.372  1.00 52.81  ? 68  ARG A C     1 
ATOM   158  O O     . ARG A 1 20  ? 4.338   5.753   -1.560  1.00 55.16  ? 68  ARG A O     1 
ATOM   159  C CB    . ARG A 1 20  ? 2.001   3.879   -1.189  1.00 61.98  ? 68  ARG A CB    1 
ATOM   160  C CG    . ARG A 1 20  ? 1.244   5.123   -1.614  1.00 69.65  ? 68  ARG A CG    1 
ATOM   161  C CD    . ARG A 1 20  ? 0.471   5.643   -0.409  1.00 72.91  ? 68  ARG A CD    1 
ATOM   162  N NE    . ARG A 1 20  ? -0.578  6.596   -0.752  1.00 86.21  ? 68  ARG A NE    1 
ATOM   163  C CZ    . ARG A 1 20  ? -1.832  6.264   -1.032  1.00 87.99  ? 68  ARG A CZ    1 
ATOM   164  N NH1   . ARG A 1 20  ? -2.216  4.997   -1.105  1.00 80.85  ? 68  ARG A NH1   1 
ATOM   165  N NH2   . ARG A 1 20  ? -2.726  7.227   -1.238  1.00 89.53  ? 68  ARG A NH2   1 
ATOM   166  N N     . GLY A 1 21  ? 4.156   5.026   -3.683  1.00 49.82  ? 69  GLY A N     1 
ATOM   167  C CA    . GLY A 1 21  ? 4.713   6.228   -4.263  1.00 45.39  ? 69  GLY A CA    1 
ATOM   168  C C     . GLY A 1 21  ? 6.144   6.109   -4.740  1.00 42.17  ? 69  GLY A C     1 
ATOM   169  O O     . GLY A 1 21  ? 6.694   7.101   -5.227  1.00 40.48  ? 69  GLY A O     1 
ATOM   170  N N     . GLN A 1 22  ? 6.773   4.947   -4.613  1.00 44.35  ? 70  GLN A N     1 
ATOM   171  C CA    . GLN A 1 22  ? 8.142   4.780   -5.085  1.00 46.86  ? 70  GLN A CA    1 
ATOM   172  C C     . GLN A 1 22  ? 8.294   3.411   -5.735  1.00 45.83  ? 70  GLN A C     1 
ATOM   173  O O     . GLN A 1 22  ? 7.480   2.509   -5.529  1.00 46.65  ? 70  GLN A O     1 
ATOM   174  C CB    . GLN A 1 22  ? 9.153   4.962   -3.952  1.00 43.71  ? 70  GLN A CB    1 
ATOM   175  C CG    . GLN A 1 22  ? 8.784   4.295   -2.666  1.00 48.26  ? 70  GLN A CG    1 
ATOM   176  C CD    . GLN A 1 22  ? 9.762   4.642   -1.556  1.00 53.80  ? 70  GLN A CD    1 
ATOM   177  O OE1   . GLN A 1 22  ? 10.511  3.788   -1.082  1.00 50.04  ? 70  GLN A OE1   1 
ATOM   178  N NE2   . GLN A 1 22  ? 9.769   5.908   -1.152  1.00 55.08  ? 70  GLN A NE2   1 
ATOM   179  N N     . GLY A 1 23  ? 9.328   3.273   -6.556  1.00 39.82  ? 71  GLY A N     1 
ATOM   180  C CA    . GLY A 1 23  ? 9.599   1.984   -7.168  1.00 39.94  ? 71  GLY A CA    1 
ATOM   181  C C     . GLY A 1 23  ? 9.829   2.014   -8.669  1.00 38.44  ? 71  GLY A C     1 
ATOM   182  O O     . GLY A 1 23  ? 10.371  1.065   -9.250  1.00 37.41  ? 71  GLY A O     1 
ATOM   183  N N     . VAL A 1 24  ? 9.415   3.093   -9.312  1.00 39.12  ? 72  VAL A N     1 
ATOM   184  C CA    . VAL A 1 24  ? 9.525   3.185   -10.766 1.00 37.05  ? 72  VAL A CA    1 
ATOM   185  C C     . VAL A 1 24  ? 10.941  3.617   -11.136 1.00 36.47  ? 72  VAL A C     1 
ATOM   186  O O     . VAL A 1 24  ? 11.410  4.666   -10.659 1.00 37.75  ? 72  VAL A O     1 
ATOM   187  C CB    . VAL A 1 24  ? 8.490   4.157   -11.321 1.00 32.92  ? 72  VAL A CB    1 
ATOM   188  C CG1   . VAL A 1 24  ? 8.742   4.404   -12.804 1.00 28.60  ? 72  VAL A CG1   1 
ATOM   189  C CG2   . VAL A 1 24  ? 7.077   3.627   -11.081 1.00 32.97  ? 72  VAL A CG2   1 
ATOM   190  N N     . PRO A 1 25  ? 11.628  2.883   -12.003 1.00 39.28  ? 73  PRO A N     1 
ATOM   191  C CA    . PRO A 1 25  ? 12.971  3.289   -12.426 1.00 31.20  ? 73  PRO A CA    1 
ATOM   192  C C     . PRO A 1 25  ? 12.960  4.642   -13.120 1.00 38.29  ? 73  PRO A C     1 
ATOM   193  O O     . PRO A 1 25  ? 11.960  5.050   -13.719 1.00 33.95  ? 73  PRO A O     1 
ATOM   194  C CB    . PRO A 1 25  ? 13.377  2.191   -13.404 1.00 32.01  ? 73  PRO A CB    1 
ATOM   195  C CG    . PRO A 1 25  ? 12.445  1.068   -13.170 1.00 33.55  ? 73  PRO A CG    1 
ATOM   196  C CD    . PRO A 1 25  ? 11.174  1.661   -12.691 1.00 33.73  ? 73  PRO A CD    1 
ATOM   197  N N     . ILE A 1 26  ? 14.094  5.348   -13.020 1.00 37.28  ? 74  ILE A N     1 
ATOM   198  C CA    . ILE A 1 26  ? 14.262  6.613   -13.724 1.00 34.15  ? 74  ILE A CA    1 
ATOM   199  C C     . ILE A 1 26  ? 14.483  6.359   -15.209 1.00 38.93  ? 74  ILE A C     1 
ATOM   200  O O     . ILE A 1 26  ? 15.239  5.458   -15.607 1.00 35.00  ? 74  ILE A O     1 
ATOM   201  C CB    . ILE A 1 26  ? 15.431  7.411   -13.126 1.00 43.75  ? 74  ILE A CB    1 
ATOM   202  C CG1   . ILE A 1 26  ? 15.089  7.878   -11.714 1.00 43.66  ? 74  ILE A CG1   1 
ATOM   203  C CG2   . ILE A 1 26  ? 15.785  8.596   -14.002 1.00 36.72  ? 74  ILE A CG2   1 
ATOM   204  C CD1   . ILE A 1 26  ? 16.307  7.946   -10.831 1.00 50.12  ? 74  ILE A CD1   1 
ATOM   205  N N     . ASN A 1 27  ? 13.839  7.182   -16.039 1.00 40.26  ? 75  ASN A N     1 
ATOM   206  C CA    . ASN A 1 27  ? 13.972  7.113   -17.491 1.00 34.97  ? 75  ASN A CA    1 
ATOM   207  C C     . ASN A 1 27  ? 13.769  8.525   -18.026 1.00 43.37  ? 75  ASN A C     1 
ATOM   208  O O     . ASN A 1 27  ? 12.656  9.059   -17.975 1.00 42.63  ? 75  ASN A O     1 
ATOM   209  C CB    . ASN A 1 27  ? 12.957  6.142   -18.078 1.00 35.62  ? 75  ASN A CB    1 
ATOM   210  C CG    . ASN A 1 27  ? 13.096  5.980   -19.562 1.00 38.73  ? 75  ASN A CG    1 
ATOM   211  O OD1   . ASN A 1 27  ? 13.883  6.674   -20.201 1.00 44.15  ? 75  ASN A OD1   1 
ATOM   212  N ND2   . ASN A 1 27  ? 12.313  5.070   -20.136 1.00 33.90  ? 75  ASN A ND2   1 
ATOM   213  N N     . THR A 1 28  ? 14.835  9.124   -18.554 1.00 43.61  ? 76  THR A N     1 
ATOM   214  C CA    . THR A 1 28  ? 14.754  10.518  -18.964 1.00 47.24  ? 76  THR A CA    1 
ATOM   215  C C     . THR A 1 28  ? 13.864  10.725  -20.183 1.00 44.57  ? 76  THR A C     1 
ATOM   216  O O     . THR A 1 28  ? 13.526  11.873  -20.484 1.00 42.19  ? 76  THR A O     1 
ATOM   217  C CB    . THR A 1 28  ? 16.158  11.077  -19.245 1.00 45.23  ? 76  THR A CB    1 
ATOM   218  O OG1   . THR A 1 28  ? 16.750  10.361  -20.332 1.00 49.03  ? 76  THR A OG1   1 
ATOM   219  C CG2   . THR A 1 28  ? 17.046  10.957  -18.012 1.00 43.95  ? 76  THR A CG2   1 
ATOM   220  N N     . ASN A 1 29  ? 13.489  9.663   -20.892 1.00 44.32  ? 77  ASN A N     1 
ATOM   221  C CA    . ASN A 1 29  ? 12.614  9.778   -22.051 1.00 47.22  ? 77  ASN A CA    1 
ATOM   222  C C     . ASN A 1 29  ? 11.133  9.683   -21.702 1.00 50.01  ? 77  ASN A C     1 
ATOM   223  O O     . ASN A 1 29  ? 10.281  9.816   -22.588 1.00 54.16  ? 77  ASN A O     1 
ATOM   224  C CB    . ASN A 1 29  ? 12.958  8.707   -23.075 1.00 50.87  ? 77  ASN A CB    1 
ATOM   225  C CG    . ASN A 1 29  ? 13.992  9.177   -24.059 1.00 61.33  ? 77  ASN A CG    1 
ATOM   226  O OD1   . ASN A 1 29  ? 13.761  10.143  -24.794 1.00 62.34  ? 77  ASN A OD1   1 
ATOM   227  N ND2   . ASN A 1 29  ? 15.145  8.500   -24.087 1.00 57.89  ? 77  ASN A ND2   1 
ATOM   228  N N     . SER A 1 30  ? 10.807  9.467   -20.445 1.00 47.14  ? 78  SER A N     1 
ATOM   229  C CA    . SER A 1 30  ? 9.437   9.310   -20.011 1.00 42.77  ? 78  SER A CA    1 
ATOM   230  C C     . SER A 1 30  ? 8.989   10.566  -19.274 1.00 47.74  ? 78  SER A C     1 
ATOM   231  O O     . SER A 1 30  ? 9.807   11.303  -18.714 1.00 51.01  ? 78  SER A O     1 
ATOM   232  C CB    . SER A 1 30  ? 9.322   8.090   -19.112 1.00 36.73  ? 78  SER A CB    1 
ATOM   233  O OG    . SER A 1 30  ? 9.998   8.342   -17.901 1.00 36.89  ? 78  SER A OG    1 
ATOM   234  N N     . SER A 1 31  ? 7.687   10.814  -19.286 1.00 43.30  ? 79  SER A N     1 
ATOM   235  C CA    . SER A 1 31  ? 7.113   11.990  -18.660 1.00 39.41  ? 79  SER A CA    1 
ATOM   236  C C     . SER A 1 31  ? 6.525   11.623  -17.309 1.00 35.78  ? 79  SER A C     1 
ATOM   237  O O     . SER A 1 31  ? 6.389   10.442  -16.981 1.00 40.28  ? 79  SER A O     1 
ATOM   238  C CB    . SER A 1 31  ? 6.053   12.601  -19.583 1.00 47.02  ? 79  SER A CB    1 
ATOM   239  O OG    . SER A 1 31  ? 4.927   11.742  -19.716 1.00 51.48  ? 79  SER A OG    1 
ATOM   240  N N     . PRO A 1 32  ? 6.181   12.608  -16.472 1.00 38.22  ? 80  PRO A N     1 
ATOM   241  C CA    . PRO A 1 32  ? 5.559   12.266  -15.175 1.00 38.65  ? 80  PRO A CA    1 
ATOM   242  C C     . PRO A 1 32  ? 4.290   11.433  -15.295 1.00 41.44  ? 80  PRO A C     1 
ATOM   243  O O     . PRO A 1 32  ? 3.984   10.645  -14.384 1.00 39.56  ? 80  PRO A O     1 
ATOM   244  C CB    . PRO A 1 32  ? 5.280   13.637  -14.559 1.00 36.56  ? 80  PRO A CB    1 
ATOM   245  C CG    . PRO A 1 32  ? 6.422   14.480  -15.097 1.00 39.56  ? 80  PRO A CG    1 
ATOM   246  C CD    . PRO A 1 32  ? 6.629   14.012  -16.507 1.00 35.52  ? 80  PRO A CD    1 
ATOM   247  N N     . ASP A 1 33  ? 3.553   11.563  -16.399 1.00 34.40  ? 81  ASP A N     1 
ATOM   248  C CA    . ASP A 1 33  ? 2.355   10.746  -16.583 1.00 42.94  ? 81  ASP A CA    1 
ATOM   249  C C     . ASP A 1 33  ? 2.672   9.268   -16.776 1.00 39.47  ? 81  ASP A C     1 
ATOM   250  O O     . ASP A 1 33  ? 1.799   8.429   -16.524 1.00 31.10  ? 81  ASP A O     1 
ATOM   251  C CB    . ASP A 1 33  ? 1.547   11.259  -17.778 1.00 44.03  ? 81  ASP A CB    1 
ATOM   252  C CG    . ASP A 1 33  ? 1.498   12.790  -17.847 1.00 53.10  ? 81  ASP A CG    1 
ATOM   253  O OD1   . ASP A 1 33  ? 2.589   13.427  -17.898 1.00 55.10  ? 81  ASP A OD1   1 
ATOM   254  O OD2   . ASP A 1 33  ? 0.379   13.357  -17.864 1.00 47.78  ? 81  ASP A OD2   1 
ATOM   255  N N     . ASP A 1 34  ? 3.906   8.928   -17.176 1.00 41.11  ? 82  ASP A N     1 
ATOM   256  C CA    . ASP A 1 34  ? 4.287   7.564   -17.533 1.00 35.09  ? 82  ASP A CA    1 
ATOM   257  C C     . ASP A 1 34  ? 4.785   6.740   -16.353 1.00 35.89  ? 82  ASP A C     1 
ATOM   258  O O     . ASP A 1 34  ? 5.068   5.544   -16.520 1.00 31.04  ? 82  ASP A O     1 
ATOM   259  C CB    . ASP A 1 34  ? 5.388   7.574   -18.598 1.00 36.13  ? 82  ASP A CB    1 
ATOM   260  C CG    . ASP A 1 34  ? 4.980   8.258   -19.900 1.00 43.96  ? 82  ASP A CG    1 
ATOM   261  O OD1   . ASP A 1 34  ? 3.775   8.267   -20.251 1.00 45.92  ? 82  ASP A OD1   1 
ATOM   262  O OD2   . ASP A 1 34  ? 5.901   8.762   -20.599 1.00 48.16  ? 82  ASP A OD2   1 
ATOM   263  N N     . GLN A 1 35  ? 4.916   7.340   -15.172 1.00 35.61  ? 83  GLN A N     1 
ATOM   264  C CA    . GLN A 1 35  ? 5.682   6.730   -14.083 1.00 34.69  ? 83  GLN A CA    1 
ATOM   265  C C     . GLN A 1 35  ? 4.824   5.735   -13.292 1.00 34.33  ? 83  GLN A C     1 
ATOM   266  O O     . GLN A 1 35  ? 4.487   5.929   -12.121 1.00 37.27  ? 83  GLN A O     1 
ATOM   267  C CB    . GLN A 1 35  ? 6.252   7.817   -13.182 1.00 37.83  ? 83  GLN A CB    1 
ATOM   268  C CG    . GLN A 1 35  ? 7.057   8.876   -13.918 1.00 39.31  ? 83  GLN A CG    1 
ATOM   269  C CD    . GLN A 1 35  ? 8.195   8.270   -14.715 1.00 39.02  ? 83  GLN A CD    1 
ATOM   270  O OE1   . GLN A 1 35  ? 8.911   7.384   -14.225 1.00 38.22  ? 83  GLN A OE1   1 
ATOM   271  N NE2   . GLN A 1 35  ? 8.360   8.728   -15.957 1.00 29.91  ? 83  GLN A NE2   1 
ATOM   272  N N     . ILE A 1 36  ? 4.501   4.620   -13.939 1.00 32.14  ? 84  ILE A N     1 
ATOM   273  C CA    . ILE A 1 36  ? 3.642   3.626   -13.307 1.00 29.84  ? 84  ILE A CA    1 
ATOM   274  C C     . ILE A 1 36  ? 3.833   2.292   -14.019 1.00 27.30  ? 84  ILE A C     1 
ATOM   275  O O     . ILE A 1 36  ? 3.860   2.232   -15.250 1.00 26.76  ? 84  ILE A O     1 
ATOM   276  C CB    . ILE A 1 36  ? 2.161   4.091   -13.334 1.00 31.73  ? 84  ILE A CB    1 
ATOM   277  C CG1   . ILE A 1 36  ? 1.230   3.022   -12.790 1.00 33.90  ? 84  ILE A CG1   1 
ATOM   278  C CG2   . ILE A 1 36  ? 1.716   4.465   -14.745 1.00 30.95  ? 84  ILE A CG2   1 
ATOM   279  C CD1   . ILE A 1 36  ? -0.233  3.540   -12.618 1.00 32.54  ? 84  ILE A CD1   1 
ATOM   280  N N     . GLY A 1 37  ? 3.923   1.217   -13.242 1.00 21.75  ? 85  GLY A N     1 
ATOM   281  C CA    . GLY A 1 37  ? 4.056   -0.091  -13.845 1.00 26.35  ? 85  GLY A CA    1 
ATOM   282  C C     . GLY A 1 37  ? 4.093   -1.205  -12.827 1.00 28.17  ? 85  GLY A C     1 
ATOM   283  O O     . GLY A 1 37  ? 3.613   -1.066  -11.700 1.00 29.50  ? 85  GLY A O     1 
ATOM   284  N N     . TYR A 1 38  ? 4.647   -2.336  -13.257 1.00 28.48  ? 86  TYR A N     1 
ATOM   285  C CA    . TYR A 1 38  ? 4.762   -3.512  -12.409 1.00 25.44  ? 86  TYR A CA    1 
ATOM   286  C C     . TYR A 1 38  ? 6.140   -4.124  -12.583 1.00 29.67  ? 86  TYR A C     1 
ATOM   287  O O     . TYR A 1 38  ? 6.797   -3.917  -13.604 1.00 29.78  ? 86  TYR A O     1 
ATOM   288  C CB    . TYR A 1 38  ? 3.695   -4.559  -12.734 1.00 25.61  ? 86  TYR A CB    1 
ATOM   289  C CG    . TYR A 1 38  ? 3.774   -5.064  -14.138 1.00 25.29  ? 86  TYR A CG    1 
ATOM   290  C CD1   . TYR A 1 38  ? 3.169   -4.378  -15.180 1.00 27.33  ? 86  TYR A CD1   1 
ATOM   291  C CD2   . TYR A 1 38  ? 4.462   -6.224  -14.437 1.00 30.78  ? 86  TYR A CD2   1 
ATOM   292  C CE1   . TYR A 1 38  ? 3.254   -4.840  -16.468 1.00 24.85  ? 86  TYR A CE1   1 
ATOM   293  C CE2   . TYR A 1 38  ? 4.566   -6.679  -15.728 1.00 28.29  ? 86  TYR A CE2   1 
ATOM   294  C CZ    . TYR A 1 38  ? 3.965   -5.988  -16.738 1.00 25.96  ? 86  TYR A CZ    1 
ATOM   295  O OH    . TYR A 1 38  ? 4.058   -6.469  -18.022 1.00 28.48  ? 86  TYR A OH    1 
ATOM   296  N N     . TYR A 1 39  ? 6.556   -4.896  -11.570 1.00 32.67  ? 87  TYR A N     1 
ATOM   297  C CA    . TYR A 1 39  ? 7.740   -5.744  -11.619 1.00 30.66  ? 87  TYR A CA    1 
ATOM   298  C C     . TYR A 1 39  ? 7.284   -7.190  -11.708 1.00 29.48  ? 87  TYR A C     1 
ATOM   299  O O     . TYR A 1 39  ? 6.484   -7.639  -10.891 1.00 30.50  ? 87  TYR A O     1 
ATOM   300  C CB    . TYR A 1 39  ? 8.624   -5.586  -10.378 1.00 28.42  ? 87  TYR A CB    1 
ATOM   301  C CG    . TYR A 1 39  ? 9.477   -4.337  -10.272 1.00 30.03  ? 87  TYR A CG    1 
ATOM   302  C CD1   . TYR A 1 39  ? 8.997   -3.215  -9.645  1.00 27.90  ? 87  TYR A CD1   1 
ATOM   303  C CD2   . TYR A 1 39  ? 10.798  -4.317  -10.726 1.00 28.49  ? 87  TYR A CD2   1 
ATOM   304  C CE1   . TYR A 1 39  ? 9.749   -2.080  -9.524  1.00 27.17  ? 87  TYR A CE1   1 
ATOM   305  C CE2   . TYR A 1 39  ? 11.573  -3.168  -10.598 1.00 27.04  ? 87  TYR A CE2   1 
ATOM   306  C CZ    . TYR A 1 39  ? 11.043  -2.061  -9.983  1.00 31.14  ? 87  TYR A CZ    1 
ATOM   307  O OH    . TYR A 1 39  ? 11.770  -0.901  -9.840  1.00 30.73  ? 87  TYR A OH    1 
ATOM   308  N N     . ARG A 1 40  ? 7.836   -7.932  -12.655 1.00 33.99  ? 88  ARG A N     1 
ATOM   309  C CA    . ARG A 1 40  ? 7.523   -9.345  -12.829 1.00 32.46  ? 88  ARG A CA    1 
ATOM   310  C C     . ARG A 1 40  ? 8.712   -10.201 -12.385 1.00 35.14  ? 88  ARG A C     1 
ATOM   311  O O     . ARG A 1 40  ? 9.862   -9.918  -12.749 1.00 38.01  ? 88  ARG A O     1 
ATOM   312  C CB    . ARG A 1 40  ? 7.157   -9.607  -14.284 1.00 29.47  ? 88  ARG A CB    1 
ATOM   313  C CG    . ARG A 1 40  ? 6.977   -11.047 -14.680 1.00 36.50  ? 88  ARG A CG    1 
ATOM   314  C CD    . ARG A 1 40  ? 6.210   -11.103 -16.008 1.00 39.37  ? 88  ARG A CD    1 
ATOM   315  N NE    . ARG A 1 40  ? 6.035   -12.463 -16.498 1.00 36.53  ? 88  ARG A NE    1 
ATOM   316  C CZ    . ARG A 1 40  ? 6.909   -13.085 -17.271 1.00 45.72  ? 88  ARG A CZ    1 
ATOM   317  N NH1   . ARG A 1 40  ? 8.027   -12.492 -17.666 1.00 43.95  ? 88  ARG A NH1   1 
ATOM   318  N NH2   . ARG A 1 40  ? 6.658   -14.332 -17.656 1.00 50.21  ? 88  ARG A NH2   1 
ATOM   319  N N     . ARG A 1 41  ? 8.438   -11.227 -11.582 1.00 33.39  ? 89  ARG A N     1 
ATOM   320  C CA    . ARG A 1 41  ? 9.486   -12.114 -11.096 1.00 40.31  ? 89  ARG A CA    1 
ATOM   321  C C     . ARG A 1 41  ? 9.916   -13.097 -12.174 1.00 42.99  ? 89  ARG A C     1 
ATOM   322  O O     . ARG A 1 41  ? 9.082   -13.655 -12.899 1.00 43.45  ? 89  ARG A O     1 
ATOM   323  C CB    . ARG A 1 41  ? 9.020   -12.886 -9.868  1.00 42.77  ? 89  ARG A CB    1 
ATOM   324  C CG    . ARG A 1 41  ? 10.017  -13.932 -9.418  1.00 39.33  ? 89  ARG A CG    1 
ATOM   325  C CD    . ARG A 1 41  ? 9.510   -14.703 -8.232  1.00 43.48  ? 89  ARG A CD    1 
ATOM   326  N NE    . ARG A 1 41  ? 8.335   -15.483 -8.591  1.00 54.95  ? 89  ARG A NE    1 
ATOM   327  C CZ    . ARG A 1 41  ? 7.160   -15.407 -7.985  1.00 45.13  ? 89  ARG A CZ    1 
ATOM   328  N NH1   . ARG A 1 41  ? 6.982   -14.656 -6.911  1.00 47.31  ? 89  ARG A NH1   1 
ATOM   329  N NH2   . ARG A 1 41  ? 6.138   -16.104 -8.470  1.00 46.41  ? 89  ARG A NH2   1 
ATOM   330  N N     . ALA A 1 42  ? 11.226  -13.304 -12.280 1.00 36.59  ? 90  ALA A N     1 
ATOM   331  C CA    . ALA A 1 42  ? 11.797  -14.254 -13.217 1.00 40.97  ? 90  ALA A CA    1 
ATOM   332  C C     . ALA A 1 42  ? 12.644  -15.247 -12.437 1.00 48.14  ? 90  ALA A C     1 
ATOM   333  O O     . ALA A 1 42  ? 13.563  -14.856 -11.710 1.00 47.47  ? 90  ALA A O     1 
ATOM   334  C CB    . ALA A 1 42  ? 12.625  -13.549 -14.291 1.00 46.05  ? 90  ALA A CB    1 
ATOM   335  N N     . THR A 1 43  ? 12.332  -16.522 -12.595 1.00 48.80  ? 91  THR A N     1 
ATOM   336  C CA    . THR A 1 43  ? 12.999  -17.609 -11.909 1.00 44.94  ? 91  THR A CA    1 
ATOM   337  C C     . THR A 1 43  ? 14.011  -18.258 -12.839 1.00 45.70  ? 91  THR A C     1 
ATOM   338  O O     . THR A 1 43  ? 13.952  -18.121 -14.062 1.00 49.03  ? 91  THR A O     1 
ATOM   339  C CB    . THR A 1 43  ? 11.976  -18.641 -11.438 1.00 51.62  ? 91  THR A CB    1 
ATOM   340  O OG1   . THR A 1 43  ? 11.312  -19.200 -12.584 1.00 51.48  ? 91  THR A OG1   1 
ATOM   341  C CG2   . THR A 1 43  ? 10.939  -17.977 -10.532 1.00 48.30  ? 91  THR A CG2   1 
ATOM   342  N N     . ARG A 1 44  ? 14.974  -18.939 -12.234 1.00 46.67  ? 92  ARG A N     1 
ATOM   343  C CA    . ARG A 1 44  ? 16.007  -19.661 -12.958 1.00 49.42  ? 92  ARG A CA    1 
ATOM   344  C C     . ARG A 1 44  ? 16.444  -20.815 -12.077 1.00 44.58  ? 92  ARG A C     1 
ATOM   345  O O     . ARG A 1 44  ? 16.445  -20.697 -10.852 1.00 47.89  ? 92  ARG A O     1 
ATOM   346  C CB    . ARG A 1 44  ? 17.220  -18.771 -13.292 1.00 51.28  ? 92  ARG A CB    1 
ATOM   347  C CG    . ARG A 1 44  ? 16.936  -17.289 -13.413 1.00 53.55  ? 92  ARG A CG    1 
ATOM   348  C CD    . ARG A 1 44  ? 18.084  -16.482 -12.900 1.00 51.48  ? 92  ARG A CD    1 
ATOM   349  N NE    . ARG A 1 44  ? 19.210  -16.554 -13.816 1.00 60.20  ? 92  ARG A NE    1 
ATOM   350  C CZ    . ARG A 1 44  ? 20.436  -16.161 -13.501 1.00 62.02  ? 92  ARG A CZ    1 
ATOM   351  N NH1   . ARG A 1 44  ? 20.713  -15.686 -12.296 1.00 54.01  ? 92  ARG A NH1   1 
ATOM   352  N NH2   . ARG A 1 44  ? 21.404  -16.249 -14.417 1.00 56.63  ? 92  ARG A NH2   1 
ATOM   353  N N     . ARG A 1 45  ? 16.802  -21.933 -12.698 1.00 45.42  ? 93  ARG A N     1 
ATOM   354  C CA    . ARG A 1 45  ? 17.365  -23.037 -11.941 1.00 49.16  ? 93  ARG A CA    1 
ATOM   355  C C     . ARG A 1 45  ? 18.353  -23.784 -12.818 1.00 53.48  ? 93  ARG A C     1 
ATOM   356  O O     . ARG A 1 45  ? 18.254  -23.763 -14.047 1.00 54.03  ? 93  ARG A O     1 
ATOM   357  C CB    . ARG A 1 45  ? 16.298  -23.990 -11.419 1.00 55.36  ? 93  ARG A CB    1 
ATOM   358  C CG    . ARG A 1 45  ? 15.422  -24.537 -12.508 1.00 55.98  ? 93  ARG A CG    1 
ATOM   359  C CD    . ARG A 1 45  ? 14.631  -25.718 -12.015 1.00 55.18  ? 93  ARG A CD    1 
ATOM   360  N NE    . ARG A 1 45  ? 13.843  -25.388 -10.839 1.00 58.03  ? 93  ARG A NE    1 
ATOM   361  C CZ    . ARG A 1 45  ? 13.080  -26.260 -10.199 1.00 60.66  ? 93  ARG A CZ    1 
ATOM   362  N NH1   . ARG A 1 45  ? 13.009  -27.525 -10.586 1.00 58.53  ? 93  ARG A NH1   1 
ATOM   363  N NH2   . ARG A 1 45  ? 12.373  -25.854 -9.146  1.00 58.86  ? 93  ARG A NH2   1 
ATOM   364  N N     . ILE A 1 46  ? 19.325  -24.426 -12.170 1.00 53.26  ? 94  ILE A N     1 
ATOM   365  C CA    . ILE A 1 46  ? 20.371  -25.140 -12.881 1.00 58.62  ? 94  ILE A CA    1 
ATOM   366  C C     . ILE A 1 46  ? 20.503  -26.542 -12.310 1.00 60.44  ? 94  ILE A C     1 
ATOM   367  O O     . ILE A 1 46  ? 20.098  -26.823 -11.180 1.00 59.31  ? 94  ILE A O     1 
ATOM   368  C CB    . ILE A 1 46  ? 21.737  -24.419 -12.817 1.00 55.17  ? 94  ILE A CB    1 
ATOM   369  C CG1   . ILE A 1 46  ? 22.187  -24.252 -11.365 1.00 60.12  ? 94  ILE A CG1   1 
ATOM   370  C CG2   . ILE A 1 46  ? 21.684  -23.099 -13.556 1.00 51.74  ? 94  ILE A CG2   1 
ATOM   371  C CD1   . ILE A 1 46  ? 23.674  -24.566 -11.137 1.00 60.48  ? 94  ILE A CD1   1 
ATOM   372  N N     . ARG A 1 47  ? 21.066  -27.429 -13.130 1.00 62.75  ? 95  ARG A N     1 
ATOM   373  C CA    . ARG A 1 47  ? 21.604  -28.685 -12.637 1.00 68.11  ? 95  ARG A CA    1 
ATOM   374  C C     . ARG A 1 47  ? 22.682  -28.352 -11.602 1.00 75.55  ? 95  ARG A C     1 
ATOM   375  O O     . ARG A 1 47  ? 23.706  -27.737 -11.929 1.00 76.06  ? 95  ARG A O     1 
ATOM   376  C CB    . ARG A 1 47  ? 22.119  -29.519 -13.816 1.00 70.57  ? 95  ARG A CB    1 
ATOM   377  C CG    . ARG A 1 47  ? 23.519  -30.117 -13.684 1.00 74.04  ? 95  ARG A CG    1 
ATOM   378  C CD    . ARG A 1 47  ? 23.520  -31.352 -12.805 1.00 79.03  ? 95  ARG A CD    1 
ATOM   379  N NE    . ARG A 1 47  ? 22.332  -32.173 -13.014 1.00 82.12  ? 95  ARG A NE    1 
ATOM   380  C CZ    . ARG A 1 47  ? 22.170  -33.032 -14.013 1.00 76.67  ? 95  ARG A CZ    1 
ATOM   381  N NH1   . ARG A 1 47  ? 23.087  -33.178 -14.958 1.00 78.00  ? 95  ARG A NH1   1 
ATOM   382  N NH2   . ARG A 1 47  ? 21.057  -33.760 -14.065 1.00 74.73  ? 95  ARG A NH2   1 
ATOM   383  N N     . GLY A 1 48  ? 22.437  -28.727 -10.338 1.00 75.90  ? 96  GLY A N     1 
ATOM   384  C CA    . GLY A 1 48  ? 23.180  -28.219 -9.195  1.00 73.07  ? 96  GLY A CA    1 
ATOM   385  C C     . GLY A 1 48  ? 24.518  -28.871 -8.911  1.00 82.29  ? 96  GLY A C     1 
ATOM   386  O O     . GLY A 1 48  ? 25.233  -28.400 -8.020  1.00 84.62  ? 96  GLY A O     1 
ATOM   387  N N     . GLY A 1 49  ? 24.885  -29.928 -9.636  1.00 82.51  ? 97  GLY A N     1 
ATOM   388  C CA    . GLY A 1 49  ? 26.153  -30.589 -9.383  1.00 80.94  ? 97  GLY A CA    1 
ATOM   389  C C     . GLY A 1 49  ? 25.992  -31.976 -8.796  1.00 81.62  ? 97  GLY A C     1 
ATOM   390  O O     . GLY A 1 49  ? 26.691  -32.913 -9.191  1.00 84.30  ? 97  GLY A O     1 
ATOM   391  N N     . ASP A 1 50  ? 25.065  -32.124 -7.852  1.00 83.23  ? 98  ASP A N     1 
ATOM   392  C CA    . ASP A 1 50  ? 24.673  -33.433 -7.353  1.00 81.60  ? 98  ASP A CA    1 
ATOM   393  C C     . ASP A 1 50  ? 23.584  -34.084 -8.209  1.00 81.06  ? 98  ASP A C     1 
ATOM   394  O O     . ASP A 1 50  ? 22.943  -35.043 -7.761  1.00 80.75  ? 98  ASP A O     1 
ATOM   395  C CB    . ASP A 1 50  ? 24.222  -33.334 -5.888  1.00 82.51  ? 98  ASP A CB    1 
ATOM   396  C CG    . ASP A 1 50  ? 23.674  -31.959 -5.519  1.00 81.38  ? 98  ASP A CG    1 
ATOM   397  O OD1   . ASP A 1 50  ? 22.483  -31.695 -5.789  1.00 80.39  ? 98  ASP A OD1   1 
ATOM   398  O OD2   . ASP A 1 50  ? 24.432  -31.149 -4.941  1.00 78.84  ? 98  ASP A OD2   1 
ATOM   399  N N     . GLY A 1 51  ? 23.370  -33.590 -9.431  1.00 77.46  ? 99  GLY A N     1 
ATOM   400  C CA    . GLY A 1 51  ? 22.325  -34.090 -10.303 1.00 75.48  ? 99  GLY A CA    1 
ATOM   401  C C     . GLY A 1 51  ? 20.953  -33.514 -10.041 1.00 75.05  ? 99  GLY A C     1 
ATOM   402  O O     . GLY A 1 51  ? 20.010  -33.833 -10.778 1.00 69.76  ? 99  GLY A O     1 
ATOM   403  N N     . LYS A 1 52  ? 20.816  -32.669 -9.026  1.00 75.77  ? 100 LYS A N     1 
ATOM   404  C CA    . LYS A 1 52  ? 19.547  -32.109 -8.608  1.00 69.22  ? 100 LYS A CA    1 
ATOM   405  C C     . LYS A 1 52  ? 19.496  -30.633 -8.971  1.00 70.39  ? 100 LYS A C     1 
ATOM   406  O O     . LYS A 1 52  ? 20.520  -29.944 -8.980  1.00 69.85  ? 100 LYS A O     1 
ATOM   407  C CB    . LYS A 1 52  ? 19.344  -32.283 -7.101  1.00 72.27  ? 100 LYS A CB    1 
ATOM   408  C CG    . LYS A 1 52  ? 19.193  -33.734 -6.659  1.00 74.87  ? 100 LYS A CG    1 
ATOM   409  C CD    . LYS A 1 52  ? 17.876  -34.338 -7.148  1.00 67.64  ? 100 LYS A CD    1 
ATOM   410  C CE    . LYS A 1 52  ? 17.870  -35.854 -6.983  1.00 71.46  ? 100 LYS A CE    1 
ATOM   411  N NZ    . LYS A 1 52  ? 19.035  -36.521 -7.650  1.00 75.15  ? 100 LYS A NZ    1 
ATOM   412  N N     . MET A 1 53  ? 18.291  -30.158 -9.272  1.00 66.29  ? 101 MET A N     1 
ATOM   413  C CA    . MET A 1 53  ? 18.108  -28.769 -9.661  1.00 62.65  ? 101 MET A CA    1 
ATOM   414  C C     . MET A 1 53  ? 18.407  -27.835 -8.495  1.00 60.78  ? 101 MET A C     1 
ATOM   415  O O     . MET A 1 53  ? 18.033  -28.103 -7.352  1.00 59.62  ? 101 MET A O     1 
ATOM   416  C CB    . MET A 1 53  ? 16.684  -28.547 -10.164 1.00 53.16  ? 101 MET A CB    1 
ATOM   417  C CG    . MET A 1 53  ? 16.367  -29.321 -11.413 1.00 53.68  ? 101 MET A CG    1 
ATOM   418  S SD    . MET A 1 53  ? 17.639  -29.200 -12.680 1.00 65.31  ? 101 MET A SD    1 
ATOM   419  C CE    . MET A 1 53  ? 17.271  -27.599 -13.384 1.00 57.88  ? 101 MET A CE    1 
ATOM   420  N N     . LYS A 1 54  ? 19.088  -26.732 -8.794  1.00 61.85  ? 102 LYS A N     1 
ATOM   421  C CA    . LYS A 1 54  ? 19.414  -25.707 -7.814  1.00 55.98  ? 102 LYS A CA    1 
ATOM   422  C C     . LYS A 1 54  ? 18.657  -24.445 -8.193  1.00 58.50  ? 102 LYS A C     1 
ATOM   423  O O     . LYS A 1 54  ? 18.797  -23.961 -9.321  1.00 54.31  ? 102 LYS A O     1 
ATOM   424  C CB    . LYS A 1 54  ? 20.923  -25.448 -7.769  1.00 62.29  ? 102 LYS A CB    1 
ATOM   425  C CG    . LYS A 1 54  ? 21.354  -24.470 -6.694  1.00 64.70  ? 102 LYS A CG    1 
ATOM   426  C CD    . LYS A 1 54  ? 22.860  -24.240 -6.699  1.00 72.67  ? 102 LYS A CD    1 
ATOM   427  C CE    . LYS A 1 54  ? 23.258  -23.179 -5.677  1.00 70.36  ? 102 LYS A CE    1 
ATOM   428  N NZ    . LYS A 1 54  ? 24.724  -22.906 -5.674  1.00 72.82  ? 102 LYS A NZ    1 
ATOM   429  N N     . ASP A 1 55  ? 17.842  -23.936 -7.264  1.00 56.88  ? 103 ASP A N     1 
ATOM   430  C CA    . ASP A 1 55  ? 17.133  -22.680 -7.463  1.00 50.76  ? 103 ASP A CA    1 
ATOM   431  C C     . ASP A 1 55  ? 18.081  -21.498 -7.242  1.00 57.71  ? 103 ASP A C     1 
ATOM   432  O O     . ASP A 1 55  ? 18.762  -21.417 -6.216  1.00 54.61  ? 103 ASP A O     1 
ATOM   433  C CB    . ASP A 1 55  ? 15.942  -22.585 -6.513  1.00 52.02  ? 103 ASP A CB    1 
ATOM   434  C CG    . ASP A 1 55  ? 14.864  -23.632 -6.802  1.00 62.71  ? 103 ASP A CG    1 
ATOM   435  O OD1   . ASP A 1 55  ? 14.479  -23.798 -7.985  1.00 63.29  ? 103 ASP A OD1   1 
ATOM   436  O OD2   . ASP A 1 55  ? 14.393  -24.290 -5.843  1.00 61.23  ? 103 ASP A OD2   1 
ATOM   437  N N     . LEU A 1 56  ? 18.126  -20.586 -8.209  1.00 52.04  ? 104 LEU A N     1 
ATOM   438  C CA    . LEU A 1 56  ? 18.939  -19.386 -8.103  1.00 50.73  ? 104 LEU A CA    1 
ATOM   439  C C     . LEU A 1 56  ? 18.092  -18.237 -7.582  1.00 47.79  ? 104 LEU A C     1 
ATOM   440  O O     . LEU A 1 56  ? 16.864  -18.317 -7.521  1.00 51.97  ? 104 LEU A O     1 
ATOM   441  C CB    . LEU A 1 56  ? 19.550  -19.025 -9.456  1.00 48.26  ? 104 LEU A CB    1 
ATOM   442  C CG    . LEU A 1 56  ? 20.252  -20.169 -10.182 1.00 49.00  ? 104 LEU A CG    1 
ATOM   443  C CD1   . LEU A 1 56  ? 20.563  -19.760 -11.606 1.00 49.55  ? 104 LEU A CD1   1 
ATOM   444  C CD2   . LEU A 1 56  ? 21.524  -20.611 -9.435  1.00 50.58  ? 104 LEU A CD2   1 
ATOM   445  N N     . SER A 1 57  ? 18.760  -17.155 -7.213  1.00 43.70  ? 105 SER A N     1 
ATOM   446  C CA    . SER A 1 57  ? 18.056  -16.001 -6.671  1.00 47.35  ? 105 SER A CA    1 
ATOM   447  C C     . SER A 1 57  ? 17.100  -15.438 -7.718  1.00 44.76  ? 105 SER A C     1 
ATOM   448  O O     . SER A 1 57  ? 17.508  -15.204 -8.862  1.00 48.28  ? 105 SER A O     1 
ATOM   449  C CB    . SER A 1 57  ? 19.035  -14.919 -6.232  1.00 44.85  ? 105 SER A CB    1 
ATOM   450  O OG    . SER A 1 57  ? 19.545  -15.211 -4.952  1.00 51.11  ? 105 SER A OG    1 
ATOM   451  N N     . PRO A 1 58  ? 15.835  -15.239 -7.382  1.00 42.77  ? 106 PRO A N     1 
ATOM   452  C CA    . PRO A 1 58  ? 14.910  -14.634 -8.339  1.00 40.73  ? 106 PRO A CA    1 
ATOM   453  C C     . PRO A 1 58  ? 15.356  -13.227 -8.707  1.00 41.90  ? 106 PRO A C     1 
ATOM   454  O O     . PRO A 1 58  ? 15.926  -12.495 -7.893  1.00 40.83  ? 106 PRO A O     1 
ATOM   455  C CB    . PRO A 1 58  ? 13.574  -14.618 -7.580  1.00 41.23  ? 106 PRO A CB    1 
ATOM   456  C CG    . PRO A 1 58  ? 13.722  -15.638 -6.514  1.00 46.79  ? 106 PRO A CG    1 
ATOM   457  C CD    . PRO A 1 58  ? 15.171  -15.632 -6.130  1.00 44.93  ? 106 PRO A CD    1 
ATOM   458  N N     . ARG A 1 59  ? 15.103  -12.858 -9.959  1.00 41.34  ? 107 ARG A N     1 
ATOM   459  C CA    . ARG A 1 59  ? 15.250  -11.485 -10.414 1.00 39.43  ? 107 ARG A CA    1 
ATOM   460  C C     . ARG A 1 59  ? 13.874  -10.908 -10.727 1.00 41.15  ? 107 ARG A C     1 
ATOM   461  O O     . ARG A 1 59  ? 12.940  -11.645 -11.052 1.00 39.14  ? 107 ARG A O     1 
ATOM   462  C CB    . ARG A 1 59  ? 16.129  -11.400 -11.661 1.00 43.50  ? 107 ARG A CB    1 
ATOM   463  C CG    . ARG A 1 59  ? 17.596  -11.795 -11.481 1.00 43.46  ? 107 ARG A CG    1 
ATOM   464  C CD    . ARG A 1 59  ? 18.151  -12.151 -12.850 1.00 44.68  ? 107 ARG A CD    1 
ATOM   465  N NE    . ARG A 1 59  ? 19.601  -12.247 -12.888 1.00 49.67  ? 107 ARG A NE    1 
ATOM   466  C CZ    . ARG A 1 59  ? 20.278  -12.793 -13.888 1.00 54.74  ? 107 ARG A CZ    1 
ATOM   467  N NH1   . ARG A 1 59  ? 19.662  -13.301 -14.944 1.00 45.16  ? 107 ARG A NH1   1 
ATOM   468  N NH2   . ARG A 1 59  ? 21.608  -12.845 -13.821 1.00 56.02  ? 107 ARG A NH2   1 
ATOM   469  N N     . TRP A 1 60  ? 13.764  -9.583  -10.647 1.00 38.63  ? 108 TRP A N     1 
ATOM   470  C CA    . TRP A 1 60  ? 12.510  -8.866  -10.854 1.00 37.32  ? 108 TRP A CA    1 
ATOM   471  C C     . TRP A 1 60  ? 12.724  -7.776  -11.893 1.00 35.20  ? 108 TRP A C     1 
ATOM   472  O O     . TRP A 1 60  ? 13.630  -6.954  -11.741 1.00 30.96  ? 108 TRP A O     1 
ATOM   473  C CB    . TRP A 1 60  ? 12.017  -8.249  -9.545  1.00 35.45  ? 108 TRP A CB    1 
ATOM   474  C CG    . TRP A 1 60  ? 11.613  -9.267  -8.507  1.00 42.27  ? 108 TRP A CG    1 
ATOM   475  C CD1   . TRP A 1 60  ? 12.442  -10.041 -7.741  1.00 38.05  ? 108 TRP A CD1   1 
ATOM   476  C CD2   . TRP A 1 60  ? 10.272  -9.594  -8.102  1.00 39.13  ? 108 TRP A CD2   1 
ATOM   477  N NE1   . TRP A 1 60  ? 11.697  -10.839 -6.894  1.00 42.10  ? 108 TRP A NE1   1 
ATOM   478  C CE2   . TRP A 1 60  ? 10.366  -10.582 -7.095  1.00 42.18  ? 108 TRP A CE2   1 
ATOM   479  C CE3   . TRP A 1 60  ? 9.006   -9.155  -8.500  1.00 39.82  ? 108 TRP A CE3   1 
ATOM   480  C CZ2   . TRP A 1 60  ? 9.238   -11.137 -6.483  1.00 46.17  ? 108 TRP A CZ2   1 
ATOM   481  C CZ3   . TRP A 1 60  ? 7.887   -9.705  -7.890  1.00 40.61  ? 108 TRP A CZ3   1 
ATOM   482  C CH2   . TRP A 1 60  ? 8.012   -10.686 -6.892  1.00 42.42  ? 108 TRP A CH2   1 
ATOM   483  N N     . TYR A 1 61  ? 11.888  -7.755  -12.934 1.00 34.25  ? 109 TYR A N     1 
ATOM   484  C CA    . TYR A 1 61  ? 12.008  -6.767  -14.003 1.00 32.46  ? 109 TYR A CA    1 
ATOM   485  C C     . TYR A 1 61  ? 10.791  -5.854  -14.038 1.00 33.84  ? 109 TYR A C     1 
ATOM   486  O O     . TYR A 1 61  ? 9.656   -6.303  -13.853 1.00 36.14  ? 109 TYR A O     1 
ATOM   487  C CB    . TYR A 1 61  ? 12.172  -7.430  -15.363 1.00 32.20  ? 109 TYR A CB    1 
ATOM   488  C CG    . TYR A 1 61  ? 13.417  -8.275  -15.523 1.00 32.94  ? 109 TYR A CG    1 
ATOM   489  C CD1   . TYR A 1 61  ? 13.440  -9.601  -15.110 1.00 35.25  ? 109 TYR A CD1   1 
ATOM   490  C CD2   . TYR A 1 61  ? 14.550  -7.755  -16.123 1.00 32.54  ? 109 TYR A CD2   1 
ATOM   491  C CE1   . TYR A 1 61  ? 14.575  -10.386 -15.281 1.00 36.38  ? 109 TYR A CE1   1 
ATOM   492  C CE2   . TYR A 1 61  ? 15.691  -8.518  -16.302 1.00 37.04  ? 109 TYR A CE2   1 
ATOM   493  C CZ    . TYR A 1 61  ? 15.700  -9.838  -15.880 1.00 41.45  ? 109 TYR A CZ    1 
ATOM   494  O OH    . TYR A 1 61  ? 16.831  -10.606 -16.051 1.00 41.59  ? 109 TYR A OH    1 
ATOM   495  N N     . PHE A 1 62  ? 11.030  -4.570  -14.298 1.00 34.60  ? 110 PHE A N     1 
ATOM   496  C CA    . PHE A 1 62  ? 9.961   -3.584  -14.360 1.00 30.10  ? 110 PHE A CA    1 
ATOM   497  C C     . PHE A 1 62  ? 9.470   -3.410  -15.791 1.00 31.04  ? 110 PHE A C     1 
ATOM   498  O O     . PHE A 1 62  ? 10.278  -3.369  -16.731 1.00 29.14  ? 110 PHE A O     1 
ATOM   499  C CB    . PHE A 1 62  ? 10.441  -2.240  -13.828 1.00 29.86  ? 110 PHE A CB    1 
ATOM   500  C CG    . PHE A 1 62  ? 9.511   -1.126  -14.123 1.00 28.14  ? 110 PHE A CG    1 
ATOM   501  C CD1   . PHE A 1 62  ? 8.452   -0.853  -13.269 1.00 30.35  ? 110 PHE A CD1   1 
ATOM   502  C CD2   . PHE A 1 62  ? 9.661   -0.366  -15.271 1.00 28.70  ? 110 PHE A CD2   1 
ATOM   503  C CE1   . PHE A 1 62  ? 7.580   0.175   -13.545 1.00 27.59  ? 110 PHE A CE1   1 
ATOM   504  C CE2   . PHE A 1 62  ? 8.783   0.656   -15.560 1.00 27.81  ? 110 PHE A CE2   1 
ATOM   505  C CZ    . PHE A 1 62  ? 7.751   0.932   -14.688 1.00 28.02  ? 110 PHE A CZ    1 
ATOM   506  N N     . TYR A 1 63  ? 8.135   -3.301  -15.939 1.00 27.07  ? 111 TYR A N     1 
ATOM   507  C CA    . TYR A 1 63  ? 7.464   -2.937  -17.185 1.00 25.06  ? 111 TYR A CA    1 
ATOM   508  C C     . TYR A 1 63  ? 6.411   -1.862  -16.921 1.00 26.26  ? 111 TYR A C     1 
ATOM   509  O O     . TYR A 1 63  ? 5.688   -1.921  -15.919 1.00 23.33  ? 111 TYR A O     1 
ATOM   510  C CB    . TYR A 1 63  ? 6.775   -4.138  -17.830 1.00 25.91  ? 111 TYR A CB    1 
ATOM   511  C CG    . TYR A 1 63  ? 7.655   -5.335  -18.138 1.00 30.03  ? 111 TYR A CG    1 
ATOM   512  C CD1   . TYR A 1 63  ? 7.955   -6.274  -17.156 1.00 29.74  ? 111 TYR A CD1   1 
ATOM   513  C CD2   . TYR A 1 63  ? 8.160   -5.540  -19.420 1.00 28.52  ? 111 TYR A CD2   1 
ATOM   514  C CE1   . TYR A 1 63  ? 8.744   -7.368  -17.424 1.00 24.98  ? 111 TYR A CE1   1 
ATOM   515  C CE2   . TYR A 1 63  ? 8.936   -6.638  -19.707 1.00 27.64  ? 111 TYR A CE2   1 
ATOM   516  C CZ    . TYR A 1 63  ? 9.227   -7.554  -18.696 1.00 32.30  ? 111 TYR A CZ    1 
ATOM   517  O OH    . TYR A 1 63  ? 10.012  -8.658  -18.963 1.00 36.12  ? 111 TYR A OH    1 
ATOM   518  N N     . TYR A 1 64  ? 6.315   -0.890  -17.831 1.00 25.07  ? 112 TYR A N     1 
ATOM   519  C CA    . TYR A 1 64  ? 5.345   0.177   -17.691 1.00 27.91  ? 112 TYR A CA    1 
ATOM   520  C C     . TYR A 1 64  ? 3.931   -0.394  -17.760 1.00 25.17  ? 112 TYR A C     1 
ATOM   521  O O     . TYR A 1 64  ? 3.694   -1.455  -18.339 1.00 24.33  ? 112 TYR A O     1 
ATOM   522  C CB    . TYR A 1 64  ? 5.534   1.222   -18.779 1.00 29.32  ? 112 TYR A CB    1 
ATOM   523  C CG    . TYR A 1 64  ? 6.770   2.046   -18.611 1.00 27.99  ? 112 TYR A CG    1 
ATOM   524  C CD1   . TYR A 1 64  ? 6.765   3.155   -17.782 1.00 27.99  ? 112 TYR A CD1   1 
ATOM   525  C CD2   . TYR A 1 64  ? 7.955   1.721   -19.292 1.00 27.24  ? 112 TYR A CD2   1 
ATOM   526  C CE1   . TYR A 1 64  ? 7.901   3.925   -17.620 1.00 32.24  ? 112 TYR A CE1   1 
ATOM   527  C CE2   . TYR A 1 64  ? 9.108   2.472   -19.116 1.00 24.14  ? 112 TYR A CE2   1 
ATOM   528  C CZ    . TYR A 1 64  ? 9.075   3.573   -18.293 1.00 30.29  ? 112 TYR A CZ    1 
ATOM   529  O OH    . TYR A 1 64  ? 10.187  4.357   -18.123 1.00 29.84  ? 112 TYR A OH    1 
ATOM   530  N N     . LEU A 1 65  ? 3.010   0.276   -17.083 1.00 26.91  ? 113 LEU A N     1 
ATOM   531  C CA    . LEU A 1 65  ? 1.623   -0.181  -17.059 1.00 29.20  ? 113 LEU A CA    1 
ATOM   532  C C     . LEU A 1 65  ? 1.138   -0.399  -18.485 1.00 25.80  ? 113 LEU A C     1 
ATOM   533  O O     . LEU A 1 65  ? 1.389   0.419   -19.364 1.00 24.45  ? 113 LEU A O     1 
ATOM   534  C CB    . LEU A 1 65  ? 0.743   0.845   -16.333 1.00 24.16  ? 113 LEU A CB    1 
ATOM   535  C CG    . LEU A 1 65  ? -0.783  0.650   -16.391 1.00 30.02  ? 113 LEU A CG    1 
ATOM   536  C CD1   . LEU A 1 65  ? -1.267  -0.538  -15.541 1.00 25.59  ? 113 LEU A CD1   1 
ATOM   537  C CD2   . LEU A 1 65  ? -1.493  1.927   -15.973 1.00 27.67  ? 113 LEU A CD2   1 
ATOM   538  N N     . GLY A 1 66  ? 0.511   -1.547  -18.726 1.00 27.51  ? 114 GLY A N     1 
ATOM   539  C CA    . GLY A 1 66  ? 0.000   -1.814  -20.050 1.00 28.00  ? 114 GLY A CA    1 
ATOM   540  C C     . GLY A 1 66  ? 1.007   -2.309  -21.066 1.00 30.36  ? 114 GLY A C     1 
ATOM   541  O O     . GLY A 1 66  ? 0.709   -2.288  -22.259 1.00 28.28  ? 114 GLY A O     1 
ATOM   542  N N     . THR A 1 67  ? 2.210   -2.705  -20.652 1.00 30.74  ? 115 THR A N     1 
ATOM   543  C CA    . THR A 1 67  ? 3.182   -3.273  -21.576 1.00 27.63  ? 115 THR A CA    1 
ATOM   544  C C     . THR A 1 67  ? 3.732   -4.559  -20.977 1.00 28.50  ? 115 THR A C     1 
ATOM   545  O O     . THR A 1 67  ? 3.500   -4.880  -19.804 1.00 29.09  ? 115 THR A O     1 
ATOM   546  C CB    . THR A 1 67  ? 4.338   -2.293  -21.895 1.00 30.67  ? 115 THR A CB    1 
ATOM   547  O OG1   . THR A 1 67  ? 5.173   -2.138  -20.748 1.00 25.56  ? 115 THR A OG1   1 
ATOM   548  C CG2   . THR A 1 67  ? 3.817   -0.911  -22.307 1.00 27.04  ? 115 THR A CG2   1 
ATOM   549  N N     . GLY A 1 68  ? 4.479   -5.296  -21.797 1.00 31.04  ? 116 GLY A N     1 
ATOM   550  C CA    . GLY A 1 68  ? 5.196   -6.461  -21.333 1.00 28.22  ? 116 GLY A CA    1 
ATOM   551  C C     . GLY A 1 68  ? 4.339   -7.703  -21.221 1.00 32.62  ? 116 GLY A C     1 
ATOM   552  O O     . GLY A 1 68  ? 3.192   -7.766  -21.710 1.00 29.93  ? 116 GLY A O     1 
ATOM   553  N N     . PRO A 1 69  ? 4.898   -8.722  -20.554 1.00 35.07  ? 117 PRO A N     1 
ATOM   554  C CA    . PRO A 1 69  ? 4.214   -10.028 -20.456 1.00 35.14  ? 117 PRO A CA    1 
ATOM   555  C C     . PRO A 1 69  ? 2.884   -9.992  -19.723 1.00 30.25  ? 117 PRO A C     1 
ATOM   556  O O     . PRO A 1 69  ? 2.062   -10.890 -19.934 1.00 31.38  ? 117 PRO A O     1 
ATOM   557  C CB    . PRO A 1 69  ? 5.234   -10.901 -19.705 1.00 30.46  ? 117 PRO A CB    1 
ATOM   558  C CG    . PRO A 1 69  ? 6.539   -10.204 -19.898 1.00 30.44  ? 117 PRO A CG    1 
ATOM   559  C CD    . PRO A 1 69  ? 6.212   -8.753  -19.894 1.00 32.15  ? 117 PRO A CD    1 
ATOM   560  N N     . GLU A 1 70  ? 2.642   -9.022  -18.857 1.00 28.53  ? 118 GLU A N     1 
ATOM   561  C CA    . GLU A 1 70  ? 1.314   -8.818  -18.281 1.00 29.23  ? 118 GLU A CA    1 
ATOM   562  C C     . GLU A 1 70  ? 0.731   -7.483  -18.734 1.00 30.12  ? 118 GLU A C     1 
ATOM   563  O O     . GLU A 1 70  ? 0.178   -6.724  -17.936 1.00 30.24  ? 118 GLU A O     1 
ATOM   564  C CB    . GLU A 1 70  ? 1.342   -8.893  -16.759 1.00 28.98  ? 118 GLU A CB    1 
ATOM   565  C CG    . GLU A 1 70  ? 1.724   -10.271 -16.201 1.00 29.87  ? 118 GLU A CG    1 
ATOM   566  C CD    . GLU A 1 70  ? 0.731   -11.381 -16.554 1.00 36.53  ? 118 GLU A CD    1 
ATOM   567  O OE1   . GLU A 1 70  ? -0.402  -11.087 -16.982 1.00 36.35  ? 118 GLU A OE1   1 
ATOM   568  O OE2   . GLU A 1 70  ? 1.084   -12.574 -16.401 1.00 41.41  ? 118 GLU A OE2   1 
ATOM   569  N N     . ALA A 1 71  ? 0.879   -7.182  -20.029 1.00 27.83  ? 119 ALA A N     1 
ATOM   570  C CA    . ALA A 1 71  ? 0.364   -5.934  -20.576 1.00 27.55  ? 119 ALA A CA    1 
ATOM   571  C C     . ALA A 1 71  ? -1.134  -5.769  -20.308 1.00 27.63  ? 119 ALA A C     1 
ATOM   572  O O     . ALA A 1 71  ? -1.605  -4.646  -20.130 1.00 26.00  ? 119 ALA A O     1 
ATOM   573  C CB    . ALA A 1 71  ? 0.640   -5.881  -22.082 1.00 27.01  ? 119 ALA A CB    1 
ATOM   574  N N     . GLY A 1 72  ? -1.891  -6.861  -20.276 1.00 21.75  ? 120 GLY A N     1 
ATOM   575  C CA    . GLY A 1 72  ? -3.339  -6.761  -20.085 1.00 33.53  ? 120 GLY A CA    1 
ATOM   576  C C     . GLY A 1 72  ? -3.838  -6.618  -18.650 1.00 32.59  ? 120 GLY A C     1 
ATOM   577  O O     . GLY A 1 72  ? -5.019  -6.295  -18.449 1.00 28.79  ? 120 GLY A O     1 
ATOM   578  N N     . LEU A 1 73  ? -2.983  -6.866  -17.658 1.00 29.86  ? 121 LEU A N     1 
ATOM   579  C CA    . LEU A 1 73  ? -3.385  -6.727  -16.258 1.00 28.51  ? 121 LEU A CA    1 
ATOM   580  C C     . LEU A 1 73  ? -3.539  -5.255  -15.891 1.00 31.87  ? 121 LEU A C     1 
ATOM   581  O O     . LEU A 1 73  ? -2.668  -4.448  -16.216 1.00 28.13  ? 121 LEU A O     1 
ATOM   582  C CB    . LEU A 1 73  ? -2.370  -7.371  -15.325 1.00 32.45  ? 121 LEU A CB    1 
ATOM   583  C CG    . LEU A 1 73  ? -2.245  -8.889  -15.299 1.00 31.89  ? 121 LEU A CG    1 
ATOM   584  C CD1   . LEU A 1 73  ? -1.414  -9.278  -14.086 1.00 33.16  ? 121 LEU A CD1   1 
ATOM   585  C CD2   . LEU A 1 73  ? -3.624  -9.525  -15.263 1.00 31.57  ? 121 LEU A CD2   1 
ATOM   586  N N     . PRO A 1 74  ? -4.619  -4.867  -15.216 1.00 32.03  ? 122 PRO A N     1 
ATOM   587  C CA    . PRO A 1 74  ? -4.776  -3.468  -14.821 1.00 28.55  ? 122 PRO A CA    1 
ATOM   588  C C     . PRO A 1 74  ? -4.020  -3.229  -13.536 1.00 23.96  ? 122 PRO A C     1 
ATOM   589  O O     . PRO A 1 74  ? -3.711  -4.161  -12.801 1.00 27.94  ? 122 PRO A O     1 
ATOM   590  C CB    . PRO A 1 74  ? -6.290  -3.347  -14.591 1.00 27.80  ? 122 PRO A CB    1 
ATOM   591  C CG    . PRO A 1 74  ? -6.606  -4.660  -13.974 1.00 24.67  ? 122 PRO A CG    1 
ATOM   592  C CD    . PRO A 1 74  ? -5.669  -5.700  -14.616 1.00 29.32  ? 122 PRO A CD    1 
ATOM   593  N N     . TYR A 1 75  ? -3.782  -1.961  -13.239 1.00 24.69  ? 123 TYR A N     1 
ATOM   594  C CA    . TYR A 1 75  ? -2.985  -1.647  -12.067 1.00 24.41  ? 123 TYR A CA    1 
ATOM   595  C C     . TYR A 1 75  ? -3.604  -2.280  -10.827 1.00 31.68  ? 123 TYR A C     1 
ATOM   596  O O     . TYR A 1 75  ? -4.828  -2.373  -10.699 1.00 31.06  ? 123 TYR A O     1 
ATOM   597  C CB    . TYR A 1 75  ? -2.839  -0.140  -11.906 1.00 28.14  ? 123 TYR A CB    1 
ATOM   598  C CG    . TYR A 1 75  ? -1.777  0.243   -10.874 1.00 34.38  ? 123 TYR A CG    1 
ATOM   599  C CD1   . TYR A 1 75  ? -0.433  0.320   -11.215 1.00 35.11  ? 123 TYR A CD1   1 
ATOM   600  C CD2   . TYR A 1 75  ? -2.130  0.510   -9.561  1.00 35.60  ? 123 TYR A CD2   1 
ATOM   601  C CE1   . TYR A 1 75  ? 0.544   0.662   -10.264 1.00 34.15  ? 123 TYR A CE1   1 
ATOM   602  C CE2   . TYR A 1 75  ? -1.198  0.850   -8.623  1.00 35.14  ? 123 TYR A CE2   1 
ATOM   603  C CZ    . TYR A 1 75  ? 0.150   0.929   -8.970  1.00 41.39  ? 123 TYR A CZ    1 
ATOM   604  O OH    . TYR A 1 75  ? 1.073   1.277   -8.000  1.00 37.29  ? 123 TYR A OH    1 
ATOM   605  N N     . GLY A 1 76  ? -2.745  -2.816  -9.960  1.00 31.89  ? 124 GLY A N     1 
ATOM   606  C CA    . GLY A 1 76  ? -3.174  -3.420  -8.715  1.00 32.25  ? 124 GLY A CA    1 
ATOM   607  C C     . GLY A 1 76  ? -3.730  -4.824  -8.828  1.00 34.23  ? 124 GLY A C     1 
ATOM   608  O O     . GLY A 1 76  ? -4.081  -5.416  -7.798  1.00 37.66  ? 124 GLY A O     1 
ATOM   609  N N     . ALA A 1 77  ? -3.814  -5.387  -10.029 1.00 30.94  ? 125 ALA A N     1 
ATOM   610  C CA    . ALA A 1 77  ? -4.327  -6.738  -10.149 1.00 30.05  ? 125 ALA A CA    1 
ATOM   611  C C     . ALA A 1 77  ? -3.440  -7.684  -9.367  1.00 40.91  ? 125 ALA A C     1 
ATOM   612  O O     . ALA A 1 77  ? -2.208  -7.564  -9.375  1.00 39.49  ? 125 ALA A O     1 
ATOM   613  C CB    . ALA A 1 77  ? -4.404  -7.180  -11.608 1.00 34.84  ? 125 ALA A CB    1 
ATOM   614  N N     . ASN A 1 78  ? -4.078  -8.632  -8.695  1.00 38.90  ? 126 ASN A N     1 
ATOM   615  C CA    . ASN A 1 78  ? -3.386  -9.564  -7.829  1.00 38.04  ? 126 ASN A CA    1 
ATOM   616  C C     . ASN A 1 78  ? -2.959  -10.781 -8.642  1.00 43.33  ? 126 ASN A C     1 
ATOM   617  O O     . ASN A 1 78  ? -3.805  -11.576 -9.078  1.00 40.59  ? 126 ASN A O     1 
ATOM   618  C CB    . ASN A 1 78  ? -4.287  -9.951  -6.669  1.00 42.45  ? 126 ASN A CB    1 
ATOM   619  C CG    . ASN A 1 78  ? -3.502  -10.377 -5.466  1.00 52.45  ? 126 ASN A CG    1 
ATOM   620  O OD1   . ASN A 1 78  ? -3.139  -9.550  -4.621  1.00 58.45  ? 126 ASN A OD1   1 
ATOM   621  N ND2   . ASN A 1 78  ? -3.211  -11.672 -5.382  1.00 47.26  ? 126 ASN A ND2   1 
ATOM   622  N N     . LYS A 1 79  ? -1.644  -10.921 -8.858  1.00 38.12  ? 127 LYS A N     1 
ATOM   623  C CA    . LYS A 1 79  ? -1.097  -12.087 -9.537  1.00 35.57  ? 127 LYS A CA    1 
ATOM   624  C C     . LYS A 1 79  ? 0.260   -12.449 -8.938  1.00 35.24  ? 127 LYS A C     1 
ATOM   625  O O     . LYS A 1 79  ? 1.115   -11.576 -8.742  1.00 35.41  ? 127 LYS A O     1 
ATOM   626  C CB    . LYS A 1 79  ? -0.979  -11.838 -11.050 1.00 34.78  ? 127 LYS A CB    1 
ATOM   627  C CG    . LYS A 1 79  ? -0.523  -13.084 -11.811 1.00 36.27  ? 127 LYS A CG    1 
ATOM   628  C CD    . LYS A 1 79  ? -0.716  -12.957 -13.312 1.00 33.54  ? 127 LYS A CD    1 
ATOM   629  C CE    . LYS A 1 79  ? -0.330  -14.246 -13.991 1.00 36.96  ? 127 LYS A CE    1 
ATOM   630  N NZ    . LYS A 1 79  ? -0.627  -14.226 -15.443 1.00 38.89  ? 127 LYS A NZ    1 
ATOM   631  N N     . ASP A 1 80  ? 0.455   -13.736 -8.646  1.00 30.78  ? 128 ASP A N     1 
ATOM   632  C CA    . ASP A 1 80  ? 1.700   -14.169 -8.025  1.00 37.36  ? 128 ASP A CA    1 
ATOM   633  C C     . ASP A 1 80  ? 2.875   -13.889 -8.958  1.00 41.58  ? 128 ASP A C     1 
ATOM   634  O O     . ASP A 1 80  ? 2.895   -14.360 -10.102 1.00 37.03  ? 128 ASP A O     1 
ATOM   635  C CB    . ASP A 1 80  ? 1.650   -15.656 -7.690  1.00 34.06  ? 128 ASP A CB    1 
ATOM   636  C CG    . ASP A 1 80  ? 3.014   -16.188 -7.240  1.00 45.67  ? 128 ASP A CG    1 
ATOM   637  O OD1   . ASP A 1 80  ? 3.578   -15.626 -6.263  1.00 45.00  ? 128 ASP A OD1   1 
ATOM   638  O OD2   . ASP A 1 80  ? 3.525   -17.153 -7.863  1.00 40.65  ? 128 ASP A OD2   1 
ATOM   639  N N     . GLY A 1 81  ? 3.859   -13.139 -8.463  1.00 35.89  ? 129 GLY A N     1 
ATOM   640  C CA    . GLY A 1 81  ? 5.000   -12.746 -9.264  1.00 37.02  ? 129 GLY A CA    1 
ATOM   641  C C     . GLY A 1 81  ? 4.903   -11.346 -9.822  1.00 35.93  ? 129 GLY A C     1 
ATOM   642  O O     . GLY A 1 81  ? 5.799   -10.925 -10.567 1.00 34.39  ? 129 GLY A O     1 
ATOM   643  N N     . ILE A 1 82  ? 3.834   -10.627 -9.495  1.00 34.78  ? 130 ILE A N     1 
ATOM   644  C CA    . ILE A 1 82  ? 3.547   -9.301  -10.022 1.00 34.75  ? 130 ILE A CA    1 
ATOM   645  C C     . ILE A 1 82  ? 3.343   -8.360  -8.841  1.00 34.65  ? 130 ILE A C     1 
ATOM   646  O O     . ILE A 1 82  ? 2.526   -8.628  -7.955  1.00 35.10  ? 130 ILE A O     1 
ATOM   647  C CB    . ILE A 1 82  ? 2.305   -9.307  -10.937 1.00 30.64  ? 130 ILE A CB    1 
ATOM   648  C CG1   . ILE A 1 82  ? 2.413   -10.369 -12.038 1.00 35.10  ? 130 ILE A CG1   1 
ATOM   649  C CG2   . ILE A 1 82  ? 2.043   -7.926  -11.503 1.00 27.62  ? 130 ILE A CG2   1 
ATOM   650  C CD1   . ILE A 1 82  ? 3.591   -10.227 -12.966 1.00 33.95  ? 130 ILE A CD1   1 
ATOM   651  N N     . ILE A 1 83  ? 4.080   -7.262  -8.822  1.00 33.11  ? 131 ILE A N     1 
ATOM   652  C CA    . ILE A 1 83  ? 3.888   -6.266  -7.785  1.00 33.03  ? 131 ILE A CA    1 
ATOM   653  C C     . ILE A 1 83  ? 3.858   -4.927  -8.494  1.00 31.42  ? 131 ILE A C     1 
ATOM   654  O O     . ILE A 1 83  ? 4.433   -4.778  -9.574  1.00 33.60  ? 131 ILE A O     1 
ATOM   655  C CB    . ILE A 1 83  ? 4.977   -6.365  -6.683  1.00 38.45  ? 131 ILE A CB    1 
ATOM   656  C CG1   . ILE A 1 83  ? 6.383   -6.075  -7.227  1.00 33.44  ? 131 ILE A CG1   1 
ATOM   657  C CG2   . ILE A 1 83  ? 4.973   -7.771  -6.068  1.00 34.14  ? 131 ILE A CG2   1 
ATOM   658  C CD1   . ILE A 1 83  ? 6.752   -4.631  -7.161  1.00 30.04  ? 131 ILE A CD1   1 
ATOM   659  N N     . TRP A 1 84  ? 3.162   -3.956  -7.904  1.00 31.10  ? 132 TRP A N     1 
ATOM   660  C CA    . TRP A 1 84  ? 2.791   -2.725  -8.596  1.00 30.15  ? 132 TRP A CA    1 
ATOM   661  C C     . TRP A 1 84  ? 3.469   -1.531  -7.943  1.00 29.75  ? 132 TRP A C     1 
ATOM   662  O O     . TRP A 1 84  ? 3.603   -1.480  -6.716  1.00 37.43  ? 132 TRP A O     1 
ATOM   663  C CB    . TRP A 1 84  ? 1.234   -2.525  -8.596  1.00 29.10  ? 132 TRP A CB    1 
ATOM   664  C CG    . TRP A 1 84  ? 0.525   -3.629  -9.346  1.00 27.18  ? 132 TRP A CG    1 
ATOM   665  C CD1   . TRP A 1 84  ? -0.004  -4.771  -8.820  1.00 29.80  ? 132 TRP A CD1   1 
