data_9KN8
# 
_entry.id   9KN8 
# 
_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   9KN8         pdb_00009kn8 10.2210/pdb9kn8/pdb 
WWPDB D_1300053908 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-04-30 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KN8 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tueno@bio.titech.ac.jp 
_pdbx_contact_author.name_first         Takafumi 
_pdbx_contact_author.name_last          Ueno 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9219-0726 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Suzuki, T.'    1 0009-0000-0827-4485 
'Hishikawa, Y.' 2 0000-0002-4545-9195 
'Maity, B.'     3 0000-0001-9347-881X 
'Abe, S.'       4 0000-0002-7308-9670 
'Ueno, T.'      5 0000-0001-9219-0726 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Adv Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2198-3844 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                e2417030 
_citation.page_last                 e2417030 
_citation.title                     
'Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/advs.202417030 
_citation.pdbx_database_id_PubMed   39973762 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hishikawa, Y.'  1  ?                   
primary 'Suzuki, T.'     2  ?                   
primary 'Maity, B.'      3  ?                   
primary 'Noya, H.'       4  ?                   
primary 'Yoshizawa, M.'  5  ?                   
primary 'Asanuma, A.'    6  ?                   
primary 'Katagiri, Y.'   7  ?                   
primary 'Abe, S.'        8  ?                   
primary 'Nagatoishi, S.' 9  ?                   
primary 'Tsumoto, K.'    10 ?                   
primary 'Ueno, T.'       11 0000-0001-9219-0726 
# 
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 'Ferritin light chain' 19952.709 1   ? E53F/E56F/E57F/R59F/E60F/E63F ? ? 
2 non-polymer syn 'CADMIUM ION'          112.411   5   ? ?                             ? ? 
3 non-polymer syn 'SULFATE ION'          96.063    1   ? ?                             ? ? 
4 non-polymer syn 'Coumarin 153'         309.283   1   ? ?                             ? ? 
5 non-polymer syn 1,2-ETHANEDIOL         62.068    3   ? ?                             ? ? 
6 non-polymer syn 'CHLORIDE ION'         35.453    1   ? ?                             ? ? 
7 water       nat water                  18.015    197 ? ?                             ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Ferritin L subunit' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRFLAFFKFFGAFRLLKMQNQRGGRALFQD
LQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAG
LGEYLFERLTLKHD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRFLAFFKFFGAFRLLKMQNQRGGRALFQD
LQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAG
LGEYLFERLTLKHD
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CADMIUM ION'  CD    
3 'SULFATE ION'  SO4   
4 'Coumarin 153' A1L54 
5 1,2-ETHANEDIOL EDO   
6 'CHLORIDE ION' CL    
7 water          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   GLN n 
1 4   ILE n 
1 5   ARG n 
1 6   GLN n 
1 7   ASN n 
1 8   TYR n 
1 9   SER n 
1 10  THR n 
1 11  GLU n 
1 12  VAL n 
1 13  GLU n 
1 14  ALA n 
1 15  ALA n 
1 16  VAL n 
1 17  ASN n 
1 18  ARG n 
1 19  LEU n 
1 20  VAL n 
1 21  ASN n 
1 22  LEU n 
1 23  TYR n 
1 24  LEU n 
1 25  ARG n 
1 26  ALA n 
1 27  SER n 
1 28  TYR n 
1 29  THR n 
1 30  TYR n 
1 31  LEU n 
1 32  SER n 
1 33  LEU n 
1 34  GLY n 
1 35  PHE n 
1 36  TYR n 
1 37  PHE n 
1 38  ASP n 
1 39  ARG n 
1 40  ASP n 
1 41  ASP n 
1 42  VAL n 
1 43  ALA n 
1 44  LEU n 
1 45  GLU n 
1 46  GLY n 
1 47  VAL n 
1 48  CYS n 
1 49  HIS n 
1 50  PHE n 
1 51  PHE n 
1 52  ARG n 
1 53  PHE n 
1 54  LEU n 
1 55  ALA n 
1 56  PHE n 
1 57  PHE n 
1 58  LYS n 
1 59  PHE n 
1 60  PHE n 
1 61  GLY n 
1 62  ALA n 
1 63  PHE n 
1 64  ARG n 
1 65  LEU n 
1 66  LEU n 
1 67  LYS n 
1 68  MET n 
1 69  GLN n 
1 70  ASN n 
1 71  GLN n 
1 72  ARG n 
1 73  GLY n 
1 74  GLY n 
1 75  ARG n 
1 76  ALA n 
1 77  LEU n 
1 78  PHE n 
1 79  GLN n 
1 80  ASP n 
1 81  LEU n 
1 82  GLN n 
1 83  LYS n 
1 84  PRO n 
1 85  SER n 
1 86  GLN n 
1 87  ASP n 
1 88  GLU n 
1 89  TRP n 
1 90  GLY n 
1 91  THR n 
1 92  THR n 
1 93  LEU n 
1 94  ASP n 
1 95  ALA n 
1 96  MET n 
1 97  LYS n 
1 98  ALA n 
1 99  ALA n 
1 100 ILE n 
1 101 VAL n 
1 102 LEU n 
1 103 GLU n 
1 104 LYS n 
1 105 SER n 
1 106 LEU n 
1 107 ASN n 
1 108 GLN n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 ASP n 
1 113 LEU n 
1 114 HIS n 
1 115 ALA n 
1 116 LEU n 
1 117 GLY n 
1 118 SER n 
1 119 ALA n 
1 120 GLN n 
1 121 ALA n 
1 122 ASP n 
1 123 PRO n 
1 124 HIS n 
1 125 LEU n 
1 126 CYS n 
1 127 ASP n 
1 128 PHE n 
1 129 LEU n 
1 130 GLU n 
1 131 SER n 
1 132 HIS n 
1 133 PHE n 
1 134 LEU n 
1 135 ASP n 
1 136 GLU n 
1 137 GLU n 
1 138 VAL n 
1 139 LYS n 
1 140 LEU n 
1 141 ILE n 
1 142 LYS n 
1 143 LYS n 
1 144 MET n 
1 145 GLY n 
1 146 ASP n 
1 147 HIS n 
1 148 LEU n 
1 149 THR n 
1 150 ASN n 
1 151 ILE n 
1 152 GLN n 
1 153 ARG n 
1 154 LEU n 
1 155 VAL n 
1 156 GLY n 
1 157 SER n 
1 158 GLN n 
1 159 ALA n 
1 160 GLY n 
1 161 LEU n 
1 162 GLY n 
1 163 GLU n 
1 164 TYR n 
1 165 LEU n 
1 166 PHE n 
1 167 GLU n 
1 168 ARG n 
1 169 LEU n 
1 170 THR n 
1 171 LEU n 
1 172 LYS n 
1 173 HIS n 
1 174 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   174 
_entity_src_gen.gene_src_common_name               horse 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FTL 
_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      'Equus caballus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9796 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L54 non-polymer         . 'Coumarin 153'  
'6-(trifluoromethyl)-3-oxa-13-azatetracyclo[7.7.1.0^{2,7}.0^{13,17}]heptadeca-1(17),2(7),5,8-tetraen-4-one' 'C16 H14 F3 N O2' 
309.283 
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 
CD    non-polymer         . 'CADMIUM ION'   ? 'Cd 2'            112.411 
CL    non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'           35.453  
CYS   'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'    121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER           ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE          ? 'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION'   ? 'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE          ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   TYR 8   8   8   TYR TYR A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  TRP 89  89  89  TRP TRP A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 GLN 108 108 108 GLN GLN A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 CYS 126 126 126 CYS CYS A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 HIS 147 147 147 HIS HIS A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L54 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L54 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CD    1   201 1   CD    CD  A . 
C 2 CD    1   202 2   CD    CD  A . 
D 2 CD    1   203 3   CD    CD  A . 
E 2 CD    1   204 4   CD    CD  A . 
F 2 CD    1   205 5   CD    CD  A . 
G 3 SO4   1   206 1   SO4   SO4 A . 
H 4 A1L54 1   207 701 A1L54 LIG A . 
I 5 EDO   1   208 301 EDO   EDO A . 
J 5 EDO   1   209 501 EDO   EDO A . 
K 5 EDO   1   210 801 EDO   EDO A . 
L 6 CL    1   211 1   CL    CL  A . 
M 7 HOH   1   301 190 HOH   HOH A . 
M 7 HOH   2   302 183 HOH   HOH A . 
M 7 HOH   3   303 145 HOH   HOH A . 
M 7 HOH   4   304 194 HOH   HOH A . 
M 7 HOH   5   305 30  HOH   HOH A . 
M 7 HOH   6   306 186 HOH   HOH A . 
M 7 HOH   7   307 217 HOH   HOH A . 
M 7 HOH   8   308 79  HOH   HOH A . 
M 7 HOH   9   309 189 HOH   HOH A . 
M 7 HOH   10  310 131 HOH   HOH A . 
M 7 HOH   11  311 52  HOH   HOH A . 
M 7 HOH   12  312 2   HOH   HOH A . 
M 7 HOH   13  313 174 HOH   HOH A . 
M 7 HOH   14  314 202 HOH   HOH A . 
M 7 HOH   15  315 195 HOH   HOH A . 
M 7 HOH   16  316 133 HOH   HOH A . 
M 7 HOH   17  317 61  HOH   HOH A . 
M 7 HOH   18  318 64  HOH   HOH A . 
M 7 HOH   19  319 63  HOH   HOH A . 
M 7 HOH   20  320 94  HOH   HOH A . 
M 7 HOH   21  321 37  HOH   HOH A . 
M 7 HOH   22  322 41  HOH   HOH A . 
M 7 HOH   23  323 109 HOH   HOH A . 
M 7 HOH   24  324 49  HOH   HOH A . 
M 7 HOH   25  325 211 HOH   HOH A . 
M 7 HOH   26  326 67  HOH   HOH A . 
M 7 HOH   27  327 4   HOH   HOH A . 
M 7 HOH   28  328 200 HOH   HOH A . 
M 7 HOH   29  329 104 HOH   HOH A . 
M 7 HOH   30  330 9   HOH   HOH A . 
M 7 HOH   31  331 5   HOH   HOH A . 
M 7 HOH   32  332 44  HOH   HOH A . 
M 7 HOH   33  333 92  HOH   HOH A . 
M 7 HOH   34  334 203 HOH   HOH A . 
M 7 HOH   35  335 220 HOH   HOH A . 
M 7 HOH   36  336 72  HOH   HOH A . 
M 7 HOH   37  337 113 HOH   HOH A . 
M 7 HOH   38  338 1   HOH   HOH A . 
M 7 HOH   39  339 16  HOH   HOH A . 
M 7 HOH   40  340 221 HOH   HOH A . 
M 7 HOH   41  341 59  HOH   HOH A . 
M 7 HOH   42  342 34  HOH   HOH A . 
M 7 HOH   43  343 57  HOH   HOH A . 
M 7 HOH   44  344 23  HOH   HOH A . 
M 7 HOH   45  345 85  HOH   HOH A . 
M 7 HOH   46  346 134 HOH   HOH A . 
M 7 HOH   47  347 26  HOH   HOH A . 
M 7 HOH   48  348 10  HOH   HOH A . 
M 7 HOH   49  349 55  HOH   HOH A . 
M 7 HOH   50  350 196 HOH   HOH A . 
M 7 HOH   51  351 21  HOH   HOH A . 
M 7 HOH   52  352 46  HOH   HOH A . 
M 7 HOH   53  353 188 HOH   HOH A . 
M 7 HOH   54  354 69  HOH   HOH A . 
M 7 HOH   55  355 17  HOH   HOH A . 
M 7 HOH   56  356 48  HOH   HOH A . 
M 7 HOH   57  357 15  HOH   HOH A . 
M 7 HOH   58  358 73  HOH   HOH A . 
M 7 HOH   59  359 45  HOH   HOH A . 
M 7 HOH   60  360 142 HOH   HOH A . 
M 7 HOH   61  361 14  HOH   HOH A . 
M 7 HOH   62  362 135 HOH   HOH A . 
M 7 HOH   63  363 210 HOH   HOH A . 
M 7 HOH   64  364 175 HOH   HOH A . 
M 7 HOH   65  365 78  HOH   HOH A . 
M 7 HOH   66  366 20  HOH   HOH A . 
M 7 HOH   67  367 101 HOH   HOH A . 
M 7 HOH   68  368 13  HOH   HOH A . 
M 7 HOH   69  369 185 HOH   HOH A . 
M 7 HOH   70  370 71  HOH   HOH A . 
M 7 HOH   71  371 193 HOH   HOH A . 
M 7 HOH   72  372 191 HOH   HOH A . 
M 7 HOH   73  373 199 HOH   HOH A . 
M 7 HOH   74  374 112 HOH   HOH A . 
M 7 HOH   75  375 18  HOH   HOH A . 
M 7 HOH   76  376 161 HOH   HOH A . 
M 7 HOH   77  377 47  HOH   HOH A . 
M 7 HOH   78  378 65  HOH   HOH A . 
M 7 HOH   79  379 43  HOH   HOH A . 
M 7 HOH   80  380 192 HOH   HOH A . 
M 7 HOH   81  381 66  HOH   HOH A . 
M 7 HOH   82  382 58  HOH   HOH A . 
M 7 HOH   83  383 31  HOH   HOH A . 
M 7 HOH   84  384 205 HOH   HOH A . 
M 7 HOH   85  385 80  HOH   HOH A . 
M 7 HOH   86  386 95  HOH   HOH A . 
M 7 HOH   87  387 3   HOH   HOH A . 
M 7 HOH   88  388 56  HOH   HOH A . 
M 7 HOH   89  389 35  HOH   HOH A . 
M 7 HOH   90  390 32  HOH   HOH A . 
M 7 HOH   91  391 6   HOH   HOH A . 
M 7 HOH   92  392 29  HOH   HOH A . 
M 7 HOH   93  393 146 HOH   HOH A . 
M 7 HOH   94  394 28  HOH   HOH A . 
M 7 HOH   95  395 74  HOH   HOH A . 
M 7 HOH   96  396 105 HOH   HOH A . 
M 7 HOH   97  397 132 HOH   HOH A . 
M 7 HOH   98  398 25  HOH   HOH A . 
M 7 HOH   99  399 93  HOH   HOH A . 
M 7 HOH   100 400 124 HOH   HOH A . 
M 7 HOH   101 401 19  HOH   HOH A . 
M 7 HOH   102 402 82  HOH   HOH A . 
M 7 HOH   103 403 33  HOH   HOH A . 
M 7 HOH   104 404 128 HOH   HOH A . 
M 7 HOH   105 405 136 HOH   HOH A . 
M 7 HOH   106 406 121 HOH   HOH A . 
M 7 HOH   107 407 11  HOH   HOH A . 
M 7 HOH   108 408 42  HOH   HOH A . 
M 7 HOH   109 409 22  HOH   HOH A . 
M 7 HOH   110 410 110 HOH   HOH A . 
M 7 HOH   111 411 24  HOH   HOH A . 
M 7 HOH   112 412 54  HOH   HOH A . 
M 7 HOH   113 413 53  HOH   HOH A . 
M 7 HOH   114 414 166 HOH   HOH A . 
M 7 HOH   115 415 100 HOH   HOH A . 
M 7 HOH   116 416 62  HOH   HOH A . 
M 7 HOH   117 417 201 HOH   HOH A . 
M 7 HOH   118 418 208 HOH   HOH A . 
M 7 HOH   119 419 144 HOH   HOH A . 
M 7 HOH   120 420 149 HOH   HOH A . 
M 7 HOH   121 421 177 HOH   HOH A . 
M 7 HOH   122 422 38  HOH   HOH A . 
M 7 HOH   123 423 176 HOH   HOH A . 
M 7 HOH   124 424 8   HOH   HOH A . 
M 7 HOH   125 425 89  HOH   HOH A . 
M 7 HOH   126 426 218 HOH   HOH A . 
M 7 HOH   127 427 27  HOH   HOH A . 
M 7 HOH   128 428 206 HOH   HOH A . 
M 7 HOH   129 429 216 HOH   HOH A . 
M 7 HOH   130 430 207 HOH   HOH A . 
M 7 HOH   131 431 155 HOH   HOH A . 
M 7 HOH   132 432 115 HOH   HOH A . 
M 7 HOH   133 433 139 HOH   HOH A . 
M 7 HOH   134 434 81  HOH   HOH A . 
M 7 HOH   135 435 197 HOH   HOH A . 
M 7 HOH   136 436 138 HOH   HOH A . 
M 7 HOH   137 437 204 HOH   HOH A . 
M 7 HOH   138 438 137 HOH   HOH A . 
M 7 HOH   139 439 215 HOH   HOH A . 
M 7 HOH   140 440 84  HOH   HOH A . 
M 7 HOH   141 441 83  HOH   HOH A . 
M 7 HOH   142 442 126 HOH   HOH A . 
M 7 HOH   143 443 150 HOH   HOH A . 
M 7 HOH   144 444 96  HOH   HOH A . 
M 7 HOH   145 445 214 HOH   HOH A . 
M 7 HOH   146 446 87  HOH   HOH A . 
M 7 HOH   147 447 91  HOH   HOH A . 
M 7 HOH   148 448 164 HOH   HOH A . 
M 7 HOH   149 449 39  HOH   HOH A . 
M 7 HOH   150 450 147 HOH   HOH A . 
M 7 HOH   151 451 68  HOH   HOH A . 
M 7 HOH   152 452 148 HOH   HOH A . 
M 7 HOH   153 453 156 HOH   HOH A . 
M 7 HOH   154 454 70  HOH   HOH A . 
M 7 HOH   155 455 198 HOH   HOH A . 
M 7 HOH   156 456 12  HOH   HOH A . 
M 7 HOH   157 457 114 HOH   HOH A . 
M 7 HOH   158 458 179 HOH   HOH A . 
M 7 HOH   159 459 125 HOH   HOH A . 
M 7 HOH   160 460 127 HOH   HOH A . 
M 7 HOH   161 461 123 HOH   HOH A . 
M 7 HOH   162 462 151 HOH   HOH A . 
M 7 HOH   163 463 170 HOH   HOH A . 
M 7 HOH   164 464 130 HOH   HOH A . 
M 7 HOH   165 465 182 HOH   HOH A . 
M 7 HOH   166 466 36  HOH   HOH A . 
M 7 HOH   167 467 219 HOH   HOH A . 
M 7 HOH   168 468 181 HOH   HOH A . 
M 7 HOH   169 469 152 HOH   HOH A . 
M 7 HOH   170 470 178 HOH   HOH A . 
M 7 HOH   171 471 160 HOH   HOH A . 
M 7 HOH   172 472 169 HOH   HOH A . 
M 7 HOH   173 473 106 HOH   HOH A . 
M 7 HOH   174 474 162 HOH   HOH A . 
M 7 HOH   175 475 209 HOH   HOH A . 
M 7 HOH   176 476 120 HOH   HOH A . 
M 7 HOH   177 477 116 HOH   HOH A . 
M 7 HOH   178 478 77  HOH   HOH A . 
M 7 HOH   179 479 129 HOH   HOH A . 
M 7 HOH   180 480 51  HOH   HOH A . 
M 7 HOH   181 481 75  HOH   HOH A . 
M 7 HOH   182 482 118 HOH   HOH A . 
M 7 HOH   183 483 99  HOH   HOH A . 
M 7 HOH   184 484 187 HOH   HOH A . 
M 7 HOH   185 485 212 HOH   HOH A . 
M 7 HOH   186 486 103 HOH   HOH A . 
M 7 HOH   187 487 165 HOH   HOH A . 
M 7 HOH   188 488 154 HOH   HOH A . 
M 7 HOH   189 489 167 HOH   HOH A . 
M 7 HOH   190 490 117 HOH   HOH A . 
M 7 HOH   191 491 102 HOH   HOH A . 
M 7 HOH   192 492 171 HOH   HOH A . 
M 7 HOH   193 493 119 HOH   HOH A . 
M 7 HOH   194 494 168 HOH   HOH A . 
M 7 HOH   195 495 180 HOH   HOH A . 
M 7 HOH   196 496 153 HOH   HOH A . 
M 7 HOH   197 497 108 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A SER 1   ? CB  ? A SER 1   CB  
2  1 Y 1 A SER 1   ? OG  ? A SER 1   OG  
3  1 Y 1 A GLN 158 ? CG  ? A GLN 158 CG  
4  1 Y 1 A GLN 158 ? CD  ? A GLN 158 CD  
5  1 Y 1 A GLN 158 ? OE1 ? A GLN 158 OE1 
6  1 Y 1 A GLN 158 ? NE2 ? A GLN 158 NE2 
7  1 Y 1 A LYS 172 ? CG  ? A LYS 172 CG  
8  1 Y 1 A LYS 172 ? CD  ? A LYS 172 CD  
9  1 Y 1 A LYS 172 ? CE  ? A LYS 172 CE  
10 1 Y 1 A LYS 172 ? NZ  ? A LYS 172 NZ  
11 1 Y 1 A ASP 174 ? C   ? A ASP 174 C   
12 1 Y 1 A ASP 174 ? O   ? A ASP 174 O   
13 1 Y 1 A ASP 174 ? CB  ? A ASP 174 CB  
14 1 Y 1 A ASP 174 ? CG  ? A ASP 174 CG  
15 1 Y 1 A ASP 174 ? OD1 ? A ASP 174 OD1 
16 1 Y 1 A ASP 174 ? OD2 ? A ASP 174 OD2 
# 
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 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? . 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? . 2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? . 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? . 4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5 5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? . 6 
# 
_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                     9KN8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     181.158 
_cell.length_a_esd                 ? 
_cell.length_b                     181.158 
_cell.length_b_esd                 ? 
_cell.length_c                     181.158 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        96 
_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                         9KN8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                209 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 4 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KN8 
_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             3.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.37 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              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    Incubation 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Ammonium sulfate, Cadmium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     93 
_diffrn.ambient_temp_details             'Liquid N2 vapour' 
_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                         'RIGAKU HyPix-6000HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-03-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54184 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-E DW' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KN8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.64 
_reflns.d_resolution_low                               18.21 
_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                                     31536 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.075 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.071 
_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                                    1.64 
_reflns_shell.d_res_low                                     1.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1587 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.2 
_reflns_shell.pdbx_chi_squared                              1.15 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.903 
_reflns_shell.pdbx_Rpim_I_all                               0.378 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.819 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.815 
_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                                 9KN8 
_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                            1.64 
_refine.ls_d_res_low                             18.21 
_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                     31414 
_refine.ls_number_reflns_R_free                  1588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.06 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1933 
_refine.ls_R_factor_R_free                       0.2082 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1925 
_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                      1DAT 
_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                 21.77 
_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                            0.14 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1391 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               1633 
_refine_hist.d_res_high                       1.64 
_refine_hist.d_res_low                        18.21 
# 
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' ? 0.015  ? 1527 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.729  ? 2073 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.468 ? 583  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.099  ? 222  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 267  ? 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' 1.64 1.69  . . 135 2668 99.00  . . . . 0.2472 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.69 1.75  . . 145 2656 100.00 . . . . 0.2387 . . . . . . . . . . . 0.2805 
'X-RAY DIFFRACTION' 1.75 1.82  . . 159 2631 99.00  . . . . 0.2361 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 1.82 1.91  . . 127 2659 98.00  . . . . 0.2274 . . . . . . . . . . . 0.2389 
'X-RAY DIFFRACTION' 1.91 2.01  . . 148 2647 99.00  . . . . 0.2109 . . . . . . . . . . . 0.2273 
'X-RAY DIFFRACTION' 2.01 2.13  . . 141 2702 99.00  . . . . 0.1890 . . . . . . . . . . . 0.2069 
'X-RAY DIFFRACTION' 2.13 2.30  . . 136 2688 99.00  . . . . 0.1828 . . . . . . . . . . . 0.1684 
'X-RAY DIFFRACTION' 2.30 2.53  . . 156 2716 99.00  . . . . 0.1854 . . . . . . . . . . . 0.2211 
'X-RAY DIFFRACTION' 2.53 2.89  . . 145 2708 99.00  . . . . 0.1825 . . . . . . . . . . . 0.2157 
'X-RAY DIFFRACTION' 2.89 3.64  . . 148 2789 99.00  . . . . 0.1741 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 3.64 18.21 . . 148 2962 99.00  . . . . 0.1798 . . . . . . . . . . . 0.1798 
# 
_struct.entry_id                     9KN8 
_struct.title                        
'Crystal structure of Horse spleen L-ferritin mutant (E53F/E56F/E57F/R59F/E60F/E63F) with Coumarin 153' 
_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        9KN8 
_struct_keywords.text            '24mer cage, Phenyl Alanine mutant, Coumarin 153, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 6 ? 
M N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FRIL_HORSE 
_struct_ref.pdbx_db_accession          P02791 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRELAEEKREGAERLLKMQNQRGGRALFQD
LQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAG
LGEYLFERLTLKHD
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KN8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 174 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02791 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  175 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       174 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9KN8 PHE A 53 ? UNP P02791 GLU 54 'engineered mutation' 53 1 
1 9KN8 PHE A 56 ? UNP P02791 GLU 57 'engineered mutation' 56 2 
1 9KN8 PHE A 57 ? UNP P02791 GLU 58 'engineered mutation' 57 3 
1 9KN8 PHE A 59 ? UNP P02791 ARG 60 'engineered mutation' 59 4 
1 9KN8 PHE A 60 ? UNP P02791 GLU 61 'engineered mutation' 60 5 
1 9KN8 PHE A 63 ? UNP P02791 GLU 64 'engineered mutation' 63 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   24-meric 
_pdbx_struct_assembly.oligomeric_count     24 
# 
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)' 119350 ? 
1 MORE         -378   ? 
1 'SSA (A^2)'  135350 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                'Size exclusion chromatography' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1  'identity operation'         1_555  x,y,z    1.0000000000  0.0000000000  0.0000000000  0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  1.0000000000  0.0000000000 
2  'crystal symmetry operation' 2_555  -x,-y,z  -1.0000000000 0.0000000000  0.0000000000  0.0000000000 0.0000000000  -1.0000000000 
0.0000000000  0.0000000000 0.0000000000  0.0000000000  1.0000000000  0.0000000000 
3  'crystal symmetry operation' 3_555  -x,y,-z  -1.0000000000 0.0000000000  0.0000000000  0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  -1.0000000000 0.0000000000 
4  'crystal symmetry operation' 4_555  x,-y,-z  1.0000000000  0.0000000000  0.0000000000  0.0000000000 0.0000000000  -1.0000000000 
0.0000000000  0.0000000000 0.0000000000  0.0000000000  -1.0000000000 0.0000000000 
5  'crystal symmetry operation' 5_555  z,x,y    0.0000000000  0.0000000000  1.0000000000  0.0000000000 1.0000000000  0.0000000000  
0.0000000000  0.0000000000 0.0000000000  1.0000000000  0.0000000000  0.0000000000 
6  'crystal symmetry operation' 6_555  z,-x,-y  0.0000000000  0.0000000000  1.0000000000  0.0000000000 -1.0000000000 0.0000000000  
0.0000000000  0.0000000000 0.0000000000  -1.0000000000 0.0000000000  0.0000000000 
7  'crystal symmetry operation' 7_555  -z,-x,y  0.0000000000  0.0000000000  -1.0000000000 0.0000000000 -1.0000000000 0.0000000000  
0.0000000000  0.0000000000 0.0000000000  1.0000000000  0.0000000000  0.0000000000 
8  'crystal symmetry operation' 8_555  -z,x,-y  0.0000000000  0.0000000000  -1.0000000000 0.0000000000 1.0000000000  0.0000000000  
0.0000000000  0.0000000000 0.0000000000  -1.0000000000 0.0000000000  0.0000000000 
9  'crystal symmetry operation' 9_555  y,z,x    0.0000000000  1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 1.0000000000  0.0000000000  0.0000000000  0.0000000000 
10 'crystal symmetry operation' 10_555 -y,z,-x  0.0000000000  -1.0000000000 0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 -1.0000000000 0.0000000000  0.0000000000  0.0000000000 
11 'crystal symmetry operation' 11_555 y,-z,-x  0.0000000000  1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
-1.0000000000 0.0000000000 -1.0000000000 0.0000000000  0.0000000000  0.0000000000 
12 'crystal symmetry operation' 12_555 -y,-z,x  0.0000000000  -1.0000000000 0.0000000000  0.0000000000 0.0000000000  0.0000000000  
-1.0000000000 0.0000000000 1.0000000000  0.0000000000  0.0000000000  0.0000000000 
13 'crystal symmetry operation' 13_555 y,x,-z   0.0000000000  1.0000000000  0.0000000000  0.0000000000 1.0000000000  0.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  -1.0000000000 0.0000000000 
14 'crystal symmetry operation' 14_555 -y,-x,-z 0.0000000000  -1.0000000000 0.0000000000  0.0000000000 -1.0000000000 0.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  -1.0000000000 0.0000000000 
15 'crystal symmetry operation' 15_555 y,-x,z   0.0000000000  1.0000000000  0.0000000000  0.0000000000 -1.0000000000 0.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  1.0000000000  0.0000000000 
16 'crystal symmetry operation' 16_555 -y,x,z   0.0000000000  -1.0000000000 0.0000000000  0.0000000000 1.0000000000  0.0000000000  
0.0000000000  0.0000000000 0.0000000000  0.0000000000  1.0000000000  0.0000000000 
17 'crystal symmetry operation' 17_555 x,z,-y   1.0000000000  0.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000  -1.0000000000 0.0000000000  0.0000000000 
18 'crystal symmetry operation' 18_555 -x,z,y   -1.0000000000 0.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000  1.0000000000  0.0000000000  0.0000000000 
19 'crystal symmetry operation' 19_555 -x,-z,-y -1.0000000000 0.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
-1.0000000000 0.0000000000 0.0000000000  -1.0000000000 0.0000000000  0.0000000000 
20 'crystal symmetry operation' 20_555 x,-z,y   1.0000000000  0.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
-1.0000000000 0.0000000000 0.0000000000  1.0000000000  0.0000000000  0.0000000000 
21 'crystal symmetry operation' 21_555 z,y,-x   0.0000000000  0.0000000000  1.0000000000  0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 -1.0000000000 0.0000000000  0.0000000000  0.0000000000 
22 'crystal symmetry operation' 22_555 z,-y,x   0.0000000000  0.0000000000  1.0000000000  0.0000000000 0.0000000000  -1.0000000000 
0.0000000000  0.0000000000 1.0000000000  0.0000000000  0.0000000000  0.0000000000 
23 'crystal symmetry operation' 23_555 -z,y,x   0.0000000000  0.0000000000  -1.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000  0.0000000000 1.0000000000  0.0000000000  0.0000000000  0.0000000000 
24 'crystal symmetry operation' 24_555 -z,-y,-x 0.0000000000  0.0000000000  -1.0000000000 0.0000000000 0.0000000000  -1.0000000000 
0.0000000000  0.0000000000 -1.0000000000 0.0000000000  0.0000000000  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 9   ? ASP A 38  ? SER A 9   ASP A 38  1 ? 30 
HELX_P HELX_P2 AA2 LEU A 44  ? GLY A 73  ? LEU A 44  GLY A 73  1 ? 30 
HELX_P HELX_P3 AA3 THR A 91  ? GLN A 120 ? THR A 91  GLN A 120 1 ? 30 
HELX_P HELX_P4 AA4 ASP A 122 ? PHE A 133 ? ASP A 122 PHE A 133 1 ? 12 
HELX_P HELX_P5 AA5 PHE A 133 ? GLY A 156 ? PHE A 133 GLY A 156 1 ? 24 
HELX_P HELX_P6 AA6 GLN A 158 ? THR A 170 ? GLN A 158 THR A 170 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 38  OD1 ? ? ? 1_555 B CD . CD ? ? A ASP 38  A CD 201 1_555  ? ? ? ? ? ? ? 2.541 ? ? 
metalc2  metalc ? ? A CYS 48  SG  ? ? ? 1_555 B CD . CD ? ? A CYS 48  A CD 201 1_555  ? ? ? ? ? ? ? 2.588 ? ? 
metalc3  metalc ? ? A ASP 80  OD1 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 1_555  ? ? ? ? ? ? ? 2.448 ? ? 
metalc4  metalc ? ? A ASP 80  OD2 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 1_555  ? ? ? ? ? ? ? 2.277 ? ? 
metalc5  metalc ? ? A ASP 80  OD1 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 72_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc6  metalc ? ? A ASP 80  OD2 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 72_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc7  metalc ? ? A GLU 130 OE1 ? ? ? 1_555 E CD . CD ? ? A GLU 130 A CD 204 1_555  ? ? ? ? ? ? ? 2.272 ? ? 
metalc8  metalc ? ? A GLU 130 OE1 ? ? ? 1_555 E CD . CD ? ? A GLU 130 A CD 204 9_555  ? ? ? ? ? ? ? 2.276 ? ? 
metalc9  metalc ? ? A GLU 130 OE1 ? ? ? 1_555 F CD . CD ? ? A GLU 130 A CD 205 1_555  ? ? ? ? ? ? ? 2.559 ? ? 
metalc10 metalc ? ? A GLU 130 OE1 ? ? ? 1_555 F CD . CD ? ? A GLU 130 A CD 205 9_555  ? ? ? ? ? ? ? 2.650 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OD1 ? A ASP 38  ? A ASP 38  ? 1_555 CD ? B CD . ? A CD 201 ? 1_555 SG  ? A CYS 48  ? A CYS 48  ? 1_555 119.9 ? 