ATOM   666  C CD2   . TRP A 1 84  ? 0.329   -3.713  -10.767 1.00 25.32  ? 132 TRP A CD2   1 
ATOM   667  N NE1   . TRP A 1 84  ? -0.544  -5.549  -9.823  1.00 31.50  ? 132 TRP A NE1   1 
ATOM   668  C CE2   . TRP A 1 84  ? -0.343  -4.917  -11.027 1.00 29.34  ? 132 TRP A CE2   1 
ATOM   669  C CE3   . TRP A 1 84  ? 0.644   -2.875  -11.837 1.00 25.71  ? 132 TRP A CE3   1 
ATOM   670  C CZ2   . TRP A 1 84  ? -0.693  -5.307  -12.313 1.00 28.35  ? 132 TRP A CZ2   1 
ATOM   671  C CZ3   . TRP A 1 84  ? 0.291   -3.258  -13.108 1.00 28.47  ? 132 TRP A CZ3   1 
ATOM   672  C CH2   . TRP A 1 84  ? -0.360  -4.468  -13.341 1.00 28.09  ? 132 TRP A CH2   1 
ATOM   673  N N     . VAL A 1 85  ? 3.870   -0.556  -8.760  1.00 30.12  ? 133 VAL A N     1 
ATOM   674  C CA    . VAL A 1 85  ? 4.565   0.636   -8.287  1.00 34.33  ? 133 VAL A CA    1 
ATOM   675  C C     . VAL A 1 85  ? 4.092   1.828   -9.098  1.00 30.99  ? 133 VAL A C     1 
ATOM   676  O O     . VAL A 1 85  ? 3.864   1.714   -10.304 1.00 36.61  ? 133 VAL A O     1 
ATOM   677  C CB    . VAL A 1 85  ? 6.105   0.502   -8.392  1.00 35.51  ? 133 VAL A CB    1 
ATOM   678  C CG1   . VAL A 1 85  ? 6.623   -0.531  -7.423  1.00 33.53  ? 133 VAL A CG1   1 
ATOM   679  C CG2   . VAL A 1 85  ? 6.544   0.149   -9.824  1.00 31.49  ? 133 VAL A CG2   1 
ATOM   680  N N     . ALA A 1 86  ? 3.968   2.979   -8.450  1.00 30.33  ? 134 ALA A N     1 
ATOM   681  C CA    . ALA A 1 86  ? 3.567   4.190   -9.149  1.00 36.54  ? 134 ALA A CA    1 
ATOM   682  C C     . ALA A 1 86  ? 4.073   5.411   -8.398  1.00 39.54  ? 134 ALA A C     1 
ATOM   683  O O     . ALA A 1 86  ? 4.035   5.446   -7.165  1.00 44.45  ? 134 ALA A O     1 
ATOM   684  C CB    . ALA A 1 86  ? 2.042   4.276   -9.299  1.00 30.80  ? 134 ALA A CB    1 
ATOM   685  N N     . THR A 1 87  ? 4.546   6.401   -9.154  1.00 35.79  ? 135 THR A N     1 
ATOM   686  C CA    . THR A 1 87  ? 4.790   7.726   -8.614  1.00 39.16  ? 135 THR A CA    1 
ATOM   687  C C     . THR A 1 87  ? 3.473   8.475   -8.495  1.00 45.47  ? 135 THR A C     1 
ATOM   688  O O     . THR A 1 87  ? 2.590   8.339   -9.345  1.00 51.91  ? 135 THR A O     1 
ATOM   689  C CB    . THR A 1 87  ? 5.749   8.504   -9.510  1.00 39.41  ? 135 THR A CB    1 
ATOM   690  O OG1   . THR A 1 87  ? 6.962   7.762   -9.677  1.00 40.49  ? 135 THR A OG1   1 
ATOM   691  C CG2   . THR A 1 87  ? 6.080   9.835   -8.897  1.00 45.73  ? 135 THR A CG2   1 
ATOM   692  N N     . GLU A 1 88  ? 3.331   9.250   -7.422  1.00 53.60  ? 136 GLU A N     1 
ATOM   693  C CA    . GLU A 1 88  ? 2.143   10.076  -7.255  1.00 51.30  ? 136 GLU A CA    1 
ATOM   694  C C     . GLU A 1 88  ? 1.969   10.985  -8.464  1.00 51.72  ? 136 GLU A C     1 
ATOM   695  O O     . GLU A 1 88  ? 2.934   11.578  -8.964  1.00 52.12  ? 136 GLU A O     1 
ATOM   696  C CB    . GLU A 1 88  ? 2.246   10.915  -5.980  1.00 56.97  ? 136 GLU A CB    1 
ATOM   697  C CG    . GLU A 1 88  ? 0.981   10.906  -5.118  1.00 71.54  ? 136 GLU A CG    1 
ATOM   698  C CD    . GLU A 1 88  ? 0.847   9.647   -4.249  1.00 79.51  ? 136 GLU A CD    1 
ATOM   699  O OE1   . GLU A 1 88  ? 1.808   8.842   -4.181  1.00 71.72  ? 136 GLU A OE1   1 
ATOM   700  O OE2   . GLU A 1 88  ? -0.228  9.467   -3.627  1.00 87.26  ? 136 GLU A OE2   1 
ATOM   701  N N     . GLY A 1 89  ? 0.730   11.073  -8.948  1.00 48.62  ? 137 GLY A N     1 
ATOM   702  C CA    . GLY A 1 89  ? 0.425   11.854  -10.123 1.00 41.91  ? 137 GLY A CA    1 
ATOM   703  C C     . GLY A 1 89  ? 0.625   11.140  -11.443 1.00 44.28  ? 137 GLY A C     1 
ATOM   704  O O     . GLY A 1 89  ? 0.403   11.748  -12.503 1.00 38.89  ? 137 GLY A O     1 
ATOM   705  N N     . ALA A 1 90  ? 1.047   9.881   -11.428 1.00 41.62  ? 138 ALA A N     1 
ATOM   706  C CA    . ALA A 1 90  ? 1.078   9.130   -12.673 1.00 41.58  ? 138 ALA A CA    1 
ATOM   707  C C     . ALA A 1 90  ? -0.348  8.780   -13.109 1.00 42.56  ? 138 ALA A C     1 
ATOM   708  O O     . ALA A 1 90  ? -1.207  8.447   -12.281 1.00 35.72  ? 138 ALA A O     1 
ATOM   709  C CB    . ALA A 1 90  ? 1.924   7.875   -12.513 1.00 35.26  ? 138 ALA A CB    1 
ATOM   710  N N     . LEU A 1 91  ? -0.592  8.894   -14.418 1.00 43.69  ? 139 LEU A N     1 
ATOM   711  C CA    . LEU A 1 91  ? -1.871  8.526   -15.014 1.00 41.01  ? 139 LEU A CA    1 
ATOM   712  C C     . LEU A 1 91  ? -2.018  7.017   -15.091 1.00 44.79  ? 139 LEU A C     1 
ATOM   713  O O     . LEU A 1 91  ? -1.053  6.305   -15.383 1.00 39.99  ? 139 LEU A O     1 
ATOM   714  C CB    . LEU A 1 91  ? -1.994  9.085   -16.420 1.00 36.58  ? 139 LEU A CB    1 
ATOM   715  C CG    . LEU A 1 91  ? -2.146  10.572  -16.672 1.00 43.38  ? 139 LEU A CG    1 
ATOM   716  C CD1   . LEU A 1 91  ? -2.558  10.737  -18.150 1.00 48.46  ? 139 LEU A CD1   1 
ATOM   717  C CD2   . LEU A 1 91  ? -3.158  11.212  -15.738 1.00 47.77  ? 139 LEU A CD2   1 
ATOM   718  N N     . ASN A 1 92  ? -3.248  6.542   -14.867 1.00 37.35  ? 140 ASN A N     1 
ATOM   719  C CA    . ASN A 1 92  ? -3.596  5.120   -14.937 1.00 35.17  ? 140 ASN A CA    1 
ATOM   720  C C     . ASN A 1 92  ? -4.136  4.823   -16.338 1.00 38.67  ? 140 ASN A C     1 
ATOM   721  O O     . ASN A 1 92  ? -5.341  4.707   -16.573 1.00 37.10  ? 140 ASN A O     1 
ATOM   722  C CB    . ASN A 1 92  ? -4.607  4.778   -13.844 1.00 37.05  ? 140 ASN A CB    1 
ATOM   723  C CG    . ASN A 1 92  ? -4.838  3.277   -13.665 1.00 36.60  ? 140 ASN A CG    1 
ATOM   724  O OD1   . ASN A 1 92  ? -4.730  2.495   -14.611 1.00 35.32  ? 140 ASN A OD1   1 
ATOM   725  N ND2   . ASN A 1 92  ? -5.170  2.871   -12.432 1.00 32.01  ? 140 ASN A ND2   1 
ATOM   726  N N     . THR A 1 93  ? -3.208  4.753   -17.290 1.00 39.91  ? 141 THR A N     1 
ATOM   727  C CA    . THR A 1 93  ? -3.476  4.498   -18.702 1.00 35.98  ? 141 THR A CA    1 
ATOM   728  C C     . THR A 1 93  ? -2.335  3.656   -19.256 1.00 36.02  ? 141 THR A C     1 
ATOM   729  O O     . THR A 1 93  ? -1.216  3.738   -18.743 1.00 32.58  ? 141 THR A O     1 
ATOM   730  C CB    . THR A 1 93  ? -3.587  5.811   -19.497 1.00 36.95  ? 141 THR A CB    1 
ATOM   731  O OG1   . THR A 1 93  ? -2.395  6.576   -19.306 1.00 41.04  ? 141 THR A OG1   1 
ATOM   732  C CG2   . THR A 1 93  ? -4.743  6.648   -19.018 1.00 35.73  ? 141 THR A CG2   1 
ATOM   733  N N     . PRO A 1 94  ? -2.586  2.825   -20.283 1.00 36.91  ? 142 PRO A N     1 
ATOM   734  C CA    . PRO A 1 94  ? -1.501  2.018   -20.878 1.00 33.19  ? 142 PRO A CA    1 
ATOM   735  C C     . PRO A 1 94  ? -0.435  2.875   -21.536 1.00 36.47  ? 142 PRO A C     1 
ATOM   736  O O     . PRO A 1 94  ? -0.748  3.856   -22.214 1.00 36.54  ? 142 PRO A O     1 
ATOM   737  C CB    . PRO A 1 94  ? -2.225  1.163   -21.927 1.00 30.29  ? 142 PRO A CB    1 
ATOM   738  C CG    . PRO A 1 94  ? -3.492  1.902   -22.239 1.00 29.15  ? 142 PRO A CG    1 
ATOM   739  C CD    . PRO A 1 94  ? -3.892  2.527   -20.909 1.00 36.53  ? 142 PRO A CD    1 
ATOM   740  N N     . LYS A 1 95  ? 0.833   2.487   -21.353 1.00 33.85  ? 143 LYS A N     1 
ATOM   741  C CA    . LYS A 1 95  ? 1.968   3.234   -21.921 1.00 34.38  ? 143 LYS A CA    1 
ATOM   742  C C     . LYS A 1 95  ? 2.484   2.598   -23.216 1.00 37.19  ? 143 LYS A C     1 
ATOM   743  O O     . LYS A 1 95  ? 3.671   2.265   -23.360 1.00 33.37  ? 143 LYS A O     1 
ATOM   744  C CB    . LYS A 1 95  ? 3.092   3.350   -20.895 1.00 33.43  ? 143 LYS A CB    1 
ATOM   745  C CG    . LYS A 1 95  ? 2.667   3.870   -19.516 1.00 39.06  ? 143 LYS A CG    1 
ATOM   746  C CD    . LYS A 1 95  ? 1.918   5.197   -19.571 1.00 38.15  ? 143 LYS A CD    1 
ATOM   747  C CE    . LYS A 1 95  ? 1.231   5.499   -18.222 1.00 39.29  ? 143 LYS A CE    1 
ATOM   748  N NZ    . LYS A 1 95  ? 0.450   6.795   -18.182 1.00 37.71  ? 143 LYS A NZ    1 
ATOM   749  N N     . ASP A 1 96  ? 1.604   2.455   -24.206 1.00 33.11  ? 144 ASP A N     1 
ATOM   750  C CA    . ASP A 1 96  ? 2.017   1.751   -25.417 1.00 36.36  ? 144 ASP A CA    1 
ATOM   751  C C     . ASP A 1 96  ? 2.960   2.578   -26.285 1.00 40.08  ? 144 ASP A C     1 
ATOM   752  O O     . ASP A 1 96  ? 3.627   2.019   -27.152 1.00 43.55  ? 144 ASP A O     1 
ATOM   753  C CB    . ASP A 1 96  ? 0.798   1.305   -26.225 1.00 36.18  ? 144 ASP A CB    1 
ATOM   754  C CG    . ASP A 1 96  ? -0.245  2.383   -26.357 1.00 47.10  ? 144 ASP A CG    1 
ATOM   755  O OD1   . ASP A 1 96  ? 0.106   3.588   -26.292 1.00 50.71  ? 144 ASP A OD1   1 
ATOM   756  O OD2   . ASP A 1 96  ? -1.431  2.025   -26.519 1.00 54.78  ? 144 ASP A OD2   1 
ATOM   757  N N     . HIS A 1 97  ? 3.035   3.889   -26.074 1.00 38.25  ? 145 HIS A N     1 
ATOM   758  C CA    . HIS A 1 97  ? 4.012   4.703   -26.772 1.00 36.21  ? 145 HIS A CA    1 
ATOM   759  C C     . HIS A 1 97  ? 5.442   4.486   -26.270 1.00 41.61  ? 145 HIS A C     1 
ATOM   760  O O     . HIS A 1 97  ? 6.385   4.932   -26.932 1.00 34.55  ? 145 HIS A O     1 
ATOM   761  C CB    . HIS A 1 97  ? 3.645   6.171   -26.629 1.00 37.30  ? 145 HIS A CB    1 
ATOM   762  C CG    . HIS A 1 97  ? 3.664   6.654   -25.218 1.00 38.34  ? 145 HIS A CG    1 
ATOM   763  N ND1   . HIS A 1 97  ? 2.753   6.232   -24.275 1.00 37.67  ? 145 HIS A ND1   1 
ATOM   764  C CD2   . HIS A 1 97  ? 4.491   7.519   -24.584 1.00 40.30  ? 145 HIS A CD2   1 
ATOM   765  C CE1   . HIS A 1 97  ? 3.011   6.826   -23.125 1.00 39.34  ? 145 HIS A CE1   1 
ATOM   766  N NE2   . HIS A 1 97  ? 4.057   7.614   -23.287 1.00 40.31  ? 145 HIS A NE2   1 
ATOM   767  N N     . ILE A 1 98  ? 5.626   3.844   -25.118 1.00 37.95  ? 146 ILE A N     1 
ATOM   768  C CA    . ILE A 1 98  ? 6.945   3.438   -24.654 1.00 31.82  ? 146 ILE A CA    1 
ATOM   769  C C     . ILE A 1 98  ? 7.215   1.980   -24.985 1.00 37.35  ? 146 ILE A C     1 
ATOM   770  O O     . ILE A 1 98  ? 8.326   1.619   -25.375 1.00 33.75  ? 146 ILE A O     1 
ATOM   771  C CB    . ILE A 1 98  ? 7.093   3.710   -23.139 1.00 31.86  ? 146 ILE A CB    1 
ATOM   772  C CG1   . ILE A 1 98  ? 6.980   5.206   -22.860 1.00 31.39  ? 146 ILE A CG1   1 
ATOM   773  C CG2   . ILE A 1 98  ? 8.432   3.176   -22.616 1.00 32.59  ? 146 ILE A CG2   1 
ATOM   774  C CD1   . ILE A 1 98  ? 6.843   5.583   -21.410 1.00 36.84  ? 146 ILE A CD1   1 
ATOM   775  N N     . GLY A 1 99  ? 6.205   1.129   -24.841 1.00 36.92  ? 147 GLY A N     1 
ATOM   776  C CA    . GLY A 1 99  ? 6.418   -0.250  -25.204 1.00 35.40  ? 147 GLY A CA    1 
ATOM   777  C C     . GLY A 1 99  ? 7.506   -0.934  -24.385 1.00 29.96  ? 147 GLY A C     1 
ATOM   778  O O     . GLY A 1 99  ? 7.895   -0.506  -23.290 1.00 27.97  ? 147 GLY A O     1 
ATOM   779  N N     . THR A 1 100 ? 7.953   -2.051  -24.939 1.00 28.84  ? 148 THR A N     1 
ATOM   780  C CA    . THR A 1 100 ? 9.016   -2.885  -24.416 1.00 29.91  ? 148 THR A CA    1 
ATOM   781  C C     . THR A 1 100 ? 10.274  -2.686  -25.269 1.00 33.82  ? 148 THR A C     1 
ATOM   782  O O     . THR A 1 100 ? 10.259  -2.003  -26.299 1.00 26.48  ? 148 THR A O     1 
ATOM   783  C CB    . THR A 1 100 ? 8.588   -4.346  -24.424 1.00 25.46  ? 148 THR A CB    1 
ATOM   784  O OG1   . THR A 1 100 ? 8.013   -4.638  -25.693 1.00 26.22  ? 148 THR A OG1   1 
ATOM   785  C CG2   . THR A 1 100 ? 7.571   -4.617  -23.337 1.00 28.23  ? 148 THR A CG2   1 
ATOM   786  N N     . ARG A 1 101 ? 11.361  -3.326  -24.854 1.00 35.35  ? 149 ARG A N     1 
ATOM   787  C CA    . ARG A 1 101 ? 12.670  -3.133  -25.467 1.00 30.93  ? 149 ARG A CA    1 
ATOM   788  C C     . ARG A 1 101 ? 12.957  -4.279  -26.420 1.00 31.04  ? 149 ARG A C     1 
ATOM   789  O O     . ARG A 1 101 ? 12.674  -5.433  -26.106 1.00 35.18  ? 149 ARG A O     1 
ATOM   790  C CB    . ARG A 1 101 ? 13.743  -3.041  -24.377 1.00 31.70  ? 149 ARG A CB    1 
ATOM   791  C CG    . ARG A 1 101 ? 15.204  -3.097  -24.861 1.00 28.29  ? 149 ARG A CG    1 
ATOM   792  C CD    . ARG A 1 101 ? 16.149  -2.818  -23.681 1.00 30.29  ? 149 ARG A CD    1 
ATOM   793  N NE    . ARG A 1 101 ? 16.300  -3.958  -22.782 1.00 27.54  ? 149 ARG A NE    1 
ATOM   794  C CZ    . ARG A 1 101 ? 17.128  -4.968  -23.009 1.00 33.28  ? 149 ARG A CZ    1 
ATOM   795  N NH1   . ARG A 1 101 ? 17.921  -4.984  -24.068 1.00 32.84  ? 149 ARG A NH1   1 
ATOM   796  N NH2   . ARG A 1 101 ? 17.144  -5.997  -22.170 1.00 34.50  ? 149 ARG A NH2   1 
ATOM   797  N N     . ASN A 1 102 ? 13.490  -3.969  -27.600 1.00 33.10  ? 150 ASN A N     1 
ATOM   798  C CA    . ASN A 1 102 ? 14.058  -5.055  -28.396 1.00 42.47  ? 150 ASN A CA    1 
ATOM   799  C C     . ASN A 1 102 ? 15.561  -5.155  -28.141 1.00 43.24  ? 150 ASN A C     1 
ATOM   800  O O     . ASN A 1 102 ? 16.302  -4.227  -28.498 1.00 43.83  ? 150 ASN A O     1 
ATOM   801  C CB    . ASN A 1 102 ? 13.789  -4.866  -29.886 1.00 44.27  ? 150 ASN A CB    1 
ATOM   802  C CG    . ASN A 1 102 ? 14.257  -6.070  -30.720 1.00 47.01  ? 150 ASN A CG    1 
ATOM   803  O OD1   . ASN A 1 102 ? 15.138  -6.825  -30.312 1.00 47.98  ? 150 ASN A OD1   1 
ATOM   804  N ND2   . ASN A 1 102 ? 13.663  -6.245  -31.887 1.00 53.49  ? 150 ASN A ND2   1 
ATOM   805  N N     . PRO A 1 103 ? 16.057  -6.253  -27.564 1.00 39.77  ? 151 PRO A N     1 
ATOM   806  C CA    . PRO A 1 103 ? 17.506  -6.355  -27.313 1.00 44.65  ? 151 PRO A CA    1 
ATOM   807  C C     . PRO A 1 103 ? 18.351  -6.208  -28.574 1.00 49.01  ? 151 PRO A C     1 
ATOM   808  O O     . PRO A 1 103 ? 19.464  -5.674  -28.503 1.00 53.83  ? 151 PRO A O     1 
ATOM   809  C CB    . PRO A 1 103 ? 17.658  -7.750  -26.688 1.00 43.42  ? 151 PRO A CB    1 
ATOM   810  C CG    . PRO A 1 103 ? 16.307  -8.089  -26.148 1.00 44.80  ? 151 PRO A CG    1 
ATOM   811  C CD    . PRO A 1 103 ? 15.318  -7.429  -27.072 1.00 44.70  ? 151 PRO A CD    1 
ATOM   812  N N     . ALA A 1 104 ? 17.854  -6.627  -29.724 1.00 46.67  ? 152 ALA A N     1 
ATOM   813  C CA    . ALA A 1 104 ? 18.610  -6.431  -30.954 1.00 43.74  ? 152 ALA A CA    1 
ATOM   814  C C     . ALA A 1 104 ? 18.667  -5.003  -31.383 1.00 50.05  ? 152 ALA A C     1 
ATOM   815  O O     . ALA A 1 104 ? 19.107  -4.806  -32.514 1.00 51.17  ? 152 ALA A O     1 
ATOM   816  C CB    . ALA A 1 104 ? 18.009  -7.269  -32.083 1.00 42.92  ? 152 ALA A CB    1 
ATOM   817  N N     . ASN A 1 105 ? 18.204  -4.025  -30.599 1.00 47.73  ? 153 ASN A N     1 
ATOM   818  C CA    . ASN A 1 105 ? 18.306  -2.617  -30.975 1.00 44.41  ? 153 ASN A CA    1 
ATOM   819  C C     . ASN A 1 105 ? 18.774  -1.760  -29.810 1.00 48.71  ? 153 ASN A C     1 
ATOM   820  O O     . ASN A 1 105 ? 19.313  -0.671  -30.017 1.00 56.60  ? 153 ASN A O     1 
ATOM   821  C CB    . ASN A 1 105 ? 16.957  -2.076  -31.470 1.00 43.92  ? 153 ASN A CB    1 
ATOM   822  C CG    . ASN A 1 105 ? 16.410  -2.853  -32.644 1.00 52.77  ? 153 ASN A CG    1 
ATOM   823  O OD1   . ASN A 1 105 ? 17.140  -3.209  -33.573 1.00 55.87  ? 153 ASN A OD1   1 
ATOM   824  N ND2   . ASN A 1 105 ? 15.116  -3.129  -32.609 1.00 59.68  ? 153 ASN A ND2   1 
ATOM   825  N N     . ASN A 1 106 ? 18.513  -2.199  -28.581 1.00 45.80  ? 154 ASN A N     1 
ATOM   826  C CA    . ASN A 1 106 ? 18.797  -1.376  -27.415 1.00 40.30  ? 154 ASN A CA    1 
ATOM   827  C C     . ASN A 1 106 ? 19.163  -2.274  -26.256 1.00 40.74  ? 154 ASN A C     1 
ATOM   828  O O     . ASN A 1 106 ? 18.445  -3.238  -25.966 1.00 37.66  ? 154 ASN A O     1 
ATOM   829  C CB    . ASN A 1 106 ? 17.605  -0.515  -27.006 1.00 39.33  ? 154 ASN A CB    1 
ATOM   830  C CG    . ASN A 1 106 ? 17.283  0.539   -28.011 1.00 42.34  ? 154 ASN A CG    1 
ATOM   831  O OD1   . ASN A 1 106 ? 16.479  0.324   -28.914 1.00 45.33  ? 154 ASN A OD1   1 
ATOM   832  N ND2   . ASN A 1 106 ? 17.892  1.702   -27.857 1.00 46.15  ? 154 ASN A ND2   1 
ATOM   833  N N     . ALA A 1 107 ? 20.268  -1.945  -25.597 1.00 38.39  ? 155 ALA A N     1 
ATOM   834  C CA    . ALA A 1 107 ? 20.563  -2.596  -24.335 1.00 42.29  ? 155 ALA A CA    1 
ATOM   835  C C     . ALA A 1 107 ? 19.676  -2.012  -23.248 1.00 33.65  ? 155 ALA A C     1 
ATOM   836  O O     . ALA A 1 107 ? 19.126  -0.921  -23.385 1.00 34.86  ? 155 ALA A O     1 
ATOM   837  C CB    . ALA A 1 107 ? 22.033  -2.428  -23.946 1.00 29.34  ? 155 ALA A CB    1 
ATOM   838  N N     . ALA A 1 108 ? 19.579  -2.743  -22.145 1.00 33.18  ? 156 ALA A N     1 
ATOM   839  C CA    . ALA A 1 108 ? 18.808  -2.279  -21.008 1.00 34.38  ? 156 ALA A CA    1 
ATOM   840  C C     . ALA A 1 108 ? 19.359  -0.961  -20.479 1.00 35.43  ? 156 ALA A C     1 
ATOM   841  O O     . ALA A 1 108 ? 20.565  -0.704  -20.522 1.00 33.54  ? 156 ALA A O     1 
ATOM   842  C CB    . ALA A 1 108 ? 18.832  -3.337  -19.917 1.00 35.23  ? 156 ALA A CB    1 
ATOM   843  N N     . ILE A 1 109 ? 18.457  -0.102  -20.019 1.00 32.75  ? 157 ILE A N     1 
ATOM   844  C CA    . ILE A 1 109 ? 18.842  1.043   -19.208 1.00 31.70  ? 157 ILE A CA    1 
ATOM   845  C C     . ILE A 1 109 ? 19.243  0.519   -17.846 1.00 30.20  ? 157 ILE A C     1 
ATOM   846  O O     . ILE A 1 109 ? 18.513  -0.286  -17.258 1.00 31.51  ? 157 ILE A O     1 
ATOM   847  C CB    . ILE A 1 109 ? 17.662  2.023   -19.081 1.00 33.49  ? 157 ILE A CB    1 
ATOM   848  C CG1   . ILE A 1 109 ? 17.230  2.570   -20.434 1.00 35.36  ? 157 ILE A CG1   1 
ATOM   849  C CG2   . ILE A 1 109 ? 17.981  3.178   -18.138 1.00 32.05  ? 157 ILE A CG2   1 
ATOM   850  C CD1   . ILE A 1 109 ? 15.779  3.022   -20.416 1.00 32.65  ? 157 ILE A CD1   1 
ATOM   851  N N     . VAL A 1 110 ? 20.396  0.966   -17.328 1.00 33.52  ? 158 VAL A N     1 
ATOM   852  C CA    . VAL A 1 110 ? 20.769  0.604   -15.957 1.00 27.83  ? 158 VAL A CA    1 
ATOM   853  C C     . VAL A 1 110 ? 19.691  1.086   -14.995 1.00 32.33  ? 158 VAL A C     1 
ATOM   854  O O     . VAL A 1 110 ? 19.303  2.264   -14.994 1.00 30.52  ? 158 VAL A O     1 
ATOM   855  C CB    . VAL A 1 110 ? 22.143  1.182   -15.581 1.00 32.47  ? 158 VAL A CB    1 
ATOM   856  C CG1   . VAL A 1 110 ? 22.505  0.787   -14.166 1.00 33.48  ? 158 VAL A CG1   1 
ATOM   857  C CG2   . VAL A 1 110 ? 23.221  0.675   -16.525 1.00 34.54  ? 158 VAL A CG2   1 
ATOM   858  N N     . LEU A 1 111 ? 19.191  0.174   -14.173 1.00 33.18  ? 159 LEU A N     1 
ATOM   859  C CA    . LEU A 1 111 ? 18.084  0.515   -13.290 1.00 33.53  ? 159 LEU A CA    1 
ATOM   860  C C     . LEU A 1 111 ? 18.587  1.380   -12.142 1.00 40.90  ? 159 LEU A C     1 
ATOM   861  O O     . LEU A 1 111 ? 19.520  0.992   -11.427 1.00 41.46  ? 159 LEU A O     1 
ATOM   862  C CB    . LEU A 1 111 ? 17.410  -0.751  -12.751 1.00 33.05  ? 159 LEU A CB    1 
ATOM   863  C CG    . LEU A 1 111 ? 16.142  -0.515  -11.908 1.00 39.30  ? 159 LEU A CG    1 
ATOM   864  C CD1   . LEU A 1 111 ? 15.137  -1.609  -12.106 1.00 37.93  ? 159 LEU A CD1   1 
ATOM   865  C CD2   . LEU A 1 111 ? 16.480  -0.437  -10.442 1.00 42.98  ? 159 LEU A CD2   1 
ATOM   866  N N     . GLN A 1 112 ? 17.978  2.560   -11.973 1.00 39.59  ? 160 GLN A N     1 
ATOM   867  C CA    . GLN A 1 112 ? 18.191  3.368   -10.783 1.00 40.33  ? 160 GLN A CA    1 
ATOM   868  C C     . GLN A 1 112 ? 16.902  4.059   -10.365 1.00 43.51  ? 160 GLN A C     1 
ATOM   869  O O     . GLN A 1 112 ? 16.091  4.471   -11.200 1.00 38.58  ? 160 GLN A O     1 
ATOM   870  C CB    . GLN A 1 112 ? 19.294  4.392   -10.988 1.00 49.73  ? 160 GLN A CB    1 
ATOM   871  C CG    . GLN A 1 112 ? 19.007  5.470   -11.974 1.00 46.41  ? 160 GLN A CG    1 
ATOM   872  C CD    . GLN A 1 112 ? 19.981  6.617   -11.793 1.00 56.58  ? 160 GLN A CD    1 
ATOM   873  O OE1   . GLN A 1 112 ? 20.003  7.262   -10.737 1.00 57.53  ? 160 GLN A OE1   1 
ATOM   874  N NE2   . GLN A 1 112 ? 20.820  6.856   -12.803 1.00 53.30  ? 160 GLN A NE2   1 
ATOM   875  N N     . LEU A 1 113 ? 16.734  4.193   -9.047  1.00 43.16  ? 161 LEU A N     1 
ATOM   876  C CA    . LEU A 1 113 ? 15.536  4.692   -8.394  1.00 44.48  ? 161 LEU A CA    1 
ATOM   877  C C     . LEU A 1 113 ? 15.683  6.159   -8.016  1.00 46.44  ? 161 LEU A C     1 
ATOM   878  O O     . LEU A 1 113 ? 16.797  6.637   -7.770  1.00 52.56  ? 161 LEU A O     1 
ATOM   879  C CB    . LEU A 1 113 ? 15.235  3.869   -7.139  1.00 44.87  ? 161 LEU A CB    1 
ATOM   880  C CG    . LEU A 1 113 ? 15.062  2.382   -7.438  1.00 39.26  ? 161 LEU A CG    1 
ATOM   881  C CD1   . LEU A 1 113 ? 14.598  1.630   -6.222  1.00 44.35  ? 161 LEU A CD1   1 
ATOM   882  C CD2   . LEU A 1 113 ? 14.076  2.201   -8.552  1.00 42.95  ? 161 LEU A CD2   1 
ATOM   883  N N     . PRO A 1 114 ? 14.562  6.883   -7.972  1.00 51.42  ? 162 PRO A N     1 
ATOM   884  C CA    . PRO A 1 114 ? 14.602  8.291   -7.560  1.00 48.35  ? 162 PRO A CA    1 
ATOM   885  C C     . PRO A 1 114 ? 15.087  8.410   -6.125  1.00 52.72  ? 162 PRO A C     1 
ATOM   886  O O     . PRO A 1 114 ? 14.921  7.490   -5.319  1.00 53.28  ? 162 PRO A O     1 
ATOM   887  C CB    . PRO A 1 114 ? 13.142  8.745   -7.691  1.00 48.65  ? 162 PRO A CB    1 
ATOM   888  C CG    . PRO A 1 114 ? 12.451  7.703   -8.480  1.00 47.31  ? 162 PRO A CG    1 
ATOM   889  C CD    . PRO A 1 114 ? 13.186  6.424   -8.235  1.00 48.83  ? 162 PRO A CD    1 
ATOM   890  N N     . GLN A 1 115 ? 15.685  9.562   -5.812  1.00 56.09  ? 163 GLN A N     1 
ATOM   891  C CA    . GLN A 1 115 ? 16.363  9.752   -4.530  1.00 56.34  ? 163 GLN A CA    1 
ATOM   892  C C     . GLN A 1 115 ? 15.421  9.521   -3.348  1.00 55.04  ? 163 GLN A C     1 
ATOM   893  O O     . GLN A 1 115 ? 14.227  9.827   -3.401  1.00 54.59  ? 163 GLN A O     1 
ATOM   894  C CB    . GLN A 1 115 ? 16.961  11.158  -4.448  1.00 56.21  ? 163 GLN A CB    1 
ATOM   895  C CG    . GLN A 1 115 ? 17.450  11.548  -3.062  1.00 55.57  ? 163 GLN A CG    1 
ATOM   896  C CD    . GLN A 1 115 ? 16.951  12.918  -2.628  1.00 62.53  ? 163 GLN A CD    1 
ATOM   897  O OE1   . GLN A 1 115 ? 17.290  13.935  -3.242  1.00 67.77  ? 163 GLN A OE1   1 
ATOM   898  N NE2   . GLN A 1 115 ? 16.138  12.953  -1.567  1.00 58.50  ? 163 GLN A NE2   1 
ATOM   899  N N     . GLY A 1 116 ? 15.975  8.963   -2.274  1.00 49.58  ? 164 GLY A N     1 
ATOM   900  C CA    . GLY A 1 116 ? 15.203  8.713   -1.083  1.00 50.44  ? 164 GLY A CA    1 
ATOM   901  C C     . GLY A 1 116 ? 14.373  7.460   -1.147  1.00 56.50  ? 164 GLY A C     1 
ATOM   902  O O     . GLY A 1 116 ? 13.454  7.299   -0.339  1.00 61.05  ? 164 GLY A O     1 
ATOM   903  N N     . THR A 1 117 ? 14.674  6.556   -2.078  1.00 56.81  ? 165 THR A N     1 
ATOM   904  C CA    . THR A 1 117 ? 13.916  5.323   -2.226  1.00 55.60  ? 165 THR A CA    1 
ATOM   905  C C     . THR A 1 117 ? 14.490  4.206   -1.359  1.00 54.99  ? 165 THR A C     1 
ATOM   906  O O     . THR A 1 117 ? 15.704  3.989   -1.316  1.00 53.69  ? 165 THR A O     1 
ATOM   907  C CB    . THR A 1 117 ? 13.912  4.875   -3.679  1.00 47.98  ? 165 THR A CB    1 
ATOM   908  O OG1   . THR A 1 117 ? 13.516  5.970   -4.510  1.00 46.41  ? 165 THR A OG1   1 
ATOM   909  C CG2   . THR A 1 117 ? 12.958  3.714   -3.846  1.00 47.44  ? 165 THR A CG2   1 
ATOM   910  N N     . THR A 1 118 ? 13.606  3.477   -0.697  1.00 50.81  ? 166 THR A N     1 
ATOM   911  C CA    . THR A 1 118 ? 14.006  2.379   0.173   1.00 56.94  ? 166 THR A CA    1 
ATOM   912  C C     . THR A 1 118 ? 13.707  1.054   -0.529  1.00 58.34  ? 166 THR A C     1 
ATOM   913  O O     . THR A 1 118 ? 12.539  0.679   -0.692  1.00 56.88  ? 166 THR A O     1 
ATOM   914  C CB    . THR A 1 118 ? 13.286  2.462   1.520   1.00 57.07  ? 166 THR A CB    1 
ATOM   915  O OG1   . THR A 1 118 ? 13.513  3.747   2.121   1.00 58.29  ? 166 THR A OG1   1 
ATOM   916  C CG2   . THR A 1 118 ? 13.786  1.377   2.461   1.00 55.83  ? 166 THR A CG2   1 
ATOM   917  N N     . LEU A 1 119 ? 14.760  0.354   -0.947  1.00 53.31  ? 167 LEU A N     1 
ATOM   918  C CA    . LEU A 1 119 ? 14.602  -1.022  -1.389  1.00 50.93  ? 167 LEU A CA    1 
ATOM   919  C C     . LEU A 1 119 ? 14.372  -1.917  -0.176  1.00 53.45  ? 167 LEU A C     1 
ATOM   920  O O     . LEU A 1 119 ? 15.030  -1.741  0.853   1.00 51.55  ? 167 LEU A O     1 
ATOM   921  C CB    . LEU A 1 119 ? 15.830  -1.511  -2.139  1.00 42.96  ? 167 LEU A CB    1 
ATOM   922  C CG    . LEU A 1 119 ? 16.245  -0.765  -3.400  1.00 50.47  ? 167 LEU A CG    1 
ATOM   923  C CD1   . LEU A 1 119 ? 16.836  0.614   -3.088  1.00 52.88  ? 167 LEU A CD1   1 
ATOM   924  C CD2   . LEU A 1 119 ? 17.235  -1.613  -4.170  1.00 48.21  ? 167 LEU A CD2   1 
ATOM   925  N N     . PRO A 1 120 ? 13.433  -2.859  -0.253  1.00 55.05  ? 168 PRO A N     1 
ATOM   926  C CA    . PRO A 1 120 ? 13.301  -3.840  0.832   1.00 56.65  ? 168 PRO A CA    1 
ATOM   927  C C     . PRO A 1 120 ? 14.582  -4.645  1.007   1.00 58.26  ? 168 PRO A C     1 
ATOM   928  O O     . PRO A 1 120 ? 15.449  -4.705  0.129   1.00 51.74  ? 168 PRO A O     1 
ATOM   929  C CB    . PRO A 1 120 ? 12.122  -4.726  0.391   1.00 55.89  ? 168 PRO A CB    1 
ATOM   930  C CG    . PRO A 1 120 ? 11.745  -4.278  -0.990  1.00 53.39  ? 168 PRO A CG    1 
ATOM   931  C CD    . PRO A 1 120 ? 12.280  -2.885  -1.166  1.00 54.25  ? 168 PRO A CD    1 
ATOM   932  N N     . LYS A 1 121 ? 14.712  -5.232  2.196   1.00 65.14  ? 169 LYS A N     1 
ATOM   933  C CA    . LYS A 1 121 ? 15.926  -5.955  2.548   1.00 58.16  ? 169 LYS A CA    1 
ATOM   934  C C     . LYS A 1 121 ? 16.153  -7.123  1.599   1.00 56.55  ? 169 LYS A C     1 
ATOM   935  O O     . LYS A 1 121 ? 15.208  -7.791  1.163   1.00 58.68  ? 169 LYS A O     1 
ATOM   936  C CB    . LYS A 1 121 ? 15.837  -6.471  3.988   1.00 59.99  ? 169 LYS A CB    1 
ATOM   937  C CG    . LYS A 1 121 ? 15.880  -5.390  5.058   1.00 65.18  ? 169 LYS A CG    1 
ATOM   938  C CD    . LYS A 1 121 ? 16.472  -5.938  6.358   1.00 67.61  ? 169 LYS A CD    1 
ATOM   939  C CE    . LYS A 1 121 ? 17.825  -6.613  6.103   1.00 60.59  ? 169 LYS A CE    1 
ATOM   940  N NZ    . LYS A 1 121 ? 18.525  -6.963  7.355   1.00 52.39  ? 169 LYS A NZ    1 
ATOM   941  N N     . GLY A 1 122 ? 17.419  -7.381  1.295   1.00 52.82  ? 170 GLY A N     1 
ATOM   942  C CA    . GLY A 1 122 ? 17.752  -8.518  0.473   1.00 54.13  ? 170 GLY A CA    1 
ATOM   943  C C     . GLY A 1 122 ? 17.524  -8.325  -1.006  1.00 51.52  ? 170 GLY A C     1 
ATOM   944  O O     . GLY A 1 122 ? 17.627  -9.302  -1.757  1.00 52.46  ? 170 GLY A O     1 
ATOM   945  N N     . PHE A 1 123 ? 17.212  -7.103  -1.445  1.00 50.31  ? 171 PHE A N     1 
ATOM   946  C CA    . PHE A 1 123 ? 17.052  -6.770  -2.856  1.00 50.21  ? 171 PHE A CA    1 
ATOM   947  C C     . PHE A 1 123 ? 18.166  -5.824  -3.249  1.00 44.16  ? 171 PHE A C     1 
ATOM   948  O O     . PHE A 1 123 ? 18.307  -4.763  -2.642  1.00 47.16  ? 171 PHE A O     1 
ATOM   949  C CB    . PHE A 1 123 ? 15.697  -6.110  -3.136  1.00 49.18  ? 171 PHE A CB    1 
ATOM   950  C CG    . PHE A 1 123 ? 14.563  -7.071  -3.222  1.00 47.54  ? 171 PHE A CG    1 
ATOM   951  C CD1   . PHE A 1 123 ? 14.307  -7.744  -4.394  1.00 44.87  ? 171 PHE A CD1   1 
ATOM   952  C CD2   . PHE A 1 123 ? 13.747  -7.305  -2.124  1.00 49.78  ? 171 PHE A CD2   1 
ATOM   953  C CE1   . PHE A 1 123 ? 13.258  -8.634  -4.476  1.00 45.46  ? 171 PHE A CE1   1 
ATOM   954  C CE2   . PHE A 1 123 ? 12.695  -8.192  -2.196  1.00 45.91  ? 171 PHE A CE2   1 
ATOM   955  C CZ    . PHE A 1 123 ? 12.454  -8.864  -3.370  1.00 48.45  ? 171 PHE A CZ    1 
ATOM   956  N N     . TYR A 1 124 ? 18.933  -6.188  -4.272  1.00 45.26  ? 172 TYR A N     1 
ATOM   957  C CA    . TYR A 1 124 ? 19.942  -5.288  -4.810  1.00 45.52  ? 172 TYR A CA    1 
ATOM   958  C C     . TYR A 1 124 ? 19.906  -5.303  -6.337  1.00 43.50  ? 172 TYR A C     1 
ATOM   959  O O     . TYR A 1 124 ? 19.501  -6.287  -6.960  1.00 45.37  ? 172 TYR A O     1 
ATOM   960  C CB    . TYR A 1 124 ? 21.369  -5.656  -4.313  1.00 51.22  ? 172 TYR A CB    1 
ATOM   961  C CG    . TYR A 1 124 ? 21.465  -5.862  -2.814  1.00 50.19  ? 172 TYR A CG    1 
ATOM   962  C CD1   . TYR A 1 124 ? 21.696  -4.791  -1.953  1.00 49.67  ? 172 TYR A CD1   1 
ATOM   963  C CD2   . TYR A 1 124 ? 21.304  -7.123  -2.259  1.00 51.33  ? 172 TYR A CD2   1 
ATOM   964  C CE1   . TYR A 1 124 ? 21.766  -4.976  -0.584  1.00 51.44  ? 172 TYR A CE1   1 
ATOM   965  C CE2   . TYR A 1 124 ? 21.380  -7.321  -0.888  1.00 52.87  ? 172 TYR A CE2   1 
ATOM   966  C CZ    . TYR A 1 124 ? 21.612  -6.243  -0.054  1.00 53.33  ? 172 TYR A CZ    1 
ATOM   967  O OH    . TYR A 1 124 ? 21.683  -6.442  1.308   1.00 48.56  ? 172 TYR A OH    1 
ATOM   968  N N     . ALA A 1 125 ? 20.346  -4.198  -6.931  1.00 44.32  ? 173 ALA A N     1 
ATOM   969  C CA    . ALA A 1 125 ? 20.583  -4.127  -8.370  1.00 41.96  ? 173 ALA A CA    1 
ATOM   970  C C     . ALA A 1 125 ? 22.002  -4.556  -8.711  1.00 42.80  ? 173 ALA A C     1 
ATOM   971  O O     . ALA A 1 125 ? 22.374  -4.628  -9.883  1.00 51.84  ? 173 ALA A O     1 
ATOM   972  C CB    . ALA A 1 125 ? 20.327  -2.723  -8.875  1.00 42.14  ? 173 ALA A CB    1 
ATOM   973  N N     . ASN B 2 1   ? 4.910   -41.631 -43.209 1.00 69.89  ? 47  ASN B N     1 
ATOM   974  C CA    . ASN B 2 1   ? 5.075   -40.240 -42.798 1.00 68.54  ? 47  ASN B CA    1 
ATOM   975  C C     . ASN B 2 1   ? 4.165   -39.873 -41.614 1.00 66.13  ? 47  ASN B C     1 
ATOM   976  O O     . ASN B 2 1   ? 3.356   -38.942 -41.686 1.00 70.71  ? 47  ASN B O     1 
ATOM   977  C CB    . ASN B 2 1   ? 4.826   -39.289 -43.985 1.00 71.77  ? 47  ASN B CB    1 
ATOM   978  C CG    . ASN B 2 1   ? 3.381   -39.317 -44.479 1.00 77.80  ? 47  ASN B CG    1 
ATOM   979  O OD1   . ASN B 2 1   ? 2.707   -38.285 -44.505 1.00 78.16  ? 47  ASN B OD1   1 
ATOM   980  N ND2   . ASN B 2 1   ? 2.901   -40.498 -44.870 1.00 78.45  ? 47  ASN B ND2   1 
ATOM   981  N N     . ASN B 2 2   ? 4.297   -40.615 -40.517 1.00 60.05  ? 48  ASN B N     1 
ATOM   982  C CA    . ASN B 2 2   ? 3.801   -40.177 -39.214 1.00 55.76  ? 48  ASN B CA    1 
ATOM   983  C C     . ASN B 2 2   ? 4.947   -40.346 -38.222 1.00 52.07  ? 48  ASN B C     1 
ATOM   984  O O     . ASN B 2 2   ? 5.394   -41.470 -37.979 1.00 52.37  ? 48  ASN B O     1 
ATOM   985  C CB    . ASN B 2 2   ? 2.558   -40.962 -38.796 1.00 46.23  ? 48  ASN B CB    1 
ATOM   986  C CG    . ASN B 2 2   ? 1.328   -40.570 -39.609 1.00 49.06  ? 48  ASN B CG    1 
ATOM   987  O OD1   . ASN B 2 2   ? 0.694   -39.555 -39.335 1.00 47.25  ? 48  ASN B OD1   1 
ATOM   988  N ND2   . ASN B 2 2   ? 1.006   -41.361 -40.628 1.00 46.33  ? 48  ASN B ND2   1 
ATOM   989  N N     . THR B 2 3   ? 5.439   -39.238 -37.661 1.00 44.23  ? 49  THR B N     1 
ATOM   990  C CA    . THR B 2 3   ? 6.722   -39.297 -36.970 1.00 46.68  ? 49  THR B CA    1 
ATOM   991  C C     . THR B 2 3   ? 6.713   -38.715 -35.563 1.00 46.12  ? 49  THR B C     1 
ATOM   992  O O     . THR B 2 3   ? 5.653   -38.384 -35.012 1.00 45.23  ? 49  THR B O     1 
ATOM   993  C CB    . THR B 2 3   ? 7.795   -38.573 -37.777 1.00 43.97  ? 49  THR B CB    1 
ATOM   994  O OG1   . THR B 2 3   ? 7.267   -37.324 -38.243 1.00 50.00  ? 49  THR B OG1   1 
ATOM   995  C CG2   . THR B 2 3   ? 8.293   -39.444 -38.951 1.00 43.53  ? 49  THR B CG2   1 
ATOM   996  N N     . ALA B 2 4   ? 7.909   -38.587 -34.990 1.00 32.48  ? 50  ALA B N     1 
ATOM   997  C CA    . ALA B 2 4   ? 8.093   -38.271 -33.586 1.00 30.40  ? 50  ALA B CA    1 
ATOM   998  C C     . ALA B 2 4   ? 9.324   -37.404 -33.415 1.00 31.44  ? 50  ALA B C     1 
ATOM   999  O O     . ALA B 2 4   ? 10.234  -37.394 -34.252 1.00 30.46  ? 50  ALA B O     1 
ATOM   1000 C CB    . ALA B 2 4   ? 8.251   -39.527 -32.731 1.00 28.45  ? 50  ALA B CB    1 
ATOM   1001 N N     . SER B 2 5   ? 9.349   -36.689 -32.300 1.00 28.08  ? 51  SER B N     1 
ATOM   1002 C CA    . SER B 2 5   ? 10.560  -35.990 -31.915 1.00 29.55  ? 51  SER B CA    1 
ATOM   1003 C C     . SER B 2 5   ? 11.698  -36.986 -31.738 1.00 32.24  ? 51  SER B C     1 
ATOM   1004 O O     . SER B 2 5   ? 11.483  -38.139 -31.358 1.00 28.96  ? 51  SER B O     1 
ATOM   1005 C CB    . SER B 2 5   ? 10.326  -35.214 -30.629 1.00 27.92  ? 51  SER B CB    1 
ATOM   1006 O OG    . SER B 2 5   ? 11.531  -34.813 -30.034 1.00 27.96  ? 51  SER B OG    1 
ATOM   1007 N N     . TRP B 2 6   ? 12.927  -36.544 -32.047 1.00 31.61  ? 52  TRP B N     1 
ATOM   1008 C CA    . TRP B 2 6   ? 14.091  -37.396 -31.788 1.00 30.12  ? 52  TRP B CA    1 
ATOM   1009 C C     . TRP B 2 6   ? 14.331  -37.593 -30.304 1.00 30.39  ? 52  TRP B C     1 
ATOM   1010 O O     . TRP B 2 6   ? 15.021  -38.544 -29.927 1.00 35.63  ? 52  TRP B O     1 
ATOM   1011 C CB    . TRP B 2 6   ? 15.370  -36.817 -32.441 1.00 31.45  ? 52  TRP B CB    1 
ATOM   1012 C CG    . TRP B 2 6   ? 15.467  -37.179 -33.891 1.00 32.00  ? 52  TRP B CG    1 
ATOM   1013 C CD1   . TRP B 2 6   ? 15.190  -36.379 -34.963 1.00 32.09  ? 52  TRP B CD1   1 
ATOM   1014 C CD2   . TRP B 2 6   ? 15.816  -38.463 -34.428 1.00 29.15  ? 52  TRP B CD2   1 
ATOM   1015 N NE1   . TRP B 2 6   ? 15.353  -37.082 -36.130 1.00 35.90  ? 52  TRP B NE1   1 
ATOM   1016 C CE2   . TRP B 2 6   ? 15.743  -38.363 -35.828 1.00 34.39  ? 52  TRP B CE2   1 
ATOM   1017 C CE3   . TRP B 2 6   ? 16.196  -39.678 -33.858 1.00 29.23  ? 52  TRP B CE3   1 
ATOM   1018 C CZ2   . TRP B 2 6   ? 16.038  -39.442 -36.672 1.00 37.00  ? 52  TRP B CZ2   1 
ATOM   1019 C CZ3   . TRP B 2 6   ? 16.473  -40.751 -34.696 1.00 30.34  ? 52  TRP B CZ3   1 
ATOM   1020 C CH2   . TRP B 2 6   ? 16.396  -40.630 -36.078 1.00 31.36  ? 52  TRP B CH2   1 
ATOM   1021 N N     . PHE B 2 7   ? 13.756  -36.749 -29.451 1.00 29.25  ? 53  PHE B N     1 
ATOM   1022 C CA    . PHE B 2 7   ? 14.073  -36.749 -28.032 1.00 31.76  ? 53  PHE B CA    1 
ATOM   1023 C C     . PHE B 2 7   ? 12.840  -36.998 -27.172 1.00 31.35  ? 53  PHE B C     1 
ATOM   1024 O O     . PHE B 2 7   ? 11.715  -36.657 -27.540 1.00 30.52  ? 53  PHE B O     1 
ATOM   1025 C CB    . PHE B 2 7   ? 14.724  -35.413 -27.614 1.00 31.90  ? 53  PHE B CB    1 
ATOM   1026 C CG    . PHE B 2 7   ? 15.860  -35.017 -28.488 1.00 29.48  ? 53  PHE B CG    1 
ATOM   1027 C CD1   . PHE B 2 7   ? 17.143  -35.460 -28.216 1.00 37.58  ? 53  PHE B CD1   1 
ATOM   1028 C CD2   . PHE B 2 7   ? 15.654  -34.235 -29.598 1.00 30.83  ? 53  PHE B CD2   1 
ATOM   1029 C CE1   . PHE B 2 7   ? 18.197  -35.122 -29.037 1.00 33.17  ? 53  PHE B CE1   1 
ATOM   1030 C CE2   . PHE B 2 7   ? 16.718  -33.875 -30.429 1.00 38.06  ? 53  PHE B CE2   1 
ATOM   1031 C CZ    . PHE B 2 7   ? 17.988  -34.328 -30.142 1.00 34.18  ? 53  PHE B CZ    1 
ATOM   1032 N N     . THR B 2 8   ? 13.074  -37.583 -26.004 1.00 30.42  ? 54  THR B N     1 
ATOM   1033 C CA    . THR B 2 8   ? 12.045  -37.629 -24.979 1.00 34.09  ? 54  THR B CA    1 
ATOM   1034 C C     . THR B 2 8   ? 11.570  -36.207 -24.643 1.00 33.72  ? 54  THR B C     1 
ATOM   1035 O O     . THR B 2 8   ? 12.215  -35.213 -24.971 1.00 34.20  ? 54  THR B O     1 
ATOM   1036 C CB    . THR B 2 8   ? 12.593  -38.345 -23.743 1.00 32.86  ? 54  THR B CB    1 
ATOM   1037 O OG1   . THR B 2 8   ? 13.595  -37.542 -23.134 1.00 27.11  ? 54  THR B OG1   1 
ATOM   1038 C CG2   . THR B 2 8   ? 13.236  -39.614 -24.135 1.00 30.19  ? 54  THR B CG2   1 
ATOM   1039 N N     . ALA B 2 9   ? 10.427  -36.111 -23.983 1.00 31.00  ? 55  ALA B N     1 
ATOM   1040 C CA    . ALA B 2 9   ? 9.821   -34.811 -23.727 1.00 30.28  ? 55  ALA B CA    1 
ATOM   1041 C C     . ALA B 2 9   ? 10.378  -34.162 -22.460 1.00 39.58  ? 55  ALA B C     1 
ATOM   1042 O O     . ALA B 2 9   ? 11.056  -34.790 -21.635 1.00 39.01  ? 55  ALA B O     1 
ATOM   1043 C CB    . ALA B 2 9   ? 8.302   -34.929 -23.593 1.00 33.75  ? 55  ALA B CB    1 
ATOM   1044 N N     . LEU B 2 10  ? 10.040  -32.883 -22.305 1.00 33.97  ? 56  LEU B N     1 
ATOM   1045 C CA    . LEU B 2 10  ? 10.377  -32.084 -21.135 1.00 38.89  ? 56  LEU B CA    1 
ATOM   1046 C C     . LEU B 2 10  ? 9.061   -31.694 -20.479 1.00 36.69  ? 56  LEU B C     1 
ATOM   1047 O O     . LEU B 2 10  ? 8.337   -30.836 -20.991 1.00 40.75  ? 56  LEU B O     1 
ATOM   1048 C CB    . LEU B 2 10  ? 11.208  -30.865 -21.538 1.00 37.05  ? 56  LEU B CB    1 
ATOM   1049 C CG    . LEU B 2 10  ? 12.161  -30.287 -20.507 1.00 43.69  ? 56  LEU B CG    1 
ATOM   1050 C CD1   . LEU B 2 10  ? 13.142  -31.366 -20.032 1.00 50.78  ? 56  LEU B CD1   1 
ATOM   1051 C CD2   . LEU B 2 10  ? 12.922  -29.115 -21.112 1.00 36.92  ? 56  LEU B CD2   1 
ATOM   1052 N N     . THR B 2 11  ? 8.731   -32.339 -19.364 1.00 39.43  ? 57  THR B N     1 
ATOM   1053 C CA    . THR B 2 11  ? 7.404   -32.203 -18.782 1.00 35.03  ? 57  THR B CA    1 
ATOM   1054 C C     . THR B 2 11  ? 7.288   -30.932 -17.963 1.00 40.63  ? 57  THR B C     1 
ATOM   1055 O O     . THR B 2 11  ? 8.128   -30.659 -17.100 1.00 43.66  ? 57  THR B O     1 
ATOM   1056 C CB    . THR B 2 11  ? 7.072   -33.402 -17.907 1.00 38.44  ? 57  THR B CB    1 
ATOM   1057 O OG1   . THR B 2 11  ? 7.034   -34.565 -18.728 1.00 42.87  ? 57  THR B OG1   1 
ATOM   1058 C CG2   . THR B 2 11  ? 5.711   -33.223 -17.263 1.00 38.90  ? 57  THR B CG2   1 
ATOM   1059 N N     . GLN B 2 12  ? 6.238   -30.158 -18.229 1.00 38.39  ? 58  GLN B N     1 
ATOM   1060 C CA    . GLN B 2 12  ? 6.019   -28.909 -17.516 1.00 38.83  ? 58  GLN B CA    1 
ATOM   1061 C C     . GLN B 2 12  ? 5.256   -29.247 -16.251 1.00 47.31  ? 58  GLN B C     1 
ATOM   1062 O O     . GLN B 2 12  ? 4.030   -29.357 -16.247 1.00 46.97  ? 58  GLN B O     1 
ATOM   1063 C CB    . GLN B 2 12  ? 5.264   -27.911 -18.371 1.00 42.17  ? 58  GLN B CB    1 
ATOM   1064 C CG    . GLN B 2 12  ? 4.841   -26.685 -17.596 1.00 45.91  ? 58  GLN B CG    1 
ATOM   1065 C CD    . GLN B 2 12  ? 4.137   -25.658 -18.458 1.00 49.72  ? 58  GLN B CD    1 
ATOM   1066 O OE1   . GLN B 2 12  ? 4.290   -25.643 -19.683 1.00 49.74  ? 58  GLN B OE1   1 
ATOM   1067 N NE2   . GLN B 2 12  ? 3.368   -24.784 -17.822 1.00 47.19  ? 58  GLN B NE2   1 
ATOM   1068 N N     . HIS B 2 13  ? 5.994   -29.445 -15.166 1.00 48.16  ? 59  HIS B N     1 
ATOM   1069 C CA    . HIS B 2 13  ? 5.340   -29.733 -13.900 1.00 50.72  ? 59  HIS B CA    1 
ATOM   1070 C C     . HIS B 2 13  ? 4.768   -28.471 -13.260 1.00 55.58  ? 59  HIS B C     1 
ATOM   1071 O O     . HIS B 2 13  ? 3.729   -28.544 -12.594 1.00 59.22  ? 59  HIS B O     1 
ATOM   1072 C CB    . HIS B 2 13  ? 6.315   -30.450 -12.961 1.00 46.44  ? 59  HIS B CB    1 
ATOM   1073 C CG    . HIS B 2 13  ? 6.694   -31.831 -13.417 1.00 44.93  ? 59  HIS B CG    1 
ATOM   1074 N ND1   . HIS B 2 13  ? 5.782   -32.862 -13.511 1.00 44.33  ? 59  HIS B ND1   1 
ATOM   1075 C CD2   . HIS B 2 13  ? 7.889   -32.352 -13.797 1.00 44.69  ? 59  HIS B CD2   1 
ATOM   1076 C CE1   . HIS B 2 13  ? 6.398   -33.959 -13.929 1.00 50.42  ? 59  HIS B CE1   1 
ATOM   1077 N NE2   . HIS B 2 13  ? 7.678   -33.679 -14.107 1.00 47.61  ? 59  HIS B NE2   1 
ATOM   1078 N N     . GLY B 2 14  ? 5.389   -27.312 -13.490 1.00 48.12  ? 60  GLY B N     1 
ATOM   1079 C CA    . GLY B 2 14  ? 4.986   -26.075 -12.859 1.00 45.94  ? 60  GLY B CA    1 
ATOM   1080 C C     . GLY B 2 14  ? 4.002   -25.268 -13.688 1.00 51.63  ? 60  GLY B C     1 
ATOM   1081 O O     . GLY B 2 14  ? 3.400   -25.753 -14.646 1.00 54.48  ? 60  GLY B O     1 
ATOM   1082 N N     . LYS B 2 15  ? 3.826   -24.004 -13.285 1.00 54.91  ? 61  LYS B N     1 
ATOM   1083 C CA    . LYS B 2 15  ? 2.899   -23.086 -13.943 1.00 55.92  ? 61  LYS B CA    1 
ATOM   1084 C C     . LYS B 2 15  ? 3.540   -22.271 -15.062 1.00 53.02  ? 61  LYS B C     1 
ATOM   1085 O O     . LYS B 2 15  ? 2.826   -21.824 -15.964 1.00 51.54  ? 61  LYS B O     1 
ATOM   1086 C CB    . LYS B 2 15  ? 2.281   -22.122 -12.917 1.00 59.72  ? 61  LYS B CB    1 
ATOM   1087 C CG    . LYS B 2 15  ? 0.956   -22.606 -12.326 1.00 66.24  ? 61  LYS B CG    1 
ATOM   1088 C CD    . LYS B 2 15  ? 0.596   -21.911 -11.010 1.00 66.78  ? 61  LYS B CD    1 
ATOM   1089 C CE    . LYS B 2 15  ? 0.210   -20.446 -11.213 1.00 65.09  ? 61  LYS B CE    1 
ATOM   1090 N NZ    . LYS B 2 15  ? -0.177  -19.783 -9.922  1.00 61.36  ? 61  LYS B NZ    1 
ATOM   1091 N N     . GLU B 2 16  ? 4.858   -22.080 -15.035 1.00 49.21  ? 62  GLU B N     1 
ATOM   1092 C CA    . GLU B 2 16  ? 5.532   -21.254 -16.025 1.00 50.51  ? 62  GLU B CA    1 
ATOM   1093 C C     . GLU B 2 16  ? 5.777   -22.024 -17.320 1.00 51.21  ? 62  GLU B C     1 
ATOM   1094 O O     . GLU B 2 16  ? 6.212   -23.178 -17.299 1.00 52.67  ? 62  GLU B O     1 
ATOM   1095 C CB    . GLU B 2 16  ? 6.856   -20.735 -15.454 1.00 52.59  ? 62  GLU B CB    1 
ATOM   1096 C CG    . GLU B 2 16  ? 6.652   -19.625 -14.430 1.00 58.23  ? 62  GLU B CG    1 
ATOM   1097 C CD    . GLU B 2 16  ? 7.942   -19.071 -13.860 1.00 62.97  ? 62  GLU B CD    1 
ATOM   1098 O OE1   . GLU B 2 16  ? 9.033   -19.624 -14.146 1.00 61.50  ? 62  GLU B OE1   1 
ATOM   1099 O OE2   . GLU B 2 16  ? 7.853   -18.065 -13.115 1.00 67.11  ? 62  GLU B OE2   1 
ATOM   1100 N N     . ASP B 2 17  ? 5.510   -21.371 -18.453 1.00 44.98  ? 63  ASP B N     1 
ATOM   1101 C CA    . ASP B 2 17  ? 5.791   -21.968 -19.754 1.00 47.04  ? 63  ASP B CA    1 
ATOM   1102 C C     . ASP B 2 17  ? 7.302   -22.134 -19.954 1.00 47.45  ? 63  ASP B C     1 
ATOM   1103 O O     . ASP B 2 17  ? 8.121   -21.502 -19.277 1.00 44.90  ? 63  ASP B O     1 
ATOM   1104 C CB    . ASP B 2 17  ? 5.208   -21.115 -20.887 1.00 46.96  ? 63  ASP B CB    1 
ATOM   1105 C CG    . ASP B 2 17  ? 3.713   -21.341 -21.093 1.00 50.31  ? 63  ASP B CG    1 
ATOM   1106 O OD1   . ASP B 2 17  ? 3.218   -22.449 -20.779 1.00 58.73  ? 63  ASP B OD1   1 
ATOM   1107 O OD2   . ASP B 2 17  ? 3.027   -20.415 -21.584 1.00 55.31  ? 63  ASP B OD2   1 
ATOM   1108 N N     . LEU B 2 18  ? 7.671   -23.011 -20.887 1.00 42.65  ? 64  LEU B N     1 
ATOM   1109 C CA    . LEU B 2 18  ? 9.086   -23.228 -21.160 1.00 42.93  ? 64  LEU B CA    1 
ATOM   1110 C C     . LEU B 2 18  ? 9.683   -22.012 -21.870 1.00 41.83  ? 64  LEU B C     1 
ATOM   1111 O O     . LEU B 2 18  ? 9.035   -21.375 -22.705 1.00 42.54  ? 64  LEU B O     1 
ATOM   1112 C CB    . LEU B 2 18  ? 9.282   -24.498 -21.993 1.00 39.32  ? 64  LEU B CB    1 
ATOM   1113 C CG    . LEU B 2 18  ? 10.714  -24.997 -22.246 1.00 38.62  ? 64  LEU B CG    1 
ATOM   1114 C CD1   . LEU B 2 18  ? 11.284  -25.598 -20.986 1.00 41.81  ? 64  LEU B CD1   1 
ATOM   1115 C CD2   . LEU B 2 18  ? 10.785  -26.016 -23.358 1.00 32.02  ? 64  LEU B CD2   1 
ATOM   1116 N N     . LYS B 2 19  ? 10.920  -21.673 -21.505 1.00 42.69  ? 65  LYS B N     1 
ATOM   1117 C CA    . LYS B 2 19  ? 11.680  -20.616 -22.158 1.00 42.24  ? 65  LYS B CA    1 
ATOM   1118 C C     . LYS B 2 19  ? 13.153  -20.822 -21.833 1.00 43.00  ? 65  LYS B C     1 
ATOM   1119 O O     . LYS B 2 19  ? 13.493  -21.339 -20.768 1.00 44.15  ? 65  LYS B O     1 
ATOM   1120 C CB    . LYS B 2 19  ? 11.210  -19.224 -21.715 1.00 43.56  ? 65  LYS B CB    1 
ATOM   1121 C CG    . LYS B 2 19  ? 11.062  -19.080 -20.198 1.00 49.61  ? 65  LYS B CG    1 
ATOM   1122 C CD    . LYS B 2 19  ? 9.759   -18.342 -19.818 1.00 57.44  ? 65  LYS B CD    1 
ATOM   1123 C CE    . LYS B 2 19  ? 9.273   -18.674 -18.391 1.00 52.92  ? 65  LYS B CE    1 
ATOM   1124 N NZ    . LYS B 2 19  ? 7.857   -18.228 -18.180 1.00 52.48  ? 65  LYS B NZ    1 
ATOM   1125 N N     . PHE B 2 20  ? 14.022  -20.436 -22.767 1.00 40.82  ? 66  PHE B N     1 
ATOM   1126 C CA    . PHE B 2 20  ? 15.462  -20.477 -22.552 1.00 43.97  ? 66  PHE B CA    1 
ATOM   1127 C C     . PHE B 2 20  ? 16.096  -19.149 -22.939 1.00 43.67  ? 66  PHE B C     1 
ATOM   1128 O O     . PHE B 2 20  ? 15.629  -18.476 -23.861 1.00 48.00  ? 66  PHE B O     1 
ATOM   1129 C CB    . PHE B 2 20  ? 16.147  -21.587 -23.372 1.00 43.50  ? 66  PHE B CB    1 
ATOM   1130 C CG    . PHE B 2 20  ? 15.801  -22.972 -22.932 1.00 43.17  ? 66  PHE B CG    1 
ATOM   1131 C CD1   . PHE B 2 20  ? 16.558  -23.609 -21.967 1.00 41.69  ? 66  PHE B CD1   1 
ATOM   1132 C CD2   . PHE B 2 20  ? 14.733  -23.650 -23.509 1.00 35.87  ? 66  PHE B CD2   1 
ATOM   1133 C CE1   . PHE B 2 20  ? 16.246  -24.883 -21.575 1.00 42.24  ? 66  PHE B CE1   1 
ATOM   1134 C CE2   . PHE B 2 20  ? 14.412  -24.929 -23.121 1.00 35.37  ? 66  PHE B CE2   1 
ATOM   1135 C CZ    . PHE B 2 20  ? 15.159  -25.546 -22.150 1.00 43.26  ? 66  PHE B CZ    1 
ATOM   1136 N N     . PRO B 2 21  ? 17.183  -18.773 -22.277 1.00 46.59  ? 67  PRO B N     1 
ATOM   1137 C CA    . PRO B 2 21  ? 17.917  -17.580 -22.697 1.00 42.94  ? 67  PRO B CA    1 
ATOM   1138 C C     . PRO B 2 21  ? 18.588  -17.811 -24.039 1.00 47.19  ? 67  PRO B C     1 
ATOM   1139 O O     . PRO B 2 21  ? 18.735  -18.943 -24.503 1.00 46.60  ? 67  PRO B O     1 
ATOM   1140 C CB    . PRO B 2 21  ? 18.951  -17.383 -21.585 1.00 46.97  ? 67  PRO B CB    1 
ATOM   1141 C CG    . PRO B 2 21  ? 18.488  -18.248 -20.440 1.00 49.36  ? 67  PRO B CG    1 
ATOM   1142 C CD    . PRO B 2 21  ? 17.770  -19.388 -21.075 1.00 50.12  ? 67  PRO B CD    1 
ATOM   1143 N N     . ARG B 2 22  ? 18.971  -16.705 -24.677 1.00 47.97  ? 68  ARG B N     1 
ATOM   1144 C CA    . ARG B 2 22  ? 19.589  -16.772 -25.994 1.00 49.15  ? 68  ARG B CA    1 
ATOM   1145 C C     . ARG B 2 22  ? 20.779  -17.721 -25.959 1.00 46.74  ? 68  ARG B C     1 
ATOM   1146 O O     . ARG B 2 22  ? 21.562  -17.710 -25.011 1.00 45.61  ? 68  ARG B O     1 
ATOM   1147 C CB    . ARG B 2 22  ? 20.025  -15.371 -26.431 1.00 53.32  ? 68  ARG B CB    1 
ATOM   1148 C CG    . ARG B 2 22  ? 20.684  -15.303 -27.802 1.00 56.53  ? 68  ARG B CG    1 
ATOM   1149 C CD    . ARG B 2 22  ? 21.171  -13.886 -28.123 1.00 58.32  ? 68  ARG B CD    1 
ATOM   1150 N NE    . ARG B 2 22  ? 22.144  -13.874 -29.212 1.00 65.59  ? 68  ARG B NE    1 
ATOM   1151 C CZ    . ARG B 2 22  ? 21.836  -13.706 -30.491 1.00 66.91  ? 68  ARG B CZ    1 
ATOM   1152 N NH1   . ARG B 2 22  ? 20.587  -13.504 -30.881 1.00 73.59  ? 68  ARG B NH1   1 
ATOM   1153 N NH2   . ARG B 2 22  ? 22.806  -13.743 -31.402 1.00 63.70  ? 68  ARG B NH2   1 
ATOM   1154 N N     . GLY B 2 23  ? 20.863  -18.596 -26.958 1.00 45.35  ? 69  GLY B N     1 
ATOM   1155 C CA    . GLY B 2 23  ? 21.971  -19.509 -27.089 1.00 47.48  ? 69  GLY B CA    1 
ATOM   1156 C C     . GLY B 2 23  ? 21.813  -20.843 -26.386 1.00 47.44  ? 69  GLY B C     1 
ATOM   1157 O O     . GLY B 2 23  ? 22.575  -21.768 -26.682 1.00 48.25  ? 69  GLY B O     1 
ATOM   1158 N N     . GLN B 2 24  ? 20.850  -20.976 -25.474 1.00 48.28  ? 70  GLN B N     1 
ATOM   1159 C CA    . GLN B 2 24  ? 20.643  -22.187 -24.689 1.00 43.11  ? 70  GLN B CA    1 
ATOM   1160 C C     . GLN B 2 24  ? 19.394  -22.947 -25.127 1.00 48.69  ? 70  GLN B C     1 
ATOM   1161 O O     . GLN B 2 24  ? 18.472  -22.394 -25.745 1.00 40.78  ? 70  GLN B O     1 
ATOM   1162 C CB    . GLN B 2 24  ? 20.489  -21.863 -23.203 1.00 44.23  ? 70  GLN B CB    1 
ATOM   1163 C CG    . GLN B 2 24  ? 21.663  -21.191 -22.541 1.00 47.85  ? 70  GLN B CG    1 
ATOM   1164 C CD    . GLN B 2 24  ? 21.442  -21.095 -21.050 1.00 49.99  ? 70  GLN B CD    1 
ATOM   1165 O OE1   . GLN B 2 24  ? 20.615  -21.815 -20.497 1.00 50.42  ? 70  GLN B OE1   1 
ATOM   1166 N NE2   . GLN B 2 24  ? 22.166  -20.202 -20.394 1.00 55.57  ? 70  GLN B NE2   1 
ATOM   1167 N N     . GLY B 2 25  ? 19.362  -24.231 -24.748 1.00 45.14  ? 71  GLY B N     1 
ATOM   1168 C CA    . GLY B 2 25  ? 18.167  -25.045 -24.805 1.00 44.19  ? 71  GLY B CA    1 
ATOM   1169 C C     . GLY B 2 25  ? 18.209  -26.189 -25.800 1.00 44.48  ? 71  GLY B C     1 
ATOM   1170 O O     . GLY B 2 25  ? 17.419  -27.135 -25.665 1.00 44.83  ? 71  GLY B O     1 
ATOM   1171 N N     . VAL B 2 26  ? 19.079  -26.134 -26.799 1.00 35.74  ? 72  VAL B N     1 
ATOM   1172 C CA    . VAL B 2 26  ? 19.094  -27.188 -27.805 1.00 41.73  ? 72  VAL B CA    1 
ATOM   1173 C C     . VAL B 2 26  ? 19.606  -28.452 -27.130 1.00 43.73  ? 72  VAL B C     1 
ATOM   1174 O O     . VAL B 2 26  ? 20.680  -28.422 -26.518 1.00 47.59  ? 72  VAL B O     1 
ATOM   1175 C CB    . VAL B 2 26  ? 19.945  -26.788 -29.016 1.00 44.26  ? 72  VAL B CB    1 
ATOM   1176 C CG1   . VAL B 2 26  ? 19.870  -27.868 -30.098 1.00 41.38  ? 72  VAL B CG1   1 
ATOM   1177 C CG2   . VAL B 2 26  ? 19.458  -25.461 -29.554 1.00 40.00  ? 72  VAL B CG2   1 
ATOM   1178 N N     . PRO B 2 27  ? 18.873  -29.562 -27.162 1.00 39.17  ? 73  PRO B N     1 
ATOM   1179 C CA    . PRO B 2 27  ? 19.340  -30.763 -26.476 1.00 42.91  ? 73  PRO B CA    1 
ATOM   1180 C C     . PRO B 2 27  ? 20.510  -31.400 -27.218 1.00 42.77  ? 73  PRO B C     1 
ATOM   1181 O O     . PRO B 2 27  ? 20.727  -31.167 -28.414 1.00 36.75  ? 73  PRO B O     1 
ATOM   1182 C CB    . PRO B 2 27  ? 18.108  -31.669 -26.471 1.00 38.68  ? 73  PRO B CB    1 
ATOM   1183 C CG    . PRO B 2 27  ? 17.348  -31.268 -27.644 1.00 35.76  ? 73  PRO B CG    1 
ATOM   1184 C CD    . PRO B 2 27  ? 17.631  -29.814 -27.907 1.00 42.40  ? 73  PRO B CD    1 
ATOM   1185 N N     . ILE B 2 28  ? 21.252  -32.234 -26.481 1.00 41.51  ? 74  ILE B N     1 
ATOM   1186 C CA    . ILE B 2 28  ? 22.521  -32.786 -26.958 1.00 45.18  ? 74  ILE B CA    1 
ATOM   1187 C C     . ILE B 2 28  ? 22.278  -33.983 -27.868 1.00 46.14  ? 74  ILE B C     1 
ATOM   1188 O O     . ILE B 2 28  ? 21.582  -34.932 -27.490 1.00 47.95  ? 74  ILE B O     1 
ATOM   1189 C CB    . ILE B 2 28  ? 23.418  -33.181 -25.779 1.00 44.64  ? 74  ILE B CB    1 
ATOM   1190 C CG1   . ILE B 2 28  ? 23.760  -31.962 -24.932 1.00 48.31  ? 74  ILE B CG1   1 
ATOM   1191 C CG2   . ILE B 2 28  ? 24.679  -33.796 -26.297 1.00 43.65  ? 74  ILE B CG2   1 
ATOM   1192 C CD1   . ILE B 2 28  ? 24.600  -32.297 -23.725 1.00 45.07  ? 74  ILE B CD1   1 
ATOM   1193 N N     . ASN B 2 29  ? 22.877  -33.946 -29.066 1.00 49.74  ? 75  ASN B N     1 
ATOM   1194 C CA    . ASN B 2 29  ? 22.753  -35.011 -30.065 1.00 51.27  ? 75  ASN B CA    1 
ATOM   1195 C C     . ASN B 2 29  ? 24.057  -35.091 -30.857 1.00 57.32  ? 75  ASN B C     1 
ATOM   1196 O O     . ASN B 2 29  ? 24.378  -34.182 -31.635 1.00 51.60  ? 75  ASN B O     1 
ATOM   1197 C CB    . ASN B 2 29  ? 21.564  -34.764 -30.993 1.00 46.95  ? 75  ASN B CB    1 
ATOM   1198 C CG    . ASN B 2 29  ? 21.429  -35.824 -32.070 1.00 51.74  ? 75  ASN B CG    1 
ATOM   1199 O OD1   . ASN B 2 29  ? 21.980  -36.917 -31.953 1.00 57.27  ? 75  ASN B OD1   1 
ATOM   1200 N ND2   . ASN B 2 29  ? 20.690  -35.506 -33.127 1.00 49.72  ? 75  ASN B ND2   1 
ATOM   1201 N N     . THR B 2 30  ? 24.788  -36.198 -30.677 1.00 55.93  ? 76  THR B N     1 
ATOM   1202 C CA    . THR B 2 30  ? 26.082  -36.383 -31.321 1.00 54.58  ? 76  THR B CA    1 
ATOM   1203 C C     . THR B 2 30  ? 25.967  -36.605 -32.827 1.00 55.78  ? 76  THR B C     1 
ATOM   1204 O O     . THR B 2 30  ? 26.933  -36.364 -33.556 1.00 56.78  ? 76  THR B O     1 
ATOM   1205 C CB    . THR B 2 30  ? 26.811  -37.553 -30.656 1.00 55.33  ? 76  THR B CB    1 
ATOM   1206 O OG1   . THR B 2 30  ? 26.243  -38.795 -31.097 1.00 56.93  ? 76  THR B OG1   1 
ATOM   1207 C CG2   . THR B 2 30  ? 26.668  -37.462 -29.138 1.00 49.56  ? 76  THR B CG2   1 
ATOM   1208 N N     . ASN B 2 31  ? 24.809  -37.026 -33.319 1.00 56.87  ? 77  ASN B N     1 
ATOM   1209 C CA    . ASN B 2 31  ? 24.620  -37.262 -34.743 1.00 56.67  ? 77  ASN B CA    1 
ATOM   1210 C C     . ASN B 2 31  ? 24.243  -35.993 -35.515 1.00 62.85  ? 77  ASN B C     1 
ATOM   1211 O O     . ASN B 2 31  ? 23.669  -36.097 -36.608 1.00 63.45  ? 77  ASN B O     1 
ATOM   1212 C CB    . ASN B 2 31  ? 23.556  -38.345 -34.958 1.00 60.80  ? 77  ASN B CB    1 
ATOM   1213 C CG    . ASN B 2 31  ? 24.154  -39.691 -35.359 1.00 65.57  ? 77  ASN B CG    1 
ATOM   1214 O OD1   . ASN B 2 31  ? 24.967  -40.277 -34.633 1.00 62.40  ? 77  ASN B OD1   1 
ATOM   1215 N ND2   . ASN B 2 31  ? 23.736  -40.195 -36.517 1.00 69.57  ? 77  ASN B ND2   1 
ATOM   1216 N N     . SER B 2 32  ? 24.554  -34.802 -34.980 1.00 63.33  ? 78  SER B N     1 
ATOM   1217 C CA    . SER B 2 32  ? 24.229  -33.541 -35.645 1.00 62.14  ? 78  SER B CA    1 
ATOM   1218 C C     . SER B 2 32  ? 25.432  -32.610 -35.617 1.00 58.09  ? 78  SER B C     1 
ATOM   1219 O O     . SER B 2 32  ? 26.171  -32.571 -34.629 1.00 61.18  ? 78  SER B O     1 
ATOM   1220 C CB    . SER B 2 32  ? 23.015  -32.836 -34.999 1.00 58.57  ? 78  SER B CB    1 
ATOM   1221 O OG    . SER B 2 32  ? 23.333  -32.275 -33.730 1.00 60.28  ? 78  SER B OG    1 
ATOM   1222 N N     . SER B 2 33  ? 25.611  -31.846 -36.730 1.00 60.91  ? 79  SER B N     1 
ATOM   1223 C CA    . SER B 2 33  ? 26.694  -30.909 -36.997 1.00 59.84  ? 79  SER B CA    1 
ATOM   1224 C C     . SER B 2 33  ? 26.378  -29.547 -36.387 1.00 61.65  ? 79  SER B C     1 
ATOM   1225 O O     . SER B 2 33  ? 25.218  -29.259 -36.067 1.00 56.78  ? 79  SER B O     1 
ATOM   1226 C CB    . SER B 2 33  ? 26.925  -30.796 -38.511 1.00 58.70  ? 79  SER B CB    1 
ATOM   1227 O OG    . SER B 2 33  ? 25.980  -29.955 -39.154 1.00 60.77  ? 79  SER B OG    1 
ATOM   1228 N N     . PRO B 2 34  ? 27.393  -28.689 -36.188 1.00 58.01  ? 80  PRO B N     1 
ATOM   1229 C CA    . PRO B 2 34  ? 27.149  -27.406 -35.491 1.00 56.59  ? 80  PRO B CA    1 
ATOM   1230 C C     . PRO B 2 34  ? 26.177  -26.466 -36.198 1.00 50.48  ? 80  PRO B C     1 
ATOM   1231 O O     . PRO B 2 34  ? 25.541  -25.642 -35.531 1.00 53.74  ? 80  PRO B O     1 
ATOM   1232 C CB    . PRO B 2 34  ? 28.556  -26.796 -35.389 1.00 55.20  ? 80  PRO B CB    1 
ATOM   1233 C CG    . PRO B 2 34  ? 29.323  -27.441 -36.460 1.00 51.61  ? 80  PRO B CG    1 
ATOM   1234 C CD    . PRO B 2 34  ? 28.810  -28.843 -36.545 1.00 55.73  ? 80  PRO B CD    1 
ATOM   1235 N N     . ASP B 2 35  ? 26.035  -26.562 -37.519 1.00 52.18  ? 81  ASP B N     1 
ATOM   1236 C CA    . ASP B 2 35  ? 25.056  -25.767 -38.260 1.00 58.52  ? 81  ASP B CA    1 
ATOM   1237 C C     . ASP B 2 35  ? 23.605  -26.211 -38.018 1.00 58.37  ? 81  ASP B C     1 
ATOM   1238 O O     . ASP B 2 35  ? 22.668  -25.489 -38.387 1.00 53.09  ? 81  ASP B O     1 
ATOM   1239 C CB    . ASP B 2 35  ? 25.391  -25.838 -39.755 1.00 57.26  ? 81  ASP B CB    1 
ATOM   1240 C CG    . ASP B 2 35  ? 26.898  -25.765 -40.022 1.00 68.43  ? 81  ASP B CG    1 
ATOM   1241 O OD1   . ASP B 2 35  ? 27.514  -24.698 -39.767 1.00 66.55  ? 81  ASP B OD1   1 
ATOM   1242 O OD2   . ASP B 2 35  ? 27.472  -26.793 -40.459 1.00 66.73  ? 81  ASP B OD2   1 
ATOM   1243 N N     . ASP B 2 36  ? 23.390  -27.382 -37.428 1.00 57.49  ? 82  ASP B N     1 
ATOM   1244 C CA    . ASP B 2 36  ? 22.044  -27.906 -37.238 1.00 55.70  ? 82  ASP B CA    1 
ATOM   1245 C C     . ASP B 2 36  ? 21.443  -27.552 -35.882 1.00 51.84  ? 82  ASP B C     1 
ATOM   1246 O O     . ASP B 2 36  ? 20.247  -27.784 -35.675 1.00 49.42  ? 82  ASP B O     1 
ATOM   1247 C CB    . ASP B 2 36  ? 22.055  -29.434 -37.416 1.00 56.69  ? 82  ASP B CB    1 
ATOM   1248 C CG    . ASP B 2 36  ? 22.519  -29.860 -38.810 1.00 61.00  ? 82  ASP B CG    1 
ATOM   1249 O OD1   . ASP B 2 36  ? 23.028  -28.981 -39.544 1.00 65.80  ? 82  ASP B OD1   1 
ATOM   1250 O OD2   . ASP B 2 36  ? 22.362  -31.052 -39.179 1.00 53.62  ? 82  ASP B OD2   1 
ATOM   1251 N N     . GLN B 2 37  ? 22.227  -26.975 -34.972 1.00 50.82  ? 83  GLN B N     1 
ATOM   1252 C CA    . GLN B 2 37  ? 21.841  -26.810 -33.576 1.00 46.28  ? 83  GLN B CA    1 
ATOM   1253 C C     . GLN B 2 37  ? 20.795  -25.718 -33.349 1.00 49.32  ? 83  GLN B C     1 
ATOM   1254 O O     . GLN B 2 37  ? 21.091  -24.692 -32.725 1.00 45.73  ? 83  GLN B O     1 
ATOM   1255 C CB    . GLN B 2 37  ? 23.091  -26.515 -32.757 1.00 44.46  ? 83  GLN B CB    1 
ATOM   1256 C CG    . GLN B 2 37  ? 23.332  -27.492 -31.619 1.00 53.37  ? 83  GLN B CG    1 
ATOM   1257 C CD    . GLN B 2 37  ? 23.388  -28.947 -32.078 1.00 52.13  ? 83  GLN B CD    1 
ATOM   1258 O OE1   . GLN B 2 37  ? 23.538  -29.241 -33.271 1.00 52.91  ? 83  GLN B OE1   1 
ATOM   1259 N NE2   . GLN B 2 37  ? 23.268  -29.865 -31.124 1.00 48.41  ? 83  GLN B NE2   1 
ATOM   1260 N N     . ILE B 2 38  ? 19.570  -25.933 -33.828 1.00 44.95  ? 84  ILE B N     1 
ATOM   1261 C CA    . ILE B 2 38  ? 18.544  -24.893 -33.801 1.00 45.34  ? 84  ILE B CA    1 
ATOM   1262 C C     . ILE B 2 38  ? 17.180  -25.541 -34.026 1.00 40.95  ? 84  ILE B C     1 
ATOM   1263 O O     . ILE B 2 38  ? 17.009  -26.361 -34.939 1.00 39.25  ? 84  ILE B O     1 
ATOM   1264 C CB    . ILE B 2 38  ? 18.854  -23.800 -34.856 1.00 45.90  ? 84  ILE B CB    1 
ATOM   1265 C CG1   . ILE B 2 38  ? 17.883  -22.622 -34.747 1.00 39.92  ? 84  ILE B CG1   1 
ATOM   1266 C CG2   . ILE B 2 38  ? 18.894  -24.398 -36.272 1.00 40.00  ? 84  ILE B CG2   1 
ATOM   1267 C CD1   . ILE B 2 38  ? 17.950  -21.696 -35.916 1.00 39.81  ? 84  ILE B CD1   1 
ATOM   1268 N N     . GLY B 2 39  ? 16.199  -25.133 -33.220 1.00 36.81  ? 85  GLY B N     1 
ATOM   1269 C CA    . GLY B 2 39  ? 14.868  -25.708 -33.331 1.00 36.49  ? 85  GLY B CA    1 
ATOM   1270 C C     . GLY B 2 39  ? 13.835  -25.073 -32.415 1.00 34.85  ? 85  GLY B C     1 
ATOM   1271 O O     . GLY B 2 39  ? 13.975  -23.933 -31.971 1.00 27.26  ? 85  GLY B O     1 
ATOM   1272 N N     . TYR B 2 40  ? 12.768  -25.828 -32.160 1.00 35.69  ? 86  TYR B N     1 
ATOM   1273 C CA    . TYR B 2 40  ? 11.686  -25.359 -31.305 1.00 35.25  ? 86  TYR B CA    1 
ATOM   1274 C C     . TYR B 2 40  ? 11.210  -26.492 -30.402 1.00 33.24  ? 86  TYR B C     1 
ATOM   1275 O O     . TYR B 2 40  ? 11.326  -27.669 -30.754 1.00 35.66  ? 86  TYR B O     1 
ATOM   1276 C CB    . TYR B 2 40  ? 10.517  -24.812 -32.154 1.00 34.46  ? 86  TYR B CB    1 
ATOM   1277 C CG    . TYR B 2 40  ? 9.882   -25.846 -33.061 1.00 36.21  ? 86  TYR B CG    1 
ATOM   1278 C CD1   . TYR B 2 40  ? 10.419  -26.123 -34.305 1.00 32.75  ? 86  TYR B CD1   1 
ATOM   1279 C CD2   . TYR B 2 40  ? 8.741   -26.544 -32.667 1.00 28.98  ? 86  TYR B CD2   1 
ATOM   1280 C CE1   . TYR B 2 40  ? 9.844   -27.061 -35.139 1.00 32.41  ? 86  TYR B CE1   1 
ATOM   1281 C CE2   . TYR B 2 40  ? 8.163   -27.480 -33.493 1.00 31.14  ? 86  TYR B CE2   1 
ATOM   1282 C CZ    . TYR B 2 40  ? 8.726   -27.733 -34.731 1.00 33.42  ? 86  TYR B CZ    1 
ATOM   1283 O OH    . TYR B 2 40  ? 8.169   -28.663 -35.552 1.00 34.28  ? 86  TYR B OH    1 
ATOM   1284 N N     . TYR B 2 41  ? 10.674  -26.138 -29.233 1.00 30.74  ? 87  TYR B N     1 
ATOM   1285 C CA    . TYR B 2 41  ? 9.878   -27.078 -28.452 1.00 31.37  ? 87  TYR B CA    1 
ATOM   1286 C C     . TYR B 2 41  ? 8.399   -26.810 -28.698 1.00 29.73  ? 87  TYR B C     1 
ATOM   1287 O O     . TYR B 2 41  ? 7.973   -25.656 -28.776 1.00 27.61  ? 87  TYR B O     1 
ATOM   1288 C CB    . TYR B 2 41  ? 10.155  -26.974 -26.955 1.00 31.67  ? 87  TYR B CB    1 
ATOM   1289 C CG    . TYR B 2 41  ? 11.524  -27.402 -26.499 1.00 29.00  ? 87  TYR B CG    1 
ATOM   1290 C CD1   . TYR B 2 41  ? 12.636  -26.592 -26.704 1.00 34.38  ? 87  TYR B CD1   1 
ATOM   1291 C CD2   . TYR B 2 41  ? 11.699  -28.593 -25.813 1.00 31.20  ? 87  TYR B CD2   1 
ATOM   1292 C CE1   . TYR B 2 41  ? 13.902  -26.985 -26.261 1.00 34.30  ? 87  TYR B CE1   1 
ATOM   1293 C CE2   . TYR B 2 41  ? 12.948  -28.991 -25.368 1.00 34.25  ? 87  TYR B CE2   1 
ATOM   1294 C CZ    . TYR B 2 41  ? 14.039  -28.182 -25.591 1.00 29.96  ? 87  TYR B CZ    1 
ATOM   1295 O OH    . TYR B 2 41  ? 15.266  -28.586 -25.147 1.00 39.11  ? 87  TYR B OH    1 
ATOM   1296 N N     . ARG B 2 42  ? 7.618   -27.881 -28.784 1.00 29.71  ? 88  ARG B N     1 
ATOM   1297 C CA    . ARG B 2 42  ? 6.184   -27.807 -29.022 1.00 30.17  ? 88  ARG B CA    1 
ATOM   1298 C C     . ARG B 2 42  ? 5.439   -28.400 -27.824 1.00 33.99  ? 88  ARG B C     1 
ATOM   1299 O O     . ARG B 2 42  ? 5.651   -29.565 -27.464 1.00 27.35  ? 88  ARG B O     1 
ATOM   1300 C CB    . ARG B 2 42  ? 5.825   -28.548 -30.307 1.00 25.63  ? 88  ARG B CB    1 
ATOM   1301 C CG    . ARG B 2 42  ? 4.339   -28.641 -30.566 1.00 30.78  ? 88  ARG B CG    1 
ATOM   1302 C CD    . ARG B 2 42  ? 4.124   -29.592 -31.713 1.00 35.32  ? 88  ARG B CD    1 
ATOM   1303 N NE    . ARG B 2 42  ? 2.755   -29.590 -32.203 1.00 39.27  ? 88  ARG B NE    1 
ATOM   1304 C CZ    . ARG B 2 42  ? 1.829   -30.452 -31.810 1.00 40.22  ? 88  ARG B CZ    1 
ATOM   1305 N NH1   . ARG B 2 42  ? 2.082   -31.360 -30.874 1.00 35.50  ? 88  ARG B NH1   1 
ATOM   1306 N NH2   . ARG B 2 42  ? 0.629   -30.410 -32.376 1.00 35.19  ? 88  ARG B NH2   1 
ATOM   1307 N N     . ARG B 2 43  ? 4.573   -27.598 -27.208 1.00 29.38  ? 89  ARG B N     1 
ATOM   1308 C CA    . ARG B 2 43  ? 3.771   -28.089 -26.098 1.00 30.12  ? 89  ARG B CA    1 
ATOM   1309 C C     . ARG B 2 43  ? 2.727   -29.091 -26.594 1.00 31.50  ? 89  ARG B C     1 
ATOM   1310 O O     . ARG B 2 43  ? 2.016   -28.837 -27.566 1.00 32.11  ? 89  ARG B O     1 
ATOM   1311 C CB    . ARG B 2 43  ? 3.102   -26.916 -25.382 1.00 32.92  ? 89  ARG B CB    1 
ATOM   1312 C CG    . ARG B 2 43  ? 2.644   -27.269 -23.969 1.00 35.62  ? 89  ARG B CG    1 
ATOM   1313 C CD    . ARG B 2 43  ? 1.700   -26.245 -23.342 1.00 41.86  ? 89  ARG B CD    1 
ATOM   1314 N NE    . ARG B 2 43  ? 0.847   -25.519 -24.280 1.00 33.23  ? 89  ARG B NE    1 
ATOM   1315 C CZ    . ARG B 2 43  ? 0.802   -24.197 -24.339 1.00 34.36  ? 89  ARG B CZ    1 
ATOM   1316 N NH1   . ARG B 2 43  ? 1.531   -23.450 -23.529 1.00 39.52  ? 89  ARG B NH1   1 
ATOM   1317 N NH2   . ARG B 2 43  ? 0.026   -23.609 -25.242 1.00 35.36  ? 89  ARG B NH2   1 
ATOM   1318 N N     . ALA B 2 44  ? 2.644   -30.245 -25.941 1.00 33.55  ? 90  ALA B N     1 
ATOM   1319 C CA    . ALA B 2 44  ? 1.553   -31.186 -26.173 1.00 35.15  ? 90  ALA B CA    1 
ATOM   1320 C C     . ALA B 2 44  ? 0.884   -31.489 -24.843 1.00 39.45  ? 90  ALA B C     1 
ATOM   1321 O O     . ALA B 2 44  ? 1.549   -31.940 -23.909 1.00 39.92  ? 90  ALA B O     1 
ATOM   1322 C CB    . ALA B 2 44  ? 2.031   -32.493 -26.813 1.00 32.18  ? 90  ALA B CB    1 
ATOM   1323 N N     . THR B 2 45  ? -0.431  -31.280 -24.771 1.00 38.28  ? 91  THR B N     1 
ATOM   1324 C CA    . THR B 2 45  ? -1.215  -31.535 -23.571 1.00 38.11  ? 91  THR B CA    1 
ATOM   1325 C C     . THR B 2 45  ? -2.208  -32.655 -23.851 1.00 43.69  ? 91  THR B C     1 
ATOM   1326 O O     . THR B 2 45  ? -3.008  -32.554 -24.784 1.00 45.74  ? 91  THR B O     1 
ATOM   1327 C CB    . THR B 2 45  ? -1.964  -30.281 -23.143 1.00 47.28  ? 91  THR B CB    1 
ATOM   1328 O OG1   . THR B 2 45  ? -1.032  -29.212 -22.935 1.00 44.40  ? 91  THR B OG1   1 
ATOM   1329 C CG2   . THR B 2 45  ? -2.763  -30.543 -21.867 1.00 48.18  ? 91  THR B CG2   1 
ATOM   1330 N N     . ARG B 2 46  ? -2.171  -33.703 -23.042 1.00 40.02  ? 92  ARG B N     1 
ATOM   1331 C CA    . ARG B 2 46  ? -3.117  -34.795 -23.176 1.00 40.50  ? 92  ARG B CA    1 
ATOM   1332 C C     . ARG B 2 46  ? -4.309  -34.578 -22.243 1.00 48.29  ? 92  ARG B C     1 
ATOM   1333 O O     . ARG B 2 46  ? -4.244  -33.804 -21.280 1.00 44.79  ? 92  ARG B O     1 
ATOM   1334 C CB    . ARG B 2 46  ? -2.431  -36.128 -22.888 1.00 41.11  ? 92  ARG B CB    1 
ATOM   1335 C CG    . ARG B 2 46  ? -1.021  -36.173 -23.437 1.00 44.60  ? 92  ARG B CG    1 
ATOM   1336 C CD    . ARG B 2 46  ? -0.407  -37.579 -23.591 1.00 43.50  ? 92  ARG B CD    1 
ATOM   1337 N NE    . ARG B 2 46  ? -0.135  -38.316 -22.354 1.00 50.81  ? 92  ARG B NE    1 
ATOM   1338 C CZ    . ARG B 2 46  ? 0.640   -37.906 -21.353 1.00 48.15  ? 92  ARG B CZ    1 
ATOM   1339 N NH1   . ARG B 2 46  ? 1.094   -36.666 -21.284 1.00 45.93  ? 92  ARG B NH1   1 
ATOM   1340 N NH2   . ARG B 2 46  ? 0.960   -38.761 -20.390 1.00 43.04  ? 92  ARG B NH2   1 
ATOM   1341 N N     . ARG B 2 47  ? -5.422  -35.245 -22.576 1.00 48.87  ? 93  ARG B N     1 
ATOM   1342 C CA    . ARG B 2 47  ? -6.633  -35.277 -21.762 1.00 44.95  ? 93  ARG B CA    1 
ATOM   1343 C C     . ARG B 2 47  ? -6.910  -36.712 -21.343 1.00 42.68  ? 93  ARG B C     1 
ATOM   1344 O O     . ARG B 2 47  ? -6.763  -37.635 -22.146 1.00 47.89  ? 93  ARG B O     1 
ATOM   1345 C CB    . ARG B 2 47  ? -7.847  -34.744 -22.520 1.00 49.50  ? 93  ARG B CB    1 
ATOM   1346 C CG    . ARG B 2 47  ? -7.617  -33.474 -23.314 1.00 55.13  ? 93  ARG B CG    1 
ATOM   1347 C CD    . ARG B 2 47  ? -8.009  -32.253 -22.523 1.00 54.74  ? 93  ARG B CD    1 
ATOM   1348 N NE    . ARG B 2 47  ? -9.423  -32.255 -22.167 1.00 53.34  ? 93  ARG B NE    1 
ATOM   1349 C CZ    . ARG B 2 47  ? -9.971  -31.438 -21.275 1.00 60.15  ? 93  ARG B CZ    1 
ATOM   1350 N NH1   . ARG B 2 47  ? -9.245  -30.543 -20.613 1.00 55.67  ? 93  ARG B NH1   1 
ATOM   1351 N NH2   . ARG B 2 47  ? -11.280 -31.520 -21.040 1.00 60.35  ? 93  ARG B NH2   1 
ATOM   1352 N N     . ILE B 2 48  ? -7.300  -36.903 -20.084 1.00 41.65  ? 94  ILE B N     1 
ATOM   1353 C CA    . ILE B 2 48  ? -7.772  -38.195 -19.598 1.00 49.01  ? 94  ILE B CA    1 
ATOM   1354 C C     . ILE B 2 48  ? -9.079  -37.980 -18.863 1.00 47.04  ? 94  ILE B C     1 
ATOM   1355 O O     . ILE B 2 48  ? -9.384  -36.881 -18.395 1.00 48.29  ? 94  ILE B O     1 
ATOM   1356 C CB    . ILE B 2 48  ? -6.801  -38.904 -18.635 1.00 40.46  ? 94  ILE B CB    1 
ATOM   1357 C CG1   . ILE B 2 48  ? -6.395  -37.952 -17.522 1.00 41.54  ? 94  ILE B CG1   1 
ATOM   1358 C CG2   . ILE B 2 48  ? -5.605  -39.453 -19.348 1.00 52.52  ? 94  ILE B CG2   1 
ATOM   1359 C CD1   . ILE B 2 48  ? -5.407  -38.572 -16.584 1.00 50.97  ? 94  ILE B CD1   1 
ATOM   1360 N N     . ARG B 2 49  ? -9.834  -39.062 -18.723 1.00 52.23  ? 95  ARG B N     1 
ATOM   1361 C CA    . ARG B 2 49  ? -10.986 -39.018 -17.834 1.00 54.79  ? 95  ARG B CA    1 
ATOM   1362 C C     . ARG B 2 49  ? -10.488 -39.032 -16.392 1.00 58.26  ? 95  ARG B C     1 
ATOM   1363 O O     . ARG B 2 49  ? -9.598  -39.813 -16.039 1.00 55.84  ? 95  ARG B O     1 
ATOM   1364 C CB    . ARG B 2 49  ? -11.922 -40.188 -18.110 1.00 53.21  ? 95  ARG B CB    1 
ATOM   1365 C CG    . ARG B 2 49  ? -13.387 -39.871 -17.853 1.00 62.01  ? 95  ARG B CG    1 
ATOM   1366 C CD    . ARG B 2 49  ? -14.253 -40.318 -19.026 1.00 64.20  ? 95  ARG B CD    1 
ATOM   1367 N NE    . ARG B 2 49  ? -15.052 -39.236 -19.593 1.00 63.67  ? 95  ARG B NE    1 
ATOM   1368 C CZ    . ARG B 2 49  ? -15.844 -39.366 -20.650 1.00 66.82  ? 95  ARG B CZ    1 
ATOM   1369 N NH1   . ARG B 2 49  ? -15.960 -40.521 -21.291 1.00 64.95  ? 95  ARG B NH1   1 
ATOM   1370 N NH2   . ARG B 2 49  ? -16.538 -38.312 -21.074 1.00 66.15  ? 95  ARG B NH2   1 
ATOM   1371 N N     . GLY B 2 50  ? -11.032 -38.141 -15.566 1.00 59.48  ? 96  GLY B N     1 
ATOM   1372 C CA    . GLY B 2 50  ? -10.589 -38.027 -14.193 1.00 59.10  ? 96  GLY B CA    1 
ATOM   1373 C C     . GLY B 2 50  ? -11.139 -39.119 -13.295 1.00 60.79  ? 96  GLY B C     1 
ATOM   1374 O O     . GLY B 2 50  ? -11.964 -39.945 -13.681 1.00 61.90  ? 96  GLY B O     1 
ATOM   1375 N N     . GLY B 2 51  ? -10.680 -39.098 -12.049 1.00 63.61  ? 97  GLY B N     1 
ATOM   1376 C CA    . GLY B 2 51  ? -11.197 -39.986 -11.028 1.00 66.39  ? 97  GLY B CA    1 
ATOM   1377 C C     . GLY B 2 51  ? -12.632 -39.663 -10.650 1.00 70.39  ? 97  GLY B C     1 
ATOM   1378 O O     . GLY B 2 51  ? -13.140 -40.119 -9.621  1.00 68.73  ? 97  GLY B O     1 
ATOM   1379 N N     . ASP B 2 52  ? -13.292 -38.852 -11.477 1.00 70.22  ? 98  ASP B N     1 
ATOM   1380 C CA    . ASP B 2 52  ? -14.708 -38.563 -11.309 1.00 66.60  ? 98  ASP B CA    1 
ATOM   1381 C C     . ASP B 2 52  ? -15.459 -38.611 -12.634 1.00 65.83  ? 98  ASP B C     1 
ATOM   1382 O O     . ASP B 2 52  ? -16.637 -38.247 -12.671 1.00 65.69  ? 98  ASP B O     1 
ATOM   1383 C CB    . ASP B 2 52  ? -14.899 -37.191 -10.643 1.00 68.98  ? 98  ASP B CB    1 
ATOM   1384 C CG    . ASP B 2 52  ? -14.142 -36.068 -11.364 1.00 78.54  ? 98  ASP B CG    1 
ATOM   1385 O OD1   . ASP B 2 52  ? -13.798 -36.224 -12.562 1.00 75.95  ? 98  ASP B OD1   1 
ATOM   1386 O OD2   . ASP B 2 52  ? -13.883 -35.020 -10.725 1.00 81.07  ? 98  ASP B OD2   1 
ATOM   1387 N N     . GLY B 2 53  ? -14.818 -39.036 -13.719 1.00 61.85  ? 99  GLY B N     1 
ATOM   1388 C CA    . GLY B 2 53  ? -15.454 -39.049 -15.017 1.00 66.04  ? 99  GLY B CA    1 
ATOM   1389 C C     . GLY B 2 53  ? -15.376 -37.745 -15.784 1.00 67.45  ? 99  GLY B C     1 
ATOM   1390 O O     . GLY B 2 53  ? -15.816 -37.698 -16.941 1.00 66.33  ? 99  GLY B O     1 
ATOM   1391 N N     . LYS B 2 54  ? -14.828 -36.689 -15.188 1.00 63.76  ? 100 LYS B N     1 
ATOM   1392 C CA    . LYS B 2 54  ? -14.639 -35.422 -15.881 1.00 64.61  ? 100 LYS B CA    1 
ATOM   1393 C C     . LYS B 2 54  ? -13.292 -35.430 -16.595 1.00 62.82  ? 100 LYS B C     1 
ATOM   1394 O O     . LYS B 2 54  ? -12.275 -35.788 -15.992 1.00 57.35  ? 100 LYS B O     1 
ATOM   1395 C CB    . LYS B 2 54  ? -14.709 -34.260 -14.890 1.00 67.40  ? 100 LYS B CB    1 
ATOM   1396 C CG    . LYS B 2 54  ? -16.002 -34.212 -14.081 1.00 72.91  ? 100 LYS B CG    1 
ATOM   1397 C CD    . LYS B 2 54  ? -15.813 -33.502 -12.739 1.00 75.08  ? 100 LYS B CD    1 
ATOM   1398 C CE    . LYS B 2 54  ? -15.337 -32.062 -12.894 1.00 80.12  ? 100 LYS B CE    1 
ATOM   1399 N NZ    . LYS B 2 54  ? -16.409 -31.131 -13.354 1.00 83.35  ? 100 LYS B NZ    1 
ATOM   1400 N N     . MET B 2 55  ? -13.289 -35.047 -17.877 1.00 59.07  ? 101 MET B N     1 
ATOM   1401 C CA    . MET B 2 55  ? -12.035 -34.920 -18.614 1.00 52.95  ? 101 MET B CA    1 
ATOM   1402 C C     . MET B 2 55  ? -11.167 -33.838 -17.985 1.00 55.35  ? 101 MET B C     1 
ATOM   1403 O O     . MET B 2 55  ? -11.662 -32.789 -17.569 1.00 56.83  ? 101 MET B O     1 
ATOM   1404 C CB    . MET B 2 55  ? -12.290 -34.575 -20.081 1.00 53.21  ? 101 MET B CB    1 
ATOM   1405 C CG    . MET B 2 55  ? -13.098 -35.588 -20.854 1.00 54.29  ? 101 MET B CG    1 
ATOM   1406 S SD    . MET B 2 55  ? -12.332 -37.209 -20.958 1.00 62.90  ? 101 MET B SD    1 
ATOM   1407 C CE    . MET B 2 55  ? -10.951 -36.884 -22.053 1.00 52.94  ? 101 MET B CE    1 
ATOM   1408 N N     . LYS B 2 56  ? -9.862  -34.095 -17.921 1.00 51.65  ? 102 LYS B N     1 
ATOM   1409 C CA    . LYS B 2 56  ? -8.933  -33.165 -17.294 1.00 52.71  ? 102 LYS B CA    1 
ATOM   1410 C C     . LYS B 2 56  ? -7.604  -33.192 -18.038 1.00 48.37  ? 102 LYS B C     1 
ATOM   1411 O O     . LYS B 2 56  ? -7.275  -34.154 -18.738 1.00 43.85  ? 102 LYS B O     1 
ATOM   1412 C CB    . LYS B 2 56  ? -8.718  -33.495 -15.808 1.00 47.46  ? 102 LYS B CB    1 
ATOM   1413 C CG    . LYS B 2 56  ? -8.092  -34.850 -15.543 1.00 48.71  ? 102 LYS B CG    1 
ATOM   1414 C CD    . LYS B 2 56  ? -7.388  -34.861 -14.203 1.00 51.17  ? 102 LYS B CD    1 
ATOM   1415 C CE    . LYS B 2 56  ? -6.749  -36.207 -13.925 1.00 54.25  ? 102 LYS B CE    1 
ATOM   1416 N NZ    . LYS B 2 56  ? -5.784  -36.167 -12.781 1.00 59.70  ? 102 LYS B NZ    1 
ATOM   1417 N N     . ASP B 2 57  ? -6.842  -32.114 -17.874 1.00 46.60  ? 103 ASP B N     1 
ATOM   1418 C CA    . ASP B 2 57  ? -5.538  -31.998 -18.517 1.00 50.62  ? 103 ASP B CA    1 
ATOM   1419 C C     . ASP B 2 57  ? -4.470  -32.748 -17.733 1.00 45.37  ? 103 ASP B C     1 
ATOM   1420 O O     . ASP B 2 57  ? -4.405  -32.669 -16.505 1.00 50.45  ? 103 ASP B O     1 
ATOM   1421 C CB    . ASP B 2 57  ? -5.121  -30.532 -18.644 1.00 50.18  ? 103 ASP B CB    1 
ATOM   1422 C CG    . ASP B 2 57  ? -5.856  -29.804 -19.755 1.00 56.25  ? 103 ASP B CG    1 
ATOM   1423 O OD1   . ASP B 2 57  ? -6.526  -30.485 -20.563 1.00 53.33  ? 103 ASP B OD1   1 
ATOM   1424 O OD2   . ASP B 2 57  ? -5.763  -28.551 -19.813 1.00 58.66  ? 103 ASP B OD2   1 
ATOM   1425 N N     . LEU B 2 58  ? -3.634  -33.480 -18.448 1.00 37.60  ? 104 LEU B N     1 
ATOM   1426 C CA    . LEU B 2 58  ? -2.389  -33.899 -17.838 1.00 42.72  ? 104 LEU B CA    1 
ATOM   1427 C C     . LEU B 2 58  ? -1.378  -32.751 -17.907 1.00 42.60  ? 104 LEU B C     1 
ATOM   1428 O O     . LEU B 2 58  ? -1.647  -31.699 -18.485 1.00 43.88  ? 104 LEU B O     1 
ATOM   1429 C CB    . LEU B 2 58  ? -1.866  -35.157 -18.526 1.00 44.44  ? 104 LEU B CB    1 
ATOM   1430 C CG    . LEU B 2 58  ? -2.726  -36.370 -18.194 1.00 40.97  ? 104 LEU B CG    1 
ATOM   1431 C CD1   . LEU B 2 58  ? -2.476  -37.477 -19.186 1.00 42.49  ? 104 LEU B CD1   1 
ATOM   1432 C CD2   . LEU B 2 58  ? -2.390  -36.811 -16.811 1.00 37.90  ? 104 LEU B CD2   1 
ATOM   1433 N N     . SER B 2 59  ? -0.212  -32.949 -17.292 1.00 43.57  ? 105 SER B N     1 
ATOM   1434 C CA    . SER B 2 59  ? 0.841   -31.943 -17.380 1.00 45.16  ? 105 SER B CA    1 
ATOM   1435 C C     . SER B 2 59  ? 1.305   -31.807 -18.824 1.00 38.16  ? 105 SER B C     1 
ATOM   1436 O O     . SER B 2 59  ? 1.473   -32.813 -19.517 1.00 42.61  ? 105 SER B O     1 
ATOM   1437 C CB    . SER B 2 59  ? 2.040   -32.300 -16.503 1.00 38.51  ? 105 SER B CB    1 
ATOM   1438 O OG    . SER B 2 59  ? 1.708   -32.176 -15.139 1.00 47.83  ? 105 SER B OG    1 
ATOM   1439 N N     . PRO B 2 60  ? 1.509   -30.591 -19.309 1.00 39.19  ? 106 PRO B N     1 
ATOM   1440 C CA    . PRO B 2 60  ? 2.020   -30.417 -20.671 1.00 40.47  ? 106 PRO B CA    1 
ATOM   1441 C C     . PRO B 2 60  ? 3.391   -31.051 -20.830 1.00 38.24  ? 106 PRO B C     1 
ATOM   1442 O O     . PRO B 2 60  ? 4.228   -31.007 -19.929 1.00 38.65  ? 106 PRO B O     1 
ATOM   1443 C CB    . PRO B 2 60  ? 2.091   -28.896 -20.831 1.00 42.87  ? 106 PRO B CB    1 
ATOM   1444 C CG    . PRO B 2 60  ? 1.174   -28.358 -19.790 1.00 44.11  ? 106 PRO B CG    1 
ATOM   1445 C CD    . PRO B 2 60  ? 1.256   -29.305 -18.646 1.00 43.07  ? 106 PRO B CD    1 
ATOM   1446 N N     . ARG B 2 61  ? 3.606   -31.647 -21.995 1.00 38.85  ? 107 ARG B N     1 
ATOM   1447 C CA    . ARG B 2 61  ? 4.908   -32.130 -22.415 1.00 34.28  ? 107 ARG B CA    1 
ATOM   1448 C C     . ARG B 2 61  ? 5.393   -31.262 -23.563 1.00 34.54  ? 107 ARG B C     1 
ATOM   1449 O O     . ARG B 2 61  ? 4.616   -30.896 -24.449 1.00 33.65  ? 107 ARG B O     1 
ATOM   1450 C CB    . ARG B 2 61  ? 4.858   -33.590 -22.866 1.00 33.07  ? 107 ARG B CB    1 
ATOM   1451 C CG    . ARG B 2 61  ? 3.802   -34.410 -22.174 1.00 43.70  ? 107 ARG B CG    1 
ATOM   1452 C CD    . ARG B 2 61  ? 4.418   -35.336 -21.187 1.00 43.99  ? 107 ARG B CD    1 
ATOM   1453 N NE    . ARG B 2 61  ? 5.324   -36.275 -21.830 1.00 53.86  ? 107 ARG B NE    1 
ATOM   1454 C CZ    . ARG B 2 61  ? 5.030   -37.532 -22.148 1.00 52.79  ? 107 ARG B CZ    1 
ATOM   1455 N NH1   . ARG B 2 61  ? 3.836   -38.048 -21.911 1.00 36.81  ? 107 ARG B NH1   1 
ATOM   1456 N NH2   . ARG B 2 61  ? 5.970   -38.294 -22.715 1.00 53.46  ? 107 ARG B NH2   1 
ATOM   1457 N N     . TRP B 2 62  ? 6.678   -30.924 -23.533 1.00 33.75  ? 108 TRP B N     1 
ATOM   1458 C CA    . TRP B 2 62  ? 7.316   -30.156 -24.586 1.00 26.84  ? 108 TRP B CA    1 
ATOM   1459 C C     . TRP B 2 62  ? 8.315   -31.069 -25.288 1.00 32.09  ? 108 TRP B C     1 
ATOM   1460 O O     . TRP B 2 62  ? 9.147   -31.706 -24.630 1.00 30.67  ? 108 TRP B O     1 
ATOM   1461 C CB    . TRP B 2 62  ? 8.016   -28.932 -24.002 1.00 31.33  ? 108 TRP B CB    1 
ATOM   1462 C CG    . TRP B 2 62  ? 7.119   -27.928 -23.350 1.00 33.42  ? 108 TRP B CG    1 
ATOM   1463 C CD1   . TRP B 2 62  ? 6.536   -28.020 -22.118 1.00 36.40  ? 108 TRP B CD1   1 
ATOM   1464 C CD2   . TRP B 2 62  ? 6.721   -26.661 -23.887 1.00 32.73  ? 108 TRP B CD2   1 
ATOM   1465 N NE1   . TRP B 2 62  ? 5.798   -26.888 -21.854 1.00 34.92  ? 108 TRP B NE1   1 
ATOM   1466 C CE2   . TRP B 2 62  ? 5.897   -26.039 -22.925 1.00 37.95  ? 108 TRP B CE2   1 
ATOM   1467 C CE3   . TRP B 2 62  ? 6.986   -25.989 -25.081 1.00 28.98  ? 108 TRP B CE3   1 
ATOM   1468 C CZ2   . TRP B 2 62  ? 5.332   -24.778 -23.131 1.00 38.55  ? 108 TRP B CZ2   1 
ATOM   1469 C CZ3   . TRP B 2 62  ? 6.432   -24.750 -25.279 1.00 31.40  ? 108 TRP B CZ3   1 
ATOM   1470 C CH2   . TRP B 2 62  ? 5.606   -24.156 -24.313 1.00 36.24  ? 108 TRP B CH2   1 
ATOM   1471 N N     . TYR B 2 63  ? 8.233   -31.145 -26.611 1.00 30.71  ? 109 TYR B N     1 
ATOM   1472 C CA    . TYR B 2 63  ? 9.115   -31.994 -27.402 1.00 24.36  ? 109 TYR B CA    1 
ATOM   1473 C C     . TYR B 2 63  ? 9.950   -31.130 -28.325 1.00 29.97  ? 109 TYR B C     1 
ATOM   1474 O O     . TYR B 2 63  ? 9.413   -30.236 -28.983 1.00 29.50  ? 109 TYR B O     1 
ATOM   1475 C CB    . TYR B 2 63  ? 8.338   -32.982 -28.263 1.00 28.86  ? 109 TYR B CB    1 
ATOM   1476 C CG    . TYR B 2 63  ? 7.556   -34.049 -27.530 1.00 31.53  ? 109 TYR B CG    1 
ATOM   1477 C CD1   . TYR B 2 63  ? 6.255   -33.805 -27.044 1.00 27.76  ? 109 TYR B CD1   1 
ATOM   1478 C CD2   . TYR B 2 63  ? 8.090   -35.317 -27.375 1.00 28.29  ? 109 TYR B CD2   1 
ATOM   1479 C CE1   . TYR B 2 63  ? 5.546   -34.817 -26.403 1.00 27.84  ? 109 TYR B CE1   1 
ATOM   1480 C CE2   . TYR B 2 63  ? 7.404   -36.319 -26.736 1.00 34.96  ? 109 TYR B CE2   1 
ATOM   1481 C CZ    . TYR B 2 63  ? 6.126   -36.067 -26.262 1.00 35.90  ? 109 TYR B CZ    1 
ATOM   1482 O OH    . TYR B 2 63  ? 5.473   -37.087 -25.643 1.00 41.66  ? 109 TYR B OH    1 
ATOM   1483 N N     . PHE B 2 64  ? 11.260  -31.417 -28.403 1.00 29.82  ? 110 PHE B N     1 
ATOM   1484 C CA    . PHE B 2 64  ? 12.132  -30.687 -29.314 1.00 28.82  ? 110 PHE B CA    1 
ATOM   1485 C C     . PHE B 2 64  ? 12.019  -31.208 -30.737 1.00 27.74  ? 110 PHE B C     1 
ATOM   1486 O O     . PHE B 2 64  ? 12.017  -32.417 -30.973 1.00 30.02  ? 110 PHE B O     1 
ATOM   1487 C CB    . PHE B 2 64  ? 13.597  -30.771 -28.875 1.00 30.96  ? 110 PHE B CB    1 
ATOM   1488 C CG    . PHE B 2 64  ? 14.512  -30.011 -29.768 1.00 32.40  ? 110 PHE B CG    1 
ATOM   1489 C CD1   . PHE B 2 64  ? 14.675  -28.650 -29.605 1.00 34.43  ? 110 PHE B CD1   1 
ATOM   1490 C CD2   . PHE B 2 64  ? 15.187  -30.643 -30.792 1.00 35.74  ? 110 PHE B CD2   1 
ATOM   1491 C CE1   . PHE B 2 64  ? 15.497  -27.935 -30.425 1.00 33.09  ? 110 PHE B CE1   1 
ATOM   1492 C CE2   . PHE B 2 64  ? 16.013  -29.927 -31.634 1.00 36.45  ? 110 PHE B CE2   1 
ATOM   1493 C CZ    . PHE B 2 64  ? 16.161  -28.569 -31.454 1.00 35.84  ? 110 PHE B CZ    1 
ATOM   1494 N N     . TYR B 2 65  ? 11.935  -30.287 -31.689 1.00 27.65  ? 111 TYR B N     1 
ATOM   1495 C CA    . TYR B 2 65  ? 12.065  -30.585 -33.108 1.00 27.73  ? 111 TYR B CA    1 
ATOM   1496 C C     . TYR B 2 65  ? 13.063  -29.617 -33.737 1.00 35.91  ? 111 TYR B C     1 
ATOM   1497 O O     . TYR B 2 65  ? 13.024  -28.413 -33.464 1.00 34.80  ? 111 TYR B O     1 
ATOM   1498 C CB    . TYR B 2 65  ? 10.741  -30.457 -33.829 1.00 33.80  ? 111 TYR B CB    1 
ATOM   1499 C CG    . TYR B 2 65  ? 9.673   -31.415 -33.364 1.00 33.45  ? 111 TYR B CG    1 
ATOM   1500 C CD1   . TYR B 2 65  ? 9.518   -32.643 -33.974 1.00 31.98  ? 111 TYR B CD1   1 
ATOM   1501 C CD2   . TYR B 2 65  ? 8.799   -31.073 -32.339 1.00 30.93  ? 111 TYR B CD2   1 
ATOM   1502 C CE1   . TYR B 2 65  ? 8.527   -33.518 -33.572 1.00 34.06  ? 111 TYR B CE1   1 
ATOM   1503 C CE2   . TYR B 2 65  ? 7.786   -31.946 -31.934 1.00 31.23  ? 111 TYR B CE2   1 
ATOM   1504 C CZ    . TYR B 2 65  ? 7.670   -33.170 -32.549 1.00 29.01  ? 111 TYR B CZ    1 
ATOM   1505 O OH    . TYR B 2 65  ? 6.695   -34.062 -32.162 1.00 34.65  ? 111 TYR B OH    1 
ATOM   1506 N N     . TYR B 2 66  ? 13.957  -30.132 -34.581 1.00 36.99  ? 112 TYR B N     1 
ATOM   1507 C CA    . TYR B 2 66  ? 14.904  -29.241 -35.238 1.00 38.48  ? 112 TYR B CA    1 
ATOM   1508 C C     . TYR B 2 66  ? 14.155  -28.307 -36.179 1.00 40.87  ? 112 TYR B C     1 
ATOM   1509 O O     . TYR B 2 66  ? 13.075  -28.637 -36.679 1.00 41.06  ? 112 TYR B O     1 
ATOM   1510 C CB    . TYR B 2 66  ? 15.966  -30.027 -36.014 1.00 37.73  ? 112 TYR B CB    1 
ATOM   1511 C CG    . TYR B 2 66  ? 16.983  -30.711 -35.130 1.00 38.74  ? 112 TYR B CG    1 
ATOM   1512 C CD1   . TYR B 2 66  ? 16.775  -31.999 -34.684 1.00 34.97  ? 112 TYR B CD1   1 
ATOM   1513 C CD2   . TYR B 2 66  ? 18.159  -30.068 -34.755 1.00 35.21  ? 112 TYR B CD2   1 
ATOM   1514 C CE1   . TYR B 2 66  ? 17.690  -32.627 -33.879 1.00 39.40  ? 112 TYR B CE1   1 
ATOM   1515 C CE2   . TYR B 2 66  ? 19.085  -30.691 -33.931 1.00 35.73  ? 112 TYR B CE2   1 
ATOM   1516 C CZ    . TYR B 2 66  ? 18.848  -31.969 -33.506 1.00 36.93  ? 112 TYR B CZ    1 
ATOM   1517 O OH    . TYR B 2 66  ? 19.744  -32.608 -32.692 1.00 42.81  ? 112 TYR B OH    1 
ATOM   1518 N N     . LEU B 2 67  ? 14.743  -27.133 -36.420 1.00 41.06  ? 113 LEU B N     1 
ATOM   1519 C CA    . LEU B 2 67  ? 14.116  -26.139 -37.283 1.00 36.71  ? 113 LEU B CA    1 
ATOM   1520 C C     . LEU B 2 67  ? 13.777  -26.739 -38.643 1.00 40.64  ? 113 LEU B C     1 
ATOM   1521 O O     . LEU B 2 67  ? 14.529  -27.542 -39.192 1.00 40.78  ? 113 LEU B O     1 
ATOM   1522 C CB    . LEU B 2 67  ? 15.047  -24.933 -37.439 1.00 37.67  ? 113 LEU B CB    1 
ATOM   1523 C CG    . LEU B 2 67  ? 14.704  -23.975 -38.579 1.00 41.50  ? 113 LEU B CG    1 
ATOM   1524 C CD1   . LEU B 2 67  ? 13.373  -23.278 -38.321 1.00 38.64  ? 113 LEU B CD1   1 
ATOM   1525 C CD2   . LEU B 2 67  ? 15.840  -22.980 -38.805 1.00 42.37  ? 113 LEU B CD2   1 
ATOM   1526 N N     . GLY B 2 68  ? 12.604  -26.401 -39.161 1.00 40.46  ? 114 GLY B N     1 
ATOM   1527 C CA    . GLY B 2 68  ? 12.217  -26.927 -40.450 1.00 42.62  ? 114 GLY B CA    1 
ATOM   1528 C C     . GLY B 2 68  ? 11.774  -28.372 -40.450 1.00 47.84  ? 114 GLY B C     1 
ATOM   1529 O O     . GLY B 2 68  ? 11.622  -28.962 -41.530 1.00 48.84  ? 114 GLY B O     1 
ATOM   1530 N N     . THR B 2 69  ? 11.565  -28.966 -39.282 1.00 45.89  ? 115 THR B N     1 
ATOM   1531 C CA    . THR B 2 69  ? 11.094  -30.336 -39.161 1.00 44.03  ? 115 THR B CA    1 
ATOM   1532 C C     . THR B 2 69  ? 9.828   -30.360 -38.310 1.00 42.07  ? 115 THR B C     1 
ATOM   1533 O O     . THR B 2 69  ? 9.438   -29.352 -37.725 1.00 42.72  ? 115 THR B O     1 
ATOM   1534 C CB    . THR B 2 69  ? 12.171  -31.231 -38.534 1.00 41.35  ? 115 THR B CB    1 
ATOM   1535 O OG1   . THR B 2 69  ? 12.330  -30.879 -37.156 1.00 41.19  ? 115 THR B OG1   1 
ATOM   1536 C CG2   . THR B 2 69  ? 13.507  -31.048 -39.240 1.00 45.71  ? 115 THR B CG2   1 
ATOM   1537 N N     . GLY B 2 70  ? 9.182   -31.524 -38.258 1.00 36.29  ? 116 GLY B N     1 
ATOM   1538 C CA    . GLY B 2 70  ? 8.146   -31.797 -37.295 1.00 38.43  ? 116 GLY B CA    1 
ATOM   1539 C C     . GLY B 2 70  ? 6.819   -31.133 -37.616 1.00 42.71  ? 116 GLY B C     1 
ATOM   1540 O O     . GLY B 2 70  ? 6.593   -30.645 -38.727 1.00 46.77  ? 116 GLY B O     1 
ATOM   1541 N N     . PRO B 2 71  ? 5.921   -31.084 -36.629 1.00 35.12  ? 117 PRO B N     1 
ATOM   1542 C CA    . PRO B 2 71  ? 4.579   -30.544 -36.886 1.00 35.93  ? 117 PRO B CA    1 
ATOM   1543 C C     . PRO B 2 71  ? 4.597   -29.122 -37.397 1.00 39.04  ? 117 PRO B C     1 
ATOM   1544 O O     . PRO B 2 71  ? 3.696   -28.733 -38.149 1.00 39.02  ? 117 PRO B O     1 
ATOM   1545 C CB    . PRO B 2 71  ? 3.900   -30.640 -35.516 1.00 36.05  ? 117 PRO B CB    1 
ATOM   1546 C CG    . PRO B 2 71  ? 4.683   -31.704 -34.772 1.00 36.66  ? 117 PRO B CG    1 
ATOM   1547 C CD    . PRO B 2 71  ? 6.085   -31.519 -35.234 1.00 36.19  ? 117 PRO B CD    1 
ATOM   1548 N N     . GLU B 2 72  ? 5.607   -28.341 -37.023 1.00 39.23  ? 118 GLU B N     1 
ATOM   1549 C CA    . GLU B 2 72  ? 5.733   -26.945 -37.416 1.00 38.26  ? 118 GLU B CA    1 
ATOM   1550 C C     . GLU B 2 72  ? 6.918   -26.735 -38.356 1.00 37.66  ? 118 GLU B C     1 
ATOM   1551 O O     . GLU B 2 72  ? 7.671   -25.772 -38.233 1.00 38.49  ? 118 GLU B O     1 
ATOM   1552 C CB    . GLU B 2 72  ? 5.860   -26.053 -36.190 1.00 32.02  ? 118 GLU B CB    1 
ATOM   1553 C CG    . GLU B 2 72  ? 4.621   -26.013 -35.335 1.00 37.36  ? 118 GLU B CG    1 
ATOM   1554 C CD    . GLU B 2 72  ? 3.408   -25.473 -36.075 1.00 47.43  ? 118 GLU B CD    1 
ATOM   1555 O OE1   . GLU B 2 72  ? 3.583   -24.695 -37.040 1.00 48.42  ? 118 GLU B OE1   1 
ATOM   1556 O OE2   . GLU B 2 72  ? 2.273   -25.831 -35.687 1.00 47.80  ? 118 GLU B OE2   1 
ATOM   1557 N N     . ALA B 2 73  ? 7.095   -27.640 -39.311 1.00 41.63  ? 119 ALA B N     1 
ATOM   1558 C CA    . ALA B 2 73  ? 8.214   -27.518 -40.239 1.00 44.52  ? 119 ALA B CA    1 
ATOM   1559 C C     . ALA B 2 73  ? 8.081   -26.306 -41.158 1.00 40.81  ? 119 ALA B C     1 
ATOM   1560 O O     . ALA B 2 73  ? 9.080   -25.877 -41.743 1.00 44.79  ? 119 ALA B O     1 
ATOM   1561 C CB    . ALA B 2 73  ? 8.347   -28.801 -41.059 1.00 43.03  ? 119 ALA B CB    1 
ATOM   1562 N N     . GLY B 2 74  ? 6.881   -25.736 -41.294 1.00 39.25  ? 120 GLY B N     1 
ATOM   1563 C CA    . GLY B 2 74  ? 6.738   -24.546 -42.114 1.00 44.11  ? 120 GLY B CA    1 
ATOM   1564 C C     . GLY B 2 74  ? 7.237   -23.274 -41.455 1.00 47.82  ? 120 GLY B C     1 
ATOM   1565 O O     . GLY B 2 74  ? 7.621   -22.322 -42.143 1.00 46.79  ? 120 GLY B O     1 
ATOM   1566 N N     . LEU B 2 75  ? 7.251   -23.231 -40.134 1.00 44.97  ? 121 LEU B N     1 
ATOM   1567 C CA    . LEU B 2 75  ? 7.523   -21.978 -39.462 1.00 41.72  ? 121 LEU B CA    1 
ATOM   1568 C C     . LEU B 2 75  ? 8.998   -21.612 -39.577 1.00 39.87  ? 121 LEU B C     1 
ATOM   1569 O O     . LEU B 2 75  ? 9.870   -22.476 -39.438 1.00 42.71  ? 121 LEU B O     1 
ATOM   1570 C CB    . LEU B 2 75  ? 7.115   -22.066 -37.999 1.00 43.84  ? 121 LEU B CB    1 
ATOM   1571 C CG    . LEU B 2 75  ? 5.610   -22.252 -37.749 1.00 43.39  ? 121 LEU B CG    1 
ATOM   1572 C CD1   . LEU B 2 75  ? 5.323   -22.035 -36.270 1.00 40.24  ? 121 LEU B CD1   1 
ATOM   1573 C CD2   . LEU B 2 75  ? 4.745   -21.335 -38.617 1.00 42.56  ? 121 LEU B CD2   1 
ATOM   1574 N N     . PRO B 2 76  ? 9.312   -20.351 -39.851 1.00 42.12  ? 122 PRO B N     1 
ATOM   1575 C CA    . PRO B 2 76  ? 10.691  -19.875 -39.693 1.00 39.40  ? 122 PRO B CA    1 
ATOM   1576 C C     . PRO B 2 76  ? 11.038  -19.719 -38.225 1.00 40.70  ? 122 PRO B C     1 
ATOM   1577 O O     . PRO B 2 76  ? 10.162  -19.696 -37.356 1.00 44.20  ? 122 PRO B O     1 
ATOM   1578 C CB    . PRO B 2 76  ? 10.691  -18.518 -40.396 1.00 36.68  ? 122 PRO B CB    1 
ATOM   1579 C CG    . PRO B 2 76  ? 9.214   -18.073 -40.338 1.00 40.73  ? 122 PRO B CG    1 
ATOM   1580 C CD    . PRO B 2 76  ? 8.417   -19.338 -40.443 1.00 40.97  ? 122 PRO B CD    1 
ATOM   1581 N N     . TYR B 2 77  ? 12.337  -19.600 -37.955 1.00 40.16  ? 123 TYR B N     1 
ATOM   1582 C CA    . TYR B 2 77  ? 12.804  -19.373 -36.592 1.00 38.89  ? 123 TYR B CA    1 
ATOM   1583 C C     . TYR B 2 77  ? 12.112  -18.156 -35.996 1.00 40.03  ? 123 TYR B C     1 
ATOM   1584 O O     . TYR B 2 77  ? 11.896  -17.155 -36.678 1.00 46.87  ? 123 TYR B O     1 
ATOM   1585 C CB    . TYR B 2 77  ? 14.322  -19.159 -36.568 1.00 36.79  ? 123 TYR B CB    1 
ATOM   1586 C CG    . TYR B 2 77  ? 14.869  -19.169 -35.167 1.00 38.14  ? 123 TYR B CG    1 
ATOM   1587 C CD1   . TYR B 2 77  ? 15.048  -20.368 -34.488 1.00 38.10  ? 123 TYR B CD1   1 
ATOM   1588 C CD2   . TYR B 2 77  ? 15.162  -17.990 -34.497 1.00 37.41  ? 123 TYR B CD2   1 
ATOM   1589 C CE1   . TYR B 2 77  ? 15.522  -20.403 -33.197 1.00 34.57  ? 123 TYR B CE1   1 
ATOM   1590 C CE2   . TYR B 2 77  ? 15.639  -18.015 -33.181 1.00 35.37  ? 123 TYR B CE2   1 
ATOM   1591 C CZ    . TYR B 2 77  ? 15.816  -19.228 -32.545 1.00 37.46  ? 123 TYR B CZ    1 
ATOM   1592 O OH    . TYR B 2 77  ? 16.292  -19.290 -31.246 1.00 39.57  ? 123 TYR B OH    1 
ATOM   1593 N N     . GLY B 2 78  ? 11.721  -18.256 -34.730 1.00 41.08  ? 124 GLY B N     1 
ATOM   1594 C CA    . GLY B 2 78  ? 11.049  -17.156 -34.055 1.00 35.53  ? 124 GLY B CA    1 
ATOM   1595 C C     . GLY B 2 78  ? 9.577   -16.944 -34.383 1.00 39.46  ? 124 GLY B C     1 
ATOM   1596 O O     . GLY B 2 78  ? 8.981   -15.997 -33.853 1.00 37.08  ? 124 GLY B O     1 
ATOM   1597 N N     . ALA B 2 79  ? 8.956   -17.796 -35.204 1.00 36.73  ? 125 ALA B N     1 
ATOM   1598 C CA    . ALA B 2 79  ? 7.556   -17.584 -35.555 1.00 42.39  ? 125 ALA B CA    1 
ATOM   1599 C C     . ALA B 2 79  ? 6.715   -17.478 -34.291 1.00 38.68  ? 125 ALA B C     1 
ATOM   1600 O O     . ALA B 2 79  ? 7.034   -18.084 -33.268 1.00 38.89  ? 125 ALA B O     1 
ATOM   1601 C CB    . ALA B 2 79  ? 7.031   -18.716 -36.443 1.00 38.98  ? 125 ALA B CB    1 
ATOM   1602 N N     . ASN B 2 80  ? 5.669   -16.651 -34.358 1.00 36.30  ? 126 ASN B N     1 
ATOM   1603 C CA    . ASN B 2 80  ? 4.760   -16.417 -33.239 1.00 36.74  ? 126 ASN B CA    1 
ATOM   1604 C C     . ASN B 2 80  ? 3.601   -17.394 -33.340 1.00 38.56  ? 126 ASN B C     1 
ATOM   1605 O O     . ASN B 2 80  ? 2.686   -17.199 -34.151 1.00 36.33  ? 126 ASN B O     1 
ATOM   1606 C CB    . ASN B 2 80  ? 4.236   -14.983 -33.239 1.00 40.34  ? 126 ASN B CB    1 
ATOM   1607 C CG    . ASN B 2 80  ? 2.962   -14.817 -32.391 1.00 43.26  ? 126 ASN B CG    1 
ATOM   1608 O OD1   . ASN B 2 80  ? 2.787   -15.474 -31.358 1.00 41.92  ? 126 ASN B OD1   1 
ATOM   1609 N ND2   . ASN B 2 80  ? 2.082   -13.913 -32.818 1.00 42.83  ? 126 ASN B ND2   1 
ATOM   1610 N N     . LYS B 2 81  ? 3.622   -18.417 -32.486 1.00 35.05  ? 127 LYS B N     1 
ATOM   1611 C CA    . LYS B 2 81  ? 2.579   -19.430 -32.468 1.00 34.14  ? 127 LYS B CA    1 
ATOM   1612 C C     . LYS B 2 81  ? 2.479   -19.990 -31.059 1.00 39.04  ? 127 LYS B C     1 
ATOM   1613 O O     . LYS B 2 81  ? 3.485   -20.394 -30.470 1.00 32.00  ? 127 LYS B O     1 
ATOM   1614 C CB    . LYS B 2 81  ? 2.873   -20.547 -33.477 1.00 39.45  ? 127 LYS B CB    1 
ATOM   1615 C CG    . LYS B 2 81  ? 1.950   -21.745 -33.375 1.00 42.62  ? 127 LYS B CG    1 
ATOM   1616 C CD    . LYS B 2 81  ? 1.068   -21.900 -34.596 1.00 46.23  ? 127 LYS B CD    1 
ATOM   1617 C CE    . LYS B 2 81  ? 0.217   -23.150 -34.473 1.00 47.91  ? 127 LYS B CE    1 
ATOM   1618 N NZ    . LYS B 2 81  ? -0.439  -23.233 -33.122 1.00 54.62  ? 127 LYS B NZ    1 
ATOM   1619 N N     . ASP B 2 82  ? 1.266   -20.007 -30.525 1.00 39.62  ? 128 ASP B N     1 
ATOM   1620 C CA    . ASP B 2 82  ? 1.059   -20.415 -29.145 1.00 39.05  ? 128 ASP B CA    1 
ATOM   1621 C C     . ASP B 2 82  ? 1.490   -21.859 -28.942 1.00 38.20  ? 128 ASP B C     1 
ATOM   1622 O O     . ASP B 2 82  ? 1.126   -22.740 -29.726 1.00 37.68  ? 128 ASP B O     1 
ATOM   1623 C CB    . ASP B 2 82  ? -0.413  -20.240 -28.790 1.00 48.78  ? 128 ASP B CB    1 
ATOM   1624 C CG    . ASP B 2 82  ? -0.816  -21.035 -27.574 1.00 56.11  ? 128 ASP B CG    1 
ATOM   1625 O OD1   . ASP B 2 82  ? -0.294  -20.730 -26.471 1.00 53.47  ? 128 ASP B OD1   1 
ATOM   1626 O OD2   . ASP B 2 82  ? -1.663  -21.954 -27.731 1.00 58.54  ? 128 ASP B OD2   1 
ATOM   1627 N N     . GLY B 2 83  ? 2.267   -22.100 -27.882 1.00 36.24  ? 129 GLY B N     1 
ATOM   1628 C CA    . GLY B 2 83  ? 2.759   -23.432 -27.579 1.00 31.47  ? 129 GLY B CA    1 
ATOM   1629 C C     . GLY B 2 83  ? 4.031   -23.814 -28.310 1.00 37.17  ? 129 GLY B C     1 
ATOM   1630 O O     . GLY B 2 83  ? 4.384   -25.002 -28.337 1.00 33.24  ? 129 GLY B O     1 
ATOM   1631 N N     . ILE B 2 84  ? 4.710   -22.850 -28.929 1.00 33.62  ? 130 ILE B N     1 
ATOM   1632 C CA    . ILE B 2 84  ? 5.965   -23.064 -29.631 1.00 31.68  ? 130 ILE B CA    1 
ATOM   1633 C C     . ILE B 2 84  ? 6.972   -22.082 -29.063 1.00 30.87  ? 130 ILE B C     1 
ATOM   1634 O O     . ILE B 2 84  ? 6.694   -20.885 -29.013 1.00 31.91  ? 130 ILE B O     1 
ATOM   1635 C CB    . ILE B 2 84  ? 5.826   -22.836 -31.146 1.00 35.51  ? 130 ILE B CB    1 
ATOM   1636 C CG1   . ILE B 2 84  ? 4.807   -23.787 -31.774 1.00 28.42  ? 130 ILE B CG1   1 
ATOM   1637 C CG2   . ILE B 2 84  ? 7.214   -22.901 -31.821 1.00 33.95  ? 130 ILE B CG2   1 
ATOM   1638 C CD1   . ILE B 2 84  ? 5.228   -25.177 -31.846 1.00 29.39  ? 130 ILE B CD1   1 
ATOM   1639 N N     . ILE B 2 85  ? 8.128   -22.577 -28.631 1.00 31.28  ? 131 ILE B N     1 
ATOM   1640 C CA    . ILE B 2 85  ? 9.224   -21.710 -28.207 1.00 32.59  ? 131 ILE B CA    1 
ATOM   1641 C C     . ILE B 2 85  ? 10.498  -22.136 -28.920 1.00 32.67  ? 131 ILE B C     1 
ATOM   1642 O O     . ILE B 2 85  ? 10.641  -23.292 -29.325 1.00 33.21  ? 131 ILE B O     1 
ATOM   1643 C CB    . ILE B 2 85  ? 9.420   -21.715 -26.671 1.00 35.54  ? 131 ILE B CB    1 
ATOM   1644 C CG1   . ILE B 2 85  ? 9.829   -23.097 -26.148 1.00 34.47  ? 131 ILE B CG1   1 
ATOM   1645 C CG2   . ILE B 2 85  ? 8.144   -21.215 -25.974 1.00 34.45  ? 131 ILE B CG2   1 
ATOM   1646 C CD1   . ILE B 2 85  ? 11.258  -23.217 -25.712 1.00 30.49  ? 131 ILE B CD1   1 
ATOM   1647 N N     . TRP B 2 86  ? 11.429  -21.192 -29.073 1.00 34.15  ? 132 TRP B N     1 
ATOM   1648 C CA    . TRP B 2 86  ? 12.544  -21.318 -29.999 1.00 33.02  ? 132 TRP B CA    1 
ATOM   1649 C C     . TRP B 2 86  ? 13.862  -21.328 -29.247 1.00 34.61  ? 132 TRP B C     1 
ATOM   1650 O O     . TRP B 2 86  ? 14.066  -20.535 -28.331 1.00 37.55  ? 132 TRP B O     1 
ATOM   1651 C CB    . TRP B 2 86  ? 12.544  -20.175 -31.028 1.00 30.92  ? 132 TRP B CB    1 
ATOM   1652 C CG    . TRP B 2 86  ? 11.368  -20.252 -31.911 1.00 34.37  ? 132 TRP B CG    1 
ATOM   1653 C CD1   . TRP B 2 86  ? 10.198  -19.589 -31.757 1.00 33.19  ? 132 TRP B CD1   1 
ATOM   1654 C CD2   . TRP B 2 86  ? 11.211  -21.086 -33.077 1.00 34.11  ? 132 TRP B CD2   1 
ATOM   1655 N NE1   . TRP B 2 86  ? 9.320   -19.937 -32.763 1.00 35.89  ? 132 TRP B NE1   1 
ATOM   1656 C CE2   . TRP B 2 86  ? 9.920   -20.862 -33.578 1.00 34.78  ? 132 TRP B CE2   1 
ATOM   1657 C CE3   . TRP B 2 86  ? 12.036  -22.002 -33.732 1.00 33.99  ? 132 TRP B CE3   1 
ATOM   1658 C CZ2   . TRP B 2 86  ? 9.431   -21.515 -34.706 1.00 38.25  ? 132 TRP B CZ2   1 
ATOM   1659 C CZ3   . TRP B 2 86  ? 11.560  -22.635 -34.863 1.00 36.11  ? 132 TRP B CZ3   1 
ATOM   1660 C CH2   . TRP B 2 86  ? 10.266  -22.389 -35.339 1.00 36.30  ? 132 TRP B CH2   1 
ATOM   1661 N N     . VAL B 2 87  ? 14.756  -22.229 -29.637 1.00 35.32  ? 133 VAL B N     1 
ATOM   1662 C CA    . VAL B 2 87  ? 16.100  -22.295 -29.073 1.00 35.47  ? 133 VAL B CA    1 
ATOM   1663 C C     . VAL B 2 87  ? 17.099  -22.418 -30.210 1.00 35.33  ? 133 VAL B C     1 
ATOM   1664 O O     . VAL B 2 87  ? 16.811  -23.010 -31.259 1.00 29.70  ? 133 VAL B O     1 
ATOM   1665 C CB    . VAL B 2 87  ? 16.286  -23.466 -28.077 1.00 36.84  ? 133 VAL B CB    1 
ATOM   1666 C CG1   . VAL B 2 87  ? 15.447  -23.251 -26.842 1.00 39.20  ? 133 VAL B CG1   1 
ATOM   1667 C CG2   . VAL B 2 87  ? 15.935  -24.779 -28.732 1.00 38.18  ? 133 VAL B CG2   1 
ATOM   1668 N N     . ALA B 2 88  ? 18.288  -21.844 -29.995 1.00 42.07  ? 134 ALA B N     1 
ATOM   1669 C CA    . ALA B 2 88  ? 19.327  -21.831 -31.013 1.00 40.23  ? 134 ALA B CA    1 
ATOM   1670 C C     . ALA B 2 88  ? 20.675  -21.754 -30.329 1.00 48.47  ? 134 ALA B C     1 
ATOM   1671 O O     . ALA B 2 88  ? 20.812  -21.133 -29.277 1.00 47.78  ? 134 ALA B O     1 
ATOM   1672 C CB    . ALA B 2 88  ? 19.181  -20.663 -31.998 1.00 38.98  ? 134 ALA B CB    1 
ATOM   1673 N N     . THR B 2 89  ? 21.658  -22.413 -30.936 1.00 51.43  ? 135 THR B N     1 
ATOM   1674 C CA    . THR B 2 89  ? 23.040  -22.410 -30.484 1.00 52.38  ? 135 THR B CA    1 
ATOM   1675 C C     . THR B 2 89  ? 23.839  -21.526 -31.424 1.00 52.69  ? 135 THR B C     1 
ATOM   1676 O O     . THR B 2 89  ? 23.613  -21.558 -32.639 1.00 51.41  ? 135 THR B O     1 
ATOM   1677 C CB    . THR B 2 89  ? 23.620  -23.830 -30.481 1.00 53.56  ? 135 THR B CB    1 
ATOM   1678 O OG1   . THR B 2 89  ? 22.923  -24.635 -29.519 1.00 53.11  ? 135 THR B OG1   1 
ATOM   1679 C CG2   . THR B 2 89  ? 25.127  -23.825 -30.166 1.00 51.95  ? 135 THR B CG2   1 
ATOM   1680 N N     . GLU B 2 90  ? 24.755  -20.730 -30.851 1.00 54.71  ? 136 GLU B N     1 
ATOM   1681 C CA    . GLU B 2 90  ? 25.650  -19.854 -31.612 1.00 54.21  ? 136 GLU B CA    1 
ATOM   1682 C C     . GLU B 2 90  ? 26.207  -20.558 -32.844 1.00 55.30  ? 136 GLU B C     1 
ATOM   1683 O O     . GLU B 2 90  ? 26.756  -21.659 -32.752 1.00 56.42  ? 136 GLU B O     1 