2 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 54.7  ? 
3 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 0.0   ? 
4 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 54.7  ? 
5 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 54.7  ? 
6 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 0.0   ? 
7 OD1 ? A ASP 80  ? A ASP 80  ? 1_555 CD ? C CD . ? A CD 202 ? 1_555 OD2 ? A ASP 80  ? A ASP 80  ? 1_555 54.7  ? 
8 OE1 ? A GLU 130 ? A GLU 130 ? 1_555 CD ? E CD . ? A CD 204 ? 1_555 OE1 ? A GLU 130 ? A GLU 130 ? 1_555 0.0   ? 
9 OE1 ? A GLU 130 ? A GLU 130 ? 1_555 CD ? F CD . ? A CD 205 ? 1_555 OE1 ? A GLU 130 ? A GLU 130 ? 1_555 0.0   ? 
# 
_pdbx_entry_details.entry_id                   9KN8 
_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 VAL A 42  ? ? -125.73 -59.79 
2 1 ASP A 122 ? ? -117.44 79.80  
3 1 PHE A 133 ? ? -131.30 -45.01 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A CD    202 ? C CD    . 
2 1 A CD    203 ? D CD    . 
3 1 A CD    204 ? E CD    . 
4 1 A A1L54 207 ? H A1L54 . 
5 1 A A1L54 207 ? H A1L54 . 
# 
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 
A1L54 N1   N  N N 1   
A1L54 C4   C  N N 2   
A1L54 C5   C  Y N 3   
A1L54 C6   C  Y N 4   
A1L54 C7   C  Y N 5   
A1L54 C8   C  N N 6   
A1L54 C10  C  N N 7   
A1L54 C13  C  N N 8   
A1L54 C15  C  Y N 9   
A1L54 C1   C  N N 10  
A1L54 C11  C  N N 11  
A1L54 C12  C  N N 12  
A1L54 C14  C  Y N 13  
A1L54 C16  C  Y N 14  
A1L54 C2   C  N N 15  
A1L54 C3   C  N N 16  
A1L54 C9   C  N N 17  
A1L54 F1   F  N N 18  
A1L54 F2   F  N N 19  
A1L54 F3   F  N N 20  
A1L54 O1   O  N N 21  
A1L54 O2   O  N N 22  
A1L54 H1   H  N N 23  
A1L54 H2   H  N N 24  
A1L54 H3   H  N N 25  
A1L54 H4   H  N N 26  
A1L54 H5   H  N N 27  
A1L54 H6   H  N N 28  
A1L54 H7   H  N N 29  
A1L54 H8   H  N N 30  
A1L54 H9   H  N N 31  
A1L54 H10  H  N N 32  
A1L54 H11  H  N N 33  
A1L54 H12  H  N N 34  
A1L54 H13  H  N N 35  
A1L54 H14  H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CD    CD   CD N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
EDO   C1   C  N N 126 
EDO   O1   O  N N 127 
EDO   C2   C  N N 128 
EDO   O2   O  N N 129 
EDO   H11  H  N N 130 
EDO   H12  H  N N 131 
EDO   HO1  H  N N 132 
EDO   H21  H  N N 133 
EDO   H22  H  N N 134 
EDO   HO2  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
SO4   S    S  N N 352 
SO4   O1   O  N N 353 
SO4   O2   O  N N 354 
SO4   O3   O  N N 355 
SO4   O4   O  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
# 
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 
A1L54 O1  C1   doub N N 1   
A1L54 C1  C2   sing N N 2   
A1L54 C1  O2   sing N N 3   
A1L54 C2  C3   doub N N 4   
A1L54 F1  C4   sing N N 5   
A1L54 O2  C16  sing N N 6   
A1L54 C3  C4   sing N N 7   
A1L54 C3  C5   sing N N 8   
A1L54 C4  F2   sing N N 9   
A1L54 C4  F3   sing N N 10  
A1L54 C16 C5   doub Y N 11  
A1L54 C16 C14  sing Y N 12  
A1L54 C5  C6   sing Y N 13  
A1L54 C13 C14  sing N N 14  
A1L54 C13 C12  sing N N 15  
A1L54 C14 C15  doub Y N 16  
A1L54 C6  C7   doub Y N 17  
A1L54 C12 C11  sing N N 18  
A1L54 C15 C7   sing Y N 19  
A1L54 C15 N1   sing N N 20  
A1L54 C7  C8   sing N N 21  
A1L54 C11 N1   sing N N 22  
A1L54 N1  C10  sing N N 23  
A1L54 C8  C9   sing N N 24  
A1L54 C10 C9   sing N N 25  
A1L54 C6  H1   sing N N 26  
A1L54 C8  H2   sing N N 27  
A1L54 C8  H3   sing N N 28  
A1L54 C10 H4   sing N N 29  
A1L54 C10 H5   sing N N 30  
A1L54 C13 H6   sing N N 31  
A1L54 C13 H7   sing N N 32  
A1L54 C11 H8   sing N N 33  
A1L54 C11 H9   sing N N 34  
A1L54 C12 H10  sing N N 35  
A1L54 C12 H11  sing N N 36  
A1L54 C2  H12  sing N N 37  
A1L54 C9  H13  sing N N 38  
A1L54 C9  H14  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
EDO   C1  O1   sing N N 122 
EDO   C1  C2   sing N N 123 
EDO   C1  H11  sing N N 124 
EDO   C1  H12  sing N N 125 
EDO   O1  HO1  sing N N 126 
EDO   C2  O2   sing N N 127 
EDO   C2  H21  sing N N 128 
EDO   C2  H22  sing N N 129 
EDO   O2  HO2  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
SO4   S   O1   doub N N 338 
SO4   S   O2   doub N N 339 
SO4   S   O3   sing N N 340 
SO4   S   O4   sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_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   1DAT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KN8 
_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]   0.005520 
_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]   0.005520 
_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]   0.005520 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CD 
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 57.013 19.001  21.760 1.00 47.75 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 55.847 18.730  22.628 1.00 54.77 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 54.625 18.463  21.743 1.00 48.31 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 54.813 18.118  20.567 1.00 55.91 ? 1   SER   A O   1 
ATOM   5    N  N   . SER   A 1 2   ? 53.437 18.659  22.285 1.00 31.87 ? 2   SER   A N   1 
ATOM   6    C  CA  . SER   A 1 2   ? 52.216 18.330  21.507 1.00 30.83 ? 2   SER   A CA  1 
ATOM   7    C  C   . SER   A 1 2   ? 52.027 19.259  20.307 1.00 30.58 ? 2   SER   A C   1 
ATOM   8    O  O   . SER   A 1 2   ? 52.136 20.492  20.469 1.00 27.83 ? 2   SER   A O   1 
ATOM   9    C  CB  . SER   A 1 2   ? 50.947 18.320  22.333 1.00 25.56 ? 2   SER   A CB  1 
ATOM   10   O  OG  . SER   A 1 2   ? 49.797 18.089  21.541 1.00 19.58 ? 2   SER   A OG  1 
ATOM   11   N  N   . GLN   A 1 3   ? 51.614 18.693  19.198 1.00 23.78 ? 3   GLN   A N   1 
ATOM   12   C  CA  . GLN   A 1 3   ? 51.367 19.495  17.983 1.00 19.39 ? 3   GLN   A CA  1 
ATOM   13   C  C   . GLN   A 1 3   ? 50.010 20.209  18.030 1.00 17.14 ? 3   GLN   A C   1 
ATOM   14   O  O   . GLN   A 1 3   ? 49.815 21.103  17.221 1.00 17.03 ? 3   GLN   A O   1 
ATOM   15   C  CB  . GLN   A 1 3   ? 51.397 18.555  16.783 1.00 19.43 ? 3   GLN   A CB  1 
ATOM   16   C  CG  . GLN   A 1 3   ? 50.239 17.571  16.736 1.00 48.59 ? 3   GLN   A CG  1 
ATOM   17   C  CD  . GLN   A 1 3   ? 50.472 16.439  15.762 1.00 56.06 ? 3   GLN   A CD  1 
ATOM   18   O  OE1 . GLN   A 1 3   ? 49.777 15.420  15.780 1.00 39.11 ? 3   GLN   A OE1 1 
ATOM   19   N  NE2 . GLN   A 1 3   ? 51.478 16.611  14.915 1.00 40.26 ? 3   GLN   A NE2 1 
ATOM   20   N  N   . ILE   A 1 4   ? 49.127 19.825  18.946 1.00 13.52 ? 4   ILE   A N   1 
ATOM   21   C  CA  . ILE   A 1 4   ? 47.762 20.441  18.984 1.00 10.11 ? 4   ILE   A CA  1 
ATOM   22   C  C   . ILE   A 1 4   ? 47.512 21.213  20.284 1.00 9.60  ? 4   ILE   A C   1 
ATOM   23   O  O   . ILE   A 1 4   ? 46.632 22.058  20.291 1.00 11.86 ? 4   ILE   A O   1 
ATOM   24   C  CB  . ILE   A 1 4   ? 46.641 19.391  18.816 1.00 12.18 ? 4   ILE   A CB  1 
ATOM   25   C  CG1 . ILE   A 1 4   ? 46.479 18.511  20.055 1.00 13.14 ? 4   ILE   A CG1 1 
ATOM   26   C  CG2 . ILE   A 1 4   ? 46.865 18.564  17.564 1.00 13.32 ? 4   ILE   A CG2 1 
ATOM   27   C  CD1 . ILE   A 1 4   ? 45.239 17.655  20.016 1.00 15.65 ? 4   ILE   A CD1 1 
ATOM   28   N  N   . ARG   A 1 5   ? 48.283 20.930  21.313 1.00 11.09 ? 5   ARG   A N   1 
ATOM   29   C  CA  . ARG   A 1 5   ? 47.965 21.517  22.637 1.00 9.45  ? 5   ARG   A CA  1 
ATOM   30   C  C   . ARG   A 1 5   ? 48.041 23.048  22.618 1.00 10.32 ? 5   ARG   A C   1 
ATOM   31   O  O   . ARG   A 1 5   ? 49.033 23.571  22.176 1.00 11.50 ? 5   ARG   A O   1 
ATOM   32   C  CB  . ARG   A 1 5   ? 48.895 20.945  23.699 1.00 10.53 ? 5   ARG   A CB  1 
ATOM   33   C  CG  . ARG   A 1 5   ? 48.443 21.206  25.126 1.00 11.52 ? 5   ARG   A CG  1 
ATOM   34   C  CD  . ARG   A 1 5   ? 49.426 20.570  26.084 1.00 17.94 ? 5   ARG   A CD  1 
ATOM   35   N  NE  . ARG   A 1 5   ? 49.006 20.728  27.465 1.00 13.19 ? 5   ARG   A NE  1 
ATOM   36   C  CZ  . ARG   A 1 5   ? 49.209 19.827  28.413 1.00 14.41 ? 5   ARG   A CZ  1 
ATOM   37   N  NH1 . ARG   A 1 5   ? 49.835 18.699  28.129 1.00 11.63 ? 5   ARG   A NH1 1 
ATOM   38   N  NH2 . ARG   A 1 5   ? 48.791 20.063  29.642 1.00 11.88 ? 5   ARG   A NH2 1 
ATOM   39   N  N   . GLN   A 1 6   ? 46.993 23.700  23.110 1.00 8.09  ? 6   GLN   A N   1 
ATOM   40   C  CA  . GLN   A 1 6   ? 46.962 25.182  23.110 1.00 8.15  ? 6   GLN   A CA  1 
ATOM   41   C  C   . GLN   A 1 6   ? 46.063 25.662  24.259 1.00 8.92  ? 6   GLN   A C   1 
ATOM   42   O  O   . GLN   A 1 6   ? 44.915 25.243  24.296 1.00 8.51  ? 6   GLN   A O   1 
ATOM   43   C  CB  . GLN   A 1 6   ? 46.433 25.721  21.778 1.00 8.61  ? 6   GLN   A CB  1 
ATOM   44   C  CG  . GLN   A 1 6   ? 46.558 27.227  21.615 1.00 11.70 ? 6   GLN   A CG  1 
ATOM   45   C  CD  . GLN   A 1 6   ? 46.200 27.658  20.212 1.00 10.83 ? 6   GLN   A CD  1 
ATOM   46   O  OE1 . GLN   A 1 6   ? 45.446 26.992  19.514 1.00 12.76 ? 6   GLN   A OE1 1 
ATOM   47   N  NE2 . GLN   A 1 6   ? 46.741 28.786  19.791 1.00 12.20 ? 6   GLN   A NE2 1 
ATOM   48   N  N   . ASN   A 1 7   ? 46.617 26.485  25.132 1.00 7.94  ? 7   ASN   A N   1 
ATOM   49   C  CA  . ASN   A 1 7   ? 45.846 27.057  26.263 1.00 8.87  ? 7   ASN   A CA  1 
ATOM   50   C  C   . ASN   A 1 7   ? 45.379 25.943  27.211 1.00 11.09 ? 7   ASN   A C   1 
ATOM   51   O  O   . ASN   A 1 7   ? 44.363 26.129  27.849 1.00 10.69 ? 7   ASN   A O   1 
ATOM   52   C  CB  . ASN   A 1 7   ? 44.649 27.884  25.795 1.00 10.96 ? 7   ASN   A CB  1 
ATOM   53   C  CG  . ASN   A 1 7   ? 44.127 28.781  26.895 1.00 10.16 ? 7   ASN   A CG  1 
ATOM   54   O  OD1 . ASN   A 1 7   ? 44.909 29.332  27.661 1.00 13.60 ? 7   ASN   A OD1 1 
ATOM   55   N  ND2 . ASN   A 1 7   ? 42.817 28.909  26.999 1.00 9.44  ? 7   ASN   A ND2 1 
ATOM   56   N  N   . TYR   A 1 8   ? 46.144 24.858  27.284 1.00 9.06  ? 8   TYR   A N   1 
ATOM   57   C  CA  . TYR   A 1 8   ? 45.761 23.708  28.150 1.00 10.31 ? 8   TYR   A CA  1 
ATOM   58   C  C   . TYR   A 1 8   ? 46.837 23.504  29.225 1.00 10.40 ? 8   TYR   A C   1 
ATOM   59   O  O   . TYR   A 1 8   ? 47.859 22.924  28.939 1.00 12.86 ? 8   TYR   A O   1 
ATOM   60   C  CB  . TYR   A 1 8   ? 45.540 22.444  27.324 1.00 10.90 ? 8   TYR   A CB  1 
ATOM   61   C  CG  . TYR   A 1 8   ? 44.768 21.351  28.018 1.00 9.77  ? 8   TYR   A CG  1 
ATOM   62   C  CD1 . TYR   A 1 8   ? 43.501 21.580  28.520 1.00 11.86 ? 8   TYR   A CD1 1 
ATOM   63   C  CD2 . TYR   A 1 8   ? 45.298 20.082  28.158 1.00 10.23 ? 8   TYR   A CD2 1 
ATOM   64   C  CE1 . TYR   A 1 8   ? 42.774 20.576  29.136 1.00 10.46 ? 8   TYR   A CE1 1 
ATOM   65   C  CE2 . TYR   A 1 8   ? 44.590 19.071  28.786 1.00 9.92  ? 8   TYR   A CE2 1 
ATOM   66   C  CZ  . TYR   A 1 8   ? 43.323 19.315  29.278 1.00 10.31 ? 8   TYR   A CZ  1 
ATOM   67   O  OH  . TYR   A 1 8   ? 42.626 18.316  29.892 1.00 9.93  ? 8   TYR   A OH  1 
ATOM   68   N  N   . SER   A 1 9   ? 46.541 23.975  30.420 1.00 8.81  ? 9   SER   A N   1 
ATOM   69   C  CA  . SER   A 1 9   ? 47.490 23.909  31.549 1.00 11.80 ? 9   SER   A CA  1 
ATOM   70   C  C   . SER   A 1 9   ? 47.794 22.485  32.017 1.00 11.43 ? 9   SER   A C   1 
ATOM   71   O  O   . SER   A 1 9   ? 46.963 21.636  31.860 1.00 11.02 ? 9   SER   A O   1 
ATOM   72   C  CB  . SER   A 1 9   ? 46.916 24.684  32.714 1.00 14.14 ? 9   SER   A CB  1 
ATOM   73   O  OG  . SER   A 1 9   ? 45.812 24.037  33.289 1.00 15.00 ? 9   SER   A OG  1 
ATOM   74   N  N   . THR   A 1 10  ? 48.988 22.318  32.582 1.00 11.36 ? 10  THR   A N   1 
ATOM   75   C  CA  . THR   A 1 10  ? 49.363 21.038  33.212 1.00 10.44 ? 10  THR   A CA  1 
ATOM   76   C  C   . THR   A 1 10  ? 48.421 20.812  34.397 1.00 12.00 ? 10  THR   A C   1 
ATOM   77   O  O   . THR   A 1 10  ? 48.125 19.679  34.714 1.00 11.65 ? 10  THR   A O   1 
ATOM   78   C  CB  . THR   A 1 10  ? 50.811 21.159  33.711 1.00 16.68 ? 10  THR   A CB  1 
ATOM   79   O  OG1 . THR   A 1 10  ? 50.946 22.301  34.549 1.00 22.13 ? 10  THR   A OG1 1 
ATOM   80   C  CG2 . THR   A 1 10  ? 51.791 21.255  32.564 1.00 19.32 ? 10  THR   A CG2 1 
ATOM   81   N  N   . GLU   A 1 11  ? 48.037 21.899  35.045 1.00 10.67 ? 11  GLU   A N   1 
ATOM   82   C  CA  . GLU   A 1 11  ? 47.177 21.789  36.247 1.00 9.82  ? 11  GLU   A CA  1 
ATOM   83   C  C   . GLU   A 1 11  ? 45.816 21.201  35.849 1.00 9.12  ? 11  GLU   A C   1 
ATOM   84   O  O   . GLU   A 1 11  ? 45.316 20.346  36.554 1.00 11.16 ? 11  GLU   A O   1 
ATOM   85   C  CB  . GLU   A 1 11  ? 47.030 23.147  36.930 1.00 13.96 ? 11  GLU   A CB  1 
ATOM   86   C  CG  . GLU   A 1 11  ? 48.309 23.644  37.570 1.00 13.67 ? 11  GLU   A CG  1 
ATOM   87   C  CD  . GLU   A 1 11  ? 49.205 24.475  36.667 1.00 22.21 ? 11  GLU   A CD  1 
ATOM   88   O  OE1 . GLU   A 1 11  ? 48.882 24.623  35.483 1.00 13.99 ? 11  GLU   A OE1 1 
ATOM   89   O  OE2 . GLU   A 1 11  ? 50.233 24.956  37.159 1.00 24.15 ? 11  GLU   A OE2 1 
ATOM   90   N  N   . VAL   A 1 12  ? 45.250 21.728  34.777 1.00 9.73  ? 12  VAL   A N   1 
ATOM   91   C  CA  . VAL   A 1 12  ? 43.938 21.211  34.288 1.00 9.26  ? 12  VAL   A CA  1 
ATOM   92   C  C   . VAL   A 1 12  ? 44.078 19.750  33.811 1.00 11.83 ? 12  VAL   A C   1 
ATOM   93   O  O   . VAL   A 1 12  ? 43.243 18.950  34.125 1.00 9.84  ? 12  VAL   A O   1 
ATOM   94   C  CB  . VAL   A 1 12  ? 43.372 22.129  33.186 1.00 10.34 ? 12  VAL   A CB  1 
ATOM   95   C  CG1 . VAL   A 1 12  ? 42.299 21.424  32.372 1.00 12.95 ? 12  VAL   A CG1 1 
ATOM   96   C  CG2 . VAL   A 1 12  ? 42.816 23.411  33.781 1.00 10.96 ? 12  VAL   A CG2 1 
ATOM   97   N  N   . GLU   A 1 13  ? 45.146 19.478  33.066 1.00 9.76  ? 13  GLU   A N   1 
ATOM   98   C  CA  . GLU   A 1 13  ? 45.381 18.101  32.572 1.00 9.32  ? 13  GLU   A CA  1 
ATOM   99   C  C   . GLU   A 1 13  ? 45.377 17.127  33.759 1.00 8.60  ? 13  GLU   A C   1 
ATOM   100  O  O   . GLU   A 1 13  ? 44.750 16.091  33.660 1.00 9.72  ? 13  GLU   A O   1 
ATOM   101  C  CB  . GLU   A 1 13  ? 46.699 18.078  31.788 1.00 11.54 ? 13  GLU   A CB  1 
ATOM   102  C  CG  . GLU   A 1 13  ? 47.153 16.705  31.326 1.00 10.91 ? 13  GLU   A CG  1 
ATOM   103  C  CD  . GLU   A 1 13  ? 48.543 16.710  30.710 1.00 14.71 ? 13  GLU   A CD  1 
ATOM   104  O  OE1 . GLU   A 1 13  ? 49.290 17.664  30.968 1.00 14.37 ? 13  GLU   A OE1 1 
ATOM   105  O  OE2 . GLU   A 1 13  ? 48.874 15.768  29.981 1.00 14.18 ? 13  GLU   A OE2 1 
ATOM   106  N  N   . ALA   A 1 14  ? 46.109 17.484  34.811 1.00 9.36  ? 14  ALA   A N   1 
ATOM   107  C  CA  . ALA   A 1 14  ? 46.208 16.583  35.983 1.00 9.29  ? 14  ALA   A CA  1 
ATOM   108  C  C   . ALA   A 1 14  ? 44.844 16.461  36.660 1.00 11.92 ? 14  ALA   A C   1 
ATOM   109  O  O   . ALA   A 1 14  ? 44.451 15.382  37.070 1.00 9.42  ? 14  ALA   A O   1 
ATOM   110  C  CB  . ALA   A 1 14  ? 47.228 17.119  36.967 1.00 12.59 ? 14  ALA   A CB  1 
ATOM   111  N  N   . ALA   A 1 15  ? 44.168 17.599  36.752 1.00 9.87  ? 15  ALA   A N   1 
ATOM   112  C  CA  . ALA   A 1 15  ? 42.870 17.580  37.458 1.00 9.23  ? 15  ALA   A CA  1 
ATOM   113  C  C   . ALA   A 1 15  ? 41.851 16.738  36.684 1.00 8.92  ? 15  ALA   A C   1 
ATOM   114  O  O   . ALA   A 1 15  ? 40.992 16.148  37.296 1.00 10.30 ? 15  ALA   A O   1 
ATOM   115  C  CB  . ALA   A 1 15  ? 42.375 18.985  37.631 1.00 11.22 ? 15  ALA   A CB  1 
ATOM   116  N  N   . VAL   A 1 16  ? 41.933 16.798  35.365 1.00 9.81  ? 16  VAL   A N   1 
ATOM   117  C  CA  . VAL   A 1 16  ? 41.009 15.976  34.533 1.00 8.37  ? 16  VAL   A CA  1 
ATOM   118  C  C   . VAL   A 1 16  ? 41.266 14.490  34.805 1.00 8.73  ? 16  VAL   A C   1 
ATOM   119  O  O   . VAL   A 1 16  ? 40.327 13.741  34.925 1.00 9.51  ? 16  VAL   A O   1 
ATOM   120  C  CB  . VAL   A 1 16  ? 41.156 16.346  33.044 1.00 8.78  ? 16  VAL   A CB  1 
ATOM   121  C  CG1 . VAL   A 1 16  ? 40.564 15.289  32.128 1.00 9.75  ? 16  VAL   A CG1 1 
ATOM   122  C  CG2 . VAL   A 1 16  ? 40.556 17.710  32.745 1.00 9.51  ? 16  VAL   A CG2 1 
ATOM   123  N  N   . ASN   A 1 17  ? 42.540 14.113  34.865 1.00 8.22  ? 17  ASN   A N   1 
ATOM   124  C  CA  . ASN   A 1 17  ? 42.872 12.698  35.127 1.00 7.50  ? 17  ASN   A CA  1 
ATOM   125  C  C   . ASN   A 1 17  ? 42.344 12.294  36.517 1.00 10.58 ? 17  ASN   A C   1 
ATOM   126  O  O   . ASN   A 1 17  ? 41.891 11.183  36.679 1.00 10.41 ? 17  ASN   A O   1 
ATOM   127  C  CB  . ASN   A 1 17  ? 44.370 12.453  35.003 1.00 10.73 ? 17  ASN   A CB  1 
ATOM   128  C  CG  . ASN   A 1 17  ? 44.830 12.317  33.569 1.00 10.25 ? 17  ASN   A CG  1 
ATOM   129  O  OD1 . ASN   A 1 17  ? 44.073 11.893  32.708 1.00 8.70  ? 17  ASN   A OD1 1 
ATOM   130  N  ND2 . ASN   A 1 17  ? 46.072 12.674  33.309 1.00 11.86 ? 17  ASN   A ND2 1 
ATOM   131  N  N   . ARG   A 1 18  ? 42.517 13.188  37.485 1.00 10.09 ? 18  ARG   A N   1 
ATOM   132  C  CA  . ARG   A 1 18  ? 41.950 12.871  38.841 1.00 8.16  ? 18  ARG   A CA  1 
ATOM   133  C  C   . ARG   A 1 18  ? 40.405 12.708  38.815 1.00 10.71 ? 18  ARG   A C   1 
ATOM   134  O  O   . ARG   A 1 18  ? 39.743 11.798  39.394 1.00 11.44 ? 18  ARG   A O   1 
ATOM   135  C  CB  . ARG   A 1 18  ? 42.368 13.955  39.841 1.00 10.32 ? 18  ARG   A CB  1 
ATOM   136  C  CG  . ARG   A 1 18  ? 43.843 13.882  40.204 1.00 10.89 ? 18  ARG   A CG  1 
ATOM   137  C  CD  . ARG   A 1 18  ? 44.188 14.676  41.447 1.00 14.87 ? 18  ARG   A CD  1 
ATOM   138  N  NE  . ARG   A 1 18  ? 44.026 16.092  41.174 1.00 22.32 ? 18  ARG   A NE  1 
ATOM   139  C  CZ  . ARG   A 1 18  ? 44.964 16.859  40.636 1.00 9.85  ? 18  ARG   A CZ  1 
ATOM   140  N  NH1 . ARG   A 1 18  ? 46.143 16.348  40.331 1.00 16.65 ? 18  ARG   A NH1 1 
ATOM   141  N  NH2 . ARG   A 1 18  ? 44.717 18.135  40.413 1.00 13.25 ? 18  ARG   A NH2 1 
ATOM   142  N  N   . LEU   A 1 19  ? 39.816 13.592  38.013 1.00 9.13  ? 19  LEU   A N   1 
ATOM   143  C  CA  . LEU   A 1 19  ? 38.329 13.567  37.902 1.00 8.92  ? 19  LEU   A CA  1 
ATOM   144  C  C   . LEU   A 1 19  ? 37.874 12.270  37.209 1.00 10.76 ? 19  LEU   A C   1 
ATOM   145  O  O   . LEU   A 1 19  ? 36.830 11.740  37.572 1.00 9.15  ? 19  LEU   A O   1 
ATOM   146  C  CB  . LEU   A 1 19  ? 37.836 14.801  37.133 1.00 9.63  ? 19  LEU   A CB  1 
ATOM   147  C  CG  . LEU   A 1 19  ? 36.324 15.021  37.156 1.00 11.24 ? 19  LEU   A CG  1 
ATOM   148  C  CD1 . LEU   A 1 19  ? 35.811 15.183  38.577 1.00 10.31 ? 19  LEU   A CD1 1 
ATOM   149  C  CD2 . LEU   A 1 19  ? 35.931 16.224  36.318 1.00 11.28 ? 19  LEU   A CD2 1 
ATOM   150  N  N   . VAL   A 1 20  ? 38.649 11.817  36.233 1.00 8.97  ? 20  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 20  ? 38.327 10.522  35.578 1.00 8.18  ? 20  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 20  ? 38.342 9.421   36.641 1.00 9.27  ? 20  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 20  ? 37.477 8.575   36.655 1.00 9.44  ? 20  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 20  ? 39.332 10.244  34.445 1.00 8.72  ? 20  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 20  ? 39.291 8.791   33.988 1.00 8.57  ? 20  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 20  ? 39.108 11.187  33.279 1.00 7.31  ? 20  VAL   A CG2 1 
ATOM   157  N  N   . ASN   A 1 21  ? 39.351 9.477   37.493 1.00 9.71  ? 21  ASN   A N   1 
ATOM   158  C  CA  . ASN   A 1 21  ? 39.449 8.458   38.557 1.00 7.57  ? 21  ASN   A CA  1 
ATOM   159  C  C   . ASN   A 1 21  ? 38.196 8.536   39.445 1.00 10.18 ? 21  ASN   A C   1 
ATOM   160  O  O   . ASN   A 1 21  ? 37.648 7.518   39.800 1.00 11.04 ? 21  ASN   A O   1 
ATOM   161  C  CB  . ASN   A 1 21  ? 40.752 8.596   39.348 1.00 10.04 ? 21  ASN   A CB  1 
ATOM   162  C  CG  . ASN   A 1 21  ? 41.017 7.436   40.289 1.00 11.08 ? 21  ASN   A CG  1 
ATOM   163  O  OD1 . ASN   A 1 21  ? 40.649 7.488   41.454 1.00 14.25 ? 21  ASN   A OD1 1 
ATOM   164  N  ND2 . ASN   A 1 21  ? 41.676 6.400   39.799 1.00 9.59  ? 21  ASN   A ND2 1 
ATOM   165  N  N   . LEU   A 1 22  ? 37.825 9.752   39.808 1.00 9.98  ? 22  LEU   A N   1 
ATOM   166  C  CA  . LEU   A 1 22  ? 36.648 9.909   40.693 1.00 10.61 ? 22  LEU   A CA  1 
ATOM   167  C  C   . LEU   A 1 22  ? 35.392 9.315   40.019 1.00 12.65 ? 22  LEU   A C   1 
ATOM   168  O  O   . LEU   A 1 22  ? 34.588 8.711   40.713 1.00 10.74 ? 22  LEU   A O   1 
ATOM   169  C  CB  . LEU   A 1 22  ? 36.457 11.400  40.977 1.00 8.60  ? 22  LEU   A CB  1 
ATOM   170  C  CG  . LEU   A 1 22  ? 37.449 12.012  41.956 1.00 10.48 ? 22  LEU   A CG  1 
ATOM   171  C  CD1 . LEU   A 1 22  ? 37.156 13.491  42.144 1.00 12.42 ? 22  LEU   A CD1 1 
ATOM   172  C  CD2 . LEU   A 1 22  ? 37.402 11.286  43.290 1.00 17.75 ? 22  LEU   A CD2 1 
ATOM   173  N  N   . TYR   A 1 23  ? 35.230 9.560   38.713 1.00 10.20 ? 23  TYR   A N   1 
ATOM   174  C  CA  . TYR   A 1 23  ? 34.004 9.074   38.024 1.00 11.55 ? 23  TYR   A CA  1 
ATOM   175  C  C   . TYR   A 1 23  ? 34.030 7.539   37.931 1.00 10.59 ? 23  TYR   A C   1 