ATOM   1684 C CB    . GLU B 2 90  ? 26.809  -19.378 -30.721 1.00 56.27  ? 136 GLU B CB    1 
ATOM   1685 C CG    . GLU B 2 90  ? 26.405  -18.457 -29.559 1.00 59.34  ? 136 GLU B CG    1 
ATOM   1686 C CD    . GLU B 2 90  ? 25.975  -17.054 -30.011 1.00 67.41  ? 136 GLU B CD    1 
ATOM   1687 O OE1   . GLU B 2 90  ? 26.728  -16.437 -30.797 1.00 63.09  ? 136 GLU B OE1   1 
ATOM   1688 O OE2   . GLU B 2 90  ? 24.888  -16.569 -29.589 1.00 66.33  ? 136 GLU B OE2   1 
ATOM   1689 N N     . GLY B 2 91  ? 26.041  -19.922 -34.004 1.00 54.81  ? 137 GLY B N     1 
ATOM   1690 C CA    . GLY B 2 91  ? 26.591  -20.425 -35.244 1.00 53.03  ? 137 GLY B CA    1 
ATOM   1691 C C     . GLY B 2 91  ? 25.691  -21.351 -36.031 1.00 61.32  ? 137 GLY B C     1 
ATOM   1692 O O     . GLY B 2 91  ? 25.981  -21.615 -37.212 1.00 61.65  ? 137 GLY B O     1 
ATOM   1693 N N     . ALA B 2 92  ? 24.608  -21.846 -35.431 1.00 50.83  ? 138 ALA B N     1 
ATOM   1694 C CA    . ALA B 2 92  ? 23.688  -22.686 -36.171 1.00 50.10  ? 138 ALA B CA    1 
ATOM   1695 C C     . ALA B 2 92  ? 23.158  -21.906 -37.361 1.00 53.07  ? 138 ALA B C     1 
ATOM   1696 O O     . ALA B 2 92  ? 23.106  -20.676 -37.352 1.00 57.31  ? 138 ALA B O     1 
ATOM   1697 C CB    . ALA B 2 92  ? 22.539  -23.146 -35.277 1.00 51.69  ? 138 ALA B CB    1 
ATOM   1698 N N     . LEU B 2 93  ? 22.797  -22.625 -38.403 1.00 53.48  ? 139 LEU B N     1 
ATOM   1699 C CA    . LEU B 2 93  ? 22.414  -22.010 -39.662 1.00 54.71  ? 139 LEU B CA    1 
ATOM   1700 C C     . LEU B 2 93  ? 20.897  -21.899 -39.726 1.00 51.28  ? 139 LEU B C     1 
ATOM   1701 O O     . LEU B 2 93  ? 20.193  -22.911 -39.692 1.00 53.10  ? 139 LEU B O     1 
ATOM   1702 C CB    . LEU B 2 93  ? 22.962  -22.815 -40.841 1.00 49.57  ? 139 LEU B CB    1 
ATOM   1703 C CG    . LEU B 2 93  ? 24.315  -22.312 -41.354 1.00 57.46  ? 139 LEU B CG    1 
ATOM   1704 C CD1   . LEU B 2 93  ? 24.141  -20.930 -41.971 1.00 55.91  ? 139 LEU B CD1   1 
ATOM   1705 C CD2   . LEU B 2 93  ? 25.389  -22.281 -40.249 1.00 54.01  ? 139 LEU B CD2   1 
ATOM   1706 N N     . ASN B 2 94  ? 20.402  -20.678 -39.866 1.00 48.63  ? 140 ASN B N     1 
ATOM   1707 C CA    . ASN B 2 94  ? 18.973  -20.456 -39.957 1.00 45.59  ? 140 ASN B CA    1 
ATOM   1708 C C     . ASN B 2 94  ? 18.465  -20.944 -41.307 1.00 52.49  ? 140 ASN B C     1 
ATOM   1709 O O     . ASN B 2 94  ? 17.992  -20.160 -42.139 1.00 58.09  ? 140 ASN B O     1 
ATOM   1710 C CB    . ASN B 2 94  ? 18.662  -18.974 -39.738 1.00 47.31  ? 140 ASN B CB    1 
ATOM   1711 C CG    . ASN B 2 94  ? 17.171  -18.672 -39.737 1.00 49.05  ? 140 ASN B CG    1 
ATOM   1712 O OD1   . ASN B 2 94  ? 16.330  -19.561 -39.568 1.00 50.99  ? 140 ASN B OD1   1 
ATOM   1713 N ND2   . ASN B 2 94  ? 16.838  -17.403 -39.924 1.00 48.93  ? 140 ASN B ND2   1 
ATOM   1714 N N     . THR B 2 95  ? 18.540  -22.252 -41.523 1.00 53.50  ? 141 THR B N     1 
ATOM   1715 C CA    . THR B 2 95  ? 18.025  -22.906 -42.718 1.00 52.47  ? 141 THR B CA    1 
ATOM   1716 C C     . THR B 2 95  ? 17.300  -24.175 -42.287 1.00 47.21  ? 141 THR B C     1 
ATOM   1717 O O     . THR B 2 95  ? 17.651  -24.763 -41.263 1.00 45.15  ? 141 THR B O     1 
ATOM   1718 C CB    . THR B 2 95  ? 19.155  -23.261 -43.700 1.00 55.50  ? 141 THR B CB    1 
ATOM   1719 O OG1   . THR B 2 95  ? 20.074  -24.157 -43.062 1.00 53.15  ? 141 THR B OG1   1 
ATOM   1720 C CG2   . THR B 2 95  ? 19.914  -22.004 -44.109 1.00 53.61  ? 141 THR B CG2   1 
ATOM   1721 N N     . PRO B 2 96  ? 16.287  -24.600 -43.036 1.00 49.72  ? 142 PRO B N     1 
ATOM   1722 C CA    . PRO B 2 96  ? 15.530  -25.782 -42.607 1.00 49.20  ? 142 PRO B CA    1 
ATOM   1723 C C     . PRO B 2 96  ? 16.442  -26.989 -42.500 1.00 50.19  ? 142 PRO B C     1 
ATOM   1724 O O     . PRO B 2 96  ? 17.375  -27.155 -43.286 1.00 54.73  ? 142 PRO B O     1 
ATOM   1725 C CB    . PRO B 2 96  ? 14.477  -25.948 -43.712 1.00 51.62  ? 142 PRO B CB    1 
ATOM   1726 C CG    . PRO B 2 96  ? 14.265  -24.558 -44.220 1.00 47.97  ? 142 PRO B CG    1 
ATOM   1727 C CD    . PRO B 2 96  ? 15.643  -23.922 -44.175 1.00 50.13  ? 142 PRO B CD    1 
ATOM   1728 N N     . LYS B 2 97  ? 16.183  -27.824 -41.495 1.00 51.41  ? 143 LYS B N     1 
ATOM   1729 C CA    . LYS B 2 97  ? 16.992  -29.013 -41.228 1.00 48.91  ? 143 LYS B CA    1 
ATOM   1730 C C     . LYS B 2 97  ? 16.291  -30.277 -41.695 1.00 48.80  ? 143 LYS B C     1 
ATOM   1731 O O     . LYS B 2 97  ? 16.347  -31.315 -41.030 1.00 50.91  ? 143 LYS B O     1 
ATOM   1732 C CB    . LYS B 2 97  ? 17.354  -29.108 -39.750 1.00 42.92  ? 143 LYS B CB    1 
ATOM   1733 C CG    . LYS B 2 97  ? 18.036  -27.889 -39.201 1.00 46.58  ? 143 LYS B CG    1 
ATOM   1734 C CD    . LYS B 2 97  ? 19.108  -27.391 -40.138 1.00 48.99  ? 143 LYS B CD    1 
ATOM   1735 C CE    . LYS B 2 97  ? 19.822  -26.199 -39.546 1.00 52.35  ? 143 LYS B CE    1 
ATOM   1736 N NZ    . LYS B 2 97  ? 20.075  -25.154 -40.580 1.00 48.01  ? 143 LYS B NZ    1 
ATOM   1737 N N     . ASP B 2 98  ? 15.623  -30.191 -42.851 1.00 52.41  ? 144 ASP B N     1 
ATOM   1738 C CA    . ASP B 2 98  ? 14.958  -31.334 -43.472 1.00 56.27  ? 144 ASP B CA    1 
ATOM   1739 C C     . ASP B 2 98  ? 15.855  -32.559 -43.586 1.00 55.33  ? 144 ASP B C     1 
ATOM   1740 O O     . ASP B 2 98  ? 15.342  -33.683 -43.676 1.00 55.04  ? 144 ASP B O     1 
ATOM   1741 C CB    . ASP B 2 98  ? 14.467  -30.946 -44.868 1.00 56.71  ? 144 ASP B CB    1 
ATOM   1742 C CG    . ASP B 2 98  ? 15.553  -30.250 -45.685 1.00 64.50  ? 144 ASP B CG    1 
ATOM   1743 O OD1   . ASP B 2 98  ? 16.539  -30.922 -46.078 1.00 67.98  ? 144 ASP B OD1   1 
ATOM   1744 O OD2   . ASP B 2 98  ? 15.434  -29.023 -45.915 1.00 63.97  ? 144 ASP B OD2   1 
ATOM   1745 N N     . HIS B 2 99  ? 17.179  -32.373 -43.608 1.00 51.45  ? 145 HIS B N     1 
ATOM   1746 C CA    . HIS B 2 99  ? 18.065  -33.527 -43.699 1.00 55.15  ? 145 HIS B CA    1 
ATOM   1747 C C     . HIS B 2 99  ? 18.063  -34.365 -42.426 1.00 52.39  ? 145 HIS B C     1 
ATOM   1748 O O     . HIS B 2 99  ? 18.356  -35.562 -42.496 1.00 51.95  ? 145 HIS B O     1 
ATOM   1749 C CB    . HIS B 2 99  ? 19.494  -33.089 -44.058 1.00 49.25  ? 145 HIS B CB    1 
ATOM   1750 C CG    . HIS B 2 99  ? 20.165  -32.219 -43.034 1.00 47.63  ? 145 HIS B CG    1 
ATOM   1751 N ND1   . HIS B 2 99  ? 20.163  -30.841 -43.112 1.00 47.85  ? 145 HIS B ND1   1 
ATOM   1752 C CD2   . HIS B 2 99  ? 20.909  -32.532 -41.946 1.00 49.92  ? 145 HIS B CD2   1 
ATOM   1753 C CE1   . HIS B 2 99  ? 20.861  -30.344 -42.106 1.00 47.92  ? 145 HIS B CE1   1 
ATOM   1754 N NE2   . HIS B 2 99  ? 21.327  -31.348 -41.384 1.00 46.51  ? 145 HIS B NE2   1 
ATOM   1755 N N     . ILE B 2 100 ? 17.747  -33.774 -41.272 1.00 52.36  ? 146 ILE B N     1 
ATOM   1756 C CA    . ILE B 2 100 ? 17.626  -34.555 -40.040 1.00 48.93  ? 146 ILE B CA    1 
ATOM   1757 C C     . ILE B 2 100 ? 16.226  -35.121 -39.887 1.00 48.51  ? 146 ILE B C     1 
ATOM   1758 O O     . ILE B 2 100 ? 16.057  -36.239 -39.393 1.00 50.14  ? 146 ILE B O     1 
ATOM   1759 C CB    . ILE B 2 100 ? 18.012  -33.716 -38.811 1.00 50.86  ? 146 ILE B CB    1 
ATOM   1760 C CG1   . ILE B 2 100 ? 19.519  -33.429 -38.804 1.00 48.68  ? 146 ILE B CG1   1 
ATOM   1761 C CG2   . ILE B 2 100 ? 17.600  -34.439 -37.532 1.00 41.95  ? 146 ILE B CG2   1 
ATOM   1762 C CD1   . ILE B 2 100 ? 20.054  -33.042 -37.434 1.00 45.60  ? 146 ILE B CD1   1 
ATOM   1763 N N     . GLY B 2 101 ? 15.220  -34.352 -40.295 1.00 45.81  ? 147 GLY B N     1 
ATOM   1764 C CA    . GLY B 2 101 ? 13.830  -34.736 -40.209 1.00 48.80  ? 147 GLY B CA    1 
ATOM   1765 C C     . GLY B 2 101 ? 13.451  -35.174 -38.809 1.00 42.74  ? 147 GLY B C     1 
ATOM   1766 O O     . GLY B 2 101 ? 13.974  -34.697 -37.796 1.00 36.33  ? 147 GLY B O     1 
ATOM   1767 N N     . THR B 2 102 ? 12.544  -36.137 -38.753 1.00 45.50  ? 148 THR B N     1 
ATOM   1768 C CA    . THR B 2 102 ? 12.021  -36.628 -37.496 1.00 39.74  ? 148 THR B CA    1 
ATOM   1769 C C     . THR B 2 102 ? 12.228  -38.132 -37.413 1.00 39.65  ? 148 THR B C     1 
ATOM   1770 O O     . THR B 2 102 ? 12.651  -38.775 -38.370 1.00 39.69  ? 148 THR B O     1 
ATOM   1771 C CB    . THR B 2 102 ? 10.551  -36.254 -37.356 1.00 40.84  ? 148 THR B CB    1 
ATOM   1772 O OG1   . THR B 2 102 ? 9.886   -36.520 -38.595 1.00 45.19  ? 148 THR B OG1   1 
ATOM   1773 C CG2   . THR B 2 102 ? 10.427  -34.770 -37.037 1.00 41.65  ? 148 THR B CG2   1 
ATOM   1774 N N     . ARG B 2 103 ? 11.923  -38.680 -36.242 1.00 38.70  ? 149 ARG B N     1 
ATOM   1775 C CA    . ARG B 2 103 ? 12.236  -40.056 -35.912 1.00 30.74  ? 149 ARG B CA    1 
ATOM   1776 C C     . ARG B 2 103 ? 11.095  -40.988 -36.281 1.00 34.95  ? 149 ARG B C     1 
ATOM   1777 O O     . ARG B 2 103 ? 9.920   -40.632 -36.151 1.00 36.92  ? 149 ARG B O     1 
ATOM   1778 C CB    . ARG B 2 103 ? 12.527  -40.162 -34.419 1.00 29.83  ? 149 ARG B CB    1 
ATOM   1779 C CG    . ARG B 2 103 ? 12.809  -41.543 -33.936 1.00 32.72  ? 149 ARG B CG    1 
ATOM   1780 C CD    . ARG B 2 103 ? 13.231  -41.505 -32.495 1.00 30.36  ? 149 ARG B CD    1 
ATOM   1781 N NE    . ARG B 2 103 ? 12.191  -40.937 -31.650 1.00 34.22  ? 149 ARG B NE    1 
ATOM   1782 C CZ    . ARG B 2 103 ? 11.326  -41.659 -30.953 1.00 31.16  ? 149 ARG B CZ    1 
ATOM   1783 N NH1   . ARG B 2 103 ? 11.301  -42.978 -31.039 1.00 29.34  ? 149 ARG B NH1   1 
ATOM   1784 N NH2   . ARG B 2 103 ? 10.492  -41.045 -30.122 1.00 32.35  ? 149 ARG B NH2   1 
ATOM   1785 N N     . ASN B 2 104 ? 11.449  -42.197 -36.715 1.00 31.95  ? 150 ASN B N     1 
ATOM   1786 C CA    . ASN B 2 104 ? 10.485  -43.278 -36.865 1.00 34.01  ? 150 ASN B CA    1 
ATOM   1787 C C     . ASN B 2 104 ? 10.654  -44.253 -35.710 1.00 32.72  ? 150 ASN B C     1 
ATOM   1788 O O     . ASN B 2 104 ? 11.625  -45.022 -35.697 1.00 31.21  ? 150 ASN B O     1 
ATOM   1789 C CB    . ASN B 2 104 ? 10.680  -43.997 -38.197 1.00 30.27  ? 150 ASN B CB    1 
ATOM   1790 C CG    . ASN B 2 104 ? 9.675   -45.102 -38.409 1.00 31.60  ? 150 ASN B CG    1 
ATOM   1791 O OD1   . ASN B 2 104 ? 8.915   -45.463 -37.506 1.00 31.68  ? 150 ASN B OD1   1 
ATOM   1792 N ND2   . ASN B 2 104 ? 9.688   -45.676 -39.593 1.00 34.65  ? 150 ASN B ND2   1 
ATOM   1793 N N     . PRO B 2 105 ? 9.735   -44.282 -34.737 1.00 30.78  ? 151 PRO B N     1 
ATOM   1794 C CA    . PRO B 2 105 ? 9.946   -45.116 -33.548 1.00 27.16  ? 151 PRO B CA    1 
ATOM   1795 C C     . PRO B 2 105 ? 10.001  -46.594 -33.844 1.00 26.90  ? 151 PRO B C     1 
ATOM   1796 O O     . PRO B 2 105 ? 10.392  -47.360 -32.958 1.00 30.07  ? 151 PRO B O     1 
ATOM   1797 C CB    . PRO B 2 105 ? 8.749   -44.763 -32.647 1.00 31.55  ? 151 PRO B CB    1 
ATOM   1798 C CG    . PRO B 2 105 ? 7.866   -43.937 -33.448 1.00 32.48  ? 151 PRO B CG    1 
ATOM   1799 C CD    . PRO B 2 105 ? 8.661   -43.308 -34.528 1.00 29.69  ? 151 PRO B CD    1 
ATOM   1800 N N     . ALA B 2 106 ? 9.643   -47.019 -35.057 1.00 27.75  ? 152 ALA B N     1 
ATOM   1801 C CA    . ALA B 2 106 ? 9.809   -48.421 -35.422 1.00 29.45  ? 152 ALA B CA    1 
ATOM   1802 C C     . ALA B 2 106 ? 11.284  -48.834 -35.434 1.00 33.66  ? 152 ALA B C     1 
ATOM   1803 O O     . ALA B 2 106 ? 11.603  -49.984 -35.108 1.00 33.21  ? 152 ALA B O     1 
ATOM   1804 C CB    . ALA B 2 106 ? 9.160   -48.696 -36.783 1.00 32.06  ? 152 ALA B CB    1 
ATOM   1805 N N     . ASN B 2 107 ? 12.202  -47.923 -35.796 1.00 32.21  ? 153 ASN B N     1 
ATOM   1806 C CA    . ASN B 2 107 ? 13.612  -48.302 -35.905 1.00 37.62  ? 153 ASN B CA    1 
ATOM   1807 C C     . ASN B 2 107 ? 14.570  -47.303 -35.271 1.00 37.92  ? 153 ASN B C     1 
ATOM   1808 O O     . ASN B 2 107 ? 15.750  -47.279 -35.646 1.00 41.91  ? 153 ASN B O     1 
ATOM   1809 C CB    . ASN B 2 107 ? 14.024  -48.504 -37.360 1.00 38.80  ? 153 ASN B CB    1 
ATOM   1810 C CG    . ASN B 2 107 ? 13.339  -47.535 -38.303 1.00 40.79  ? 153 ASN B CG    1 
ATOM   1811 O OD1   . ASN B 2 107 ? 13.701  -46.357 -38.384 1.00 40.68  ? 153 ASN B OD1   1 
ATOM   1812 N ND2   . ASN B 2 107 ? 12.343  -48.035 -39.037 1.00 35.94  ? 153 ASN B ND2   1 
ATOM   1813 N N     . ASN B 2 108 ? 14.104  -46.479 -34.334 1.00 35.03  ? 154 ASN B N     1 
ATOM   1814 C CA    . ASN B 2 108 ? 15.001  -45.642 -33.542 1.00 32.86  ? 154 ASN B CA    1 
ATOM   1815 C C     . ASN B 2 108 ? 14.388  -45.448 -32.174 1.00 35.91  ? 154 ASN B C     1 
ATOM   1816 O O     . ASN B 2 108 ? 13.248  -44.992 -32.074 1.00 33.65  ? 154 ASN B O     1 
ATOM   1817 C CB    . ASN B 2 108 ? 15.218  -44.277 -34.181 1.00 29.33  ? 154 ASN B CB    1 
ATOM   1818 C CG    . ASN B 2 108 ? 15.936  -44.371 -35.483 1.00 41.24  ? 154 ASN B CG    1 
ATOM   1819 O OD1   . ASN B 2 108 ? 15.316  -44.403 -36.555 1.00 45.69  ? 154 ASN B OD1   1 
ATOM   1820 N ND2   . ASN B 2 108 ? 17.251  -44.469 -35.411 1.00 35.06  ? 154 ASN B ND2   1 
ATOM   1821 N N     . ALA B 2 109 ? 15.130  -45.788 -31.134 1.00 34.69  ? 155 ALA B N     1 
ATOM   1822 C CA    . ALA B 2 109 ? 14.709  -45.364 -29.816 1.00 30.13  ? 155 ALA B CA    1 
ATOM   1823 C C     . ALA B 2 109 ? 14.783  -43.851 -29.739 1.00 34.27  ? 155 ALA B C     1 
ATOM   1824 O O     . ALA B 2 109 ? 15.445  -43.202 -30.549 1.00 34.96  ? 155 ALA B O     1 
ATOM   1825 C CB    . ALA B 2 109 ? 15.589  -45.990 -28.743 1.00 30.27  ? 155 ALA B CB    1 
ATOM   1826 N N     . ALA B 2 110 ? 14.085  -43.277 -28.770 1.00 30.72  ? 156 ALA B N     1 
ATOM   1827 C CA    . ALA B 2 110 ? 14.224  -41.851 -28.538 1.00 31.91  ? 156 ALA B CA    1 
ATOM   1828 C C     . ALA B 2 110 ? 15.522  -41.587 -27.786 1.00 35.86  ? 156 ALA B C     1 
ATOM   1829 O O     . ALA B 2 110 ? 15.950  -42.389 -26.950 1.00 35.73  ? 156 ALA B O     1 
ATOM   1830 C CB    . ALA B 2 110 ? 13.035  -41.310 -27.750 1.00 27.14  ? 156 ALA B CB    1 
ATOM   1831 N N     . ILE B 2 111 ? 16.160  -40.469 -28.101 1.00 37.19  ? 157 ILE B N     1 
ATOM   1832 C CA    . ILE B 2 111 ? 17.338  -40.035 -27.359 1.00 33.90  ? 157 ILE B CA    1 
ATOM   1833 C C     . ILE B 2 111 ? 16.871  -39.361 -26.078 1.00 35.77  ? 157 ILE B C     1 
ATOM   1834 O O     . ILE B 2 111 ? 16.124  -38.379 -26.125 1.00 36.08  ? 157 ILE B O     1 
ATOM   1835 C CB    . ILE B 2 111 ? 18.184  -39.077 -28.199 1.00 37.37  ? 157 ILE B CB    1 
ATOM   1836 C CG1   . ILE B 2 111 ? 18.782  -39.816 -29.381 1.00 38.50  ? 157 ILE B CG1   1 
ATOM   1837 C CG2   . ILE B 2 111 ? 19.242  -38.438 -27.341 1.00 33.54  ? 157 ILE B CG2   1 
ATOM   1838 C CD1   . ILE B 2 111 ? 18.771  -39.034 -30.637 1.00 35.05  ? 157 ILE B CD1   1 
ATOM   1839 N N     . VAL B 2 112 ? 17.302  -39.882 -24.928 1.00 37.07  ? 158 VAL B N     1 
ATOM   1840 C CA    . VAL B 2 112 ? 16.950  -39.238 -23.665 1.00 39.21  ? 158 VAL B CA    1 
ATOM   1841 C C     . VAL B 2 112 ? 17.390  -37.783 -23.721 1.00 42.35  ? 158 VAL B C     1 
ATOM   1842 O O     . VAL B 2 112 ? 18.515  -37.477 -24.138 1.00 43.06  ? 158 VAL B O     1 
ATOM   1843 C CB    . VAL B 2 112 ? 17.591  -39.976 -22.481 1.00 38.87  ? 158 VAL B CB    1 
ATOM   1844 C CG1   . VAL B 2 112 ? 17.317  -39.234 -21.190 1.00 44.77  ? 158 VAL B CG1   1 
ATOM   1845 C CG2   . VAL B 2 112 ? 17.050  -41.392 -22.370 1.00 44.21  ? 158 VAL B CG2   1 
ATOM   1846 N N     . LEU B 2 113 ? 16.494  -36.873 -23.342 1.00 38.55  ? 159 LEU B N     1 
ATOM   1847 C CA    . LEU B 2 113 ? 16.770  -35.453 -23.518 1.00 37.68  ? 159 LEU B CA    1 
ATOM   1848 C C     . LEU B 2 113 ? 17.753  -34.982 -22.456 1.00 42.99  ? 159 LEU B C     1 
ATOM   1849 O O     . LEU B 2 113 ? 17.454  -35.041 -21.257 1.00 41.73  ? 159 LEU B O     1 
ATOM   1850 C CB    . LEU B 2 113 ? 15.493  -34.622 -23.459 1.00 33.96  ? 159 LEU B CB    1 
ATOM   1851 C CG    . LEU B 2 113 ? 15.775  -33.174 -23.878 1.00 35.23  ? 159 LEU B CG    1 
ATOM   1852 C CD1   . LEU B 2 113 ? 14.926  -32.779 -25.057 1.00 39.04  ? 159 LEU B CD1   1 
ATOM   1853 C CD2   . LEU B 2 113 ? 15.570  -32.199 -22.740 1.00 38.25  ? 159 LEU B CD2   1 
ATOM   1854 N N     . GLN B 2 114 ? 18.912  -34.489 -22.905 1.00 41.28  ? 160 GLN B N     1 
ATOM   1855 C CA    . GLN B 2 114 ? 19.938  -33.922 -22.037 1.00 42.89  ? 160 GLN B CA    1 
ATOM   1856 C C     . GLN B 2 114 ? 20.373  -32.562 -22.567 1.00 42.53  ? 160 GLN B C     1 
ATOM   1857 O O     . GLN B 2 114 ? 20.613  -32.408 -23.769 1.00 49.43  ? 160 GLN B O     1 
ATOM   1858 C CB    . GLN B 2 114 ? 21.137  -34.870 -21.935 1.00 48.25  ? 160 GLN B CB    1 
ATOM   1859 C CG    . GLN B 2 114 ? 20.838  -36.121 -21.123 1.00 48.34  ? 160 GLN B CG    1 
ATOM   1860 C CD    . GLN B 2 114 ? 22.065  -36.972 -20.873 1.00 56.49  ? 160 GLN B CD    1 
ATOM   1861 O OE1   . GLN B 2 114 ? 22.270  -37.452 -19.763 1.00 67.74  ? 160 GLN B OE1   1 
ATOM   1862 N NE2   . GLN B 2 114 ? 22.881  -37.172 -21.902 1.00 54.29  ? 160 GLN B NE2   1 
ATOM   1863 N N     . LEU B 2 115 ? 20.478  -31.564 -21.659 1.00 47.03  ? 161 LEU B N     1 
ATOM   1864 C CA    . LEU B 2 115 ? 20.859  -30.200 -22.011 1.00 48.67  ? 161 LEU B CA    1 
ATOM   1865 C C     . LEU B 2 115 ? 22.319  -29.927 -21.648 1.00 52.74  ? 161 LEU B C     1 
ATOM   1866 O O     . LEU B 2 115 ? 22.857  -30.536 -20.717 1.00 54.27  ? 161 LEU B O     1 
ATOM   1867 C CB    . LEU B 2 115 ? 19.964  -29.192 -21.290 1.00 47.45  ? 161 LEU B CB    1 
ATOM   1868 C CG    . LEU B 2 115 ? 18.486  -29.419 -21.588 1.00 45.35  ? 161 LEU B CG    1 
ATOM   1869 C CD1   . LEU B 2 115 ? 17.634  -28.538 -20.714 1.00 42.72  ? 161 LEU B CD1   1 
ATOM   1870 C CD2   . LEU B 2 115 ? 18.235  -29.148 -23.059 1.00 41.24  ? 161 LEU B CD2   1 
ATOM   1871 N N     . PRO B 2 116 ? 22.988  -29.014 -22.361 1.00 50.88  ? 162 PRO B N     1 
ATOM   1872 C CA    . PRO B 2 116 ? 24.401  -28.747 -22.070 1.00 49.93  ? 162 PRO B CA    1 
ATOM   1873 C C     . PRO B 2 116 ? 24.599  -28.222 -20.657 1.00 49.68  ? 162 PRO B C     1 
ATOM   1874 O O     . PRO B 2 116 ? 23.693  -27.663 -20.037 1.00 48.59  ? 162 PRO B O     1 
ATOM   1875 C CB    . PRO B 2 116 ? 24.790  -27.702 -23.118 1.00 51.28  ? 162 PRO B CB    1 
ATOM   1876 C CG    . PRO B 2 116 ? 23.820  -27.901 -24.235 1.00 50.51  ? 162 PRO B CG    1 
ATOM   1877 C CD    . PRO B 2 116 ? 22.536  -28.312 -23.578 1.00 50.32  ? 162 PRO B CD    1 
ATOM   1878 N N     . GLN B 2 117 ? 25.805  -28.444 -20.146 1.00 57.81  ? 163 GLN B N     1 
ATOM   1879 C CA    . GLN B 2 117 ? 26.142  -28.098 -18.770 1.00 62.96  ? 163 GLN B CA    1 
ATOM   1880 C C     . GLN B 2 117 ? 25.871  -26.621 -18.489 1.00 53.91  ? 163 GLN B C     1 
ATOM   1881 O O     . GLN B 2 117 ? 26.258  -25.741 -19.265 1.00 52.65  ? 163 GLN B O     1 
ATOM   1882 C CB    . GLN B 2 117 ? 27.616  -28.444 -18.509 1.00 54.61  ? 163 GLN B CB    1 
ATOM   1883 C CG    . GLN B 2 117 ? 27.912  -28.863 -17.084 1.00 59.52  ? 163 GLN B CG    1 
ATOM   1884 C CD    . GLN B 2 117 ? 28.201  -27.675 -16.195 1.00 61.94  ? 163 GLN B CD    1 
ATOM   1885 O OE1   . GLN B 2 117 ? 28.722  -26.663 -16.661 1.00 62.77  ? 163 GLN B OE1   1 
ATOM   1886 N NE2   . GLN B 2 117 ? 27.865  -27.787 -14.911 1.00 63.47  ? 163 GLN B NE2   1 
ATOM   1887 N N     . GLY B 2 118 ? 25.198  -26.351 -17.372 1.00 52.07  ? 164 GLY B N     1 
ATOM   1888 C CA    . GLY B 2 118 ? 24.881  -24.994 -16.985 1.00 55.19  ? 164 GLY B CA    1 
ATOM   1889 C C     . GLY B 2 118 ? 23.580  -24.439 -17.528 1.00 59.56  ? 164 GLY B C     1 
ATOM   1890 O O     . GLY B 2 118 ? 23.254  -23.274 -17.242 1.00 59.44  ? 164 GLY B O     1 
ATOM   1891 N N     . THR B 2 119 ? 22.822  -25.220 -18.296 1.00 53.05  ? 165 THR B N     1 
ATOM   1892 C CA    . THR B 2 119 ? 21.626  -24.672 -18.918 1.00 53.02  ? 165 THR B CA    1 
ATOM   1893 C C     . THR B 2 119 ? 20.640  -24.244 -17.846 1.00 51.04  ? 165 THR B C     1 
ATOM   1894 O O     . THR B 2 119 ? 20.393  -24.973 -16.885 1.00 55.20  ? 165 THR B O     1 
ATOM   1895 C CB    . THR B 2 119 ? 21.001  -25.689 -19.875 1.00 54.29  ? 165 THR B CB    1 
ATOM   1896 O OG1   . THR B 2 119 ? 21.734  -25.673 -21.107 1.00 53.33  ? 165 THR B OG1   1 
ATOM   1897 C CG2   . THR B 2 119 ? 19.552  -25.339 -20.182 1.00 51.92  ? 165 THR B CG2   1 
ATOM   1898 N N     . THR B 2 120 ? 20.123  -23.028 -17.985 1.00 52.49  ? 166 THR B N     1 
ATOM   1899 C CA    . THR B 2 120 ? 19.118  -22.516 -17.063 1.00 54.32  ? 166 THR B CA    1 
ATOM   1900 C C     . THR B 2 120 ? 17.738  -23.013 -17.469 1.00 51.98  ? 166 THR B C     1 
ATOM   1901 O O     . THR B 2 120 ? 17.430  -23.107 -18.658 1.00 55.12  ? 166 THR B O     1 
ATOM   1902 C CB    . THR B 2 120 ? 19.131  -20.986 -17.054 1.00 57.04  ? 166 THR B CB    1 
ATOM   1903 O OG1   . THR B 2 120 ? 20.407  -20.506 -16.597 1.00 59.15  ? 166 THR B OG1   1 
ATOM   1904 C CG2   . THR B 2 120 ? 18.037  -20.458 -16.158 1.00 51.86  ? 166 THR B CG2   1 
ATOM   1905 N N     . LEU B 2 121 ? 16.909  -23.333 -16.480 1.00 50.97  ? 167 LEU B N     1 
ATOM   1906 C CA    . LEU B 2 121 ? 15.547  -23.774 -16.738 1.00 48.22  ? 167 LEU B CA    1 
ATOM   1907 C C     . LEU B 2 121 ? 14.585  -22.917 -15.933 1.00 50.81  ? 167 LEU B C     1 
ATOM   1908 O O     . LEU B 2 121 ? 14.963  -22.380 -14.885 1.00 48.46  ? 167 LEU B O     1 
ATOM   1909 C CB    . LEU B 2 121 ? 15.339  -25.253 -16.363 1.00 46.33  ? 167 LEU B CB    1 
ATOM   1910 C CG    . LEU B 2 121 ? 15.660  -26.322 -17.407 1.00 43.87  ? 167 LEU B CG    1 
ATOM   1911 C CD1   . LEU B 2 121 ? 15.352  -27.716 -16.892 1.00 45.11  ? 167 LEU B CD1   1 
ATOM   1912 C CD2   . LEU B 2 121 ? 14.900  -26.057 -18.674 1.00 42.57  ? 167 LEU B CD2   1 
ATOM   1913 N N     . PRO B 2 122 ? 13.344  -22.750 -16.407 1.00 50.73  ? 168 PRO B N     1 
ATOM   1914 C CA    . PRO B 2 122 ? 12.323  -22.144 -15.551 1.00 44.53  ? 168 PRO B CA    1 
ATOM   1915 C C     . PRO B 2 122 ? 11.979  -23.090 -14.417 1.00 50.25  ? 168 PRO B C     1 
ATOM   1916 O O     . PRO B 2 122 ? 12.113  -24.310 -14.538 1.00 47.70  ? 168 PRO B O     1 
ATOM   1917 C CB    . PRO B 2 122 ? 11.126  -21.940 -16.486 1.00 40.46  ? 168 PRO B CB    1 
ATOM   1918 C CG    . PRO B 2 122 ? 11.611  -22.228 -17.858 1.00 42.61  ? 168 PRO B CG    1 
ATOM   1919 C CD    . PRO B 2 122 ? 12.790  -23.138 -17.717 1.00 43.46  ? 168 PRO B CD    1 
ATOM   1920 N N     . LYS B 2 123 ? 11.546  -22.506 -13.300 1.00 53.49  ? 169 LYS B N     1 
ATOM   1921 C CA    . LYS B 2 123 ? 11.010  -23.298 -12.206 1.00 51.85  ? 169 LYS B CA    1 
ATOM   1922 C C     . LYS B 2 123 ? 9.874   -24.160 -12.732 1.00 50.02  ? 169 LYS B C     1 
ATOM   1923 O O     . LYS B 2 123 ? 9.136   -23.749 -13.632 1.00 48.67  ? 169 LYS B O     1 
ATOM   1924 C CB    . LYS B 2 123 ? 10.517  -22.388 -11.081 1.00 57.14  ? 169 LYS B CB    1 
ATOM   1925 C CG    . LYS B 2 123 ? 10.401  -23.060 -9.712  1.00 58.15  ? 169 LYS B CG    1 
ATOM   1926 C CD    . LYS B 2 123 ? 10.243  -22.028 -8.590  1.00 54.06  ? 169 LYS B CD    1 
ATOM   1927 C CE    . LYS B 2 123 ? 8.775   -21.818 -8.204  1.00 54.72  ? 169 LYS B CE    1 
ATOM   1928 N NZ    . LYS B 2 123 ? 8.243   -22.893 -7.300  1.00 52.16  ? 169 LYS B NZ    1 
ATOM   1929 N N     . GLY B 2 124 ? 9.762   -25.378 -12.183 1.00 53.00  ? 170 GLY B N     1 
ATOM   1930 C CA    . GLY B 2 124 ? 8.825   -26.377 -12.654 1.00 48.28  ? 170 GLY B CA    1 
ATOM   1931 C C     . GLY B 2 124 ? 9.389   -27.345 -13.672 1.00 46.73  ? 170 GLY B C     1 
ATOM   1932 O O     . GLY B 2 124 ? 8.705   -28.308 -14.030 1.00 47.34  ? 170 GLY B O     1 
ATOM   1933 N N     . PHE B 2 125 ? 10.612  -27.128 -14.143 1.00 48.12  ? 171 PHE B N     1 
ATOM   1934 C CA    . PHE B 2 125 ? 11.260  -27.996 -15.113 1.00 49.14  ? 171 PHE B CA    1 
ATOM   1935 C C     . PHE B 2 125 ? 12.499  -28.628 -14.495 1.00 48.16  ? 171 PHE B C     1 
ATOM   1936 O O     . PHE B 2 125 ? 13.130  -28.045 -13.607 1.00 49.75  ? 171 PHE B O     1 
ATOM   1937 C CB    . PHE B 2 125 ? 11.648  -27.222 -16.375 1.00 47.56  ? 171 PHE B CB    1 
ATOM   1938 C CG    . PHE B 2 125 ? 10.487  -26.809 -17.190 1.00 44.30  ? 171 PHE B CG    1 
ATOM   1939 C CD1   . PHE B 2 125 ? 9.829   -25.621 -16.927 1.00 47.42  ? 171 PHE B CD1   1 
ATOM   1940 C CD2   . PHE B 2 125 ? 10.025  -27.618 -18.197 1.00 41.68  ? 171 PHE B CD2   1 
ATOM   1941 C CE1   . PHE B 2 125 ? 8.736   -25.233 -17.674 1.00 46.97  ? 171 PHE B CE1   1 
ATOM   1942 C CE2   . PHE B 2 125 ? 8.937   -27.241 -18.947 1.00 43.82  ? 171 PHE B CE2   1 
ATOM   1943 C CZ    . PHE B 2 125 ? 8.292   -26.042 -18.687 1.00 47.62  ? 171 PHE B CZ    1 
ATOM   1944 N N     . TYR B 2 126 ? 12.843  -29.824 -14.978 1.00 49.45  ? 172 TYR B N     1 
ATOM   1945 C CA    . TYR B 2 126 ? 13.948  -30.605 -14.436 1.00 51.00  ? 172 TYR B CA    1 
ATOM   1946 C C     . TYR B 2 126 ? 14.840  -31.127 -15.556 1.00 55.07  ? 172 TYR B C     1 
ATOM   1947 O O     . TYR B 2 126 ? 14.344  -31.637 -16.564 1.00 49.67  ? 172 TYR B O     1 
ATOM   1948 C CB    . TYR B 2 126 ? 13.424  -31.766 -13.579 1.00 46.75  ? 172 TYR B CB    1 
ATOM   1949 C CG    . TYR B 2 126 ? 12.701  -31.278 -12.346 1.00 46.06  ? 172 TYR B CG    1 
ATOM   1950 C CD1   . TYR B 2 126 ? 11.376  -30.902 -12.402 1.00 48.78  ? 172 TYR B CD1   1 
ATOM   1951 C CD2   . TYR B 2 126 ? 13.355  -31.168 -11.133 1.00 51.37  ? 172 TYR B CD2   1 
ATOM   1952 C CE1   . TYR B 2 126 ? 10.721  -30.433 -11.284 1.00 49.08  ? 172 TYR B CE1   1 
ATOM   1953 C CE2   . TYR B 2 126 ? 12.707  -30.706 -10.013 1.00 50.53  ? 172 TYR B CE2   1 
ATOM   1954 C CZ    . TYR B 2 126 ? 11.390  -30.342 -10.092 1.00 47.31  ? 172 TYR B CZ    1 
ATOM   1955 O OH    . TYR B 2 126 ? 10.736  -29.881 -8.970  1.00 48.34  ? 172 TYR B OH    1 
ATOM   1956 N N     . ALA B 2 127 ? 16.160  -31.003 -15.360 1.00 58.56  ? 173 ALA B N     1 
ATOM   1957 C CA    . ALA B 2 127 ? 17.174  -31.466 -16.305 1.00 58.36  ? 173 ALA B CA    1 
ATOM   1958 C C     . ALA B 2 127 ? 17.852  -32.717 -15.766 1.00 64.84  ? 173 ALA B C     1 
ATOM   1959 O O     . ALA B 2 127 ? 18.271  -32.750 -14.602 1.00 66.42  ? 173 ALA B O     1 
ATOM   1960 C CB    . ALA B 2 127 ? 18.229  -30.387 -16.566 1.00 55.84  ? 173 ALA B CB    1 
ATOM   1961 N N     . GLU B 2 128 ? 17.970  -33.736 -16.611 1.00 63.06  ? 174 GLU B N     1 
ATOM   1962 C CA    . GLU B 2 128 ? 18.611  -34.982 -16.198 1.00 67.58  ? 174 GLU B CA    1 
ATOM   1963 C C     . GLU B 2 128 ? 20.072  -35.056 -16.638 1.00 66.70  ? 174 GLU B C     1 
ATOM   1964 O O     . GLU B 2 128 ? 20.425  -34.616 -17.729 1.00 64.85  ? 174 GLU B O     1 
ATOM   1965 C CB    . GLU B 2 128 ? 17.846  -36.183 -16.746 1.00 59.95  ? 174 GLU B CB    1 
ATOM   1966 C CG    . GLU B 2 128 ? 16.632  -36.573 -15.928 1.00 57.83  ? 174 GLU B CG    1 
ATOM   1967 C CD    . GLU B 2 128 ? 15.871  -37.721 -16.573 1.00 63.14  ? 174 GLU B CD    1 
ATOM   1968 O OE1   . GLU B 2 128 ? 16.049  -37.932 -17.795 1.00 61.54  ? 174 GLU B OE1   1 
ATOM   1969 O OE2   . GLU B 2 128 ? 15.104  -38.417 -15.869 1.00 60.99  ? 174 GLU B OE2   1 
ATOM   1970 N N     . ASN C 3 1   ? 7.821   -65.204 -17.247 1.00 69.88  ? 47  ASN C N     1 
ATOM   1971 C CA    . ASN C 3 1   ? 8.131   -64.319 -18.372 1.00 69.83  ? 47  ASN C CA    1 
ATOM   1972 C C     . ASN C 3 1   ? 8.629   -62.951 -17.926 1.00 68.09  ? 47  ASN C C     1 
ATOM   1973 O O     . ASN C 3 1   ? 8.953   -62.738 -16.756 1.00 72.35  ? 47  ASN C O     1 
ATOM   1974 C CB    . ASN C 3 1   ? 6.908   -64.127 -19.264 1.00 65.32  ? 47  ASN C CB    1 
ATOM   1975 C CG    . ASN C 3 1   ? 6.185   -65.414 -19.529 1.00 73.93  ? 47  ASN C CG    1 
ATOM   1976 O OD1   . ASN C 3 1   ? 6.778   -66.497 -19.471 1.00 74.08  ? 47  ASN C OD1   1 
ATOM   1977 N ND2   . ASN C 3 1   ? 4.884   -65.315 -19.813 1.00 73.44  ? 47  ASN C ND2   1 
ATOM   1978 N N     . ASN C 3 2   ? 8.660   -62.019 -18.877 1.00 60.98  ? 48  ASN C N     1 
ATOM   1979 C CA    . ASN C 3 2   ? 9.211   -60.683 -18.681 1.00 56.12  ? 48  ASN C CA    1 
ATOM   1980 C C     . ASN C 3 2   ? 8.075   -59.668 -18.745 1.00 57.11  ? 48  ASN C C     1 
ATOM   1981 O O     . ASN C 3 2   ? 7.514   -59.420 -19.820 1.00 52.40  ? 48  ASN C O     1 
ATOM   1982 C CB    . ASN C 3 2   ? 10.271  -60.400 -19.737 1.00 47.72  ? 48  ASN C CB    1 
ATOM   1983 C CG    . ASN C 3 2   ? 11.465  -61.311 -19.601 1.00 56.95  ? 48  ASN C CG    1 
ATOM   1984 O OD1   . ASN C 3 2   ? 12.488  -60.923 -19.023 1.00 52.35  ? 48  ASN C OD1   1 
ATOM   1985 N ND2   . ASN C 3 2   ? 11.333  -62.548 -20.094 1.00 54.98  ? 48  ASN C ND2   1 
ATOM   1986 N N     . THR C 3 3   ? 7.752   -59.061 -17.603 1.00 54.03  ? 49  THR C N     1 
ATOM   1987 C CA    . THR C 3 3   ? 6.549   -58.245 -17.499 1.00 47.33  ? 49  THR C CA    1 
ATOM   1988 C C     . THR C 3 3   ? 6.892   -56.855 -16.972 1.00 46.12  ? 49  THR C C     1 
ATOM   1989 O O     . THR C 3 3   ? 8.055   -56.544 -16.678 1.00 47.76  ? 49  THR C O     1 
ATOM   1990 C CB    . THR C 3 3   ? 5.496   -58.937 -16.627 1.00 48.13  ? 49  THR C CB    1 
ATOM   1991 O OG1   . THR C 3 3   ? 6.153   -59.712 -15.607 1.00 50.24  ? 49  THR C OG1   1 
ATOM   1992 C CG2   . THR C 3 3   ? 4.613   -59.846 -17.507 1.00 40.12  ? 49  THR C CG2   1 
ATOM   1993 N N     . ALA C 3 4   ? 5.859   -56.009 -16.892 1.00 38.98  ? 50  ALA C N     1 
ATOM   1994 C CA    . ALA C 3 4   ? 6.003   -54.608 -16.539 1.00 36.21  ? 50  ALA C CA    1 
ATOM   1995 C C     . ALA C 3 4   ? 4.911   -54.220 -15.553 1.00 36.27  ? 50  ALA C C     1 
ATOM   1996 O O     . ALA C 3 4   ? 3.909   -54.922 -15.386 1.00 39.65  ? 50  ALA C O     1 
ATOM   1997 C CB    . ALA C 3 4   ? 5.952   -53.725 -17.791 1.00 35.59  ? 50  ALA C CB    1 
ATOM   1998 N N     . SER C 3 5   ? 5.117   -53.095 -14.886 1.00 35.24  ? 51  SER C N     1 
ATOM   1999 C CA    . SER C 3 5   ? 4.072   -52.540 -14.034 1.00 34.30  ? 51  SER C CA    1 
ATOM   2000 C C     . SER C 3 5   ? 2.843   -52.202 -14.868 1.00 38.75  ? 51  SER C C     1 
ATOM   2001 O O     . SER C 3 5   ? 2.960   -51.779 -16.022 1.00 34.43  ? 51  SER C O     1 
ATOM   2002 C CB    . SER C 3 5   ? 4.582   -51.280 -13.337 1.00 33.35  ? 51  SER C CB    1 
ATOM   2003 O OG    . SER C 3 5   ? 3.516   -50.515 -12.806 1.00 35.04  ? 51  SER C OG    1 
ATOM   2004 N N     . TRP C 3 6   ? 1.657   -52.379 -14.279 1.00 33.63  ? 52  TRP C N     1 
ATOM   2005 C CA    . TRP C 3 6   ? 0.442   -52.005 -14.985 1.00 32.19  ? 52  TRP C CA    1 
ATOM   2006 C C     . TRP C 3 6   ? 0.341   -50.505 -15.224 1.00 32.83  ? 52  TRP C C     1 
ATOM   2007 O O     . TRP C 3 6   ? -0.444  -50.082 -16.081 1.00 33.02  ? 52  TRP C O     1 
ATOM   2008 C CB    . TRP C 3 6   ? -0.799  -52.491 -14.222 1.00 34.06  ? 52  TRP C CB    1 
ATOM   2009 C CG    . TRP C 3 6   ? -1.107  -53.906 -14.535 1.00 37.50  ? 52  TRP C CG    1 
ATOM   2010 C CD1   . TRP C 3 6   ? -0.836  -54.992 -13.762 1.00 36.98  ? 52  TRP C CD1   1 
ATOM   2011 C CD2   . TRP C 3 6   ? -1.714  -54.408 -15.735 1.00 36.66  ? 52  TRP C CD2   1 
ATOM   2012 N NE1   . TRP C 3 6   ? -1.244  -56.140 -14.395 1.00 35.02  ? 52  TRP C NE1   1 
ATOM   2013 C CE2   . TRP C 3 6   ? -1.781  -55.809 -15.612 1.00 37.95  ? 52  TRP C CE2   1 
ATOM   2014 C CE3   . TRP C 3 6   ? -2.194  -53.810 -16.903 1.00 36.90  ? 52  TRP C CE3   1 
ATOM   2015 C CZ2   . TRP C 3 6   ? -2.317  -56.625 -16.614 1.00 34.37  ? 52  TRP C CZ2   1 
ATOM   2016 C CZ3   . TRP C 3 6   ? -2.725  -54.622 -17.895 1.00 36.54  ? 52  TRP C CZ3   1 
ATOM   2017 C CH2   . TRP C 3 6   ? -2.783  -56.013 -17.741 1.00 32.20  ? 52  TRP C CH2   1 
ATOM   2018 N N     . PHE C 3 7   ? 1.114   -49.696 -14.503 1.00 33.62  ? 53  PHE C N     1 
ATOM   2019 C CA    . PHE C 3 7   ? 0.952   -48.249 -14.488 1.00 34.57  ? 53  PHE C CA    1 
ATOM   2020 C C     . PHE C 3 7   ? 2.257   -47.564 -14.891 1.00 35.07  ? 53  PHE C C     1 
ATOM   2021 O O     . PHE C 3 7   ? 3.338   -48.147 -14.817 1.00 33.61  ? 53  PHE C O     1 
ATOM   2022 C CB    . PHE C 3 7   ? 0.532   -47.726 -13.096 1.00 35.57  ? 53  PHE C CB    1 
ATOM   2023 C CG    . PHE C 3 7   ? -0.670  -48.405 -12.503 1.00 31.08  ? 53  PHE C CG    1 
ATOM   2024 C CD1   . PHE C 3 7   ? -0.529  -49.566 -11.761 1.00 34.05  ? 53  PHE C CD1   1 
ATOM   2025 C CD2   . PHE C 3 7   ? -1.931  -47.867 -12.666 1.00 30.13  ? 53  PHE C CD2   1 
ATOM   2026 C CE1   . PHE C 3 7   ? -1.636  -50.191 -11.207 1.00 38.94  ? 53  PHE C CE1   1 
ATOM   2027 C CE2   . PHE C 3 7   ? -3.049  -48.488 -12.118 1.00 40.25  ? 53  PHE C CE2   1 
ATOM   2028 C CZ    . PHE C 3 7   ? -2.900  -49.650 -11.386 1.00 37.97  ? 53  PHE C CZ    1 
ATOM   2029 N N     . THR C 3 8   ? 2.146   -46.310 -15.317 1.00 34.58  ? 54  THR C N     1 
ATOM   2030 C CA    . THR C 3 8   ? 3.333   -45.517 -15.588 1.00 36.85  ? 54  THR C CA    1 
ATOM   2031 C C     . THR C 3 8   ? 4.026   -45.135 -14.275 1.00 39.28  ? 54  THR C C     1 
ATOM   2032 O O     . THR C 3 8   ? 3.495   -45.321 -13.181 1.00 44.27  ? 54  THR C O     1 
ATOM   2033 C CB    . THR C 3 8   ? 2.973   -44.265 -16.386 1.00 35.64  ? 54  THR C CB    1 
ATOM   2034 O OG1   . THR C 3 8   ? 1.923   -43.544 -15.727 1.00 32.85  ? 54  THR C OG1   1 
ATOM   2035 C CG2   . THR C 3 8   ? 2.524   -44.639 -17.773 1.00 33.18  ? 54  THR C CG2   1 
ATOM   2036 N N     . ALA C 3 9   ? 5.227   -44.590 -14.393 1.00 41.99  ? 55  ALA C N     1 
ATOM   2037 C CA    . ALA C 3 9   ? 6.083   -44.356 -13.237 1.00 41.24  ? 55  ALA C CA    1 
ATOM   2038 C C     . ALA C 3 9   ? 5.810   -43.006 -12.569 1.00 41.56  ? 55  ALA C C     1 
ATOM   2039 O O     . ALA C 3 9   ? 5.229   -42.088 -13.156 1.00 40.47  ? 55  ALA C O     1 
ATOM   2040 C CB    . ALA C 3 9   ? 7.546   -44.443 -13.653 1.00 38.28  ? 55  ALA C CB    1 
ATOM   2041 N N     . LEU C 3 10  ? 6.220   -42.909 -11.306 1.00 42.82  ? 56  LEU C N     1 
ATOM   2042 C CA    . LEU C 3 10  ? 6.387   -41.638 -10.612 1.00 44.83  ? 56  LEU C CA    1 
ATOM   2043 C C     . LEU C 3 10  ? 7.869   -41.284 -10.626 1.00 42.68  ? 56  LEU C C     1 
ATOM   2044 O O     . LEU C 3 10  ? 8.688   -42.074 -10.152 1.00 44.70  ? 56  LEU C O     1 
ATOM   2045 C CB    . LEU C 3 10  ? 5.901   -41.732 -9.174  1.00 44.08  ? 56  LEU C CB    1 
ATOM   2046 C CG    . LEU C 3 10  ? 4.456   -41.453 -8.878  1.00 48.10  ? 56  LEU C CG    1 
ATOM   2047 C CD1   . LEU C 3 10  ? 4.311   -41.417 -7.371  1.00 45.38  ? 56  LEU C CD1   1 
ATOM   2048 C CD2   . LEU C 3 10  ? 4.081   -40.120 -9.514  1.00 52.25  ? 56  LEU C CD2   1 
ATOM   2049 N N     . THR C 3 11  ? 8.218   -40.106 -11.151 1.00 43.82  ? 57  THR C N     1 
ATOM   2050 C CA    . THR C 3 11  ? 9.625   -39.719 -11.266 1.00 44.61  ? 57  THR C CA    1 
ATOM   2051 C C     . THR C 3 11  ? 10.063  -38.901 -10.062 1.00 41.07  ? 57  THR C C     1 
ATOM   2052 O O     . THR C 3 11  ? 9.428   -37.911 -9.708  1.00 44.59  ? 57  THR C O     1 
ATOM   2053 C CB    . THR C 3 11  ? 9.906   -38.915 -12.534 1.00 42.09  ? 57  THR C CB    1 
ATOM   2054 O OG1   . THR C 3 11  ? 9.495   -39.657 -13.681 1.00 41.86  ? 57  THR C OG1   1 
ATOM   2055 C CG2   . THR C 3 11  ? 11.401  -38.645 -12.651 1.00 46.65  ? 57  THR C CG2   1 
ATOM   2056 N N     . GLN C 3 12  ? 11.169  -39.305 -9.453  1.00 47.10  ? 58  GLN C N     1 
ATOM   2057 C CA    . GLN C 3 12  ? 11.718  -38.591 -8.304  1.00 53.15  ? 58  GLN C CA    1 
ATOM   2058 C C     . GLN C 3 12  ? 12.585  -37.448 -8.814  1.00 49.35  ? 58  GLN C C     1 
ATOM   2059 O O     . GLN C 3 12  ? 13.779  -37.601 -9.043  1.00 50.23  ? 58  GLN C O     1 
ATOM   2060 C CB    . GLN C 3 12  ? 12.513  -39.542 -7.424  1.00 56.55  ? 58  GLN C CB    1 
ATOM   2061 C CG    . GLN C 3 12  ? 12.906  -38.974 -6.084  1.00 55.91  ? 58  GLN C CG    1 
ATOM   2062 C CD    . GLN C 3 12  ? 13.613  -40.006 -5.230  1.00 60.34  ? 58  GLN C CD    1 
ATOM   2063 O OE1   . GLN C 3 12  ? 14.176  -40.969 -5.745  1.00 58.44  ? 58  GLN C OE1   1 
ATOM   2064 N NE2   . GLN C 3 12  ? 13.583  -39.811 -3.920  1.00 64.40  ? 58  GLN C NE2   1 
ATOM   2065 N N     . HIS C 3 13  ? 11.962  -36.288 -9.017  1.00 54.67  ? 59  HIS C N     1 
ATOM   2066 C CA    . HIS C 3 13  ? 12.692  -35.118 -9.486  1.00 50.45  ? 59  HIS C CA    1 
ATOM   2067 C C     . HIS C 3 13  ? 13.509  -34.490 -8.362  1.00 56.30  ? 59  HIS C C     1 
ATOM   2068 O O     . HIS C 3 13  ? 14.576  -33.919 -8.617  1.00 53.33  ? 59  HIS C O     1 
ATOM   2069 C CB    . HIS C 3 13  ? 11.717  -34.096 -10.098 1.00 48.76  ? 59  HIS C CB    1 
ATOM   2070 C CG    . HIS C 3 13  ? 11.112  -34.527 -11.407 1.00 46.95  ? 59  HIS C CG    1 
ATOM   2071 N ND1   . HIS C 3 13  ? 11.873  -34.846 -12.512 1.00 52.03  ? 59  HIS C ND1   1 
ATOM   2072 C CD2   . HIS C 3 13  ? 9.820   -34.685 -11.787 1.00 48.47  ? 59  HIS C CD2   1 
ATOM   2073 C CE1   . HIS C 3 13  ? 11.077  -35.184 -13.513 1.00 50.34  ? 59  HIS C CE1   1 
ATOM   2074 N NE2   . HIS C 3 13  ? 9.825   -35.091 -13.101 1.00 47.11  ? 59  HIS C NE2   1 
ATOM   2075 N N     . GLY C 3 14  ? 13.051  -34.625 -7.123  1.00 58.36  ? 60  GLY C N     1 
ATOM   2076 C CA    . GLY C 3 14  ? 13.682  -34.045 -5.950  1.00 61.88  ? 60  GLY C CA    1 
ATOM   2077 C C     . GLY C 3 14  ? 14.501  -35.041 -5.155  1.00 62.80  ? 60  GLY C C     1 
ATOM   2078 O O     . GLY C 3 14  ? 15.023  -36.028 -5.688  1.00 62.05  ? 60  GLY C O     1 
ATOM   2079 N N     . LYS C 3 15  ? 14.622  -34.779 -3.855  1.00 60.18  ? 61  LYS C N     1 
ATOM   2080 C CA    . LYS C 3 15  ? 15.504  -35.558 -3.000  1.00 66.57  ? 61  LYS C CA    1 
ATOM   2081 C C     . LYS C 3 15  ? 14.775  -36.432 -1.991  1.00 66.07  ? 61  LYS C C     1 
ATOM   2082 O O     . LYS C 3 15  ? 15.321  -37.459 -1.584  1.00 60.62  ? 61  LYS C O     1 
ATOM   2083 C CB    . LYS C 3 15  ? 16.478  -34.628 -2.260  1.00 74.43  ? 61  LYS C CB    1 
ATOM   2084 C CG    . LYS C 3 15  ? 15.985  -33.182 -2.119  1.00 76.26  ? 61  LYS C CG    1 
ATOM   2085 C CD    . LYS C 3 15  ? 17.018  -32.271 -1.441  1.00 77.64  ? 61  LYS C CD    1 
ATOM   2086 C CE    . LYS C 3 15  ? 18.148  -31.879 -2.391  1.00 83.28  ? 61  LYS C CE    1 
ATOM   2087 N NZ    . LYS C 3 15  ? 19.182  -31.011 -1.739  1.00 78.43  ? 61  LYS C NZ    1 
ATOM   2088 N N     . GLU C 3 16  ? 13.554  -36.068 -1.595  1.00 66.68  ? 62  GLU C N     1 
ATOM   2089 C CA    . GLU C 3 16  ? 12.755  -36.937 -0.738  1.00 66.51  ? 62  GLU C CA    1 
ATOM   2090 C C     . GLU C 3 16  ? 12.486  -38.274 -1.430  1.00 70.71  ? 62  GLU C C     1 
ATOM   2091 O O     . GLU C 3 16  ? 12.364  -38.350 -2.656  1.00 72.29  ? 62  GLU C O     1 
ATOM   2092 C CB    . GLU C 3 16  ? 11.418  -36.275 -0.386  1.00 64.21  ? 62  GLU C CB    1 
ATOM   2093 C CG    . GLU C 3 16  ? 11.479  -35.039 0.504   1.00 70.64  ? 62  GLU C CG    1 
ATOM   2094 C CD    . GLU C 3 16  ? 10.144  -34.763 1.231   1.00 76.43  ? 62  GLU C CD    1 
ATOM   2095 O OE1   . GLU C 3 16  ? 9.798   -35.532 2.162   1.00 72.40  ? 62  GLU C OE1   1 
ATOM   2096 O OE2   . GLU C 3 16  ? 9.437   -33.787 0.871   1.00 72.18  ? 62  GLU C OE2   1 
ATOM   2097 N N     . ASP C 3 17  ? 12.402  -39.342 -0.639  1.00 66.96  ? 63  ASP C N     1 
ATOM   2098 C CA    . ASP C 3 17  ? 11.992  -40.626 -1.184  1.00 59.25  ? 63  ASP C CA    1 
ATOM   2099 C C     . ASP C 3 17  ? 10.476  -40.763 -1.073  1.00 64.19  ? 63  ASP C C     1 
ATOM   2100 O O     . ASP C 3 17  ? 9.793   -39.943 -0.452  1.00 60.96  ? 63  ASP C O     1 
ATOM   2101 C CB    . ASP C 3 17  ? 12.723  -41.780 -0.487  1.00 64.12  ? 63  ASP C CB    1 
ATOM   2102 C CG    . ASP C 3 17  ? 14.197  -41.872 -0.901  1.00 68.35  ? 63  ASP C CG    1 
ATOM   2103 O OD1   . ASP C 3 17  ? 14.747  -40.840 -1.347  1.00 69.10  ? 63  ASP C OD1   1 
ATOM   2104 O OD2   . ASP C 3 17  ? 14.805  -42.966 -0.798  1.00 60.39  ? 63  ASP C OD2   1 
ATOM   2105 N N     . LEU C 3 18  ? 9.938   -41.802 -1.707  1.00 59.45  ? 64  LEU C N     1 
ATOM   2106 C CA    . LEU C 3 18  ? 8.492   -41.912 -1.828  1.00 53.63  ? 64  LEU C CA    1 
ATOM   2107 C C     . LEU C 3 18  ? 7.882   -42.417 -0.524  1.00 49.43  ? 64  LEU C C     1 
ATOM   2108 O O     . LEU C 3 18  ? 8.437   -43.288 0.144   1.00 57.85  ? 64  LEU C O     1 
ATOM   2109 C CB    . LEU C 3 18  ? 8.139   -42.825 -3.000  1.00 50.36  ? 64  LEU C CB    1 
ATOM   2110 C CG    . LEU C 3 18  ? 6.735   -42.773 -3.581  1.00 50.45  ? 64  LEU C CG    1 
ATOM   2111 C CD1   . LEU C 3 18  ? 6.160   -41.364 -3.577  1.00 49.30  ? 64  LEU C CD1   1 
ATOM   2112 C CD2   . LEU C 3 18  ? 6.794   -43.322 -4.985  1.00 47.38  ? 64  LEU C CD2   1 
ATOM   2113 N N     . LYS C 3 19  ? 6.742   -41.847 -0.149  1.00 47.64  ? 65  LYS C N     1 
ATOM   2114 C CA    . LYS C 3 19  ? 6.154   -42.125 1.149   1.00 46.29  ? 65  LYS C CA    1 
ATOM   2115 C C     . LYS C 3 19  ? 4.689   -41.737 1.092   1.00 53.07  ? 65  LYS C C     1 
ATOM   2116 O O     . LYS C 3 19  ? 4.338   -40.729 0.472   1.00 50.23  ? 65  LYS C O     1 
ATOM   2117 C CB    . LYS C 3 19  ? 6.881   -41.340 2.252   1.00 57.34  ? 65  LYS C CB    1 
ATOM   2118 C CG    . LYS C 3 19  ? 6.559   -41.750 3.691   1.00 57.27  ? 65  LYS C CG    1 
ATOM   2119 C CD    . LYS C 3 19  ? 7.605   -41.217 4.703   1.00 63.51  ? 65  LYS C CD    1 
ATOM   2120 C CE    . LYS C 3 19  ? 7.348   -39.761 5.130   1.00 62.62  ? 65  LYS C CE    1 
ATOM   2121 N NZ    . LYS C 3 19  ? 8.270   -39.282 6.217   1.00 52.87  ? 65  LYS C NZ    1 
ATOM   2122 N N     . PHE C 3 20  ? 3.839   -42.528 1.742   1.00 51.37  ? 66  PHE C N     1 
ATOM   2123 C CA    . PHE C 3 20  ? 2.429   -42.212 1.754   1.00 51.79  ? 66  PHE C CA    1 
ATOM   2124 C C     . PHE C 3 20  ? 1.794   -42.409 3.126   1.00 50.22  ? 66  PHE C C     1 
ATOM   2125 O O     . PHE C 3 20  ? 2.101   -43.382 3.830   1.00 50.71  ? 66  PHE C O     1 
ATOM   2126 C CB    . PHE C 3 20  ? 1.678   -43.065 0.719   1.00 51.82  ? 66  PHE C CB    1 
ATOM   2127 C CG    . PHE C 3 20  ? 1.953   -42.679 -0.717  1.00 50.06  ? 66  PHE C CG    1 
ATOM   2128 C CD1   . PHE C 3 20  ? 2.995   -43.251 -1.414  1.00 49.33  ? 66  PHE C CD1   1 
ATOM   2129 C CD2   . PHE C 3 20  ? 1.153   -41.758 -1.365  1.00 46.06  ? 66  PHE C CD2   1 
ATOM   2130 C CE1   . PHE C 3 20  ? 3.243   -42.905 -2.723  1.00 50.98  ? 66  PHE C CE1   1 
ATOM   2131 C CE2   . PHE C 3 20  ? 1.396   -41.412 -2.671  1.00 47.75  ? 66  PHE C CE2   1 
ATOM   2132 C CZ    . PHE C 3 20  ? 2.446   -41.983 -3.350  1.00 46.63  ? 66  PHE C CZ    1 
ATOM   2133 N N     . PRO C 3 21  ? 0.889   -41.519 3.516   1.00 49.97  ? 67  PRO C N     1 
ATOM   2134 C CA    . PRO C 3 21  ? 0.035   -41.805 4.674   1.00 54.52  ? 67  PRO C CA    1 
ATOM   2135 C C     . PRO C 3 21  ? -0.736  -43.105 4.469   1.00 57.66  ? 67  PRO C C     1 
ATOM   2136 O O     . PRO C 3 21  ? -1.182  -43.419 3.358   1.00 57.05  ? 67  PRO C O     1 
ATOM   2137 C CB    . PRO C 3 21  ? -0.913  -40.601 4.728   1.00 51.16  ? 67  PRO C CB    1 
ATOM   2138 C CG    . PRO C 3 21  ? -0.307  -39.560 3.843   1.00 53.97  ? 67  PRO C CG    1 
ATOM   2139 C CD    . PRO C 3 21  ? 0.538   -40.257 2.841   1.00 49.67  ? 67  PRO C CD    1 
ATOM   2140 N N     . ARG C 3 22  ? -0.875  -43.871 5.551   1.00 56.91  ? 68  ARG C N     1 
ATOM   2141 C CA    . ARG C 3 22  ? -1.724  -45.056 5.527   1.00 57.58  ? 68  ARG C CA    1 
ATOM   2142 C C     . ARG C 3 22  ? -3.076  -44.723 4.900   1.00 55.01  ? 68  ARG C C     1 
ATOM   2143 O O     . ARG C 3 22  ? -3.640  -43.646 5.121   1.00 52.65  ? 68  ARG C O     1 
ATOM   2144 C CB    . ARG C 3 22  ? -1.919  -45.596 6.950   1.00 65.33  ? 68  ARG C CB    1 
ATOM   2145 C CG    . ARG C 3 22  ? -0.945  -46.693 7.404   1.00 65.76  ? 68  ARG C CG    1 
ATOM   2146 C CD    . ARG C 3 22  ? -1.150  -47.074 8.890   1.00 66.62  ? 68  ARG C CD    1 
ATOM   2147 N NE    . ARG C 3 22  ? -2.557  -47.249 9.253   1.00 67.24  ? 68  ARG C NE    1 
ATOM   2148 C CZ    . ARG C 3 22  ? -3.309  -46.338 9.869   1.00 62.58  ? 68  ARG C CZ    1 
ATOM   2149 N NH1   . ARG C 3 22  ? -2.815  -45.167 10.242  1.00 54.10  ? 68  ARG C NH1   1 
ATOM   2150 N NH2   . ARG C 3 22  ? -4.596  -46.604 10.102  1.00 61.14  ? 68  ARG C NH2   1 
ATOM   2151 N N     . GLY C 3 23  ? -3.580  -45.646 4.087   1.00 51.83  ? 69  GLY C N     1 
ATOM   2152 C CA    . GLY C 3 23  ? -4.819  -45.426 3.369   1.00 55.55  ? 69  GLY C CA    1 
ATOM   2153 C C     . GLY C 3 23  ? -4.681  -44.683 2.060   1.00 47.16  ? 69  GLY C C     1 
ATOM   2154 O O     . GLY C 3 23  ? -5.694  -44.440 1.397   1.00 49.80  ? 69  GLY C O     1 
ATOM   2155 N N     . GLN C 3 24  ? -3.466  -44.332 1.662   1.00 44.45  ? 70  GLN C N     1 
ATOM   2156 C CA    . GLN C 3 24  ? -3.229  -43.487 0.500   1.00 49.49  ? 70  GLN C CA    1 
ATOM   2157 C C     . GLN C 3 24  ? -2.084  -44.040 -0.325  1.00 46.91  ? 70  GLN C C     1 
ATOM   2158 O O     . GLN C 3 24  ? -1.173  -44.676 0.210   1.00 43.12  ? 70  GLN C O     1 
ATOM   2159 C CB    . GLN C 3 24  ? -2.860  -42.060 0.890   1.00 49.60  ? 70  GLN C CB    1 
ATOM   2160 C CG    . GLN C 3 24  ? -4.012  -41.260 1.402   1.00 50.15  ? 70  GLN C CG    1 
ATOM   2161 C CD    . GLN C 3 24  ? -3.629  -39.829 1.560   1.00 49.60  ? 70  GLN C CD    1 
ATOM   2162 O OE1   . GLN C 3 24  ? -2.467  -39.479 1.410   1.00 53.90  ? 70  GLN C OE1   1 
ATOM   2163 N NE2   . GLN C 3 24  ? -4.602  -38.983 1.864   1.00 55.20  ? 70  GLN C NE2   1 
ATOM   2164 N N     . GLY C 3 25  ? -2.121  -43.744 -1.626  1.00 41.35  ? 71  GLY C N     1 
ATOM   2165 C CA    . GLY C 3 25  ? -1.023  -44.042 -2.522  1.00 44.50  ? 71  GLY C CA    1 
ATOM   2166 C C     . GLY C 3 25  ? -1.235  -45.196 -3.477  1.00 46.06  ? 71  GLY C C     1 
ATOM   2167 O O     . GLY C 3 25  ? -0.308  -45.522 -4.232  1.00 42.93  ? 71  GLY C O     1 
ATOM   2168 N N     . VAL C 3 26  ? -2.403  -45.837 -3.466  1.00 47.70  ? 72  VAL C N     1 
ATOM   2169 C CA    . VAL C 3 26  ? -2.684  -46.914 -4.415  1.00 45.52  ? 72  VAL C CA    1 
ATOM   2170 C C     . VAL C 3 26  ? -3.275  -46.285 -5.669  1.00 42.13  ? 72  VAL C C     1 
ATOM   2171 O O     . VAL C 3 26  ? -4.246  -45.520 -5.575  1.00 48.05  ? 72  VAL C O     1 
ATOM   2172 C CB    . VAL C 3 26  ? -3.621  -47.982 -3.825  1.00 46.09  ? 72  VAL C CB    1 
ATOM   2173 C CG1   . VAL C 3 26  ? -3.866  -49.094 -4.845  1.00 48.23  ? 72  VAL C CG1   1 
ATOM   2174 C CG2   . VAL C 3 26  ? -3.040  -48.573 -2.550  1.00 47.63  ? 72  VAL C CG2   1 
ATOM   2175 N N     . PRO C 3 27  ? -2.721  -46.557 -6.846  1.00 43.42  ? 73  PRO C N     1 
ATOM   2176 C CA    . PRO C 3 27  ? -3.246  -45.941 -8.071  1.00 43.71  ? 73  PRO C CA    1 
ATOM   2177 C C     . PRO C 3 27  ? -4.702  -46.298 -8.329  1.00 45.67  ? 73  PRO C C     1 
ATOM   2178 O O     . PRO C 3 27  ? -5.171  -47.384 -7.989  1.00 53.36  ? 73  PRO C O     1 
ATOM   2179 C CB    . PRO C 3 27  ? -2.336  -46.504 -9.167  1.00 39.01  ? 73  PRO C CB    1 
ATOM   2180 C CG    . PRO C 3 27  ? -1.056  -46.837 -8.461  1.00 39.85  ? 73  PRO C CG    1 
ATOM   2181 C CD    . PRO C 3 27  ? -1.430  -47.242 -7.067  1.00 39.92  ? 73  PRO C CD    1 
ATOM   2182 N N     . ILE C 3 28  ? -5.424  -45.349 -8.929  1.00 40.90  ? 74  ILE C N     1 
ATOM   2183 C CA    . ILE C 3 28  ? -6.790  -45.608 -9.368  1.00 47.29  ? 74  ILE C CA    1 
ATOM   2184 C C     . ILE C 3 28  ? -6.792  -46.653 -10.476 1.00 49.76  ? 74  ILE C C     1 
ATOM   2185 O O     . ILE C 3 28  ? -6.108  -46.497 -11.499 1.00 45.88  ? 74  ILE C O     1 
ATOM   2186 C CB    . ILE C 3 28  ? -7.440  -44.305 -9.851  1.00 47.73  ? 74  ILE C CB    1 
ATOM   2187 C CG1   . ILE C 3 28  ? -7.441  -43.260 -8.743  1.00 46.54  ? 74  ILE C CG1   1 
ATOM   2188 C CG2   . ILE C 3 28  ? -8.848  -44.572 -10.331 1.00 51.73  ? 74  ILE C CG2   1 
ATOM   2189 C CD1   . ILE C 3 28  ? -7.719  -41.866 -9.246  1.00 48.04  ? 74  ILE C CD1   1 
ATOM   2190 N N     . ASN C 3 29  ? -7.565  -47.731 -10.279 1.00 48.18  ? 75  ASN C N     1 
ATOM   2191 C CA    . ASN C 3 29  ? -7.740  -48.766 -11.307 1.00 47.94  ? 75  ASN C CA    1 
ATOM   2192 C C     . ASN C 3 29  ? -9.125  -49.388 -11.128 1.00 48.74  ? 75  ASN C C     1 
ATOM   2193 O O     . ASN C 3 29  ? -9.304  -50.275 -10.289 1.00 45.13  ? 75  ASN C O     1 
ATOM   2194 C CB    . ASN C 3 29  ? -6.650  -49.830 -11.239 1.00 45.70  ? 75  ASN C CB    1 
ATOM   2195 C CG    . ASN C 3 29  ? -6.906  -50.998 -12.198 1.00 48.75  ? 75  ASN C CG    1 
ATOM   2196 O OD1   . ASN C 3 29  ? -7.719  -50.895 -13.122 1.00 47.14  ? 75  ASN C OD1   1 
ATOM   2197 N ND2   . ASN C 3 29  ? -6.207  -52.108 -11.984 1.00 42.97  ? 75  ASN C ND2   1 
ATOM   2198 N N     . THR C 3 30  ? -10.077 -48.952 -11.957 1.00 53.47  ? 76  THR C N     1 
ATOM   2199 C CA    . THR C 3 30  ? -11.449 -49.452 -11.917 1.00 54.55  ? 76  THR C CA    1 
ATOM   2200 C C     . THR C 3 30  ? -11.569 -50.923 -12.317 1.00 56.12  ? 76  THR C C     1 
ATOM   2201 O O     . THR C 3 30  ? -12.617 -51.524 -12.076 1.00 63.71  ? 76  THR C O     1 
ATOM   2202 C CB    . THR C 3 30  ? -12.351 -48.594 -12.821 1.00 56.83  ? 76  THR C CB    1 
ATOM   2203 O OG1   . THR C 3 30  ? -11.883 -48.641 -14.174 1.00 57.75  ? 76  THR C OG1   1 
ATOM   2204 C CG2   . THR C 3 30  ? -12.353 -47.149 -12.364 1.00 56.35  ? 76  THR C CG2   1 
ATOM   2205 N N     . ASN C 3 31  ? -10.545 -51.521 -12.919 1.00 56.35  ? 77  ASN C N     1 
ATOM   2206 C CA    . ASN C 3 31  ? -10.563 -52.950 -13.218 1.00 58.51  ? 77  ASN C CA    1 
ATOM   2207 C C     . ASN C 3 31  ? -10.148 -53.809 -12.027 1.00 53.17  ? 77  ASN C C     1 
ATOM   2208 O O     . ASN C 3 31  ? -9.747  -54.961 -12.218 1.00 56.82  ? 77  ASN C O     1 
ATOM   2209 C CB    . ASN C 3 31  ? -9.656  -53.254 -14.416 1.00 58.53  ? 77  ASN C CB    1 
ATOM   2210 C CG    . ASN C 3 31  ? -10.232 -52.749 -15.720 1.00 61.06  ? 77  ASN C CG    1 
ATOM   2211 O OD1   . ASN C 3 31  ? -11.305 -52.140 -15.741 1.00 59.82  ? 77  ASN C OD1   1 
ATOM   2212 N ND2   . ASN C 3 31  ? -9.522  -52.996 -16.819 1.00 65.50  ? 77  ASN C ND2   1 
ATOM   2213 N N     . SER C 3 32  ? -10.208 -53.267 -10.817 1.00 50.66  ? 78  SER C N     1 
ATOM   2214 C CA    . SER C 3 32  ? -9.823  -53.981 -9.612  1.00 51.16  ? 78  SER C CA    1 
ATOM   2215 C C     . SER C 3 32  ? -10.836 -53.666 -8.518  1.00 50.88  ? 78  SER C C     1 
ATOM   2216 O O     . SER C 3 32  ? -11.585 -52.690 -8.598  1.00 51.25  ? 78  SER C O     1 
ATOM   2217 C CB    . SER C 3 32  ? -8.403  -53.608 -9.171  1.00 46.44  ? 78  SER C CB    1 
ATOM   2218 O OG    . SER C 3 32  ? -8.334  -52.219 -8.899  1.00 48.65  ? 78  SER C OG    1 
ATOM   2219 N N     . SER C 3 33  ? -10.854 -54.506 -7.503  1.00 56.67  ? 79  SER C N     1 
ATOM   2220 C CA    . SER C 3 33  ? -11.830 -54.477 -6.421  1.00 54.41  ? 79  SER C CA    1 
ATOM   2221 C C     . SER C 3 33  ? -11.227 -53.865 -5.166  1.00 52.38  ? 79  SER C C     1 
ATOM   2222 O O     . SER C 3 33  ? -10.006 -53.723 -5.063  1.00 50.84  ? 79  SER C O     1 
ATOM   2223 C CB    . SER C 3 33  ? -12.314 -55.895 -6.128  1.00 48.80  ? 79  SER C CB    1 
ATOM   2224 O OG    . SER C 3 33  ? -12.916 -56.443 -7.275  1.00 51.78  ? 79  SER C OG    1 
ATOM   2225 N N     . PRO C 3 34  ? -12.060 -53.476 -4.189  1.00 49.53  ? 80  PRO C N     1 
ATOM   2226 C CA    . PRO C 3 34  ? -11.507 -52.909 -2.950  1.00 49.92  ? 80  PRO C CA    1 
ATOM   2227 C C     . PRO C 3 34  ? -10.536 -53.836 -2.246  1.00 55.37  ? 80  PRO C C     1 
ATOM   2228 O O     . PRO C 3 34  ? -9.622  -53.358 -1.560  1.00 52.75  ? 80  PRO C O     1 
ATOM   2229 C CB    . PRO C 3 34  ? -12.754 -52.632 -2.092  1.00 56.20  ? 80  PRO C CB    1 
ATOM   2230 C CG    . PRO C 3 34  ? -13.923 -53.237 -2.836  1.00 54.43  ? 80  PRO C CG    1 
ATOM   2231 C CD    . PRO C 3 34  ? -13.522 -53.304 -4.263  1.00 55.81  ? 80  PRO C CD    1 
ATOM   2232 N N     . ASP C 3 35  ? -10.682 -55.150 -2.418  1.00 54.29  ? 81  ASP C N     1 
ATOM   2233 C CA    . ASP C 3 35  ? -9.746  -56.079 -1.791  1.00 53.28  ? 81  ASP C CA    1 
ATOM   2234 C C     . ASP C 3 35  ? -8.346  -56.007 -2.396  1.00 55.21  ? 81  ASP C C     1 
ATOM   2235 O O     . ASP C 3 35  ? -7.358  -56.276 -1.694  1.00 50.79  ? 81  ASP C O     1 
ATOM   2236 C CB    . ASP C 3 35  ? -10.292 -57.495 -1.899  1.00 52.49  ? 81  ASP C CB    1 
ATOM   2237 C CG    . ASP C 3 35  ? -11.288 -57.807 -0.813  1.00 63.49  ? 81  ASP C CG    1 
ATOM   2238 O OD1   . ASP C 3 35  ? -12.413 -57.243 -0.824  1.00 57.09  ? 81  ASP C OD1   1 
ATOM   2239 O OD2   . ASP C 3 35  ? -10.925 -58.616 0.068   1.00 65.61  ? 81  ASP C OD2   1 
ATOM   2240 N N     . ASP C 3 36  ? -8.235  -55.677 -3.690  1.00 53.93  ? 82  ASP C N     1 
ATOM   2241 C CA    . ASP C 3 36  ? -6.946  -55.684 -4.390  1.00 52.68  ? 82  ASP C CA    1 
ATOM   2242 C C     . ASP C 3 36  ? -6.089  -54.465 -4.098  1.00 50.50  ? 82  ASP C C     1 
ATOM   2243 O O     . ASP C 3 36  ? -4.917  -54.440 -4.492  1.00 48.86  ? 82  ASP C O     1 
ATOM   2244 C CB    . ASP C 3 36  ? -7.141  -55.726 -5.906  1.00 49.21  ? 82  ASP C CB    1 
ATOM   2245 C CG    . ASP C 3 36  ? -8.154  -56.734 -6.337  1.00 52.12  ? 82  ASP C CG    1 
ATOM   2246 O OD1   . ASP C 3 36  ? -7.967  -57.934 -6.045  1.00 56.86  ? 82  ASP C OD1   1 
ATOM   2247 O OD2   . ASP C 3 36  ? -9.142  -56.315 -6.969  1.00 52.19  ? 82  ASP C OD2   1 
ATOM   2248 N N     . GLN C 3 37  ? -6.652  -53.448 -3.454  1.00 51.22  ? 83  GLN C N     1 
ATOM   2249 C CA    . GLN C 3 37  ? -6.048  -52.126 -3.414  1.00 47.87  ? 83  GLN C CA    1 
ATOM   2250 C C     . GLN C 3 37  ? -4.924  -52.089 -2.381  1.00 43.81  ? 83  GLN C C     1 
ATOM   2251 O O     . GLN C 3 37  ? -5.006  -51.418 -1.355  1.00 48.41  ? 83  GLN C O     1 
ATOM   2252 C CB    . GLN C 3 37  ? -7.116  -51.093 -3.114  1.00 45.21  ? 83  GLN C CB    1 
ATOM   2253 C CG    . GLN C 3 37  ? -8.301  -51.178 -4.035  1.00 53.16  ? 83  GLN C CG    1 
ATOM   2254 C CD    . GLN C 3 37  ? -7.922  -50.878 -5.464  1.00 53.31  ? 83  GLN C CD    1 
ATOM   2255 O OE1   . GLN C 3 37  ? -7.022  -50.074 -5.724  1.00 52.49  ? 83  GLN C OE1   1 
ATOM   2256 N NE2   . GLN C 3 37  ? -8.606  -51.524 -6.405  1.00 50.39  ? 83  GLN C NE2   1 
ATOM   2257 N N     . ILE C 3 38  ? -3.835  -52.786 -2.705  1.00 45.51  ? 84  ILE C N     1 
ATOM   2258 C CA    . ILE C 3 38  ? -2.684  -52.934 -1.815  1.00 40.88  ? 84  ILE C CA    1 
ATOM   2259 C C     . ILE C 3 38  ? -1.501  -53.412 -2.647  1.00 41.60  ? 84  ILE C C     1 
ATOM   2260 O O     . ILE C 3 38  ? -1.661  -54.227 -3.557  1.00 50.06  ? 84  ILE C O     1 
ATOM   2261 C CB    . ILE C 3 38  ? -3.000  -53.919 -0.662  1.00 48.41  ? 84  ILE C CB    1 
ATOM   2262 C CG1   . ILE C 3 38  ? -1.773  -54.188 0.216   1.00 47.72  ? 84  ILE C CG1   1 
ATOM   2263 C CG2   . ILE C 3 38  ? -3.502  -55.234 -1.211  1.00 47.50  ? 84  ILE C CG2   1 
ATOM   2264 C CD1   . ILE C 3 38  ? -2.106  -54.876 1.537   1.00 43.84  ? 84  ILE C CD1   1 
ATOM   2265 N N     . GLY C 3 39  ? -0.311  -52.919 -2.319  1.00 44.18  ? 85  GLY C N     1 
ATOM   2266 C CA    . GLY C 3 39  ? 0.890   -53.312 -3.036  1.00 38.98  ? 85  GLY C CA    1 
ATOM   2267 C C     . GLY C 3 39  ? 2.039   -52.396 -2.662  1.00 44.80  ? 85  GLY C C     1 
ATOM   2268 O O     . GLY C 3 39  ? 1.981   -51.725 -1.631  1.00 49.47  ? 85  GLY C O     1 
ATOM   2269 N N     . TYR C 3 40  ? 3.069   -52.356 -3.528  1.00 42.05  ? 86  TYR C N     1 
ATOM   2270 C CA    . TYR C 3 40  ? 4.299   -51.592 -3.305  1.00 41.50  ? 86  TYR C CA    1 
ATOM   2271 C C     . TYR C 3 40  ? 4.738   -50.800 -4.541  1.00 45.27  ? 86  TYR C C     1 
ATOM   2272 O O     . TYR C 3 40  ? 4.394   -51.131 -5.675  1.00 43.59  ? 86  TYR C O     1 
ATOM   2273 C CB    . TYR C 3 40  ? 5.469   -52.499 -2.911  1.00 42.46  ? 86  TYR C CB    1 
ATOM   2274 C CG    . TYR C 3 40  ? 5.840   -53.515 -3.957  1.00 41.91  ? 86  TYR C CG    1 
ATOM   2275 C CD1   . TYR C 3 40  ? 5.128   -54.696 -4.073  1.00 41.40  ? 86  TYR C CD1   1 
ATOM   2276 C CD2   . TYR C 3 40  ? 6.899   -53.303 -4.827  1.00 44.28  ? 86  TYR C CD2   1 
ATOM   2277 C CE1   . TYR C 3 40  ? 5.451   -55.632 -5.014  1.00 40.61  ? 86  TYR C CE1   1 
ATOM   2278 C CE2   . TYR C 3 40  ? 7.230   -54.243 -5.784  1.00 39.71  ? 86  TYR C CE2   1 
ATOM   2279 C CZ    . TYR C 3 40  ? 6.494   -55.406 -5.868  1.00 40.33  ? 86  TYR C CZ    1 
ATOM   2280 O OH    . TYR C 3 40  ? 6.785   -56.366 -6.806  1.00 41.40  ? 86  TYR C OH    1 
ATOM   2281 N N     . TYR C 3 41  ? 5.542   -49.755 -4.300  1.00 49.82  ? 87  TYR C N     1 
ATOM   2282 C CA    . TYR C 3 41  ? 6.315   -49.062 -5.326  1.00 39.69  ? 87  TYR C CA    1 
ATOM   2283 C C     . TYR C 3 41  ? 7.763   -49.500 -5.264  1.00 41.84  ? 87  TYR C C     1 
ATOM   2284 O O     . TYR C 3 41  ? 8.353   -49.557 -4.185  1.00 49.02  ? 87  TYR C O     1 
ATOM   2285 C CB    . TYR C 3 41  ? 6.289   -47.546 -5.142  1.00 40.14  ? 87  TYR C CB    1 
ATOM   2286 C CG    . TYR C 3 41  ? 4.995   -46.884 -5.462  1.00 43.04  ? 87  TYR C CG    1 
ATOM   2287 C CD1   . TYR C 3 41  ? 3.965   -46.905 -4.556  1.00 41.59  ? 87  TYR C CD1   1 
ATOM   2288 C CD2   . TYR C 3 41  ? 4.803   -46.221 -6.664  1.00 41.36  ? 87  TYR C CD2   1 
ATOM   2289 C CE1   . TYR C 3 41  ? 2.775   -46.300 -4.821  1.00 43.73  ? 87  TYR C CE1   1 
ATOM   2290 C CE2   . TYR C 3 41  ? 3.594   -45.609 -6.945  1.00 36.67  ? 87  TYR C CE2   1 
ATOM   2291 C CZ    . TYR C 3 41  ? 2.585   -45.655 -6.016  1.00 41.18  ? 87  TYR C CZ    1 
ATOM   2292 O OH    . TYR C 3 41  ? 1.360   -45.062 -6.239  1.00 39.14  ? 87  TYR C OH    1 
ATOM   2293 N N     . ARG C 3 42  ? 8.354   -49.746 -6.426  1.00 40.63  ? 88  ARG C N     1 
ATOM   2294 C CA    . ARG C 3 42  ? 9.741   -50.157 -6.528  1.00 40.87  ? 88  ARG C CA    1 
ATOM   2295 C C     . ARG C 3 42  ? 10.528  -49.109 -7.302  1.00 45.93  ? 88  ARG C C     1 
ATOM   2296 O O     . ARG C 3 42  ? 10.094  -48.657 -8.365  1.00 44.88  ? 88  ARG C O     1 
ATOM   2297 C CB    . ARG C 3 42  ? 9.859   -51.507 -7.216  1.00 42.58  ? 88  ARG C CB    1 
ATOM   2298 C CG    . ARG C 3 42  ? 11.277  -51.905 -7.505  1.00 42.52  ? 88  ARG C CG    1 
ATOM   2299 C CD    . ARG C 3 42  ? 11.342  -53.219 -8.260  1.00 43.69  ? 88  ARG C CD    1 
ATOM   2300 N NE    . ARG C 3 42  ? 12.720  -53.625 -8.505  1.00 46.63  ? 88  ARG C NE    1 
ATOM   2301 C CZ    . ARG C 3 42  ? 13.401  -53.339 -9.604  1.00 51.43  ? 88  ARG C CZ    1 
ATOM   2302 N NH1   . ARG C 3 42  ? 12.880  -52.595 -10.567 1.00 51.00  ? 88  ARG C NH1   1 
ATOM   2303 N NH2   . ARG C 3 42  ? 14.635  -53.812 -9.741  1.00 54.24  ? 88  ARG C NH2   1 
ATOM   2304 N N     . ARG C 3 43  ? 11.684  -48.736 -6.775  1.00 46.26  ? 89  ARG C N     1 
ATOM   2305 C CA    . ARG C 3 43  ? 12.503  -47.695 -7.366  1.00 47.42  ? 89  ARG C CA    1 
ATOM   2306 C C     . ARG C 3 43  ? 13.444  -48.290 -8.403  1.00 52.11  ? 89  ARG C C     1 
ATOM   2307 O O     . ARG C 3 43  ? 14.171  -49.251 -8.124  1.00 51.80  ? 89  ARG C O     1 
ATOM   2308 C CB    . ARG C 3 43  ? 13.300  -46.958 -6.291  1.00 49.63  ? 89  ARG C CB    1 
ATOM   2309 C CG    . ARG C 3 43  ? 14.320  -45.978 -6.857  1.00 56.00  ? 89  ARG C CG    1 
ATOM   2310 C CD    . ARG C 3 43  ? 15.162  -45.388 -5.747  1.00 59.52  ? 89  ARG C CD    1 
ATOM   2311 N NE    . ARG C 3 43  ? 15.805  -46.441 -4.973  1.00 64.07  ? 89  ARG C NE    1 
ATOM   2312 C CZ    . ARG C 3 43  ? 16.074  -46.365 -3.677  1.00 62.85  ? 89  ARG C CZ    1 
ATOM   2313 N NH1   . ARG C 3 43  ? 15.795  -45.276 -2.977  1.00 61.68  ? 89  ARG C NH1   1 
ATOM   2314 N NH2   . ARG C 3 43  ? 16.626  -47.411 -3.067  1.00 63.35  ? 89  ARG C NH2   1 
ATOM   2315 N N     . ALA C 3 44  ? 13.428  -47.714 -9.598  1.00 50.60  ? 90  ALA C N     1 
ATOM   2316 C CA    . ALA C 3 44  ? 14.323  -48.100 -10.670 1.00 49.20  ? 90  ALA C CA    1 
ATOM   2317 C C     . ALA C 3 44  ? 15.128  -46.881 -11.076 1.00 53.08  ? 90  ALA C C     1 
ATOM   2318 O O     . ALA C 3 44  ? 14.598  -45.766 -11.136 1.00 51.86  ? 90  ALA C O     1 
ATOM   2319 C CB    . ALA C 3 44  ? 13.555  -48.653 -11.871 1.00 52.51  ? 90  ALA C CB    1 
ATOM   2320 N N     . THR C 3 45  ? 16.409  -47.097 -11.349 1.00 51.14  ? 91  THR C N     1 
ATOM   2321 C CA    . THR C 3 45  ? 17.338  -46.002 -11.572 1.00 52.72  ? 91  THR C CA    1 
ATOM   2322 C C     . THR C 3 45  ? 18.202  -46.353 -12.763 1.00 55.08  ? 91  THR C C     1 
ATOM   2323 O O     . THR C 3 45  ? 18.938  -47.344 -12.731 1.00 58.09  ? 91  THR C O     1 
ATOM   2324 C CB    . THR C 3 45  ? 18.201  -45.741 -10.335 1.00 53.96  ? 91  THR C CB    1 
ATOM   2325 O OG1   . THR C 3 45  ? 17.442  -44.979 -9.392  1.00 51.14  ? 91  THR C OG1   1 
ATOM   2326 C CG2   . THR C 3 45  ? 19.456  -44.968 -10.709 1.00 56.05  ? 91  THR C CG2   1 
ATOM   2327 N N     . ARG C 3 46  ? 18.109  -45.537 -13.801 1.00 51.38  ? 92  ARG C N     1 
ATOM   2328 C CA    . ARG C 3 46  ? 18.841  -45.746 -15.035 1.00 56.26  ? 92  ARG C CA    1 
ATOM   2329 C C     . ARG C 3 46  ? 20.112  -44.888 -15.043 1.00 55.69  ? 92  ARG C C     1 
ATOM   2330 O O     . ARG C 3 46  ? 20.282  -43.978 -14.225 1.00 49.85  ? 92  ARG C O     1 
ATOM   2331 C CB    . ARG C 3 46  ? 17.922  -45.424 -16.216 1.00 54.86  ? 92  ARG C CB    1 
ATOM   2332 C CG    . ARG C 3 46  ? 16.425  -45.422 -15.823 1.00 52.91  ? 92  ARG C CG    1 
ATOM   2333 C CD    . ARG C 3 46  ? 15.501  -45.197 -17.025 1.00 48.73  ? 92  ARG C CD    1 
ATOM   2334 N NE    . ARG C 3 46  ? 15.262  -43.782 -17.305 1.00 48.18  ? 92  ARG C NE    1 
ATOM   2335 C CZ    . ARG C 3 46  ? 15.018  -43.293 -18.515 1.00 48.06  ? 92  ARG C CZ    1 
ATOM   2336 N NH1   . ARG C 3 46  ? 15.031  -44.070 -19.593 1.00 39.71  ? 92  ARG C NH1   1 
ATOM   2337 N NH2   . ARG C 3 46  ? 14.763  -41.993 -18.649 1.00 50.13  ? 92  ARG C NH2   1 
ATOM   2338 N N     . ARG C 3 47  ? 21.019  -45.203 -15.974 1.00 53.83  ? 93  ARG C N     1 
ATOM   2339 C CA    . ARG C 3 47  ? 22.314  -44.543 -16.074 1.00 50.79  ? 93  ARG C CA    1 
ATOM   2340 C C     . ARG C 3 47  ? 22.670  -44.273 -17.531 1.00 52.92  ? 93  ARG C C     1 
ATOM   2341 O O     . ARG C 3 47  ? 22.690  -45.202 -18.343 1.00 55.36  ? 93  ARG C O     1 
ATOM   2342 C CB    . ARG C 3 47  ? 23.414  -45.400 -15.430 1.00 59.44  ? 93  ARG C CB    1 
ATOM   2343 C CG    . ARG C 3 47  ? 23.231  -45.679 -13.947 1.00 59.90  ? 93  ARG C CG    1 
ATOM   2344 C CD    . ARG C 3 47  ? 24.440  -45.192 -13.163 1.00 64.08  ? 93  ARG C CD    1 
ATOM   2345 N NE    . ARG C 3 47  ? 25.684  -45.847 -13.557 1.00 65.64  ? 93  ARG C NE    1 
ATOM   2346 C CZ    . ARG C 3 47  ? 26.895  -45.366 -13.301 1.00 70.27  ? 93  ARG C CZ    1 
ATOM   2347 N NH1   . ARG C 3 47  ? 27.065  -44.186 -12.721 1.00 65.10  ? 93  ARG C NH1   1 
ATOM   2348 N NH2   . ARG C 3 47  ? 27.965  -46.079 -13.644 1.00 71.24  ? 93  ARG C NH2   1 
ATOM   2349 N N     . ILE C 3 48  ? 23.006  -43.017 -17.844 1.00 55.00  ? 94  ILE C N     1 
ATOM   2350 C CA    . ILE C 3 48  ? 23.400  -42.590 -19.188 1.00 56.95  ? 94  ILE C CA    1 
ATOM   2351 C C     . ILE C 3 48  ? 24.857  -42.144 -19.186 1.00 61.91  ? 94  ILE C C     1 
ATOM   2352 O O     . ILE C 3 48  ? 25.412  -41.733 -18.163 1.00 62.53  ? 94  ILE C O     1 
ATOM   2353 C CB    . ILE C 3 48  ? 22.526  -41.430 -19.716 1.00 58.98  ? 94  ILE C CB    1 
ATOM   2354 C CG1   . ILE C 3 48  ? 21.902  -40.679 -18.545 1.00 58.78  ? 94  ILE C CG1   1 
ATOM   2355 C CG2   . ILE C 3 48  ? 21.489  -41.889 -20.762 1.00 54.02  ? 94  ILE C CG2   1 
ATOM   2356 C CD1   . ILE C 3 48  ? 22.870  -39.815 -17.743 1.00 65.97  ? 94  ILE C CD1   1 
ATOM   2357 N N     . ARG C 3 49  ? 25.465  -42.180 -20.372 1.00 64.62  ? 95  ARG C N     1 
ATOM   2358 C CA    . ARG C 3 49  ? 26.722  -41.479 -20.594 1.00 71.22  ? 95  ARG C CA    1 
ATOM   2359 C C     . ARG C 3 49  ? 26.440  -39.984 -20.683 1.00 75.08  ? 95  ARG C C     1 
ATOM   2360 O O     . ARG C 3 49  ? 25.621  -39.545 -21.500 1.00 67.99  ? 95  ARG C O     1 
ATOM   2361 C CB    . ARG C 3 49  ? 27.406  -41.978 -21.863 1.00 77.87  ? 95  ARG C CB    1 
ATOM   2362 C CG    . ARG C 3 49  ? 28.703  -41.232 -22.211 1.00 82.26  ? 95  ARG C CG    1 
ATOM   2363 C CD    . ARG C 3 49  ? 29.469  -41.926 -23.343 1.00 83.26  ? 95  ARG C CD    1 
ATOM   2364 N NE    . ARG C 3 49  ? 29.974  -43.234 -22.935 1.00 88.23  ? 95  ARG C NE    1 
ATOM   2365 C CZ    . ARG C 3 49  ? 31.238  -43.493 -22.621 1.00 93.52  ? 95  ARG C CZ    1 
ATOM   2366 N NH1   . ARG C 3 49  ? 32.181  -42.568 -22.722 1.00 88.08  ? 95  ARG C NH1   1 
ATOM   2367 N NH2   . ARG C 3 49  ? 31.564  -44.711 -22.193 1.00 92.18  ? 95  ARG C NH2   1 
ATOM   2368 N N     . GLY C 3 50  ? 27.119  -39.205 -19.846 1.00 78.22  ? 96  GLY C N     1 
ATOM   2369 C CA    . GLY C 3 50  ? 26.762  -37.814 -19.666 1.00 79.63  ? 96  GLY C CA    1 
ATOM   2370 C C     . GLY C 3 50  ? 27.756  -36.789 -20.171 1.00 90.39  ? 96  GLY C C     1 
ATOM   2371 O O     . GLY C 3 50  ? 27.992  -35.779 -19.499 1.00 93.27  ? 96  GLY C O     1 
ATOM   2372 N N     . GLY C 3 51  ? 28.342  -37.020 -21.344 1.00 89.40  ? 97  GLY C N     1 
ATOM   2373 C CA    . GLY C 3 51  ? 29.171  -36.003 -21.968 1.00 90.31  ? 97  GLY C CA    1 
ATOM   2374 C C     . GLY C 3 51  ? 30.614  -35.996 -21.508 1.00 91.61  ? 97  GLY C C     1 
ATOM   2375 O O     . GLY C 3 51  ? 31.532  -35.883 -22.327 1.00 83.14  ? 97  GLY C O     1 
ATOM   2376 N N     . ASP C 3 52  ? 30.834  -36.119 -20.201 1.00 90.04  ? 98  ASP C N     1 
ATOM   2377 C CA    . ASP C 3 52  ? 32.189  -36.267 -19.692 1.00 92.98  ? 98  ASP C CA    1 
ATOM   2378 C C     . ASP C 3 52  ? 32.744  -37.659 -19.940 1.00 94.32  ? 98  ASP C C     1 
ATOM   2379 O O     . ASP C 3 52  ? 33.779  -38.011 -19.363 1.00 91.79  ? 98  ASP C O     1 
ATOM   2380 C CB    . ASP C 3 52  ? 32.252  -35.953 -18.191 1.00 91.91  ? 98  ASP C CB    1 
ATOM   2381 C CG    . ASP C 3 52  ? 30.895  -35.628 -17.594 1.00 94.52  ? 98  ASP C CG    1 
ATOM   2382 O OD1   . ASP C 3 52  ? 30.125  -34.888 -18.239 1.00 92.30  ? 98  ASP C OD1   1 
ATOM   2383 O OD2   . ASP C 3 52  ? 30.604  -36.105 -16.470 1.00 94.16  ? 98  ASP C OD2   1 
ATOM   2384 N N     . GLY C 3 53  ? 32.078  -38.449 -20.786 1.00 91.96  ? 99  GLY C N     1 
ATOM   2385 C CA    . GLY C 3 53  ? 32.345  -39.865 -20.909 1.00 89.76  ? 99  GLY C CA    1 
ATOM   2386 C C     . GLY C 3 53  ? 31.933  -40.676 -19.706 1.00 92.02  ? 99  GLY C C     1 
ATOM   2387 O O     . GLY C 3 53  ? 31.877  -41.910 -19.800 1.00 91.23  ? 99  GLY C O     1 
ATOM   2388 N N     . LYS C 3 54  ? 31.628  -40.023 -18.585 1.00 90.11  ? 100 LYS C N     1 
ATOM   2389 C CA    . LYS C 3 54  ? 31.231  -40.693 -17.362 1.00 85.15  ? 100 LYS C CA    1 
ATOM   2390 C C     . LYS C 3 54  ? 29.817  -41.240 -17.501 1.00 78.54  ? 100 LYS C C     1 
ATOM   2391 O O     . LYS C 3 54  ? 29.053  -40.857 -18.392 1.00 76.95  ? 100 LYS C O     1 
ATOM   2392 C CB    . LYS C 3 54  ? 31.304  -39.729 -16.170 1.00 84.16  ? 100 LYS C CB    1 
ATOM   2393 C CG    . LYS C 3 54  ? 32.550  -38.841 -16.160 1.00 90.12  ? 100 LYS C CG    1 
ATOM   2394 C CD    . LYS C 3 54  ? 32.661  -37.976 -14.903 1.00 91.30  ? 100 LYS C CD    1 
ATOM   2395 C CE    . LYS C 3 54  ? 33.804  -36.949 -15.021 1.00 94.88  ? 100 LYS C CE    1 
ATOM   2396 N NZ    . LYS C 3 54  ? 35.168  -37.551 -15.172 1.00 87.94  ? 100 LYS C NZ    1 
ATOM   2397 N N     . MET C 3 55  ? 29.481  -42.162 -16.610 1.00 72.90  ? 101 MET C N     1 
ATOM   2398 C CA    . MET C 3 55  ? 28.106  -42.578 -16.434 1.00 66.02  ? 101 MET C CA    1 
ATOM   2399 C C     . MET C 3 55  ? 27.477  -41.717 -15.353 1.00 65.74  ? 101 MET C C     1 
ATOM   2400 O O     . MET C 3 55  ? 28.122  -41.376 -14.357 1.00 62.88  ? 101 MET C O     1 
ATOM   2401 C CB    . MET C 3 55  ? 28.020  -44.057 -16.063 1.00 67.15  ? 101 MET C CB    1 
ATOM   2402 C CG    . MET C 3 55  ? 28.648  -45.002 -17.079 1.00 67.16  ? 101 MET C CG    1 
ATOM   2403 S SD    . MET C 3 55  ? 27.871  -44.941 -18.712 1.00 68.79  ? 101 MET C SD    1 
ATOM   2404 C CE    . MET C 3 55  ? 26.363  -45.861 -18.391 1.00 65.15  ? 101 MET C CE    1 
ATOM   2405 N N     . LYS C 3 56  ? 26.218  -41.349 -15.569 1.00 63.78  ? 102 LYS C N     1 
ATOM   2406 C CA    . LYS C 3 56  ? 25.475  -40.500 -14.655 1.00 60.22  ? 102 LYS C CA    1 
ATOM   2407 C C     . LYS C 3 56  ? 24.115  -41.129 -14.406 1.00 59.94  ? 102 LYS C C     1 
ATOM   2408 O O     . LYS C 3 56  ? 23.567  -41.808 -15.274 1.00 56.85  ? 102 LYS C O     1 
ATOM   2409 C CB    . LYS C 3 56  ? 25.323  -39.084 -15.233 1.00 62.37  ? 102 LYS C CB    1 
ATOM   2410 C CG    . LYS C 3 56  ? 24.338  -38.210 -14.501 1.00 65.65  ? 102 LYS C CG    1 
ATOM   2411 C CD    . LYS C 3 56  ? 23.831  -37.077 -15.373 1.00 69.32  ? 102 LYS C CD    1 
ATOM   2412 C CE    . LYS C 3 56  ? 22.614  -36.442 -14.723 1.00 75.30  ? 102 LYS C CE    1 
ATOM   2413 N NZ    . LYS C 3 56  ? 22.818  -36.234 -13.253 1.00 75.30  ? 102 LYS C NZ    1 
ATOM   2414 N N     . ASP C 3 57  ? 23.584  -40.919 -13.209 1.00 59.07  ? 103 ASP C N     1 
ATOM   2415 C CA    . ASP C 3 57  ? 22.239  -41.372 -12.899 1.00 57.94  ? 103 ASP C CA    1 
ATOM   2416 C C     . ASP C 3 57  ? 21.210  -40.388 -13.431 1.00 58.23  ? 103 ASP C C     1 
ATOM   2417 O O     . ASP C 3 57  ? 21.294  -39.183 -13.174 1.00 56.33  ? 103 ASP C O     1 
ATOM   2418 C CB    . ASP C 3 57  ? 22.059  -41.530 -11.395 1.00 57.36  ? 103 ASP C CB    1 
ATOM   2419 C CG    . ASP C 3 57  ? 22.913  -42.619 -10.837 1.00 63.18  ? 103 ASP C CG    1 
ATOM   2420 O OD1   . ASP C 3 57  ? 24.110  -42.653 -11.191 1.00 70.81  ? 103 ASP C OD1   1 
ATOM   2421 O OD2   . ASP C 3 57  ? 22.391  -43.437 -10.053 1.00 63.00  ? 103 ASP C OD2   1 
ATOM   2422 N N     . LEU C 3 58  ? 20.235  -40.908 -14.169 1.00 52.51  ? 104 LEU C N     1 
ATOM   2423 C CA    . LEU C 3 58  ? 19.031  -40.146 -14.423 1.00 49.27  ? 104 LEU C CA    1 
ATOM   2424 C C     . LEU C 3 58  ? 18.234  -40.033 -13.135 1.00 47.75  ? 104 LEU C C     1 
ATOM   2425 O O     . LEU C 3 58  ? 18.545  -40.666 -12.125 1.00 53.80  ? 104 LEU C O     1 
ATOM   2426 C CB    . LEU C 3 58  ? 18.196  -40.816 -15.509 1.00 50.84  ? 104 LEU C CB    1 
ATOM   2427 C CG    . LEU C 3 58  ? 18.885  -40.923 -16.865 1.00 48.07  ? 104 LEU C CG    1 
ATOM   2428 C CD1   . LEU C 3 58  ? 18.323  -42.065 -17.684 1.00 48.50  ? 104 LEU C CD1   1 
ATOM   2429 C CD2   . LEU C 3 58  ? 18.747  -39.610 -17.614 1.00 52.37  ? 104 LEU C CD2   1 
ATOM   2430 N N     . SER C 3 59  ? 17.192  -39.223 -13.177 1.00 51.08  ? 105 SER C N     1 
ATOM   2431 C CA    . SER C 3 59  ? 16.277  -39.157 -12.053 1.00 51.26  ? 105 SER C CA    1 
ATOM   2432 C C     . SER C 3 59  ? 15.653  -40.536 -11.830 1.00 57.02  ? 105 SER C C     1 
ATOM   2433 O O     . SER C 3 59  ? 15.404  -41.267 -12.798 1.00 57.74  ? 105 SER C O     1 
ATOM   2434 C CB    . SER C 3 59  ? 15.199  -38.103 -12.319 1.00 50.95  ? 105 SER C CB    1 
ATOM   2435 O OG    . SER C 3 59  ? 14.932  -37.320 -11.172 1.00 51.54  ? 105 SER C OG    1 
ATOM   2436 N N     . PRO C 3 60  ? 15.441  -40.949 -10.583 1.00 55.62  ? 106 PRO C N     1 
ATOM   2437 C CA    . PRO C 3 60  ? 14.877  -42.277 -10.327 1.00 49.22  ? 106 PRO C CA    1 
ATOM   2438 C C     . PRO C 3 60  ? 13.371  -42.323 -10.548 1.00 50.43  ? 106 PRO C C     1 
ATOM   2439 O O     . PRO C 3 60  ? 12.652  -41.346 -10.319 1.00 48.15  ? 106 PRO C O     1 
ATOM   2440 C CB    . PRO C 3 60  ? 15.219  -42.527 -8.850  1.00 54.54  ? 106 PRO C CB    1 
ATOM   2441 C CG    . PRO C 3 60  ? 16.197  -41.473 -8.473  1.00 54.09  ? 106 PRO C CG    1 
ATOM   2442 C CD    . PRO C 3 60  ? 15.891  -40.303 -9.343  1.00 55.55  ? 106 PRO C CD    1 
ATOM   2443 N N     . ARG C 3 61  ? 12.891  -43.500 -10.963 1.00 46.95  ? 107 ARG C N     1 
ATOM   2444 C CA    . ARG C 3 61  ? 11.483  -43.714 -11.293 1.00 46.70  ? 107 ARG C CA    1 
ATOM   2445 C C     . ARG C 3 61  ? 10.888  -44.835 -10.448 1.00 41.85  ? 107 ARG C C     1 
ATOM   2446 O O     . ARG C 3 61  ? 11.489  -45.905 -10.316 1.00 45.88  ? 107 ARG C O     1 
ATOM   2447 C CB    . ARG C 3 61  ? 11.317  -44.018 -12.790 1.00 44.31  ? 107 ARG C CB    1 
ATOM   2448 C CG    . ARG C 3 61  ? 10.653  -42.870 -13.538 1.00 45.31  ? 107 ARG C CG    1 
ATOM   2449 C CD    . ARG C 3 61  ? 11.238  -42.587 -14.924 1.00 52.32  ? 107 ARG C CD    1 
ATOM   2450 N NE    . ARG C 3 61  ? 11.301  -43.760 -15.791 1.00 50.16  ? 107 ARG C NE    1 
ATOM   2451 C CZ    . ARG C 3 61  ? 11.533  -43.708 -17.096 1.00 52.39  ? 107 ARG C CZ    1 
ATOM   2452 N NH1   . ARG C 3 61  ? 11.659  -42.550 -17.731 1.00 50.43  ? 107 ARG C NH1   1 
ATOM   2453 N NH2   . ARG C 3 61  ? 11.633  -44.845 -17.784 1.00 50.88  ? 107 ARG C NH2   1 
ATOM   2454 N N     . TRP C 3 62  ? 9.702   -44.587 -9.893  1.00 42.05  ? 108 TRP C N     1 
ATOM   2455 C CA    . TRP C 3 62  ? 9.008   -45.505 -8.990  1.00 45.38  ? 108 TRP C CA    1 
ATOM   2456 C C     . TRP C 3 62  ? 7.815   -46.153 -9.693  1.00 45.77  ? 108 TRP C C     1 
ATOM   2457 O O     . TRP C 3 62  ? 6.859   -45.460 -10.062 1.00 44.44  ? 108 TRP C O     1 
ATOM   2458 C CB    . TRP C 3 62  ? 8.530   -44.769 -7.737  1.00 40.10  ? 108 TRP C CB    1 
ATOM   2459 C CG    . TRP C 3 62  ? 9.651   -44.332 -6.836  1.00 49.03  ? 108 TRP C CG    1 
ATOM   2460 C CD1   . TRP C 3 62  ? 10.507  -43.298 -7.048  1.00 50.08  ? 108 TRP C CD1   1 
ATOM   2461 C CD2   . TRP C 3 62  ? 10.036  -44.923 -5.589  1.00 47.93  ? 108 TRP C CD2   1 
ATOM   2462 N NE1   . TRP C 3 62  ? 11.401  -43.201 -6.014  1.00 59.82  ? 108 TRP C NE1   1 
ATOM   2463 C CE2   . TRP C 3 62  ? 11.135  -44.188 -5.102  1.00 60.11  ? 108 TRP C CE2   1 
ATOM   2464 C CE3   . TRP C 3 62  ? 9.556   -45.999 -4.834  1.00 48.02  ? 108 TRP C CE3   1 
ATOM   2465 C CZ2   . TRP C 3 62  ? 11.772  -44.497 -3.893  1.00 57.45  ? 108 TRP C CZ2   1 
ATOM   2466 C CZ3   . TRP C 3 62  ? 10.188  -46.307 -3.630  1.00 49.02  ? 108 TRP C CZ3   1 
ATOM   2467 C CH2   . TRP C 3 62  ? 11.281  -45.555 -3.175  1.00 52.51  ? 108 TRP C CH2   1 
ATOM   2468 N N     . TYR C 3 63  ? 7.848   -47.482 -9.822  1.00 46.03  ? 109 TYR C N     1 
ATOM   2469 C CA    . TYR C 3 63  ? 6.782   -48.258 -10.443 1.00 37.99  ? 109 TYR C CA    1 
ATOM   2470 C C     . TYR C 3 63  ? 5.987   -49.013 -9.389  1.00 39.67  ? 109 TYR C C     1 
ATOM   2471 O O     . TYR C 3 63  ? 6.565   -49.558 -8.450  1.00 49.07  ? 109 TYR C O     1 
ATOM   2472 C CB    . TYR C 3 63  ? 7.352   -49.258 -11.446 1.00 39.78  ? 109 TYR C CB    1 
ATOM   2473 C CG    . TYR C 3 63  ? 7.935   -48.630 -12.680 1.00 42.27  ? 109 TYR C CG    1 
ATOM   2474 C CD1   . TYR C 3 63  ? 7.136   -48.349 -13.775 1.00 42.58  ? 109 TYR C CD1   1 
ATOM   2475 C CD2   . TYR C 3 63  ? 9.279   -48.324 -12.756 1.00 41.45  ? 109 TYR C CD2   1 
ATOM   2476 C CE1   . TYR C 3 63  ? 7.652   -47.774 -14.909 1.00 41.80  ? 109 TYR C CE1   1 
ATOM   2477 C CE2   . TYR C 3 63  ? 9.813   -47.757 -13.902 1.00 46.97  ? 109 TYR C CE2   1 
ATOM   2478 C CZ    . TYR C 3 63  ? 8.986   -47.481 -14.970 1.00 47.40  ? 109 TYR C CZ    1 
ATOM   2479 O OH    . TYR C 3 63  ? 9.490   -46.918 -16.112 1.00 51.27  ? 109 TYR C OH    1 
ATOM   2480 N N     . PHE C 3 64  ? 4.667   -49.073 -9.564  1.00 40.20  ? 110 PHE C N     1 
ATOM   2481 C CA    . PHE C 3 64  ? 3.773   -49.718 -8.612  1.00 40.29  ? 110 PHE C CA    1 
ATOM   2482 C C     . PHE C 3 64  ? 3.360   -51.108 -9.073  1.00 42.78  ? 110 PHE C C     1 
ATOM   2483 O O     . PHE C 3 64  ? 2.999   -51.315 -10.235 1.00 42.31  ? 110 PHE C O     1 
ATOM   2484 C CB    . PHE C 3 64  ? 2.516   -48.899 -8.366  1.00 39.82  ? 110 PHE C CB    1 
ATOM   2485 C CG    . PHE C 3 64  ? 1.476   -49.645 -7.581  1.00 44.32  ? 110 PHE C CG    1 
ATOM   2486 C CD1   . PHE C 3 64  ? 1.593   -49.770 -6.210  1.00 42.03  ? 110 PHE C CD1   1 
ATOM   2487 C CD2   . PHE C 3 64  ? 0.397   -50.252 -8.218  1.00 41.15  ? 110 PHE C CD2   1 
ATOM   2488 C CE1   . PHE C 3 64  ? 0.663   -50.458 -5.481  1.00 41.70  ? 110 PHE C CE1   1 
ATOM   2489 C CE2   . PHE C 3 64  ? -0.548  -50.953 -7.486  1.00 42.96  ? 110 PHE C CE2   1 
ATOM   2490 C CZ    . PHE C 3 64  ? -0.416  -51.053 -6.116  1.00 45.78  ? 110 PHE C CZ    1 
ATOM   2491 N N     . TYR C 3 65  ? 3.393   -52.047 -8.133  1.00 42.35  ? 111 TYR C N     1 
ATOM   2492 C CA    . TYR C 3 65  ? 3.061   -53.444 -8.347  1.00 39.92  ? 111 TYR C CA    1 
ATOM   2493 C C     . TYR C 3 65  ? 2.103   -53.878 -7.252  1.00 40.46  ? 111 TYR C C     1 
ATOM   2494 O O     . TYR C 3 65  ? 2.347   -53.609 -6.077  1.00 44.57  ? 111 TYR C O     1 
ATOM   2495 C CB    . TYR C 3 65  ? 4.317   -54.312 -8.308  1.00 41.43  ? 111 TYR C CB    1 
ATOM   2496 C CG    . TYR C 3 65  ? 5.312   -54.028 -9.402  1.00 41.28  ? 111 TYR C CG    1 
ATOM   2497 C CD1   . TYR C 3 65  ? 5.185   -54.616 -10.651 1.00 40.33  ? 111 TYR C CD1   1 
ATOM   2498 C CD2   . TYR C 3 65  ? 6.394   -53.189 -9.183  1.00 40.29  ? 111 TYR C CD2   1 
ATOM   2499 C CE1   . TYR C 3 65  ? 6.106   -54.367 -11.662 1.00 39.34  ? 111 TYR C CE1   1 
ATOM   2500 C CE2   . TYR C 3 65  ? 7.322   -52.934 -10.179 1.00 42.25  ? 111 TYR C CE2   1 
ATOM   2501 C CZ    . TYR C 3 65  ? 7.173   -53.520 -11.421 1.00 43.70  ? 111 TYR C CZ    1 
ATOM   2502 O OH    . TYR C 3 65  ? 8.104   -53.276 -12.420 1.00 48.74  ? 111 TYR C OH    1 
ATOM   2503 N N     . TYR C 3 66  ? 1.016   -54.540 -7.625  1.00 41.56  ? 112 TYR C N     1 
ATOM   2504 C CA    . TYR C 3 66  ? 0.110   -55.026 -6.602  1.00 41.91  ? 112 TYR C CA    1 
ATOM   2505 C C     . TYR C 3 66  ? 0.828   -56.031 -5.711  1.00 44.88  ? 112 TYR C C     1 
ATOM   2506 O O     . TYR C 3 66  ? 1.820   -56.657 -6.107  1.00 39.60  ? 112 TYR C O     1 
ATOM   2507 C CB    . TYR C 3 66  ? -1.124  -55.661 -7.229  1.00 39.78  ? 112 TYR C CB    1 
ATOM   2508 C CG    . TYR C 3 66  ? -2.035  -54.653 -7.853  1.00 41.04  ? 112 TYR C CG    1 
ATOM   2509 C CD1   . TYR C 3 66  ? -2.952  -53.973 -7.086  1.00 39.56  ? 112 TYR C CD1   1 
ATOM   2510 C CD2   . TYR C 3 66  ? -1.982  -54.383 -9.207  1.00 37.07  ? 112 TYR C CD2   1 
ATOM   2511 C CE1   . TYR C 3 66  ? -3.799  -53.055 -7.638  1.00 43.71  ? 112 TYR C CE1   1 
ATOM   2512 C CE2   . TYR C 3 66  ? -2.813  -53.458 -9.771  1.00 38.37  ? 112 TYR C CE2   1 
ATOM   2513 C CZ    . TYR C 3 66  ? -3.736  -52.790 -8.982  1.00 45.57  ? 112 TYR C CZ    1 
ATOM   2514 O OH    . TYR C 3 66  ? -4.608  -51.847 -9.518  1.00 36.47  ? 112 TYR C OH    1 
ATOM   2515 N N     . LEU C 3 67  ? 0.328   -56.156 -4.479  1.00 46.60  ? 113 LEU C N     1 
ATOM   2516 C CA    . LEU C 3 67  ? 0.910   -57.096 -3.527  1.00 46.45  ? 113 LEU C CA    1 
ATOM   2517 C C     . LEU C 3 67  ? 0.972   -58.494 -4.132  1.00 45.33  ? 113 LEU C C     1 
ATOM   2518 O O     . LEU C 3 67  ? -0.022  -58.995 -4.674  1.00 40.07  ? 113 LEU C O     1 
ATOM   2519 C CB    . LEU C 3 67  ? 0.084   -57.104 -2.235  1.00 44.08  ? 113 LEU C CB    1 
ATOM   2520 C CG    . LEU C 3 67  ? 0.439   -58.132 -1.152  1.00 46.03  ? 113 LEU C CG    1 
ATOM   2521 C CD1   . LEU C 3 67  ? 1.821   -57.876 -0.576  1.00 36.48  ? 113 LEU C CD1   1 
ATOM   2522 C CD2   . LEU C 3 67  ? -0.640  -58.176 -0.041  1.00 44.67  ? 113 LEU C CD2   1 
ATOM   2523 N N     . GLY C 3 68  ? 2.153   -59.115 -4.044  1.00 39.69  ? 114 GLY C N     1 
ATOM   2524 C CA    . GLY C 3 68  ? 2.354   -60.454 -4.553  1.00 40.82  ? 114 GLY C CA    1 
ATOM   2525 C C     . GLY C 3 68  ? 2.554   -60.572 -6.050  1.00 42.61  ? 114 GLY C C     1 
ATOM   2526 O O     . GLY C 3 68  ? 2.447   -61.677 -6.585  1.00 43.83  ? 114 GLY C O     1 
ATOM   2527 N N     . THR C 3 69  ? 2.825   -59.476 -6.746  1.00 45.09  ? 115 THR C N     1 
ATOM   2528 C CA    . THR C 3 69  ? 3.184   -59.485 -8.159  1.00 41.68  ? 115 THR C CA    1 
ATOM   2529 C C     . THR C 3 69  ? 4.468   -58.685 -8.344  1.00 37.27  ? 115 THR C C     1 
ATOM   2530 O O     . THR C 3 69  ? 4.974   -58.069 -7.408  1.00 42.03  ? 115 THR C O     1 
ATOM   2531 C CB    . THR C 3 69  ? 2.068   -58.888 -9.020  1.00 39.50  ? 115 THR C CB    1 
ATOM   2532 O OG1   . THR C 3 69  ? 2.004   -57.470 -8.801  1.00 41.22  ? 115 THR C OG1   1 
ATOM   2533 C CG2   . THR C 3 69  ? 0.723   -59.502 -8.652  1.00 43.21  ? 115 THR C CG2   1 
ATOM   2534 N N     . GLY C 3 70  ? 4.987   -58.680 -9.567  1.00 43.44  ? 116 GLY C N     1 
ATOM   2535 C CA    . GLY C 3 70  ? 6.147   -57.882 -9.907  1.00 42.23  ? 116 GLY C CA    1 
ATOM   2536 C C     . GLY C 3 70  ? 7.435   -58.497 -9.412  1.00 38.49  ? 116 GLY C C     1 
ATOM   2537 O O     . GLY C 3 70  ? 7.436   -59.590 -8.848  1.00 44.05  ? 116 GLY C O     1 
ATOM   2538 N N     . PRO C 3 71  ? 8.555   -57.788 -9.576  1.00 43.91  ? 117 PRO C N     1 
ATOM   2539 C CA    . PRO C 3 71  ? 9.855   -58.373 -9.191  1.00 49.11  ? 117 PRO C CA    1 
ATOM   2540 C C     . PRO C 3 71  ? 9.959   -58.712 -7.709  1.00 47.31  ? 117 PRO C C     1 
ATOM   2541 O O     . PRO C 3 71  ? 10.816  -59.516 -7.333  1.00 43.53  ? 117 PRO C O     1 
ATOM   2542 C CB    . PRO C 3 71  ? 10.875  -57.287 -9.586  1.00 44.93  ? 117 PRO C CB    1 
ATOM   2543 C CG    . PRO C 3 71  ? 10.122  -56.269 -10.380 1.00 46.57  ? 117 PRO C CG    1 
ATOM   2544 C CD    . PRO C 3 71  ? 8.684   -56.365 -9.931  1.00 44.92  ? 117 PRO C CD    1 
ATOM   2545 N N     . GLU C 3 72  ? 9.113   -58.130 -6.861  1.00 49.21  ? 118 GLU C N     1 
ATOM   2546 C CA    . GLU C 3 72  ? 9.123   -58.384 -5.425  1.00 45.69  ? 118 GLU C CA    1 
ATOM   2547 C C     . GLU C 3 72  ? 7.886   -59.157 -4.986  1.00 45.56  ? 118 GLU C C     1 
ATOM   2548 O O     . GLU C 3 72  ? 7.306   -58.897 -3.925  1.00 45.42  ? 118 GLU C O     1 
ATOM   2549 C CB    . GLU C 3 72  ? 9.257   -57.074 -4.652  1.00 45.66  ? 118 GLU C CB    1 
ATOM   2550 C CG    . GLU C 3 72  ? 10.648  -56.442 -4.791  1.00 48.32  ? 118 GLU C CG    1 
ATOM   2551 C CD    . GLU C 3 72  ? 11.772  -57.408 -4.419  1.00 50.29  ? 118 GLU C CD    1 
ATOM   2552 O OE1   . GLU C 3 72  ? 11.534  -58.296 -3.569  1.00 49.59  ? 118 GLU C OE1   1 
ATOM   2553 O OE2   . GLU C 3 72  ? 12.893  -57.282 -4.973  1.00 56.70  ? 118 GLU C OE2   1 
ATOM   2554 N N     . ALA C 3 73  ? 7.477   -60.122 -5.814  1.00 44.15  ? 119 ALA C N     1 
ATOM   2555 C CA    . ALA C 3 73  ? 6.256   -60.877 -5.552  1.00 45.57  ? 119 ALA C CA    1 
ATOM   2556 C C     . ALA C 3 73  ? 6.367   -61.774 -4.324  1.00 48.42  ? 119 ALA C C     1 
ATOM   2557 O O     . ALA C 3 73  ? 5.333   -62.190 -3.787  1.00 49.00  ? 119 ALA C O     1 
ATOM   2558 C CB    . ALA C 3 73  ? 5.886   -61.713 -6.776  1.00 39.65  ? 119 ALA C CB    1 
ATOM   2559 N N     . GLY C 3 74  ? 7.584   -62.084 -3.867  1.00 44.95  ? 120 GLY C N     1 
ATOM   2560 C CA    . GLY C 3 74  ? 7.727   -62.872 -2.656  1.00 45.83  ? 120 GLY C CA    1 
ATOM   2561 C C     . GLY C 3 74  ? 7.432   -62.103 -1.382  1.00 52.35  ? 120 GLY C C     1 
ATOM   2562 O O     . GLY C 3 74  ? 7.101   -62.719 -0.361  1.00 52.06  ? 120 GLY C O     1 
ATOM   2563 N N     . LEU C 3 75  ? 7.508   -60.771 -1.431  1.00 45.37  ? 121 LEU C N     1 
ATOM   2564 C CA    . LEU C 3 75  ? 7.532   -59.948 -0.226  1.00 43.38  ? 121 LEU C CA    1 
ATOM   2565 C C     . LEU C 3 75  ? 6.133   -59.791 0.366   1.00 49.50  ? 121 LEU C C     1 
ATOM   2566 O O     . LEU C 3 75  ? 5.176   -59.494 -0.364  1.00 47.35  ? 121 LEU C O     1 
ATOM   2567 C CB    . LEU C 3 75  ? 8.127   -58.582 -0.537  1.00 43.96  ? 121 LEU C CB    1 
ATOM   2568 C CG    . LEU C 3 75  ? 9.620   -58.617 -0.923  1.00 46.21  ? 121 LEU C CG    1 
ATOM   2569 C CD1   . LEU C 3 75  ? 10.298  -57.259 -0.731  1.00 42.62  ? 121 LEU C CD1   1 
ATOM   2570 C CD2   . LEU C 3 75  ? 10.324  -59.680 -0.132  1.00 46.60  ? 121 LEU C CD2   1 
ATOM   2571 N N     . PRO C 3 76  ? 5.975   -59.977 1.671   1.00 48.50  ? 122 PRO C N     1 
ATOM   2572 C CA    . PRO C 3 76  ? 4.690   -59.687 2.310   1.00 46.31  ? 122 PRO C CA    1 
ATOM   2573 C C     . PRO C 3 76  ? 4.547   -58.191 2.528   1.00 46.11  ? 122 PRO C C     1 
ATOM   2574 O O     . PRO C 3 76  ? 5.514   -57.431 2.474   1.00 43.07  ? 122 PRO C O     1 
ATOM   2575 C CB    . PRO C 3 76  ? 4.777   -60.437 3.641   1.00 48.05  ? 122 PRO C CB    1 
ATOM   2576 C CG    . PRO C 3 76  ? 6.264   -60.410 3.962   1.00 46.90  ? 122 PRO C CG    1 
ATOM   2577 C CD    . PRO C 3 76  ? 7.003   -60.409 2.637   1.00 44.90  ? 122 PRO C CD    1 
ATOM   2578 N N     . TYR C 3 77  ? 3.317   -57.774 2.776   1.00 43.28  ? 123 TYR C N     1 
ATOM   2579 C CA    . TYR C 3 77  ? 3.059   -56.351 2.904   1.00 45.48  ? 123 TYR C CA    1 
ATOM   2580 C C     . TYR C 3 77  ? 3.835   -55.802 4.086   1.00 41.97  ? 123 TYR C C     1 
ATOM   2581 O O     . TYR C 3 77  ? 3.970   -56.465 5.113   1.00 45.81  ? 123 TYR C O     1 
ATOM   2582 C CB    . TYR C 3 77  ? 1.557   -56.076 3.072   1.00 44.54  ? 123 TYR C CB    1 
ATOM   2583 C CG    . TYR C 3 77  ? 1.303   -54.604 3.163   1.00 48.37  ? 123 TYR C CG    1 
ATOM   2584 C CD1   . TYR C 3 77  ? 1.255   -53.826 2.014   1.00 51.24  ? 123 TYR C CD1   1 
ATOM   2585 C CD2   . TYR C 3 77  ? 1.190   -53.971 4.397   1.00 51.25  ? 123 TYR C CD2   1 
ATOM   2586 C CE1   . TYR C 3 77  ? 1.056   -52.459 2.087   1.00 54.30  ? 123 TYR C CE1   1 
ATOM   2587 C CE2   . TYR C 3 77  ? 0.997   -52.604 4.483   1.00 55.46  ? 123 TYR C CE2   1 
ATOM   2588 C CZ    . TYR C 3 77  ? 0.928   -51.851 3.324   1.00 56.16  ? 123 TYR C CZ    1 
ATOM   2589 O OH    . TYR C 3 77  ? 0.723   -50.492 3.395   1.00 55.31  ? 123 TYR C OH    1 
ATOM   2590 N N     . GLY C 3 78  ? 4.352   -54.585 3.938   1.00 47.62  ? 124 GLY C N     1 
ATOM   2591 C CA    . GLY C 3 78  ? 5.232   -54.002 4.934   1.00 45.43  ? 124 GLY C CA    1 
ATOM   2592 C C     . GLY C 3 78  ? 6.661   -54.517 4.913   1.00 45.13  ? 124 GLY C C     1 
ATOM   2593 O O     . GLY C 3 78  ? 7.453   -54.135 5.785   1.00 40.94  ? 124 GLY C O     1 
ATOM   2594 N N     . ALA C 3 79  ? 7.018   -55.360 3.950   1.00 40.22  ? 125 ALA C N     1 
ATOM   2595 C CA    . ALA C 3 79  ? 8.357   -55.919 3.924   1.00 43.22  ? 125 ALA C CA    1 
ATOM   2596 C C     . ALA C 3 79  ? 9.387   -54.801 3.884   1.00 45.46  ? 125 ALA C C     1 
ATOM   2597 O O     . ALA C 3 79  ? 9.250   -53.837 3.123   1.00 51.45  ? 125 ALA C O     1 
ATOM   2598 C CB    . ALA C 3 79  ? 8.518   -56.851 2.724   1.00 44.45  ? 125 ALA C CB    1 
ATOM   2599 N N     . ASN C 3 80  ? 10.410  -54.912 4.721   1.00 47.25  ? 126 ASN C N     1 
ATOM   2600 C CA    . ASN C 3 80  ? 11.444  -53.877 4.791   1.00 54.09  ? 126 ASN C CA    1 
ATOM   2601 C C     . ASN C 3 80  ? 12.525  -54.190 3.765   1.00 45.03  ? 126 ASN C C     1 
ATOM   2602 O O     . ASN C 3 80  ? 13.358  -55.080 3.968   1.00 53.40  ? 126 ASN C O     1 
ATOM   2603 C CB    . ASN C 3 80  ? 12.028  -53.772 6.196   1.00 55.12  ? 126 ASN C CB    1 
ATOM   2604 C CG    . ASN C 3 80  ? 12.919  -52.555 6.357   1.00 61.41  ? 126 ASN C CG    1 
ATOM   2605 O OD1   . ASN C 3 80  ? 14.060  -52.530 5.873   1.00 61.50  ? 126 ASN C OD1   1 
ATOM   2606 N ND2   . ASN C 3 80  ? 12.401  -51.530 7.029   1.00 65.77  ? 126 ASN C ND2   1 
ATOM   2607 N N     . LYS C 3 81  ? 12.522  -53.450 2.660   1.00 40.07  ? 127 LYS C N     1 
ATOM   2608 C CA    . LYS C 3 81  ? 13.593  -53.560 1.681   1.00 50.66  ? 127 LYS C CA    1 
ATOM   2609 C C     . LYS C 3 81  ? 13.927  -52.179 1.150   1.00 50.50  ? 127 LYS C C     1 
ATOM   2610 O O     . LYS C 3 81  ? 13.061  -51.305 1.070   1.00 53.21  ? 127 LYS C O     1 
ATOM   2611 C CB    . LYS C 3 81  ? 13.231  -54.492 0.508   1.00 49.24  ? 127 LYS C CB    1 
ATOM   2612 C CG    . LYS C 3 81  ? 14.383  -54.682 -0.494  1.00 51.84  ? 127 LYS C CG    1 
ATOM   2613 C CD    . LYS C 3 81  ? 14.227  -55.939 -1.339  1.00 54.71  ? 127 LYS C CD    1 
ATOM   2614 C CE    . LYS C 3 81  ? 15.418  -56.138 -2.262  1.00 51.13  ? 127 LYS C CE    1 
ATOM   2615 N NZ    . LYS C 3 81  ? 15.444  -57.529 -2.796  1.00 61.92  ? 127 LYS C NZ    1 
ATOM   2616 N N     . ASP C 3 82  ? 15.197  -51.994 0.787   1.00 52.48  ? 128 ASP C N     1 
ATOM   2617 C CA    . ASP C 3 82  ? 15.615  -50.768 0.122   1.00 54.77  ? 128 ASP C CA    1 
ATOM   2618 C C     . ASP C 3 82  ? 14.871  -50.620 -1.200  1.00 53.92  ? 128 ASP C C     1 
ATOM   2619 O O     . ASP C 3 82  ? 14.616  -51.600 -1.908  1.00 57.37  ? 128 ASP C O     1 
ATOM   2620 C CB    . ASP C 3 82  ? 17.136  -50.779 -0.111  1.00 51.49  ? 128 ASP C CB    1 
ATOM   2621 C CG    . ASP C 3 82  ? 17.680  -49.425 -0.582  1.00 62.97  ? 128 ASP C CG    1 
ATOM   2622 O OD1   . ASP C 3 82  ? 16.971  -48.394 -0.444  1.00 53.89  ? 128 ASP C OD1   1 
ATOM   2623 O OD2   . ASP C 3 82  ? 18.832  -49.397 -1.091  1.00 66.24  ? 128 ASP C OD2   1 
ATOM   2624 N N     . GLY C 3 83  ? 14.498  -49.390 -1.525  1.00 54.31  ? 129 GLY C N     1 
ATOM   2625 C CA    . GLY C 3 83  ? 13.850  -49.172 -2.799  1.00 50.96  ? 129 GLY C CA    1 
ATOM   2626 C C     . GLY C 3 83  ? 12.435  -49.672 -2.884  1.00 45.92  ? 129 GLY C C     1 
ATOM   2627 O O     . GLY C 3 83  ? 11.882  -49.699 -3.985  1.00 47.00  ? 129 GLY C O     1 
ATOM   2628 N N     . ILE C 3 84  ? 11.835  -50.067 -1.756  1.00 43.30  ? 130 ILE C N     1 
ATOM   2629 C CA    . ILE C 3 84  ? 10.461  -50.555 -1.698  1.00 43.51  ? 130 ILE C CA    1 
ATOM   2630 C C     . ILE C 3 84  ? 9.720   -49.777 -0.618  1.00 46.27  ? 130 ILE C C     1 
ATOM   2631 O O     . ILE C 3 84  ? 10.221  -49.628 0.500   1.00 54.54  ? 130 ILE C O     1 
ATOM   2632 C CB    . ILE C 3 84  ? 10.403  -52.070 -1.408  1.00 43.63  ? 130 ILE C CB    1 
ATOM   2633 C CG1   . ILE C 3 84  ? 11.119  -52.870 -2.490  1.00 41.88  ? 130 ILE C CG1   1 
ATOM   2634 C CG2   . ILE C 3 84  ? 8.966   -52.547 -1.262  1.00 46.28  ? 130 ILE C CG2   1 
ATOM   2635 C CD1   . ILE C 3 84  ? 10.374  -52.947 -3.802  1.00 40.92  ? 130 ILE C CD1   1 
ATOM   2636 N N     . ILE C 3 85  ? 8.536   -49.275 -0.946  1.00 44.72  ? 131 ILE C N     1 
ATOM   2637 C CA    . ILE C 3 85  ? 7.621   -48.699 0.026   1.00 43.78  ? 131 ILE C CA    1 
ATOM   2638 C C     . ILE C 3 85  ? 6.277   -49.388 -0.178  1.00 50.72  ? 131 ILE C C     1 
ATOM   2639 O O     . ILE C 3 85  ? 6.113   -50.168 -1.113  1.00 51.51  ? 131 ILE C O     1 
ATOM   2640 C CB    . ILE C 3 85  ? 7.511   -47.167 -0.124  1.00 50.64  ? 131 ILE C CB    1 
ATOM   2641 C CG1   . ILE C 3 85  ? 6.838   -46.804 -1.450  1.00 48.27  ? 131 ILE C CG1   1 
ATOM   2642 C CG2   . ILE C 3 85  ? 8.901   -46.542 -0.093  1.00 46.98  ? 131 ILE C CG2   1 
ATOM   2643 C CD1   . ILE C 3 85  ? 5.640   -45.921 -1.280  1.00 49.99  ? 131 ILE C CD1   1 
ATOM   2644 N N     . TRP C 3 86  ? 5.304   -49.101 0.700   1.00 42.14  ? 132 TRP C N     1 
ATOM   2645 C CA    . TRP C 3 86  ? 4.069   -49.876 0.699   1.00 42.43  ? 132 TRP C CA    1 
ATOM   2646 C C     . TRP C 3 86  ? 2.861   -48.965 0.842   1.00 44.96  ? 132 TRP C C     1 
ATOM   2647 O O     . TRP C 3 86  ? 2.923   -47.935 1.516   1.00 52.11  ? 132 TRP C O     1 
ATOM   2648 C CB    . TRP C 3 86  ? 4.066   -50.928 1.828   1.00 48.09  ? 132 TRP C CB    1 
ATOM   2649 C CG    . TRP C 3 86  ? 5.105   -51.981 1.626   1.00 43.37  ? 132 TRP C CG    1 
ATOM   2650 C CD1   . TRP C 3 86  ? 6.349   -51.998 2.147   1.00 42.11  ? 132 TRP C CD1   1 
ATOM   2651 C CD2   . TRP C 3 86  ? 4.989   -53.160 0.813   1.00 47.33  ? 132 TRP C CD2   1 
ATOM   2652 N NE1   . TRP C 3 86  ? 7.031   -53.120 1.724   1.00 46.29  ? 132 TRP C NE1   1 
ATOM   2653 C CE2   . TRP C 3 86  ? 6.216   -53.847 0.897   1.00 41.53  ? 132 TRP C CE2   1 
ATOM   2654 C CE3   . TRP C 3 86  ? 3.960   -53.706 0.032   1.00 42.95  ? 132 TRP C CE3   1 
ATOM   2655 C CZ2   . TRP C 3 86  ? 6.454   -55.044 0.226   1.00 39.24  ? 132 TRP C CZ2   1 
ATOM   2656 C CZ3   . TRP C 3 86  ? 4.195   -54.902 -0.629  1.00 42.74  ? 132 TRP C CZ3   1 
ATOM   2657 C CH2   . TRP C 3 86  ? 5.437   -55.557 -0.527  1.00 39.20  ? 132 TRP C CH2   1 
ATOM   2658 N N     . VAL C 3 87  ? 1.744   -49.356 0.222   1.00 39.78  ? 133 VAL C N     1 
ATOM   2659 C CA    . VAL C 3 87  ? 0.499   -48.607 0.365   1.00 44.49  ? 133 VAL C CA    1 
ATOM   2660 C C     . VAL C 3 87  ? -0.672  -49.576 0.401   1.00 46.99  ? 133 VAL C C     1 
ATOM   2661 O O     . VAL C 3 87  ? -0.607  -50.687 -0.135  1.00 41.44  ? 133 VAL C O     1 
ATOM   2662 C CB    . VAL C 3 87  ? 0.277   -47.568 -0.764  1.00 44.49  ? 133 VAL C CB    1 
ATOM   2663 C CG1   . VAL C 3 87  ? 1.236   -46.405 -0.622  1.00 43.17  ? 133 VAL C CG1   1 
ATOM   2664 C CG2   . VAL C 3 87  ? 0.408   -48.232 -2.151  1.00 41.30  ? 133 VAL C CG2   1 
ATOM   2665 N N     . ALA C 3 88  ? -1.766  -49.128 1.022   1.00 42.73  ? 134 ALA C N     1 
ATOM   2666 C CA    . ALA C 3 88  ? -2.969  -49.942 1.047   1.00 44.17  ? 134 ALA C CA    1 
ATOM   2667 C C     . ALA C 3 88  ? -4.181  -49.064 1.299   1.00 44.69  ? 134 ALA C C     1 
ATOM   2668 O O     . ALA C 3 88  ? -4.141  -48.174 2.139   1.00 48.42  ? 134 ALA C O     1 
ATOM   2669 C CB    . ALA C 3 88  ? -2.870  -51.025 2.120   1.00 51.72  ? 134 ALA C CB    1 
ATOM   2670 N N     . THR C 3 89  ? -5.253  -49.331 0.579   1.00 45.13  ? 135 THR C N     1 
ATOM   2671 C CA    . THR C 3 89  ? -6.508  -48.650 0.813   1.00 42.79  ? 135 THR C CA    1 
ATOM   2672 C C     . THR C 3 89  ? -7.272  -49.352 1.935   1.00 52.03  ? 135 THR C C     1 
ATOM   2673 O O     . THR C 3 89  ? -7.178  -50.571 2.112   1.00 51.33  ? 135 THR C O     1 
ATOM   2674 C CB    . THR C 3 89  ? -7.316  -48.631 -0.479  1.00 48.57  ? 135 THR C CB    1 
ATOM   2675 O OG1   . THR C 3 89  ? -6.424  -48.378 -1.573  1.00 49.53  ? 135 THR C OG1   1 
ATOM   2676 C CG2   . THR C 3 89  ? -8.404  -47.556 -0.456  1.00 45.92  ? 135 THR C CG2   1 
ATOM   2677 N N     . GLU C 3 90  ? -8.007  -48.563 2.721   1.00 54.45  ? 136 GLU C N     1 
ATOM   2678 C CA    . GLU C 3 90  ? -8.865  -49.141 3.749   1.00 53.19  ? 136 GLU C CA    1 
ATOM   2679 C C     . GLU C 3 90  ? -9.922  -50.017 3.085   1.00 53.77  ? 136 GLU C C     1 
ATOM   2680 O O     . GLU C 3 90  ? -10.657 -49.562 2.199   1.00 50.74  ? 136 GLU C O     1 
ATOM   2681 C CB    . GLU C 3 90  ? -9.509  -48.034 4.592   1.00 59.69  ? 136 GLU C CB    1 
ATOM   2682 C CG    . GLU C 3 90  ? -10.264 -48.500 5.875   1.00 58.37  ? 136 GLU C CG    1 
ATOM   2683 C CD    . GLU C 3 90  ? -9.353  -49.040 6.995   1.00 60.46  ? 136 GLU C CD    1 
ATOM   2684 O OE1   . GLU C 3 90  ? -8.173  -48.625 7.091   1.00 63.65  ? 136 GLU C OE1   1 
ATOM   2685 O OE2   . GLU C 3 90  ? -9.832  -49.883 7.791   1.00 54.99  ? 136 GLU C OE2   1 
ATOM   2686 N N     . GLY C 3 91  ? -9.969  -51.287 3.497   1.00 58.02  ? 137 GLY C N     1 
ATOM   2687 C CA    . GLY C 3 91  ? -10.818 -52.301 2.894   1.00 56.88  ? 137 GLY C CA    1 
ATOM   2688 C C     . GLY C 3 91  ? -10.050 -53.403 2.197   1.00 53.45  ? 137 GLY C C     1 
ATOM   2689 O O     . GLY C 3 91  ? -10.660 -54.394 1.769   1.00 50.59  ? 137 GLY C O     1 
ATOM   2690 N N     . ALA C 3 92  ? -8.730  -53.262 2.082   1.00 54.19  ? 138 ALA C N     1 
ATOM   2691 C CA    . ALA C 3 92  ? -7.913  -54.214 1.343   1.00 53.42  ? 138 ALA C CA    1 
ATOM   2692 C C     . ALA C 3 92  ? -7.844  -55.561 2.053   1.00 54.84  ? 138 ALA C C     1 
ATOM   2693 O O     . ALA C 3 92  ? -7.922  -55.655 3.283   1.00 57.15  ? 138 ALA C O     1 
ATOM   2694 C CB    . ALA C 3 92  ? -6.496  -53.672 1.143   1.00 51.63  ? 138 ALA C CB    1 
ATOM   2695 N N     . LEU C 3 93  ? -7.736  -56.611 1.247   1.00 52.76  ? 139 LEU C N     1 
ATOM   2696 C CA    . LEU C 3 93  ? -7.362  -57.936 1.711   1.00 55.00  ? 139 LEU C CA    1 
ATOM   2697 C C     . LEU C 3 93  ? -5.860  -58.064 1.556   1.00 45.68  ? 139 LEU C C     1 
ATOM   2698 O O     . LEU C 3 93  ? -5.294  -57.581 0.577   1.00 53.27  ? 139 LEU C O     1 
ATOM   2699 C CB    . LEU C 3 93  ? -8.059  -59.014 0.884   1.00 56.98  ? 139 LEU C CB    1 
ATOM   2700 C CG    . LEU C 3 93  ? -8.600  -60.275 1.547   1.00 61.27  ? 139 LEU C CG    1 