ATOM   176  O  O   . TYR   A 1 23  ? 33.008 6.910   38.062 1.00 9.44  ? 23  TYR   A O   1 
ATOM   177  C  CB  . TYR   A 1 23  ? 33.857 9.750   36.655 1.00 7.55  ? 23  TYR   A CB  1 
ATOM   178  C  CG  . TYR   A 1 23  ? 33.012 10.994  36.724 1.00 9.16  ? 23  TYR   A CG  1 
ATOM   179  C  CD1 . TYR   A 1 23  ? 33.502 12.146  37.313 1.00 13.59 ? 23  TYR   A CD1 1 
ATOM   180  C  CD2 . TYR   A 1 23  ? 31.705 11.001  36.270 1.00 9.52  ? 23  TYR   A CD2 1 
ATOM   181  C  CE1 . TYR   A 1 23  ? 32.723 13.283  37.431 1.00 12.97 ? 23  TYR   A CE1 1 
ATOM   182  C  CE2 . TYR   A 1 23  ? 30.917 12.136  36.368 1.00 11.50 ? 23  TYR   A CE2 1 
ATOM   183  C  CZ  . TYR   A 1 23  ? 31.424 13.278  36.958 1.00 14.55 ? 23  TYR   A CZ  1 
ATOM   184  O  OH  . TYR   A 1 23  ? 30.670 14.407  37.078 1.00 14.26 ? 23  TYR   A OH  1 
ATOM   185  N  N   . LEU   A 1 24  ? 35.216 7.000   37.648 1.00 9.37  ? 24  LEU   A N   1 
ATOM   186  C  CA  . LEU   A 1 24  ? 35.313 5.523   37.561 1.00 9.30  ? 24  LEU   A CA  1 
ATOM   187  C  C   . LEU   A 1 24  ? 35.052 4.907   38.944 1.00 10.82 ? 24  LEU   A C   1 
ATOM   188  O  O   . LEU   A 1 24  ? 34.432 3.868   39.015 1.00 11.13 ? 24  LEU   A O   1 
ATOM   189  C  CB  . LEU   A 1 24  ? 36.687 5.130   37.025 1.00 9.78  ? 24  LEU   A CB  1 
ATOM   190  C  CG  . LEU   A 1 24  ? 36.897 5.412   35.539 1.00 10.48 ? 24  LEU   A CG  1 
ATOM   191  C  CD1 . LEU   A 1 24  ? 38.303 5.031   35.106 1.00 11.91 ? 24  LEU   A CD1 1 
ATOM   192  C  CD2 . LEU   A 1 24  ? 35.864 4.684   34.696 1.00 14.03 ? 24  LEU   A CD2 1 
ATOM   193  N  N   . ARG   A 1 25  ? 35.567 5.549   39.983 1.00 9.83  ? 25  ARG   A N   1 
ATOM   194  C  CA  . ARG   A 1 25  ? 35.279 5.072   41.364 1.00 10.19 ? 25  ARG   A CA  1 
ATOM   195  C  C   . ARG   A 1 25  ? 33.760 5.092   41.603 1.00 11.81 ? 25  ARG   A C   1 
ATOM   196  O  O   . ARG   A 1 25  ? 33.257 4.164   42.197 1.00 11.05 ? 25  ARG   A O   1 
ATOM   197  C  CB  . ARG   A 1 25  ? 35.944 5.966   42.411 1.00 12.63 ? 25  ARG   A CB  1 
ATOM   198  C  CG  . ARG   A 1 25  ? 37.444 5.782   42.571 1.00 19.57 ? 25  ARG   A CG  1 
ATOM   199  C  CD  . ARG   A 1 25  ? 38.050 6.836   43.482 1.00 23.86 ? 25  ARG   A CD  1 
ATOM   200  N  NE  . ARG   A 1 25  ? 37.497 6.812   44.827 1.00 22.60 ? 25  ARG   A NE  1 
ATOM   201  C  CZ  . ARG   A 1 25  ? 37.683 7.759   45.740 1.00 34.51 ? 25  ARG   A CZ  1 
ATOM   202  N  NH1 . ARG   A 1 25  ? 38.421 8.816   45.458 1.00 21.90 ? 25  ARG   A NH1 1 
ATOM   203  N  NH2 . ARG   A 1 25  ? 37.138 7.639   46.940 1.00 34.15 ? 25  ARG   A NH2 1 
ATOM   204  N  N   . ALA   A 1 26  ? 33.113 6.184   41.186 1.00 9.58  ? 26  ALA   A N   1 
ATOM   205  C  CA  . ALA   A 1 26  ? 31.655 6.312   41.381 1.00 9.18  ? 26  ALA   A CA  1 
ATOM   206  C  C   . ALA   A 1 26  ? 30.923 5.198   40.611 1.00 11.12 ? 26  ALA   A C   1 
ATOM   207  O  O   . ALA   A 1 26  ? 30.021 4.596   41.156 1.00 9.47  ? 26  ALA   A O   1 
ATOM   208  C  CB  . ALA   A 1 26  ? 31.221 7.682   40.918 1.00 11.53 ? 26  ALA   A CB  1 
ATOM   209  N  N   . SER   A 1 27  ? 31.367 4.961   39.375 1.00 9.68  ? 27  SER   A N   1 
ATOM   210  C  CA  . SER   A 1 27  ? 30.771 3.870   38.550 1.00 8.84  ? 27  SER   A CA  1 
ATOM   211  C  C   . SER   A 1 27  ? 30.895 2.540   39.297 1.00 11.69 ? 27  SER   A C   1 
ATOM   212  O  O   . SER   A 1 27  ? 29.934 1.807   39.354 1.00 10.21 ? 27  SER   A O   1 
ATOM   213  C  CB  . SER   A 1 27  ? 31.420 3.751   37.167 1.00 10.36 ? 27  SER   A CB  1 
ATOM   214  O  OG  . SER   A 1 27  ? 30.817 2.770   36.355 1.00 12.30 ? 27  SER   A OG  1 
ATOM   215  N  N   . TYR   A 1 28  ? 32.098 2.282   39.809 1.00 7.68  ? 28  TYR   A N   1 
ATOM   216  C  CA  . TYR   A 1 28  ? 32.348 1.024   40.554 1.00 5.66  ? 28  TYR   A CA  1 
ATOM   217  C  C   . TYR   A 1 28  ? 31.436 0.955   41.786 1.00 9.02  ? 28  TYR   A C   1 
ATOM   218  O  O   . TYR   A 1 28  ? 30.933 -0.097  42.110 1.00 8.74  ? 28  TYR   A O   1 
ATOM   219  C  CB  . TYR   A 1 28  ? 33.822 1.021   40.960 1.00 8.81  ? 28  TYR   A CB  1 
ATOM   220  C  CG  . TYR   A 1 28  ? 34.478 -0.301  41.257 1.00 8.58  ? 28  TYR   A CG  1 
ATOM   221  C  CD1 . TYR   A 1 28  ? 33.959 -1.492  40.789 1.00 9.59  ? 28  TYR   A CD1 1 
ATOM   222  C  CD2 . TYR   A 1 28  ? 35.651 -0.347  41.986 1.00 10.80 ? 28  TYR   A CD2 1 
ATOM   223  C  CE1 . TYR   A 1 28  ? 34.581 -2.699  41.060 1.00 9.50  ? 28  TYR   A CE1 1 
ATOM   224  C  CE2 . TYR   A 1 28  ? 36.288 -1.543  42.260 1.00 11.80 ? 28  TYR   A CE2 1 
ATOM   225  C  CZ  . TYR   A 1 28  ? 35.752 -2.726  41.792 1.00 8.58  ? 28  TYR   A CZ  1 
ATOM   226  O  OH  . TYR   A 1 28  ? 36.381 -3.905  42.067 1.00 11.80 ? 28  TYR   A OH  1 
ATOM   227  N  N   . THR   A 1 29  ? 31.302 2.086   42.477 1.00 7.72  ? 29  THR   A N   1 
ATOM   228  C  CA  . THR   A 1 29  ? 30.419 2.126   43.667 1.00 9.71  ? 29  THR   A CA  1 
ATOM   229  C  C   . THR   A 1 29  ? 28.995 1.740   43.247 1.00 8.18  ? 29  THR   A C   1 
ATOM   230  O  O   . THR   A 1 29  ? 28.378 0.924   43.918 1.00 9.45  ? 29  THR   A O   1 
ATOM   231  C  CB  . THR   A 1 29  ? 30.502 3.514   44.317 1.00 10.54 ? 29  THR   A CB  1 
ATOM   232  O  OG1 . THR   A 1 29  ? 31.812 3.649   44.860 1.00 9.36  ? 29  THR   A OG1 1 
ATOM   233  C  CG2 . THR   A 1 29  ? 29.450 3.716   45.384 1.00 11.62 ? 29  THR   A CG2 1 
ATOM   234  N  N   . TYR   A 1 30  ? 28.528 2.317   42.147 1.00 8.60  ? 30  TYR   A N   1 
ATOM   235  C  CA  . TYR   A 1 30  ? 27.141 2.047   41.694 1.00 10.82 ? 30  TYR   A CA  1 
ATOM   236  C  C   . TYR   A 1 30  ? 27.000 0.589   41.213 1.00 9.07  ? 30  TYR   A C   1 
ATOM   237  O  O   . TYR   A 1 30  ? 25.939 0.012   41.333 1.00 9.72  ? 30  TYR   A O   1 
ATOM   238  C  CB  . TYR   A 1 30  ? 26.710 3.082   40.646 1.00 7.77  ? 30  TYR   A CB  1 
ATOM   239  C  CG  . TYR   A 1 30  ? 26.402 4.434   41.226 1.00 8.13  ? 30  TYR   A CG  1 
ATOM   240  C  CD1 . TYR   A 1 30  ? 25.565 4.557   42.318 1.00 12.35 ? 30  TYR   A CD1 1 
ATOM   241  C  CD2 . TYR   A 1 30  ? 26.960 5.583   40.700 1.00 10.27 ? 30  TYR   A CD2 1 
ATOM   242  C  CE1 . TYR   A 1 30  ? 25.281 5.792   42.870 1.00 13.33 ? 30  TYR   A CE1 1 
ATOM   243  C  CE2 . TYR   A 1 30  ? 26.686 6.828   41.239 1.00 9.50  ? 30  TYR   A CE2 1 
ATOM   244  C  CZ  . TYR   A 1 30  ? 25.841 6.932   42.326 1.00 11.43 ? 30  TYR   A CZ  1 
ATOM   245  O  OH  . TYR   A 1 30  ? 25.556 8.145   42.871 1.00 12.31 ? 30  TYR   A OH  1 
ATOM   246  N  N   . LEU   A 1 31  ? 28.076 0.054   40.653 1.00 7.73  ? 31  LEU   A N   1 
ATOM   247  C  CA  . LEU   A 1 31  ? 28.043 -1.369  40.239 1.00 8.67  ? 31  LEU   A CA  1 
ATOM   248  C  C   . LEU   A 1 31  ? 27.811 -2.225  41.499 1.00 9.95  ? 31  LEU   A C   1 
ATOM   249  O  O   . LEU   A 1 31  ? 27.042 -3.156  41.432 1.00 10.75 ? 31  LEU   A O   1 
ATOM   250  C  CB  . LEU   A 1 31  ? 29.360 -1.736  39.543 1.00 9.37  ? 31  LEU   A CB  1 
ATOM   251  C  CG  . LEU   A 1 31  ? 29.448 -3.147  38.968 1.00 12.35 ? 31  LEU   A CG  1 
ATOM   252  C  CD1 . LEU   A 1 31  ? 28.563 -3.279  37.740 1.00 11.51 ? 31  LEU   A CD1 1 
ATOM   253  C  CD2 . LEU   A 1 31  ? 30.885 -3.494  38.620 1.00 11.69 ? 31  LEU   A CD2 1 
ATOM   254  N  N   . SER   A 1 32  ? 28.549 -1.906  42.569 1.00 8.24  ? 32  SER   A N   1 
ATOM   255  C  CA  . SER   A 1 32  ? 28.405 -2.683  43.829 1.00 7.61  ? 32  SER   A CA  1 
ATOM   256  C  C   . SER   A 1 32  ? 26.986 -2.514  44.391 1.00 8.12  ? 32  SER   A C   1 
ATOM   257  O  O   . SER   A 1 32  ? 26.385 -3.482  44.813 1.00 10.84 ? 32  SER   A O   1 
ATOM   258  C  CB  . SER   A 1 32  ? 29.436 -2.280  44.879 1.00 9.71  ? 32  SER   A CB  1 
ATOM   259  O  OG  . SER   A 1 32  ? 29.184 -2.911  46.116 1.00 10.30 ? 32  SER   A OG  1 
ATOM   260  N  N   . LEU   A 1 33  ? 26.529 -1.272  44.390 1.00 7.58  ? 33  LEU   A N   1 
ATOM   261  C  CA  . LEU   A 1 33  ? 25.153 -0.987  44.908 1.00 7.67  ? 33  LEU   A CA  1 
ATOM   262  C  C   . LEU   A 1 33  ? 24.114 -1.811  44.129 1.00 8.91  ? 33  LEU   A C   1 
ATOM   263  O  O   . LEU   A 1 33  ? 23.260 -2.428  44.744 1.00 10.74 ? 33  LEU   A O   1 
ATOM   264  C  CB  . LEU   A 1 33  ? 24.877 0.516   44.807 1.00 10.27 ? 33  LEU   A CB  1 
ATOM   265  C  CG  . LEU   A 1 33  ? 25.316 1.341   46.008 1.00 9.99  ? 33  LEU   A CG  1 
ATOM   266  C  CD1 . LEU   A 1 33  ? 25.521 2.790   45.601 1.00 10.26 ? 33  LEU   A CD1 1 
ATOM   267  C  CD2 . LEU   A 1 33  ? 24.286 1.237   47.116 1.00 10.04 ? 33  LEU   A CD2 1 
ATOM   268  N  N   . GLY   A 1 34  ? 24.225 -1.808  42.813 1.00 9.18  ? 34  GLY   A N   1 
ATOM   269  C  CA  . GLY   A 1 34  ? 23.266 -2.566  41.994 1.00 8.50  ? 34  GLY   A CA  1 
ATOM   270  C  C   . GLY   A 1 34  ? 23.255 -4.048  42.335 1.00 9.20  ? 34  GLY   A C   1 
ATOM   271  O  O   . GLY   A 1 34  ? 22.208 -4.617  42.440 1.00 11.15 ? 34  GLY   A O   1 
ATOM   272  N  N   . PHE   A 1 35  ? 24.451 -4.618  42.440 1.00 9.25  ? 35  PHE   A N   1 
ATOM   273  C  CA  . PHE   A 1 35  ? 24.493 -6.087  42.646 1.00 7.95  ? 35  PHE   A CA  1 
ATOM   274  C  C   . PHE   A 1 35  ? 24.058 -6.412  44.072 1.00 10.14 ? 35  PHE   A C   1 
ATOM   275  O  O   . PHE   A 1 35  ? 23.560 -7.499  44.299 1.00 11.62 ? 35  PHE   A O   1 
ATOM   276  C  CB  . PHE   A 1 35  ? 25.858 -6.677  42.299 1.00 10.26 ? 35  PHE   A CB  1 
ATOM   277  C  CG  . PHE   A 1 35  ? 25.941 -6.981  40.827 1.00 9.46  ? 35  PHE   A CG  1 
ATOM   278  C  CD1 . PHE   A 1 35  ? 25.284 -8.078  40.302 1.00 11.45 ? 35  PHE   A CD1 1 
ATOM   279  C  CD2 . PHE   A 1 35  ? 26.600 -6.127  39.961 1.00 10.99 ? 35  PHE   A CD2 1 
ATOM   280  C  CE1 . PHE   A 1 35  ? 25.316 -8.337  38.944 1.00 12.51 ? 35  PHE   A CE1 1 
ATOM   281  C  CE2 . PHE   A 1 35  ? 26.635 -6.390  38.601 1.00 13.42 ? 35  PHE   A CE2 1 
ATOM   282  C  CZ  . PHE   A 1 35  ? 25.993 -7.495  38.096 1.00 13.87 ? 35  PHE   A CZ  1 
ATOM   283  N  N   . TYR   A 1 36  ? 24.254 -5.470  45.001 1.00 8.88  ? 36  TYR   A N   1 
ATOM   284  C  CA  . TYR   A 1 36  ? 23.759 -5.742  46.368 1.00 8.34  ? 36  TYR   A CA  1 
ATOM   285  C  C   . TYR   A 1 36  ? 22.227 -5.877  46.334 1.00 8.13  ? 36  TYR   A C   1 
ATOM   286  O  O   . TYR   A 1 36  ? 21.678 -6.749  46.969 1.00 8.97  ? 36  TYR   A O   1 
ATOM   287  C  CB  . TYR   A 1 36  ? 24.180 -4.610  47.310 1.00 6.71  ? 36  TYR   A CB  1 
ATOM   288  C  CG  . TYR   A 1 36  ? 23.489 -4.564  48.647 1.00 8.37  ? 36  TYR   A CG  1 
ATOM   289  C  CD1 . TYR   A 1 36  ? 23.870 -5.406  49.673 1.00 8.47  ? 36  TYR   A CD1 1 
ATOM   290  C  CD2 . TYR   A 1 36  ? 22.477 -3.655  48.895 1.00 12.71 ? 36  TYR   A CD2 1 
ATOM   291  C  CE1 . TYR   A 1 36  ? 23.241 -5.368  50.904 1.00 9.88  ? 36  TYR   A CE1 1 
ATOM   292  C  CE2 . TYR   A 1 36  ? 21.836 -3.604  50.119 1.00 11.00 ? 36  TYR   A CE2 1 
ATOM   293  C  CZ  . TYR   A 1 36  ? 22.226 -4.459  51.131 1.00 10.67 ? 36  TYR   A CZ  1 
ATOM   294  O  OH  . TYR   A 1 36  ? 21.601 -4.408  52.339 1.00 12.65 ? 36  TYR   A OH  1 
ATOM   295  N  N   . PHE   A 1 37  ? 21.578 -4.966  45.612 1.00 8.22  ? 37  PHE   A N   1 
ATOM   296  C  CA  . PHE   A 1 37  ? 20.088 -4.976  45.604 1.00 8.15  ? 37  PHE   A CA  1 
ATOM   297  C  C   . PHE   A 1 37  ? 19.569 -6.161  44.758 1.00 11.66 ? 37  PHE   A C   1 
ATOM   298  O  O   . PHE   A 1 37  ? 18.372 -6.417  44.816 1.00 11.25 ? 37  PHE   A O   1 
ATOM   299  C  CB  . PHE   A 1 37  ? 19.560 -3.589  45.216 1.00 11.25 ? 37  PHE   A CB  1 
ATOM   300  C  CG  . PHE   A 1 37  ? 19.640 -2.598  46.347 1.00 8.56  ? 37  PHE   A CG  1 
ATOM   301  C  CD1 . PHE   A 1 37  ? 18.679 -2.585  47.341 1.00 8.79  ? 37  PHE   A CD1 1 
ATOM   302  C  CD2 . PHE   A 1 37  ? 20.690 -1.700  46.434 1.00 9.18  ? 37  PHE   A CD2 1 
ATOM   303  C  CE1 . PHE   A 1 37  ? 18.758 -1.689  48.393 1.00 9.94  ? 37  PHE   A CE1 1 
ATOM   304  C  CE2 . PHE   A 1 37  ? 20.770 -0.805  47.485 1.00 9.74  ? 37  PHE   A CE2 1 
ATOM   305  C  CZ  . PHE   A 1 37  ? 19.801 -0.798  48.461 1.00 9.05  ? 37  PHE   A CZ  1 
ATOM   306  N  N   . ASP   A 1 38  ? 20.439 -6.773  43.956 1.00 8.69  ? 38  ASP   A N   1 
ATOM   307  C  CA  . ASP   A 1 38  ? 20.083 -7.956  43.133 1.00 9.96  ? 38  ASP   A CA  1 
ATOM   308  C  C   . ASP   A 1 38  ? 20.206 -9.237  43.975 1.00 9.56  ? 38  ASP   A C   1 
ATOM   309  O  O   . ASP   A 1 38  ? 19.826 -10.285 43.487 1.00 13.92 ? 38  ASP   A O   1 
ATOM   310  C  CB  . ASP   A 1 38  ? 20.991 -8.039  41.908 1.00 9.75  ? 38  ASP   A CB  1 
ATOM   311  C  CG  . ASP   A 1 38  ? 20.750 -9.218  40.993 1.00 12.58 ? 38  ASP   A CG  1 
ATOM   312  O  OD1 . ASP   A 1 38  ? 19.692 -9.259  40.366 1.00 15.90 ? 38  ASP   A OD1 1 
ATOM   313  O  OD2 . ASP   A 1 38  ? 21.646 -10.055 40.902 1.00 12.39 ? 38  ASP   A OD2 1 
ATOM   314  N  N   . ARG   A 1 39  ? 20.743 -9.110  45.181 1.00 8.72  ? 39  ARG   A N   1 
ATOM   315  C  CA  . ARG   A 1 39  ? 20.875 -10.305 46.047 1.00 9.26  ? 39  ARG   A CA  1 
ATOM   316  C  C   . ARG   A 1 39  ? 19.493 -10.915 46.323 1.00 10.16 ? 39  ARG   A C   1 
ATOM   317  O  O   . ARG   A 1 39  ? 18.562 -10.177 46.556 1.00 9.83  ? 39  ARG   A O   1 
ATOM   318  C  CB  . ARG   A 1 39  ? 21.578 -9.965  47.363 1.00 9.75  ? 39  ARG   A CB  1 
ATOM   319  C  CG  . ARG   A 1 39  ? 23.060 -9.652  47.238 1.00 9.86  ? 39  ARG   A CG  1 
ATOM   320  C  CD  . ARG   A 1 39  ? 23.630 -9.369  48.613 1.00 11.09 ? 39  ARG   A CD  1 
ATOM   321  N  NE  . ARG   A 1 39  ? 23.362 -10.519 49.464 1.00 11.98 ? 39  ARG   A NE  1 
ATOM   322  C  CZ  . ARG   A 1 39  ? 24.094 -11.634 49.490 1.00 15.24 ? 39  ARG   A CZ  1 
ATOM   323  N  NH1 . ARG   A 1 39  ? 25.182 -11.740 48.746 1.00 11.28 ? 39  ARG   A NH1 1 
ATOM   324  N  NH2 . ARG   A 1 39  ? 23.746 -12.638 50.274 1.00 13.79 ? 39  ARG   A NH2 1 
ATOM   325  N  N   . ASP   A 1 40  ? 19.453 -12.242 46.453 1.00 8.61  ? 40  ASP   A N   1 
ATOM   326  C  CA  . ASP   A 1 40  ? 18.155 -12.914 46.737 1.00 9.08  ? 40  ASP   A CA  1 
ATOM   327  C  C   . ASP   A 1 40  ? 17.621 -12.496 48.110 1.00 10.35 ? 40  ASP   A C   1 
ATOM   328  O  O   . ASP   A 1 40  ? 16.421 -12.594 48.312 1.00 11.51 ? 40  ASP   A O   1 
ATOM   329  C  CB  . ASP   A 1 40  ? 18.267 -14.441 46.681 1.00 8.92  ? 40  ASP   A CB  1 
ATOM   330  C  CG  . ASP   A 1 40  ? 19.053 -15.042 47.830 1.00 11.90 ? 40  ASP   A CG  1 
ATOM   331  O  OD1 . ASP   A 1 40  ? 20.280 -15.143 47.697 1.00 12.31 ? 40  ASP   A OD1 1 
ATOM   332  O  OD2 . ASP   A 1 40  ? 18.421 -15.421 48.828 1.00 12.32 ? 40  ASP   A OD2 1 
ATOM   333  N  N   . ASP   A 1 41  ? 18.510 -12.049 48.992 1.00 8.99  ? 41  ASP   A N   1 
ATOM   334  C  CA  . ASP   A 1 41  ? 18.112 -11.654 50.368 1.00 9.98  ? 41  ASP   A CA  1 
ATOM   335  C  C   . ASP   A 1 41  ? 17.907 -10.128 50.478 1.00 8.85  ? 41  ASP   A C   1 
ATOM   336  O  O   . ASP   A 1 41  ? 17.726 -9.653  51.598 1.00 9.95  ? 41  ASP   A O   1 
ATOM   337  C  CB  . ASP   A 1 41  ? 19.063 -12.213 51.433 1.00 10.15 ? 41  ASP   A CB  1 
ATOM   338  C  CG  . ASP   A 1 41  ? 20.496 -11.732 51.299 1.00 12.48 ? 41  ASP   A CG  1 
ATOM   339  O  OD1 . ASP   A 1 41  ? 20.774 -10.964 50.369 1.00 12.46 ? 41  ASP   A OD1 1 
ATOM   340  O  OD2 . ASP   A 1 41  ? 21.311 -12.143 52.132 1.00 17.19 ? 41  ASP   A OD2 1 
ATOM   341  N  N   . VAL   A 1 42  ? 17.914 -9.430  49.355 1.00 8.39  ? 42  VAL   A N   1 
ATOM   342  C  CA  . VAL   A 1 42  ? 17.630 -7.960  49.326 1.00 8.87  ? 42  VAL   A CA  1 
ATOM   343  C  C   . VAL   A 1 42  ? 16.492 -7.813  48.307 1.00 10.78 ? 42  VAL   A C   1 
ATOM   344  O  O   . VAL   A 1 42  ? 15.422 -7.349  48.686 1.00 11.19 ? 42  VAL   A O   1 
ATOM   345  C  CB  . VAL   A 1 42  ? 18.885 -7.160  48.943 1.00 8.73  ? 42  VAL   A CB  1 
ATOM   346  C  CG1 . VAL   A 1 42  ? 18.573 -5.674  48.873 1.00 11.12 ? 42  VAL   A CG1 1 
ATOM   347  C  CG2 . VAL   A 1 42  ? 20.038 -7.417  49.900 1.00 10.42 ? 42  VAL   A CG2 1 
ATOM   348  N  N   . ALA   A 1 43  ? 16.745 -8.229  47.072 1.00 9.29  ? 43  ALA   A N   1 
ATOM   349  C  CA  . ALA   A 1 43  ? 15.663 -8.401  46.067 1.00 7.95  ? 43  ALA   A CA  1 
ATOM   350  C  C   . ALA   A 1 43  ? 14.785 -7.167  45.853 1.00 7.75  ? 43  ALA   A C   1 
ATOM   351  O  O   . ALA   A 1 43  ? 13.590 -7.271  46.020 1.00 11.29 ? 43  ALA   A O   1 
ATOM   352  C  CB  . ALA   A 1 43  ? 14.839 -9.606  46.446 1.00 12.07 ? 43  ALA   A CB  1 
ATOM   353  N  N   . LEU   A 1 44  ? 15.425 -6.073  45.473 1.00 9.88  ? 44  LEU   A N   1 
ATOM   354  C  CA  . LEU   A 1 44  ? 14.687 -4.840  45.137 1.00 8.21  ? 44  LEU   A CA  1 
ATOM   355  C  C   . LEU   A 1 44  ? 15.132 -4.459  43.714 1.00 8.71  ? 44  LEU   A C   1 
ATOM   356  O  O   . LEU   A 1 44  ? 16.002 -3.638  43.555 1.00 10.13 ? 44  LEU   A O   1 
ATOM   357  C  CB  . LEU   A 1 44  ? 15.021 -3.809  46.206 1.00 9.19  ? 44  LEU   A CB  1 
ATOM   358  C  CG  . LEU   A 1 44  ? 14.396 -4.085  47.570 1.00 7.68  ? 44  LEU   A CG  1 
ATOM   359  C  CD1 . LEU   A 1 44  ? 15.027 -3.220  48.646 1.00 7.80  ? 44  LEU   A CD1 1 
ATOM   360  C  CD2 . LEU   A 1 44  ? 12.889 -3.864  47.528 1.00 10.53 ? 44  LEU   A CD2 1 
ATOM   361  N  N   . GLU   A 1 45  ? 14.449 -5.031  42.726 1.00 8.59  ? 45  GLU   A N   1 
ATOM   362  C  CA  . GLU   A 1 45  ? 14.857 -4.885  41.301 1.00 10.70 ? 45  GLU   A CA  1 
ATOM   363  C  C   . GLU   A 1 45  ? 14.927 -3.413  40.856 1.00 9.06  ? 45  GLU   A C   1 
ATOM   364  O  O   . GLU   A 1 45  ? 15.854 -3.044  40.166 1.00 10.77 ? 45  GLU   A O   1 
ATOM   365  C  CB  . GLU   A 1 45  ? 13.912 -5.722  40.430 1.00 13.05 ? 45  GLU   A CB  1 
ATOM   366  C  CG  . GLU   A 1 45  ? 14.109 -5.600  38.936 1.00 18.97 ? 45  GLU   A CG  1 
ATOM   367  C  CD  . GLU   A 1 45  ? 13.026 -6.346  38.167 1.00 53.09 ? 45  GLU   A CD  1 
ATOM   368  O  OE1 . GLU   A 1 45  ? 12.821 -7.540  38.448 1.00 40.50 ? 45  GLU   A OE1 1 
ATOM   369  O  OE2 . GLU   A 1 45  ? 12.363 -5.721  37.321 1.00 43.05 ? 45  GLU   A OE2 1 
ATOM   370  N  N   . GLY   A 1 46  ? 13.939 -2.647  41.251 1.00 9.11  ? 46  GLY   A N   1 
ATOM   371  C  CA  . GLY   A 1 46  ? 13.956 -1.234  40.825 1.00 10.21 ? 46  GLY   A CA  1 
ATOM   372  C  C   . GLY   A 1 46  ? 15.180 -0.503  41.369 1.00 8.82  ? 46  GLY   A C   1 
ATOM   373  O  O   . GLY   A 1 46  ? 15.616 0.433   40.733 1.00 10.07 ? 46  GLY   A O   1 
ATOM   374  N  N   . VAL   A 1 47  ? 15.582 -0.865  42.573 1.00 9.76  ? 47  VAL   A N   1 
ATOM   375  C  CA  . VAL   A 1 47  ? 16.759 -0.203  43.204 1.00 7.20  ? 47  VAL   A CA  1 
ATOM   376  C  C   . VAL   A 1 47  ? 18.024 -0.700  42.485 1.00 11.30 ? 47  VAL   A C   1 
ATOM   377  O  O   . VAL   A 1 47  ? 18.902 0.087   42.150 1.00 10.31 ? 47  VAL   A O   1 
ATOM   378  C  CB  . VAL   A 1 47  ? 16.806 -0.470  44.720 1.00 8.29  ? 47  VAL   A CB  1 
ATOM   379  C  CG1 . VAL   A 1 47  ? 17.887 0.359   45.390 1.00 9.78  ? 47  VAL   A CG1 1 
ATOM   380  C  CG2 . VAL   A 1 47  ? 15.457 -0.222  45.375 1.00 9.88  ? 47  VAL   A CG2 1 
ATOM   381  N  N   . CYS   A 1 48  ? 18.045 -2.003  42.211 1.00 8.72  ? 48  CYS   A N   1 
ATOM   382  C  CA  . CYS   A 1 48  ? 19.161 -2.566  41.421 1.00 7.58  ? 48  CYS   A CA  1 
ATOM   383  C  C   . CYS   A 1 48  ? 19.273 -1.821  40.079 1.00 10.28 ? 48  CYS   A C   1 
ATOM   384  O  O   . CYS   A 1 48  ? 20.349 -1.387  39.713 1.00 11.71 ? 48  CYS   A O   1 
ATOM   385  C  CB  . CYS   A 1 48  ? 18.886 -4.048  41.220 1.00 9.78  ? 48  CYS   A CB  1 
ATOM   386  S  SG  . CYS   A 1 48  ? 19.895 -4.845  39.939 1.00 13.81 ? 48  CYS   A SG  1 
ATOM   387  N  N   . HIS   A 1 49  ? 18.140 -1.679  39.397 1.00 10.21 ? 49  HIS   A N   1 
ATOM   388  C  CA  . HIS   A 1 49  ? 18.162 -1.021  38.070 1.00 10.52 ? 49  HIS   A CA  1 
ATOM   389  C  C   . HIS   A 1 49  ? 18.601 0.445   38.190 1.00 10.11 ? 49  HIS   A C   1 
ATOM   390  O  O   . HIS   A 1 49  ? 19.314 0.912   37.316 1.00 10.64 ? 49  HIS   A O   1 
ATOM   391  C  CB  . HIS   A 1 49  ? 16.794 -1.164  37.396 1.00 14.27 ? 49  HIS   A CB  1 
ATOM   392  C  CG  . HIS   A 1 49  ? 16.528 -2.559  36.935 1.00 23.67 ? 49  HIS   A CG  1 
ATOM   393  N  ND1 . HIS   A 1 49  ? 15.482 -2.878  36.091 1.00 40.01 ? 49  HIS   A ND1 1 
ATOM   394  C  CD2 . HIS   A 1 49  ? 17.161 -3.720  37.203 1.00 32.28 ? 49  HIS   A CD2 1 
ATOM   395  C  CE1 . HIS   A 1 49  ? 15.487 -4.174  35.856 1.00 28.88 ? 49  HIS   A CE1 1 
ATOM   396  N  NE2 . HIS   A 1 49  ? 16.505 -4.712  36.529 1.00 30.31 ? 49  HIS   A NE2 1 
ATOM   397  N  N   . PHE   A 1 50  ? 18.158 1.125   39.236 1.00 8.46  ? 50  PHE   A N   1 
ATOM   398  C  CA  . PHE   A 1 50  ? 18.518 2.559   39.380 1.00 9.97  ? 50  PHE   A CA  1 
ATOM   399  C  C   . PHE   A 1 50  ? 20.048 2.675   39.439 1.00 8.70  ? 50  PHE   A C   1 
ATOM   400  O  O   . PHE   A 1 50  ? 20.644 3.455   38.728 1.00 11.05 ? 50  PHE   A O   1 
ATOM   401  C  CB  . PHE   A 1 50  ? 17.873 3.129   40.647 1.00 9.05  ? 50  PHE   A CB  1 