ATOM   2701 C CD1   . LEU C 3 93  ? -8.602  -61.432 0.548   1.00 59.20  ? 139 LEU C CD1   1 
ATOM   2702 C CD2   . LEU C 3 93  ? -7.830  -60.629 2.814   1.00 60.23  ? 139 LEU C CD2   1 
ATOM   2703 N N     . ASN C 3 94  ? -5.220  -58.734 2.508   1.00 47.60  ? 140 ASN C N     1 
ATOM   2704 C CA    . ASN C 3 94  ? -3.765  -58.821 2.579   1.00 47.93  ? 140 ASN C CA    1 
ATOM   2705 C C     . ASN C 3 94  ? -3.215  -60.106 1.960   1.00 53.60  ? 140 ASN C C     1 
ATOM   2706 O O     . ASN C 3 94  ? -2.210  -60.652 2.442   1.00 57.71  ? 140 ASN C O     1 
ATOM   2707 C CB    . ASN C 3 94  ? -3.327  -58.708 4.037   1.00 52.84  ? 140 ASN C CB    1 
ATOM   2708 C CG    . ASN C 3 94  ? -1.867  -58.337 4.195   1.00 43.60  ? 140 ASN C CG    1 
ATOM   2709 O OD1   . ASN C 3 94  ? -1.525  -57.553 5.072   1.00 52.22  ? 140 ASN C OD1   1 
ATOM   2710 N ND2   . ASN C 3 94  ? -1.008  -58.895 3.364   1.00 44.55  ? 140 ASN C ND2   1 
ATOM   2711 N N     . THR C 3 95  ? -3.842  -60.597 0.919   1.00 55.32  ? 141 THR C N     1 
ATOM   2712 C CA    . THR C 3 95  ? -3.428  -61.791 0.203   1.00 53.40  ? 141 THR C CA    1 
ATOM   2713 C C     . THR C 3 95  ? -2.757  -61.413 -1.110  1.00 57.14  ? 141 THR C C     1 
ATOM   2714 O O     . THR C 3 95  ? -2.972  -60.312 -1.629  1.00 52.72  ? 141 THR C O     1 
ATOM   2715 C CB    . THR C 3 95  ? -4.644  -62.673 -0.075  1.00 56.59  ? 141 THR C CB    1 
ATOM   2716 O OG1   . THR C 3 95  ? -5.571  -61.944 -0.885  1.00 55.97  ? 141 THR C OG1   1 
ATOM   2717 C CG2   . THR C 3 95  ? -5.329  -63.045 1.230   1.00 61.81  ? 141 THR C CG2   1 
ATOM   2718 N N     . PRO C 3 96  ? -1.925  -62.290 -1.677  1.00 55.27  ? 142 PRO C N     1 
ATOM   2719 C CA    . PRO C 3 96  ? -1.306  -61.966 -2.968  1.00 51.22  ? 142 PRO C CA    1 
ATOM   2720 C C     . PRO C 3 96  ? -2.353  -61.714 -4.051  1.00 55.21  ? 142 PRO C C     1 
ATOM   2721 O O     . PRO C 3 96  ? -3.423  -62.327 -4.078  1.00 52.58  ? 142 PRO C O     1 
ATOM   2722 C CB    . PRO C 3 96  ? -0.454  -63.203 -3.274  1.00 50.24  ? 142 PRO C CB    1 
ATOM   2723 C CG    . PRO C 3 96  ? -0.119  -63.757 -1.943  1.00 48.95  ? 142 PRO C CG    1 
ATOM   2724 C CD    . PRO C 3 96  ? -1.378  -63.539 -1.120  1.00 57.25  ? 142 PRO C CD    1 
ATOM   2725 N N     . LYS C 3 97  ? -2.036  -60.768 -4.935  1.00 52.68  ? 143 LYS C N     1 
ATOM   2726 C CA    . LYS C 3 97  ? -2.878  -60.407 -6.063  1.00 46.02  ? 143 LYS C CA    1 
ATOM   2727 C C     . LYS C 3 97  ? -2.361  -61.003 -7.371  1.00 48.50  ? 143 LYS C C     1 
ATOM   2728 O O     . LYS C 3 97  ? -2.489  -60.386 -8.437  1.00 41.37  ? 143 LYS C O     1 
ATOM   2729 C CB    . LYS C 3 97  ? -2.982  -58.884 -6.149  1.00 48.16  ? 143 LYS C CB    1 
ATOM   2730 C CG    . LYS C 3 97  ? -3.449  -58.251 -4.844  1.00 50.64  ? 143 LYS C CG    1 
ATOM   2731 C CD    . LYS C 3 97  ? -4.923  -58.544 -4.619  1.00 52.50  ? 143 LYS C CD    1 
ATOM   2732 C CE    . LYS C 3 97  ? -5.236  -58.934 -3.177  1.00 56.41  ? 143 LYS C CE    1 
ATOM   2733 N NZ    . LYS C 3 97  ? -4.975  -57.842 -2.216  1.00 56.12  ? 143 LYS C NZ    1 
ATOM   2734 N N     . ASP C 3 98  ? -1.770  -62.203 -7.304  1.00 49.19  ? 144 ASP C N     1 
ATOM   2735 C CA    . ASP C 3 98  ? -1.278  -62.869 -8.505  1.00 52.44  ? 144 ASP C CA    1 
ATOM   2736 C C     . ASP C 3 98  ? -2.349  -62.997 -9.575  1.00 43.62  ? 144 ASP C C     1 
ATOM   2737 O O     . ASP C 3 98  ? -2.024  -63.246 -10.736 1.00 48.26  ? 144 ASP C O     1 
ATOM   2738 C CB    . ASP C 3 98  ? -0.739  -64.256 -8.172  1.00 48.93  ? 144 ASP C CB    1 
ATOM   2739 C CG    . ASP C 3 98  ? -1.731  -65.085 -7.388  1.00 56.17  ? 144 ASP C CG    1 
ATOM   2740 O OD1   . ASP C 3 98  ? -1.788  -64.932 -6.146  1.00 59.19  ? 144 ASP C OD1   1 
ATOM   2741 O OD2   . ASP C 3 98  ? -2.470  -65.870 -8.013  1.00 55.94  ? 144 ASP C OD2   1 
ATOM   2742 N N     . HIS C 3 99  ? -3.614  -62.827 -9.218  1.00 42.71  ? 145 HIS C N     1 
ATOM   2743 C CA    . HIS C 3 99  ? -4.664  -62.835 -10.222 1.00 41.72  ? 145 HIS C CA    1 
ATOM   2744 C C     . HIS C 3 99  ? -4.730  -61.540 -11.029 1.00 43.91  ? 145 HIS C C     1 
ATOM   2745 O O     . HIS C 3 99  ? -5.329  -61.523 -12.106 1.00 41.62  ? 145 HIS C O     1 
ATOM   2746 C CB    . HIS C 3 99  ? -6.006  -63.110 -9.554  1.00 44.04  ? 145 HIS C CB    1 
ATOM   2747 C CG    . HIS C 3 99  ? -6.417  -62.070 -8.564  1.00 45.52  ? 145 HIS C CG    1 
ATOM   2748 N ND1   . HIS C 3 99  ? -5.949  -62.054 -7.267  1.00 47.01  ? 145 HIS C ND1   1 
ATOM   2749 C CD2   . HIS C 3 99  ? -7.272  -61.027 -8.672  1.00 47.14  ? 145 HIS C CD2   1 
ATOM   2750 C CE1   . HIS C 3 99  ? -6.485  -61.033 -6.625  1.00 50.29  ? 145 HIS C CE1   1 
ATOM   2751 N NE2   . HIS C 3 99  ? -7.298  -60.398 -7.452  1.00 49.52  ? 145 HIS C NE2   1 
ATOM   2752 N N     . ILE C 3 100 ? -4.167  -60.449 -10.529 1.00 48.51  ? 146 ILE C N     1 
ATOM   2753 C CA    . ILE C 3 100 ? -4.014  -59.246 -11.338 1.00 41.75  ? 146 ILE C CA    1 
ATOM   2754 C C     . ILE C 3 100 ? -2.717  -59.307 -12.131 1.00 45.49  ? 146 ILE C C     1 
ATOM   2755 O O     . ILE C 3 100 ? -2.660  -58.854 -13.276 1.00 40.04  ? 146 ILE C O     1 
ATOM   2756 C CB    . ILE C 3 100 ? -4.056  -57.984 -10.451 1.00 46.98  ? 146 ILE C CB    1 
ATOM   2757 C CG1   . ILE C 3 100 ? -5.336  -57.925 -9.620  1.00 50.36  ? 146 ILE C CG1   1 
ATOM   2758 C CG2   . ILE C 3 100 ? -3.899  -56.729 -11.303 1.00 43.89  ? 146 ILE C CG2   1 
ATOM   2759 C CD1   . ILE C 3 100 ? -5.577  -56.564 -8.981  1.00 49.92  ? 146 ILE C CD1   1 
ATOM   2760 N N     . GLY C 3 101 ? -1.665  -59.848 -11.512 1.00 40.12  ? 147 GLY C N     1 
ATOM   2761 C CA    . GLY C 3 101 ? -0.390  -60.073 -12.109 1.00 37.42  ? 147 GLY C CA    1 
ATOM   2762 C C     . GLY C 3 101 ? 0.275   -58.778 -12.537 1.00 38.45  ? 147 GLY C C     1 
ATOM   2763 O O     . GLY C 3 101 ? -0.023  -57.683 -12.060 1.00 36.78  ? 147 GLY C O     1 
ATOM   2764 N N     . THR C 3 102 ? 1.187   -58.923 -13.481 1.00 41.44  ? 148 THR C N     1 
ATOM   2765 C CA    . THR C 3 102 ? 1.832   -57.792 -14.124 1.00 37.52  ? 148 THR C CA    1 
ATOM   2766 C C     . THR C 3 102 ? 1.496   -57.783 -15.611 1.00 36.87  ? 148 THR C C     1 
ATOM   2767 O O     . THR C 3 102 ? 0.909   -58.722 -16.144 1.00 38.86  ? 148 THR C O     1 
ATOM   2768 C CB    . THR C 3 102 ? 3.330   -57.863 -13.914 1.00 38.46  ? 148 THR C CB    1 
ATOM   2769 O OG1   . THR C 3 102 ? 3.722   -59.235 -14.035 1.00 37.87  ? 148 THR C OG1   1 
ATOM   2770 C CG2   . THR C 3 102 ? 3.673   -57.331 -12.532 1.00 41.99  ? 148 THR C CG2   1 
ATOM   2771 N N     . ARG C 3 103 ? 1.910   -56.716 -16.283 1.00 36.33  ? 149 ARG C N     1 
ATOM   2772 C CA    . ARG C 3 103 ? 1.493   -56.415 -17.643 1.00 33.77  ? 149 ARG C CA    1 
ATOM   2773 C C     . ARG C 3 103 ? 2.508   -56.895 -18.675 1.00 35.18  ? 149 ARG C C     1 
ATOM   2774 O O     . ARG C 3 103 ? 3.716   -56.710 -18.516 1.00 36.89  ? 149 ARG C O     1 
ATOM   2775 C CB    . ARG C 3 103 ? 1.299   -54.915 -17.806 1.00 34.81  ? 149 ARG C CB    1 
ATOM   2776 C CG    . ARG C 3 103 ? 1.060   -54.457 -19.232 1.00 31.55  ? 149 ARG C CG    1 
ATOM   2777 C CD    . ARG C 3 103 ? 0.826   -52.980 -19.173 1.00 31.43  ? 149 ARG C CD    1 
ATOM   2778 N NE    . ARG C 3 103 ? 2.029   -52.276 -18.749 1.00 32.16  ? 149 ARG C NE    1 
ATOM   2779 C CZ    . ARG C 3 103 ? 2.807   -51.591 -19.577 1.00 33.16  ? 149 ARG C CZ    1 
ATOM   2780 N NH1   . ARG C 3 103 ? 2.509   -51.483 -20.858 1.00 30.57  ? 149 ARG C NH1   1 
ATOM   2781 N NH2   . ARG C 3 103 ? 3.915   -51.012 -19.110 1.00 27.22  ? 149 ARG C NH2   1 
ATOM   2782 N N     . ASN C 3 104 ? 2.005   -57.500 -19.739 1.00 36.91  ? 150 ASN C N     1 
ATOM   2783 C CA    . ASN C 3 104 ? 2.799   -57.736 -20.930 1.00 28.92  ? 150 ASN C CA    1 
ATOM   2784 C C     . ASN C 3 104 ? 2.579   -56.566 -21.888 1.00 29.44  ? 150 ASN C C     1 
ATOM   2785 O O     . ASN C 3 104 ? 1.473   -56.432 -22.443 1.00 28.79  ? 150 ASN C O     1 
ATOM   2786 C CB    . ASN C 3 104 ? 2.400   -59.045 -21.569 1.00 31.14  ? 150 ASN C CB    1 
ATOM   2787 C CG    . ASN C 3 104 ? 3.182   -59.350 -22.819 1.00 33.19  ? 150 ASN C CG    1 
ATOM   2788 O OD1   . ASN C 3 104 ? 3.786   -58.476 -23.428 1.00 34.67  ? 150 ASN C OD1   1 
ATOM   2789 N ND2   . ASN C 3 104 ? 3.153   -60.608 -23.221 1.00 37.86  ? 150 ASN C ND2   1 
ATOM   2790 N N     . PRO C 3 105 ? 3.580   -55.710 -22.114 1.00 31.04  ? 151 PRO C N     1 
ATOM   2791 C CA    . PRO C 3 105 ? 3.365   -54.536 -22.974 1.00 29.66  ? 151 PRO C CA    1 
ATOM   2792 C C     . PRO C 3 105 ? 3.096   -54.874 -24.438 1.00 31.56  ? 151 PRO C C     1 
ATOM   2793 O O     . PRO C 3 105 ? 2.681   -53.987 -25.189 1.00 32.59  ? 151 PRO C O     1 
ATOM   2794 C CB    . PRO C 3 105 ? 4.659   -53.729 -22.803 1.00 31.09  ? 151 PRO C CB    1 
ATOM   2795 C CG    . PRO C 3 105 ? 5.667   -54.696 -22.248 1.00 31.09  ? 151 PRO C CG    1 
ATOM   2796 C CD    . PRO C 3 105 ? 4.896   -55.676 -21.443 1.00 34.08  ? 151 PRO C CD    1 
ATOM   2797 N N     . ALA C 3 106 ? 3.293   -56.115 -24.874 1.00 30.76  ? 152 ALA C N     1 
ATOM   2798 C CA    . ALA C 3 106 ? 2.951   -56.434 -26.250 1.00 30.60  ? 152 ALA C CA    1 
ATOM   2799 C C     . ALA C 3 106 ? 1.470   -56.219 -26.510 1.00 33.53  ? 152 ALA C C     1 
ATOM   2800 O O     . ALA C 3 106 ? 1.089   -55.861 -27.630 1.00 34.47  ? 152 ALA C O     1 
ATOM   2801 C CB    . ALA C 3 106 ? 3.348   -57.868 -26.580 1.00 33.37  ? 152 ALA C CB    1 
ATOM   2802 N N     . ASN C 3 107 ? 0.623   -56.391 -25.484 1.00 33.75  ? 153 ASN C N     1 
ATOM   2803 C CA    . ASN C 3 107 ? -0.813  -56.338 -25.711 1.00 33.98  ? 153 ASN C CA    1 
ATOM   2804 C C     . ASN C 3 107 ? -1.586  -55.592 -24.623 1.00 33.62  ? 153 ASN C C     1 
ATOM   2805 O O     . ASN C 3 107 ? -2.775  -55.846 -24.433 1.00 36.32  ? 153 ASN C O     1 
ATOM   2806 C CB    . ASN C 3 107 ? -1.379  -57.735 -25.853 1.00 39.29  ? 153 ASN C CB    1 
ATOM   2807 C CG    . ASN C 3 107 ? -0.953  -58.644 -24.751 1.00 42.85  ? 153 ASN C CG    1 
ATOM   2808 O OD1   . ASN C 3 107 ? -1.362  -58.484 -23.596 1.00 43.45  ? 153 ASN C OD1   1 
ATOM   2809 N ND2   . ASN C 3 107 ? -0.150  -59.639 -25.100 1.00 41.20  ? 153 ASN C ND2   1 
ATOM   2810 N N     . ASN C 3 108 ? -0.949  -54.672 -23.909 1.00 32.09  ? 154 ASN C N     1 
ATOM   2811 C CA    . ASN C 3 108 ? -1.652  -53.782 -22.994 1.00 29.31  ? 154 ASN C CA    1 
ATOM   2812 C C     . ASN C 3 108 ? -0.818  -52.528 -22.849 1.00 32.56  ? 154 ASN C C     1 
ATOM   2813 O O     . ASN C 3 108 ? 0.388   -52.625 -22.591 1.00 32.78  ? 154 ASN C O     1 
ATOM   2814 C CB    . ASN C 3 108 ? -1.850  -54.391 -21.605 1.00 31.88  ? 154 ASN C CB    1 
ATOM   2815 C CG    . ASN C 3 108 ? -3.124  -55.154 -21.483 1.00 38.22  ? 154 ASN C CG    1 
ATOM   2816 O OD1   . ASN C 3 108 ? -4.217  -54.570 -21.484 1.00 42.23  ? 154 ASN C OD1   1 
ATOM   2817 N ND2   . ASN C 3 108 ? -3.005  -56.466 -21.345 1.00 35.15  ? 154 ASN C ND2   1 
ATOM   2818 N N     . ALA C 3 109 ? -1.453  -51.371 -23.023 1.00 33.50  ? 155 ALA C N     1 
ATOM   2819 C CA    . ALA C 3 109 ? -0.805  -50.118 -22.685 1.00 32.79  ? 155 ALA C CA    1 
ATOM   2820 C C     . ALA C 3 109 ? -0.768  -49.959 -21.173 1.00 36.15  ? 155 ALA C C     1 
ATOM   2821 O O     . ALA C 3 109 ? -1.591  -50.520 -20.448 1.00 38.51  ? 155 ALA C O     1 
ATOM   2822 C CB    . ALA C 3 109 ? -1.542  -48.942 -23.321 1.00 29.25  ? 155 ALA C CB    1 
ATOM   2823 N N     . ALA C 3 110 ? 0.207   -49.201 -20.699 1.00 32.97  ? 156 ALA C N     1 
ATOM   2824 C CA    . ALA C 3 110 ? 0.245   -48.820 -19.302 1.00 31.43  ? 156 ALA C CA    1 
ATOM   2825 C C     . ALA C 3 110 ? -0.904  -47.883 -18.986 1.00 35.00  ? 156 ALA C C     1 
ATOM   2826 O O     . ALA C 3 110 ? -1.346  -47.103 -19.835 1.00 37.75  ? 156 ALA C O     1 
ATOM   2827 C CB    . ALA C 3 110 ? 1.566   -48.134 -18.979 1.00 34.16  ? 156 ALA C CB    1 
ATOM   2828 N N     . ILE C 3 111 ? -1.393  -47.966 -17.752 1.00 36.63  ? 157 ILE C N     1 
ATOM   2829 C CA    . ILE C 3 111 ? -2.415  -47.046 -17.250 1.00 36.75  ? 157 ILE C CA    1 
ATOM   2830 C C     . ILE C 3 111 ? -1.712  -45.814 -16.709 1.00 36.34  ? 157 ILE C C     1 
ATOM   2831 O O     . ILE C 3 111 ? -0.772  -45.937 -15.916 1.00 34.61  ? 157 ILE C O     1 
ATOM   2832 C CB    . ILE C 3 111 ? -3.252  -47.702 -16.143 1.00 33.60  ? 157 ILE C CB    1 
ATOM   2833 C CG1   . ILE C 3 111 ? -3.784  -49.049 -16.604 1.00 32.06  ? 157 ILE C CG1   1 
ATOM   2834 C CG2   . ILE C 3 111 ? -4.361  -46.772 -15.693 1.00 35.03  ? 157 ILE C CG2   1 
ATOM   2835 C CD1   . ILE C 3 111 ? -4.054  -49.954 -15.467 1.00 36.90  ? 157 ILE C CD1   1 
ATOM   2836 N N     . VAL C 3 112 ? -2.143  -44.629 -17.151 1.00 33.47  ? 158 VAL C N     1 
ATOM   2837 C CA    . VAL C 3 112 ? -1.597  -43.394 -16.594 1.00 38.11  ? 158 VAL C CA    1 
ATOM   2838 C C     . VAL C 3 112 ? -1.801  -43.419 -15.089 1.00 41.68  ? 158 VAL C C     1 
ATOM   2839 O O     . VAL C 3 112 ? -2.930  -43.548 -14.600 1.00 35.32  ? 158 VAL C O     1 
ATOM   2840 C CB    . VAL C 3 112 ? -2.268  -42.161 -17.210 1.00 43.58  ? 158 VAL C CB    1 
ATOM   2841 C CG1   . VAL C 3 112 ? -1.797  -40.892 -16.491 1.00 36.70  ? 158 VAL C CG1   1 
ATOM   2842 C CG2   . VAL C 3 112 ? -1.982  -42.082 -18.697 1.00 43.28  ? 158 VAL C CG2   1 
ATOM   2843 N N     . LEU C 3 113 ? -0.707  -43.305 -14.348 1.00 44.87  ? 159 LEU C N     1 
ATOM   2844 C CA    . LEU C 3 113 ? -0.783  -43.373 -12.898 1.00 42.87  ? 159 LEU C CA    1 
ATOM   2845 C C     . LEU C 3 113 ? -1.541  -42.155 -12.376 1.00 39.74  ? 159 LEU C C     1 
ATOM   2846 O O     . LEU C 3 113 ? -1.108  -41.019 -12.573 1.00 45.99  ? 159 LEU C O     1 
ATOM   2847 C CB    . LEU C 3 113 ? 0.630   -43.469 -12.316 1.00 34.99  ? 159 LEU C CB    1 
ATOM   2848 C CG    . LEU C 3 113 ? 0.703   -43.974 -10.869 1.00 36.27  ? 159 LEU C CG    1 
ATOM   2849 C CD1   . LEU C 3 113 ? 1.961   -44.710 -10.579 1.00 39.42  ? 159 LEU C CD1   1 
ATOM   2850 C CD2   . LEU C 3 113 ? 0.562   -42.826 -9.899  1.00 46.71  ? 159 LEU C CD2   1 
ATOM   2851 N N     . GLN C 3 114 ? -2.693  -42.391 -11.755 1.00 37.94  ? 160 GLN C N     1 
ATOM   2852 C CA    . GLN C 3 114 ? -3.527  -41.351 -11.161 1.00 40.59  ? 160 GLN C CA    1 
ATOM   2853 C C     . GLN C 3 114 ? -3.837  -41.727 -9.722  1.00 43.68  ? 160 GLN C C     1 
ATOM   2854 O O     . GLN C 3 114 ? -4.000  -42.906 -9.400  1.00 46.26  ? 160 GLN C O     1 
ATOM   2855 C CB    . GLN C 3 114 ? -4.863  -41.154 -11.898 1.00 38.06  ? 160 GLN C CB    1 
ATOM   2856 C CG    . GLN C 3 114 ? -4.775  -40.803 -13.373 1.00 35.84  ? 160 GLN C CG    1 
ATOM   2857 C CD    . GLN C 3 114 ? -6.128  -40.431 -13.944 1.00 49.04  ? 160 GLN C CD    1 
ATOM   2858 O OE1   . GLN C 3 114 ? -6.668  -39.369 -13.639 1.00 52.97  ? 160 GLN C OE1   1 
ATOM   2859 N NE2   . GLN C 3 114 ? -6.692  -41.307 -14.767 1.00 46.36  ? 160 GLN C NE2   1 
ATOM   2860 N N     . LEU C 3 115 ? -3.937  -40.718 -8.864  1.00 40.35  ? 161 LEU C N     1 
ATOM   2861 C CA    . LEU C 3 115 ? -4.173  -40.930 -7.448  1.00 42.69  ? 161 LEU C CA    1 
ATOM   2862 C C     . LEU C 3 115 ? -5.454  -40.220 -7.024  1.00 45.32  ? 161 LEU C C     1 
ATOM   2863 O O     . LEU C 3 115 ? -5.831  -39.210 -7.626  1.00 43.45  ? 161 LEU C O     1 
ATOM   2864 C CB    . LEU C 3 115 ? -2.988  -40.419 -6.618  1.00 39.84  ? 161 LEU C CB    1 
ATOM   2865 C CG    . LEU C 3 115 ? -1.675  -41.164 -6.887  1.00 44.56  ? 161 LEU C CG    1 
ATOM   2866 C CD1   . LEU C 3 115 ? -0.555  -40.670 -6.001  1.00 41.15  ? 161 LEU C CD1   1 
ATOM   2867 C CD2   . LEU C 3 115 ? -1.871  -42.647 -6.676  1.00 46.12  ? 161 LEU C CD2   1 
ATOM   2868 N N     . PRO C 3 116 ? -6.155  -40.728 -6.011  1.00 48.23  ? 162 PRO C N     1 
ATOM   2869 C CA    . PRO C 3 116 ? -7.486  -40.195 -5.703  1.00 49.16  ? 162 PRO C CA    1 
ATOM   2870 C C     . PRO C 3 116 ? -7.402  -38.780 -5.150  1.00 50.75  ? 162 PRO C C     1 
ATOM   2871 O O     . PRO C 3 116 ? -6.369  -38.347 -4.636  1.00 47.88  ? 162 PRO C O     1 
ATOM   2872 C CB    . PRO C 3 116 ? -8.033  -41.169 -4.651  1.00 48.99  ? 162 PRO C CB    1 
ATOM   2873 C CG    . PRO C 3 116 ? -7.112  -42.358 -4.688  1.00 47.45  ? 162 PRO C CG    1 
ATOM   2874 C CD    . PRO C 3 116 ? -5.783  -41.817 -5.097  1.00 44.83  ? 162 PRO C CD    1 
ATOM   2875 N N     . GLN C 3 117 ? -8.514  -38.050 -5.268  1.00 52.38  ? 163 GLN C N     1 
ATOM   2876 C CA    . GLN C 3 117 ? -8.531  -36.688 -4.755  1.00 52.89  ? 163 GLN C CA    1 
ATOM   2877 C C     . GLN C 3 117 ? -8.199  -36.693 -3.268  1.00 57.72  ? 163 GLN C C     1 
ATOM   2878 O O     . GLN C 3 117 ? -8.683  -37.534 -2.502  1.00 56.14  ? 163 GLN C O     1 
ATOM   2879 C CB    . GLN C 3 117 ? -9.884  -36.016 -5.009  1.00 56.11  ? 163 GLN C CB    1 
ATOM   2880 C CG    . GLN C 3 117 ? -10.980 -36.291 -3.980  1.00 61.02  ? 163 GLN C CG    1 
ATOM   2881 C CD    . GLN C 3 117 ? -11.779 -35.035 -3.628  1.00 67.49  ? 163 GLN C CD    1 
ATOM   2882 O OE1   . GLN C 3 117 ? -11.205 -33.986 -3.307  1.00 66.03  ? 163 GLN C OE1   1 
ATOM   2883 N NE2   . GLN C 3 117 ? -13.109 -35.139 -3.693  1.00 65.07  ? 163 GLN C NE2   1 
ATOM   2884 N N     . GLY C 3 118 ? -7.324  -35.777 -2.873  1.00 60.11  ? 164 GLY C N     1 
ATOM   2885 C CA    . GLY C 3 118 ? -6.894  -35.699 -1.498  1.00 53.08  ? 164 GLY C CA    1 
ATOM   2886 C C     . GLY C 3 118 ? -5.604  -36.412 -1.178  1.00 52.30  ? 164 GLY C C     1 
ATOM   2887 O O     . GLY C 3 118 ? -5.237  -36.469 0.000   1.00 55.47  ? 164 GLY C O     1 
ATOM   2888 N N     . THR C 3 119 ? -4.896  -36.945 -2.173  1.00 50.13  ? 165 THR C N     1 
ATOM   2889 C CA    . THR C 3 119 ? -3.658  -37.675 -1.906  1.00 53.17  ? 165 THR C CA    1 
ATOM   2890 C C     . THR C 3 119 ? -2.468  -36.719 -1.808  1.00 58.63  ? 165 THR C C     1 
ATOM   2891 O O     . THR C 3 119 ? -2.389  -35.721 -2.528  1.00 60.22  ? 165 THR C O     1 
ATOM   2892 C CB    . THR C 3 119 ? -3.381  -38.723 -2.999  1.00 53.42  ? 165 THR C CB    1 
ATOM   2893 O OG1   . THR C 3 119 ? -4.581  -39.443 -3.321  1.00 47.31  ? 165 THR C OG1   1 
ATOM   2894 C CG2   . THR C 3 119 ? -2.299  -39.715 -2.544  1.00 40.51  ? 165 THR C CG2   1 
ATOM   2895 N N     . THR C 3 120 ? -1.524  -37.050 -0.924  1.00 55.03  ? 166 THR C N     1 
ATOM   2896 C CA    . THR C 3 120 ? -0.356  -36.224 -0.665  1.00 54.52  ? 166 THR C CA    1 
ATOM   2897 C C     . THR C 3 120 ? 0.909   -36.930 -1.128  1.00 51.85  ? 166 THR C C     1 
ATOM   2898 O O     . THR C 3 120 ? 1.009   -38.154 -1.084  1.00 56.20  ? 166 THR C O     1 
ATOM   2899 C CB    . THR C 3 120 ? -0.216  -35.882 0.829   1.00 61.78  ? 166 THR C CB    1 
ATOM   2900 O OG1   . THR C 3 120 ? 0.138   -37.060 1.560   1.00 57.89  ? 166 THR C OG1   1 
ATOM   2901 C CG2   . THR C 3 120 ? -1.520  -35.316 1.399   1.00 55.64  ? 166 THR C CG2   1 
ATOM   2902 N N     . LEU C 3 121 ? 1.879   -36.144 -1.558  1.00 52.63  ? 167 LEU C N     1 
ATOM   2903 C CA    . LEU C 3 121 ? 3.140   -36.630 -2.089  1.00 52.77  ? 167 LEU C CA    1 
ATOM   2904 C C     . LEU C 3 121 ? 4.289   -35.958 -1.367  1.00 55.66  ? 167 LEU C C     1 
ATOM   2905 O O     . LEU C 3 121 ? 4.133   -34.863 -0.812  1.00 58.54  ? 167 LEU C O     1 
ATOM   2906 C CB    . LEU C 3 121 ? 3.258   -36.341 -3.592  1.00 52.21  ? 167 LEU C CB    1 
ATOM   2907 C CG    . LEU C 3 121 ? 2.558   -37.277 -4.566  1.00 52.71  ? 167 LEU C CG    1 
ATOM   2908 C CD1   . LEU C 3 121 ? 2.601   -36.691 -5.960  1.00 55.50  ? 167 LEU C CD1   1 
ATOM   2909 C CD2   . LEU C 3 121 ? 3.225   -38.628 -4.557  1.00 50.13  ? 167 LEU C CD2   1 
ATOM   2910 N N     . PRO C 3 122 ? 5.465   -36.580 -1.360  1.00 54.47  ? 168 PRO C N     1 
ATOM   2911 C CA    . PRO C 3 122 ? 6.675   -35.874 -0.926  1.00 56.76  ? 168 PRO C CA    1 
ATOM   2912 C C     . PRO C 3 122 ? 7.046   -34.775 -1.902  1.00 62.07  ? 168 PRO C C     1 
ATOM   2913 O O     . PRO C 3 122 ? 6.296   -34.490 -2.837  1.00 61.73  ? 168 PRO C O     1 
ATOM   2914 C CB    . PRO C 3 122 ? 7.747   -36.972 -0.901  1.00 53.96  ? 168 PRO C CB    1 
ATOM   2915 C CG    . PRO C 3 122 ? 6.985   -38.234 -0.753  1.00 57.71  ? 168 PRO C CG    1 
ATOM   2916 C CD    . PRO C 3 122 ? 5.680   -38.030 -1.476  1.00 55.28  ? 168 PRO C CD    1 
ATOM   2917 N N     . LYS C 3 123 ? 8.190   -34.140 -1.685  1.00 62.63  ? 169 LYS C N     1 
ATOM   2918 C CA    . LYS C 3 123 ? 8.703   -33.140 -2.603  1.00 57.80  ? 169 LYS C CA    1 
ATOM   2919 C C     . LYS C 3 123 ? 9.542   -33.804 -3.685  1.00 57.26  ? 169 LYS C C     1 
ATOM   2920 O O     . LYS C 3 123 ? 10.265  -34.772 -3.438  1.00 58.97  ? 169 LYS C O     1 
ATOM   2921 C CB    . LYS C 3 123 ? 9.545   -32.102 -1.859  1.00 66.42  ? 169 LYS C CB    1 
ATOM   2922 C CG    . LYS C 3 123 ? 8.938   -30.703 -1.811  1.00 68.85  ? 169 LYS C CG    1 
ATOM   2923 C CD    . LYS C 3 123 ? 8.118   -30.468 -0.552  1.00 69.51  ? 169 LYS C CD    1 
ATOM   2924 C CE    . LYS C 3 123 ? 7.919   -28.979 -0.324  1.00 66.39  ? 169 LYS C CE    1 
ATOM   2925 N NZ    . LYS C 3 123 ? 7.499   -28.311 -1.592  1.00 69.58  ? 169 LYS C NZ    1 
ATOM   2926 N N     . GLY C 3 124 ? 9.462   -33.250 -4.887  1.00 55.51  ? 170 GLY C N     1 
ATOM   2927 C CA    . GLY C 3 124 ? 10.118  -33.834 -6.025  1.00 49.97  ? 170 GLY C CA    1 
ATOM   2928 C C     . GLY C 3 124 ? 9.274   -34.825 -6.784  1.00 51.32  ? 170 GLY C C     1 
ATOM   2929 O O     . GLY C 3 124 ? 9.732   -35.330 -7.814  1.00 54.07  ? 170 GLY C O     1 
ATOM   2930 N N     . PHE C 3 125 ? 8.062   -35.114 -6.301  1.00 53.49  ? 171 PHE C N     1 
ATOM   2931 C CA    . PHE C 3 125 ? 7.095   -36.003 -6.935  1.00 53.80  ? 171 PHE C CA    1 
ATOM   2932 C C     . PHE C 3 125 ? 5.881   -35.195 -7.379  1.00 52.40  ? 171 PHE C C     1 
ATOM   2933 O O     . PHE C 3 125 ? 5.434   -34.293 -6.665  1.00 53.99  ? 171 PHE C O     1 
ATOM   2934 C CB    . PHE C 3 125 ? 6.625   -37.111 -5.976  1.00 50.98  ? 171 PHE C CB    1 
ATOM   2935 C CG    . PHE C 3 125 ? 7.705   -38.073 -5.558  1.00 52.01  ? 171 PHE C CG    1 
ATOM   2936 C CD1   . PHE C 3 125 ? 8.187   -39.028 -6.444  1.00 50.59  ? 171 PHE C CD1   1 
ATOM   2937 C CD2   . PHE C 3 125 ? 8.210   -38.046 -4.273  1.00 52.95  ? 171 PHE C CD2   1 
ATOM   2938 C CE1   . PHE C 3 125 ? 9.151   -39.917 -6.074  1.00 50.94  ? 171 PHE C CE1   1 
ATOM   2939 C CE2   . PHE C 3 125 ? 9.183   -38.935 -3.889  1.00 56.89  ? 171 PHE C CE2   1 
ATOM   2940 C CZ    . PHE C 3 125 ? 9.660   -39.875 -4.795  1.00 58.83  ? 171 PHE C CZ    1 
ATOM   2941 N N     . TYR C 3 126 ? 5.324   -35.532 -8.538  1.00 47.27  ? 172 TYR C N     1 
ATOM   2942 C CA    . TYR C 3 126 ? 4.247   -34.739 -9.119  1.00 51.18  ? 172 TYR C CA    1 
ATOM   2943 C C     . TYR C 3 126 ? 3.087   -35.638 -9.524  1.00 52.83  ? 172 TYR C C     1 
ATOM   2944 O O     . TYR C 3 126 ? 3.283   -36.637 -10.226 1.00 53.72  ? 172 TYR C O     1 
ATOM   2945 C CB    . TYR C 3 126 ? 4.765   -33.930 -10.317 1.00 52.25  ? 172 TYR C CB    1 
ATOM   2946 C CG    . TYR C 3 126 ? 5.793   -32.892 -9.920  1.00 49.57  ? 172 TYR C CG    1 
ATOM   2947 C CD1   . TYR C 3 126 ? 7.149   -33.211 -9.837  1.00 48.94  ? 172 TYR C CD1   1 
ATOM   2948 C CD2   . TYR C 3 126 ? 5.399   -31.601 -9.594  1.00 49.37  ? 172 TYR C CD2   1 
ATOM   2949 C CE1   . TYR C 3 126 ? 8.083   -32.263 -9.454  1.00 45.31  ? 172 TYR C CE1   1 
ATOM   2950 C CE2   . TYR C 3 126 ? 6.309   -30.655 -9.212  1.00 44.57  ? 172 TYR C CE2   1 
ATOM   2951 C CZ    . TYR C 3 126 ? 7.649   -30.985 -9.142  1.00 50.47  ? 172 TYR C CZ    1 
ATOM   2952 O OH    . TYR C 3 126 ? 8.539   -30.010 -8.769  1.00 50.35  ? 172 TYR C OH    1 
ATOM   2953 N N     . ALA C 3 127 ? 1.885   -35.281 -9.075  1.00 55.90  ? 173 ALA C N     1 
ATOM   2954 C CA    . ALA C 3 127 ? 0.668   -36.033 -9.386  1.00 57.23  ? 173 ALA C CA    1 
ATOM   2955 C C     . ALA C 3 127 ? -0.092  -35.433 -10.572 1.00 54.52  ? 173 ALA C C     1 
ATOM   2956 O O     . ALA C 3 127 ? -0.588  -36.156 -11.436 1.00 61.03  ? 173 ALA C O     1 
ATOM   2957 C CB    . ALA C 3 127 ? -0.236  -36.097 -8.160  1.00 63.21  ? 173 ALA C CB    1 
ATOM   2958 N N     . ASN D 4 1   ? 32.052  2.764   -10.959 1.00 66.73  ? 48  ASN D N     1 
ATOM   2959 C CA    . ASN D 4 1   ? 33.298  3.213   -11.580 1.00 65.19  ? 48  ASN D CA    1 
ATOM   2960 C C     . ASN D 4 1   ? 33.780  2.245   -12.680 1.00 58.21  ? 48  ASN D C     1 
ATOM   2961 O O     . ASN D 4 1   ? 33.687  2.572   -13.865 1.00 55.31  ? 48  ASN D O     1 
ATOM   2962 C CB    . ASN D 4 1   ? 34.401  3.426   -10.516 1.00 66.75  ? 48  ASN D CB    1 
ATOM   2963 C CG    . ASN D 4 1   ? 34.390  2.368   -9.418  1.00 68.54  ? 48  ASN D CG    1 
ATOM   2964 O OD1   . ASN D 4 1   ? 35.286  1.526   -9.349  1.00 70.30  ? 48  ASN D OD1   1 
ATOM   2965 N ND2   . ASN D 4 1   ? 33.389  2.423   -8.543  1.00 66.59  ? 48  ASN D ND2   1 
ATOM   2966 N N     . THR D 4 2   ? 34.277  1.063   -12.302 1.00 59.05  ? 49  THR D N     1 
ATOM   2967 C CA    . THR D 4 2   ? 34.913  0.146   -13.241 1.00 50.95  ? 49  THR D CA    1 
ATOM   2968 C C     . THR D 4 2   ? 34.309  -1.251  -13.129 1.00 54.52  ? 49  THR D C     1 
ATOM   2969 O O     . THR D 4 2   ? 33.960  -1.703  -12.032 1.00 61.46  ? 49  THR D O     1 
ATOM   2970 C CB    . THR D 4 2   ? 36.413  0.075   -12.993 1.00 60.13  ? 49  THR D CB    1 
ATOM   2971 O OG1   . THR D 4 2   ? 37.015  -0.807  -13.949 1.00 57.15  ? 49  THR D OG1   1 
ATOM   2972 C CG2   . THR D 4 2   ? 36.703  -0.425  -11.563 1.00 62.31  ? 49  THR D CG2   1 
ATOM   2973 N N     . ALA D 4 3   ? 34.183  -1.936  -14.265 1.00 44.60  ? 50  ALA D N     1 
ATOM   2974 C CA    . ALA D 4 3   ? 33.563  -3.250  -14.244 1.00 37.31  ? 50  ALA D CA    1 
ATOM   2975 C C     . ALA D 4 3   ? 33.888  -4.016  -15.521 1.00 29.47  ? 50  ALA D C     1 
ATOM   2976 O O     . ALA D 4 3   ? 34.241  -3.440  -16.551 1.00 32.89  ? 50  ALA D O     1 
ATOM   2977 C CB    . ALA D 4 3   ? 32.044  -3.134  -14.055 1.00 40.85  ? 50  ALA D CB    1 
ATOM   2978 N N     . SER D 4 4   ? 33.771  -5.333  -15.426 1.00 31.55  ? 51  SER D N     1 
ATOM   2979 C CA    . SER D 4 4   ? 33.790  -6.168  -16.614 1.00 34.72  ? 51  SER D CA    1 
ATOM   2980 C C     . SER D 4 4   ? 32.673  -5.738  -17.538 1.00 35.09  ? 51  SER D C     1 
ATOM   2981 O O     . SER D 4 4   ? 31.612  -5.289  -17.090 1.00 33.87  ? 51  SER D O     1 
ATOM   2982 C CB    . SER D 4 4   ? 33.603  -7.648  -16.255 1.00 34.74  ? 51  SER D CB    1 
ATOM   2983 O OG    . SER D 4 4   ? 33.497  -8.443  -17.433 1.00 31.45  ? 51  SER D OG    1 
ATOM   2984 N N     . TRP D 4 5   ? 32.931  -5.850  -18.839 1.00 32.30  ? 52  TRP D N     1 
ATOM   2985 C CA    . TRP D 4 5   ? 31.893  -5.575  -19.816 1.00 34.33  ? 52  TRP D CA    1 
ATOM   2986 C C     . TRP D 4 5   ? 30.831  -6.679  -19.889 1.00 37.60  ? 52  TRP D C     1 
ATOM   2987 O O     . TRP D 4 5   ? 29.779  -6.459  -20.498 1.00 34.95  ? 52  TRP D O     1 
ATOM   2988 C CB    . TRP D 4 5   ? 32.524  -5.365  -21.184 1.00 30.89  ? 52  TRP D CB    1 
ATOM   2989 C CG    . TRP D 4 5   ? 32.808  -3.941  -21.496 1.00 35.72  ? 52  TRP D CG    1 
ATOM   2990 C CD1   . TRP D 4 5   ? 34.031  -3.368  -21.682 1.00 36.88  ? 52  TRP D CD1   1 
ATOM   2991 C CD2   . TRP D 4 5   ? 31.848  -2.897  -21.668 1.00 40.92  ? 52  TRP D CD2   1 
ATOM   2992 N NE1   . TRP D 4 5   ? 33.893  -2.032  -21.966 1.00 35.57  ? 52  TRP D NE1   1 
ATOM   2993 C CE2   . TRP D 4 5   ? 32.563  -1.714  -21.960 1.00 42.45  ? 52  TRP D CE2   1 
ATOM   2994 C CE3   . TRP D 4 5   ? 30.455  -2.846  -21.615 1.00 37.64  ? 52  TRP D CE3   1 
ATOM   2995 C CZ2   . TRP D 4 5   ? 31.930  -0.495  -22.184 1.00 42.05  ? 52  TRP D CZ2   1 
ATOM   2996 C CZ3   . TRP D 4 5   ? 29.831  -1.636  -21.831 1.00 42.87  ? 52  TRP D CZ3   1 
ATOM   2997 C CH2   . TRP D 4 5   ? 30.565  -0.476  -22.116 1.00 38.95  ? 52  TRP D CH2   1 
ATOM   2998 N N     . PHE D 4 6   ? 31.059  -7.833  -19.262 1.00 34.08  ? 53  PHE D N     1 
ATOM   2999 C CA    . PHE D 4 6   ? 30.250  -9.025  -19.470 1.00 36.39  ? 53  PHE D CA    1 
ATOM   3000 C C     . PHE D 4 6   ? 29.749  -9.565  -18.140 1.00 39.16  ? 53  PHE D C     1 
ATOM   3001 O O     . PHE D 4 6   ? 30.293  -9.255  -17.078 1.00 38.92  ? 53  PHE D O     1 
ATOM   3002 C CB    . PHE D 4 6   ? 31.044  -10.115 -20.192 1.00 29.47  ? 53  PHE D CB    1 
ATOM   3003 C CG    . PHE D 4 6   ? 31.541  -9.691  -21.519 1.00 34.42  ? 53  PHE D CG    1 
ATOM   3004 C CD1   . PHE D 4 6   ? 32.762  -9.022  -21.635 1.00 35.04  ? 53  PHE D CD1   1 
ATOM   3005 C CD2   . PHE D 4 6   ? 30.799  -9.944  -22.663 1.00 32.39  ? 53  PHE D CD2   1 
ATOM   3006 C CE1   . PHE D 4 6   ? 33.227  -8.617  -22.874 1.00 36.05  ? 53  PHE D CE1   1 
ATOM   3007 C CE2   . PHE D 4 6   ? 31.246  -9.538  -23.899 1.00 34.03  ? 53  PHE D CE2   1 
ATOM   3008 C CZ    . PHE D 4 6   ? 32.467  -8.864  -24.013 1.00 38.90  ? 53  PHE D CZ    1 
ATOM   3009 N N     . THR D 4 7   ? 28.689  -10.374 -18.212 1.00 35.61  ? 54  THR D N     1 
ATOM   3010 C CA    . THR D 4 7   ? 28.197  -11.071 -17.031 1.00 40.41  ? 54  THR D CA    1 
ATOM   3011 C C     . THR D 4 7   ? 29.161  -12.203 -16.651 1.00 38.71  ? 54  THR D C     1 
ATOM   3012 O O     . THR D 4 7   ? 29.893  -12.736 -17.486 1.00 43.04  ? 54  THR D O     1 
ATOM   3013 C CB    . THR D 4 7   ? 26.759  -11.611 -17.258 1.00 38.15  ? 54  THR D CB    1 
ATOM   3014 O OG1   . THR D 4 7   ? 26.640  -12.193 -18.566 1.00 40.21  ? 54  THR D OG1   1 
ATOM   3015 C CG2   . THR D 4 7   ? 25.733  -10.502 -17.169 1.00 34.70  ? 54  THR D CG2   1 
ATOM   3016 N N     . ALA D 4 8   ? 29.137  -12.572 -15.370 1.00 36.70  ? 55  ALA D N     1 
ATOM   3017 C CA    . ALA D 4 8   ? 30.058  -13.533 -14.773 1.00 41.49  ? 55  ALA D CA    1 
ATOM   3018 C C     . ALA D 4 8   ? 29.820  -14.974 -15.256 1.00 49.42  ? 55  ALA D C     1 
ATOM   3019 O O     . ALA D 4 8   ? 28.731  -15.348 -15.692 1.00 47.50  ? 55  ALA D O     1 
ATOM   3020 C CB    . ALA D 4 8   ? 29.926  -13.482 -13.251 1.00 43.78  ? 55  ALA D CB    1 
ATOM   3021 N N     . LEU D 4 9   ? 30.873  -15.794 -15.168 1.00 46.69  ? 56  LEU D N     1 
ATOM   3022 C CA    . LEU D 4 9   ? 30.753  -17.249 -15.227 1.00 48.14  ? 56  LEU D CA    1 
ATOM   3023 C C     . LEU D 4 9   ? 30.814  -17.772 -13.803 1.00 48.51  ? 56  LEU D C     1 
ATOM   3024 O O     . LEU D 4 9   ? 31.833  -17.591 -13.125 1.00 46.13  ? 56  LEU D O     1 
ATOM   3025 C CB    . LEU D 4 9   ? 31.871  -17.893 -16.050 1.00 39.55  ? 56  LEU D CB    1 
ATOM   3026 C CG    . LEU D 4 9   ? 31.830  -17.869 -17.577 1.00 40.67  ? 56  LEU D CG    1 
ATOM   3027 C CD1   . LEU D 4 9   ? 33.088  -18.491 -18.140 1.00 43.72  ? 56  LEU D CD1   1 
ATOM   3028 C CD2   . LEU D 4 9   ? 30.617  -18.601 -18.092 1.00 45.86  ? 56  LEU D CD2   1 
ATOM   3029 N N     . THR D 4 10  ? 29.748  -18.435 -13.357 1.00 39.55  ? 57  THR D N     1 
ATOM   3030 C CA    . THR D 4 10  ? 29.691  -18.938 -11.990 1.00 45.15  ? 57  THR D CA    1 
ATOM   3031 C C     . THR D 4 10  ? 30.243  -20.360 -11.936 1.00 52.01  ? 57  THR D C     1 
ATOM   3032 O O     . THR D 4 10  ? 29.828  -21.226 -12.715 1.00 53.08  ? 57  THR D O     1 
ATOM   3033 C CB    . THR D 4 10  ? 28.259  -18.897 -11.442 1.00 44.13  ? 57  THR D CB    1 
ATOM   3034 O OG1   . THR D 4 10  ? 27.793  -17.542 -11.405 1.00 45.09  ? 57  THR D OG1   1 
ATOM   3035 C CG2   . THR D 4 10  ? 28.205  -19.471 -10.035 1.00 43.83  ? 57  THR D CG2   1 
ATOM   3036 N N     . GLN D 4 11  ? 31.182  -20.594 -11.020 1.00 46.69  ? 58  GLN D N     1 
ATOM   3037 C CA    . GLN D 4 11  ? 31.824  -21.898 -10.850 1.00 53.33  ? 58  GLN D CA    1 
ATOM   3038 C C     . GLN D 4 11  ? 31.190  -22.588 -9.646  1.00 56.98  ? 58  GLN D C     1 
ATOM   3039 O O     . GLN D 4 11  ? 31.680  -22.486 -8.521  1.00 57.68  ? 58  GLN D O     1 
ATOM   3040 C CB    . GLN D 4 11  ? 33.332  -21.738 -10.664 1.00 50.47  ? 58  GLN D CB    1 
ATOM   3041 C CG    . GLN D 4 11  ? 34.089  -23.034 -10.406 1.00 50.85  ? 58  GLN D CG    1 
ATOM   3042 C CD    . GLN D 4 11  ? 35.416  -22.808 -9.701  1.00 58.27  ? 58  GLN D CD    1 
ATOM   3043 O OE1   . GLN D 4 11  ? 36.005  -21.729 -9.787  1.00 56.94  ? 58  GLN D OE1   1 
ATOM   3044 N NE2   . GLN D 4 11  ? 35.890  -23.825 -8.992  1.00 60.06  ? 58  GLN D NE2   1 
ATOM   3045 N N     . HIS D 4 12  ? 30.097  -23.309 -9.873  1.00 61.51  ? 59  HIS D N     1 
ATOM   3046 C CA    . HIS D 4 12  ? 29.492  -24.047 -8.770  1.00 65.37  ? 59  HIS D CA    1 
ATOM   3047 C C     . HIS D 4 12  ? 30.105  -25.429 -8.582  1.00 65.49  ? 59  HIS D C     1 
ATOM   3048 O O     . HIS D 4 12  ? 29.680  -26.159 -7.681  1.00 70.79  ? 59  HIS D O     1 
ATOM   3049 C CB    . HIS D 4 12  ? 27.982  -24.167 -8.958  1.00 64.35  ? 59  HIS D CB    1 
ATOM   3050 C CG    . HIS D 4 12  ? 27.580  -25.169 -9.988  1.00 71.26  ? 59  HIS D CG    1 
ATOM   3051 N ND1   . HIS D 4 12  ? 27.571  -24.885 -11.337 1.00 70.36  ? 59  HIS D ND1   1 
ATOM   3052 C CD2   . HIS D 4 12  ? 27.161  -26.452 -9.869  1.00 75.14  ? 59  HIS D CD2   1 
ATOM   3053 C CE1   . HIS D 4 12  ? 27.167  -25.952 -12.006 1.00 74.14  ? 59  HIS D CE1   1 
ATOM   3054 N NE2   . HIS D 4 12  ? 26.912  -26.917 -11.139 1.00 77.43  ? 59  HIS D NE2   1 
ATOM   3055 N N     . GLY D 4 13  ? 31.086  -25.795 -9.397  1.00 59.68  ? 60  GLY D N     1 
ATOM   3056 C CA    . GLY D 4 13  ? 31.844  -27.022 -9.263  1.00 59.50  ? 60  GLY D CA    1 
ATOM   3057 C C     . GLY D 4 13  ? 33.138  -26.823 -8.499  1.00 65.93  ? 60  GLY D C     1 
ATOM   3058 O O     . GLY D 4 13  ? 33.268  -25.918 -7.666  1.00 67.82  ? 60  GLY D O     1 
ATOM   3059 N N     . LYS D 4 14  ? 34.123  -27.667 -8.798  1.00 65.77  ? 61  LYS D N     1 
ATOM   3060 C CA    . LYS D 4 14  ? 35.320  -27.763 -7.971  1.00 71.29  ? 61  LYS D CA    1 
ATOM   3061 C C     . LYS D 4 14  ? 36.614  -27.332 -8.654  1.00 67.38  ? 61  LYS D C     1 
ATOM   3062 O O     . LYS D 4 14  ? 37.508  -26.826 -7.973  1.00 65.72  ? 61  LYS D O     1 
ATOM   3063 C CB    . LYS D 4 14  ? 35.478  -29.198 -7.448  1.00 70.63  ? 61  LYS D CB    1 
ATOM   3064 C CG    . LYS D 4 14  ? 34.938  -29.419 -6.026  1.00 73.53  ? 61  LYS D CG    1 
ATOM   3065 C CD    . LYS D 4 14  ? 33.612  -28.683 -5.760  1.00 75.12  ? 61  LYS D CD    1 
ATOM   3066 C CE    . LYS D 4 14  ? 33.769  -27.575 -4.707  1.00 72.29  ? 61  LYS D CE    1 
ATOM   3067 N NZ    . LYS D 4 14  ? 32.476  -26.930 -4.318  1.00 71.21  ? 61  LYS D NZ    1 
ATOM   3068 N N     . GLU D 4 15  ? 36.748  -27.505 -9.966  1.00 67.08  ? 62  GLU D N     1 
ATOM   3069 C CA    . GLU D 4 15  ? 37.995  -27.170 -10.646 1.00 65.71  ? 62  GLU D CA    1 
ATOM   3070 C C     . GLU D 4 15  ? 37.934  -25.767 -11.244 1.00 63.28  ? 62  GLU D C     1 
ATOM   3071 O O     . GLU D 4 15  ? 36.872  -25.285 -11.654 1.00 59.83  ? 62  GLU D O     1 
ATOM   3072 C CB    . GLU D 4 15  ? 38.322  -28.195 -11.739 1.00 64.43  ? 62  GLU D CB    1 
ATOM   3073 C CG    . GLU D 4 15  ? 37.144  -28.577 -12.625 1.00 73.07  ? 62  GLU D CG    1 
ATOM   3074 C CD    . GLU D 4 15  ? 36.505  -29.910 -12.231 1.00 81.34  ? 62  GLU D CD    1 
ATOM   3075 O OE1   . GLU D 4 15  ? 37.265  -30.861 -11.921 1.00 84.59  ? 62  GLU D OE1   1 
ATOM   3076 O OE2   . GLU D 4 15  ? 35.249  -30.005 -12.233 1.00 70.62  ? 62  GLU D OE2   1 
ATOM   3077 N N     . ASP D 4 16  ? 39.096  -25.116 -11.296 1.00 59.83  ? 63  ASP D N     1 
ATOM   3078 C CA    . ASP D 4 16  ? 39.195  -23.751 -11.792 1.00 55.97  ? 63  ASP D CA    1 
ATOM   3079 C C     . ASP D 4 16  ? 38.833  -23.674 -13.273 1.00 56.17  ? 63  ASP D C     1 
ATOM   3080 O O     . ASP D 4 16  ? 38.802  -24.672 -13.999 1.00 52.17  ? 63  ASP D O     1 
ATOM   3081 C CB    . ASP D 4 16  ? 40.607  -23.197 -11.595 1.00 55.46  ? 63  ASP D CB    1 
ATOM   3082 C CG    . ASP D 4 16  ? 41.008  -23.110 -10.134 1.00 62.45  ? 63  ASP D CG    1 
ATOM   3083 O OD1   . ASP D 4 16  ? 40.175  -22.690 -9.296  1.00 63.40  ? 63  ASP D OD1   1 
ATOM   3084 O OD2   . ASP D 4 16  ? 42.165  -23.468 -9.829  1.00 67.66  ? 63  ASP D OD2   1 
ATOM   3085 N N     . LEU D 4 17  ? 38.557  -22.454 -13.715 1.00 54.80  ? 64  LEU D N     1 
ATOM   3086 C CA    . LEU D 4 17  ? 38.248  -22.218 -15.113 1.00 49.77  ? 64  LEU D CA    1 
ATOM   3087 C C     . LEU D 4 17  ? 39.461  -22.528 -15.981 1.00 47.63  ? 64  LEU D C     1 
ATOM   3088 O O     . LEU D 4 17  ? 40.605  -22.326 -15.581 1.00 47.43  ? 64  LEU D O     1 
ATOM   3089 C CB    . LEU D 4 17  ? 37.809  -20.765 -15.300 1.00 48.08  ? 64  LEU D CB    1 
ATOM   3090 C CG    . LEU D 4 17  ? 37.223  -20.347 -16.634 1.00 44.08  ? 64  LEU D CG    1 
ATOM   3091 C CD1   . LEU D 4 17  ? 36.297  -21.427 -17.125 1.00 49.43  ? 64  LEU D CD1   1 
ATOM   3092 C CD2   . LEU D 4 17  ? 36.452  -19.068 -16.428 1.00 43.24  ? 64  LEU D CD2   1 
ATOM   3093 N N     . LYS D 4 18  ? 39.200  -23.030 -17.180 1.00 50.71  ? 65  LYS D N     1 
ATOM   3094 C CA    . LYS D 4 18  ? 40.252  -23.237 -18.163 1.00 52.33  ? 65  LYS D CA    1 
ATOM   3095 C C     . LYS D 4 18  ? 39.589  -23.512 -19.499 1.00 47.42  ? 65  LYS D C     1 
ATOM   3096 O O     . LYS D 4 18  ? 38.608  -24.251 -19.560 1.00 55.71  ? 65  LYS D O     1 
ATOM   3097 C CB    . LYS D 4 18  ? 41.177  -24.401 -17.773 1.00 54.08  ? 65  LYS D CB    1 
ATOM   3098 C CG    . LYS D 4 18  ? 42.184  -24.787 -18.858 1.00 58.15  ? 65  LYS D CG    1 
ATOM   3099 C CD    . LYS D 4 18  ? 42.862  -26.131 -18.556 1.00 63.63  ? 65  LYS D CD    1 
ATOM   3100 C CE    . LYS D 4 18  ? 41.861  -27.292 -18.666 1.00 66.00  ? 65  LYS D CE    1 
ATOM   3101 N NZ    . LYS D 4 18  ? 42.437  -28.647 -18.387 1.00 64.43  ? 65  LYS D NZ    1 
ATOM   3102 N N     . PHE D 4 19  ? 40.121  -22.907 -20.555 1.00 47.74  ? 66  PHE D N     1 
ATOM   3103 C CA    . PHE D 4 19  ? 39.676  -23.121 -21.917 1.00 48.41  ? 66  PHE D CA    1 
ATOM   3104 C C     . PHE D 4 19  ? 40.843  -23.569 -22.789 1.00 52.45  ? 66  PHE D C     1 
ATOM   3105 O O     . PHE D 4 19  ? 41.953  -23.038 -22.665 1.00 52.20  ? 66  PHE D O     1 
ATOM   3106 C CB    . PHE D 4 19  ? 39.075  -21.843 -22.527 1.00 52.07  ? 66  PHE D CB    1 
ATOM   3107 C CG    . PHE D 4 19  ? 37.764  -21.429 -21.920 1.00 51.62  ? 66  PHE D CG    1 
ATOM   3108 C CD1   . PHE D 4 19  ? 36.573  -21.936 -22.410 1.00 46.45  ? 66  PHE D CD1   1 
ATOM   3109 C CD2   . PHE D 4 19  ? 37.722  -20.508 -20.877 1.00 48.32  ? 66  PHE D CD2   1 
ATOM   3110 C CE1   . PHE D 4 19  ? 35.368  -21.557 -21.859 1.00 45.75  ? 66  PHE D CE1   1 
ATOM   3111 C CE2   . PHE D 4 19  ? 36.511  -20.117 -20.319 1.00 48.24  ? 66  PHE D CE2   1 
ATOM   3112 C CZ    . PHE D 4 19  ? 35.333  -20.645 -20.810 1.00 44.71  ? 66  PHE D CZ    1 
ATOM   3113 N N     . PRO D 4 20  ? 40.616  -24.514 -23.694 1.00 55.18  ? 67  PRO D N     1 
ATOM   3114 C CA    . PRO D 4 20  ? 41.651  -24.864 -24.670 1.00 55.37  ? 67  PRO D CA    1 
ATOM   3115 C C     . PRO D 4 20  ? 41.984  -23.678 -25.562 1.00 56.91  ? 67  PRO D C     1 
ATOM   3116 O O     . PRO D 4 20  ? 41.165  -22.776 -25.762 1.00 57.17  ? 67  PRO D O     1 
ATOM   3117 C CB    . PRO D 4 20  ? 41.011  -26.000 -25.476 1.00 56.91  ? 67  PRO D CB    1 
ATOM   3118 C CG    . PRO D 4 20  ? 39.866  -26.474 -24.627 1.00 56.31  ? 67  PRO D CG    1 
ATOM   3119 C CD    . PRO D 4 20  ? 39.387  -25.297 -23.877 1.00 51.94  ? 67  PRO D CD    1 
ATOM   3120 N N     . ARG D 4 21  ? 43.210  -23.697 -26.092 1.00 57.07  ? 68  ARG D N     1 
ATOM   3121 C CA    . ARG D 4 21  ? 43.720  -22.631 -26.946 1.00 54.90  ? 68  ARG D CA    1 
ATOM   3122 C C     . ARG D 4 21  ? 42.739  -22.347 -28.079 1.00 54.83  ? 68  ARG D C     1 
ATOM   3123 O O     . ARG D 4 21  ? 42.202  -23.269 -28.696 1.00 59.39  ? 68  ARG D O     1 
ATOM   3124 C CB    . ARG D 4 21  ? 45.095  -23.048 -27.505 1.00 60.90  ? 68  ARG D CB    1 
ATOM   3125 C CG    . ARG D 4 21  ? 46.128  -21.929 -27.684 1.00 65.15  ? 68  ARG D CG    1 
ATOM   3126 C CD    . ARG D 4 21  ? 47.531  -22.473 -28.076 1.00 72.55  ? 68  ARG D CD    1 
ATOM   3127 N NE    . ARG D 4 21  ? 47.741  -22.562 -29.521 1.00 77.96  ? 68  ARG D NE    1 
ATOM   3128 C CZ    . ARG D 4 21  ? 48.575  -21.794 -30.216 1.00 77.00  ? 68  ARG D CZ    1 
ATOM   3129 N NH1   . ARG D 4 21  ? 49.322  -20.875 -29.627 1.00 75.17  ? 68  ARG D NH1   1 
ATOM   3130 N NH2   . ARG D 4 21  ? 48.664  -21.956 -31.535 1.00 71.76  ? 68  ARG D NH2   1 
ATOM   3131 N N     . GLY D 4 22  ? 42.476  -21.059 -28.326 1.00 55.24  ? 69  GLY D N     1 
ATOM   3132 C CA    . GLY D 4 22  ? 41.547  -20.634 -29.360 1.00 48.16  ? 69  GLY D CA    1 
ATOM   3133 C C     . GLY D 4 22  ? 40.120  -20.382 -28.905 1.00 49.60  ? 69  GLY D C     1 
ATOM   3134 O O     . GLY D 4 22  ? 39.342  -19.806 -29.673 1.00 52.33  ? 69  GLY D O     1 
ATOM   3135 N N     . GLN D 4 23  ? 39.762  -20.761 -27.678 1.00 47.76  ? 70  GLN D N     1 
ATOM   3136 C CA    . GLN D 4 23  ? 38.389  -20.741 -27.197 1.00 51.81  ? 70  GLN D CA    1 
ATOM   3137 C C     . GLN D 4 23  ? 38.246  -19.867 -25.957 1.00 51.15  ? 70  GLN D C     1 
ATOM   3138 O O     . GLN D 4 23  ? 39.217  -19.583 -25.261 1.00 46.62  ? 70  GLN D O     1 
ATOM   3139 C CB    . GLN D 4 23  ? 37.918  -22.157 -26.858 1.00 52.78  ? 70  GLN D CB    1 
ATOM   3140 C CG    . GLN D 4 23  ? 37.873  -23.108 -28.037 1.00 56.28  ? 70  GLN D CG    1 
ATOM   3141 C CD    . GLN D 4 23  ? 37.507  -24.506 -27.609 1.00 57.41  ? 70  GLN D CD    1 
ATOM   3142 O OE1   . GLN D 4 23  ? 36.533  -24.705 -26.884 1.00 63.57  ? 70  GLN D OE1   1 
ATOM   3143 N NE2   . GLN D 4 23  ? 38.298  -25.483 -28.031 1.00 56.59  ? 70  GLN D NE2   1 
ATOM   3144 N N     . GLY D 4 24  ? 37.007  -19.462 -25.664 1.00 49.69  ? 71  GLY D N     1 
ATOM   3145 C CA    . GLY D 4 24  ? 36.671  -18.822 -24.405 1.00 38.44  ? 71  GLY D CA    1 
ATOM   3146 C C     . GLY D 4 24  ? 36.401  -17.330 -24.471 1.00 42.16  ? 71  GLY D C     1 
ATOM   3147 O O     . GLY D 4 24  ? 35.839  -16.788 -23.512 1.00 42.88  ? 71  GLY D O     1 
ATOM   3148 N N     . VAL D 4 25  ? 36.754  -16.649 -25.559 1.00 39.82  ? 72  VAL D N     1 
ATOM   3149 C CA    . VAL D 4 25  ? 36.566  -15.200 -25.662 1.00 43.18  ? 72  VAL D CA    1 
ATOM   3150 C C     . VAL D 4 25  ? 35.085  -14.872 -25.852 1.00 44.61  ? 72  VAL D C     1 
ATOM   3151 O O     . VAL D 4 25  ? 34.464  -15.349 -26.813 1.00 45.19  ? 72  VAL D O     1 
ATOM   3152 C CB    . VAL D 4 25  ? 37.415  -14.616 -26.804 1.00 44.68  ? 72  VAL D CB    1 
ATOM   3153 C CG1   . VAL D 4 25  ? 38.918  -14.744 -26.481 1.00 43.32  ? 72  VAL D CG1   1 
ATOM   3154 C CG2   . VAL D 4 25  ? 37.118  -15.343 -28.108 1.00 47.12  ? 72  VAL D CG2   1 
ATOM   3155 N N     . PRO D 4 26  ? 34.474  -14.075 -24.975 1.00 43.28  ? 73  PRO D N     1 
ATOM   3156 C CA    . PRO D 4 26  ? 33.037  -13.799 -25.111 1.00 41.89  ? 73  PRO D CA    1 
ATOM   3157 C C     . PRO D 4 26  ? 32.732  -13.022 -26.380 1.00 44.01  ? 73  PRO D C     1 
ATOM   3158 O O     . PRO D 4 26  ? 33.578  -12.291 -26.905 1.00 42.22  ? 73  PRO D O     1 
ATOM   3159 C CB    . PRO D 4 26  ? 32.716  -12.976 -23.862 1.00 40.32  ? 73  PRO D CB    1 
ATOM   3160 C CG    . PRO D 4 26  ? 33.782  -13.359 -22.889 1.00 39.66  ? 73  PRO D CG    1 
ATOM   3161 C CD    . PRO D 4 26  ? 35.016  -13.521 -23.728 1.00 40.06  ? 73  PRO D CD    1 
ATOM   3162 N N     . ILE D 4 27  ? 31.516  -13.219 -26.892 1.00 41.60  ? 74  ILE D N     1 
ATOM   3163 C CA    . ILE D 4 27  ? 31.109  -12.592 -28.148 1.00 43.04  ? 74  ILE D CA    1 
ATOM   3164 C C     . ILE D 4 27  ? 30.717  -11.144 -27.890 1.00 40.04  ? 74  ILE D C     1 
ATOM   3165 O O     . ILE D 4 27  ? 29.928  -10.841 -26.987 1.00 42.23  ? 74  ILE D O     1 
ATOM   3166 C CB    . ILE D 4 27  ? 29.962  -13.376 -28.815 1.00 45.99  ? 74  ILE D CB    1 
ATOM   3167 C CG1   . ILE D 4 27  ? 30.511  -14.627 -29.498 1.00 50.07  ? 74  ILE D CG1   1 
ATOM   3168 C CG2   . ILE D 4 27  ? 29.250  -12.515 -29.857 1.00 45.01  ? 74  ILE D CG2   1 
ATOM   3169 C CD1   . ILE D 4 27  ? 29.515  -15.735 -29.635 1.00 53.58  ? 74  ILE D CD1   1 
ATOM   3170 N N     . ASN D 4 28  ? 31.287  -10.239 -28.673 1.00 45.35  ? 75  ASN D N     1 
ATOM   3171 C CA    . ASN D 4 28  ? 30.931  -8.831  -28.618 1.00 42.52  ? 75  ASN D CA    1 
ATOM   3172 C C     . ASN D 4 28  ? 31.015  -8.314  -30.037 1.00 50.57  ? 75  ASN D C     1 
ATOM   3173 O O     . ASN D 4 28  ? 32.097  -8.292  -30.629 1.00 52.64  ? 75  ASN D O     1 
ATOM   3174 C CB    . ASN D 4 28  ? 31.847  -8.043  -27.688 1.00 46.84  ? 75  ASN D CB    1 
ATOM   3175 C CG    . ASN D 4 28  ? 31.498  -6.571  -27.648 1.00 50.84  ? 75  ASN D CG    1 
ATOM   3176 O OD1   . ASN D 4 28  ? 30.525  -6.132  -28.274 1.00 56.50  ? 75  ASN D OD1   1 
ATOM   3177 N ND2   . ASN D 4 28  ? 32.293  -5.795  -26.921 1.00 46.52  ? 75  ASN D ND2   1 
ATOM   3178 N N     . THR D 4 29  ? 29.866  -7.926  -30.582 1.00 57.52  ? 76  THR D N     1 
ATOM   3179 C CA    . THR D 4 29  ? 29.783  -7.502  -31.969 1.00 55.28  ? 76  THR D CA    1 
ATOM   3180 C C     . THR D 4 29  ? 30.323  -6.101  -32.171 1.00 58.07  ? 76  THR D C     1 
ATOM   3181 O O     . THR D 4 29  ? 30.460  -5.668  -33.319 1.00 61.66  ? 76  THR D O     1 
ATOM   3182 C CB    . THR D 4 29  ? 28.335  -7.591  -32.464 1.00 60.78  ? 76  THR D CB    1 
ATOM   3183 O OG1   . THR D 4 29  ? 27.476  -6.842  -31.589 1.00 57.58  ? 76  THR D OG1   1 
ATOM   3184 C CG2   . THR D 4 29  ? 27.881  -9.054  -32.512 1.00 52.65  ? 76  THR D CG2   1 
ATOM   3185 N N     . ASN D 4 30  ? 30.643  -5.392  -31.088 1.00 60.05  ? 77  ASN D N     1 
ATOM   3186 C CA    . ASN D 4 30  ? 31.370  -4.132  -31.179 1.00 60.70  ? 77  ASN D CA    1 
ATOM   3187 C C     . ASN D 4 30  ? 32.872  -4.318  -31.032 1.00 61.44  ? 77  ASN D C     1 
ATOM   3188 O O     . ASN D 4 30  ? 33.555  -3.426  -30.512 1.00 62.52  ? 77  ASN D O     1 
ATOM   3189 C CB    . ASN D 4 30  ? 30.850  -3.145  -30.136 1.00 58.49  ? 77  ASN D CB    1 
ATOM   3190 C CG    . ASN D 4 30  ? 29.767  -2.246  -30.690 1.00 66.02  ? 77  ASN D CG    1 
ATOM   3191 O OD1   . ASN D 4 30  ? 29.771  -1.910  -31.884 1.00 65.38  ? 77  ASN D OD1   1 
ATOM   3192 N ND2   . ASN D 4 30  ? 28.827  -1.852  -29.831 1.00 59.46  ? 77  ASN D ND2   1 
ATOM   3193 N N     . SER D 4 31  ? 33.406  -5.458  -31.467 1.00 56.07  ? 78  SER D N     1 
ATOM   3194 C CA    . SER D 4 31  ? 34.827  -5.733  -31.340 1.00 55.86  ? 78  SER D CA    1 
ATOM   3195 C C     . SER D 4 31  ? 35.326  -6.450  -32.588 1.00 55.49  ? 78  SER D C     1 
ATOM   3196 O O     . SER D 4 31  ? 34.642  -7.317  -33.137 1.00 62.42  ? 78  SER D O     1 
ATOM   3197 C CB    . SER D 4 31  ? 35.121  -6.556  -30.064 1.00 52.46  ? 78  SER D CB    1 
ATOM   3198 O OG    . SER D 4 31  ? 34.638  -7.889  -30.119 1.00 46.75  ? 78  SER D OG    1 
ATOM   3199 N N     . SER D 4 32  ? 36.517  -6.071  -33.028 1.00 52.96  ? 79  SER D N     1 
ATOM   3200 C CA    . SER D 4 32  ? 37.197  -6.656  -34.174 1.00 56.95  ? 79  SER D CA    1 
ATOM   3201 C C     . SER D 4 32  ? 37.770  -8.038  -33.847 1.00 56.07  ? 79  SER D C     1 
ATOM   3202 O O     . SER D 4 32  ? 37.871  -8.426  -32.678 1.00 50.59  ? 79  SER D O     1 
ATOM   3203 C CB    . SER D 4 32  ? 38.318  -5.727  -34.632 1.00 59.34  ? 79  SER D CB    1 
ATOM   3204 O OG    . SER D 4 32  ? 37.796  -4.477  -35.048 1.00 64.42  ? 79  SER D OG    1 
ATOM   3205 N N     . PRO D 4 33  ? 38.121  -8.823  -34.872 1.00 55.63  ? 80  PRO D N     1 
ATOM   3206 C CA    . PRO D 4 33  ? 38.814  -10.092 -34.599 1.00 54.74  ? 80  PRO D CA    1 
ATOM   3207 C C     . PRO D 4 33  ? 40.145  -9.904  -33.891 1.00 50.35  ? 80  PRO D C     1 
ATOM   3208 O O     . PRO D 4 33  ? 40.517  -10.753 -33.072 1.00 49.85  ? 80  PRO D O     1 
ATOM   3209 C CB    . PRO D 4 33  ? 38.990  -10.708 -35.997 1.00 53.75  ? 80  PRO D CB    1 