ATOM   402  C  CG  . PHE   A 1 50  ? 18.184 4.565   40.978 1.00 10.44 ? 50  PHE   A CG  1 
ATOM   403  C  CD1 . PHE   A 1 50  ? 17.598 5.594   40.265 1.00 14.04 ? 50  PHE   A CD1 1 
ATOM   404  C  CD2 . PHE   A 1 50  ? 19.026 4.886   42.027 1.00 10.39 ? 50  PHE   A CD2 1 
ATOM   405  C  CE1 . PHE   A 1 50  ? 17.876 6.915   40.572 1.00 15.13 ? 50  PHE   A CE1 1 
ATOM   406  C  CE2 . PHE   A 1 50  ? 19.300 6.208   42.333 1.00 12.22 ? 50  PHE   A CE2 1 
ATOM   407  C  CZ  . PHE   A 1 50  ? 18.718 7.218   41.610 1.00 13.29 ? 50  PHE   A CZ  1 
ATOM   408  N  N   . PHE   A 1 51  ? 20.640 1.902   40.334 1.00 8.85  ? 51  PHE   A N   1 
ATOM   409  C  CA  . PHE   A 1 51  ? 22.106 2.065   40.545 1.00 9.36  ? 51  PHE   A CA  1 
ATOM   410  C  C   . PHE   A 1 51  ? 22.917 1.477   39.384 1.00 10.90 ? 51  PHE   A C   1 
ATOM   411  O  O   . PHE   A 1 51  ? 23.939 2.029   39.029 1.00 12.76 ? 51  PHE   A O   1 
ATOM   412  C  CB  . PHE   A 1 51  ? 22.519 1.442   41.884 1.00 7.97  ? 51  PHE   A CB  1 
ATOM   413  C  CG  . PHE   A 1 51  ? 22.025 2.211   43.082 1.00 8.57  ? 51  PHE   A CG  1 
ATOM   414  C  CD1 . PHE   A 1 51  ? 22.257 3.569   43.194 1.00 11.42 ? 51  PHE   A CD1 1 
ATOM   415  C  CD2 . PHE   A 1 51  ? 21.317 1.584   44.092 1.00 8.11  ? 51  PHE   A CD2 1 
ATOM   416  C  CE1 . PHE   A 1 51  ? 21.801 4.278   44.292 1.00 9.17  ? 51  PHE   A CE1 1 
ATOM   417  C  CE2 . PHE   A 1 51  ? 20.856 2.296   45.187 1.00 9.26  ? 51  PHE   A CE2 1 
ATOM   418  C  CZ  . PHE   A 1 51  ? 21.102 3.641   45.288 1.00 10.50 ? 51  PHE   A CZ  1 
ATOM   419  N  N   . ARG   A 1 52  ? 22.438 0.394   38.803 1.00 12.24 ? 52  ARG   A N   1 
ATOM   420  C  CA  . ARG   A 1 52  ? 23.144 -0.117  37.586 1.00 12.25 ? 52  ARG   A CA  1 
ATOM   421  C  C   . ARG   A 1 52  ? 23.249 0.940   36.450 1.00 13.28 ? 52  ARG   A C   1 
ATOM   422  O  O   . ARG   A 1 52  ? 24.273 1.243   35.758 1.00 15.12 ? 52  ARG   A O   1 
ATOM   423  C  CB  . ARG   A 1 52  ? 22.474 -1.394  37.068 1.00 15.49 ? 52  ARG   A CB  1 
ATOM   424  C  CG  . ARG   A 1 52  ? 23.055 -1.907  35.761 1.00 13.89 ? 52  ARG   A CG  1 
ATOM   425  C  CD  . ARG   A 1 52  ? 22.308 -3.125  35.258 1.00 20.48 ? 52  ARG   A CD  1 
ATOM   426  N  NE  . ARG   A 1 52  ? 20.919 -2.834  34.944 1.00 19.46 ? 52  ARG   A NE  1 
ATOM   427  C  CZ  . ARG   A 1 52  ? 19.975 -3.755  34.808 1.00 20.30 ? 52  ARG   A CZ  1 
ATOM   428  N  NH1 . ARG   A 1 52  ? 20.273 -5.032  34.960 1.00 25.66 ? 52  ARG   A NH1 1 
ATOM   429  N  NH2 . ARG   A 1 52  ? 18.738 -3.396  34.520 1.00 27.42 ? 52  ARG   A NH2 1 
ATOM   430  N  N   . PHE   A 1 53  ? 22.104 1.610   36.279 1.00 13.54 ? 53  PHE   A N   1 
ATOM   431  C  CA  . PHE   A 1 53  ? 22.064 2.691   35.261 1.00 13.11 ? 53  PHE   A CA  1 
ATOM   432  C  C   . PHE   A 1 53  ? 23.085 3.782   35.605 1.00 15.70 ? 53  PHE   A C   1 
ATOM   433  O  O   . PHE   A 1 53  ? 23.759 4.278   34.725 1.00 14.94 ? 53  PHE   A O   1 
ATOM   434  C  CB  . PHE   A 1 53  ? 20.675 3.316   35.126 1.00 16.07 ? 53  PHE   A CB  1 
ATOM   435  C  CG  . PHE   A 1 53  ? 20.697 4.579   34.306 1.00 21.50 ? 53  PHE   A CG  1 
ATOM   436  C  CD1 . PHE   A 1 53  ? 20.664 4.521   32.925 1.00 42.47 ? 53  PHE   A CD1 1 
ATOM   437  C  CD2 . PHE   A 1 53  ? 20.802 5.820   34.909 1.00 24.41 ? 53  PHE   A CD2 1 
ATOM   438  C  CE1 . PHE   A 1 53  ? 20.710 5.678   32.166 1.00 33.77 ? 53  PHE   A CE1 1 
ATOM   439  C  CE2 . PHE   A 1 53  ? 20.850 6.978   34.149 1.00 36.40 ? 53  PHE   A CE2 1 
ATOM   440  C  CZ  . PHE   A 1 53  ? 20.804 6.903   32.779 1.00 40.43 ? 53  PHE   A CZ  1 
ATOM   441  N  N   . LEU   A 1 54  ? 23.157 4.128   36.888 1.00 11.65 ? 54  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 54  ? 24.106 5.201   37.274 1.00 11.41 ? 54  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 54  ? 25.555 4.713   37.085 1.00 10.92 ? 54  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 54  ? 26.400 5.513   36.782 1.00 11.34 ? 54  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 54  ? 23.857 5.606   38.723 1.00 10.85 ? 54  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 54  ? 22.558 6.370   38.942 1.00 10.82 ? 54  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 54  ? 22.367 6.717   40.406 1.00 13.18 ? 54  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 54  ? 22.525 7.616   38.075 1.00 18.55 ? 54  LEU   A CD2 1 
ATOM   449  N  N   . ALA   A 1 55  ? 25.786 3.408   37.236 1.00 11.10 ? 55  ALA   A N   1 
ATOM   450  C  CA  . ALA   A 1 55  ? 27.145 2.893   36.997 1.00 10.84 ? 55  ALA   A CA  1 
ATOM   451  C  C   . ALA   A 1 55  ? 27.541 3.246   35.560 1.00 15.74 ? 55  ALA   A C   1 
ATOM   452  O  O   . ALA   A 1 55  ? 28.631 3.721   35.332 1.00 12.03 ? 55  ALA   A O   1 
ATOM   453  C  CB  . ALA   A 1 55  ? 27.183 1.397   37.231 1.00 11.34 ? 55  ALA   A CB  1 
ATOM   454  N  N   . PHE   A 1 56  ? 26.623 2.982   34.643 1.00 11.59 ? 56  PHE   A N   1 
ATOM   455  C  CA  . PHE   A 1 56  ? 26.942 3.226   33.213 1.00 11.99 ? 56  PHE   A CA  1 
ATOM   456  C  C   . PHE   A 1 56  ? 27.084 4.732   32.982 1.00 12.85 ? 56  PHE   A C   1 
ATOM   457  O  O   . PHE   A 1 56  ? 27.973 5.153   32.247 1.00 13.38 ? 56  PHE   A O   1 
ATOM   458  C  CB  . PHE   A 1 56  ? 25.876 2.629   32.295 1.00 12.95 ? 56  PHE   A CB  1 
ATOM   459  C  CG  . PHE   A 1 56  ? 25.633 1.138   32.481 1.00 30.09 ? 56  PHE   A CG  1 
ATOM   460  C  CD1 . PHE   A 1 56  ? 26.639 0.291   32.927 1.00 42.02 ? 56  PHE   A CD1 1 
ATOM   461  C  CD2 . PHE   A 1 56  ? 24.387 0.585   32.216 1.00 47.44 ? 56  PHE   A CD2 1 
ATOM   462  C  CE1 . PHE   A 1 56  ? 26.401 -1.066  33.093 1.00 41.38 ? 56  PHE   A CE1 1 
ATOM   463  C  CE2 . PHE   A 1 56  ? 24.162 -0.774  32.371 1.00 40.19 ? 56  PHE   A CE2 1 
ATOM   464  C  CZ  . PHE   A 1 56  ? 25.169 -1.594  32.813 1.00 35.12 ? 56  PHE   A CZ  1 
ATOM   465  N  N   . PHE   A 1 57  ? 26.184 5.496   33.589 1.00 13.54 ? 57  PHE   A N   1 
ATOM   466  C  CA  . PHE   A 1 57  ? 26.187 6.962   33.367 1.00 11.94 ? 57  PHE   A CA  1 
ATOM   467  C  C   . PHE   A 1 57  ? 27.528 7.547   33.831 1.00 11.02 ? 57  PHE   A C   1 
ATOM   468  O  O   . PHE   A 1 57  ? 28.069 8.433   33.190 1.00 13.06 ? 57  PHE   A O   1 
ATOM   469  C  CB  . PHE   A 1 57  ? 24.961 7.553   34.066 1.00 13.62 ? 57  PHE   A CB  1 
ATOM   470  C  CG  . PHE   A 1 57  ? 24.626 8.990   33.781 1.00 22.12 ? 57  PHE   A CG  1 
ATOM   471  C  CD1 . PHE   A 1 57  ? 24.655 9.486   32.491 1.00 38.83 ? 57  PHE   A CD1 1 
ATOM   472  C  CD2 . PHE   A 1 57  ? 24.248 9.836   34.807 1.00 28.78 ? 57  PHE   A CD2 1 
ATOM   473  C  CE1 . PHE   A 1 57  ? 24.336 10.809  32.236 1.00 38.66 ? 57  PHE   A CE1 1 
ATOM   474  C  CE2 . PHE   A 1 57  ? 23.919 11.156  34.550 1.00 33.71 ? 57  PHE   A CE2 1 
ATOM   475  C  CZ  . PHE   A 1 57  ? 23.969 11.639  33.266 1.00 31.70 ? 57  PHE   A CZ  1 
ATOM   476  N  N   . LYS   A 1 58  ? 27.972 7.105   34.991 1.00 9.94  ? 58  LYS   A N   1 
ATOM   477  C  CA  . LYS   A 1 58  ? 29.243 7.650   35.523 1.00 8.61  ? 58  LYS   A CA  1 
ATOM   478  C  C   . LYS   A 1 58  ? 30.409 7.165   34.659 1.00 12.06 ? 58  LYS   A C   1 
ATOM   479  O  O   . LYS   A 1 58  ? 31.330 7.939   34.458 1.00 11.71 ? 58  LYS   A O   1 
ATOM   480  C  CB  . LYS   A 1 58  ? 29.438 7.220   36.978 1.00 9.26  ? 58  LYS   A CB  1 
ATOM   481  C  CG  . LYS   A 1 58  ? 28.519 7.898   37.976 1.00 9.43  ? 58  LYS   A CG  1 
ATOM   482  C  CD  . LYS   A 1 58  ? 28.539 9.397   37.812 1.00 13.42 ? 58  LYS   A CD  1 
ATOM   483  C  CE  . LYS   A 1 58  ? 27.404 10.077  38.537 1.00 21.89 ? 58  LYS   A CE  1 
ATOM   484  N  NZ  . LYS   A 1 58  ? 27.532 11.552  38.512 1.00 17.45 ? 58  LYS   A NZ  1 
ATOM   485  N  N   . PHE   A 1 59  ? 30.343 5.928   34.154 1.00 10.70 ? 59  PHE   A N   1 
ATOM   486  C  CA  . PHE   A 1 59  ? 31.411 5.469   33.223 1.00 10.37 ? 59  PHE   A CA  1 
ATOM   487  C  C   . PHE   A 1 59  ? 31.449 6.393   32.005 1.00 10.94 ? 59  PHE   A C   1 
ATOM   488  O  O   . PHE   A 1 59  ? 32.518 6.807   31.577 1.00 9.88  ? 59  PHE   A O   1 
ATOM   489  C  CB  . PHE   A 1 59  ? 31.193 4.039   32.730 1.00 10.41 ? 59  PHE   A CB  1 
ATOM   490  C  CG  . PHE   A 1 59  ? 32.161 3.705   31.631 1.00 10.97 ? 59  PHE   A CG  1 
ATOM   491  C  CD1 . PHE   A 1 59  ? 33.477 3.404   31.926 1.00 12.64 ? 59  PHE   A CD1 1 
ATOM   492  C  CD2 . PHE   A 1 59  ? 31.777 3.786   30.306 1.00 15.72 ? 59  PHE   A CD2 1 
ATOM   493  C  CE1 . PHE   A 1 59  ? 34.381 3.145   30.911 1.00 16.49 ? 59  PHE   A CE1 1 
ATOM   494  C  CE2 . PHE   A 1 59  ? 32.685 3.535   29.293 1.00 19.70 ? 59  PHE   A CE2 1 
ATOM   495  C  CZ  . PHE   A 1 59  ? 33.981 3.212   29.600 1.00 20.31 ? 59  PHE   A CZ  1 
ATOM   496  N  N   . PHE   A 1 60  ? 30.272 6.765   31.522 1.00 10.83 ? 60  PHE   A N   1 
ATOM   497  C  CA  . PHE   A 1 60  ? 30.187 7.615   30.302 1.00 12.02 ? 60  PHE   A CA  1 
ATOM   498  C  C   . PHE   A 1 60  ? 30.788 8.998   30.566 1.00 11.92 ? 60  PHE   A C   1 
ATOM   499  O  O   . PHE   A 1 60  ? 31.367 9.580   29.676 1.00 12.40 ? 60  PHE   A O   1 
ATOM   500  C  CB  . PHE   A 1 60  ? 28.728 7.716   29.862 1.00 18.17 ? 60  PHE   A CB  1 
ATOM   501  C  CG  . PHE   A 1 60  ? 28.396 8.768   28.839 1.00 35.42 ? 60  PHE   A CG  1 
ATOM   502  C  CD1 . PHE   A 1 60  ? 28.746 8.595   27.512 1.00 38.31 ? 60  PHE   A CD1 1 
ATOM   503  C  CD2 . PHE   A 1 60  ? 27.684 9.901   29.197 1.00 41.55 ? 60  PHE   A CD2 1 
ATOM   504  C  CE1 . PHE   A 1 60  ? 28.418 9.554   26.568 1.00 38.14 ? 60  PHE   A CE1 1 
ATOM   505  C  CE2 . PHE   A 1 60  ? 27.357 10.856  28.251 1.00 40.27 ? 60  PHE   A CE2 1 
ATOM   506  C  CZ  . PHE   A 1 60  ? 27.723 10.680  26.940 1.00 37.92 ? 60  PHE   A CZ  1 
ATOM   507  N  N   . GLY   A 1 61  ? 30.628 9.467   31.788 1.00 10.29 ? 61  GLY   A N   1 
ATOM   508  C  CA  . GLY   A 1 61  ? 31.228 10.756  32.174 1.00 10.67 ? 61  GLY   A CA  1 
ATOM   509  C  C   . GLY   A 1 61  ? 32.737 10.669  32.113 1.00 11.01 ? 61  GLY   A C   1 
ATOM   510  O  O   . GLY   A 1 61  ? 33.376 11.551  31.601 1.00 11.20 ? 61  GLY   A O   1 
ATOM   511  N  N   . ALA   A 1 62  ? 33.255 9.565   32.655 1.00 10.86 ? 62  ALA   A N   1 
ATOM   512  C  CA  . ALA   A 1 62  ? 34.717 9.364   32.593 1.00 9.32  ? 62  ALA   A CA  1 
ATOM   513  C  C   . ALA   A 1 62  ? 35.176 9.280   31.136 1.00 10.42 ? 62  ALA   A C   1 
ATOM   514  O  O   . ALA   A 1 62  ? 36.211 9.828   30.802 1.00 10.43 ? 62  ALA   A O   1 
ATOM   515  C  CB  . ALA   A 1 62  ? 35.086 8.096   33.316 1.00 10.63 ? 62  ALA   A CB  1 
ATOM   516  N  N   . PHE   A 1 63  ? 34.416 8.558   30.326 1.00 9.85  ? 63  PHE   A N   1 
ATOM   517  C  CA  . PHE   A 1 63  ? 34.757 8.403   28.899 1.00 10.55 ? 63  PHE   A CA  1 
ATOM   518  C  C   . PHE   A 1 63  ? 34.835 9.780   28.215 1.00 11.58 ? 63  PHE   A C   1 
ATOM   519  O  O   . PHE   A 1 63  ? 35.751 10.026  27.458 1.00 10.52 ? 63  PHE   A O   1 
ATOM   520  C  CB  . PHE   A 1 63  ? 33.712 7.505   28.228 1.00 9.60  ? 63  PHE   A CB  1 
ATOM   521  C  CG  . PHE   A 1 63  ? 34.075 7.034   26.847 1.00 12.59 ? 63  PHE   A CG  1 
ATOM   522  C  CD1 . PHE   A 1 63  ? 33.755 7.789   25.734 1.00 15.88 ? 63  PHE   A CD1 1 
ATOM   523  C  CD2 . PHE   A 1 63  ? 34.756 5.845   26.667 1.00 21.25 ? 63  PHE   A CD2 1 
ATOM   524  C  CE1 . PHE   A 1 63  ? 34.100 7.358   24.465 1.00 21.11 ? 63  PHE   A CE1 1 
ATOM   525  C  CE2 . PHE   A 1 63  ? 35.099 5.415   25.398 1.00 20.83 ? 63  PHE   A CE2 1 
ATOM   526  C  CZ  . PHE   A 1 63  ? 34.772 6.173   24.303 1.00 19.85 ? 63  PHE   A CZ  1 
ATOM   527  N  N   . ARG   A 1 64  ? 33.835 10.596  28.499 1.00 10.68 ? 64  ARG   A N   1 
ATOM   528  C  CA  A ARG   A 1 64  ? 33.816 11.949  27.872 0.36 10.37 ? 64  ARG   A CA  1 
ATOM   529  C  CA  B ARG   A 1 64  ? 33.832 11.948  27.866 0.64 10.31 ? 64  ARG   A CA  1 
ATOM   530  C  C   . ARG   A 1 64  ? 35.058 12.814  28.271 1.00 8.82  ? 64  ARG   A C   1 
ATOM   531  O  O   . ARG   A 1 64  ? 35.712 13.585  27.519 1.00 11.34 ? 64  ARG   A O   1 
ATOM   532  C  CB  A ARG   A 1 64  ? 32.482 12.641  28.180 0.36 12.37 ? 64  ARG   A CB  1 
ATOM   533  C  CB  B ARG   A 1 64  ? 32.526 12.694  28.161 0.64 12.30 ? 64  ARG   A CB  1 
ATOM   534  C  CG  A ARG   A 1 64  ? 32.339 14.053  27.637 0.36 18.66 ? 64  ARG   A CG  1 
ATOM   535  C  CG  B ARG   A 1 64  ? 31.295 12.067  27.526 0.64 15.54 ? 64  ARG   A CG  1 
ATOM   536  C  CD  A ARG   A 1 64  ? 30.881 14.470  27.607 0.36 22.63 ? 64  ARG   A CD  1 
ATOM   537  C  CD  B ARG   A 1 64  ? 30.121 13.022  27.602 0.64 23.80 ? 64  ARG   A CD  1 
ATOM   538  N  NE  A ARG   A 1 64  ? 30.167 13.794  26.534 0.36 36.17 ? 64  ARG   A NE  1 
ATOM   539  N  NE  B ARG   A 1 64  ? 30.065 13.915  26.459 0.64 36.66 ? 64  ARG   A NE  1 
ATOM   540  C  CZ  A ARG   A 1 64  ? 28.888 13.978  26.237 0.36 35.77 ? 64  ARG   A CZ  1 
ATOM   541  C  CZ  B ARG   A 1 64  ? 28.968 14.527  26.039 0.64 36.56 ? 64  ARG   A CZ  1 
ATOM   542  N  NH1 A ARG   A 1 64  ? 28.153 14.818  26.943 0.36 39.80 ? 64  ARG   A NH1 1 
ATOM   543  N  NH1 B ARG   A 1 64  ? 27.825 14.345  26.675 0.64 38.09 ? 64  ARG   A NH1 1 
ATOM   544  N  NH2 A ARG   A 1 64  ? 28.341 13.311  25.238 0.36 35.76 ? 64  ARG   A NH2 1 
ATOM   545  N  NH2 B ARG   A 1 64  ? 29.019 15.321  24.985 0.64 35.32 ? 64  ARG   A NH2 1 
ATOM   546  N  N   . LEU   A 1 65  ? 35.357 12.725  29.575 1.00 8.06  ? 65  LEU   A N   1 
ATOM   547  C  CA  . LEU   A 1 65  ? 36.538 13.465  30.073 1.00 8.13  ? 65  LEU   A CA  1 
ATOM   548  C  C   . LEU   A 1 65  ? 37.797 12.969  29.357 1.00 9.85  ? 65  LEU   A C   1 
ATOM   549  O  O   . LEU   A 1 65  ? 38.616 13.795  28.998 1.00 10.81 ? 65  LEU   A O   1 
ATOM   550  C  CB  . LEU   A 1 65  ? 36.664 13.261  31.586 1.00 8.45  ? 65  LEU   A CB  1 
ATOM   551  C  CG  . LEU   A 1 65  ? 35.682 14.064  32.431 1.00 10.04 ? 65  LEU   A CG  1 
ATOM   552  C  CD1 . LEU   A 1 65  ? 35.476 13.421  33.793 1.00 11.62 ? 65  LEU   A CD1 1 
ATOM   553  C  CD2 . LEU   A 1 65  ? 36.174 15.490  32.587 1.00 11.18 ? 65  LEU   A CD2 1 
ATOM   554  N  N   . LEU   A 1 66  ? 37.885 11.651  29.160 1.00 9.15  ? 66  LEU   A N   1 
ATOM   555  C  CA  . LEU   A 1 66  ? 39.111 11.075  28.545 1.00 7.37  ? 66  LEU   A CA  1 
ATOM   556  C  C   . LEU   A 1 66  ? 39.186 11.497  27.084 1.00 8.88  ? 66  LEU   A C   1 
ATOM   557  O  O   . LEU   A 1 66  ? 40.271 11.798  26.619 1.00 10.22 ? 66  LEU   A O   1 
ATOM   558  C  CB  . LEU   A 1 66  ? 39.049 9.545   28.661 1.00 8.95  ? 66  LEU   A CB  1 
ATOM   559  C  CG  . LEU   A 1 66  ? 39.357 8.994   30.047 1.00 8.97  ? 66  LEU   A CG  1 
ATOM   560  C  CD1 . LEU   A 1 66  ? 38.914 7.547   30.161 1.00 11.33 ? 66  LEU   A CD1 1 
ATOM   561  C  CD2 . LEU   A 1 66  ? 40.834 9.132   30.358 1.00 10.83 ? 66  LEU   A CD2 1 
ATOM   562  N  N   . LYS   A 1 67  ? 38.042 11.502  26.411 1.00 7.87  ? 67  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 67  ? 38.019 11.954  24.999 1.00 6.44  ? 67  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 67  ? 38.458 13.427  24.933 1.00 10.43 ? 67  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 67  ? 39.191 13.799  24.038 1.00 10.02 ? 67  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 67  ? 36.615 11.766  24.426 1.00 9.78  ? 67  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 67  ? 36.373 12.289  23.019 1.00 16.81 ? 67  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 67  ? 34.990 11.920  22.525 1.00 37.39 ? 67  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 67  ? 34.627 12.528  21.187 1.00 51.95 ? 67  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 67  ? 33.290 12.080  20.730 1.00 52.03 ? 67  LYS   A NZ  1 
ATOM   571  N  N   . MET   A 1 68  ? 37.982 14.190  25.899 1.00 10.30 ? 68  MET   A N   1 
ATOM   572  C  CA  . MET   A 1 68  ? 38.282 15.653  25.897 1.00 10.72 ? 68  MET   A CA  1 
ATOM   573  C  C   . MET   A 1 68  ? 39.781 15.856  26.189 1.00 9.17  ? 68  MET   A C   1 
ATOM   574  O  O   . MET   A 1 68  ? 40.396 16.725  25.578 1.00 10.66 ? 68  MET   A O   1 
ATOM   575  C  CB  . MET   A 1 68  ? 37.463 16.399  26.951 1.00 8.26  ? 68  MET   A CB  1 
ATOM   576  C  CG  . MET   A 1 68  ? 37.735 17.883  27.014 1.00 8.22  ? 68  MET   A CG  1 
ATOM   577  S  SD  . MET   A 1 68  ? 39.082 18.234  28.166 1.00 12.37 ? 68  MET   A SD  1 
ATOM   578  C  CE  . MET   A 1 68  ? 38.287 17.934  29.745 1.00 11.18 ? 68  MET   A CE  1 
ATOM   579  N  N   . GLN   A 1 69  ? 40.342 15.025  27.063 1.00 10.24 ? 69  GLN   A N   1 
ATOM   580  C  CA  . GLN   A 1 69  ? 41.780 15.144  27.388 1.00 8.70  ? 69  GLN   A CA  1 
ATOM   581  C  C   . GLN   A 1 69  ? 42.541 15.024  26.062 1.00 9.48  ? 69  GLN   A C   1 
ATOM   582  O  O   . GLN   A 1 69  ? 43.424 15.820  25.785 1.00 10.37 ? 69  GLN   A O   1 
ATOM   583  C  CB  . GLN   A 1 69  ? 42.141 14.051  28.399 1.00 9.62  ? 69  GLN   A CB  1 
ATOM   584  C  CG  . GLN   A 1 69  ? 43.601 13.989  28.816 1.00 12.84 ? 69  GLN   A CG  1 
ATOM   585  C  CD  . GLN   A 1 69  ? 43.920 14.988  29.899 1.00 12.53 ? 69  GLN   A CD  1 
ATOM   586  O  OE1 . GLN   A 1 69  ? 44.036 16.178  29.640 1.00 14.48 ? 69  GLN   A OE1 1 
ATOM   587  N  NE2 . GLN   A 1 69  ? 44.045 14.506  31.124 1.00 12.56 ? 69  GLN   A NE2 1 
ATOM   588  N  N   . ASN   A 1 70  ? 42.165 14.015  25.295 1.00 7.75  ? 70  ASN   A N   1 
ATOM   589  C  CA  . ASN   A 1 70  ? 42.907 13.772  24.029 1.00 9.05  ? 70  ASN   A CA  1 
ATOM   590  C  C   . ASN   A 1 70  ? 42.620 14.910  23.037 1.00 8.88  ? 70  ASN   A C   1 
ATOM   591  O  O   . ASN   A 1 70  ? 43.506 15.306  22.301 1.00 10.02 ? 70  ASN   A O   1 
ATOM   592  C  CB  . ASN   A 1 70  ? 42.540 12.416  23.432 1.00 8.46  ? 70  ASN   A CB  1 
ATOM   593  C  CG  . ASN   A 1 70  ? 43.367 11.273  23.982 1.00 11.90 ? 70  ASN   A CG  1 
ATOM   594  O  OD1 . ASN   A 1 70  ? 44.300 11.487  24.742 1.00 11.38 ? 70  ASN   A OD1 1 
ATOM   595  N  ND2 . ASN   A 1 70  ? 43.019 10.055  23.606 1.00 9.01  ? 70  ASN   A ND2 1 
ATOM   596  N  N   . GLN   A 1 71  ? 41.379 15.378  23.047 1.00 9.43  ? 71  GLN   A N   1 
ATOM   597  C  CA  . GLN   A 1 71  ? 41.045 16.473  22.091 1.00 12.06 ? 71  GLN   A CA  1 
ATOM   598  C  C   . GLN   A 1 71  ? 41.918 17.735  22.338 1.00 9.43  ? 71  GLN   A C   1 
ATOM   599  O  O   . GLN   A 1 71  ? 42.322 18.555  21.460 1.00 11.21 ? 71  GLN   A O   1 
ATOM   600  C  CB  . GLN   A 1 71  ? 39.549 16.803  22.162 1.00 10.63 ? 71  GLN   A CB  1 
ATOM   601  C  CG  . GLN   A 1 71  ? 38.691 15.817  21.389 1.00 12.19 ? 71  GLN   A CG  1 
ATOM   602  C  CD  . GLN   A 1 71  ? 37.230 15.939  21.741 1.00 25.71 ? 71  GLN   A CD  1 
ATOM   603  O  OE1 . GLN   A 1 71  ? 36.867 16.467  22.787 1.00 30.72 ? 71  GLN   A OE1 1 
ATOM   604  N  NE2 . GLN   A 1 71  ? 36.379 15.437  20.864 1.00 40.35 ? 71  GLN   A NE2 1 
ATOM   605  N  N   . ARG   A 1 72  ? 42.228 17.899  23.625 1.00 9.94  ? 72  ARG   A N   1 
ATOM   606  C  CA  . ARG   A 1 72  ? 43.020 19.092  24.049 1.00 10.44 ? 72  ARG   A CA  1 
ATOM   607  C  C   . ARG   A 1 72  ? 44.546 18.855  23.988 1.00 10.32 ? 72  ARG   A C   1 
ATOM   608  O  O   . ARG   A 1 72  ? 45.292 19.797  24.130 1.00 12.46 ? 72  ARG   A O   1 
ATOM   609  C  CB  . ARG   A 1 72  ? 42.593 19.533  25.452 1.00 8.05  ? 72  ARG   A CB  1 
ATOM   610  C  CG  . ARG   A 1 72  ? 41.206 20.146  25.531 1.00 9.53  ? 72  ARG   A CG  1 
ATOM   611  C  CD  . ARG   A 1 72  ? 41.045 21.431  24.747 1.00 9.63  ? 72  ARG   A CD  1 
ATOM   612  N  NE  . ARG   A 1 72  ? 41.985 22.495  25.060 1.00 7.26  ? 72  ARG   A NE  1 
ATOM   613  C  CZ  . ARG   A 1 72  ? 41.840 23.371  26.049 1.00 10.61 ? 72  ARG   A CZ  1 
ATOM   614  N  NH1 . ARG   A 1 72  ? 40.805 23.293  26.866 1.00 8.19  ? 72  ARG   A NH1 1 
ATOM   615  N  NH2 . ARG   A 1 72  ? 42.740 24.322  26.220 1.00 8.57  ? 72  ARG   A NH2 1 
ATOM   616  N  N   . GLY   A 1 73  ? 44.978 17.620  23.758 1.00 11.69 ? 73  GLY   A N   1 
ATOM   617  C  CA  . GLY   A 1 73  ? 46.430 17.385  23.637 1.00 10.77 ? 73  GLY   A CA  1 
ATOM   618  C  C   . GLY   A 1 73  ? 47.048 16.939  24.941 1.00 11.98 ? 73  GLY   A C   1 
ATOM   619  O  O   . GLY   A 1 73  ? 48.260 16.810  24.990 1.00 12.24 ? 73  GLY   A O   1 
ATOM   620  N  N   . GLY   A 1 74  ? 46.210 16.744  25.953 1.00 10.92 ? 74  GLY   A N   1 
ATOM   621  C  CA  . GLY   A 1 74  ? 46.699 16.206  27.228 1.00 10.84 ? 74  GLY   A CA  1 
ATOM   622  C  C   . GLY   A 1 74  ? 46.897 14.685  27.183 1.00 10.00 ? 74  GLY   A C   1 
ATOM   623  O  O   . GLY   A 1 74  ? 46.517 14.076  26.209 1.00 13.59 ? 74  GLY   A O   1 
ATOM   624  N  N   . ARG   A 1 75  ? 47.487 14.142  28.237 1.00 10.08 ? 75  ARG   A N   1 
ATOM   625  C  CA  . ARG   A 1 75  ? 47.785 12.696  28.248 1.00 9.90  ? 75  ARG   A CA  1 
ATOM   626  C  C   . ARG   A 1 75  ? 46.956 12.015  29.343 1.00 11.58 ? 75  ARG   A C   1 
ATOM   627  O  O   . ARG   A 1 75  ? 47.120 12.346  30.503 1.00 10.82 ? 75  ARG   A O   1 
ATOM   628  C  CB  . ARG   A 1 75  ? 49.270 12.442  28.484 1.00 15.63 ? 75  ARG   A CB  1 
ATOM   629  C  CG  . ARG   A 1 75  ? 49.513 10.940  28.573 1.00 19.76 ? 75  ARG   A CG  1 
ATOM   630  C  CD  . ARG   A 1 75  ? 50.968 10.510  28.645 1.00 23.87 ? 75  ARG   A CD  1 
ATOM   631  N  NE  . ARG   A 1 75  ? 51.792 11.129  27.602 1.00 17.65 ? 75  ARG   A NE  1 
ATOM   632  C  CZ  . ARG   A 1 75  ? 52.149 10.559  26.460 1.00 22.68 ? 75  ARG   A CZ  1 
ATOM   633  N  NH1 . ARG   A 1 75  ? 51.542 9.465   26.034 1.00 12.05 ? 75  ARG   A NH1 1 
ATOM   634  N  NH2 . ARG   A 1 75  ? 53.124 11.093  25.750 1.00 15.78 ? 75  ARG   A NH2 1 
ATOM   635  N  N   . ALA   A 1 76  ? 46.053 11.143  28.919 1.00 10.36 ? 76  ALA   A N   1 
ATOM   636  C  CA  . ALA   A 1 76  ? 45.262 10.358  29.881 1.00 10.57 ? 76  ALA   A CA  1 
ATOM   637  C  C   . ALA   A 1 76  ? 46.197 9.478   30.705 1.00 13.85 ? 76  ALA   A C   1 
ATOM   638  O  O   . ALA   A 1 76  ? 47.002 8.767   30.101 1.00 14.24 ? 76  ALA   A O   1 
ATOM   639  C  CB  . ALA   A 1 76  ? 44.315 9.485   29.126 1.00 12.83 ? 76  ALA   A CB  1 
ATOM   640  N  N   . LEU   A 1 77  ? 46.073 9.553   32.021 1.00 10.04 ? 77  LEU   A N   1 
ATOM   641  C  CA  . LEU   A 1 77  ? 46.886 8.726   32.919 1.00 11.34 ? 77  LEU   A CA  1 
ATOM   642  C  C   . LEU   A 1 77  ? 45.907 8.064   33.869 1.00 17.16 ? 77  LEU   A C   1 
ATOM   643  O  O   . LEU   A 1 77  ? 45.120 8.749   34.481 1.00 15.82 ? 77  LEU   A O   1 
ATOM   644  C  CB  . LEU   A 1 77  ? 47.879 9.603   33.675 1.00 12.10 ? 77  LEU   A CB  1 
ATOM   645  C  CG  . LEU   A 1 77  ? 49.102 10.050  32.884 1.00 19.26 ? 77  LEU   A CG  1 
ATOM   646  C  CD1 . LEU   A 1 77  ? 50.046 10.834  33.775 1.00 24.86 ? 77  LEU   A CD1 1 
ATOM   647  C  CD2 . LEU   A 1 77  ? 49.816 8.857   32.271 1.00 17.04 ? 77  LEU   A CD2 1 
ATOM   648  N  N   . PHE   A 1 78  ? 46.043 6.759   33.958 1.00 10.96 ? 78  PHE   A N   1 
ATOM   649  C  CA  . PHE   A 1 78  ? 45.112 6.006   34.812 1.00 10.67 ? 78  PHE   A CA  1 
ATOM   650  C  C   . PHE   A 1 78  ? 45.803 5.631   36.126 1.00 14.16 ? 78  PHE   A C   1 
ATOM   651  O  O   . PHE   A 1 78  ? 47.004 5.408   36.170 1.00 18.18 ? 78  PHE   A O   1 
ATOM   652  C  CB  . PHE   A 1 78  ? 44.550 4.823   34.030 1.00 12.98 ? 78  PHE   A CB  1 
ATOM   653  C  CG  . PHE   A 1 78  ? 43.774 5.194   32.796 1.00 16.41 ? 78  PHE   A CG  1 
ATOM   654  C  CD1 . PHE   A 1 78  ? 42.422 5.480   32.872 1.00 19.80 ? 78  PHE   A CD1 1 
ATOM   655  C  CD2 . PHE   A 1 78  ? 44.396 5.267   31.563 1.00 10.37 ? 78  PHE   A CD2 1 
ATOM   656  C  CE1 . PHE   A 1 78  ? 41.712 5.824   31.734 1.00 17.29 ? 78  PHE   A CE1 1 
ATOM   657  C  CE2 . PHE   A 1 78  ? 43.683 5.604   30.425 1.00 10.90 ? 78  PHE   A CE2 1 
ATOM   658  C  CZ  . PHE   A 1 78  ? 42.341 5.877   30.514 1.00 15.02 ? 78  PHE   A CZ  1 
ATOM   659  N  N   . GLN   A 1 79  ? 44.998 5.641   37.165 1.00 10.49 ? 79  GLN   A N   1 
ATOM   660  C  CA  . GLN   A 1 79  ? 45.534 5.241   38.470 1.00 12.46 ? 79  GLN   A CA  1 
ATOM   661  C  C   . GLN   A 1 79  ? 44.735 4.057   38.997 1.00 11.11 ? 79  GLN   A C   1 
ATOM   662  O  O   . GLN   A 1 79  ? 43.717 3.703   38.439 1.00 10.53 ? 79  GLN   A O   1 
ATOM   663  C  CB  . GLN   A 1 79  ? 45.441 6.398   39.470 1.00 14.53 ? 79  GLN   A CB  1 
ATOM   664  C  CG  . GLN   A 1 79  ? 46.303 7.600   39.112 1.00 17.46 ? 79  GLN   A CG  1 
ATOM   665  C  CD  . GLN   A 1 79  ? 47.759 7.278   38.870 1.00 41.45 ? 79  GLN   A CD  1 
ATOM   666  O  OE1 . GLN   A 1 79  ? 48.330 6.359   39.455 1.00 36.20 ? 79  GLN   A OE1 1 
ATOM   667  N  NE2 . GLN   A 1 79  ? 48.383 8.058   38.000 1.00 37.97 ? 79  GLN   A NE2 1 
ATOM   668  N  N   . ASP   A 1 80  ? 45.230 3.522   40.103 1.00 11.85 ? 80  ASP   A N   1 
ATOM   669  C  CA  . ASP   A 1 80  ? 44.490 2.426   40.757 1.00 13.73 ? 80  ASP   A CA  1 
ATOM   670  C  C   . ASP   A 1 80  ? 43.091 2.940   41.085 1.00 16.53 ? 80  ASP   A C   1 
ATOM   671  O  O   . ASP   A 1 80  ? 42.945 4.119   41.374 1.00 15.32 ? 80  ASP   A O   1 
ATOM   672  C  CB  . ASP   A 1 80  ? 45.218 1.944   42.017 1.00 14.65 ? 80  ASP   A CB  1 
ATOM   673  C  CG  . ASP   A 1 80  ? 46.566 1.284   41.789 1.00 15.37 ? 80  ASP   A CG  1 
ATOM   674  O  OD1 . ASP   A 1 80  ? 46.756 0.716   40.722 1.00 12.61 ? 80  ASP   A OD1 1 
ATOM   675  O  OD2 . ASP   A 1 80  ? 47.392 1.331   42.710 1.00 18.61 ? 80  ASP   A OD2 1 
ATOM   676  N  N   . LEU   A 1 81  ? 42.122 2.038   41.026 1.00 12.25 ? 81  LEU   A N   1 
ATOM   677  C  CA  A LEU   A 1 81  ? 40.727 2.393   41.388 0.51 11.22 ? 81  LEU   A CA  1 
ATOM   678  C  CA  B LEU   A 1 81  ? 40.725 2.389   41.383 0.49 11.23 ? 81  LEU   A CA  1 
ATOM   679  C  C   . LEU   A 1 81  ? 40.353 1.767   42.754 1.00 13.88 ? 81  LEU   A C   1 
ATOM   680  O  O   . LEU   A 1 81  ? 40.271 0.493   43.033 1.00 16.43 ? 81  LEU   A O   1 
ATOM   681  C  CB  A LEU   A 1 81  ? 39.788 1.881   40.293 0.51 14.35 ? 81  LEU   A CB  1 
ATOM   682  C  CB  B LEU   A 1 81  ? 39.806 1.858   40.281 0.49 14.35 ? 81  LEU   A CB  1 
ATOM   683  C  CG  A LEU   A 1 81  ? 39.647 2.782   39.070 0.51 16.43 ? 81  LEU   A CG  1 
ATOM   684  C  CG  B LEU   A 1 81  ? 38.499 2.618   40.077 0.49 14.95 ? 81  LEU   A CG  1 
ATOM   685  C  CD1 A LEU   A 1 81  ? 38.756 2.124   38.029 0.51 11.81 ? 81  LEU   A CD1 1 
ATOM   686  C  CD1 B LEU   A 1 81  ? 38.785 4.043   39.630 0.49 19.60 ? 81  LEU   A CD1 1 
ATOM   687  C  CD2 A LEU   A 1 81  ? 39.095 4.142   39.466 0.51 18.91 ? 81  LEU   A CD2 1 
ATOM   688  C  CD2 B LEU   A 1 81  ? 37.623 1.903   39.057 0.49 13.49 ? 81  LEU   A CD2 1 
ATOM   689  N  N   . GLN   A 1 82  ? 40.243 2.665   43.718 1.00 10.96 ? 82  GLN   A N   1 
ATOM   690  C  CA  A GLN   A 1 82  ? 39.822 2.144   45.043 0.50 12.63 ? 82  GLN   A CA  1 
ATOM   691  C  CA  B GLN   A 1 82  ? 39.786 2.208   45.056 0.50 12.68 ? 82  GLN   A CA  1 
ATOM   692  C  C   . GLN   A 1 82  ? 38.425 1.479   45.006 1.00 13.60 ? 82  GLN   A C   1 
ATOM   693  O  O   . GLN   A 1 82  ? 37.377 1.841   44.323 1.00 14.28 ? 82  GLN   A O   1 
ATOM   694  C  CB  A GLN   A 1 82  ? 39.905 3.202   46.150 0.50 14.88 ? 82  GLN   A CB  1 
ATOM   695  C  CB  B GLN   A 1 82  ? 39.570 3.356   46.045 0.50 13.15 ? 82  GLN   A CB  1 
ATOM   696  C  CG  A GLN   A 1 82  ? 38.950 4.362   46.001 0.50 16.45 ? 82  GLN   A CG  1 
ATOM   697  C  CG  B GLN   A 1 82  ? 40.770 4.250   46.272 0.50 17.25 ? 82  GLN   A CG  1 
ATOM   698  C  CD  A GLN   A 1 82  ? 39.530 5.512   46.783 0.50 30.35 ? 82  GLN   A CD  1 
ATOM   699  C  CD  B GLN   A 1 82  ? 40.255 5.585   46.747 0.50 27.86 ? 82  GLN   A CD  1 
ATOM   700  O  OE1 A GLN   A 1 82  ? 40.225 6.367   46.240 0.50 31.74 ? 82  GLN   A OE1 1 
ATOM   701  O  OE1 B GLN   A 1 82  ? 40.442 6.609   46.099 0.50 33.70 ? 82  GLN   A OE1 1 
ATOM   702  N  NE2 A GLN   A 1 82  ? 39.275 5.515   48.081 0.50 29.16 ? 82  GLN   A NE2 1 
ATOM   703  N  NE2 B GLN   A 1 82  ? 39.558 5.567   47.871 0.50 31.08 ? 82  GLN   A NE2 1 
ATOM   704  N  N   . LYS   A 1 83  ? 38.374 0.408   45.794 1.00 14.13 ? 83  LYS   A N   1 
ATOM   705  C  CA  . LYS   A 1 83  ? 37.079 -0.293  45.896 1.00 12.49 ? 83  LYS   A CA  1 
ATOM   706  C  C   . LYS   A 1 83  ? 36.076 0.613   46.610 1.00 13.01 ? 83  LYS   A C   1 
ATOM   707  O  O   . LYS   A 1 83  ? 36.447 1.525   47.312 1.00 12.12 ? 83  LYS   A O   1 
ATOM   708  C  CB  . LYS   A 1 83  ? 37.181 -1.576  46.715 1.00 11.08 ? 83  LYS   A CB  1 
ATOM   709  C  CG  . LYS   A 1 83  ? 37.576 -1.404  48.169 1.00 11.44 ? 83  LYS   A CG  1 
ATOM   710  C  CD  . LYS   A 1 83  ? 37.797 -2.737  48.826 1.00 15.28 ? 83  LYS   A CD  1 
ATOM   711  C  CE  . LYS   A 1 83  ? 37.545 -2.749  50.316 1.00 16.00 ? 83  LYS   A CE  1 
ATOM   712  N  NZ  . LYS   A 1 83  ? 37.916 -4.058  50.903 1.00 23.14 ? 83  LYS   A NZ  1 
ATOM   713  N  N   . PRO   A 1 84  ? 34.777 0.290   46.489 1.00 8.36  ? 84  PRO   A N   1 
ATOM   714  C  CA  . PRO   A 1 84  ? 33.766 1.062   47.174 1.00 9.24  ? 84  PRO   A CA  1 
ATOM   715  C  C   . PRO   A 1 84  ? 33.889 1.082   48.706 1.00 11.50 ? 84  PRO   A C   1 
ATOM   716  O  O   . PRO   A 1 84  ? 34.463 0.197   49.246 1.00 13.01 ? 84  PRO   A O   1 
ATOM   717  C  CB  . PRO   A 1 84  ? 32.431 0.454   46.688 1.00 8.45  ? 84  PRO   A CB  1 
ATOM   718  C  CG  . PRO   A 1 84  ? 32.786 -0.175  45.372 1.00 9.56  ? 84  PRO   A CG  1 
ATOM   719  C  CD  . PRO   A 1 84  ? 34.171 -0.732  45.618 1.00 8.42  ? 84  PRO   A CD  1 
ATOM   720  N  N   . SER   A 1 85  ? 33.231 2.071   49.306 1.00 11.96 ? 85  SER   A N   1 
ATOM   721  C  CA  . SER   A 1 85  ? 33.394 2.286   50.758 1.00 12.89 ? 85  SER   A CA  1 
ATOM   722  C  C   . SER   A 1 85  ? 32.735 1.174   51.555 1.00 13.69 ? 85  SER   A C   1 
ATOM   723  O  O   . SER   A 1 85  ? 33.103 1.005   52.700 1.00 14.48 ? 85  SER   A O   1 
ATOM   724  C  CB  . SER   A 1 85  ? 32.844 3.630   51.157 1.00 15.25 ? 85  SER   A CB  1 
ATOM   725  O  OG  . SER   A 1 85  ? 31.459 3.707   50.885 1.00 19.86 ? 85  SER   A OG  1 
ATOM   726  N  N   . GLN   A 1 86  ? 31.774 0.498   50.957 1.00 12.26 ? 86  GLN   A N   1 
ATOM   727  C  CA  A GLN   A 1 86  ? 31.034 -0.572  51.672 0.46 11.16 ? 86  GLN   A CA  1 
ATOM   728  C  CA  B GLN   A 1 86  ? 31.047 -0.587  51.659 0.54 11.16 ? 86  GLN   A CA  1 
ATOM   729  C  C   . GLN   A 1 86  ? 30.865 -1.872  50.801 1.00 9.19  ? 86  GLN   A C   1 
ATOM   730  O  O   . GLN   A 1 86  ? 30.964 -1.869  49.533 1.00 11.00 ? 86  GLN   A O   1 
ATOM   731  C  CB  A GLN   A 1 86  ? 29.627 -0.092  52.050 0.46 12.24 ? 86  GLN   A CB  1 
ATOM   732  C  CB  B GLN   A 1 86  ? 29.650 -0.113  52.075 0.54 12.26 ? 86  GLN   A CB  1 
ATOM   733  C  CG  A GLN   A 1 86  ? 29.615 1.180   52.875 0.46 12.48 ? 86  GLN   A CG  1 
ATOM   734  C  CG  B GLN   A 1 86  ? 29.658 1.161   52.905 0.54 12.46 ? 86  GLN   A CG  1 
ATOM   735  C  CD  A GLN   A 1 86  ? 30.045 0.882   54.288 0.46 13.73 ? 86  GLN   A CD  1 
ATOM   736  C  CD  B GLN   A 1 86  ? 28.269 1.712   53.108 0.54 15.27 ? 86  GLN   A CD  1 
ATOM   737  O  OE1 A GLN   A 1 86  ? 29.917 -0.240  54.770 0.46 17.75 ? 86  GLN   A OE1 1 
ATOM   738  O  OE1 B GLN   A 1 86  ? 28.056 2.921   53.114 0.54 18.50 ? 86  GLN   A OE1 1 
ATOM   739  N  NE2 A GLN   A 1 86  ? 30.558 1.896   54.964 0.46 22.28 ? 86  GLN   A NE2 1 
ATOM   740  N  NE2 B GLN   A 1 86  ? 27.306 0.821   53.279 0.54 13.83 ? 86  GLN   A NE2 1 
ATOM   741  N  N   . ASP   A 1 87  ? 30.812 -3.004  51.517 1.00 10.30 ? 87  ASP   A N   1 
ATOM   742  C  CA  . ASP   A 1 87  ? 30.533 -4.292  50.843 1.00 11.11 ? 87  ASP   A CA  1 
ATOM   743  C  C   . ASP   A 1 87  ? 29.025 -4.557  50.870 1.00 13.12 ? 87  ASP   A C   1 
ATOM   744  O  O   . ASP   A 1 87  ? 28.546 -5.255  49.976 1.00 13.68 ? 87  ASP   A O   1 
ATOM   745  C  CB  . ASP   A 1 87  ? 31.257 -5.434  51.551 1.00 10.41 ? 87  ASP   A CB  1 
ATOM   746  C  CG  . ASP   A 1 87  ? 32.769 -5.333  51.452 1.00 13.66 ? 87  ASP   A CG  1 
ATOM   747  O  OD1 . ASP   A 1 87  ? 33.250 -4.863  50.416 1.00 12.87 ? 87  ASP   A OD1 1 
ATOM   748  O  OD2 . ASP   A 1 87  ? 33.441 -5.739  52.411 1.00 14.60 ? 87  ASP   A OD2 1 
ATOM   749  N  N   . GLU   A 1 88  ? 28.364 -4.040  51.903 1.00 10.40 ? 88  GLU   A N   1 
ATOM   750  C  CA  . GLU   A 1 88  ? 26.893 -4.174  52.078 1.00 11.92 ? 88  GLU   A CA  1 
ATOM   751  C  C   . GLU   A 1 88  ? 26.336 -2.761  52.262 1.00 12.39 ? 88  GLU   A C   1 
ATOM   752  O  O   . GLU   A 1 88  ? 26.932 -2.031  53.015 1.00 15.06 ? 88  GLU   A O   1 
ATOM   753  C  CB  . GLU   A 1 88  ? 26.602 -5.038  53.303 1.00 12.18 ? 88  GLU   A CB  1 
ATOM   754  C  CG  . GLU   A 1 88  ? 27.084 -6.458  53.119 1.00 21.29 ? 88  GLU   A CG  1 
ATOM   755  C  CD  . GLU   A 1 88  ? 26.668 -7.370  54.256 1.00 39.19 ? 88  GLU   A CD  1 
ATOM   756  O  OE1 . GLU   A 1 88  ? 27.200 -7.200  55.358 1.00 46.61 ? 88  GLU   A OE1 1 
ATOM   757  O  OE2 . GLU   A 1 88  ? 25.807 -8.226  54.033 1.00 40.29 ? 88  GLU   A OE2 1 
ATOM   758  N  N   . TRP   A 1 89  ? 25.209 -2.447  51.635 1.00 9.66  ? 89  TRP   A N   1 
ATOM   759  C  CA  . TRP   A 1 89  ? 24.716 -1.043  51.609 1.00 10.45 ? 89  TRP   A CA  1 
ATOM   760  C  C   . TRP   A 1 89  ? 23.441 -0.769  52.425 1.00 10.39 ? 89  TRP   A C   1 
ATOM   761  O  O   . TRP   A 1 89  ? 22.910 0.315   52.282 1.00 11.82 ? 89  TRP   A O   1 
ATOM   762  C  CB  . TRP   A 1 89  ? 24.543 -0.621  50.143 1.00 10.50 ? 89  TRP   A CB  1 
ATOM   763  C  CG  . TRP   A 1 89  ? 25.819 -0.720  49.364 1.00 11.07 ? 89  TRP   A CG  1 
ATOM   764  C  CD1 . TRP   A 1 89  ? 26.251 -1.750  48.578 1.00 10.41 ? 89  TRP   A CD1 1 
ATOM   765  C  CD2 . TRP   A 1 89  ? 26.851 0.277   49.311 1.00 10.26 ? 89  TRP   A CD2 1 
ATOM   766  N  NE1 . TRP   A 1 89  ? 27.476 -1.460  48.038 1.00 10.19 ? 89  TRP   A NE1 1 
ATOM   767  C  CE2 . TRP   A 1 89  ? 27.866 -0.219  48.467 1.00 11.13 ? 89  TRP   A CE2 1 
ATOM   768  C  CE3 . TRP   A 1 89  ? 27.002 1.542   49.883 1.00 9.04  ? 89  TRP   A CE3 1 
ATOM   769  C  CZ2 . TRP   A 1 89  ? 29.021 0.509   48.197 1.00 12.29 ? 89  TRP   A CZ2 1 
ATOM   770  C  CZ3 . TRP   A 1 89  ? 28.142 2.261   49.613 1.00 11.98 ? 89  TRP   A CZ3 1 
ATOM   771  C  CH2 . TRP   A 1 89  ? 29.135 1.746   48.785 1.00 10.19 ? 89  TRP   A CH2 1 
ATOM   772  N  N   . GLY   A 1 90  ? 23.030 -1.721  53.233 1.00 11.41 ? 90  GLY   A N   1 
ATOM   773  C  CA  . GLY   A 1 90  ? 21.868 -1.511  54.110 1.00 11.94 ? 90  GLY   A CA  1 
ATOM   774  C  C   . GLY   A 1 90  ? 20.541 -1.360  53.391 1.00 9.37  ? 90  GLY   A C   1 
ATOM   775  O  O   . GLY   A 1 90  ? 20.250 -2.159  52.528 1.00 11.47 ? 90  GLY   A O   1 
ATOM   776  N  N   . THR   A 1 91  ? 19.769 -0.400  53.864 1.00 8.57  ? 91  THR   A N   1 
ATOM   777  C  CA  . THR   A 1 91  ? 18.429 -0.179  53.300 1.00 10.03 ? 91  THR   A CA  1 
ATOM   778  C  C   . THR   A 1 91  ? 18.489 0.674   52.033 1.00 7.67  ? 91  THR   A C   1 
ATOM   779  O  O   . THR   A 1 91  ? 19.523 1.236   51.725 1.00 9.29  ? 91  THR   A O   1 
ATOM   780  C  CB  . THR   A 1 91  ? 17.573 0.585   54.319 1.00 12.33 ? 91  THR   A CB  1 
ATOM   781  O  OG1 . THR   A 1 91  ? 18.154 1.840   54.642 1.00 12.71 ? 91  THR   A OG1 1 
ATOM   782  C  CG2 . THR   A 1 91  ? 17.368 -0.219  55.585 1.00 12.12 ? 91  THR   A CG2 1 
ATOM   783  N  N   . THR   A 1 92  ? 17.351 0.764   51.348 1.00 9.65  ? 92  THR   A N   1 
ATOM   784  C  CA  . THR   A 1 92  ? 17.287 1.671   50.184 1.00 7.03  ? 92  THR   A CA  1 
ATOM   785  C  C   . THR   A 1 92  ? 17.644 3.071   50.685 1.00 8.60  ? 92  THR   A C   1 
ATOM   786  O  O   . THR   A 1 92  ? 18.290 3.797   49.965 1.00 11.34 ? 92  THR   A O   1 
ATOM   787  C  CB  . THR   A 1 92  ? 15.904 1.634   49.513 1.00 11.48 ? 92  THR   A CB  1 
ATOM   788  O  OG1 . THR   A 1 92  ? 15.591 0.296   49.132 1.00 10.24 ? 92  THR   A OG1 1 
ATOM   789  C  CG2 . THR   A 1 92  ? 15.836 2.530   48.297 1.00 9.83  ? 92  THR   A CG2 1 
ATOM   790  N  N   . LEU   A 1 93  ? 17.163 3.399   51.881 1.00 10.72 ? 93  LEU   A N   1 
ATOM   791  C  CA  . LEU   A 1 93  ? 17.397 4.771   52.397 1.00 8.06  ? 93  LEU   A CA  1 
ATOM   792  C  C   . LEU   A 1 93  ? 18.908 4.964   52.605 1.00 12.97 ? 93  LEU   A C   1 
ATOM   793  O  O   . LEU   A 1 93  ? 19.430 6.004   52.291 1.00 11.78 ? 93  LEU   A O   1 
ATOM   794  C  CB  . LEU   A 1 93  ? 16.638 4.972   53.708 1.00 8.81  ? 93  LEU   A CB  1 
ATOM   795  C  CG  . LEU   A 1 93  ? 16.852 6.302   54.422 1.00 13.32 ? 93  LEU   A CG  1 
ATOM   796  C  CD1 . LEU   A 1 93  ? 16.505 7.467   53.511 1.00 15.87 ? 93  LEU   A CD1 1 
ATOM   797  C  CD2 . LEU   A 1 93  ? 16.020 6.349   55.693 1.00 18.56 ? 93  LEU   A CD2 1 
ATOM   798  N  N   . ASP   A 1 94  ? 19.537 3.956   53.199 1.00 10.97 ? 94  ASP   A N   1 
ATOM   799  C  CA  . ASP   A 1 94  ? 20.993 4.066   53.443 1.00 8.49  ? 94  ASP   A CA  1 
ATOM   800  C  C   . ASP   A 1 94  ? 21.699 4.274   52.108 1.00 9.19  ? 94  ASP   A C   1 
ATOM   801  O  O   . ASP   A 1 94  ? 22.641 5.040   52.041 1.00 9.32  ? 94  ASP   A O   1 
ATOM   802  C  CB  . ASP   A 1 94  ? 21.550 2.792   54.079 1.00 10.40 ? 94  ASP   A CB  1 
ATOM   803  C  CG  . ASP   A 1 94  ? 21.083 2.569   55.507 1.00 14.54 ? 94  ASP   A CG  1 
ATOM   804  O  OD1 . ASP   A 1 94  ? 20.992 3.558   56.245 1.00 15.05 ? 94  ASP   A OD1 1 
ATOM   805  O  OD2 . ASP   A 1 94  ? 20.836 1.412   55.866 1.00 13.55 ? 94  ASP   A OD2 1 
ATOM   806  N  N   . ALA   A 1 95  ? 21.266 3.511   51.125 1.00 7.49  ? 95  ALA   A N   1 
ATOM   807  C  CA  . ALA   A 1 95  ? 21.951 3.542   49.822 1.00 9.43  ? 95  ALA   A CA  1 
ATOM   808  C  C   . ALA   A 1 95  ? 21.748 4.892   49.124 1.00 9.44  ? 95  ALA   A C   1 
ATOM   809  O  O   . ALA   A 1 95  ? 22.687 5.412   48.562 1.00 9.94  ? 95  ALA   A O   1 
ATOM   810  C  CB  . ALA   A 1 95  ? 21.438 2.383   49.000 1.00 8.82  ? 95  ALA   A CB  1 
ATOM   811  N  N   . MET   A 1 96  ? 20.511 5.378   49.168 1.00 8.21  ? 96  MET   A N   1 
ATOM   812  C  CA  . MET   A 1 96  ? 20.237 6.658   48.484 1.00 8.46  ? 96  MET   A CA  1 
ATOM   813  C  C   . MET   A 1 96  ? 20.984 7.791   49.210 1.00 11.14 ? 96  MET   A C   1 
ATOM   814  O  O   . MET   A 1 96  ? 21.431 8.694   48.544 1.00 11.02 ? 96  MET   A O   1 
ATOM   815  C  CB  . MET   A 1 96  ? 18.728 6.931   48.440 1.00 8.04  ? 96  MET   A CB  1 
ATOM   816  C  CG  . MET   A 1 96  ? 18.319 8.026   47.485 1.00 9.29  ? 96  MET   A CG  1 
ATOM   817  S  SD  . MET   A 1 96  ? 18.573 7.566   45.755 1.00 12.33 ? 96  MET   A SD  1 
ATOM   818  C  CE  . MET   A 1 96  ? 17.440 6.185   45.590 1.00 10.15 ? 96  MET   A CE  1 
ATOM   819  N  N   . LYS   A 1 97  ? 21.111 7.690   50.536 1.00 8.92  ? 97  LYS   A N   1 
ATOM   820  C  CA  . LYS   A 1 97  ? 21.905 8.701   51.281 1.00 12.19 ? 97  LYS   A CA  1 
ATOM   821  C  C   . LYS   A 1 97  ? 23.380 8.606   50.825 1.00 14.94 ? 97  LYS   A C   1 
ATOM   822  O  O   . LYS   A 1 97  ? 23.997 9.633   50.604 1.00 13.52 ? 97  LYS   A O   1 
ATOM   823  C  CB  . LYS   A 1 97  ? 21.790 8.501   52.795 1.00 14.08 ? 97  LYS   A CB  1 
ATOM   824  C  CG  . LYS   A 1 97  ? 20.488 8.929   53.453 1.00 16.66 ? 97  LYS   A CG  1 
ATOM   825  C  CD  . LYS   A 1 97  ? 20.450 8.512   54.907 1.00 17.48 ? 97  LYS   A CD  1 
ATOM   826  C  CE  . LYS   A 1 97  ? 19.306 9.103   55.702 1.00 34.54 ? 97  LYS   A CE  1 
ATOM   827  N  NZ  . LYS   A 1 97  ? 19.185 8.469   57.038 1.00 36.40 ? 97  LYS   A NZ  1 
ATOM   828  N  N   . ALA   A 1 98  ? 23.893 7.382   50.712 1.00 9.85  ? 98  ALA   A N   1 
ATOM   829  C  CA  . ALA   A 1 98  ? 25.307 7.242   50.297 1.00 9.90  ? 98  ALA   A CA  1 
ATOM   830  C  C   . ALA   A 1 98  ? 25.473 7.806   48.886 1.00 11.26 ? 98  ALA   A C   1 
ATOM   831  O  O   . ALA   A 1 98  ? 26.518 8.365   48.599 1.00 9.80  ? 98  ALA   A O   1 
ATOM   832  C  CB  . ALA   A 1 98  ? 25.753 5.812   50.365 1.00 10.54 ? 98  ALA   A CB  1 
ATOM   833  N  N   . ALA   A 1 99  ? 24.462 7.600   48.046 1.00 9.52  ? 99  ALA   A N   1 
ATOM   834  C  CA  . ALA   A 1 99  ? 24.543 8.051   46.643 1.00 9.04  ? 99  ALA   A CA  1 
ATOM   835  C  C   . ALA   A 1 99  ? 24.572 9.579   46.595 1.00 12.50 ? 99  ALA   A C   1 
ATOM   836  O  O   . ALA   A 1 99  ? 25.323 10.133  45.819 1.00 12.00 ? 99  ALA   A O   1 
ATOM   837  C  CB  . ALA   A 1 99  ? 23.384 7.514   45.859 1.00 11.96 ? 99  ALA   A CB  1 
ATOM   838  N  N   . ILE   A 1 100 ? 23.727 10.194  47.420 1.00 11.08 ? 100 ILE   A N   1 
ATOM   839  C  CA  A ILE   A 1 100 ? 23.687 11.689  47.354 0.56 10.44 ? 100 ILE   A CA  1 
ATOM   840  C  CA  B ILE   A 1 100 ? 23.679 11.696  47.396 0.44 10.47 ? 100 ILE   A CA  1 
ATOM   841  C  C   . ILE   A 1 100 ? 25.017 12.316  47.877 1.00 10.51 ? 100 ILE   A C   1 
ATOM   842  O  O   . ILE   A 1 100 ? 25.624 13.310  47.398 1.00 12.32 ? 100 ILE   A O   1 
ATOM   843  C  CB  A ILE   A 1 100 ? 22.430 12.249  48.055 0.56 10.77 ? 100 ILE   A CB  1 
ATOM   844  C  CB  B ILE   A 1 100 ? 22.494 12.219  48.230 0.44 10.69 ? 100 ILE   A CB  1 
ATOM   845  C  CG1 A ILE   A 1 100 ? 22.106 13.653  47.539 0.56 11.62 ? 100 ILE   A CG1 1 
ATOM   846  C  CG1 B ILE   A 1 100 ? 21.164 11.999  47.511 0.44 9.69  ? 100 ILE   A CG1 1 
ATOM   847  C  CG2 A ILE   A 1 100 ? 22.577 12.222  49.563 0.56 11.01 ? 100 ILE   A CG2 1 
ATOM   848  C  CG2 B ILE   A 1 100 ? 22.703 13.678  48.597 0.44 13.55 ? 100 ILE   A CG2 1 
ATOM   849  C  CD1 A ILE   A 1 100 ? 20.642 14.012  47.600 0.56 10.98 ? 100 ILE   A CD1 1 
ATOM   850  C  CD1 B ILE   A 1 100 ? 19.955 12.199  48.390 0.44 9.86  ? 100 ILE   A CD1 1 
ATOM   851  N  N   . VAL   A 1 101 ? 25.550 11.630  48.883 1.00 10.73 ? 101 VAL   A N   1 