ATOM   3210 C CG    . PRO D 4 33  ? 38.854  -9.558  -36.948 1.00 58.79  ? 80  PRO D CG    1 
ATOM   3211 C CD    . PRO D 4 33  ? 37.859  -8.636  -36.311 1.00 56.15  ? 80  PRO D CD    1 
ATOM   3212 N N     . ASP D 4 34  ? 40.862  -8.809  -34.175 1.00 50.90  ? 81  ASP D N     1 
ATOM   3213 C CA    . ASP D 4 34  ? 42.105  -8.510  -33.464 1.00 49.35  ? 81  ASP D CA    1 
ATOM   3214 C C     . ASP D 4 34  ? 41.880  -8.352  -31.970 1.00 48.00  ? 81  ASP D C     1 
ATOM   3215 O O     . ASP D 4 34  ? 42.790  -8.607  -31.177 1.00 43.88  ? 81  ASP D O     1 
ATOM   3216 C CB    . ASP D 4 34  ? 42.733  -7.227  -33.998 1.00 50.19  ? 81  ASP D CB    1 
ATOM   3217 C CG    . ASP D 4 34  ? 42.591  -7.086  -35.488 1.00 57.77  ? 81  ASP D CG    1 
ATOM   3218 O OD1   . ASP D 4 34  ? 41.434  -6.924  -35.963 1.00 66.42  ? 81  ASP D OD1   1 
ATOM   3219 O OD2   . ASP D 4 34  ? 43.630  -7.122  -36.180 1.00 53.60  ? 81  ASP D OD2   1 
ATOM   3220 N N     . ASP D 4 35  ? 40.684  -7.939  -31.566 1.00 42.56  ? 82  ASP D N     1 
ATOM   3221 C CA    . ASP D 4 35  ? 40.405  -7.661  -30.169 1.00 39.46  ? 82  ASP D CA    1 
ATOM   3222 C C     . ASP D 4 35  ? 40.183  -8.911  -29.340 1.00 41.82  ? 82  ASP D C     1 
ATOM   3223 O O     . ASP D 4 35  ? 40.026  -8.795  -28.121 1.00 46.04  ? 82  ASP D O     1 
ATOM   3224 C CB    . ASP D 4 35  ? 39.171  -6.767  -30.044 1.00 44.85  ? 82  ASP D CB    1 
ATOM   3225 C CG    . ASP D 4 35  ? 39.378  -5.391  -30.641 1.00 51.97  ? 82  ASP D CG    1 
ATOM   3226 O OD1   . ASP D 4 35  ? 40.549  -4.970  -30.790 1.00 50.19  ? 82  ASP D OD1   1 
ATOM   3227 O OD2   . ASP D 4 35  ? 38.366  -4.718  -30.941 1.00 54.55  ? 82  ASP D OD2   1 
ATOM   3228 N N     . GLN D 4 36  ? 40.167  -10.096 -29.951 1.00 41.96  ? 83  GLN D N     1 
ATOM   3229 C CA    . GLN D 4 36  ? 39.621  -11.282 -29.294 1.00 40.86  ? 83  GLN D CA    1 
ATOM   3230 C C     . GLN D 4 36  ? 40.686  -11.942 -28.418 1.00 39.83  ? 83  GLN D C     1 
ATOM   3231 O O     . GLN D 4 36  ? 41.167  -13.041 -28.687 1.00 41.26  ? 83  GLN D O     1 
ATOM   3232 C CB    . GLN D 4 36  ? 39.069  -12.248 -30.332 1.00 42.10  ? 83  GLN D CB    1 
ATOM   3233 C CG    . GLN D 4 36  ? 38.029  -11.634 -31.220 1.00 39.80  ? 83  GLN D CG    1 
ATOM   3234 C CD    . GLN D 4 36  ? 36.967  -10.931 -30.423 1.00 45.03  ? 83  GLN D CD    1 
ATOM   3235 O OE1   . GLN D 4 36  ? 36.280  -11.546 -29.598 1.00 43.91  ? 83  GLN D OE1   1 
ATOM   3236 N NE2   . GLN D 4 36  ? 36.823  -9.626  -30.653 1.00 44.61  ? 83  GLN D NE2   1 
ATOM   3237 N N     . ILE D 4 37  ? 41.017  -11.268 -27.320 1.00 36.11  ? 84  ILE D N     1 
ATOM   3238 C CA    . ILE D 4 37  ? 42.057  -11.771 -26.429 1.00 35.99  ? 84  ILE D CA    1 
ATOM   3239 C C     . ILE D 4 37  ? 41.957  -11.055 -25.088 1.00 32.52  ? 84  ILE D C     1 
ATOM   3240 O O     . ILE D 4 37  ? 41.797  -9.832  -25.017 1.00 31.34  ? 84  ILE D O     1 
ATOM   3241 C CB    . ILE D 4 37  ? 43.438  -11.600 -27.099 1.00 35.42  ? 84  ILE D CB    1 
ATOM   3242 C CG1   . ILE D 4 37  ? 44.591  -11.964 -26.155 1.00 37.04  ? 84  ILE D CG1   1 
ATOM   3243 C CG2   . ILE D 4 37  ? 43.555  -10.201 -27.633 1.00 34.79  ? 84  ILE D CG2   1 
ATOM   3244 C CD1   . ILE D 4 37  ? 45.941  -12.083 -26.896 1.00 36.88  ? 84  ILE D CD1   1 
ATOM   3245 N N     . GLY D 4 38  ? 42.087  -11.823 -24.017 1.00 30.88  ? 85  GLY D N     1 
ATOM   3246 C CA    . GLY D 4 38  ? 41.975  -11.254 -22.697 1.00 28.43  ? 85  GLY D CA    1 
ATOM   3247 C C     . GLY D 4 38  ? 42.098  -12.344 -21.671 1.00 29.46  ? 85  GLY D C     1 
ATOM   3248 O O     . GLY D 4 38  ? 42.628  -13.417 -21.955 1.00 32.17  ? 85  GLY D O     1 
ATOM   3249 N N     . TYR D 4 39  ? 41.583  -12.068 -20.478 1.00 25.67  ? 86  TYR D N     1 
ATOM   3250 C CA    . TYR D 4 39  ? 41.658  -12.992 -19.363 1.00 30.65  ? 86  TYR D CA    1 
ATOM   3251 C C     . TYR D 4 39  ? 40.331  -13.031 -18.614 1.00 34.58  ? 86  TYR D C     1 
ATOM   3252 O O     . TYR D 4 39  ? 39.498  -12.139 -18.757 1.00 35.03  ? 86  TYR D O     1 
ATOM   3253 C CB    . TYR D 4 39  ? 42.780  -12.595 -18.394 1.00 32.84  ? 86  TYR D CB    1 
ATOM   3254 C CG    . TYR D 4 39  ? 42.651  -11.215 -17.813 1.00 25.95  ? 86  TYR D CG    1 
ATOM   3255 C CD1   . TYR D 4 39  ? 43.032  -10.093 -18.540 1.00 24.83  ? 86  TYR D CD1   1 
ATOM   3256 C CD2   . TYR D 4 39  ? 42.160  -11.031 -16.521 1.00 29.69  ? 86  TYR D CD2   1 
ATOM   3257 C CE1   . TYR D 4 39  ? 42.933  -8.813  -17.984 1.00 30.86  ? 86  TYR D CE1   1 
ATOM   3258 C CE2   . TYR D 4 39  ? 42.043  -9.750  -15.959 1.00 26.43  ? 86  TYR D CE2   1 
ATOM   3259 C CZ    . TYR D 4 39  ? 42.421  -8.654  -16.694 1.00 28.65  ? 86  TYR D CZ    1 
ATOM   3260 O OH    . TYR D 4 39  ? 42.300  -7.400  -16.142 1.00 29.95  ? 86  TYR D OH    1 
ATOM   3261 N N     . TYR D 4 40  ? 40.158  -14.077 -17.800 1.00 31.45  ? 87  TYR D N     1 
ATOM   3262 C CA    . TYR D 4 40  ? 39.116  -14.163 -16.790 1.00 34.33  ? 87  TYR D CA    1 
ATOM   3263 C C     . TYR D 4 40  ? 39.748  -14.064 -15.416 1.00 36.38  ? 87  TYR D C     1 
ATOM   3264 O O     . TYR D 4 40  ? 40.728  -14.760 -15.123 1.00 38.46  ? 87  TYR D O     1 
ATOM   3265 C CB    . TYR D 4 40  ? 38.337  -15.486 -16.852 1.00 30.97  ? 87  TYR D CB    1 
ATOM   3266 C CG    . TYR D 4 40  ? 37.391  -15.655 -18.009 1.00 34.07  ? 87  TYR D CG    1 
ATOM   3267 C CD1   . TYR D 4 40  ? 37.820  -16.197 -19.207 1.00 36.51  ? 87  TYR D CD1   1 
ATOM   3268 C CD2   . TYR D 4 40  ? 36.032  -15.344 -17.878 1.00 39.93  ? 87  TYR D CD2   1 
ATOM   3269 C CE1   . TYR D 4 40  ? 36.942  -16.382 -20.263 1.00 36.87  ? 87  TYR D CE1   1 
ATOM   3270 C CE2   . TYR D 4 40  ? 35.149  -15.523 -18.928 1.00 30.44  ? 87  TYR D CE2   1 
ATOM   3271 C CZ    . TYR D 4 40  ? 35.612  -16.045 -20.111 1.00 39.68  ? 87  TYR D CZ    1 
ATOM   3272 O OH    . TYR D 4 40  ? 34.752  -16.230 -21.165 1.00 44.24  ? 87  TYR D OH    1 
ATOM   3273 N N     . ARG D 4 41  ? 39.145  -13.262 -14.554 1.00 34.97  ? 88  ARG D N     1 
ATOM   3274 C CA    . ARG D 4 41  ? 39.593  -13.099 -13.184 1.00 33.48  ? 88  ARG D CA    1 
ATOM   3275 C C     . ARG D 4 41  ? 38.585  -13.693 -12.207 1.00 42.98  ? 88  ARG D C     1 
ATOM   3276 O O     . ARG D 4 41  ? 37.420  -13.275 -12.172 1.00 43.77  ? 88  ARG D O     1 
ATOM   3277 C CB    . ARG D 4 41  ? 39.814  -11.628 -12.870 1.00 34.26  ? 88  ARG D CB    1 
ATOM   3278 C CG    . ARG D 4 41  ? 40.173  -11.377 -11.438 1.00 39.67  ? 88  ARG D CG    1 
ATOM   3279 C CD    . ARG D 4 41  ? 40.998  -10.110 -11.373 1.00 45.70  ? 88  ARG D CD    1 
ATOM   3280 N NE    . ARG D 4 41  ? 41.299  -9.686  -10.014 1.00 44.77  ? 88  ARG D NE    1 
ATOM   3281 C CZ    . ARG D 4 41  ? 40.520  -8.878  -9.311  1.00 48.46  ? 88  ARG D CZ    1 
ATOM   3282 N NH1   . ARG D 4 41  ? 39.352  -8.466  -9.787  1.00 46.65  ? 88  ARG D NH1   1 
ATOM   3283 N NH2   . ARG D 4 41  ? 40.927  -8.462  -8.112  1.00 39.02  ? 88  ARG D NH2   1 
ATOM   3284 N N     . ARG D 4 42  ? 39.049  -14.643 -11.399 1.00 42.01  ? 89  ARG D N     1 
ATOM   3285 C CA    . ARG D 4 42  ? 38.240  -15.197 -10.329 1.00 43.23  ? 89  ARG D CA    1 
ATOM   3286 C C     . ARG D 4 42  ? 37.936  -14.119 -9.302  1.00 44.01  ? 89  ARG D C     1 
ATOM   3287 O O     . ARG D 4 42  ? 38.777  -13.268 -9.016  1.00 39.27  ? 89  ARG D O     1 
ATOM   3288 C CB    . ARG D 4 42  ? 38.980  -16.358 -9.665  1.00 45.66  ? 89  ARG D CB    1 
ATOM   3289 C CG    . ARG D 4 42  ? 38.086  -17.322 -8.909  1.00 46.91  ? 89  ARG D CG    1 
ATOM   3290 C CD    . ARG D 4 42  ? 38.638  -17.652 -7.547  1.00 42.24  ? 89  ARG D CD    1 
ATOM   3291 N NE    . ARG D 4 42  ? 40.048  -18.007 -7.597  1.00 48.41  ? 89  ARG D NE    1 
ATOM   3292 C CZ    . ARG D 4 42  ? 40.508  -19.208 -7.918  1.00 51.63  ? 89  ARG D CZ    1 
ATOM   3293 N NH1   . ARG D 4 42  ? 39.688  -20.197 -8.248  1.00 58.08  ? 89  ARG D NH1   1 
ATOM   3294 N NH2   . ARG D 4 42  ? 41.823  -19.420 -7.911  1.00 50.75  ? 89  ARG D NH2   1 
ATOM   3295 N N     . ALA D 4 43  ? 36.719  -14.160 -8.753  1.00 41.71  ? 90  ALA D N     1 
ATOM   3296 C CA    . ALA D 4 43  ? 36.275  -13.253 -7.691  1.00 47.33  ? 90  ALA D CA    1 
ATOM   3297 C C     . ALA D 4 43  ? 35.402  -14.045 -6.728  1.00 46.49  ? 90  ALA D C     1 
ATOM   3298 O O     . ALA D 4 43  ? 34.297  -14.454 -7.092  1.00 49.73  ? 90  ALA D O     1 
ATOM   3299 C CB    . ALA D 4 43  ? 35.500  -12.060 -8.254  1.00 43.12  ? 90  ALA D CB    1 
ATOM   3300 N N     . THR D 4 44  ? 35.891  -14.267 -5.515  1.00 50.56  ? 91  THR D N     1 
ATOM   3301 C CA    . THR D 4 44  ? 35.185  -15.042 -4.506  1.00 51.46  ? 91  THR D CA    1 
ATOM   3302 C C     . THR D 4 44  ? 34.444  -14.122 -3.554  1.00 56.40  ? 91  THR D C     1 
ATOM   3303 O O     . THR D 4 44  ? 34.876  -13.001 -3.268  1.00 61.08  ? 91  THR D O     1 
ATOM   3304 C CB    . THR D 4 44  ? 36.130  -15.903 -3.675  1.00 56.01  ? 91  THR D CB    1 
ATOM   3305 O OG1   . THR D 4 44  ? 36.906  -15.045 -2.824  1.00 59.86  ? 91  THR D OG1   1 
ATOM   3306 C CG2   . THR D 4 44  ? 37.036  -16.736 -4.571  1.00 47.13  ? 91  THR D CG2   1 
ATOM   3307 N N     . ARG D 4 45  ? 33.342  -14.635 -3.027  1.00 51.96  ? 92  ARG D N     1 
ATOM   3308 C CA    . ARG D 4 45  ? 32.468  -13.860 -2.179  1.00 49.61  ? 92  ARG D CA    1 
ATOM   3309 C C     . ARG D 4 45  ? 32.019  -14.717 -1.011  1.00 51.08  ? 92  ARG D C     1 
ATOM   3310 O O     . ARG D 4 45  ? 31.874  -15.933 -1.138  1.00 50.38  ? 92  ARG D O     1 
ATOM   3311 C CB    . ARG D 4 45  ? 31.281  -13.372 -2.996  1.00 59.47  ? 92  ARG D CB    1 
ATOM   3312 C CG    . ARG D 4 45  ? 31.141  -14.117 -4.320  1.00 61.14  ? 92  ARG D CG    1 
ATOM   3313 C CD    . ARG D 4 45  ? 30.235  -13.375 -5.296  1.00 52.10  ? 92  ARG D CD    1 
ATOM   3314 N NE    . ARG D 4 45  ? 29.091  -14.190 -5.672  1.00 62.09  ? 92  ARG D NE    1 
ATOM   3315 C CZ    . ARG D 4 45  ? 28.131  -13.797 -6.497  1.00 65.92  ? 92  ARG D CZ    1 
ATOM   3316 N NH1   . ARG D 4 45  ? 28.154  -12.600 -7.070  1.00 62.65  ? 92  ARG D NH1   1 
ATOM   3317 N NH2   . ARG D 4 45  ? 27.128  -14.629 -6.765  1.00 66.44  ? 92  ARG D NH2   1 
ATOM   3318 N N     . ARG D 4 46  ? 31.795  -14.076 0.128   1.00 45.56  ? 93  ARG D N     1 
ATOM   3319 C CA    . ARG D 4 46  ? 31.293  -14.762 1.306   1.00 53.61  ? 93  ARG D CA    1 
ATOM   3320 C C     . ARG D 4 46  ? 30.145  -13.955 1.880   1.00 55.11  ? 93  ARG D C     1 
ATOM   3321 O O     . ARG D 4 46  ? 30.172  -12.726 1.829   1.00 59.64  ? 93  ARG D O     1 
ATOM   3322 C CB    . ARG D 4 46  ? 32.389  -14.948 2.356   1.00 57.05  ? 93  ARG D CB    1 
ATOM   3323 C CG    . ARG D 4 46  ? 33.773  -15.141 1.757   1.00 52.41  ? 93  ARG D CG    1 
ATOM   3324 C CD    . ARG D 4 46  ? 34.762  -15.686 2.783   1.00 68.69  ? 93  ARG D CD    1 
ATOM   3325 N NE    . ARG D 4 46  ? 34.988  -14.782 3.907   1.00 66.77  ? 93  ARG D NE    1 
ATOM   3326 C CZ    . ARG D 4 46  ? 35.608  -15.121 5.029   1.00 59.98  ? 93  ARG D CZ    1 
ATOM   3327 N NH1   . ARG D 4 46  ? 36.077  -16.343 5.222   1.00 60.55  ? 93  ARG D NH1   1 
ATOM   3328 N NH2   . ARG D 4 46  ? 35.760  -14.210 5.983   1.00 61.94  ? 93  ARG D NH2   1 
ATOM   3329 N N     . ILE D 4 47  ? 29.126  -14.645 2.398   1.00 55.55  ? 94  ILE D N     1 
ATOM   3330 C CA    . ILE D 4 47  ? 28.002  -14.024 3.094   1.00 58.55  ? 94  ILE D CA    1 
ATOM   3331 C C     . ILE D 4 47  ? 27.832  -14.708 4.448   1.00 65.53  ? 94  ILE D C     1 
ATOM   3332 O O     . ILE D 4 47  ? 28.516  -15.681 4.763   1.00 62.93  ? 94  ILE D O     1 
ATOM   3333 C CB    . ILE D 4 47  ? 26.679  -14.092 2.294   1.00 50.24  ? 94  ILE D CB    1 
ATOM   3334 C CG1   . ILE D 4 47  ? 26.213  -15.530 2.128   1.00 53.40  ? 94  ILE D CG1   1 
ATOM   3335 C CG2   . ILE D 4 47  ? 26.792  -13.415 0.947   1.00 54.37  ? 94  ILE D CG2   1 
ATOM   3336 C CD1   . ILE D 4 47  ? 24.887  -15.627 1.437   1.00 54.01  ? 94  ILE D CD1   1 
ATOM   3337 N N     . ARG D 4 48  ? 26.895  -14.190 5.246   1.00 67.02  ? 95  ARG D N     1 
ATOM   3338 C CA    . ARG D 4 48  ? 26.492  -14.854 6.480   1.00 65.84  ? 95  ARG D CA    1 
ATOM   3339 C C     . ARG D 4 48  ? 25.459  -15.907 6.121   1.00 69.01  ? 95  ARG D C     1 
ATOM   3340 O O     . ARG D 4 48  ? 24.352  -15.574 5.687   1.00 68.85  ? 95  ARG D O     1 
ATOM   3341 C CB    . ARG D 4 48  ? 25.944  -13.856 7.496   1.00 64.59  ? 95  ARG D CB    1 
ATOM   3342 C CG    . ARG D 4 48  ? 27.018  -13.263 8.390   1.00 65.10  ? 95  ARG D CG    1 
ATOM   3343 C CD    . ARG D 4 48  ? 26.460  -12.265 9.391   1.00 67.06  ? 95  ARG D CD    1 
ATOM   3344 N NE    . ARG D 4 48  ? 25.969  -12.901 10.606  1.00 67.02  ? 95  ARG D NE    1 
ATOM   3345 C CZ    . ARG D 4 48  ? 24.704  -13.243 10.811  1.00 69.34  ? 95  ARG D CZ    1 
ATOM   3346 N NH1   . ARG D 4 48  ? 23.778  -13.054 9.884   1.00 66.76  ? 95  ARG D NH1   1 
ATOM   3347 N NH2   . ARG D 4 48  ? 24.359  -13.789 11.976  1.00 67.93  ? 95  ARG D NH2   1 
ATOM   3348 N N     . GLY D 4 49  ? 25.822  -17.176 6.308   1.00 72.93  ? 96  GLY D N     1 
ATOM   3349 C CA    . GLY D 4 49  ? 25.059  -18.288 5.776   1.00 74.81  ? 96  GLY D CA    1 
ATOM   3350 C C     . GLY D 4 49  ? 23.992  -18.858 6.686   1.00 80.19  ? 96  GLY D C     1 
ATOM   3351 O O     . GLY D 4 49  ? 23.956  -20.073 6.912   1.00 77.29  ? 96  GLY D O     1 
ATOM   3352 N N     . GLY D 4 50  ? 23.119  -17.994 7.212   1.00 85.91  ? 97  GLY D N     1 
ATOM   3353 C CA    . GLY D 4 50  ? 21.948  -18.431 7.953   1.00 87.67  ? 97  GLY D CA    1 
ATOM   3354 C C     . GLY D 4 50  ? 22.297  -18.980 9.318   1.00 88.68  ? 97  GLY D C     1 
ATOM   3355 O O     . GLY D 4 50  ? 21.810  -18.492 10.344  1.00 88.64  ? 97  GLY D O     1 
ATOM   3356 N N     . ASP D 4 51  ? 23.159  -20.000 9.337   1.00 88.01  ? 98  ASP D N     1 
ATOM   3357 C CA    . ASP D 4 51  ? 23.723  -20.505 10.580  1.00 84.04  ? 98  ASP D CA    1 
ATOM   3358 C C     . ASP D 4 51  ? 24.512  -19.440 11.322  1.00 84.50  ? 98  ASP D C     1 
ATOM   3359 O O     . ASP D 4 51  ? 24.979  -19.696 12.436  1.00 83.09  ? 98  ASP D O     1 
ATOM   3360 C CB    . ASP D 4 51  ? 24.630  -21.705 10.297  1.00 89.15  ? 98  ASP D CB    1 
ATOM   3361 C CG    . ASP D 4 51  ? 23.911  -22.827 9.561   1.00 98.16  ? 98  ASP D CG    1 
ATOM   3362 O OD1   . ASP D 4 51  ? 22.686  -23.001 9.777   1.00 95.61  ? 98  ASP D OD1   1 
ATOM   3363 O OD2   . ASP D 4 51  ? 24.578  -23.537 8.772   1.00 100.34 ? 98  ASP D OD2   1 
ATOM   3364 N N     . GLY D 4 52  ? 24.677  -18.261 10.730  1.00 84.16  ? 99  GLY D N     1 
ATOM   3365 C CA    . GLY D 4 52  ? 25.443  -17.200 11.327  1.00 76.90  ? 99  GLY D CA    1 
ATOM   3366 C C     . GLY D 4 52  ? 26.915  -17.235 11.012  1.00 73.38  ? 99  GLY D C     1 
ATOM   3367 O O     . GLY D 4 52  ? 27.631  -16.306 11.400  1.00 80.30  ? 99  GLY D O     1 
ATOM   3368 N N     . LYS D 4 53  ? 27.395  -18.267 10.324  1.00 75.51  ? 100 LYS D N     1 
ATOM   3369 C CA    . LYS D 4 53  ? 28.808  -18.383 9.993   1.00 75.58  ? 100 LYS D CA    1 
ATOM   3370 C C     . LYS D 4 53  ? 29.045  -17.943 8.550   1.00 72.02  ? 100 LYS D C     1 
ATOM   3371 O O     . LYS D 4 53  ? 28.160  -18.048 7.696   1.00 70.47  ? 100 LYS D O     1 
ATOM   3372 C CB    . LYS D 4 53  ? 29.306  -19.820 10.202  1.00 73.17  ? 100 LYS D CB    1 
ATOM   3373 C CG    . LYS D 4 53  ? 30.785  -19.947 10.630  1.00 72.40  ? 100 LYS D CG    1 
ATOM   3374 C CD    . LYS D 4 53  ? 31.801  -19.918 9.466   1.00 68.02  ? 100 LYS D CD    1 
ATOM   3375 C CE    . LYS D 4 53  ? 32.827  -18.787 9.650   1.00 66.93  ? 100 LYS D CE    1 
ATOM   3376 N NZ    . LYS D 4 53  ? 33.969  -18.785 8.670   1.00 69.88  ? 100 LYS D NZ    1 
ATOM   3377 N N     . MET D 4 54  ? 30.248  -17.427 8.294   1.00 69.54  ? 101 MET D N     1 
ATOM   3378 C CA    . MET D 4 54  ? 30.619  -17.032 6.943   1.00 64.85  ? 101 MET D CA    1 
ATOM   3379 C C     . MET D 4 54  ? 30.585  -18.233 6.014   1.00 67.50  ? 101 MET D C     1 
ATOM   3380 O O     . MET D 4 54  ? 31.157  -19.287 6.307   1.00 65.78  ? 101 MET D O     1 
ATOM   3381 C CB    . MET D 4 54  ? 32.003  -16.387 6.920   1.00 61.87  ? 101 MET D CB    1 
ATOM   3382 C CG    . MET D 4 54  ? 32.045  -15.043 7.601   1.00 58.53  ? 101 MET D CG    1 
ATOM   3383 S SD    . MET D 4 54  ? 30.657  -14.003 7.129   1.00 61.30  ? 101 MET D SD    1 
ATOM   3384 C CE    . MET D 4 54  ? 31.147  -13.519 5.474   1.00 60.95  ? 101 MET D CE    1 
ATOM   3385 N N     . LYS D 4 55  ? 29.916  -18.052 4.882   1.00 69.67  ? 102 LYS D N     1 
ATOM   3386 C CA    . LYS D 4 55  ? 29.672  -19.090 3.898   1.00 64.59  ? 102 LYS D CA    1 
ATOM   3387 C C     . LYS D 4 55  ? 30.292  -18.649 2.584   1.00 58.92  ? 102 LYS D C     1 
ATOM   3388 O O     . LYS D 4 55  ? 30.081  -17.515 2.146   1.00 61.26  ? 102 LYS D O     1 
ATOM   3389 C CB    . LYS D 4 55  ? 28.159  -19.326 3.757   1.00 65.01  ? 102 LYS D CB    1 
ATOM   3390 C CG    . LYS D 4 55  ? 27.678  -19.874 2.425   1.00 63.95  ? 102 LYS D CG    1 
ATOM   3391 C CD    . LYS D 4 55  ? 26.152  -19.933 2.409   1.00 65.21  ? 102 LYS D CD    1 
ATOM   3392 C CE    . LYS D 4 55  ? 25.608  -20.735 1.228   1.00 67.15  ? 102 LYS D CE    1 
ATOM   3393 N NZ    . LYS D 4 55  ? 24.173  -21.095 1.429   1.00 57.98  ? 102 LYS D NZ    1 
ATOM   3394 N N     . ASP D 4 56  ? 31.081  -19.525 1.976   1.00 57.28  ? 103 ASP D N     1 
ATOM   3395 C CA    . ASP D 4 56  ? 31.608  -19.238 0.648   1.00 62.13  ? 103 ASP D CA    1 
ATOM   3396 C C     . ASP D 4 56  ? 30.504  -19.399 -0.391  1.00 60.27  ? 103 ASP D C     1 
ATOM   3397 O O     . ASP D 4 56  ? 29.765  -20.390 -0.384  1.00 59.33  ? 103 ASP D O     1 
ATOM   3398 C CB    . ASP D 4 56  ? 32.777  -20.168 0.314   1.00 56.07  ? 103 ASP D CB    1 
ATOM   3399 C CG    . ASP D 4 56  ? 33.881  -20.132 1.364   1.00 68.65  ? 103 ASP D CG    1 
ATOM   3400 O OD1   . ASP D 4 56  ? 34.461  -19.047 1.591   1.00 69.50  ? 103 ASP D OD1   1 
ATOM   3401 O OD2   . ASP D 4 56  ? 34.168  -21.194 1.964   1.00 73.90  ? 103 ASP D OD2   1 
ATOM   3402 N N     . LEU D 4 57  ? 30.382  -18.425 -1.277  1.00 51.93  ? 104 LEU D N     1 
ATOM   3403 C CA    . LEU D 4 57  ? 29.565  -18.629 -2.457  1.00 50.19  ? 104 LEU D CA    1 
ATOM   3404 C C     . LEU D 4 57  ? 30.429  -19.226 -3.555  1.00 51.79  ? 104 LEU D C     1 
ATOM   3405 O O     . LEU D 4 57  ? 31.652  -19.288 -3.456  1.00 45.76  ? 104 LEU D O     1 
ATOM   3406 C CB    . LEU D 4 57  ? 28.935  -17.319 -2.927  1.00 53.97  ? 104 LEU D CB    1 
ATOM   3407 C CG    . LEU D 4 57  ? 28.237  -16.481 -1.862  1.00 52.22  ? 104 LEU D CG    1 
ATOM   3408 C CD1   . LEU D 4 57  ? 27.641  -15.222 -2.482  1.00 47.57  ? 104 LEU D CD1   1 
ATOM   3409 C CD2   . LEU D 4 57  ? 27.190  -17.319 -1.146  1.00 51.02  ? 104 LEU D CD2   1 
ATOM   3410 N N     . SER D 4 58  ? 29.784  -19.675 -4.607  1.00 53.19  ? 105 SER D N     1 
ATOM   3411 C CA    . SER D 4 58  ? 30.541  -20.166 -5.738  1.00 54.13  ? 105 SER D CA    1 
ATOM   3412 C C     . SER D 4 58  ? 31.324  -19.007 -6.350  1.00 55.99  ? 105 SER D C     1 
ATOM   3413 O O     . SER D 4 58  ? 30.770  -17.904 -6.519  1.00 50.24  ? 105 SER D O     1 
ATOM   3414 C CB    . SER D 4 58  ? 29.616  -20.825 -6.767  1.00 53.84  ? 105 SER D CB    1 
ATOM   3415 O OG    . SER D 4 58  ? 28.361  -20.175 -6.818  1.00 60.25  ? 105 SER D OG    1 
ATOM   3416 N N     . PRO D 4 59  ? 32.610  -19.191 -6.654  1.00 53.74  ? 106 PRO D N     1 
ATOM   3417 C CA    . PRO D 4 59  ? 33.381  -18.121 -7.286  1.00 47.80  ? 106 PRO D CA    1 
ATOM   3418 C C     . PRO D 4 59  ? 32.771  -17.726 -8.620  1.00 45.09  ? 106 PRO D C     1 
ATOM   3419 O O     . PRO D 4 59  ? 32.240  -18.564 -9.350  1.00 44.70  ? 106 PRO D O     1 
ATOM   3420 C CB    . PRO D 4 59  ? 34.773  -18.746 -7.476  1.00 49.07  ? 106 PRO D CB    1 
ATOM   3421 C CG    . PRO D 4 59  ? 34.836  -19.856 -6.499  1.00 49.27  ? 106 PRO D CG    1 
ATOM   3422 C CD    . PRO D 4 59  ? 33.433  -20.386 -6.389  1.00 54.34  ? 106 PRO D CD    1 
ATOM   3423 N N     . ARG D 4 60  ? 32.853  -16.435 -8.926  1.00 42.42  ? 107 ARG D N     1 
ATOM   3424 C CA    . ARG D 4 60  ? 32.507  -15.901 -10.235 1.00 44.73  ? 107 ARG D CA    1 
ATOM   3425 C C     . ARG D 4 60  ? 33.770  -15.439 -10.958 1.00 45.47  ? 107 ARG D C     1 
ATOM   3426 O O     . ARG D 4 60  ? 34.662  -14.839 -10.350 1.00 44.20  ? 107 ARG D O     1 
ATOM   3427 C CB    . ARG D 4 60  ? 31.516  -14.738 -10.111 1.00 47.79  ? 107 ARG D CB    1 
ATOM   3428 C CG    . ARG D 4 60  ? 30.074  -15.157 -9.795  1.00 51.35  ? 107 ARG D CG    1 
ATOM   3429 C CD    . ARG D 4 60  ? 29.128  -13.962 -9.815  1.00 57.03  ? 107 ARG D CD    1 
ATOM   3430 N NE    . ARG D 4 60  ? 27.725  -14.369 -9.747  1.00 62.09  ? 107 ARG D NE    1 
ATOM   3431 C CZ    . ARG D 4 60  ? 26.703  -13.595 -10.087 1.00 62.35  ? 107 ARG D CZ    1 
ATOM   3432 N NH1   . ARG D 4 60  ? 26.885  -12.353 -10.510 1.00 67.49  ? 107 ARG D NH1   1 
ATOM   3433 N NH2   . ARG D 4 60  ? 25.467  -14.083 -10.014 1.00 69.22  ? 107 ARG D NH2   1 
ATOM   3434 N N     . TRP D 4 61  ? 33.850  -15.739 -12.247 1.00 39.61  ? 108 TRP D N     1 
ATOM   3435 C CA    . TRP D 4 61  ? 34.954  -15.313 -13.098 1.00 42.26  ? 108 TRP D CA    1 
ATOM   3436 C C     . TRP D 4 61  ? 34.423  -14.266 -14.073 1.00 46.40  ? 108 TRP D C     1 
ATOM   3437 O O     . TRP D 4 61  ? 33.391  -14.489 -14.722 1.00 38.33  ? 108 TRP D O     1 
ATOM   3438 C CB    . TRP D 4 61  ? 35.565  -16.501 -13.865 1.00 38.22  ? 108 TRP D CB    1 
ATOM   3439 C CG    . TRP D 4 61  ? 36.078  -17.630 -12.985 1.00 43.89  ? 108 TRP D CG    1 
ATOM   3440 C CD1   . TRP D 4 61  ? 35.335  -18.447 -12.173 1.00 45.58  ? 108 TRP D CD1   1 
ATOM   3441 C CD2   . TRP D 4 61  ? 37.437  -18.066 -12.844 1.00 44.75  ? 108 TRP D CD2   1 
ATOM   3442 N NE1   . TRP D 4 61  ? 36.151  -19.349 -11.527 1.00 45.82  ? 108 TRP D NE1   1 
ATOM   3443 C CE2   . TRP D 4 61  ? 37.445  -19.135 -11.921 1.00 49.80  ? 108 TRP D CE2   1 
ATOM   3444 C CE3   . TRP D 4 61  ? 38.650  -17.649 -13.395 1.00 45.44  ? 108 TRP D CE3   1 
ATOM   3445 C CZ2   . TRP D 4 61  ? 38.624  -19.792 -11.544 1.00 49.91  ? 108 TRP D CZ2   1 
ATOM   3446 C CZ3   . TRP D 4 61  ? 39.823  -18.316 -13.020 1.00 43.74  ? 108 TRP D CZ3   1 
ATOM   3447 C CH2   . TRP D 4 61  ? 39.796  -19.366 -12.106 1.00 46.04  ? 108 TRP D CH2   1 
ATOM   3448 N N     . TYR D 4 62  ? 35.124  -13.132 -14.173 1.00 43.06  ? 109 TYR D N     1 
ATOM   3449 C CA    . TYR D 4 62  ? 34.766  -12.053 -15.084 1.00 34.72  ? 109 TYR D CA    1 
ATOM   3450 C C     . TYR D 4 62  ? 35.818  -11.906 -16.172 1.00 36.12  ? 109 TYR D C     1 
ATOM   3451 O O     . TYR D 4 62  ? 37.017  -12.080 -15.932 1.00 36.09  ? 109 TYR D O     1 
ATOM   3452 C CB    . TYR D 4 62  ? 34.626  -10.721 -14.346 1.00 38.42  ? 109 TYR D CB    1 
ATOM   3453 C CG    . TYR D 4 62  ? 33.498  -10.656 -13.327 1.00 43.30  ? 109 TYR D CG    1 
ATOM   3454 C CD1   . TYR D 4 62  ? 32.208  -10.268 -13.699 1.00 38.27  ? 109 TYR D CD1   1 
ATOM   3455 C CD2   . TYR D 4 62  ? 33.728  -10.952 -11.988 1.00 44.26  ? 109 TYR D CD2   1 
ATOM   3456 C CE1   . TYR D 4 62  ? 31.182  -10.189 -12.758 1.00 37.25  ? 109 TYR D CE1   1 
ATOM   3457 C CE2   . TYR D 4 62  ? 32.705  -10.880 -11.052 1.00 37.39  ? 109 TYR D CE2   1 
ATOM   3458 C CZ    . TYR D 4 62  ? 31.441  -10.506 -11.445 1.00 38.37  ? 109 TYR D CZ    1 
ATOM   3459 O OH    . TYR D 4 62  ? 30.447  -10.438 -10.499 1.00 40.66  ? 109 TYR D OH    1 
ATOM   3460 N N     . PHE D 4 63  ? 35.370  -11.547 -17.366 1.00 32.39  ? 110 PHE D N     1 
ATOM   3461 C CA    . PHE D 4 63  ? 36.252  -11.417 -18.510 1.00 32.55  ? 110 PHE D CA    1 
ATOM   3462 C C     . PHE D 4 63  ? 36.665  -9.969  -18.716 1.00 36.38  ? 110 PHE D C     1 
ATOM   3463 O O     . PHE D 4 63  ? 35.828  -9.063  -18.715 1.00 30.21  ? 110 PHE D O     1 
ATOM   3464 C CB    . PHE D 4 63  ? 35.609  -11.940 -19.790 1.00 32.44  ? 110 PHE D CB    1 
ATOM   3465 C CG    . PHE D 4 63  ? 36.451  -11.709 -21.007 1.00 31.56  ? 110 PHE D CG    1 
ATOM   3466 C CD1   . PHE D 4 63  ? 37.450  -12.597 -21.347 1.00 34.96  ? 110 PHE D CD1   1 
ATOM   3467 C CD2   . PHE D 4 63  ? 36.276  -10.584 -21.784 1.00 32.11  ? 110 PHE D CD2   1 
ATOM   3468 C CE1   . PHE D 4 63  ? 38.253  -12.378 -22.468 1.00 34.39  ? 110 PHE D CE1   1 
ATOM   3469 C CE2   . PHE D 4 63  ? 37.076  -10.352 -22.897 1.00 38.33  ? 110 PHE D CE2   1 
ATOM   3470 C CZ    . PHE D 4 63  ? 38.070  -11.255 -23.243 1.00 33.58  ? 110 PHE D CZ    1 
ATOM   3471 N N     . TYR D 4 64  ? 37.958  -9.767  -18.941 1.00 33.29  ? 111 TYR D N     1 
ATOM   3472 C CA    . TYR D 4 64  ? 38.507  -8.460  -19.258 1.00 30.43  ? 111 TYR D CA    1 
ATOM   3473 C C     . TYR D 4 64  ? 39.399  -8.590  -20.481 1.00 31.62  ? 111 TYR D C     1 
ATOM   3474 O O     . TYR D 4 64  ? 40.157  -9.558  -20.606 1.00 32.84  ? 111 TYR D O     1 
ATOM   3475 C CB    . TYR D 4 64  ? 39.283  -7.915  -18.086 1.00 31.55  ? 111 TYR D CB    1 
ATOM   3476 C CG    . TYR D 4 64  ? 38.452  -7.613  -16.864 1.00 28.30  ? 111 TYR D CG    1 
ATOM   3477 C CD1   . TYR D 4 64  ? 37.865  -6.375  -16.703 1.00 29.39  ? 111 TYR D CD1   1 
ATOM   3478 C CD2   . TYR D 4 64  ? 38.299  -8.543  -15.848 1.00 29.22  ? 111 TYR D CD2   1 
ATOM   3479 C CE1   . TYR D 4 64  ? 37.139  -6.079  -15.580 1.00 31.31  ? 111 TYR D CE1   1 
ATOM   3480 C CE2   . TYR D 4 64  ? 37.557  -8.249  -14.712 1.00 27.20  ? 111 TYR D CE2   1 
ATOM   3481 C CZ    . TYR D 4 64  ? 36.984  -7.013  -14.588 1.00 29.76  ? 111 TYR D CZ    1 
ATOM   3482 O OH    . TYR D 4 64  ? 36.242  -6.673  -13.468 1.00 39.41  ? 111 TYR D OH    1 
ATOM   3483 N N     . TYR D 4 65  ? 39.287  -7.640  -21.395 1.00 26.57  ? 112 TYR D N     1 
ATOM   3484 C CA    . TYR D 4 65  ? 40.132  -7.678  -22.571 1.00 30.29  ? 112 TYR D CA    1 
ATOM   3485 C C     . TYR D 4 65  ? 41.595  -7.462  -22.177 1.00 31.53  ? 112 TYR D C     1 
ATOM   3486 O O     . TYR D 4 65  ? 41.900  -6.867  -21.137 1.00 31.00  ? 112 TYR D O     1 
ATOM   3487 C CB    . TYR D 4 65  ? 39.706  -6.615  -23.570 1.00 27.15  ? 112 TYR D CB    1 
ATOM   3488 C CG    . TYR D 4 65  ? 38.447  -6.949  -24.298 1.00 37.33  ? 112 TYR D CG    1 
ATOM   3489 C CD1   . TYR D 4 65  ? 37.200  -6.752  -23.700 1.00 32.47  ? 112 TYR D CD1   1 
ATOM   3490 C CD2   . TYR D 4 65  ? 38.495  -7.468  -25.586 1.00 36.23  ? 112 TYR D CD2   1 
ATOM   3491 C CE1   . TYR D 4 65  ? 36.028  -7.056  -24.381 1.00 42.26  ? 112 TYR D CE1   1 
ATOM   3492 C CE2   . TYR D 4 65  ? 37.345  -7.774  -26.263 1.00 43.03  ? 112 TYR D CE2   1 
ATOM   3493 C CZ    . TYR D 4 65  ? 36.118  -7.561  -25.664 1.00 41.67  ? 112 TYR D CZ    1 
ATOM   3494 O OH    . TYR D 4 65  ? 34.996  -7.864  -26.365 1.00 42.11  ? 112 TYR D OH    1 
ATOM   3495 N N     . LEU D 4 66  ? 42.502  -7.970  -23.016 1.00 33.91  ? 113 LEU D N     1 
ATOM   3496 C CA    . LEU D 4 66  ? 43.928  -7.810  -22.763 1.00 30.11  ? 113 LEU D CA    1 
ATOM   3497 C C     . LEU D 4 66  ? 44.258  -6.333  -22.580 1.00 32.16  ? 113 LEU D C     1 
ATOM   3498 O O     . LEU D 4 66  ? 43.835  -5.480  -23.372 1.00 29.67  ? 113 LEU D O     1 
ATOM   3499 C CB    . LEU D 4 66  ? 44.750  -8.397  -23.923 1.00 31.04  ? 113 LEU D CB    1 
ATOM   3500 C CG    . LEU D 4 66  ? 46.273  -8.191  -23.802 1.00 30.26  ? 113 LEU D CG    1 
ATOM   3501 C CD1   . LEU D 4 66  ? 46.854  -8.922  -22.586 1.00 29.60  ? 113 LEU D CD1   1 
ATOM   3502 C CD2   . LEU D 4 66  ? 46.991  -8.631  -25.045 1.00 31.19  ? 113 LEU D CD2   1 
ATOM   3503 N N     . GLY D 4 67  ? 45.010  -6.036  -21.525 1.00 35.86  ? 114 GLY D N     1 
ATOM   3504 C CA    . GLY D 4 67  ? 45.411  -4.674  -21.248 1.00 31.65  ? 114 GLY D CA    1 
ATOM   3505 C C     . GLY D 4 67  ? 44.399  -3.829  -20.514 1.00 28.13  ? 114 GLY D C     1 
ATOM   3506 O O     . GLY D 4 67  ? 44.619  -2.626  -20.364 1.00 32.43  ? 114 GLY D O     1 
ATOM   3507 N N     . THR D 4 68  ? 43.289  -4.400  -20.063 1.00 31.36  ? 115 THR D N     1 
ATOM   3508 C CA    . THR D 4 68  ? 42.261  -3.647  -19.358 1.00 27.74  ? 115 THR D CA    1 
ATOM   3509 C C     . THR D 4 68  ? 41.950  -4.352  -18.054 1.00 30.35  ? 115 THR D C     1 
ATOM   3510 O O     . THR D 4 68  ? 42.302  -5.519  -17.856 1.00 25.31  ? 115 THR D O     1 
ATOM   3511 C CB    . THR D 4 68  ? 40.972  -3.540  -20.182 1.00 31.33  ? 115 THR D CB    1 
ATOM   3512 O OG1   . THR D 4 68  ? 40.266  -4.774  -20.061 1.00 31.10  ? 115 THR D OG1   1 
ATOM   3513 C CG2   . THR D 4 68  ? 41.280  -3.327  -21.644 1.00 28.25  ? 115 THR D CG2   1 
ATOM   3514 N N     . GLY D 4 69  ? 41.246  -3.642  -17.172 1.00 34.53  ? 116 GLY D N     1 
ATOM   3515 C CA    . GLY D 4 69  ? 40.715  -4.238  -15.967 1.00 29.76  ? 116 GLY D CA    1 
ATOM   3516 C C     . GLY D 4 69  ? 41.697  -4.252  -14.814 1.00 34.82  ? 116 GLY D C     1 
ATOM   3517 O O     . GLY D 4 69  ? 42.764  -3.629  -14.858 1.00 31.80  ? 116 GLY D O     1 
ATOM   3518 N N     . PRO D 4 70  ? 41.344  -4.972  -13.753 1.00 32.19  ? 117 PRO D N     1 
ATOM   3519 C CA    . PRO D 4 70  ? 42.205  -4.992  -12.556 1.00 33.92  ? 117 PRO D CA    1 
ATOM   3520 C C     . PRO D 4 70  ? 43.584  -5.601  -12.780 1.00 35.10  ? 117 PRO D C     1 
ATOM   3521 O O     . PRO D 4 70  ? 44.459  -5.437  -11.926 1.00 32.39  ? 117 PRO D O     1 
ATOM   3522 C CB    . PRO D 4 70  ? 41.390  -5.808  -11.543 1.00 33.96  ? 117 PRO D CB    1 
ATOM   3523 C CG    . PRO D 4 70  ? 40.354  -6.526  -12.341 1.00 35.16  ? 117 PRO D CG    1 
ATOM   3524 C CD    . PRO D 4 70  ? 40.096  -5.736  -13.577 1.00 32.00  ? 117 PRO D CD    1 
ATOM   3525 N N     . GLU D 4 71  ? 43.804  -6.320  -13.869 1.00 34.84  ? 118 GLU D N     1 
ATOM   3526 C CA    . GLU D 4 71  ? 45.141  -6.772  -14.246 1.00 33.22  ? 118 GLU D CA    1 
ATOM   3527 C C     . GLU D 4 71  ? 45.521  -6.210  -15.609 1.00 31.02  ? 118 GLU D C     1 
ATOM   3528 O O     . GLU D 4 71  ? 46.151  -6.886  -16.437 1.00 31.30  ? 118 GLU D O     1 
ATOM   3529 C CB    . GLU D 4 71  ? 45.239  -8.297  -14.234 1.00 31.40  ? 118 GLU D CB    1 
ATOM   3530 C CG    . GLU D 4 71  ? 45.061  -8.939  -12.850 1.00 32.89  ? 118 GLU D CG    1 
ATOM   3531 C CD    . GLU D 4 71  ? 46.102  -8.484  -11.814 1.00 45.52  ? 118 GLU D CD    1 
ATOM   3532 O OE1   . GLU D 4 71  ? 47.149  -7.870  -12.186 1.00 40.31  ? 118 GLU D OE1   1 
ATOM   3533 O OE2   . GLU D 4 71  ? 45.865  -8.750  -10.614 1.00 39.76  ? 118 GLU D OE2   1 
ATOM   3534 N N     . ALA D 4 72  ? 45.136  -4.947  -15.845 1.00 28.90  ? 119 ALA D N     1 
ATOM   3535 C CA    . ALA D 4 72  ? 45.423  -4.280  -17.112 1.00 28.63  ? 119 ALA D CA    1 
ATOM   3536 C C     . ALA D 4 72  ? 46.914  -4.304  -17.464 1.00 29.81  ? 119 ALA D C     1 
ATOM   3537 O O     . ALA D 4 72  ? 47.273  -4.286  -18.647 1.00 33.48  ? 119 ALA D O     1 
ATOM   3538 C CB    . ALA D 4 72  ? 44.944  -2.834  -17.058 1.00 30.12  ? 119 ALA D CB    1 
ATOM   3539 N N     . GLY D 4 73  ? 47.792  -4.314  -16.466 1.00 31.19  ? 120 GLY D N     1 
ATOM   3540 C CA    . GLY D 4 73  ? 49.220  -4.313  -16.737 1.00 30.50  ? 120 GLY D CA    1 
ATOM   3541 C C     . GLY D 4 73  ? 49.831  -5.682  -16.966 1.00 36.70  ? 120 GLY D C     1 
ATOM   3542 O O     . GLY D 4 73  ? 51.023  -5.770  -17.305 1.00 32.98  ? 120 GLY D O     1 
ATOM   3543 N N     . LEU D 4 74  ? 49.042  -6.776  -16.769 1.00 28.78  ? 121 LEU D N     1 
ATOM   3544 C CA    . LEU D 4 74  ? 49.621  -8.095  -16.959 1.00 30.29  ? 121 LEU D CA    1 
ATOM   3545 C C     . LEU D 4 74  ? 49.770  -8.403  -18.441 1.00 36.33  ? 121 LEU D C     1 
ATOM   3546 O O     . LEU D 4 74  ? 48.881  -8.078  -19.237 1.00 29.33  ? 121 LEU D O     1 
ATOM   3547 C CB    . LEU D 4 74  ? 48.787  -9.182  -16.308 1.00 32.36  ? 121 LEU D CB    1 
ATOM   3548 C CG    . LEU D 4 74  ? 49.016  -9.456  -14.823 1.00 41.35  ? 121 LEU D CG    1 
ATOM   3549 C CD1   . LEU D 4 74  ? 48.573  -10.879 -14.491 1.00 31.19  ? 121 LEU D CD1   1 
ATOM   3550 C CD2   . LEU D 4 74  ? 50.473  -9.209  -14.401 1.00 31.95  ? 121 LEU D CD2   1 
ATOM   3551 N N     . PRO D 4 75  ? 50.894  -8.999  -18.836 1.00 34.08  ? 122 PRO D N     1 
ATOM   3552 C CA    . PRO D 4 75  ? 51.047  -9.459  -20.212 1.00 31.51  ? 122 PRO D CA    1 
ATOM   3553 C C     . PRO D 4 75  ? 50.340  -10.787 -20.402 1.00 33.65  ? 122 PRO D C     1 
ATOM   3554 O O     . PRO D 4 75  ? 50.199  -11.575 -19.463 1.00 34.38  ? 122 PRO D O     1 
ATOM   3555 C CB    . PRO D 4 75  ? 52.567  -9.619  -20.359 1.00 33.09  ? 122 PRO D CB    1 
ATOM   3556 C CG    . PRO D 4 75  ? 53.016  -9.999  -18.978 1.00 30.13  ? 122 PRO D CG    1 
ATOM   3557 C CD    . PRO D 4 75  ? 52.085  -9.298  -18.015 1.00 34.48  ? 122 PRO D CD    1 
ATOM   3558 N N     . TYR D 4 76  ? 49.933  -11.041 -21.651 1.00 34.28  ? 123 TYR D N     1 
ATOM   3559 C CA    . TYR D 4 76  ? 49.270  -12.297 -21.990 1.00 31.68  ? 123 TYR D CA    1 
ATOM   3560 C C     . TYR D 4 76  ? 50.087  -13.490 -21.526 1.00 40.68  ? 123 TYR D C     1 
ATOM   3561 O O     . TYR D 4 76  ? 51.293  -13.564 -21.765 1.00 33.52  ? 123 TYR D O     1 
ATOM   3562 C CB    . TYR D 4 76  ? 49.056  -12.413 -23.492 1.00 33.98  ? 123 TYR D CB    1 
ATOM   3563 C CG    . TYR D 4 76  ? 48.131  -13.564 -23.804 1.00 42.11  ? 123 TYR D CG    1 
ATOM   3564 C CD1   . TYR D 4 76  ? 46.755  -13.434 -23.605 1.00 38.30  ? 123 TYR D CD1   1 
ATOM   3565 C CD2   . TYR D 4 76  ? 48.617  -14.783 -24.247 1.00 36.47  ? 123 TYR D CD2   1 
ATOM   3566 C CE1   . TYR D 4 76  ? 45.890  -14.479 -23.845 1.00 37.31  ? 123 TYR D CE1   1 
ATOM   3567 C CE2   . TYR D 4 76  ? 47.747  -15.840 -24.499 1.00 39.40  ? 123 TYR D CE2   1 
ATOM   3568 C CZ    . TYR D 4 76  ? 46.377  -15.672 -24.296 1.00 38.63  ? 123 TYR D CZ    1 
ATOM   3569 O OH    . TYR D 4 76  ? 45.490  -16.699 -24.542 1.00 36.80  ? 123 TYR D OH    1 
ATOM   3570 N N     . GLY D 4 77  ? 49.424  -14.432 -20.865 1.00 44.09  ? 124 GLY D N     1 
ATOM   3571 C CA    . GLY D 4 77  ? 50.093  -15.639 -20.436 1.00 37.13  ? 124 GLY D CA    1 
ATOM   3572 C C     . GLY D 4 77  ? 50.812  -15.555 -19.112 1.00 37.41  ? 124 GLY D C     1 
ATOM   3573 O O     . GLY D 4 77  ? 51.342  -16.581 -18.658 1.00 40.85  ? 124 GLY D O     1 
ATOM   3574 N N     . ALA D 4 78  ? 50.843  -14.384 -18.473 1.00 34.54  ? 125 ALA D N     1 
ATOM   3575 C CA    . ALA D 4 78  ? 51.489  -14.269 -17.168 1.00 41.10  ? 125 ALA D CA    1 
ATOM   3576 C C     . ALA D 4 78  ? 50.820  -15.177 -16.145 1.00 39.86  ? 125 ALA D C     1 
ATOM   3577 O O     . ALA D 4 78  ? 49.593  -15.245 -16.063 1.00 38.39  ? 125 ALA D O     1 
ATOM   3578 C CB    . ALA D 4 78  ? 51.439  -12.825 -16.669 1.00 40.02  ? 125 ALA D CB    1 
ATOM   3579 N N     . ASN D 4 79  ? 51.629  -15.853 -15.338 1.00 38.85  ? 126 ASN D N     1 
ATOM   3580 C CA    . ASN D 4 79  ? 51.081  -16.666 -14.264 1.00 42.39  ? 126 ASN D CA    1 
ATOM   3581 C C     . ASN D 4 79  ? 50.701  -15.785 -13.082 1.00 41.69  ? 126 ASN D C     1 
ATOM   3582 O O     . ASN D 4 79  ? 51.493  -14.950 -12.637 1.00 40.26  ? 126 ASN D O     1 
ATOM   3583 C CB    . ASN D 4 79  ? 52.079  -17.736 -13.818 1.00 46.28  ? 126 ASN D CB    1 
ATOM   3584 C CG    . ASN D 4 79  ? 51.422  -18.814 -12.944 1.00 58.05  ? 126 ASN D CG    1 
ATOM   3585 O OD1   . ASN D 4 79  ? 51.185  -18.615 -11.741 1.00 54.94  ? 126 ASN D OD1   1 
ATOM   3586 N ND2   . ASN D 4 79  ? 51.110  -19.954 -13.554 1.00 60.01  ? 126 ASN D ND2   1 
ATOM   3587 N N     . LYS D 4 80  ? 49.476  -15.964 -12.597 1.00 40.65  ? 127 LYS D N     1 
ATOM   3588 C CA    . LYS D 4 80  ? 48.973  -15.371 -11.366 1.00 38.75  ? 127 LYS D CA    1 
ATOM   3589 C C     . LYS D 4 80  ? 47.760  -16.185 -10.932 1.00 38.99  ? 127 LYS D C     1 
ATOM   3590 O O     . LYS D 4 80  ? 46.983  -16.626 -11.776 1.00 48.31  ? 127 LYS D O     1 
ATOM   3591 C CB    . LYS D 4 80  ? 48.592  -13.901 -11.557 1.00 35.58  ? 127 LYS D CB    1 
ATOM   3592 C CG    . LYS D 4 80  ? 48.274  -13.186 -10.259 1.00 38.85  ? 127 LYS D CG    1 
ATOM   3593 C CD    . LYS D 4 80  ? 48.121  -11.665 -10.442 1.00 44.08  ? 127 LYS D CD    1 
ATOM   3594 C CE    . LYS D 4 80  ? 47.891  -10.983 -9.087  1.00 42.24  ? 127 LYS D CE    1 
ATOM   3595 N NZ    . LYS D 4 80  ? 48.403  -9.582  -8.987  1.00 41.75  ? 127 LYS D NZ    1 
ATOM   3596 N N     . ASP D 4 81  ? 47.595  -16.385 -9.629  1.00 42.20  ? 128 ASP D N     1 
ATOM   3597 C CA    . ASP D 4 81  ? 46.471  -17.181 -9.149  1.00 45.75  ? 128 ASP D CA    1 
ATOM   3598 C C     . ASP D 4 81  ? 45.161  -16.434 -9.378  1.00 42.03  ? 128 ASP D C     1 
ATOM   3599 O O     . ASP D 4 81  ? 45.050  -15.246 -9.064  1.00 40.06  ? 128 ASP D O     1 
ATOM   3600 C CB    . ASP D 4 81  ? 46.637  -17.525 -7.664  1.00 45.27  ? 128 ASP D CB    1 
ATOM   3601 C CG    . ASP D 4 81  ? 45.460  -18.360 -7.110  1.00 56.13  ? 128 ASP D CG    1 
ATOM   3602 O OD1   . ASP D 4 81  ? 45.229  -19.502 -7.604  1.00 51.29  ? 128 ASP D OD1   1 
ATOM   3603 O OD2   . ASP D 4 81  ? 44.772  -17.869 -6.172  1.00 52.51  ? 128 ASP D OD2   1 
ATOM   3604 N N     . GLY D 4 82  ? 44.165  -17.136 -9.917  1.00 43.66  ? 129 GLY D N     1 
ATOM   3605 C CA    . GLY D 4 82  ? 42.862  -16.548 -10.175 1.00 40.56  ? 129 GLY D CA    1 
ATOM   3606 C C     . GLY D 4 82  ? 42.721  -15.881 -11.524 1.00 40.66  ? 129 GLY D C     1 
ATOM   3607 O O     . GLY D 4 82  ? 41.645  -15.347 -11.829 1.00 36.38  ? 129 GLY D O     1 
ATOM   3608 N N     . ILE D 4 83  ? 43.771  -15.887 -12.338 1.00 37.01  ? 130 ILE D N     1 
ATOM   3609 C CA    . ILE D 4 83  ? 43.748  -15.314 -13.676 1.00 37.52  ? 130 ILE D CA    1 
ATOM   3610 C C     . ILE D 4 83  ? 44.023  -16.431 -14.664 1.00 39.86  ? 130 ILE D C     1 
ATOM   3611 O O     . ILE D 4 83  ? 44.982  -17.193 -14.485 1.00 43.78  ? 130 ILE D O     1 
ATOM   3612 C CB    . ILE D 4 83  ? 44.792  -14.195 -13.830 1.00 40.32  ? 130 ILE D CB    1 
ATOM   3613 C CG1   . ILE D 4 83  ? 44.693  -13.216 -12.665 1.00 39.56  ? 130 ILE D CG1   1 
ATOM   3614 C CG2   . ILE D 4 83  ? 44.595  -13.459 -15.149 1.00 37.15  ? 130 ILE D CG2   1 
ATOM   3615 C CD1   . ILE D 4 83  ? 43.509  -12.289 -12.766 1.00 34.85  ? 130 ILE D CD1   1 
ATOM   3616 N N     . ILE D 4 84  ? 43.193  -16.532 -15.701 1.00 35.27  ? 131 ILE D N     1 
ATOM   3617 C CA    . ILE D 4 84  ? 43.423  -17.478 -16.784 1.00 39.36  ? 131 ILE D CA    1 
ATOM   3618 C C     . ILE D 4 84  ? 43.199  -16.753 -18.102 1.00 35.83  ? 131 ILE D C     1 
ATOM   3619 O O     . ILE D 4 84  ? 42.489  -15.747 -18.162 1.00 35.34  ? 131 ILE D O     1 
ATOM   3620 C CB    . ILE D 4 84  ? 42.536  -18.744 -16.652 1.00 39.81  ? 131 ILE D CB    1 
ATOM   3621 C CG1   . ILE D 4 84  ? 41.056  -18.428 -16.878 1.00 36.71  ? 131 ILE D CG1   1 
ATOM   3622 C CG2   . ILE D 4 84  ? 42.767  -19.414 -15.268 1.00 36.71  ? 131 ILE D CG2   1 
ATOM   3623 C CD1   . ILE D 4 84  ? 40.540  -18.906 -18.210 1.00 38.76  ? 131 ILE D CD1   1 
ATOM   3624 N N     . TRP D 4 85  ? 43.830  -17.248 -19.159 1.00 34.56  ? 132 TRP D N     1 
ATOM   3625 C CA    . TRP D 4 85  ? 43.958  -16.495 -20.395 1.00 36.28  ? 132 TRP D CA    1 
ATOM   3626 C C     . TRP D 4 85  ? 43.169  -17.143 -21.523 1.00 37.16  ? 132 TRP D C     1 
ATOM   3627 O O     . TRP D 4 85  ? 43.072  -18.368 -21.621 1.00 42.67  ? 132 TRP D O     1 
ATOM   3628 C CB    . TRP D 4 85  ? 45.439  -16.349 -20.801 1.00 36.19  ? 132 TRP D CB    1 
ATOM   3629 C CG    . TRP D 4 85  ? 46.212  -15.529 -19.812 1.00 37.01  ? 132 TRP D CG    1 
ATOM   3630 C CD1   . TRP D 4 85  ? 46.988  -15.992 -18.778 1.00 36.23  ? 132 TRP D CD1   1 
ATOM   3631 C CD2   . TRP D 4 85  ? 46.244  -14.102 -19.724 1.00 34.93  ? 132 TRP D CD2   1 
ATOM   3632 N NE1   . TRP D 4 85  ? 47.506  -14.942 -18.070 1.00 36.09  ? 132 TRP D NE1   1 
ATOM   3633 C CE2   . TRP D 4 85  ? 47.062  -13.770 -18.627 1.00 35.16  ? 132 TRP D CE2   1 
ATOM   3634 C CE3   . TRP D 4 85  ? 45.680  -13.073 -20.480 1.00 35.19  ? 132 TRP D CE3   1 
ATOM   3635 C CZ2   . TRP D 4 85  ? 47.318  -12.457 -18.263 1.00 33.69  ? 132 TRP D CZ2   1 
ATOM   3636 C CZ3   . TRP D 4 85  ? 45.945  -11.762 -20.120 1.00 33.41  ? 132 TRP D CZ3   1 
ATOM   3637 C CH2   . TRP D 4 85  ? 46.759  -11.469 -19.026 1.00 34.93  ? 132 TRP D CH2   1 
ATOM   3638 N N     . VAL D 4 86  ? 42.627  -16.306 -22.391 1.00 32.52  ? 133 VAL D N     1 
ATOM   3639 C CA    . VAL D 4 86  ? 41.848  -16.757 -23.530 1.00 35.22  ? 133 VAL D CA    1 
ATOM   3640 C C     . VAL D 4 86  ? 42.257  -15.941 -24.744 1.00 36.52  ? 133 VAL D C     1 
ATOM   3641 O O     . VAL D 4 86  ? 42.503  -14.737 -24.636 1.00 40.80  ? 133 VAL D O     1 
ATOM   3642 C CB    . VAL D 4 86  ? 40.341  -16.605 -23.255 1.00 39.10  ? 133 VAL D CB    1 
ATOM   3643 C CG1   . VAL D 4 86  ? 39.856  -17.723 -22.347 1.00 40.93  ? 133 VAL D CG1   1 
ATOM   3644 C CG2   . VAL D 4 86  ? 40.090  -15.270 -22.610 1.00 32.86  ? 133 VAL D CG2   1 
ATOM   3645 N N     . ALA D 4 87  ? 42.342  -16.589 -25.900 1.00 34.89  ? 134 ALA D N     1 
ATOM   3646 C CA    . ALA D 4 87  ? 42.615  -15.843 -27.116 1.00 42.44  ? 134 ALA D CA    1 
ATOM   3647 C C     . ALA D 4 87  ? 42.107  -16.608 -28.325 1.00 44.16  ? 134 ALA D C     1 
ATOM   3648 O O     . ALA D 4 87  ? 42.407  -17.793 -28.487 1.00 42.20  ? 134 ALA D O     1 
ATOM   3649 C CB    . ALA D 4 87  ? 44.113  -15.557 -27.262 1.00 44.01  ? 134 ALA D CB    1 
ATOM   3650 N N     . THR D 4 88  ? 41.340  -15.926 -29.165 1.00 46.43  ? 135 THR D N     1 
ATOM   3651 C CA    . THR D 4 88  ? 41.055  -16.433 -30.495 1.00 50.46  ? 135 THR D CA    1 
ATOM   3652 C C     . THR D 4 88  ? 42.322  -16.365 -31.326 1.00 53.60  ? 135 THR D C     1 
ATOM   3653 O O     . THR D 4 88  ? 42.983  -15.325 -31.367 1.00 56.03  ? 135 THR D O     1 
ATOM   3654 C CB    . THR D 4 88  ? 39.950  -15.608 -31.145 1.00 44.88  ? 135 THR D CB    1 
ATOM   3655 O OG1   . THR D 4 88  ? 38.698  -16.050 -30.643 1.00 52.73  ? 135 THR D OG1   1 
ATOM   3656 C CG2   . THR D 4 88  ? 39.943  -15.764 -32.646 1.00 53.05  ? 135 THR D CG2   1 
ATOM   3657 N N     . GLU D 4 89  ? 42.685  -17.470 -31.970 1.00 58.22  ? 136 GLU D N     1 
ATOM   3658 C CA    . GLU D 4 89  ? 43.817  -17.406 -32.884 1.00 62.67  ? 136 GLU D CA    1 
ATOM   3659 C C     . GLU D 4 89  ? 43.530  -16.348 -33.945 1.00 62.55  ? 136 GLU D C     1 
ATOM   3660 O O     . GLU D 4 89  ? 42.408  -16.230 -34.448 1.00 64.08  ? 136 GLU D O     1 
ATOM   3661 C CB    . GLU D 4 89  ? 44.085  -18.771 -33.525 1.00 67.65  ? 136 GLU D CB    1 
ATOM   3662 C CG    . GLU D 4 89  ? 45.446  -18.860 -34.237 1.00 74.56  ? 136 GLU D CG    1 
ATOM   3663 C CD    . GLU D 4 89  ? 46.615  -19.149 -33.285 1.00 82.47  ? 136 GLU D CD    1 
ATOM   3664 O OE1   . GLU D 4 89  ? 46.443  -19.996 -32.372 1.00 80.07  ? 136 GLU D OE1   1 
ATOM   3665 O OE2   . GLU D 4 89  ? 47.701  -18.532 -33.455 1.00 80.82  ? 136 GLU D OE2   1 
ATOM   3666 N N     . GLY D 4 90  ? 44.535  -15.543 -34.253 1.00 59.38  ? 137 GLY D N     1 
ATOM   3667 C CA    . GLY D 4 90  ? 44.319  -14.347 -35.029 1.00 51.18  ? 137 GLY D CA    1 
ATOM   3668 C C     . GLY D 4 90  ? 44.070  -13.108 -34.198 1.00 49.60  ? 137 GLY D C     1 
ATOM   3669 O O     . GLY D 4 90  ? 44.047  -12.003 -34.749 1.00 50.10  ? 137 GLY D O     1 
ATOM   3670 N N     . ALA D 4 91  ? 43.865  -13.249 -32.895 1.00 42.53  ? 138 ALA D N     1 
ATOM   3671 C CA    . ALA D 4 91  ? 43.864  -12.074 -32.047 1.00 43.15  ? 138 ALA D CA    1 
ATOM   3672 C C     . ALA D 4 91  ? 45.268  -11.488 -31.989 1.00 50.11  ? 138 ALA D C     1 
ATOM   3673 O O     . ALA D 4 91  ? 46.275  -12.204 -32.098 1.00 45.09  ? 138 ALA D O     1 
ATOM   3674 C CB    . ALA D 4 91  ? 43.393  -12.413 -30.644 1.00 41.08  ? 138 ALA D CB    1 
ATOM   3675 N N     . LEU D 4 92  ? 45.333  -10.172 -31.830 1.00 42.54  ? 139 LEU D N     1 
ATOM   3676 C CA    . LEU D 4 92  ? 46.606  -9.479  -31.780 1.00 47.03  ? 139 LEU D CA    1 
ATOM   3677 C C     . LEU D 4 92  ? 46.984  -9.239  -30.328 1.00 43.24  ? 139 LEU D C     1 
ATOM   3678 O O     . LEU D 4 92  ? 46.116  -9.013  -29.480 1.00 41.80  ? 139 LEU D O     1 
ATOM   3679 C CB    . LEU D 4 92  ? 46.549  -8.170  -32.566 1.00 45.81  ? 139 LEU D CB    1 
ATOM   3680 C CG    . LEU D 4 92  ? 46.315  -8.422  -34.067 1.00 50.91  ? 139 LEU D CG    1 
ATOM   3681 C CD1   . LEU D 4 92  ? 46.752  -7.236  -34.924 1.00 58.92  ? 139 LEU D CD1   1 
ATOM   3682 C CD2   . LEU D 4 92  ? 46.998  -9.702  -34.549 1.00 48.90  ? 139 LEU D CD2   1 
ATOM   3683 N N     . ASN D 4 93  ? 48.281  -9.335  -30.040 1.00 42.91  ? 140 ASN D N     1 
ATOM   3684 C CA    . ASN D 4 93  ? 48.788  -9.188  -28.675 1.00 39.71  ? 140 ASN D CA    1 
ATOM   3685 C C     . ASN D 4 93  ? 49.163  -7.728  -28.440 1.00 38.88  ? 140 ASN D C     1 
ATOM   3686 O O     . ASN D 4 93  ? 50.333  -7.358  -28.414 1.00 33.96  ? 140 ASN D O     1 
ATOM   3687 C CB    . ASN D 4 93  ? 49.974  -10.121 -28.445 1.00 43.60  ? 140 ASN D CB    1 
ATOM   3688 C CG    . ASN D 4 93  ? 50.272  -10.347 -26.968 1.00 41.31  ? 140 ASN D CG    1 
ATOM   3689 O OD1   . ASN D 4 93  ? 49.987  -9.487  -26.130 1.00 41.26  ? 140 ASN D OD1   1 
ATOM   3690 N ND2   . ASN D 4 93  ? 50.852  -11.509 -26.641 1.00 37.13  ? 140 ASN D ND2   1 
ATOM   3691 N N     . THR D 4 94  ? 48.131  -6.893  -28.312 1.00 37.37  ? 141 THR D N     1 
ATOM   3692 C CA    . THR D 4 94  ? 48.217  -5.478  -27.998 1.00 38.32  ? 141 THR D CA    1 
ATOM   3693 C C     . THR D 4 94  ? 47.169  -5.152  -26.947 1.00 36.81  ? 141 THR D C     1 
ATOM   3694 O O     . THR D 4 94  ? 46.223  -5.930  -26.751 1.00 39.90  ? 141 THR D O     1 
ATOM   3695 C CB    . THR D 4 94  ? 48.001  -4.583  -29.231 1.00 37.69  ? 141 THR D CB    1 
ATOM   3696 O OG1   . THR D 4 94  ? 46.724  -4.842  -29.787 1.00 39.94  ? 141 THR D OG1   1 
ATOM   3697 C CG2   . THR D 4 94  ? 49.046  -4.834  -30.289 1.00 40.62  ? 141 THR D CG2   1 
ATOM   3698 N N     . PRO D 4 95  ? 47.312  -4.037  -26.226 1.00 33.53  ? 142 PRO D N     1 
ATOM   3699 C CA    . PRO D 4 95  ? 46.344  -3.698  -25.165 1.00 30.39  ? 142 PRO D CA    1 
ATOM   3700 C C     . PRO D 4 95  ? 45.060  -3.107  -25.739 1.00 39.18  ? 142 PRO D C     1 
ATOM   3701 O O     . PRO D 4 95  ? 45.092  -2.190  -26.562 1.00 37.03  ? 142 PRO D O     1 
ATOM   3702 C CB    . PRO D 4 95  ? 47.082  -2.659  -24.318 1.00 32.89  ? 142 PRO D CB    1 
ATOM   3703 C CG    . PRO D 4 95  ? 48.049  -2.034  -25.286 1.00 40.37  ? 142 PRO D CG    1 
ATOM   3704 C CD    . PRO D 4 95  ? 48.512  -3.181  -26.152 1.00 38.47  ? 142 PRO D CD    1 
ATOM   3705 N N     . LYS D 4 96  ? 43.927  -3.581  -25.245 1.00 31.96  ? 143 LYS D N     1 
ATOM   3706 C CA    . LYS D 4 96  ? 42.648  -3.160  -25.817 1.00 38.16  ? 143 LYS D CA    1 
ATOM   3707 C C     . LYS D 4 96  ? 42.094  -1.949  -25.063 1.00 38.27  ? 143 LYS D C     1 
ATOM   3708 O O     . LYS D 4 96  ? 41.038  -1.969  -24.434 1.00 36.79  ? 143 LYS D O     1 
ATOM   3709 C CB    . LYS D 4 96  ? 41.675  -4.331  -25.833 1.00 30.48  ? 143 LYS D CB    1 
ATOM   3710 C CG    . LYS D 4 96  ? 42.205  -5.591  -26.532 1.00 32.64  ? 143 LYS D CG    1 
ATOM   3711 C CD    . LYS D 4 96  ? 42.858  -5.320  -27.881 1.00 32.92  ? 143 LYS D CD    1 
ATOM   3712 C CE    . LYS D 4 96  ? 43.388  -6.620  -28.447 1.00 38.35  ? 143 LYS D CE    1 
ATOM   3713 N NZ    . LYS D 4 96  ? 44.469  -6.452  -29.463 1.00 37.82  ? 143 LYS D NZ    1 
ATOM   3714 N N     . ASP D 4 97  ? 42.838  -0.854  -25.149 1.00 39.92  ? 144 ASP D N     1 
ATOM   3715 C CA    . ASP D 4 97  ? 42.442  0.327   -24.395 1.00 43.26  ? 144 ASP D CA    1 
ATOM   3716 C C     . ASP D 4 97  ? 41.305  1.089   -25.061 1.00 41.64  ? 144 ASP D C     1 
ATOM   3717 O O     . ASP D 4 97  ? 40.671  1.923   -24.406 1.00 43.39  ? 144 ASP D O     1 