ATOM   852  C  CA  . VAL   A 1 101 ? 26.886 12.055  49.409 1.00 10.74 ? 101 VAL   A CA  1 
ATOM   853  C  C   . VAL   A 1 101 ? 27.941 11.940  48.287 1.00 12.43 ? 101 VAL   A C   1 
ATOM   854  O  O   . VAL   A 1 101 ? 28.734 12.855  48.107 1.00 12.69 ? 101 VAL   A O   1 
ATOM   855  C  CB  . VAL   A 1 101 ? 27.283 11.252  50.660 1.00 12.34 ? 101 VAL   A CB  1 
ATOM   856  C  CG1 . VAL   A 1 101 ? 28.767 11.388  50.970 1.00 12.68 ? 101 VAL   A CG1 1 
ATOM   857  C  CG2 . VAL   A 1 101 ? 26.438 11.623  51.866 1.00 12.33 ? 101 VAL   A CG2 1 
ATOM   858  N  N   . LEU   A 1 102 ? 27.925 10.830  47.575 1.00 9.59  ? 102 LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 102 ? 28.894 10.620  46.468 1.00 9.91  ? 102 LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 102 ? 28.680 11.680  45.386 1.00 10.04 ? 102 LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 102 ? 29.630 12.265  44.908 1.00 11.50 ? 102 LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 102 ? 28.670 9.214   45.896 1.00 11.35 ? 102 LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 102 ? 29.420 8.852   44.622 1.00 12.54 ? 102 LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 102 ? 30.916 9.002   44.836 1.00 16.57 ? 102 LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 102 ? 29.081 7.423   44.225 1.00 12.95 ? 102 LEU   A CD2 1 
ATOM   866  N  N   . GLU   A 1 103 ? 27.413 11.877  45.037 1.00 11.75 ? 103 GLU   A N   1 
ATOM   867  C  CA  . GLU   A 1 103 ? 27.139 12.850  43.956 1.00 9.70  ? 103 GLU   A CA  1 
ATOM   868  C  C   . GLU   A 1 103 ? 27.581 14.272  44.371 1.00 9.05  ? 103 GLU   A C   1 
ATOM   869  O  O   . GLU   A 1 103 ? 28.103 14.986  43.533 1.00 12.96 ? 103 GLU   A O   1 
ATOM   870  C  CB  . GLU   A 1 103 ? 25.664 12.811  43.569 1.00 9.95  ? 103 GLU   A CB  1 
ATOM   871  C  CG  . GLU   A 1 103 ? 25.279 11.555  42.823 1.00 9.85  ? 103 GLU   A CG  1 
ATOM   872  C  CD  . GLU   A 1 103 ? 26.134 11.225  41.613 1.00 13.96 ? 103 GLU   A CD  1 
ATOM   873  O  OE1 . GLU   A 1 103 ? 26.535 12.156  40.902 1.00 12.14 ? 103 GLU   A OE1 1 
ATOM   874  O  OE2 . GLU   A 1 103 ? 26.378 10.039  41.384 1.00 13.64 ? 103 GLU   A OE2 1 
ATOM   875  N  N   . LYS   A 1 104 ? 27.347 14.631  45.624 1.00 11.88 ? 104 LYS   A N   1 
ATOM   876  C  CA  . LYS   A 1 104 ? 27.811 15.972  46.070 1.00 9.33  ? 104 LYS   A CA  1 
ATOM   877  C  C   . LYS   A 1 104 ? 29.347 16.079  45.946 1.00 14.18 ? 104 LYS   A C   1 
ATOM   878  O  O   . LYS   A 1 104 ? 29.847 17.154  45.666 1.00 11.26 ? 104 LYS   A O   1 
ATOM   879  C  CB  . LYS   A 1 104 ? 27.380 16.262  47.508 1.00 13.57 ? 104 LYS   A CB  1 
ATOM   880  C  CG  . LYS   A 1 104 ? 25.921 16.672  47.621 1.00 16.85 ? 104 LYS   A CG  1 
ATOM   881  C  CD  . LYS   A 1 104 ? 25.411 16.658  49.033 1.00 22.48 ? 104 LYS   A CD  1 
ATOM   882  C  CE  . LYS   A 1 104 ? 24.126 17.433  49.199 1.00 29.94 ? 104 LYS   A CE  1 
ATOM   883  N  NZ  . LYS   A 1 104 ? 23.582 17.256  50.563 1.00 29.37 ? 104 LYS   A NZ  1 
ATOM   884  N  N   . SER   A 1 105 ? 30.025 14.974  46.229 1.00 13.36 ? 105 SER   A N   1 
ATOM   885  C  CA  . SER   A 1 105 ? 31.505 15.015  46.153 1.00 12.17 ? 105 SER   A CA  1 
ATOM   886  C  C   . SER   A 1 105 ? 31.931 15.206  44.693 1.00 13.01 ? 105 SER   A C   1 
ATOM   887  O  O   . SER   A 1 105 ? 32.895 15.927  44.434 1.00 12.15 ? 105 SER   A O   1 
ATOM   888  C  CB  . SER   A 1 105 ? 32.124 13.777  46.776 1.00 12.76 ? 105 SER   A CB  1 
ATOM   889  O  OG  . SER   A 1 105 ? 31.980 12.642  45.940 1.00 19.60 ? 105 SER   A OG  1 
ATOM   890  N  N   . LEU   A 1 106 ? 31.254 14.510  43.788 1.00 10.33 ? 106 LEU   A N   1 
ATOM   891  C  CA  . LEU   A 1 106 ? 31.585 14.663  42.352 1.00 10.26 ? 106 LEU   A CA  1 
ATOM   892  C  C   . LEU   A 1 106 ? 31.275 16.107  41.911 1.00 10.43 ? 106 LEU   A C   1 
ATOM   893  O  O   . LEU   A 1 106 ? 32.048 16.685  41.168 1.00 9.88  ? 106 LEU   A O   1 
ATOM   894  C  CB  . LEU   A 1 106 ? 30.746 13.661  41.550 1.00 12.61 ? 106 LEU   A CB  1 
ATOM   895  C  CG  . LEU   A 1 106 ? 31.074 12.184  41.751 1.00 15.08 ? 106 LEU   A CG  1 
ATOM   896  C  CD1 . LEU   A 1 106 ? 30.267 11.321  40.795 1.00 18.79 ? 106 LEU   A CD1 1 
ATOM   897  C  CD2 . LEU   A 1 106 ? 32.561 11.923  41.572 1.00 15.51 ? 106 LEU   A CD2 1 
ATOM   898  N  N   . ASN   A 1 107 ? 30.142 16.619  42.370 1.00 10.09 ? 107 ASN   A N   1 
ATOM   899  C  CA  . ASN   A 1 107 ? 29.725 17.990  41.975 1.00 10.57 ? 107 ASN   A CA  1 
ATOM   900  C  C   . ASN   A 1 107 ? 30.776 19.011  42.446 1.00 8.56  ? 107 ASN   A C   1 
ATOM   901  O  O   . ASN   A 1 107 ? 31.144 19.888  41.683 1.00 9.68  ? 107 ASN   A O   1 
ATOM   902  C  CB  . ASN   A 1 107 ? 28.337 18.288  42.524 1.00 11.20 ? 107 ASN   A CB  1 
ATOM   903  C  CG  . ASN   A 1 107 ? 27.657 19.440  41.823 1.00 8.11  ? 107 ASN   A CG  1 
ATOM   904  O  OD1 . ASN   A 1 107 ? 27.794 19.593  40.619 1.00 11.93 ? 107 ASN   A OD1 1 
ATOM   905  N  ND2 . ASN   A 1 107 ? 26.914 20.233  42.571 1.00 9.50  ? 107 ASN   A ND2 1 
ATOM   906  N  N   . GLN   A 1 108 ? 31.217 18.848  43.688 1.00 9.19  ? 108 GLN   A N   1 
ATOM   907  C  CA  . GLN   A 1 108 ? 32.239 19.787  44.207 1.00 9.18  ? 108 GLN   A CA  1 
ATOM   908  C  C   . GLN   A 1 108 ? 33.513 19.678  43.364 1.00 8.47  ? 108 GLN   A C   1 
ATOM   909  O  O   . GLN   A 1 108 ? 34.150 20.670  43.113 1.00 9.12  ? 108 GLN   A O   1 
ATOM   910  C  CB  . GLN   A 1 108 ? 32.551 19.522  45.676 1.00 12.09 ? 108 GLN   A CB  1 
ATOM   911  C  CG  . GLN   A 1 108 ? 33.404 20.613  46.307 1.00 12.26 ? 108 GLN   A CG  1 
ATOM   912  C  CD  . GLN   A 1 108 ? 32.747 21.966  46.185 1.00 15.29 ? 108 GLN   A CD  1 
ATOM   913  O  OE1 . GLN   A 1 108 ? 31.652 22.187  46.681 1.00 14.04 ? 108 GLN   A OE1 1 
ATOM   914  N  NE2 . GLN   A 1 108 ? 33.417 22.886  45.513 1.00 14.26 ? 108 GLN   A NE2 1 
ATOM   915  N  N   . ALA   A 1 109 ? 33.848 18.448  42.976 1.00 9.45  ? 109 ALA   A N   1 
ATOM   916  C  CA  . ALA   A 1 109 ? 35.040 18.255  42.116 1.00 9.53  ? 109 ALA   A CA  1 
ATOM   917  C  C   . ALA   A 1 109 ? 34.840 18.954  40.764 1.00 9.69  ? 109 ALA   A C   1 
ATOM   918  O  O   . ALA   A 1 109 ? 35.794 19.511  40.246 1.00 10.05 ? 109 ALA   A O   1 
ATOM   919  C  CB  . ALA   A 1 109 ? 35.341 16.788  41.958 1.00 10.62 ? 109 ALA   A CB  1 
ATOM   920  N  N   . LEU   A 1 110 ? 33.627 18.885  40.227 1.00 7.75  ? 110 LEU   A N   1 
ATOM   921  C  CA  . LEU   A 1 110 ? 33.345 19.588  38.949 1.00 7.70  ? 110 LEU   A CA  1 
ATOM   922  C  C   . LEU   A 1 110 ? 33.511 21.097  39.166 1.00 9.21  ? 110 LEU   A C   1 
ATOM   923  O  O   . LEU   A 1 110 ? 34.055 21.756  38.315 1.00 10.01 ? 110 LEU   A O   1 
ATOM   924  C  CB  . LEU   A 1 110 ? 31.894 19.324  38.536 1.00 10.09 ? 110 LEU   A CB  1 
ATOM   925  C  CG  . LEU   A 1 110 ? 31.599 17.928  38.003 1.00 11.65 ? 110 LEU   A CG  1 
ATOM   926  C  CD1 . LEU   A 1 110 ? 30.103 17.738  37.816 1.00 14.26 ? 110 LEU   A CD1 1 
ATOM   927  C  CD2 . LEU   A 1 110 ? 32.336 17.689  36.695 1.00 13.77 ? 110 LEU   A CD2 1 
ATOM   928  N  N   . LEU   A 1 111 ? 32.963 21.562  40.286 1.00 9.62  ? 111 LEU   A N   1 
ATOM   929  C  CA  . LEU   A 1 111 ? 32.993 23.022  40.533 1.00 8.32  ? 111 LEU   A CA  1 
ATOM   930  C  C   . LEU   A 1 111 ? 34.444 23.457  40.742 1.00 11.10 ? 111 LEU   A C   1 
ATOM   931  O  O   . LEU   A 1 111 ? 34.819 24.531  40.302 1.00 10.41 ? 111 LEU   A O   1 
ATOM   932  C  CB  . LEU   A 1 111 ? 32.135 23.344  41.768 1.00 8.72  ? 111 LEU   A CB  1 
ATOM   933  C  CG  . LEU   A 1 111 ? 30.647 23.046  41.606 1.00 9.01  ? 111 LEU   A CG  1 
ATOM   934  C  CD1 . LEU   A 1 111 ? 29.897 23.245  42.913 1.00 10.10 ? 111 LEU   A CD1 1 
ATOM   935  C  CD2 . LEU   A 1 111 ? 30.048 23.911  40.507 1.00 12.77 ? 111 LEU   A CD2 1 
ATOM   936  N  N   . ASP   A 1 112 ? 35.191 22.627  41.447 1.00 7.90  ? 112 ASP   A N   1 
ATOM   937  C  CA  . ASP   A 1 112 ? 36.614 22.955  41.670 1.00 8.42  ? 112 ASP   A CA  1 
ATOM   938  C  C   . ASP   A 1 112 ? 37.349 23.052  40.325 1.00 11.13 ? 112 ASP   A C   1 
ATOM   939  O  O   . ASP   A 1 112 ? 38.160 23.964  40.170 1.00 11.83 ? 112 ASP   A O   1 
ATOM   940  C  CB  . ASP   A 1 112 ? 37.238 21.931  42.613 1.00 10.53 ? 112 ASP   A CB  1 
ATOM   941  C  CG  . ASP   A 1 112 ? 36.758 22.024  44.049 1.00 12.84 ? 112 ASP   A CG  1 
ATOM   942  O  OD1 . ASP   A 1 112 ? 36.103 23.010  44.383 1.00 13.52 ? 112 ASP   A OD1 1 
ATOM   943  O  OD2 . ASP   A 1 112 ? 37.063 21.102  44.811 1.00 17.11 ? 112 ASP   A OD2 1 
ATOM   944  N  N   . LEU   A 1 113 ? 37.103 22.097  39.423 1.00 9.60  ? 113 LEU   A N   1 
ATOM   945  C  CA  . LEU   A 1 113 ? 37.825 22.096  38.118 1.00 8.74  ? 113 LEU   A CA  1 
ATOM   946  C  C   . LEU   A 1 113 ? 37.382 23.313  37.299 1.00 8.98  ? 113 LEU   A C   1 
ATOM   947  O  O   . LEU   A 1 113 ? 38.185 23.899  36.615 1.00 10.80 ? 113 LEU   A O   1 
ATOM   948  C  CB  . LEU   A 1 113 ? 37.563 20.792  37.352 1.00 8.45  ? 113 LEU   A CB  1 
ATOM   949  C  CG  . LEU   A 1 113 ? 38.218 20.676  35.979 1.00 9.08  ? 113 LEU   A CG  1 
ATOM   950  C  CD1 . LEU   A 1 113 ? 39.722 20.884  36.079 1.00 12.61 ? 113 LEU   A CD1 1 
ATOM   951  C  CD2 . LEU   A 1 113 ? 37.912 19.326  35.353 1.00 11.99 ? 113 LEU   A CD2 1 
ATOM   952  N  N   . HIS   A 1 114 ? 36.089 23.618  37.387 1.00 10.09 ? 114 HIS   A N   1 
ATOM   953  C  CA  . HIS   A 1 114 ? 35.578 24.802  36.658 1.00 8.21  ? 114 HIS   A CA  1 
ATOM   954  C  C   . HIS   A 1 114 ? 36.306 26.053  37.164 1.00 10.66 ? 114 HIS   A C   1 
ATOM   955  O  O   . HIS   A 1 114 ? 36.689 26.880  36.358 1.00 11.97 ? 114 HIS   A O   1 
ATOM   956  C  CB  . HIS   A 1 114 ? 34.055 24.935  36.819 1.00 10.51 ? 114 HIS   A CB  1 
ATOM   957  C  CG  . HIS   A 1 114 ? 33.481 25.970  35.916 1.00 10.86 ? 114 HIS   A CG  1 
ATOM   958  N  ND1 . HIS   A 1 114 ? 33.583 27.314  36.181 1.00 12.97 ? 114 HIS   A ND1 1 
ATOM   959  C  CD2 . HIS   A 1 114 ? 32.823 25.865  34.746 1.00 10.44 ? 114 HIS   A CD2 1 
ATOM   960  C  CE1 . HIS   A 1 114 ? 33.007 27.995  35.215 1.00 9.96  ? 114 HIS   A CE1 1 
ATOM   961  N  NE2 . HIS   A 1 114 ? 32.537 27.134  34.325 1.00 9.79  ? 114 HIS   A NE2 1 
ATOM   962  N  N   . ALA   A 1 115 ? 36.466 26.127  38.475 1.00 9.97  ? 115 ALA   A N   1 
ATOM   963  C  CA  . ALA   A 1 115 ? 37.126 27.314  39.053 1.00 9.84  ? 115 ALA   A CA  1 
ATOM   964  C  C   . ALA   A 1 115 ? 38.574 27.379  38.562 1.00 10.34 ? 115 ALA   A C   1 
ATOM   965  O  O   . ALA   A 1 115 ? 39.065 28.478  38.335 1.00 12.55 ? 115 ALA   A O   1 
ATOM   966  C  CB  . ALA   A 1 115 ? 37.037 27.278  40.563 1.00 9.32  ? 115 ALA   A CB  1 
ATOM   967  N  N   . LEU   A 1 116 ? 39.214 26.223  38.488 1.00 11.80 ? 116 LEU   A N   1 
ATOM   968  C  CA  . LEU   A 1 116 ? 40.631 26.192  38.027 1.00 11.60 ? 116 LEU   A CA  1 
ATOM   969  C  C   . LEU   A 1 116 ? 40.684 26.667  36.571 1.00 12.10 ? 116 LEU   A C   1 
ATOM   970  O  O   . LEU   A 1 116 ? 41.558 27.448  36.225 1.00 13.24 ? 116 LEU   A O   1 
ATOM   971  C  CB  . LEU   A 1 116 ? 41.170 24.763  38.159 1.00 11.35 ? 116 LEU   A CB  1 
ATOM   972  C  CG  . LEU   A 1 116 ? 42.559 24.524  37.573 1.00 12.90 ? 116 LEU   A CG  1 
ATOM   973  C  CD1 . LEU   A 1 116 ? 43.586 25.412  38.252 1.00 14.12 ? 116 LEU   A CD1 1 
ATOM   974  C  CD2 . LEU   A 1 116 ? 42.956 23.065  37.701 1.00 13.27 ? 116 LEU   A CD2 1 
ATOM   975  N  N   . GLY   A 1 117 ? 39.756 26.169  35.761 1.00 12.29 ? 117 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 117 ? 39.731 26.584  34.352 1.00 11.30 ? 117 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 117 ? 39.452 28.062  34.223 1.00 11.01 ? 117 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 117 ? 40.028 28.704  33.391 1.00 13.76 ? 117 GLY   A O   1 
ATOM   979  N  N   . SER   A 1 118 ? 38.554 28.561  35.056 1.00 12.03 ? 118 SER   A N   1 
ATOM   980  C  CA  A SER   A 1 118 ? 38.306 30.028  35.039 0.31 10.87 ? 118 SER   A CA  1 
ATOM   981  C  CA  B SER   A 1 118 ? 38.306 30.025  35.037 0.69 10.73 ? 118 SER   A CA  1 
ATOM   982  C  C   . SER   A 1 118 ? 39.575 30.843  35.407 1.00 13.47 ? 118 SER   A C   1 
ATOM   983  O  O   . SER   A 1 118 ? 40.041 31.886  34.784 1.00 14.29 ? 118 SER   A O   1 
ATOM   984  C  CB  A SER   A 1 118 ? 37.144 30.402  35.928 0.31 16.07 ? 118 SER   A CB  1 
ATOM   985  C  CB  B SER   A 1 118 ? 37.138 30.381  35.922 0.69 16.16 ? 118 SER   A CB  1 
ATOM   986  O  OG  A SER   A 1 118 ? 36.074 29.485  35.773 0.31 12.79 ? 118 SER   A OG  1 
ATOM   987  O  OG  B SER   A 1 118 ? 36.855 31.766  35.834 0.69 16.32 ? 118 SER   A OG  1 
ATOM   988  N  N   . ALA   A 1 119 ? 40.254 30.329  36.424 1.00 12.07 ? 119 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 119 ? 41.497 31.015  36.865 1.00 14.68 ? 119 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 119 ? 42.569 30.941  35.777 1.00 17.64 ? 119 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 119 ? 43.385 31.865  35.695 1.00 18.63 ? 119 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 119 ? 42.030 30.413  38.120 1.00 16.10 ? 119 ALA   A CB  1 
ATOM   993  N  N   . GLN   A 1 120 ? 42.580 29.856  35.022 1.00 13.72 ? 120 GLN   A N   1 
ATOM   994  C  CA  . GLN   A 1 120 ? 43.618 29.668  33.986 1.00 16.18 ? 120 GLN   A CA  1 
ATOM   995  C  C   . GLN   A 1 120 ? 43.140 30.214  32.628 1.00 16.14 ? 120 GLN   A C   1 
ATOM   996  O  O   . GLN   A 1 120 ? 43.834 29.985  31.648 1.00 17.75 ? 120 GLN   A O   1 
ATOM   997  C  CB  . GLN   A 1 120 ? 43.919 28.180  33.868 1.00 11.45 ? 120 GLN   A CB  1 
ATOM   998  C  CG  . GLN   A 1 120 ? 44.555 27.568  35.104 1.00 19.32 ? 120 GLN   A CG  1 
ATOM   999  C  CD  . GLN   A 1 120 ? 46.060 27.650  35.078 1.00 32.48 ? 120 GLN   A CD  1 
ATOM   1000 O  OE1 . GLN   A 1 120 ? 46.665 27.973  34.062 1.00 33.71 ? 120 GLN   A OE1 1 
ATOM   1001 N  NE2 . GLN   A 1 120 ? 46.678 27.374  36.213 1.00 31.83 ? 120 GLN   A NE2 1 
ATOM   1002 N  N   . ALA   A 1 121 ? 42.003 30.878  32.605 1.00 11.42 ? 121 ALA   A N   1 
ATOM   1003 C  CA  . ALA   A 1 121 ? 41.487 31.450  31.348 1.00 12.58 ? 121 ALA   A CA  1 
ATOM   1004 C  C   . ALA   A 1 121 ? 41.423 30.327  30.316 1.00 12.24 ? 121 ALA   A C   1 
ATOM   1005 O  O   . ALA   A 1 121 ? 41.895 30.523  29.208 1.00 10.88 ? 121 ALA   A O   1 
ATOM   1006 C  CB  . ALA   A 1 121 ? 42.309 32.623  30.899 1.00 17.09 ? 121 ALA   A CB  1 
ATOM   1007 N  N   . ASP   A 1 122 ? 40.727 29.248  30.706 1.00 9.34  ? 122 ASP   A N   1 
ATOM   1008 C  CA  . ASP   A 1 122 ? 40.519 28.084  29.804 1.00 9.28  ? 122 ASP   A CA  1 
ATOM   1009 C  C   . ASP   A 1 122 ? 39.013 27.924  29.537 1.00 10.84 ? 122 ASP   A C   1 
ATOM   1010 O  O   . ASP   A 1 122 ? 38.376 27.101  30.143 1.00 10.68 ? 122 ASP   A O   1 
ATOM   1011 C  CB  . ASP   A 1 122 ? 41.086 26.814  30.425 1.00 13.12 ? 122 ASP   A CB  1 
ATOM   1012 C  CG  . ASP   A 1 122 ? 41.149 25.633  29.478 1.00 9.74  ? 122 ASP   A CG  1 
ATOM   1013 O  OD1 . ASP   A 1 122 ? 40.422 25.651  28.478 1.00 8.62  ? 122 ASP   A OD1 1 
ATOM   1014 O  OD2 . ASP   A 1 122 ? 41.927 24.723  29.767 1.00 10.49 ? 122 ASP   A OD2 1 
ATOM   1015 N  N   . PRO   A 1 123 ? 38.438 28.723  28.624 1.00 8.00  ? 123 PRO   A N   1 
ATOM   1016 C  CA  . PRO   A 1 123 ? 37.003 28.673  28.435 1.00 9.85  ? 123 PRO   A CA  1 
ATOM   1017 C  C   . PRO   A 1 123 ? 36.480 27.399  27.756 1.00 9.69  ? 123 PRO   A C   1 
ATOM   1018 O  O   . PRO   A 1 123 ? 35.351 27.102  27.904 1.00 10.89 ? 123 PRO   A O   1 
ATOM   1019 C  CB  . PRO   A 1 123 ? 36.738 29.888  27.531 1.00 11.10 ? 123 PRO   A CB  1 
ATOM   1020 C  CG  . PRO   A 1 123 ? 38.025 30.115  26.783 1.00 9.27  ? 123 PRO   A CG  1 
ATOM   1021 C  CD  . PRO   A 1 123 ? 39.092 29.750  27.791 1.00 10.15 ? 123 PRO   A CD  1 
ATOM   1022 N  N   . HIS   A 1 124 ? 37.340 26.737  26.987 1.00 9.37  ? 124 HIS   A N   1 
ATOM   1023 C  CA  . HIS   A 1 124 ? 36.846 25.467  26.408 1.00 7.76  ? 124 HIS   A CA  1 
ATOM   1024 C  C   . HIS   A 1 124 ? 36.532 24.518  27.574 1.00 8.88  ? 124 HIS   A C   1 
ATOM   1025 O  O   . HIS   A 1 124 ? 35.492 23.877  27.543 1.00 9.58  ? 124 HIS   A O   1 
ATOM   1026 C  CB  . HIS   A 1 124 ? 37.839 24.881  25.406 1.00 8.29  ? 124 HIS   A CB  1 
ATOM   1027 C  CG  . HIS   A 1 124 ? 37.336 23.619  24.798 1.00 11.35 ? 124 HIS   A CG  1 
ATOM   1028 N  ND1 . HIS   A 1 124 ? 37.506 22.391  25.399 1.00 10.31 ? 124 HIS   A ND1 1 
ATOM   1029 C  CD2 . HIS   A 1 124 ? 36.642 23.396  23.666 1.00 12.48 ? 124 HIS   A CD2 1 
ATOM   1030 C  CE1 . HIS   A 1 124 ? 36.949 21.465  24.651 1.00 10.32 ? 124 HIS   A CE1 1 
ATOM   1031 N  NE2 . HIS   A 1 124 ? 36.414 22.054  23.586 1.00 10.97 ? 124 HIS   A NE2 1 
ATOM   1032 N  N   . LEU   A 1 125 ? 37.460 24.451  28.521 1.00 8.55  ? 125 LEU   A N   1 
ATOM   1033 C  CA  A LEU   A 1 125 ? 37.236 23.518  29.668 0.44 7.64  ? 125 LEU   A CA  1 
ATOM   1034 C  CA  B LEU   A 1 125 ? 37.243 23.537  29.685 0.56 7.63  ? 125 LEU   A CA  1 
ATOM   1035 C  C   . LEU   A 1 125 ? 35.938 23.911  30.452 1.00 8.67  ? 125 LEU   A C   1 
ATOM   1036 O  O   . LEU   A 1 125 ? 35.003 23.134  30.810 1.00 9.34  ? 125 LEU   A O   1 
ATOM   1037 C  CB  A LEU   A 1 125 ? 38.448 23.547  30.604 0.44 9.20  ? 125 LEU   A CB  1 
ATOM   1038 C  CB  B LEU   A 1 125 ? 38.479 23.597  30.593 0.56 9.17  ? 125 LEU   A CB  1 
ATOM   1039 C  CG  A LEU   A 1 125 ? 38.268 22.730  31.880 0.44 12.34 ? 125 LEU   A CG  1 
ATOM   1040 C  CG  B LEU   A 1 125 ? 38.523 22.668  31.807 0.56 11.81 ? 125 LEU   A CG  1 
ATOM   1041 C  CD1 A LEU   A 1 125 ? 38.376 21.247  31.589 0.44 9.14  ? 125 LEU   A CD1 1 
ATOM   1042 C  CD1 B LEU   A 1 125 ? 37.739 23.238  32.979 0.56 8.21  ? 125 LEU   A CD1 1 
ATOM   1043 C  CD2 A LEU   A 1 125 ? 39.260 23.142  32.944 0.44 8.67  ? 125 LEU   A CD2 1 
ATOM   1044 C  CD2 B LEU   A 1 125 ? 38.055 21.267  31.461 0.56 10.56 ? 125 LEU   A CD2 1 
ATOM   1045 N  N   . CYS   A 1 126 ? 35.857 25.230  30.666 1.00 11.48 ? 126 CYS   A N   1 
ATOM   1046 C  CA  . CYS   A 1 126 ? 34.694 25.704  31.447 1.00 9.28  ? 126 CYS   A CA  1 
ATOM   1047 C  C   . CYS   A 1 126 ? 33.404 25.345  30.714 1.00 11.74 ? 126 CYS   A C   1 
ATOM   1048 O  O   . CYS   A 1 126 ? 32.499 24.851  31.340 1.00 12.36 ? 126 CYS   A O   1 
ATOM   1049 C  CB  . CYS   A 1 126 ? 34.812 27.201  31.682 1.00 11.69 ? 126 CYS   A CB  1 
ATOM   1050 S  SG  . CYS   A 1 126 ? 36.129 27.604  32.863 1.00 13.45 ? 126 CYS   A SG  1 
ATOM   1051 N  N   A ASP   A 1 127 ? 33.370 25.595  29.417 0.52 11.98 ? 127 ASP   A N   1 
ATOM   1052 N  N   B ASP   A 1 127 ? 33.374 25.584  29.410 0.48 11.99 ? 127 ASP   A N   1 
ATOM   1053 C  CA  A ASP   A 1 127 ? 32.154 25.289  28.613 0.52 13.65 ? 127 ASP   A CA  1 
ATOM   1054 C  CA  B ASP   A 1 127 ? 32.142 25.289  28.635 0.48 13.67 ? 127 ASP   A CA  1 
ATOM   1055 C  C   A ASP   A 1 127 ? 31.905 23.773  28.566 0.52 12.23 ? 127 ASP   A C   1 
ATOM   1056 C  C   B ASP   A 1 127 ? 31.906 23.773  28.589 0.48 12.24 ? 127 ASP   A C   1 
ATOM   1057 O  O   A ASP   A 1 127 ? 30.756 23.364  28.579 0.52 12.92 ? 127 ASP   A O   1 
ATOM   1058 O  O   B ASP   A 1 127 ? 30.746 23.360  28.566 0.48 12.94 ? 127 ASP   A O   1 
ATOM   1059 C  CB  A ASP   A 1 127 ? 32.250 25.869  27.207 0.52 15.56 ? 127 ASP   A CB  1 
ATOM   1060 C  CB  B ASP   A 1 127 ? 32.173 25.882  27.230 0.48 15.58 ? 127 ASP   A CB  1 
ATOM   1061 C  CG  A ASP   A 1 127 ? 31.261 25.285  26.213 0.52 16.14 ? 127 ASP   A CG  1 
ATOM   1062 C  CG  B ASP   A 1 127 ? 30.812 25.809  26.563 0.48 16.85 ? 127 ASP   A CG  1 
ATOM   1063 O  OD1 A ASP   A 1 127 ? 30.178 25.829  26.122 0.52 14.15 ? 127 ASP   A OD1 1 
ATOM   1064 O  OD1 B ASP   A 1 127 ? 29.839 26.302  27.163 0.48 20.34 ? 127 ASP   A OD1 1 
ATOM   1065 O  OD2 A ASP   A 1 127 ? 31.600 24.295  25.538 0.52 17.06 ? 127 ASP   A OD2 1 
ATOM   1066 O  OD2 B ASP   A 1 127 ? 30.734 25.244  25.473 0.48 21.14 ? 127 ASP   A OD2 1 
ATOM   1067 N  N   . PHE   A 1 128 ? 32.991 23.000  28.480 1.00 9.74  ? 128 PHE   A N   1 
ATOM   1068 C  CA  . PHE   A 1 128 ? 32.841 21.528  28.431 1.00 9.48  ? 128 PHE   A CA  1 
ATOM   1069 C  C   . PHE   A 1 128 ? 32.087 21.083  29.691 1.00 12.38 ? 128 PHE   A C   1 
ATOM   1070 O  O   . PHE   A 1 128 ? 31.164 20.294  29.599 1.00 9.95  ? 128 PHE   A O   1 
ATOM   1071 C  CB  . PHE   A 1 128 ? 34.213 20.860  28.287 1.00 10.21 ? 128 PHE   A CB  1 
ATOM   1072 C  CG  . PHE   A 1 128 ? 34.215 19.372  28.488 1.00 10.53 ? 128 PHE   A CG  1 
ATOM   1073 C  CD1 . PHE   A 1 128 ? 33.930 18.522  27.437 1.00 14.30 ? 128 PHE   A CD1 1 
ATOM   1074 C  CD2 . PHE   A 1 128 ? 34.499 18.827  29.726 1.00 14.37 ? 128 PHE   A CD2 1 
ATOM   1075 C  CE1 . PHE   A 1 128 ? 33.919 17.152  27.622 1.00 14.04 ? 128 PHE   A CE1 1 
ATOM   1076 C  CE2 . PHE   A 1 128 ? 34.502 17.456  29.904 1.00 14.77 ? 128 PHE   A CE2 1 
ATOM   1077 C  CZ  . PHE   A 1 128 ? 34.208 16.625  28.854 1.00 14.77 ? 128 PHE   A CZ  1 
ATOM   1078 N  N   . LEU   A 1 129 ? 32.530 21.601  30.831 1.00 9.40  ? 129 LEU   A N   1 
ATOM   1079 C  CA  . LEU   A 1 129 ? 31.889 21.157  32.093 1.00 6.70  ? 129 LEU   A CA  1 
ATOM   1080 C  C   . LEU   A 1 129 ? 30.444 21.654  32.149 1.00 11.85 ? 129 LEU   A C   1 
ATOM   1081 O  O   . LEU   A 1 129 ? 29.566 20.927  32.586 1.00 11.20 ? 129 LEU   A O   1 
ATOM   1082 C  CB  . LEU   A 1 129 ? 32.706 21.708  33.264 1.00 9.30  ? 129 LEU   A CB  1 
ATOM   1083 C  CG  . LEU   A 1 129 ? 34.104 21.115  33.392 1.00 11.54 ? 129 LEU   A CG  1 
ATOM   1084 C  CD1 . LEU   A 1 129 ? 34.857 21.753  34.548 1.00 10.14 ? 129 LEU   A CD1 1 
ATOM   1085 C  CD2 . LEU   A 1 129 ? 34.033 19.606  33.560 1.00 11.44 ? 129 LEU   A CD2 1 
ATOM   1086 N  N   . GLU   A 1 130 ? 30.268 22.893  31.728 1.00 13.15 ? 130 GLU   A N   1 
ATOM   1087 C  CA  . GLU   A 1 130 ? 28.914 23.487  31.784 1.00 15.29 ? 130 GLU   A CA  1 
ATOM   1088 C  C   . GLU   A 1 130 ? 27.976 22.699  30.878 1.00 16.25 ? 130 GLU   A C   1 
ATOM   1089 O  O   . GLU   A 1 130 ? 26.851 22.432  31.299 1.00 18.23 ? 130 GLU   A O   1 
ATOM   1090 C  CB  . GLU   A 1 130 ? 28.976 24.933  31.301 1.00 14.88 ? 130 GLU   A CB  1 
ATOM   1091 C  CG  . GLU   A 1 130 ? 29.677 25.871  32.261 1.00 15.79 ? 130 GLU   A CG  1 
ATOM   1092 C  CD  . GLU   A 1 130 ? 30.124 27.179  31.627 1.00 22.55 ? 130 GLU   A CD  1 
ATOM   1093 O  OE1 . GLU   A 1 130 ? 29.650 27.490  30.520 1.00 22.90 ? 130 GLU   A OE1 1 
ATOM   1094 O  OE2 . GLU   A 1 130 ? 30.940 27.876  32.237 1.00 17.14 ? 130 GLU   A OE2 1 
ATOM   1095 N  N   . SER   A 1 131 ? 28.423 22.413  29.671 1.00 13.37 ? 131 SER   A N   1 
ATOM   1096 C  CA  . SER   A 1 131 ? 27.539 21.779  28.662 1.00 15.42 ? 131 SER   A CA  1 
ATOM   1097 C  C   . SER   A 1 131 ? 27.232 20.307  28.948 1.00 15.67 ? 131 SER   A C   1 
ATOM   1098 O  O   . SER   A 1 131 ? 26.129 19.893  28.619 1.00 19.62 ? 131 SER   A O   1 
ATOM   1099 C  CB  . SER   A 1 131 ? 28.157 21.963  27.290 1.00 22.19 ? 131 SER   A CB  1 
ATOM   1100 O  OG  . SER   A 1 131 ? 28.448 23.333  27.083 1.00 31.46 ? 131 SER   A OG  1 
ATOM   1101 N  N   . HIS   A 1 132 ? 28.193 19.563  29.484 1.00 11.96 ? 132 HIS   A N   1 
ATOM   1102 C  CA  . HIS   A 1 132 ? 27.963 18.106  29.628 1.00 17.08 ? 132 HIS   A CA  1 
ATOM   1103 C  C   . HIS   A 1 132 ? 27.901 17.593  31.079 1.00 14.32 ? 132 HIS   A C   1 
ATOM   1104 O  O   . HIS   A 1 132 ? 27.606 16.424  31.238 1.00 17.89 ? 132 HIS   A O   1 
ATOM   1105 C  CB  . HIS   A 1 132 ? 29.054 17.379  28.849 1.00 18.54 ? 132 HIS   A CB  1 
ATOM   1106 C  CG  . HIS   A 1 132 ? 29.151 17.861  27.449 1.00 24.48 ? 132 HIS   A CG  1 
ATOM   1107 N  ND1 . HIS   A 1 132 ? 28.079 17.810  26.592 1.00 27.65 ? 132 HIS   A ND1 1 
ATOM   1108 C  CD2 . HIS   A 1 132 ? 30.165 18.431  26.769 1.00 29.06 ? 132 HIS   A CD2 1 
ATOM   1109 C  CE1 . HIS   A 1 132 ? 28.433 18.304  25.427 1.00 32.63 ? 132 HIS   A CE1 1 
ATOM   1110 N  NE2 . HIS   A 1 132 ? 29.706 18.690  25.511 1.00 35.79 ? 132 HIS   A NE2 1 
ATOM   1111 N  N   . PHE   A 1 133 ? 28.204 18.419  32.077 1.00 9.84  ? 133 PHE   A N   1 
ATOM   1112 C  CA  . PHE   A 1 133 ? 28.294 17.844  33.444 1.00 11.17 ? 133 PHE   A CA  1 
ATOM   1113 C  C   . PHE   A 1 133 ? 27.526 18.613  34.524 1.00 10.70 ? 133 PHE   A C   1 
ATOM   1114 O  O   . PHE   A 1 133 ? 26.843 17.988  35.307 1.00 12.20 ? 133 PHE   A O   1 
ATOM   1115 C  CB  . PHE   A 1 133 ? 29.757 17.770  33.875 1.00 11.50 ? 133 PHE   A CB  1 
ATOM   1116 C  CG  . PHE   A 1 133 ? 30.554 16.687  33.194 1.00 13.66 ? 133 PHE   A CG  1 
ATOM   1117 C  CD1 . PHE   A 1 133 ? 31.096 16.883  31.937 1.00 14.85 ? 133 PHE   A CD1 1 
ATOM   1118 C  CD2 . PHE   A 1 133 ? 30.747 15.464  33.809 1.00 14.56 ? 133 PHE   A CD2 1 
ATOM   1119 C  CE1 . PHE   A 1 133 ? 31.806 15.875  31.307 1.00 13.60 ? 133 PHE   A CE1 1 
ATOM   1120 C  CE2 . PHE   A 1 133 ? 31.465 14.461  33.183 1.00 15.46 ? 133 PHE   A CE2 1 
ATOM   1121 C  CZ  . PHE   A 1 133 ? 31.993 14.668  31.933 1.00 13.05 ? 133 PHE   A CZ  1 
ATOM   1122 N  N   . LEU   A 1 134 ? 27.646 19.929  34.531 1.00 11.96 ? 134 LEU   A N   1 
ATOM   1123 C  CA  . LEU   A 1 134 ? 27.054 20.660  35.681 1.00 9.48  ? 134 LEU   A CA  1 
ATOM   1124 C  C   . LEU   A 1 134 ? 25.530 20.439  35.802 1.00 11.44 ? 134 LEU   A C   1 
ATOM   1125 O  O   . LEU   A 1 134 ? 25.059 20.278  36.914 1.00 10.03 ? 134 LEU   A O   1 
ATOM   1126 C  CB  . LEU   A 1 134 ? 27.353 22.154  35.548 1.00 11.38 ? 134 LEU   A CB  1 
ATOM   1127 C  CG  . LEU   A 1 134 ? 28.840 22.492  35.645 1.00 10.72 ? 134 LEU   A CG  1 
ATOM   1128 C  CD1 . LEU   A 1 134 ? 29.060 23.986  35.805 1.00 13.59 ? 134 LEU   A CD1 1 
ATOM   1129 C  CD2 . LEU   A 1 134 ? 29.487 21.730  36.790 1.00 11.58 ? 134 LEU   A CD2 1 
ATOM   1130 N  N   . ASP   A 1 135 ? 24.823 20.615  34.695 1.00 11.75 ? 135 ASP   A N   1 
ATOM   1131 C  CA  . ASP   A 1 135 ? 23.342 20.514  34.784 1.00 10.13 ? 135 ASP   A CA  1 
ATOM   1132 C  C   . ASP   A 1 135 ? 22.919 19.048  34.981 1.00 9.83  ? 135 ASP   A C   1 
ATOM   1133 O  O   . ASP   A 1 135 ? 22.001 18.789  35.732 1.00 13.82 ? 135 ASP   A O   1 
ATOM   1134 C  CB  . ASP   A 1 135 ? 22.632 21.132  33.580 1.00 13.38 ? 135 ASP   A CB  1 
ATOM   1135 C  CG  . ASP   A 1 135 ? 21.133 21.218  33.792 1.00 21.87 ? 135 ASP   A CG  1 
ATOM   1136 O  OD1 . ASP   A 1 135 ? 20.723 21.726  34.842 1.00 17.89 ? 135 ASP   A OD1 1 
ATOM   1137 O  OD2 . ASP   A 1 135 ? 20.401 20.756  32.916 1.00 23.40 ? 135 ASP   A OD2 1 
ATOM   1138 N  N   . GLU   A 1 136 ? 23.616 18.129  34.319 1.00 12.32 ? 136 GLU   A N   1 
ATOM   1139 C  CA  . GLU   A 1 136 ? 23.265 16.709  34.540 1.00 15.17 ? 136 GLU   A CA  1 
ATOM   1140 C  C   . GLU   A 1 136 ? 23.397 16.389  36.037 1.00 11.39 ? 136 GLU   A C   1 
ATOM   1141 O  O   . GLU   A 1 136 ? 22.595 15.656  36.569 1.00 13.01 ? 136 GLU   A O   1 
ATOM   1142 C  CB  . GLU   A 1 136 ? 24.169 15.814  33.697 1.00 17.82 ? 136 GLU   A CB  1 
ATOM   1143 C  CG  . GLU   A 1 136 ? 24.066 16.089  32.209 1.00 21.65 ? 136 GLU   A CG  1 
ATOM   1144 C  CD  . GLU   A 1 136 ? 22.775 15.627  31.555 1.00 52.40 ? 136 GLU   A CD  1 
ATOM   1145 O  OE1 . GLU   A 1 136 ? 21.803 16.406  31.549 1.00 64.33 ? 136 GLU   A OE1 1 
ATOM   1146 O  OE2 . GLU   A 1 136 ? 22.748 14.493  31.040 1.00 49.57 ? 136 GLU   A OE2 1 
ATOM   1147 N  N   . GLU   A 1 137 ? 24.466 16.880  36.640 1.00 10.14 ? 137 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 137 ? 24.729 16.615  38.064 1.00 10.31 ? 137 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 137 ? 23.619 17.260  38.892 1.00 9.98  ? 137 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 137 ? 23.129 16.635  39.811 1.00 9.85  ? 137 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 137 ? 26.133 17.110  38.436 1.00 11.70 ? 137 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 137 ? 26.592 16.645  39.794 1.00 11.18 ? 137 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 137 ? 26.597 15.135  39.942 1.00 9.71  ? 137 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 137 ? 26.890 14.446  38.959 1.00 11.27 ? 137 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 137 ? 26.276 14.676  41.028 1.00 15.11 ? 137 GLU   A OE2 1 
ATOM   1156 N  N   . VAL   A 1 138 ? 23.277 18.499  38.564 1.00 9.00  ? 138 VAL   A N   1 
ATOM   1157 C  CA  . VAL   A 1 138 ? 22.239 19.150  39.407 1.00 9.27  ? 138 VAL   A CA  1 
ATOM   1158 C  C   . VAL   A 1 138 ? 20.924 18.362  39.280 1.00 8.39  ? 138 VAL   A C   1 
ATOM   1159 O  O   . VAL   A 1 138 ? 20.250 18.180  40.281 1.00 11.11 ? 138 VAL   A O   1 
ATOM   1160 C  CB  . VAL   A 1 138 ? 22.076 20.632  39.003 1.00 8.41  ? 138 VAL   A CB  1 
ATOM   1161 C  CG1 . VAL   A 1 138 ? 20.675 21.162  39.279 1.00 10.96 ? 138 VAL   A CG1 1 
ATOM   1162 C  CG2 . VAL   A 1 138 ? 23.128 21.502  39.663 1.00 12.04 ? 138 VAL   A CG2 1 
ATOM   1163 N  N   . LYS   A 1 139 ? 20.610 17.946  38.065 1.00 9.41  ? 139 LYS   A N   1 
ATOM   1164 C  CA  . LYS   A 1 139 ? 19.347 17.202  37.820 1.00 9.27  ? 139 LYS   A CA  1 
ATOM   1165 C  C   . LYS   A 1 139 ? 19.365 15.862  38.578 1.00 12.81 ? 139 LYS   A C   1 
ATOM   1166 O  O   . LYS   A 1 139 ? 18.345 15.460  39.114 1.00 12.12 ? 139 LYS   A O   1 
ATOM   1167 C  CB  . LYS   A 1 139 ? 19.139 17.011  36.316 1.00 9.33  ? 139 LYS   A CB  1 
ATOM   1168 C  CG  . LYS   A 1 139 ? 18.495 18.198  35.617 1.00 19.52 ? 139 LYS   A CG  1 
ATOM   1169 C  CD  . LYS   A 1 139 ? 18.592 18.155  34.113 1.00 26.77 ? 139 LYS   A CD  1 
ATOM   1170 C  CE  . LYS   A 1 139 ? 17.678 19.159  33.438 1.00 45.08 ? 139 LYS   A CE  1 
ATOM   1171 N  NZ  . LYS   A 1 139 ? 17.854 20.534  33.963 1.00 32.75 ? 139 LYS   A NZ  1 
ATOM   1172 N  N   . LEU   A 1 140 ? 20.519 15.211  38.583 1.00 8.70  ? 140 LEU   A N   1 
ATOM   1173 C  CA  . LEU   A 1 140 ? 20.589 13.886  39.262 1.00 11.85 ? 140 LEU   A CA  1 
ATOM   1174 C  C   . LEU   A 1 140 ? 20.440 14.062  40.781 1.00 14.88 ? 140 LEU   A C   1 
ATOM   1175 O  O   . LEU   A 1 140 ? 19.785 13.255  41.408 1.00 12.85 ? 140 LEU   A O   1 
ATOM   1176 C  CB  . LEU   A 1 140 ? 21.905 13.190  38.890 1.00 10.64 ? 140 LEU   A CB  1 
ATOM   1177 C  CG  . LEU   A 1 140 ? 22.201 11.858  39.571 1.00 11.10 ? 140 LEU   A CG  1 
ATOM   1178 C  CD1 . LEU   A 1 140 ? 21.080 10.861  39.327 1.00 12.65 ? 140 LEU   A CD1 1 
ATOM   1179 C  CD2 . LEU   A 1 140 ? 23.524 11.303  39.067 1.00 13.70 ? 140 LEU   A CD2 1 
ATOM   1180 N  N   . ILE   A 1 141 ? 21.085 15.085  41.331 1.00 10.34 ? 141 ILE   A N   1 
ATOM   1181 C  CA  . ILE   A 1 141 ? 21.013 15.305  42.798 1.00 7.44  ? 141 ILE   A CA  1 
ATOM   1182 C  C   . ILE   A 1 141 ? 19.569 15.677  43.189 1.00 7.81  ? 141 ILE   A C   1 
ATOM   1183 O  O   . ILE   A 1 141 ? 19.098 15.244  44.231 1.00 11.11 ? 141 ILE   A O   1 
ATOM   1184 C  CB  . ILE   A 1 141 ? 22.056 16.350  43.244 1.00 9.21  ? 141 ILE   A CB  1 
ATOM   1185 C  CG1 . ILE   A 1 141 ? 23.476 15.824  43.021 1.00 9.09  ? 141 ILE   A CG1 1 
ATOM   1186 C  CG2 . ILE   A 1 141 ? 21.824 16.772  44.685 1.00 13.10 ? 141 ILE   A CG2 1 
ATOM   1187 C  CD1 . ILE   A 1 141 ? 24.559 16.844  43.253 1.00 11.42 ? 141 ILE   A CD1 1 
ATOM   1188 N  N   . LYS   A 1 142 ? 18.915 16.458  42.337 1.00 9.44  ? 142 LYS   A N   1 
ATOM   1189 C  CA  . LYS   A 1 142 ? 17.488 16.787  42.623 1.00 9.79  ? 142 LYS   A CA  1 
ATOM   1190 C  C   . LYS   A 1 142 ? 16.632 15.509  42.649 1.00 9.45  ? 142 LYS   A C   1 
ATOM   1191 O  O   . LYS   A 1 142 ? 15.812 15.368  43.524 1.00 10.67 ? 142 LYS   A O   1 
ATOM   1192 C  CB  . LYS   A 1 142 ? 16.950 17.772  41.582 1.00 8.60  ? 142 LYS   A CB  1 
ATOM   1193 C  CG  . LYS   A 1 142 ? 15.447 18.024  41.624 1.00 9.77  ? 142 LYS   A CG  1 
ATOM   1194 C  CD  . LYS   A 1 142 ? 14.970 18.705  42.882 1.00 9.94  ? 142 LYS   A CD  1 
ATOM   1195 C  CE  . LYS   A 1 142 ? 13.595 19.319  42.734 1.00 11.18 ? 142 LYS   A CE  1 
ATOM   1196 N  NZ  . LYS   A 1 142 ? 12.545 18.285  42.582 1.00 10.37 ? 142 LYS   A NZ  1 
ATOM   1197 N  N   . LYS   A 1 143 ? 16.854 14.646  41.680 1.00 11.30 ? 143 LYS   A N   1 
ATOM   1198 C  CA  . LYS   A 1 143 ? 16.088 13.375  41.626 1.00 11.79 ? 143 LYS   A CA  1 
ATOM   1199 C  C   . LYS   A 1 143 ? 16.353 12.519  42.883 1.00 11.51 ? 143 LYS   A C   1 
ATOM   1200 O  O   . LYS   A 1 143 ? 15.422 11.976  43.443 1.00 11.13 ? 143 LYS   A O   1 
ATOM   1201 C  CB  . LYS   A 1 143 ? 16.437 12.614  40.341 1.00 10.32 ? 143 LYS   A CB  1 
ATOM   1202 C  CG  . LYS   A 1 143 ? 15.840 11.220  40.250 1.00 16.53 ? 143 LYS   A CG  1 
ATOM   1203 C  CD  . LYS   A 1 143 ? 14.342 11.238  40.335 1.00 31.64 ? 143 LYS   A CD  1 
ATOM   1204 C  CE  . LYS   A 1 143 ? 13.706 11.893  39.134 1.00 30.12 ? 143 LYS   A CE  1 
ATOM   1205 N  NZ  . LYS   A 1 143 ? 12.278 11.521  39.004 1.00 33.62 ? 143 LYS   A NZ  1 
ATOM   1206 N  N   . MET   A 1 144 ? 17.614 12.429  43.284 1.00 11.70 ? 144 MET   A N   1 
ATOM   1207 C  CA  . MET   A 1 144 ? 17.921 11.650  44.502 1.00 10.75 ? 144 MET   A CA  1 
ATOM   1208 C  C   . MET   A 1 144 ? 17.261 12.289  45.728 1.00 13.05 ? 144 MET   A C   1 
ATOM   1209 O  O   . MET   A 1 144 ? 16.843 11.568  46.609 1.00 13.59 ? 144 MET   A O   1 
ATOM   1210 C  CB  . MET   A 1 144 ? 19.434 11.539  44.721 1.00 13.16 ? 144 MET   A CB  1 
ATOM   1211 C  CG  . MET   A 1 144 ? 20.093 10.716  43.656 1.00 11.82 ? 144 MET   A CG  1 
ATOM   1212 S  SD  . MET   A 1 144 ? 21.875 10.643  43.936 1.00 12.68 ? 144 MET   A SD  1 
ATOM   1213 C  CE  . MET   A 1 144 ? 22.322 9.339   42.791 1.00 10.12 ? 144 MET   A CE  1 
ATOM   1214 N  N   . GLY   A 1 145 ? 17.257 13.621  45.777 1.00 9.93  ? 145 GLY   A N   1 
ATOM   1215 C  CA  . GLY   A 1 145 ? 16.626 14.308  46.911 1.00 8.78  ? 145 GLY   A CA  1 
ATOM   1216 C  C   . GLY   A 1 145 ? 15.122 14.002  46.929 1.00 9.04  ? 145 GLY   A C   1 
ATOM   1217 O  O   . GLY   A 1 145 ? 14.581 13.726  47.984 1.00 9.07  ? 145 GLY   A O   1 
ATOM   1218 N  N   . ASP   A 1 146 ? 14.520 14.037  45.747 1.00 10.13 ? 146 ASP   A N   1 
ATOM   1219 C  CA  . ASP   A 1 146 ? 13.099 13.656  45.639 1.00 9.70  ? 146 ASP   A CA  1 
ATOM   1220 C  C   . ASP   A 1 146 ? 12.909 12.240  46.202 1.00 12.14 ? 146 ASP   A C   1 
ATOM   1221 O  O   . ASP   A 1 146 ? 11.947 12.002  46.909 1.00 10.88 ? 146 ASP   A O   1 
ATOM   1222 C  CB  . ASP   A 1 146 ? 12.633 13.724  44.184 1.00 9.81  ? 146 ASP   A CB  1 
ATOM   1223 C  CG  . ASP   A 1 146 ? 12.642 15.110  43.562 1.00 14.82 ? 146 ASP   A CG  1 
ATOM   1224 O  OD1 . ASP   A 1 146 ? 12.750 16.087  44.306 1.00 10.43 ? 146 ASP   A OD1 1 
ATOM   1225 O  OD2 . ASP   A 1 146 ? 12.515 15.187  42.334 1.00 14.59 ? 146 ASP   A OD2 1 
ATOM   1226 N  N   . HIS   A 1 147 ? 13.769 11.321  45.774 1.00 11.33 ? 147 HIS   A N   1 
ATOM   1227 C  CA  . HIS   A 1 147 ? 13.630 9.923   46.231 1.00 10.59 ? 147 HIS   A CA  1 
ATOM   1228 C  C   . HIS   A 1 147 ? 13.790 9.841   47.750 1.00 13.59 ? 147 HIS   A C   1 
ATOM   1229 O  O   . HIS   A 1 147 ? 13.042 9.137   48.392 1.00 11.35 ? 147 HIS   A O   1 
ATOM   1230 C  CB  . HIS   A 1 147 ? 14.681 9.044   45.537 1.00 10.15 ? 147 HIS   A CB  1 
ATOM   1231 C  CG  . HIS   A 1 147 ? 14.397 8.751   44.103 1.00 12.60 ? 147 HIS   A CG  1 
ATOM   1232 N  ND1 . HIS   A 1 147 ? 13.159 8.956   43.539 1.00 11.86 ? 147 HIS   A ND1 1 
ATOM   1233 C  CD2 . HIS   A 1 147 ? 15.181 8.258   43.123 1.00 11.23 ? 147 HIS   A CD2 1 
ATOM   1234 C  CE1 . HIS   A 1 147 ? 13.194 8.608   42.274 1.00 13.66 ? 147 HIS   A CE1 1 
ATOM   1235 N  NE2 . HIS   A 1 147 ? 14.423 8.174   41.995 1.00 13.81 ? 147 HIS   A NE2 1 
ATOM   1236 N  N   . LEU   A 1 148 ? 14.836 10.487  48.256 1.00 11.16 ? 148 LEU   A N   1 
ATOM   1237 C  CA  A LEU   A 1 148 ? 15.086 10.420  49.712 0.58 10.96 ? 148 LEU   A CA  1 
ATOM   1238 C  CA  B LEU   A 1 148 ? 15.071 10.428  49.720 0.42 10.98 ? 148 LEU   A CA  1 
ATOM   1239 C  C   . LEU   A 1 148 ? 13.822 10.872  50.532 1.00 12.98 ? 148 LEU   A C   1 
ATOM   1240 O  O   . LEU   A 1 148 ? 13.367 10.334  51.587 1.00 12.08 ? 148 LEU   A O   1 
ATOM   1241 C  CB  A LEU   A 1 148 ? 16.266 11.330  50.075 0.58 12.89 ? 148 LEU   A CB  1 
ATOM   1242 C  CB  B LEU   A 1 148 ? 16.277 11.312  50.053 0.42 12.92 ? 148 LEU   A CB  1 
ATOM   1243 C  CG  A LEU   A 1 148 ? 17.659 10.732  49.923 0.58 12.66 ? 148 LEU   A CG  1 
ATOM   1244 C  CG  B LEU   A 1 148 ? 17.150 10.836  51.209 0.42 16.48 ? 148 LEU   A CG  1 
ATOM   1245 C  CD1 A LEU   A 1 148 ? 18.714 11.762  50.294 0.58 14.44 ? 148 LEU   A CD1 1 
ATOM   1246 C  CD1 B LEU   A 1 148 ? 17.837 9.527   50.856 0.42 17.10 ? 148 LEU   A CD1 1 
ATOM   1247 C  CD2 A LEU   A 1 148 ? 17.803 9.501   50.799 0.58 17.17 ? 148 LEU   A CD2 1 
ATOM   1248 C  CD2 B LEU   A 1 148 ? 18.179 11.897  51.562 0.42 15.39 ? 148 LEU   A CD2 1 
ATOM   1249 N  N   . THR   A 1 149 ? 13.200 11.915  49.964 1.00 10.17 ? 149 THR   A N   1 
ATOM   1250 C  CA  . THR   A 1 149 ? 12.022 12.450  50.673 1.00 9.66  ? 149 THR   A CA  1 
ATOM   1251 C  C   . THR   A 1 149 ? 10.903 11.392  50.655 1.00 9.72  ? 149 THR   A C   1 
ATOM   1252 O  O   . THR   A 1 149 ? 10.229 11.227  51.654 1.00 11.88 ? 149 THR   A O   1 
ATOM   1253 C  CB  . THR   A 1 149 ? 11.621 13.795  50.041 1.00 9.97  ? 149 THR   A CB  1 
ATOM   1254 O  OG1 . THR   A 1 149 ? 12.624 14.770  50.315 1.00 10.89 ? 149 THR   A OG1 1 
ATOM   1255 C  CG2 . THR   A 1 149 ? 10.271 14.273  50.530 1.00 11.06 ? 149 THR   A CG2 1 
ATOM   1256 N  N   . ASN   A 1 150 ? 10.720 10.770  49.513 1.00 11.08 ? 150 ASN   A N   1 
ATOM   1257 C  CA  . ASN   A 1 150 ? 9.624  9.775   49.407 1.00 9.14  ? 150 ASN   A CA  1 
ATOM   1258 C  C   . ASN   A 1 150 ? 9.971  8.523   50.234 1.00 13.00 ? 150 ASN   A C   1 
ATOM   1259 O  O   . ASN   A 1 150 ? 9.082  7.963   50.849 1.00 10.07 ? 150 ASN   A O   1 
ATOM   1260 C  CB  . ASN   A 1 150 ? 9.340  9.418   47.955 1.00 10.85 ? 150 ASN   A CB  1 
ATOM   1261 C  CG  . ASN   A 1 150 ? 8.455  10.456  47.310 1.00 11.71 ? 150 ASN   A CG  1 
ATOM   1262 O  OD1 . ASN   A 1 150 ? 7.246  10.427  47.492 1.00 10.28 ? 150 ASN   A OD1 1 
ATOM   1263 N  ND2 . ASN   A 1 150 ? 9.061  11.394  46.602 1.00 10.00 ? 150 ASN   A ND2 1 
ATOM   1264 N  N   . ILE   A 1 151 ? 11.234 8.112   50.184 1.00 10.78 ? 151 ILE   A N   1 
ATOM   1265 C  CA  . ILE   A 1 151 ? 11.629 6.944   51.016 1.00 10.60 ? 151 ILE   A CA  1 
ATOM   1266 C  C   . ILE   A 1 151 ? 11.378 7.295   52.486 1.00 12.95 ? 151 ILE   A C   1 
ATOM   1267 O  O   . ILE   A 1 151 ? 10.799 6.470   53.192 1.00 12.71 ? 151 ILE   A O   1 
ATOM   1268 C  CB  . ILE   A 1 151 ? 13.100 6.580   50.738 1.00 10.41 ? 151 ILE   A CB  1 
ATOM   1269 C  CG1 . ILE   A 1 151 ? 13.310 6.055   49.318 1.00 11.15 ? 151 ILE   A CG1 1 
ATOM   1270 C  CG2 . ILE   A 1 151 ? 13.616 5.606   51.787 1.00 13.69 ? 151 ILE   A CG2 1 
ATOM   1271 C  CD1 . ILE   A 1 151 ? 14.735 6.178   48.835 1.00 16.91 ? 151 ILE   A CD1 1 
ATOM   1272 N  N   . GLN   A 1 152 ? 11.797 8.485   52.915 1.00 12.38 ? 152 GLN   A N   1 
ATOM   1273 C  CA  . GLN   A 1 152 ? 11.639 8.920   54.332 1.00 11.46 ? 152 GLN   A CA  1 
ATOM   1274 C  C   . GLN   A 1 152 ? 10.159 8.984   54.810 1.00 16.87 ? 152 GLN   A C   1 
ATOM   1275 O  O   . GLN   A 1 152 ? 9.676  8.554   55.902 1.00 17.17 ? 152 GLN   A O   1 
ATOM   1276 C  CB  . GLN   A 1 152 ? 12.328 10.277  54.525 1.00 16.79 ? 152 GLN   A CB  1 
ATOM   1277 C  CG  . GLN   A 1 152 ? 13.843 10.163  54.604 1.00 19.98 ? 152 GLN   A CG  1 
ATOM   1278 C  CD  . GLN   A 1 152 ? 14.572 11.429  54.220 1.00 20.64 ? 152 GLN   A CD  1 
ATOM   1279 O  OE1 . GLN   A 1 152 ? 15.701 11.666  54.638 1.00 22.76 ? 152 GLN   A OE1 1 
ATOM   1280 N  NE2 . GLN   A 1 152 ? 13.929 12.255  53.412 1.00 24.64 ? 152 GLN   A NE2 1 
ATOM   1281 N  N   . ARG   A 1 153 ? 9.371  9.498   53.875 1.00 13.53 ? 153 ARG   A N   1 
ATOM   1282 C  CA  A ARG   A 1 153 ? 7.904  9.552   54.136 0.52 15.66 ? 153 ARG   A CA  1 
ATOM   1283 C  CA  B ARG   A 1 153 ? 7.906  9.558   54.151 0.48 15.66 ? 153 ARG   A CA  1 
ATOM   1284 C  C   . ARG   A 1 153 ? 7.267  8.158   54.361 1.00 17.06 ? 153 ARG   A C   1 
ATOM   1285 O  O   . ARG   A 1 153 ? 6.250  7.858   55.119 1.00 19.12 ? 153 ARG   A O   1 
ATOM   1286 C  CB  A ARG   A 1 153 ? 7.176  10.257  52.983 0.52 14.98 ? 153 ARG   A CB  1 
ATOM   1287 C  CB  B ARG   A 1 153 ? 7.184  10.371  53.063 0.48 15.11 ? 153 ARG   A CB  1 
ATOM   1288 C  CG  A ARG   A 1 153 ? 5.777  10.731  53.343 0.52 16.63 ? 153 ARG   A CG  1 
ATOM   1289 C  CG  B ARG   A 1 153 ? 6.595  9.581   51.907 0.48 18.09 ? 153 ARG   A CG  1 
ATOM   1290 C  CD  A ARG   A 1 153 ? 5.300  11.880  52.476 0.52 15.80 ? 153 ARG   A CD  1 
ATOM   1291 C  CD  B ARG   A 1 153 ? 5.798  10.501  50.994 0.48 15.93 ? 153 ARG   A CD  1 
ATOM   1292 N  NE  A ARG   A 1 153 ? 5.919  11.857  51.166 0.52 17.47 ? 153 ARG   A NE  1 
ATOM   1293 N  NE  B ARG   A 1 153 ? 5.804  11.904  51.395 0.48 16.07 ? 153 ARG   A NE  1 
ATOM   1294 C  CZ  A ARG   A 1 153 ? 6.394  12.922  50.536 0.52 15.46 ? 153 ARG   A CZ  1 
ATOM   1295 C  CZ  B ARG   A 1 153 ? 6.316  12.898  50.675 0.48 15.14 ? 153 ARG   A CZ  1 
ATOM   1296 N  NH1 A ARG   A 1 153 ? 6.312  14.117  51.096 0.52 19.45 ? 153 ARG   A NH1 1 
ATOM   1297 N  NH1 B ARG   A 1 153 ? 6.875  12.653  49.502 0.48 12.66 ? 153 ARG   A NH1 1 
ATOM   1298 N  NH2 A ARG   A 1 153 ? 6.950  12.783  49.346 0.52 12.15 ? 153 ARG   A NH2 1 
ATOM   1299 N  NH2 B ARG   A 1 153 ? 6.268  14.137  51.133 0.48 19.37 ? 153 ARG   A NH2 1 
ATOM   1300 N  N   . LEU   A 1 154 ? 7.932  7.191   53.739 1.00 17.15 ? 154 LEU   A N   1 