ATOM   3718 C CB    . ASP D 4 97  ? 43.649  1.255   -24.168 1.00 44.26  ? 144 ASP D CB    1 
ATOM   3719 C CG    . ASP D 4 97  ? 44.374  1.621   -25.456 1.00 49.99  ? 144 ASP D CG    1 
ATOM   3720 O OD1   . ASP D 4 97  ? 44.408  0.802   -26.410 1.00 52.13  ? 144 ASP D OD1   1 
ATOM   3721 O OD2   . ASP D 4 97  ? 44.919  2.736   -25.506 1.00 51.90  ? 144 ASP D OD2   1 
ATOM   3722 N N     . HIS D 4 98  ? 41.042  0.839   -26.342 1.00 40.07  ? 145 HIS D N     1 
ATOM   3723 C CA    . HIS D 4 98  ? 39.914  1.500   -26.976 1.00 43.54  ? 145 HIS D CA    1 
ATOM   3724 C C     . HIS D 4 98  ? 38.593  0.908   -26.519 1.00 43.67  ? 145 HIS D C     1 
ATOM   3725 O O     . HIS D 4 98  ? 37.543  1.461   -26.837 1.00 48.41  ? 145 HIS D O     1 
ATOM   3726 C CB    . HIS D 4 98  ? 40.031  1.400   -28.486 1.00 40.34  ? 145 HIS D CB    1 
ATOM   3727 C CG    . HIS D 4 98  ? 40.012  -0.008  -28.987 1.00 48.72  ? 145 HIS D CG    1 
ATOM   3728 N ND1   . HIS D 4 98  ? 41.122  -0.827  -28.950 1.00 51.78  ? 145 HIS D ND1   1 
ATOM   3729 C CD2   . HIS D 4 98  ? 39.015  -0.750  -29.526 1.00 48.69  ? 145 HIS D CD2   1 
ATOM   3730 C CE1   . HIS D 4 98  ? 40.811  -2.010  -29.452 1.00 48.46  ? 145 HIS D CE1   1 
ATOM   3731 N NE2   . HIS D 4 98  ? 39.538  -1.990  -29.808 1.00 52.04  ? 145 HIS D NE2   1 
ATOM   3732 N N     . ILE D 4 99  ? 38.629  -0.196  -25.789 1.00 42.66  ? 146 ILE D N     1 
ATOM   3733 C CA    . ILE D 4 99  ? 37.445  -0.855  -25.277 1.00 37.86  ? 146 ILE D CA    1 
ATOM   3734 C C     . ILE D 4 99  ? 37.295  -0.612  -23.790 1.00 43.31  ? 146 ILE D C     1 
ATOM   3735 O O     . ILE D 4 99  ? 36.245  -0.177  -23.326 1.00 45.61  ? 146 ILE D O     1 
ATOM   3736 C CB    . ILE D 4 99  ? 37.476  -2.366  -25.587 1.00 35.54  ? 146 ILE D CB    1 
ATOM   3737 C CG1   . ILE D 4 99  ? 37.447  -2.589  -27.091 1.00 38.56  ? 146 ILE D CG1   1 
ATOM   3738 C CG2   . ILE D 4 99  ? 36.307  -3.067  -24.924 1.00 41.00  ? 146 ILE D CG2   1 
ATOM   3739 C CD1   . ILE D 4 99  ? 37.577  -4.038  -27.486 1.00 41.62  ? 146 ILE D CD1   1 
ATOM   3740 N N     . GLY D 4 100 ? 38.345  -0.879  -23.027 1.00 45.18  ? 147 GLY D N     1 
ATOM   3741 C CA    . GLY D 4 100 ? 38.352  -0.499  -21.631 1.00 40.40  ? 147 GLY D CA    1 
ATOM   3742 C C     . GLY D 4 100 ? 37.406  -1.337  -20.792 1.00 39.96  ? 147 GLY D C     1 
ATOM   3743 O O     . GLY D 4 100 ? 36.993  -2.440  -21.163 1.00 33.14  ? 147 GLY D O     1 
ATOM   3744 N N     . THR D 4 101 ? 37.100  -0.795  -19.616 1.00 33.71  ? 148 THR D N     1 
ATOM   3745 C CA    . THR D 4 101 ? 36.157  -1.390  -18.701 1.00 38.27  ? 148 THR D CA    1 
ATOM   3746 C C     . THR D 4 101 ? 34.807  -0.689  -18.831 1.00 37.33  ? 148 THR D C     1 
ATOM   3747 O O     . THR D 4 101 ? 34.650  0.302   -19.546 1.00 33.30  ? 148 THR D O     1 
ATOM   3748 C CB    . THR D 4 101 ? 36.668  -1.296  -17.271 1.00 36.20  ? 148 THR D CB    1 
ATOM   3749 O OG1   . THR D 4 101 ? 37.175  0.020   -17.059 1.00 39.50  ? 148 THR D OG1   1 
ATOM   3750 C CG2   . THR D 4 101 ? 37.738  -2.339  -17.017 1.00 35.09  ? 148 THR D CG2   1 
ATOM   3751 N N     . ARG D 4 102 ? 33.833  -1.202  -18.096 1.00 40.26  ? 149 ARG D N     1 
ATOM   3752 C CA    . ARG D 4 102 ? 32.464  -0.711  -18.118 1.00 33.34  ? 149 ARG D CA    1 
ATOM   3753 C C     . ARG D 4 102 ? 32.231  0.088   -16.860 1.00 34.83  ? 149 ARG D C     1 
ATOM   3754 O O     . ARG D 4 102 ? 32.562  -0.375  -15.766 1.00 36.76  ? 149 ARG D O     1 
ATOM   3755 C CB    . ARG D 4 102 ? 31.474  -1.874  -18.182 1.00 39.97  ? 149 ARG D CB    1 
ATOM   3756 C CG    . ARG D 4 102 ? 30.003  -1.497  -18.036 1.00 35.51  ? 149 ARG D CG    1 
ATOM   3757 C CD    . ARG D 4 102 ? 29.142  -2.700  -18.353 1.00 34.02  ? 149 ARG D CD    1 
ATOM   3758 N NE    . ARG D 4 102 ? 29.237  -3.740  -17.336 1.00 29.06  ? 149 ARG D NE    1 
ATOM   3759 C CZ    . ARG D 4 102 ? 28.514  -3.773  -16.229 1.00 37.08  ? 149 ARG D CZ    1 
ATOM   3760 N NH1   . ARG D 4 102 ? 27.566  -2.869  -15.994 1.00 44.22  ? 149 ARG D NH1   1 
ATOM   3761 N NH2   . ARG D 4 102 ? 28.738  -4.733  -15.335 1.00 32.89  ? 149 ARG D NH2   1 
ATOM   3762 N N     . ASN D 4 103 ? 31.692  1.293   -17.018 1.00 37.56  ? 150 ASN D N     1 
ATOM   3763 C CA    . ASN D 4 103 ? 31.204  2.041   -15.869 1.00 38.43  ? 150 ASN D CA    1 
ATOM   3764 C C     . ASN D 4 103 ? 29.764  1.609   -15.617 1.00 41.04  ? 150 ASN D C     1 
ATOM   3765 O O     . ASN D 4 103 ? 28.861  2.050   -16.330 1.00 39.38  ? 150 ASN D O     1 
ATOM   3766 C CB    . ASN D 4 103 ? 31.299  3.545   -16.116 1.00 39.44  ? 150 ASN D CB    1 
ATOM   3767 C CG    . ASN D 4 103 ? 30.521  4.363   -15.086 1.00 44.61  ? 150 ASN D CG    1 
ATOM   3768 O OD1   . ASN D 4 103 ? 30.127  3.867   -14.025 1.00 42.11  ? 150 ASN D OD1   1 
ATOM   3769 N ND2   . ASN D 4 103 ? 30.303  5.630   -15.401 1.00 49.22  ? 150 ASN D ND2   1 
ATOM   3770 N N     . PRO D 4 104 ? 29.509  0.778   -14.608 1.00 38.18  ? 151 PRO D N     1 
ATOM   3771 C CA    . PRO D 4 104 ? 28.186  0.145   -14.497 1.00 40.51  ? 151 PRO D CA    1 
ATOM   3772 C C     . PRO D 4 104 ? 27.059  1.138   -14.288 1.00 44.70  ? 151 PRO D C     1 
ATOM   3773 O O     . PRO D 4 104 ? 25.883  0.779   -14.449 1.00 44.46  ? 151 PRO D O     1 
ATOM   3774 C CB    . PRO D 4 104 ? 28.346  -0.794  -13.292 1.00 43.12  ? 151 PRO D CB    1 
ATOM   3775 C CG    . PRO D 4 104 ? 29.455  -0.185  -12.472 1.00 44.34  ? 151 PRO D CG    1 
ATOM   3776 C CD    . PRO D 4 104 ? 30.344  0.574   -13.410 1.00 40.69  ? 151 PRO D CD    1 
ATOM   3777 N N     . ALA D 4 105 ? 27.380  2.370   -13.917 1.00 43.15  ? 152 ALA D N     1 
ATOM   3778 C CA    . ALA D 4 105 ? 26.349  3.380   -13.739 1.00 46.70  ? 152 ALA D CA    1 
ATOM   3779 C C     . ALA D 4 105 ? 25.766  3.841   -15.071 1.00 46.26  ? 152 ALA D C     1 
ATOM   3780 O O     . ALA D 4 105 ? 24.636  4.337   -15.105 1.00 44.25  ? 152 ALA D O     1 
ATOM   3781 C CB    . ALA D 4 105 ? 26.932  4.563   -12.976 1.00 41.67  ? 152 ALA D CB    1 
ATOM   3782 N N     . ASN D 4 106 ? 26.526  3.714   -16.166 1.00 42.03  ? 153 ASN D N     1 
ATOM   3783 C CA    . ASN D 4 106 ? 26.149  4.249   -17.467 1.00 40.20  ? 153 ASN D CA    1 
ATOM   3784 C C     . ASN D 4 106 ? 25.799  3.185   -18.492 1.00 43.61  ? 153 ASN D C     1 
ATOM   3785 O O     . ASN D 4 106 ? 25.218  3.527   -19.524 1.00 44.64  ? 153 ASN D O     1 
ATOM   3786 C CB    . ASN D 4 106 ? 27.284  5.091   -18.077 1.00 40.61  ? 153 ASN D CB    1 
ATOM   3787 C CG    . ASN D 4 106 ? 27.677  6.285   -17.232 1.00 44.37  ? 153 ASN D CG    1 
ATOM   3788 O OD1   . ASN D 4 106 ? 27.178  6.489   -16.128 1.00 46.88  ? 153 ASN D OD1   1 
ATOM   3789 N ND2   . ASN D 4 106 ? 28.606  7.077   -17.749 1.00 48.70  ? 153 ASN D ND2   1 
ATOM   3790 N N     . ASN D 4 107 ? 26.194  1.930   -18.275 1.00 39.81  ? 154 ASN D N     1 
ATOM   3791 C CA    . ASN D 4 107 ? 25.996  0.892   -19.275 1.00 37.54  ? 154 ASN D CA    1 
ATOM   3792 C C     . ASN D 4 107 ? 25.774  -0.445  -18.588 1.00 40.09  ? 154 ASN D C     1 
ATOM   3793 O O     . ASN D 4 107 ? 26.479  -0.798  -17.634 1.00 35.49  ? 154 ASN D O     1 
ATOM   3794 C CB    . ASN D 4 107 ? 27.184  0.777   -20.238 1.00 43.65  ? 154 ASN D CB    1 
ATOM   3795 C CG    . ASN D 4 107 ? 27.279  1.946   -21.202 1.00 45.61  ? 154 ASN D CG    1 
ATOM   3796 O OD1   . ASN D 4 107 ? 28.011  2.898   -20.960 1.00 50.83  ? 154 ASN D OD1   1 
ATOM   3797 N ND2   . ASN D 4 107 ? 26.547  1.873   -22.302 1.00 44.89  ? 154 ASN D ND2   1 
ATOM   3798 N N     . ALA D 4 108 ? 24.775  -1.172  -19.085 1.00 39.52  ? 155 ALA D N     1 
ATOM   3799 C CA    . ALA D 4 108 ? 24.506  -2.517  -18.613 1.00 39.20  ? 155 ALA D CA    1 
ATOM   3800 C C     . ALA D 4 108 ? 25.567  -3.493  -19.122 1.00 38.46  ? 155 ALA D C     1 
ATOM   3801 O O     . ALA D 4 108 ? 26.166  -3.309  -20.184 1.00 37.09  ? 155 ALA D O     1 
ATOM   3802 C CB    . ALA D 4 108 ? 23.117  -2.974  -19.064 1.00 37.16  ? 155 ALA D CB    1 
ATOM   3803 N N     . ALA D 4 109 ? 25.774  -4.546  -18.347 1.00 33.95  ? 156 ALA D N     1 
ATOM   3804 C CA    . ALA D 4 109 ? 26.637  -5.641  -18.744 1.00 34.43  ? 156 ALA D CA    1 
ATOM   3805 C C     . ALA D 4 109 ? 26.118  -6.313  -20.011 1.00 37.55  ? 156 ALA D C     1 
ATOM   3806 O O     . ALA D 4 109 ? 24.912  -6.376  -20.268 1.00 39.68  ? 156 ALA D O     1 
ATOM   3807 C CB    . ALA D 4 109 ? 26.733  -6.655  -17.596 1.00 32.56  ? 156 ALA D CB    1 
ATOM   3808 N N     . ILE D 4 110 ? 27.047  -6.788  -20.824 1.00 36.65  ? 157 ILE D N     1 
ATOM   3809 C CA    . ILE D 4 110 ? 26.717  -7.652  -21.951 1.00 37.94  ? 157 ILE D CA    1 
ATOM   3810 C C     . ILE D 4 110 ? 26.573  -9.078  -21.447 1.00 41.76  ? 157 ILE D C     1 
ATOM   3811 O O     . ILE D 4 110 ? 27.397  -9.550  -20.654 1.00 37.23  ? 157 ILE D O     1 
ATOM   3812 C CB    . ILE D 4 110 ? 27.796  -7.569  -23.038 1.00 37.41  ? 157 ILE D CB    1 
ATOM   3813 C CG1   . ILE D 4 110 ? 28.019  -6.125  -23.468 1.00 36.52  ? 157 ILE D CG1   1 
ATOM   3814 C CG2   . ILE D 4 110 ? 27.426  -8.454  -24.223 1.00 41.77  ? 157 ILE D CG2   1 
ATOM   3815 C CD1   . ILE D 4 110 ? 29.235  -5.963  -24.343 1.00 38.56  ? 157 ILE D CD1   1 
ATOM   3816 N N     . VAL D 4 111 ? 25.519  -9.773  -21.890 1.00 39.11  ? 158 VAL D N     1 
ATOM   3817 C CA    . VAL D 4 111 ? 25.367  -11.172 -21.520 1.00 38.01  ? 158 VAL D CA    1 
ATOM   3818 C C     . VAL D 4 111 ? 26.444  -12.007 -22.210 1.00 41.16  ? 158 VAL D C     1 
ATOM   3819 O O     . VAL D 4 111 ? 26.725  -11.836 -23.403 1.00 42.16  ? 158 VAL D O     1 
ATOM   3820 C CB    . VAL D 4 111 ? 23.960  -11.685 -21.864 1.00 39.93  ? 158 VAL D CB    1 
ATOM   3821 C CG1   . VAL D 4 111 ? 23.821  -13.083 -21.347 1.00 38.90  ? 158 VAL D CG1   1 
ATOM   3822 C CG2   . VAL D 4 111 ? 22.886  -10.786 -21.235 1.00 32.54  ? 158 VAL D CG2   1 
ATOM   3823 N N     . LEU D 4 112 ? 27.050  -12.922 -21.454 1.00 39.44  ? 159 LEU D N     1 
ATOM   3824 C CA    . LEU D 4 112 ? 28.238  -13.653 -21.885 1.00 38.20  ? 159 LEU D CA    1 
ATOM   3825 C C     . LEU D 4 112 ? 27.843  -14.795 -22.822 1.00 39.60  ? 159 LEU D C     1 
ATOM   3826 O O     . LEU D 4 112 ? 27.224  -15.773 -22.392 1.00 45.24  ? 159 LEU D O     1 
ATOM   3827 C CB    . LEU D 4 112 ? 28.973  -14.174 -20.651 1.00 39.07  ? 159 LEU D CB    1 
ATOM   3828 C CG    . LEU D 4 112 ? 30.494  -14.357 -20.672 1.00 40.12  ? 159 LEU D CG    1 
ATOM   3829 C CD1   . LEU D 4 112 ? 30.946  -14.861 -19.330 1.00 46.26  ? 159 LEU D CD1   1 
ATOM   3830 C CD2   . LEU D 4 112 ? 30.950  -15.324 -21.751 1.00 43.99  ? 159 LEU D CD2   1 
ATOM   3831 N N     . GLN D 4 113 ? 28.198  -14.672 -24.099 1.00 41.77  ? 160 GLN D N     1 
ATOM   3832 C CA    . GLN D 4 113 ? 27.979  -15.702 -25.110 1.00 44.96  ? 160 GLN D CA    1 
ATOM   3833 C C     . GLN D 4 113 ? 29.327  -16.240 -25.557 1.00 51.55  ? 160 GLN D C     1 
ATOM   3834 O O     . GLN D 4 113 ? 30.161  -15.478 -26.063 1.00 50.17  ? 160 GLN D O     1 
ATOM   3835 C CB    . GLN D 4 113 ? 27.248  -15.149 -26.333 1.00 50.41  ? 160 GLN D CB    1 
ATOM   3836 C CG    . GLN D 4 113 ? 25.956  -14.431 -26.040 1.00 57.01  ? 160 GLN D CG    1 
ATOM   3837 C CD    . GLN D 4 113 ? 24.762  -15.366 -25.959 1.00 60.36  ? 160 GLN D CD    1 
ATOM   3838 O OE1   . GLN D 4 113 ? 24.901  -16.597 -25.942 1.00 58.22  ? 160 GLN D OE1   1 
ATOM   3839 N NE2   . GLN D 4 113 ? 23.575  -14.779 -25.913 1.00 59.39  ? 160 GLN D NE2   1 
ATOM   3840 N N     . LEU D 4 114 ? 29.529  -17.539 -25.398 1.00 48.90  ? 161 LEU D N     1 
ATOM   3841 C CA    . LEU D 4 114 ? 30.760  -18.081 -25.938 1.00 44.72  ? 161 LEU D CA    1 
ATOM   3842 C C     . LEU D 4 114 ? 30.547  -18.542 -27.374 1.00 52.15  ? 161 LEU D C     1 
ATOM   3843 O O     . LEU D 4 114 ? 29.445  -18.959 -27.744 1.00 51.25  ? 161 LEU D O     1 
ATOM   3844 C CB    . LEU D 4 114 ? 31.243  -19.238 -25.086 1.00 45.95  ? 161 LEU D CB    1 
ATOM   3845 C CG    . LEU D 4 114 ? 31.475  -18.820 -23.640 1.00 44.41  ? 161 LEU D CG    1 
ATOM   3846 C CD1   . LEU D 4 114 ? 31.737  -19.998 -22.733 1.00 44.37  ? 161 LEU D CD1   1 
ATOM   3847 C CD2   . LEU D 4 114 ? 32.648  -17.870 -23.596 1.00 47.53  ? 161 LEU D CD2   1 
ATOM   3848 N N     . PRO D 4 115 ? 31.594  -18.472 -28.200 1.00 57.48  ? 162 PRO D N     1 
ATOM   3849 C CA    . PRO D 4 115 ? 31.425  -18.751 -29.631 1.00 58.81  ? 162 PRO D CA    1 
ATOM   3850 C C     . PRO D 4 115 ? 31.096  -20.208 -29.928 1.00 58.80  ? 162 PRO D C     1 
ATOM   3851 O O     . PRO D 4 115 ? 31.023  -21.042 -29.020 1.00 61.35  ? 162 PRO D O     1 
ATOM   3852 C CB    . PRO D 4 115 ? 32.787  -18.350 -30.224 1.00 60.17  ? 162 PRO D CB    1 
ATOM   3853 C CG    . PRO D 4 115 ? 33.452  -17.479 -29.164 1.00 52.10  ? 162 PRO D CG    1 
ATOM   3854 C CD    . PRO D 4 115 ? 32.978  -18.072 -27.878 1.00 55.38  ? 162 PRO D CD    1 
ATOM   3855 N N     . GLN D 4 116 ? 30.895  -20.517 -31.207 1.00 60.21  ? 163 GLN D N     1 
ATOM   3856 C CA    . GLN D 4 116 ? 30.698  -21.898 -31.627 1.00 61.07  ? 163 GLN D CA    1 
ATOM   3857 C C     . GLN D 4 116 ? 31.868  -22.749 -31.161 1.00 65.44  ? 163 GLN D C     1 
ATOM   3858 O O     . GLN D 4 116 ? 33.018  -22.296 -31.147 1.00 65.68  ? 163 GLN D O     1 
ATOM   3859 C CB    . GLN D 4 116 ? 30.590  -21.989 -33.153 1.00 65.42  ? 163 GLN D CB    1 
ATOM   3860 C CG    . GLN D 4 116 ? 29.659  -20.975 -33.807 1.00 68.71  ? 163 GLN D CG    1 
ATOM   3861 C CD    . GLN D 4 116 ? 30.265  -19.580 -33.998 1.00 71.97  ? 163 GLN D CD    1 
ATOM   3862 O OE1   . GLN D 4 116 ? 30.433  -18.816 -33.035 1.00 67.80  ? 163 GLN D OE1   1 
ATOM   3863 N NE2   . GLN D 4 116 ? 30.569  -19.235 -35.253 1.00 69.67  ? 163 GLN D NE2   1 
ATOM   3864 N N     . GLY D 4 117 ? 31.570  -23.982 -30.761 1.00 60.76  ? 164 GLY D N     1 
ATOM   3865 C CA    . GLY D 4 117 ? 32.645  -24.900 -30.437 1.00 71.99  ? 164 GLY D CA    1 
ATOM   3866 C C     . GLY D 4 117 ? 33.470  -24.530 -29.227 1.00 68.03  ? 164 GLY D C     1 
ATOM   3867 O O     . GLY D 4 117 ? 34.556  -25.092 -29.033 1.00 67.45  ? 164 GLY D O     1 
ATOM   3868 N N     . THR D 4 118 ? 33.003  -23.581 -28.424 1.00 61.81  ? 165 THR D N     1 
ATOM   3869 C CA    . THR D 4 118 ? 33.525  -23.351 -27.089 1.00 63.32  ? 165 THR D CA    1 
ATOM   3870 C C     . THR D 4 118 ? 32.496  -23.890 -26.110 1.00 65.83  ? 165 THR D C     1 
ATOM   3871 O O     . THR D 4 118 ? 31.296  -23.635 -26.266 1.00 60.38  ? 165 THR D O     1 
ATOM   3872 C CB    . THR D 4 118 ? 33.798  -21.868 -26.842 1.00 62.94  ? 165 THR D CB    1 
ATOM   3873 O OG1   . THR D 4 118 ? 34.703  -21.365 -27.843 1.00 61.79  ? 165 THR D OG1   1 
ATOM   3874 C CG2   . THR D 4 118 ? 34.405  -21.675 -25.460 1.00 60.00  ? 165 THR D CG2   1 
ATOM   3875 N N     . THR D 4 119 ? 32.957  -24.674 -25.137 1.00 67.97  ? 166 THR D N     1 
ATOM   3876 C CA    . THR D 4 119 ? 32.068  -25.395 -24.235 1.00 66.97  ? 166 THR D CA    1 
ATOM   3877 C C     . THR D 4 119 ? 32.441  -25.093 -22.793 1.00 64.46  ? 166 THR D C     1 
ATOM   3878 O O     . THR D 4 119 ? 33.619  -25.144 -22.427 1.00 63.95  ? 166 THR D O     1 
ATOM   3879 C CB    . THR D 4 119 ? 32.129  -26.903 -24.492 1.00 66.74  ? 166 THR D CB    1 
ATOM   3880 O OG1   . THR D 4 119 ? 31.963  -27.147 -25.894 1.00 71.30  ? 166 THR D OG1   1 
ATOM   3881 C CG2   . THR D 4 119 ? 31.027  -27.621 -23.727 1.00 63.50  ? 166 THR D CG2   1 
ATOM   3882 N N     . LEU D 4 120 ? 31.438  -24.779 -21.988 1.00 65.04  ? 167 LEU D N     1 
ATOM   3883 C CA    . LEU D 4 120 ? 31.666  -24.538 -20.574 1.00 61.43  ? 167 LEU D CA    1 
ATOM   3884 C C     . LEU D 4 120 ? 32.190  -25.799 -19.907 1.00 61.73  ? 167 LEU D C     1 
ATOM   3885 O O     . LEU D 4 120 ? 31.561  -26.862 -20.015 1.00 61.07  ? 167 LEU D O     1 
ATOM   3886 C CB    . LEU D 4 120 ? 30.376  -24.094 -19.890 1.00 62.40  ? 167 LEU D CB    1 
ATOM   3887 C CG    . LEU D 4 120 ? 30.122  -22.596 -19.931 1.00 59.11  ? 167 LEU D CG    1 
ATOM   3888 C CD1   . LEU D 4 120 ? 28.837  -22.250 -19.197 1.00 56.58  ? 167 LEU D CD1   1 
ATOM   3889 C CD2   . LEU D 4 120 ? 31.319  -21.891 -19.322 1.00 53.20  ? 167 LEU D CD2   1 
ATOM   3890 N N     . PRO D 4 121 ? 33.315  -25.738 -19.219 1.00 65.27  ? 168 PRO D N     1 
ATOM   3891 C CA    . PRO D 4 121 ? 33.773  -26.902 -18.451 1.00 63.48  ? 168 PRO D CA    1 
ATOM   3892 C C     . PRO D 4 121 ? 32.825  -27.277 -17.318 1.00 59.95  ? 168 PRO D C     1 
ATOM   3893 O O     . PRO D 4 121 ? 31.823  -26.598 -17.086 1.00 59.53  ? 168 PRO D O     1 
ATOM   3894 C CB    . PRO D 4 121 ? 35.139  -26.451 -17.925 1.00 63.23  ? 168 PRO D CB    1 
ATOM   3895 C CG    . PRO D 4 121 ? 35.602  -25.447 -18.949 1.00 61.45  ? 168 PRO D CG    1 
ATOM   3896 C CD    . PRO D 4 121 ? 34.364  -24.712 -19.364 1.00 54.86  ? 168 PRO D CD    1 
ATOM   3897 N N     . LYS D 4 122 ? 33.141  -28.360 -16.612 1.00 64.77  ? 169 LYS D N     1 
ATOM   3898 C CA    . LYS D 4 122 ? 32.268  -28.875 -15.565 1.00 62.38  ? 169 LYS D CA    1 
ATOM   3899 C C     . LYS D 4 122 ? 32.049  -27.829 -14.481 1.00 64.28  ? 169 LYS D C     1 
ATOM   3900 O O     . LYS D 4 122 ? 32.985  -27.154 -14.050 1.00 65.55  ? 169 LYS D O     1 
ATOM   3901 C CB    . LYS D 4 122 ? 32.879  -30.145 -14.963 1.00 67.84  ? 169 LYS D CB    1 
ATOM   3902 C CG    . LYS D 4 122 ? 31.917  -31.030 -14.178 1.00 70.25  ? 169 LYS D CG    1 
ATOM   3903 C CD    . LYS D 4 122 ? 32.520  -32.417 -13.959 1.00 74.91  ? 169 LYS D CD    1 
ATOM   3904 C CE    . LYS D 4 122 ? 31.480  -33.429 -13.501 1.00 76.23  ? 169 LYS D CE    1 
ATOM   3905 N NZ    . LYS D 4 122 ? 32.044  -34.802 -13.401 1.00 74.49  ? 169 LYS D NZ    1 
ATOM   3906 N N     . GLY D 4 123 ? 30.796  -27.685 -14.053 1.00 63.50  ? 170 GLY D N     1 
ATOM   3907 C CA    . GLY D 4 123 ? 30.473  -26.832 -12.926 1.00 63.60  ? 170 GLY D CA    1 
ATOM   3908 C C     . GLY D 4 123 ? 30.491  -25.342 -13.176 1.00 62.11  ? 170 GLY D C     1 
ATOM   3909 O O     . GLY D 4 123 ? 30.658  -24.580 -12.221 1.00 62.81  ? 170 GLY D O     1 
ATOM   3910 N N     . PHE D 4 124 ? 30.323  -24.898 -14.425 1.00 58.51  ? 171 PHE D N     1 
ATOM   3911 C CA    . PHE D 4 124 ? 30.243  -23.486 -14.769 1.00 53.56  ? 171 PHE D CA    1 
ATOM   3912 C C     . PHE D 4 124 ? 28.925  -23.191 -15.478 1.00 58.24  ? 171 PHE D C     1 
ATOM   3913 O O     . PHE D 4 124 ? 28.429  -24.011 -16.251 1.00 58.05  ? 171 PHE D O     1 
ATOM   3914 C CB    . PHE D 4 124 ? 31.413  -23.056 -15.672 1.00 57.77  ? 171 PHE D CB    1 
ATOM   3915 C CG    . PHE D 4 124 ? 32.768  -23.154 -15.009 1.00 61.91  ? 171 PHE D CG    1 
ATOM   3916 C CD1   . PHE D 4 124 ? 33.481  -24.346 -15.031 1.00 58.36  ? 171 PHE D CD1   1 
ATOM   3917 C CD2   . PHE D 4 124 ? 33.330  -22.055 -14.367 1.00 53.32  ? 171 PHE D CD2   1 
ATOM   3918 C CE1   . PHE D 4 124 ? 34.705  -24.439 -14.423 1.00 57.25  ? 171 PHE D CE1   1 
ATOM   3919 C CE2   . PHE D 4 124 ? 34.566  -22.151 -13.761 1.00 49.08  ? 171 PHE D CE2   1 
ATOM   3920 C CZ    . PHE D 4 124 ? 35.246  -23.339 -13.784 1.00 52.18  ? 171 PHE D CZ    1 
ATOM   3921 N N     . TYR D 4 125 ? 28.367  -22.003 -15.227 1.00 54.29  ? 172 TYR D N     1 
ATOM   3922 C CA    . TYR D 4 125 ? 27.139  -21.576 -15.887 1.00 55.78  ? 172 TYR D CA    1 
ATOM   3923 C C     . TYR D 4 125 ? 27.087  -20.052 -15.954 1.00 49.73  ? 172 TYR D C     1 
ATOM   3924 O O     . TYR D 4 125 ? 27.935  -19.357 -15.398 1.00 49.85  ? 172 TYR D O     1 
ATOM   3925 C CB    . TYR D 4 125 ? 25.897  -22.140 -15.168 1.00 50.11  ? 172 TYR D CB    1 
ATOM   3926 C CG    . TYR D 4 125 ? 25.629  -21.588 -13.777 1.00 48.94  ? 172 TYR D CG    1 
ATOM   3927 C CD1   . TYR D 4 125 ? 24.988  -20.365 -13.603 1.00 49.54  ? 172 TYR D CD1   1 
ATOM   3928 C CD2   . TYR D 4 125 ? 25.983  -22.306 -12.640 1.00 50.67  ? 172 TYR D CD2   1 
ATOM   3929 C CE1   . TYR D 4 125 ? 24.725  -19.851 -12.332 1.00 49.19  ? 172 TYR D CE1   1 
ATOM   3930 C CE2   . TYR D 4 125 ? 25.722  -21.807 -11.360 1.00 50.31  ? 172 TYR D CE2   1 
ATOM   3931 C CZ    . TYR D 4 125 ? 25.093  -20.574 -11.211 1.00 51.68  ? 172 TYR D CZ    1 
ATOM   3932 O OH    . TYR D 4 125 ? 24.828  -20.059 -9.950  1.00 50.90  ? 172 TYR D OH    1 
ATOM   3933 N N     . ALA D 4 126 ? 26.057  -19.549 -16.642 1.00 58.02  ? 173 ALA D N     1 
ATOM   3934 C CA    . ALA D 4 126 ? 25.640  -18.133 -16.672 1.00 56.15  ? 173 ALA D CA    1 
ATOM   3935 C C     . ALA D 4 126 ? 26.011  -17.312 -15.442 1.00 54.12  ? 173 ALA D C     1 
ATOM   3936 O O     . ALA D 4 126 ? 25.543  -16.182 -15.278 1.00 53.50  ? 173 ALA D O     1 
ATOM   3937 C CB    . ALA D 4 126 ? 24.104  -18.046 -16.879 1.00 47.59  ? 173 ALA D CB    1 
HETATM 3938 O OP3   . U   E 5 .   ? 17.737  -14.255 -23.677 0.73 43.47  ? 201 U   A OP3   1 
HETATM 3939 P P     . U   E 5 .   ? 16.426  -13.918 -22.820 0.73 56.31  ? 201 U   A P     1 
HETATM 3940 O OP1   . U   E 5 .   ? 16.573  -14.773 -21.616 0.73 51.70  ? 201 U   A OP1   1 
HETATM 3941 O OP2   . U   E 5 .   ? 15.170  -14.013 -23.616 0.73 55.54  ? 201 U   A OP2   1 
HETATM 3942 O "O5'" . U   E 5 .   ? 16.537  -12.405 -22.324 0.73 55.45  ? 201 U   A "O5'" 1 
HETATM 3943 C "C5'" . U   E 5 .   ? 16.792  -11.342 -23.246 0.73 49.26  ? 201 U   A "C5'" 1 
HETATM 3944 C "C4'" . U   E 5 .   ? 16.827  -10.000 -22.561 0.73 42.72  ? 201 U   A "C4'" 1 
HETATM 3945 O "O4'" . U   E 5 .   ? 15.578  -9.813  -21.850 0.73 42.00  ? 201 U   A "O4'" 1 
HETATM 3946 C "C3'" . U   E 5 .   ? 17.936  -9.819  -21.526 0.73 44.88  ? 201 U   A "C3'" 1 
HETATM 3947 O "O3'" . U   E 5 .   ? 18.373  -8.462  -21.550 0.73 52.24  ? 201 U   A "O3'" 1 
HETATM 3948 C "C2'" . U   E 5 .   ? 17.218  -10.101 -20.208 0.73 45.23  ? 201 U   A "C2'" 1 
HETATM 3949 O "O2'" . U   E 5 .   ? 17.801  -9.499  -19.070 0.73 43.22  ? 201 U   A "O2'" 1 
HETATM 3950 C "C1'" . U   E 5 .   ? 15.838  -9.528  -20.492 0.73 40.32  ? 201 U   A "C1'" 1 
HETATM 3951 N N1    . U   E 5 .   ? 14.761  -10.112 -19.680 0.73 41.37  ? 201 U   A N1    1 
HETATM 3952 C C2    . U   E 5 .   ? 13.720  -9.248  -19.398 0.73 36.87  ? 201 U   A C2    1 
HETATM 3953 O O2    . U   E 5 .   ? 13.711  -8.095  -19.802 0.73 33.97  ? 201 U   A O2    1 
HETATM 3954 N N3    . U   E 5 .   ? 12.707  -9.774  -18.640 0.73 33.63  ? 201 U   A N3    1 
HETATM 3955 C C4    . U   E 5 .   ? 12.647  -11.055 -18.144 0.73 39.67  ? 201 U   A C4    1 
HETATM 3956 O O4    . U   E 5 .   ? 11.664  -11.363 -17.463 0.73 38.65  ? 201 U   A O4    1 
HETATM 3957 C C5    . U   E 5 .   ? 13.772  -11.901 -18.475 0.73 40.41  ? 201 U   A C5    1 
HETATM 3958 C C6    . U   E 5 .   ? 14.774  -11.413 -19.219 0.73 39.03  ? 201 U   A C6    1 
HETATM 3959 P P     . PO4 F 6 .   ? 1.257   -36.333 -15.203 0.68 53.70  ? 201 PO4 B P     1 
HETATM 3960 O O1    . PO4 F 6 .   ? 2.568   -36.397 -14.435 0.68 54.21  ? 201 PO4 B O1    1 
HETATM 3961 O O2    . PO4 F 6 .   ? 1.341   -35.271 -16.268 0.68 47.64  ? 201 PO4 B O2    1 
HETATM 3962 O O3    . PO4 F 6 .   ? 1.008   -37.654 -15.896 0.68 41.97  ? 201 PO4 B O3    1 
HETATM 3963 O O4    . PO4 F 6 .   ? 0.128   -35.963 -14.253 0.68 51.01  ? 201 PO4 B O4    1 
HETATM 3964 O O     . HOH G 7 .   ? 9.983   -7.159  -0.435  1.00 45.49  ? 301 HOH A O     1 
HETATM 3965 O O     . HOH G 7 .   ? 24.032  -5.620  -11.064 1.00 47.25  ? 302 HOH A O     1 
HETATM 3966 O O     . HOH G 7 .   ? 19.919  -4.048  -12.069 1.00 38.50  ? 303 HOH A O     1 
HETATM 3967 O O     . HOH G 7 .   ? 5.519   9.095   -5.427  1.00 40.58  ? 304 HOH A O     1 
HETATM 3968 O O     . HOH G 7 .   ? -4.862  0.146   -14.736 1.00 29.85  ? 305 HOH A O     1 
HETATM 3969 O O     . HOH G 7 .   ? 1.751   13.128  -13.880 1.00 38.23  ? 306 HOH A O     1 
HETATM 3970 O O     . HOH G 7 .   ? -1.956  -10.424 -18.693 1.00 32.52  ? 307 HOH A O     1 
HETATM 3971 O O     . HOH G 7 .   ? 9.909   -10.725 -15.927 1.00 39.64  ? 308 HOH A O     1 
HETATM 3972 O O     . HOH G 7 .   ? 15.026  -26.658 -6.046  1.00 53.75  ? 309 HOH A O     1 
HETATM 3973 O O     . HOH G 7 .   ? 1.057   8.380   -19.969 1.00 41.30  ? 310 HOH A O     1 
HETATM 3974 O O     . HOH G 7 .   ? 3.821   -13.260 -15.595 1.00 44.50  ? 311 HOH A O     1 
HETATM 3975 O O     . HOH G 7 .   ? 4.894   11.006  -12.042 1.00 40.19  ? 312 HOH A O     1 
HETATM 3976 O O     . HOH G 7 .   ? 3.341   -1.292  -0.953  1.00 50.53  ? 313 HOH A O     1 
HETATM 3977 O O     . HOH G 7 .   ? 13.103  -10.448 -28.513 1.00 51.61  ? 314 HOH A O     1 
HETATM 3978 O O     . HOH G 7 .   ? 18.278  -3.929  -0.216  1.00 48.77  ? 315 HOH A O     1 
HETATM 3979 O O     . HOH G 7 .   ? 10.136  5.698   -15.927 1.00 32.29  ? 316 HOH A O     1 
HETATM 3980 O O     . HOH G 7 .   ? 3.394   -11.991 -2.280  1.00 47.07  ? 317 HOH A O     1 
HETATM 3981 O O     . HOH G 7 .   ? -0.115  -9.112  -7.805  1.00 34.08  ? 318 HOH A O     1 
HETATM 3982 O O     . HOH G 7 .   ? 16.460  3.545   -14.321 1.00 37.63  ? 319 HOH A O     1 
HETATM 3983 O O     . HOH G 7 .   ? 7.775   -1.780  -20.621 1.00 21.42  ? 320 HOH A O     1 
HETATM 3984 O O     . HOH G 7 .   ? 10.344  -1.832  -19.429 1.00 24.67  ? 321 HOH A O     1 
HETATM 3985 O O     . HOH G 7 .   ? 4.610   -7.592  -2.843  1.00 46.26  ? 322 HOH A O     1 
HETATM 3986 O O     . HOH G 7 .   ? 22.959  0.444   -20.798 1.00 41.71  ? 323 HOH A O     1 
HETATM 3987 O O     . HOH G 7 .   ? 14.775  -10.115 -0.646  1.00 52.01  ? 324 HOH A O     1 
HETATM 3988 O O     . HOH G 7 .   ? 6.642   -14.691 -13.272 1.00 38.23  ? 325 HOH A O     1 
HETATM 3989 O O     . HOH G 7 .   ? 12.033  5.911   1.480   1.00 52.97  ? 326 HOH A O     1 
HETATM 3990 O O     . HOH G 7 .   ? 14.945  -18.459 -9.429  1.00 47.48  ? 327 HOH A O     1 
HETATM 3991 O O     . HOH G 7 .   ? 8.830   -0.248  -27.808 1.00 37.93  ? 328 HOH A O     1 
HETATM 3992 O O     . HOH G 7 .   ? 11.398  5.241   -6.081  1.00 52.34  ? 329 HOH A O     1 
HETATM 3993 O O     . HOH G 7 .   ? 17.566  -12.651 -25.901 1.00 55.91  ? 330 HOH A O     1 
HETATM 3994 O O     . HOH G 7 .   ? -0.040  -4.075  -16.934 1.00 25.24  ? 331 HOH A O     1 
HETATM 3995 O O     . HOH G 7 .   ? 5.057   -15.612 -3.942  1.00 47.30  ? 332 HOH A O     1 
HETATM 3996 O O     . HOH G 7 .   ? 13.985  -3.958  -14.945 1.00 30.87  ? 333 HOH A O     1 
HETATM 3997 O O     . HOH G 7 .   ? 20.696  -6.067  -26.050 1.00 40.98  ? 334 HOH A O     1 
HETATM 3998 O O     . HOH G 7 .   ? 20.056  -13.217 -22.531 1.00 43.13  ? 335 HOH A O     1 
HETATM 3999 O O     . HOH G 7 .   ? 21.173  -5.028  -21.941 1.00 34.21  ? 336 HOH A O     1 
HETATM 4000 O O     . HOH G 7 .   ? 13.905  -1.407  -28.668 1.00 37.43  ? 337 HOH A O     1 
HETATM 4001 O O     . HOH G 7 .   ? 4.671   2.667   -5.542  1.00 38.67  ? 338 HOH A O     1 
HETATM 4002 O O     . HOH G 7 .   ? 10.353  7.681   -11.822 1.00 43.79  ? 339 HOH A O     1 
HETATM 4003 O O     . HOH G 7 .   ? 5.078   -3.033  -4.242  1.00 43.33  ? 340 HOH A O     1 
HETATM 4004 O O     . HOH G 7 .   ? 14.214  12.715  0.497   1.00 44.21  ? 341 HOH A O     1 
HETATM 4005 O O     . HOH G 7 .   ? -3.428  -3.035  -18.636 1.00 28.60  ? 342 HOH A O     1 
HETATM 4006 O O     . HOH G 7 .   ? -1.965  -2.401  -23.255 1.00 33.47  ? 343 HOH A O     1 
HETATM 4007 O O     . HOH G 7 .   ? 18.922  1.913   -23.698 1.00 42.05  ? 344 HOH A O     1 
HETATM 4008 O O     . HOH G 7 .   ? -7.292  4.540   -18.667 1.00 38.09  ? 345 HOH A O     1 
HETATM 4009 O O     . HOH G 7 .   ? 20.086  -6.851  -23.814 1.00 34.86  ? 346 HOH A O     1 
HETATM 4010 O O     . HOH G 7 .   ? 16.005  -6.223  -19.291 1.00 35.34  ? 347 HOH A O     1 
HETATM 4011 O O     . HOH G 7 .   ? 19.959  4.960   -15.802 1.00 39.57  ? 348 HOH A O     1 
HETATM 4012 O O     . HOH G 7 .   ? 10.185  -14.779 -5.041  1.00 46.39  ? 349 HOH A O     1 
HETATM 4013 O O     . HOH G 7 .   ? -6.934  -5.887  -20.608 1.00 28.84  ? 350 HOH A O     1 
HETATM 4014 O O     . HOH G 7 .   ? 10.044  12.571  -21.632 1.00 54.81  ? 351 HOH A O     1 
HETATM 4015 O O     . HOH G 7 .   ? 4.525   -5.257  -24.736 1.00 28.22  ? 352 HOH A O     1 
HETATM 4016 O O     . HOH G 7 .   ? 17.972  6.371   -16.200 1.00 44.60  ? 353 HOH A O     1 
HETATM 4017 O O     . HOH G 7 .   ? 5.810   10.308  -23.124 1.00 40.89  ? 354 HOH A O     1 
HETATM 4018 O O     . HOH G 7 .   ? 15.942  5.796   -23.154 1.00 52.95  ? 355 HOH A O     1 
HETATM 4019 O O     . HOH G 7 .   ? 9.790   -9.562  -21.789 1.00 39.99  ? 356 HOH A O     1 
HETATM 4020 O O     . HOH G 7 .   ? 8.368   5.711   -7.968  1.00 41.61  ? 357 HOH A O     1 
HETATM 4021 O O     . HOH G 7 .   ? 10.410  8.701   -1.977  1.00 50.33  ? 358 HOH A O     1 
HETATM 4022 O O     . HOH G 7 .   ? 4.171   -13.672 -12.786 1.00 44.59  ? 359 HOH A O     1 
HETATM 4023 O O     . HOH G 7 .   ? -1.422  -16.151 -8.775  1.00 36.07  ? 360 HOH A O     1 
HETATM 4024 O O     . HOH G 7 .   ? 2.373   11.551  -21.424 1.00 51.87  ? 361 HOH A O     1 
HETATM 4025 O O     . HOH G 7 .   ? 8.908   -15.119 -15.664 1.00 46.20  ? 362 HOH A O     1 
HETATM 4026 O O     . HOH G 7 .   ? -3.630  -13.483 -15.806 1.00 41.27  ? 363 HOH A O     1 
HETATM 4027 O O     . HOH G 7 .   ? 1.600   -5.020  -5.415  1.00 31.98  ? 364 HOH A O     1 
HETATM 4028 O O     . HOH G 7 .   ? 21.888  -17.302 -7.933  1.00 45.67  ? 365 HOH A O     1 
HETATM 4029 O O     . HOH G 7 .   ? 9.151   12.271  -15.142 1.00 40.86  ? 366 HOH A O     1 
HETATM 4030 O O     . HOH G 7 .   ? 19.491  -8.735  -15.607 1.00 34.41  ? 367 HOH A O     1 
HETATM 4031 O O     . HOH G 7 .   ? -0.603  7.643   -21.976 1.00 42.53  ? 368 HOH A O     1 
HETATM 4032 O O     . HOH G 7 .   ? 5.050   -3.039  -26.486 1.00 37.59  ? 369 HOH A O     1 
HETATM 4033 O O     . HOH G 7 .   ? 2.005   -3.051  -1.545  1.00 53.32  ? 370 HOH A O     1 
HETATM 4034 O O     . HOH G 7 .   ? -0.189  11.121  -20.729 1.00 46.50  ? 371 HOH A O     1 
HETATM 4035 O O     . HOH G 7 .   ? 20.330  -11.857 -24.741 1.00 49.50  ? 372 HOH A O     1 
HETATM 4036 O O     . HOH G 7 .   ? -3.102  -0.746  -18.788 1.00 29.78  ? 373 HOH A O     1 
HETATM 4037 O O     . HOH G 7 .   ? 0.041   -8.531  -3.001  1.00 47.12  ? 374 HOH A O     1 
HETATM 4038 O O     . HOH G 7 .   ? -0.171  -7.199  -5.760  1.00 36.52  ? 375 HOH A O     1 
HETATM 4039 O O     . HOH G 7 .   ? -4.156  -1.976  -21.512 1.00 36.42  ? 376 HOH A O     1 
HETATM 4040 O O     . HOH G 7 .   ? 19.892  -13.229 -20.070 1.00 41.80  ? 377 HOH A O     1 
HETATM 4041 O O     . HOH G 7 .   ? -5.583  -4.090  -21.714 1.00 35.48  ? 378 HOH A O     1 
HETATM 4042 O O     . HOH G 7 .   ? -0.922  -4.332  -5.578  1.00 46.16  ? 379 HOH A O     1 
HETATM 4043 O O     . HOH G 7 .   ? -3.768  -12.842 -18.378 1.00 38.61  ? 380 HOH A O     1 
HETATM 4044 O O     . HOH G 7 .   ? 23.413  -14.850 -2.325  1.00 43.83  ? 381 HOH A O     1 
HETATM 4045 O O     . HOH G 7 .   ? 22.447  -18.911 -5.692  1.00 44.77  ? 382 HOH A O     1 
HETATM 4046 O O     . HOH G 7 .   ? 3.324   -4.720  -3.455  1.00 45.28  ? 383 HOH A O     1 
HETATM 4047 O O     . HOH G 7 .   ? 20.812  3.507   -21.930 1.00 42.01  ? 384 HOH A O     1 
HETATM 4048 O O     . HOH G 7 .   ? 9.353   12.407  -12.818 1.00 41.97  ? 385 HOH A O     1 
HETATM 4049 O O     . HOH H 7 .   ? 13.987  -43.061 -37.745 1.00 36.23  ? 301 HOH B O     1 
HETATM 4050 O O     . HOH H 7 .   ? 26.066  -24.745 -33.505 1.00 49.67  ? 302 HOH B O     1 
HETATM 4051 O O     . HOH H 7 .   ? 11.957  -50.288 -38.833 1.00 45.31  ? 303 HOH B O     1 
HETATM 4052 O O     . HOH H 7 .   ? 21.932  -25.357 -23.401 1.00 47.83  ? 304 HOH B O     1 
HETATM 4053 O O     . HOH H 7 .   ? 24.303  -31.625 -29.839 1.00 45.80  ? 305 HOH B O     1 
HETATM 4054 O O     . HOH H 7 .   ? 22.632  -17.361 -30.039 1.00 53.34  ? 306 HOH B O     1 
HETATM 4055 O O     . HOH H 7 .   ? 12.890  -36.449 -21.059 1.00 33.78  ? 307 HOH B O     1 
HETATM 4056 O O     . HOH H 7 .   ? 19.750  -35.104 -25.858 1.00 37.70  ? 308 HOH B O     1 
HETATM 4057 O O     . HOH H 7 .   ? 9.571   -27.752 -9.393  1.00 47.55  ? 309 HOH B O     1 
HETATM 4058 O O     . HOH H 7 .   ? 24.347  -27.526 -15.320 1.00 59.85  ? 310 HOH B O     1 
HETATM 4059 O O     . HOH H 7 .   ? 20.794  -38.563 -24.189 1.00 41.94  ? 311 HOH B O     1 
HETATM 4060 O O     . HOH H 7 .   ? 0.410   -34.092 -21.434 1.00 39.90  ? 312 HOH B O     1 
HETATM 4061 O O     . HOH H 7 .   ? -0.760  -27.184 -25.367 1.00 40.77  ? 313 HOH B O     1 
HETATM 4062 O O     . HOH H 7 .   ? 3.368   -32.124 -13.050 1.00 52.88  ? 314 HOH B O     1 
HETATM 4063 O O     . HOH H 7 .   ? 1.755   -35.687 -19.006 1.00 44.51  ? 315 HOH B O     1 
HETATM 4064 O O     . HOH H 7 .   ? 15.006  -20.815 -18.761 1.00 45.28  ? 316 HOH B O     1 
HETATM 4065 O O     . HOH H 7 .   ? 9.035   -36.101 -19.373 1.00 43.21  ? 317 HOH B O     1 
HETATM 4066 O O     . HOH H 7 .   ? 6.413   -46.183 -37.332 1.00 36.08  ? 318 HOH B O     1 
HETATM 4067 O O     . HOH H 7 .   ? 2.866   -36.867 -25.419 1.00 42.29  ? 319 HOH B O     1 
HETATM 4068 O O     . HOH H 7 .   ? 18.445  -20.378 -27.459 1.00 36.94  ? 320 HOH B O     1 
HETATM 4069 O O     . HOH H 7 .   ? 7.205   -16.458 -11.113 1.00 44.01  ? 321 HOH B O     1 
HETATM 4070 O O     . HOH H 7 .   ? 1.606   -34.541 -24.467 1.00 41.41  ? 322 HOH B O     1 
HETATM 4071 O O     . HOH H 7 .   ? 15.037  -38.572 -40.166 1.00 38.24  ? 323 HOH B O     1 
HETATM 4072 O O     . HOH H 7 .   ? 21.880  -25.045 -27.102 1.00 45.80  ? 324 HOH B O     1 
HETATM 4073 O O     . HOH H 7 .   ? 11.620  -33.899 -27.226 1.00 29.38  ? 325 HOH B O     1 
HETATM 4074 O O     . HOH H 7 .   ? 11.864  -37.077 -41.169 1.00 49.58  ? 326 HOH B O     1 
HETATM 4075 O O     . HOH H 7 .   ? -1.526  -26.773 -21.932 1.00 38.94  ? 327 HOH B O     1 
HETATM 4076 O O     . HOH H 7 .   ? 10.211  -24.911 -38.067 1.00 38.49  ? 328 HOH B O     1 
HETATM 4077 O O     . HOH H 7 .   ? -1.038  -19.477 -31.815 1.00 40.43  ? 329 HOH B O     1 
HETATM 4078 O O     . HOH H 7 .   ? 24.944  -21.177 -28.201 1.00 49.12  ? 330 HOH B O     1 
HETATM 4079 O O     . HOH H 7 .   ? 6.819   -24.556 -14.749 1.00 47.93  ? 331 HOH B O     1 
HETATM 4080 O O     . HOH H 7 .   ? 10.692  -31.162 -16.384 1.00 46.29  ? 332 HOH B O     1 
HETATM 4081 O O     . HOH H 7 .   ? 14.472  -41.056 -15.692 1.00 50.96  ? 333 HOH B O     1 
HETATM 4082 O O     . HOH H 7 .   ? 6.095   -18.720 -30.554 1.00 31.36  ? 334 HOH B O     1 
HETATM 4083 O O     . HOH H 7 .   ? 13.497  -32.812 -35.571 1.00 33.75  ? 335 HOH B O     1 
HETATM 4084 O O     . HOH H 7 .   ? 24.428  -17.697 -34.272 1.00 50.41  ? 336 HOH B O     1 
HETATM 4085 O O     . HOH H 7 .   ? 18.239  -43.846 -27.472 1.00 40.67  ? 337 HOH B O     1 
HETATM 4086 O O     . HOH H 7 .   ? 9.960   -44.480 -29.144 1.00 37.75  ? 338 HOH B O     1 
HETATM 4087 O O     . HOH H 7 .   ? 6.092   -43.384 -45.005 1.00 52.68  ? 339 HOH B O     1 
HETATM 4088 O O     . HOH H 7 .   ? 10.278  -47.140 -30.188 1.00 30.81  ? 340 HOH B O     1 
HETATM 4089 O O     . HOH H 7 .   ? 4.261   -25.798 -40.337 1.00 44.60  ? 341 HOH B O     1 
HETATM 4090 O O     . HOH H 7 .   ? 3.857   -43.729 -41.679 1.00 53.96  ? 342 HOH B O     1 
HETATM 4091 O O     . HOH H 7 .   ? 9.903   -38.626 -28.406 1.00 37.03  ? 343 HOH B O     1 
HETATM 4092 O O     . HOH H 7 .   ? 1.532   -25.189 -31.050 1.00 43.66  ? 344 HOH B O     1 
HETATM 4093 O O     . HOH H 7 .   ? 7.455   -19.097 -23.196 1.00 46.69  ? 345 HOH B O     1 
HETATM 4094 O O     . HOH H 7 .   ? 13.269  -33.927 -33.047 1.00 31.57  ? 346 HOH B O     1 
HETATM 4095 O O     . HOH H 7 .   ? 6.241   -35.617 -34.497 1.00 43.48  ? 347 HOH B O     1 
HETATM 4096 O O     . HOH H 7 .   ? 19.499  -41.694 -24.680 1.00 33.49  ? 348 HOH B O     1 
HETATM 4097 O O     . HOH H 7 .   ? 8.863   -38.489 -23.514 1.00 32.34  ? 349 HOH B O     1 
HETATM 4098 O O     . HOH H 7 .   ? 21.509  -15.652 -22.985 1.00 45.38  ? 350 HOH B O     1 
HETATM 4099 O O     . HOH H 7 .   ? 0.764   -26.663 -28.998 1.00 43.73  ? 351 HOH B O     1 
HETATM 4100 O O     . HOH H 7 .   ? 17.949  -43.306 -32.013 1.00 34.05  ? 352 HOH B O     1 
HETATM 4101 O O     . HOH H 7 .   ? 24.462  -18.121 -37.014 1.00 50.19  ? 353 HOH B O     1 
HETATM 4102 O O     . HOH H 7 .   ? 13.641  -19.846 -40.775 1.00 45.09  ? 354 HOH B O     1 
HETATM 4103 O O     . HOH H 7 .   ? 1.413   -26.498 -32.933 1.00 41.38  ? 355 HOH B O     1 
HETATM 4104 O O     . HOH H 7 .   ? 10.664  -17.423 -15.309 1.00 52.32  ? 356 HOH B O     1 
HETATM 4105 O O     . HOH H 7 .   ? 6.188   -34.712 -37.282 1.00 49.03  ? 357 HOH B O     1 
HETATM 4106 O O     . HOH H 7 .   ? 11.926  -44.913 -27.472 1.00 31.56  ? 358 HOH B O     1 
HETATM 4107 O O     . HOH H 7 .   ? 12.844  -19.934 -25.641 1.00 42.76  ? 359 HOH B O     1 
HETATM 4108 O O     . HOH H 7 .   ? 5.041   -32.605 -30.104 1.00 42.20  ? 360 HOH B O     1 
HETATM 4109 O O     . HOH H 7 .   ? 21.669  -29.476 -18.119 1.00 51.76  ? 361 HOH B O     1 
HETATM 4110 O O     . HOH H 7 .   ? 7.373   -37.516 -30.102 1.00 37.05  ? 362 HOH B O     1 
HETATM 4111 O O     . HOH H 7 .   ? 19.125  -29.496 -46.925 1.00 54.11  ? 363 HOH B O     1 
HETATM 4112 O O     . HOH H 7 .   ? -11.013 -33.884 -24.236 1.00 56.43  ? 364 HOH B O     1 
HETATM 4113 O O     . HOH H 7 .   ? 11.506  -23.278 -41.919 1.00 44.76  ? 365 HOH B O     1 
HETATM 4114 O O     . HOH H 7 .   ? 27.187  -29.850 -33.307 1.00 46.66  ? 366 HOH B O     1 
HETATM 4115 O O     . HOH H 7 .   ? 9.740   -15.337 -38.001 1.00 46.39  ? 367 HOH B O     1 
HETATM 4116 O O     . HOH H 7 .   ? 23.259  -28.029 -28.256 1.00 50.04  ? 368 HOH B O     1 
HETATM 4117 O O     . HOH H 7 .   ? 4.438   -36.466 -18.430 1.00 42.44  ? 369 HOH B O     1 
HETATM 4118 O O     . HOH H 7 .   ? 5.119   -20.090 -24.067 1.00 44.64  ? 370 HOH B O     1 
HETATM 4119 O O     . HOH H 7 .   ? 0.406   -26.454 -13.554 1.00 58.71  ? 371 HOH B O     1 
HETATM 4120 O O     . HOH H 7 .   ? 12.584  -35.420 -43.272 1.00 48.68  ? 372 HOH B O     1 
HETATM 4121 O O     . HOH H 7 .   ? 24.462  -29.366 -42.481 1.00 51.16  ? 373 HOH B O     1 
HETATM 4122 O O     . HOH H 7 .   ? 21.387  -28.450 -45.539 1.00 50.06  ? 374 HOH B O     1 
HETATM 4123 O O     . HOH H 7 .   ? -17.329 -42.367 -24.343 1.00 46.84  ? 375 HOH B O     1 
HETATM 4124 O O     . HOH H 7 .   ? 28.021  -26.011 -32.173 1.00 54.68  ? 376 HOH B O     1 
HETATM 4125 O O     . HOH H 7 .   ? 27.174  -27.544 -29.876 1.00 42.16  ? 377 HOH B O     1 
HETATM 4126 O O     . HOH H 7 .   ? 24.963  -15.812 -37.594 1.00 55.64  ? 378 HOH B O     1 
HETATM 4127 O O     . HOH I 7 .   ? 7.084   -37.694 -9.660  1.00 48.43  ? 201 HOH C O     1 
HETATM 4128 O O     . HOH I 7 .   ? 4.157   -58.531 6.462   1.00 44.05  ? 202 HOH C O     1 
HETATM 4129 O O     . HOH I 7 .   ? 4.455   -67.687 -19.056 1.00 57.29  ? 203 HOH C O     1 
HETATM 4130 O O     . HOH I 7 .   ? 0.967   -55.683 -10.261 1.00 39.04  ? 204 HOH C O     1 
HETATM 4131 O O     . HOH I 7 .   ? 4.824   -37.728 -11.944 1.00 47.52  ? 205 HOH C O     1 
HETATM 4132 O O     . HOH I 7 .   ? 3.350   -41.224 -14.659 1.00 35.19  ? 206 HOH C O     1 
HETATM 4133 O O     . HOH I 7 .   ? -5.464  -43.637 -15.263 1.00 44.77  ? 207 HOH C O     1 
HETATM 4134 O O     . HOH I 7 .   ? 4.789   -58.676 -2.843  1.00 43.20  ? 208 HOH C O     1 
HETATM 4135 O O     . HOH I 7 .   ? -0.869  -57.747 -20.452 1.00 41.70  ? 209 HOH C O     1 
HETATM 4136 O O     . HOH I 7 .   ? 7.708   -55.799 -14.152 1.00 47.22  ? 210 HOH C O     1 
HETATM 4137 O O     . HOH I 7 .   ? -4.424  -44.360 -18.537 1.00 46.03  ? 211 HOH C O     1 
HETATM 4138 O O     . HOH I 7 .   ? -0.876  -60.858 -22.398 1.00 39.87  ? 212 HOH C O     1 
HETATM 4139 O O     . HOH I 7 .   ? 6.345   -58.611 -24.295 1.00 40.44  ? 213 HOH C O     1 
HETATM 4140 O O     . HOH I 7 .   ? -10.339 -50.859 -0.800  1.00 50.80  ? 214 HOH C O     1 
HETATM 4141 O O     . HOH I 7 .   ? 3.313   -51.338 -25.208 1.00 32.66  ? 215 HOH C O     1 
HETATM 4142 O O     . HOH I 7 .   ? 4.556   -49.522 -16.832 1.00 42.43  ? 216 HOH C O     1 
HETATM 4143 O O     . HOH I 7 .   ? -4.041  -44.856 -12.191 1.00 39.84  ? 217 HOH C O     1 
HETATM 4144 O O     . HOH I 7 .   ? 1.429   -53.084 -11.653 1.00 39.56  ? 218 HOH C O     1 
HETATM 4145 O O     . HOH I 7 .   ? 2.166   -48.203 -22.320 1.00 34.14  ? 219 HOH C O     1 
HETATM 4146 O O     . HOH I 7 .   ? 3.940   -47.811 -11.882 1.00 33.53  ? 220 HOH C O     1 
HETATM 4147 O O     . HOH I 7 .   ? -3.848  -47.394 -20.979 1.00 38.53  ? 221 HOH C O     1 
HETATM 4148 O O     . HOH I 7 .   ? 21.528  -48.221 -12.214 1.00 51.49  ? 222 HOH C O     1 
HETATM 4149 O O     . HOH I 7 .   ? -8.099  -45.413 2.481   1.00 40.84  ? 223 HOH C O     1 
HETATM 4150 O O     . HOH I 7 .   ? 2.052   -61.437 -14.598 1.00 40.30  ? 224 HOH C O     1 
HETATM 4151 O O     . HOH I 7 .   ? 10.490  -51.002 2.963   1.00 48.07  ? 225 HOH C O     1 
HETATM 4152 O O     . HOH I 7 .   ? 4.165   -49.848 -22.503 1.00 37.95  ? 226 HOH C O     1 
HETATM 4153 O O     . HOH I 7 .   ? -0.834  -48.755 5.071   1.00 48.67  ? 227 HOH C O     1 
HETATM 4154 O O     . HOH I 7 .   ? -9.719  -59.108 -8.518  1.00 55.18  ? 228 HOH C O     1 
HETATM 4155 O O     . HOH I 7 .   ? 10.235  -61.091 -2.977  1.00 49.20  ? 229 HOH C O     1 
HETATM 4156 O O     . HOH I 7 .   ? -0.509  -55.527 7.014   1.00 54.46  ? 230 HOH C O     1 
HETATM 4157 O O     . HOH I 7 .   ? -7.530  -46.507 9.549   1.00 48.28  ? 231 HOH C O     1 
HETATM 4158 O O     . HOH I 7 .   ? -8.831  -47.761 -7.534  1.00 47.06  ? 232 HOH C O     1 
HETATM 4159 O O     . HOH I 7 .   ? -6.489  -51.025 5.040   1.00 50.94  ? 233 HOH C O     1 
HETATM 4160 O O     . HOH I 7 .   ? -8.185  -47.448 -3.967  1.00 43.02  ? 234 HOH C O     1 
HETATM 4161 O O     . HOH I 7 .   ? -2.533  -54.685 5.856   1.00 48.18  ? 235 HOH C O     1 
HETATM 4162 O O     . HOH I 7 .   ? 7.082   -50.998 -16.229 1.00 47.05  ? 236 HOH C O     1 
HETATM 4163 O O     . HOH I 7 .   ? 3.140   -36.237 2.290   1.00 53.40  ? 237 HOH C O     1 
HETATM 4164 O O     . HOH I 7 .   ? 3.253   -64.694 -5.856  1.00 43.96  ? 238 HOH C O     1 
HETATM 4165 O O     . HOH I 7 .   ? -11.243 -49.704 -7.430  1.00 49.96  ? 239 HOH C O     1 
HETATM 4166 O O     . HOH I 7 .   ? -5.219  -33.846 1.890   1.00 41.02  ? 240 HOH C O     1 
HETATM 4167 O O     . HOH I 7 .   ? 1.220   -66.418 -5.434  1.00 51.90  ? 241 HOH C O     1 
HETATM 4168 O O     . HOH I 7 .   ? -9.624  -44.667 0.413   1.00 49.72  ? 242 HOH C O     1 
HETATM 4169 O O     . HOH J 7 .   ? 26.206  -18.564 -26.409 1.00 53.25  ? 201 HOH D O     1 
HETATM 4170 O O     . HOH J 7 .   ? 34.535  -10.129 -27.432 1.00 43.27  ? 202 HOH D O     1 
HETATM 4171 O O     . HOH J 7 .   ? 28.184  -16.831 -6.569  1.00 53.55  ? 203 HOH D O     1 
HETATM 4172 O O     . HOH J 7 .   ? 42.944  -20.939 -23.502 1.00 44.25  ? 204 HOH D O     1 
HETATM 4173 O O     . HOH J 7 .   ? 43.008  -10.711 -36.623 1.00 53.57  ? 205 HOH D O     1 
HETATM 4174 O O     . HOH J 7 .   ? 25.428  -1.702  -14.408 1.00 43.02  ? 206 HOH D O     1 
HETATM 4175 O O     . HOH J 7 .   ? 50.442  -9.330  -23.457 1.00 31.95  ? 207 HOH D O     1 
HETATM 4176 O O     . HOH J 7 .   ? 37.755  -5.209  -20.478 1.00 26.28  ? 208 HOH D O     1 
HETATM 4177 O O     . HOH J 7 .   ? 41.808  -19.696 -25.505 1.00 39.93  ? 209 HOH D O     1 
HETATM 4178 O O     . HOH J 7 .   ? 35.447  -6.776  -19.905 1.00 32.87  ? 210 HOH D O     1 
HETATM 4179 O O     . HOH J 7 .   ? 25.767  -15.488 -12.725 1.00 53.38  ? 211 HOH D O     1 
HETATM 4180 O O     . HOH J 7 .   ? 25.167  -10.826 -25.331 1.00 47.11  ? 212 HOH D O     1 
HETATM 4181 O O     . HOH J 7 .   ? 47.629  -17.195 -14.898 1.00 39.48  ? 213 HOH D O     1 
HETATM 4182 O O     . HOH J 7 .   ? 48.954  -5.792  -20.639 1.00 34.85  ? 214 HOH D O     1 
HETATM 4183 O O     . HOH J 7 .   ? 48.763  -6.052  -13.359 1.00 30.02  ? 215 HOH D O     1 
HETATM 4184 O O     . HOH J 7 .   ? 40.919  -19.464 -32.449 1.00 52.03  ? 216 HOH D O     1 
HETATM 4185 O O     . HOH J 7 .   ? 35.550  1.883   -21.569 1.00 42.28  ? 217 HOH D O     1 
HETATM 4186 O O     . HOH J 7 .   ? 41.333  -13.590 -8.115  1.00 46.49  ? 218 HOH D O     1 
HETATM 4187 O O     . HOH J 7 .   ? 43.158  -4.619  -31.524 1.00 42.10  ? 219 HOH D O     1 
HETATM 4188 O O     . HOH J 7 .   ? 30.041  -7.136  -15.264 1.00 34.46  ? 220 HOH D O     1 
HETATM 4189 O O     . HOH J 7 .   ? 46.078  -7.532  -19.437 1.00 28.15  ? 221 HOH D O     1 
HETATM 4190 O O     . HOH J 7 .   ? 28.946  -24.225 -29.866 1.00 49.51  ? 222 HOH D O     1 
HETATM 4191 O O     . HOH J 7 .   ? 34.356  -26.476 -11.653 1.00 57.28  ? 223 HOH D O     1 
HETATM 4192 O O     . HOH J 7 .   ? 33.317  -9.972  -32.495 1.00 48.17  ? 224 HOH D O     1 
HETATM 4193 O O     . HOH J 7 .   ? 48.614  -13.458 -33.052 1.00 53.01  ? 225 HOH D O     1 
HETATM 4194 O O     . HOH J 7 .   ? 46.866  -0.929  -20.571 1.00 32.64  ? 226 HOH D O     1 
HETATM 4195 O O     . HOH J 7 .   ? 26.038  -19.856 -5.226  1.00 54.75  ? 227 HOH D O     1 
HETATM 4196 O O     . HOH J 7 .   ? 24.486  -4.935  -15.842 1.00 45.57  ? 228 HOH D O     1 
HETATM 4197 O O     . HOH J 7 .   ? 36.516  -19.444 -29.743 1.00 58.41  ? 229 HOH D O     1 
HETATM 4198 O O     . HOH J 7 .   ? 51.077  -21.329 -32.944 1.00 65.69  ? 230 HOH D O     1 
HETATM 4199 O O     . HOH J 7 .   ? 27.077  -10.450 -27.223 1.00 40.46  ? 231 HOH D O     1 
HETATM 4200 O O     . HOH J 7 .   ? 54.487  -16.194 -15.693 1.00 38.39  ? 232 HOH D O     1 
HETATM 4201 O O     . HOH J 7 .   ? 44.956  -18.993 -27.784 1.00 50.46  ? 233 HOH D O     1 
HETATM 4202 O O     . HOH J 7 .   ? 31.351  -29.753 -20.312 1.00 46.72  ? 234 HOH D O     1 
HETATM 4203 O O     . HOH J 7 .   ? 23.016  -7.247  -18.216 1.00 38.13  ? 235 HOH D O     1 
HETATM 4204 O O     . HOH J 7 .   ? 36.958  -9.231  -11.291 1.00 48.57  ? 236 HOH D O     1 
HETATM 4205 O O     . HOH J 7 .   ? 30.596  2.430   -19.485 1.00 36.07  ? 237 HOH D O     1 
HETATM 4206 O O     . HOH J 7 .   ? 43.839  -11.187 -9.637  1.00 47.12  ? 238 HOH D O     1 
HETATM 4207 O O     . HOH J 7 .   ? 52.479  -3.284  -18.065 1.00 21.28  ? 239 HOH D O     1 
HETATM 4208 O O     . HOH J 7 .   ? 25.177  -2.481  -22.874 1.00 48.37  ? 240 HOH D O     1 
HETATM 4209 O O     . HOH J 7 .   ? 24.448  -0.279  -22.646 1.00 48.14  ? 241 HOH D O     1 
HETATM 4210 O O     . HOH J 7 .   ? 51.216  -9.297  -10.117 1.00 43.39  ? 242 HOH D O     1 
HETATM 4211 O O     . HOH J 7 .   ? 39.883  -3.057  -33.321 1.00 60.29  ? 243 HOH D O     1 
HETATM 4212 O O     . HOH J 7 .   ? 45.708  -19.842 -13.126 1.00 39.06  ? 244 HOH D O     1 
HETATM 4213 O O     . HOH J 7 .   ? 32.114  -2.948  -25.790 1.00 42.48  ? 245 HOH D O     1 
HETATM 4214 O O     . HOH J 7 .   ? 47.806  -6.585  -9.322  1.00 46.14  ? 246 HOH D O     1 
HETATM 4215 O O     . HOH J 7 .   ? 53.838  -14.123 -20.088 1.00 38.74  ? 247 HOH D O     1 
HETATM 4216 O O     . HOH J 7 .   ? 40.932  -15.333 -6.251  1.00 42.14  ? 248 HOH D O     1 
HETATM 4217 O O     . HOH J 7 .   ? 26.879  -11.481 -13.511 1.00 38.07  ? 249 HOH D O     1 
HETATM 4218 O O     . HOH J 7 .   ? 46.027  -19.523 -18.933 1.00 36.15  ? 250 HOH D O     1 
HETATM 4219 O O     . HOH J 7 .   ? 48.550  -5.181  -23.048 1.00 34.71  ? 251 HOH D O     1 
HETATM 4220 O O     . HOH J 7 .   ? 25.405  -17.839 -6.499  1.00 53.08  ? 252 HOH D O     1 
HETATM 4221 O O     . HOH J 7 .   ? 29.904  -2.988  -26.001 1.00 48.58  ? 253 HOH D O     1 
HETATM 4222 O O     . HOH J 7 .   ? 50.706  -6.380  -10.964 1.00 35.40  ? 254 HOH D O     1 
HETATM 4223 O O     . HOH J 7 .   ? 47.912  -19.352 -16.743 1.00 45.47  ? 255 HOH D O     1 
HETATM 4224 O O     . HOH J 7 .   ? 50.839  -1.992  -19.405 1.00 37.67  ? 256 HOH D O     1 
HETATM 4225 O O     . HOH J 7 .   ? 47.203  -21.392 -15.066 1.00 51.79  ? 257 HOH D O     1 
HETATM 4226 O O     . HOH J 7 .   ? 22.204  -7.162  -15.849 1.00 45.87  ? 258 HOH D O     1 
# 