ATOM   1301 C  CA  . LEU   A 1 154 ? 7.348  5.824   53.778 1.00 18.32 ? 154 LEU   A CA  1 
ATOM   1302 C  C   . LEU   A 1 154 ? 7.865  5.055   55.004 1.00 24.15 ? 154 LEU   A C   1 
ATOM   1303 O  O   . LEU   A 1 154 ? 7.271  4.014   55.280 1.00 29.79 ? 154 LEU   A O   1 
ATOM   1304 C  CB  . LEU   A 1 154 ? 7.661  5.085   52.480 1.00 14.74 ? 154 LEU   A CB  1 
ATOM   1305 C  CG  . LEU   A 1 154 ? 6.769  5.434   51.290 1.00 13.45 ? 154 LEU   A CG  1 
ATOM   1306 C  CD1 . LEU   A 1 154 ? 7.398  4.984   49.980 1.00 14.27 ? 154 LEU   A CD1 1 
ATOM   1307 C  CD2 . LEU   A 1 154 ? 5.389  4.818   51.454 1.00 17.62 ? 154 LEU   A CD2 1 
ATOM   1308 N  N   . VAL   A 1 155 ? 8.935  5.499   55.632 1.00 21.36 ? 155 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 155 ? 9.521  4.710   56.749 1.00 31.10 ? 155 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 155 ? 8.468  4.544   57.835 1.00 40.69 ? 155 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 155 ? 8.091  3.389   58.123 1.00 38.05 ? 155 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 155 ? 10.779 5.373   57.311 1.00 28.65 ? 155 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 155 ? 11.269 4.610   58.530 1.00 31.55 ? 155 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 155 ? 11.871 5.440   56.260 1.00 21.93 ? 155 VAL   A CG2 1 
ATOM   1315 N  N   . GLY   A 1 156 ? 8.027  5.653   58.415 1.00 34.17 ? 156 GLY   A N   1 
ATOM   1316 C  CA  . GLY   A 1 156 ? 6.970  5.478   59.422 1.00 51.86 ? 156 GLY   A CA  1 
ATOM   1317 C  C   . GLY   A 1 156 ? 7.286  4.343   60.387 1.00 50.14 ? 156 GLY   A C   1 
ATOM   1318 O  O   . GLY   A 1 156 ? 8.369  4.388   60.944 1.00 57.29 ? 156 GLY   A O   1 
ATOM   1319 N  N   . SER   A 1 157 ? 6.352  3.411   60.592 1.00 60.98 ? 157 SER   A N   1 
ATOM   1320 C  CA  . SER   A 1 157 ? 6.507  2.256   61.527 1.00 68.61 ? 157 SER   A CA  1 
ATOM   1321 C  C   . SER   A 1 157 ? 6.428  0.903   60.792 1.00 68.30 ? 157 SER   A C   1 
ATOM   1322 O  O   . SER   A 1 157 ? 6.478  -0.127  61.467 1.00 55.44 ? 157 SER   A O   1 
ATOM   1323 C  CB  . SER   A 1 157 ? 5.470  2.265   62.618 1.00 66.79 ? 157 SER   A CB  1 
ATOM   1324 O  OG  . SER   A 1 157 ? 4.165  2.232   62.053 1.00 57.05 ? 157 SER   A OG  1 
ATOM   1325 N  N   . GLN   A 1 158 ? 6.313  0.917   59.466 1.00 49.04 ? 158 GLN   A N   1 
ATOM   1326 C  CA  . GLN   A 1 158 ? 6.275  -0.346  58.704 1.00 42.66 ? 158 GLN   A CA  1 
ATOM   1327 C  C   . GLN   A 1 158 ? 7.323  -0.188  57.606 1.00 31.05 ? 158 GLN   A C   1 
ATOM   1328 O  O   . GLN   A 1 158 ? 6.928  0.080   56.467 1.00 26.07 ? 158 GLN   A O   1 
ATOM   1329 C  CB  . GLN   A 1 158 ? 4.858  -0.542  58.181 1.00 38.39 ? 158 GLN   A CB  1 
ATOM   1330 N  N   . ALA   A 1 159 ? 8.598  -0.304  57.969 1.00 26.87 ? 159 ALA   A N   1 
ATOM   1331 C  CA  . ALA   A 1 159 ? 9.686  0.011   57.016 1.00 21.30 ? 159 ALA   A CA  1 
ATOM   1332 C  C   . ALA   A 1 159 ? 9.684  -0.932  55.807 1.00 16.33 ? 159 ALA   A C   1 
ATOM   1333 O  O   . ALA   A 1 159 ? 9.902  -0.460  54.719 1.00 16.20 ? 159 ALA   A O   1 
ATOM   1334 C  CB  . ALA   A 1 159 ? 10.971 -0.035  57.755 1.00 27.39 ? 159 ALA   A CB  1 
ATOM   1335 N  N   . GLY   A 1 160 ? 9.495  -2.223  56.059 1.00 17.90 ? 160 GLY   A N   1 
ATOM   1336 C  CA  . GLY   A 1 160 ? 9.502  -3.182  54.943 1.00 14.30 ? 160 GLY   A CA  1 
ATOM   1337 C  C   . GLY   A 1 160 ? 8.428  -2.863  53.898 1.00 12.65 ? 160 GLY   A C   1 
ATOM   1338 O  O   . GLY   A 1 160 ? 8.711  -2.906  52.726 1.00 13.02 ? 160 GLY   A O   1 
ATOM   1339 N  N   . LEU   A 1 161 ? 7.212  -2.606  54.369 1.00 12.30 ? 161 LEU   A N   1 
ATOM   1340 C  CA  . LEU   A 1 161 ? 6.095  -2.236  53.462 1.00 12.43 ? 161 LEU   A CA  1 
ATOM   1341 C  C   . LEU   A 1 161 ? 6.471  -1.001  52.629 1.00 10.54 ? 161 LEU   A C   1 
ATOM   1342 O  O   . LEU   A 1 161 ? 6.288  -1.010  51.439 1.00 11.58 ? 161 LEU   A O   1 
ATOM   1343 C  CB  . LEU   A 1 161 ? 4.886  -1.913  54.338 1.00 15.00 ? 161 LEU   A CB  1 
ATOM   1344 C  CG  . LEU   A 1 161 ? 3.673  -1.320  53.633 1.00 14.87 ? 161 LEU   A CG  1 
ATOM   1345 C  CD1 . LEU   A 1 161 ? 3.093  -2.316  52.647 1.00 16.97 ? 161 LEU   A CD1 1 
ATOM   1346 C  CD2 . LEU   A 1 161 ? 2.628  -0.918  54.661 1.00 16.77 ? 161 LEU   A CD2 1 
ATOM   1347 N  N   . GLY   A 1 162 ? 6.982  0.013   53.304 1.00 11.59 ? 162 GLY   A N   1 
ATOM   1348 C  CA  . GLY   A 1 162 ? 7.369  1.232   52.578 1.00 10.96 ? 162 GLY   A CA  1 
ATOM   1349 C  C   . GLY   A 1 162 ? 8.510  0.961   51.602 1.00 11.51 ? 162 GLY   A C   1 
ATOM   1350 O  O   . GLY   A 1 162 ? 8.535  1.540   50.547 1.00 14.22 ? 162 GLY   A O   1 
ATOM   1351 N  N   . GLU   A 1 163 ? 9.451  0.131   52.021 1.00 9.86  ? 163 GLU   A N   1 
ATOM   1352 C  CA  . GLU   A 1 163 ? 10.603 -0.105  51.118 1.00 14.18 ? 163 GLU   A CA  1 
ATOM   1353 C  C   . GLU   A 1 163 ? 10.101 -0.812  49.852 1.00 10.26 ? 163 GLU   A C   1 
ATOM   1354 O  O   . GLU   A 1 163 ? 10.521 -0.469  48.763 1.00 11.44 ? 163 GLU   A O   1 
ATOM   1355 C  CB  . GLU   A 1 163 ? 11.702 -0.909  51.818 1.00 15.61 ? 163 GLU   A CB  1 
ATOM   1356 C  CG  . GLU   A 1 163 ? 13.017 -0.924  51.065 1.00 14.96 ? 163 GLU   A CG  1 
ATOM   1357 C  CD  . GLU   A 1 163 ? 14.258 -1.332  51.846 1.00 16.38 ? 163 GLU   A CD  1 
ATOM   1358 O  OE1 . GLU   A 1 163 ? 14.118 -1.794  52.991 1.00 21.17 ? 163 GLU   A OE1 1 
ATOM   1359 O  OE2 . GLU   A 1 163 ? 15.353 -1.206  51.293 1.00 14.62 ? 163 GLU   A OE2 1 
ATOM   1360 N  N   . TYR   A 1 164 ? 9.207  -1.773  50.036 1.00 10.22 ? 164 TYR   A N   1 
ATOM   1361 C  CA  . TYR   A 1 164 ? 8.638  -2.484  48.874 1.00 10.33 ? 164 TYR   A CA  1 
ATOM   1362 C  C   . TYR   A 1 164 ? 7.845  -1.533  47.974 1.00 7.37  ? 164 TYR   A C   1 
ATOM   1363 O  O   . TYR   A 1 164 ? 8.002  -1.543  46.783 1.00 9.66  ? 164 TYR   A O   1 
ATOM   1364 C  CB  . TYR   A 1 164 ? 7.713  -3.588  49.394 1.00 8.26  ? 164 TYR   A CB  1 
ATOM   1365 C  CG  . TYR   A 1 164 ? 6.955  -4.350  48.341 1.00 10.15 ? 164 TYR   A CG  1 
ATOM   1366 C  CD1 . TYR   A 1 164 ? 7.574  -5.340  47.602 1.00 9.62  ? 164 TYR   A CD1 1 
ATOM   1367 C  CD2 . TYR   A 1 164 ? 5.614  -4.108  48.108 1.00 13.57 ? 164 TYR   A CD2 1 
ATOM   1368 C  CE1 . TYR   A 1 164 ? 6.890  -6.053  46.636 1.00 11.14 ? 164 TYR   A CE1 1 
ATOM   1369 C  CE2 . TYR   A 1 164 ? 4.914  -4.817  47.146 1.00 10.05 ? 164 TYR   A CE2 1 
ATOM   1370 C  CZ  . TYR   A 1 164 ? 5.553  -5.797  46.411 1.00 11.06 ? 164 TYR   A CZ  1 
ATOM   1371 O  OH  . TYR   A 1 164 ? 4.887  -6.504  45.458 1.00 10.48 ? 164 TYR   A OH  1 
ATOM   1372 N  N   . LEU   A 1 165 ? 6.990  -0.733  48.610 1.00 9.36  ? 165 LEU   A N   1 
ATOM   1373 C  CA  . LEU   A 1 165 ? 6.113  0.144   47.821 1.00 8.04  ? 165 LEU   A CA  1 
ATOM   1374 C  C   . LEU   A 1 165 ? 6.931  1.147   46.990 1.00 9.36  ? 165 LEU   A C   1 
ATOM   1375 O  O   . LEU   A 1 165 ? 6.572  1.401   45.859 1.00 10.33 ? 165 LEU   A O   1 
ATOM   1376 C  CB  . LEU   A 1 165 ? 5.140  0.869   48.767 1.00 10.44 ? 165 LEU   A CB  1 
ATOM   1377 C  CG  . LEU   A 1 165 ? 4.010  -0.013  49.292 1.00 11.13 ? 165 LEU   A CG  1 
ATOM   1378 C  CD1 . LEU   A 1 165 ? 3.191  0.709   50.347 1.00 13.54 ? 165 LEU   A CD1 1 
ATOM   1379 C  CD2 . LEU   A 1 165 ? 3.125  -0.488  48.153 1.00 13.14 ? 165 LEU   A CD2 1 
ATOM   1380 N  N   . PHE   A 1 166 ? 7.964  1.704   47.610 1.00 11.22 ? 166 PHE   A N   1 
ATOM   1381 C  CA  . PHE   A 1 166 ? 8.806  2.678   46.873 1.00 11.37 ? 166 PHE   A CA  1 
ATOM   1382 C  C   . PHE   A 1 166 ? 9.432  2.009   45.634 1.00 12.83 ? 166 PHE   A C   1 
ATOM   1383 O  O   . PHE   A 1 166 ? 9.442  2.565   44.546 1.00 10.17 ? 166 PHE   A O   1 
ATOM   1384 C  CB  . PHE   A 1 166 ? 9.905  3.246   47.768 1.00 9.71  ? 166 PHE   A CB  1 
ATOM   1385 C  CG  . PHE   A 1 166 ? 10.734 4.288   47.067 1.00 11.39 ? 166 PHE   A CG  1 
ATOM   1386 C  CD1 . PHE   A 1 166 ? 10.230 5.557   46.849 1.00 13.35 ? 166 PHE   A CD1 1 
ATOM   1387 C  CD2 . PHE   A 1 166 ? 11.996 3.990   46.587 1.00 12.59 ? 166 PHE   A CD2 1 
ATOM   1388 C  CE1 . PHE   A 1 166 ? 10.974 6.509   46.175 1.00 11.96 ? 166 PHE   A CE1 1 
ATOM   1389 C  CE2 . PHE   A 1 166 ? 12.741 4.945   45.915 1.00 13.89 ? 166 PHE   A CE2 1 
ATOM   1390 C  CZ  . PHE   A 1 166 ? 12.230 6.203   45.714 1.00 12.16 ? 166 PHE   A CZ  1 
ATOM   1391 N  N   . GLU   A 1 167 ? 9.950  0.807   45.849 1.00 9.16  ? 167 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 167 ? 10.610 0.119   44.722 1.00 9.35  ? 167 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 167 ? 9.573  -0.179  43.631 1.00 11.22 ? 167 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 167 ? 9.895  -0.066  42.470 1.00 11.27 ? 167 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 167 ? 11.283 -1.174  45.219 1.00 8.99  ? 167 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 167 ? 12.007 -1.941  44.132 1.00 9.46  ? 167 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 167 ? 11.151 -3.030  43.511 1.00 10.43 ? 167 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 167 ? 10.216 -3.488  44.185 1.00 12.11 ? 167 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 167 ? 11.409 -3.393  42.363 1.00 10.44 ? 167 GLU   A OE2 1 
ATOM   1400 N  N   . ARG   A 1 168 ? 8.388  -0.595  44.065 1.00 11.81 ? 168 ARG   A N   1 
ATOM   1401 C  CA  . ARG   A 1 168 ? 7.375  -1.014  43.075 1.00 8.06  ? 168 ARG   A CA  1 
ATOM   1402 C  C   . ARG   A 1 168 ? 6.728  0.163   42.358 1.00 8.46  ? 168 ARG   A C   1 
ATOM   1403 O  O   . ARG   A 1 168 ? 6.432  0.027   41.181 1.00 11.75 ? 168 ARG   A O   1 
ATOM   1404 C  CB  . ARG   A 1 168 ? 6.206  -1.691  43.795 1.00 9.76  ? 168 ARG   A CB  1 
ATOM   1405 C  CG  . ARG   A 1 168 ? 6.510  -3.083  44.327 1.00 8.67  ? 168 ARG   A CG  1 
ATOM   1406 C  CD  . ARG   A 1 168 ? 6.581  -4.113  43.217 1.00 11.98 ? 168 ARG   A CD  1 
ATOM   1407 N  NE  . ARG   A 1 168 ? 7.924  -4.281  42.685 1.00 10.43 ? 168 ARG   A NE  1 
ATOM   1408 C  CZ  . ARG   A 1 168 ? 8.224  -5.047  41.647 1.00 11.28 ? 168 ARG   A CZ  1 
ATOM   1409 N  NH1 . ARG   A 1 168 ? 7.272  -5.719  41.026 1.00 14.27 ? 168 ARG   A NH1 1 
ATOM   1410 N  NH2 . ARG   A 1 168 ? 9.473  -5.149  41.232 1.00 13.73 ? 168 ARG   A NH2 1 
ATOM   1411 N  N   . LEU   A 1 169 ? 6.473  1.254   43.083 1.00 11.56 ? 169 LEU   A N   1 
ATOM   1412 C  CA  . LEU   A 1 169 ? 5.642  2.327   42.477 1.00 10.46 ? 169 LEU   A CA  1 
ATOM   1413 C  C   . LEU   A 1 169 ? 6.436  3.555   42.024 1.00 12.90 ? 169 LEU   A C   1 
ATOM   1414 O  O   . LEU   A 1 169 ? 5.892  4.316   41.229 1.00 11.15 ? 169 LEU   A O   1 
ATOM   1415 C  CB  . LEU   A 1 169 ? 4.569  2.735   43.495 1.00 10.71 ? 169 LEU   A CB  1 
ATOM   1416 C  CG  . LEU   A 1 169 ? 3.653  1.605   43.957 1.00 11.92 ? 169 LEU   A CG  1 
ATOM   1417 C  CD1 . LEU   A 1 169 ? 2.616  2.122   44.942 1.00 14.20 ? 169 LEU   A CD1 1 
ATOM   1418 C  CD2 . LEU   A 1 169 ? 2.981  0.950   42.763 1.00 14.83 ? 169 LEU   A CD2 1 
ATOM   1419 N  N   . THR   A 1 170 ? 7.648  3.726   42.533 1.00 10.67 ? 170 THR   A N   1 
ATOM   1420 C  CA  . THR   A 1 170 ? 8.449  4.867   42.034 1.00 10.83 ? 170 THR   A CA  1 
ATOM   1421 C  C   . THR   A 1 170 ? 9.519  4.372   41.057 1.00 12.52 ? 170 THR   A C   1 
ATOM   1422 O  O   . THR   A 1 170 ? 9.664  4.941   39.995 1.00 13.72 ? 170 THR   A O   1 
ATOM   1423 C  CB  . THR   A 1 170 ? 9.078  5.609   43.209 1.00 9.73  ? 170 THR   A CB  1 
ATOM   1424 O  OG1 . THR   A 1 170 ? 8.047  6.286   43.923 1.00 12.11 ? 170 THR   A OG1 1 
ATOM   1425 C  CG2 . THR   A 1 170 ? 10.119 6.613   42.760 1.00 12.84 ? 170 THR   A CG2 1 
ATOM   1426 N  N   . LEU   A 1 171 ? 10.258 3.355   41.485 1.00 13.08 ? 171 LEU   A N   1 
ATOM   1427 C  CA  . LEU   A 1 171 ? 11.429 2.966   40.664 1.00 13.08 ? 171 LEU   A CA  1 
ATOM   1428 C  C   . LEU   A 1 171 ? 11.018 2.106   39.470 1.00 24.24 ? 171 LEU   A C   1 
ATOM   1429 O  O   . LEU   A 1 171 ? 10.069 1.343   39.580 1.00 20.45 ? 171 LEU   A O   1 
ATOM   1430 C  CB  . LEU   A 1 171 ? 12.503 2.311   41.538 1.00 12.56 ? 171 LEU   A CB  1 
ATOM   1431 C  CG  . LEU   A 1 171 ? 13.065 3.211   42.633 1.00 16.53 ? 171 LEU   A CG  1 
ATOM   1432 C  CD1 . LEU   A 1 171 ? 14.084 2.470   43.481 1.00 16.25 ? 171 LEU   A CD1 1 
ATOM   1433 C  CD2 . LEU   A 1 171 ? 13.671 4.473   42.038 1.00 13.20 ? 171 LEU   A CD2 1 
ATOM   1434 N  N   . LYS   A 1 172 ? 11.732 2.255   38.362 1.00 23.70 ? 172 LYS   A N   1 
ATOM   1435 C  CA  . LYS   A 1 172 ? 11.380 1.532   37.121 1.00 35.71 ? 172 LYS   A CA  1 
ATOM   1436 C  C   . LYS   A 1 172 ? 11.850 0.086   37.257 1.00 39.33 ? 172 LYS   A C   1 
ATOM   1437 O  O   . LYS   A 1 172 ? 12.996 -0.127  37.667 1.00 35.14 ? 172 LYS   A O   1 
ATOM   1438 C  CB  . LYS   A 1 172 ? 12.025 2.226   35.919 1.00 29.63 ? 172 LYS   A CB  1 
ATOM   1439 N  N   . HIS   A 1 173 ? 10.968 -0.862  36.963 1.00 37.98 ? 173 HIS   A N   1 
ATOM   1440 C  CA  . HIS   A 1 173 ? 11.331 -2.296  37.049 1.00 36.86 ? 173 HIS   A CA  1 
ATOM   1441 C  C   . HIS   A 1 173 ? 10.592 -3.044  35.943 1.00 46.49 ? 173 HIS   A C   1 
ATOM   1442 O  O   . HIS   A 1 173 ? 9.778  -2.420  35.274 1.00 46.04 ? 173 HIS   A O   1 
ATOM   1443 C  CB  . HIS   A 1 173 ? 11.008 -2.862  38.431 1.00 31.15 ? 173 HIS   A CB  1 
ATOM   1444 C  CG  . HIS   A 1 173 ? 9.610  -2.595  38.857 1.00 31.75 ? 173 HIS   A CG  1 
ATOM   1445 N  ND1 . HIS   A 1 173 ? 8.554  -3.354  38.412 1.00 28.52 ? 173 HIS   A ND1 1 
ATOM   1446 C  CD2 . HIS   A 1 173 ? 9.093  -1.657  39.676 1.00 23.15 ? 173 HIS   A CD2 1 
ATOM   1447 C  CE1 . HIS   A 1 173 ? 7.440  -2.907  38.946 1.00 35.60 ? 173 HIS   A CE1 1 
ATOM   1448 N  NE2 . HIS   A 1 173 ? 7.744  -1.867  39.724 1.00 33.34 ? 173 HIS   A NE2 1 
ATOM   1449 N  N   . ASP   A 1 174 ? 10.902 -4.327  35.752 1.00 51.78 ? 174 ASP   A N   1 
ATOM   1450 C  CA  . ASP   A 1 174 ? 10.279 -5.080  34.629 1.00 41.49 ? 174 ASP   A CA  1 
HETATM 1451 CD CD  . CD    B 2 .   ? 18.708 -7.096  39.467 0.37 14.19 ? 201 CD    A CD  1 
HETATM 1452 CD CD  . CD    C 2 .   ? 48.885 -0.036  41.668 0.42 11.69 ? 202 CD    A CD  1 
HETATM 1453 CD CD  . CD    D 2 .   ? 27.120 27.098  27.109 0.16 24.53 ? 203 CD    A CD  1 
HETATM 1454 CD CD  . CD    E 2 .   ? 29.577 29.547  29.559 0.15 33.66 ? 204 CD    A CD  1 
HETATM 1455 CD CD  . CD    F 2 .   ? 31.241 29.434  30.031 0.22 16.72 ? 205 CD    A CD  1 
HETATM 1456 S  S   . SO4   G 3 .   ? 49.787 28.090  24.635 1.00 29.49 ? 206 SO4   A S   1 
HETATM 1457 O  O1  . SO4   G 3 .   ? 51.016 28.316  25.322 1.00 33.69 ? 206 SO4   A O1  1 
HETATM 1458 O  O2  . SO4   G 3 .   ? 49.947 28.438  23.254 1.00 31.65 ? 206 SO4   A O2  1 
HETATM 1459 O  O3  . SO4   G 3 .   ? 49.429 26.719  24.743 1.00 30.34 ? 206 SO4   A O3  1 
HETATM 1460 O  O4  . SO4   G 3 .   ? 48.763 28.891  25.218 1.00 34.54 ? 206 SO4   A O4  1 
HETATM 1461 N  N1  . A1L54 H 4 .   ? 35.492 -0.035  35.571 0.46 21.28 ? 207 A1L54 A N1  1 
HETATM 1462 C  C4  . A1L54 H 4 .   ? 30.536 -0.110  31.283 0.46 23.23 ? 207 A1L54 A C4  1 
HETATM 1463 C  C5  . A1L54 H 4 .   ? 32.868 -0.074  32.315 0.46 18.28 ? 207 A1L54 A C5  1 
HETATM 1464 C  C6  . A1L54 H 4 .   ? 32.376 -0.084  33.633 0.46 19.33 ? 207 A1L54 A C6  1 
HETATM 1465 C  C7  . A1L54 H 4 .   ? 33.224 -0.070  34.722 0.46 18.83 ? 207 A1L54 A C7  1 
HETATM 1466 C  C8  . A1L54 H 4 .   ? 32.683 -0.092  36.129 0.46 20.69 ? 207 A1L54 A C8  1 
HETATM 1467 C  C10 . A1L54 H 4 .   ? 35.014 -0.063  36.951 0.46 23.36 ? 207 A1L54 A C10 1 
HETATM 1468 C  C13 . A1L54 H 4 .   ? 36.631 -0.010  32.951 0.46 18.92 ? 207 A1L54 A C13 1 
HETATM 1469 C  C15 . A1L54 H 4 .   ? 34.642 -0.048  34.508 0.46 19.44 ? 207 A1L54 A C15 1 
HETATM 1470 C  C1  . A1L54 H 4 .   ? 33.991 -0.053  29.748 0.46 19.90 ? 207 A1L54 A C1  1 
HETATM 1471 C  C11 . A1L54 H 4 .   ? 36.942 0.021   35.417 0.46 24.06 ? 207 A1L54 A C11 1 
HETATM 1472 C  C12 . A1L54 H 4 .   ? 37.341 0.662   34.112 0.46 25.74 ? 207 A1L54 A C12 1 
HETATM 1473 C  C14 . A1L54 H 4 .   ? 35.143 -0.037  33.199 0.46 20.74 ? 207 A1L54 A C14 1 
HETATM 1474 C  C16 . A1L54 H 4 .   ? 34.252 -0.052  32.136 0.46 21.63 ? 207 A1L54 A C16 1 
HETATM 1475 C  C2  . A1L54 H 4 .   ? 32.592 -0.075  29.933 0.46 26.48 ? 207 A1L54 A C2  1 
HETATM 1476 C  C3  . A1L54 H 4 .   ? 32.029 -0.086  31.149 0.46 19.90 ? 207 A1L54 A C3  1 
HETATM 1477 C  C9  . A1L54 H 4 .   ? 33.656 0.581   37.078 0.46 18.97 ? 207 A1L54 A C9  1 
HETATM 1478 F  F1  . A1L54 H 4 .   ? 29.930 -0.543  30.173 0.46 31.88 ? 207 A1L54 A F1  1 
HETATM 1479 F  F2  . A1L54 H 4 .   ? 30.031 1.097   31.548 0.46 21.31 ? 207 A1L54 A F2  1 
HETATM 1480 F  F3  . A1L54 H 4 .   ? 30.134 -0.911  32.272 0.46 34.14 ? 207 A1L54 A F3  1 
HETATM 1481 O  O1  . A1L54 H 4 .   ? 34.570 -0.034  28.689 0.46 26.40 ? 207 A1L54 A O1  1 
HETATM 1482 O  O2  . A1L54 H 4 .   ? 34.785 -0.038  30.866 0.46 26.98 ? 207 A1L54 A O2  1 
HETATM 1483 C  C1  . EDO   I 5 .   ? 18.184 -4.617  52.565 1.00 19.30 ? 208 EDO   A C1  1 
HETATM 1484 O  O1  . EDO   I 5 .   ? 17.504 -5.809  52.873 1.00 28.73 ? 208 EDO   A O1  1 
HETATM 1485 C  C2  . EDO   I 5 .   ? 17.262 -3.538  52.156 1.00 17.61 ? 208 EDO   A C2  1 
HETATM 1486 O  O2  . EDO   I 5 .   ? 16.438 -3.117  53.221 1.00 18.33 ? 208 EDO   A O2  1 
HETATM 1487 C  C1  . EDO   J 5 .   ? 27.384 14.276  35.443 1.00 19.85 ? 209 EDO   A C1  1 
HETATM 1488 O  O1  . EDO   J 5 .   ? 28.139 14.365  36.619 1.00 18.53 ? 209 EDO   A O1  1 
HETATM 1489 C  C2  . EDO   J 5 .   ? 26.222 13.369  35.600 1.00 23.38 ? 209 EDO   A C2  1 
HETATM 1490 O  O2  . EDO   J 5 .   ? 26.618 12.052  35.933 1.00 24.73 ? 209 EDO   A O2  1 
HETATM 1491 C  C1  . EDO   K 5 .   ? 28.778 13.564  30.392 0.79 30.25 ? 210 EDO   A C1  1 
HETATM 1492 O  O1  . EDO   K 5 .   ? 27.863 14.294  29.596 0.79 27.48 ? 210 EDO   A O1  1 
HETATM 1493 C  C2  . EDO   K 5 .   ? 28.208 13.130  31.686 0.79 26.46 ? 210 EDO   A C2  1 
HETATM 1494 O  O2  . EDO   K 5 .   ? 27.143 12.231  31.494 0.79 31.35 ? 210 EDO   A O2  1 
HETATM 1495 CL CL  . CL    L 6 .   ? 50.543 1.816   41.063 1.00 28.59 ? 211 CL    A CL  1 
HETATM 1496 O  O   . HOH   M 7 .   ? 8.184  7.976   57.992 1.00 35.20 ? 301 HOH   A O   1 
HETATM 1497 O  O   . HOH   M 7 .   ? 49.412 15.763  22.223 1.00 22.16 ? 302 HOH   A O   1 
HETATM 1498 O  O   . HOH   M 7 .   ? 29.617 4.786   52.520 1.00 33.50 ? 303 HOH   A O   1 
HETATM 1499 O  O   . HOH   M 7 .   ? 53.089 13.292  24.549 0.96 35.15 ? 304 HOH   A O   1 
HETATM 1500 O  O   . HOH   M 7 .   ? 45.877 20.040  39.190 1.00 17.71 ? 305 HOH   A O   1 
HETATM 1501 O  O   . HOH   M 7 .   ? 36.436 25.535  44.268 1.00 29.70 ? 306 HOH   A O   1 
HETATM 1502 O  O   . HOH   M 7 .   ? 23.331 -10.210 52.002 1.00 30.00 ? 307 HOH   A O   1 
HETATM 1503 O  O   . HOH   M 7 .   ? 27.866 26.184  25.083 1.00 25.15 ? 308 HOH   A O   1 
HETATM 1504 O  O   . HOH   M 7 .   ? 25.584 23.682  33.164 1.00 27.26 ? 309 HOH   A O   1 
HETATM 1505 O  O   . HOH   M 7 .   ? 33.849 23.066  25.252 1.00 18.00 ? 310 HOH   A O   1 
HETATM 1506 O  O   . HOH   M 7 .   ? 8.275  8.800   44.464 1.00 16.90 ? 311 HOH   A O   1 
HETATM 1507 O  O   . HOH   M 7 .   ? 31.645 -2.822  47.228 1.00 10.46 ? 312 HOH   A O   1 
HETATM 1508 O  O   . HOH   M 7 .   ? 12.305 13.967  54.478 1.00 33.14 ? 313 HOH   A O   1 
HETATM 1509 O  O   . HOH   M 7 .   ? 20.386 0.271   58.154 1.00 26.71 ? 314 HOH   A O   1 
HETATM 1510 O  O   . HOH   M 7 .   ? 51.082 15.608  28.623 1.00 24.05 ? 315 HOH   A O   1 
HETATM 1511 O  O   . HOH   M 7 .   ? 30.933 19.972  23.612 1.00 28.83 ? 316 HOH   A O   1 
HETATM 1512 O  O   . HOH   M 7 .   ? 46.594 30.045  24.361 1.00 18.01 ? 317 HOH   A O   1 
HETATM 1513 O  O   . HOH   M 7 .   ? 12.970 15.525  52.784 1.00 24.33 ? 318 HOH   A O   1 
HETATM 1514 O  O   . HOH   M 7 .   ? 45.031 31.342  29.318 1.00 28.53 ? 319 HOH   A O   1 
HETATM 1515 O  O   . HOH   M 7 .   ? 35.729 18.560  23.858 1.00 28.88 ? 320 HOH   A O   1 
HETATM 1516 O  O   . HOH   M 7 .   ? 30.221 21.311  48.687 1.00 18.86 ? 321 HOH   A O   1 
HETATM 1517 O  O   . HOH   M 7 .   ? 38.468 30.627  39.706 1.00 22.12 ? 322 HOH   A O   1 
HETATM 1518 O  O   . HOH   M 7 .   ? 51.788 17.495  31.753 1.00 33.14 ? 323 HOH   A O   1 
HETATM 1519 O  O   . HOH   M 7 .   ? 34.969 2.897   44.344 1.00 19.60 ? 324 HOH   A O   1 
HETATM 1520 O  O   . HOH   M 7 .   ? 40.035 9.351   43.211 1.00 27.40 ? 325 HOH   A O   1 
HETATM 1521 O  O   . HOH   M 7 .   ? 28.162 11.036  34.048 1.00 21.27 ? 326 HOH   A O   1 
HETATM 1522 O  O   . HOH   M 7 .   ? 21.612 -13.993 45.717 1.00 10.39 ? 327 HOH   A O   1 
HETATM 1523 O  O   . HOH   M 7 .   ? 19.081 5.263   56.953 1.00 26.19 ? 328 HOH   A O   1 
HETATM 1524 O  O   . HOH   M 7 .   ? 35.931 -4.897  52.820 1.00 27.53 ? 329 HOH   A O   1 
HETATM 1525 O  O   . HOH   M 7 .   ? 42.632 20.467  19.629 1.00 11.94 ? 330 HOH   A O   1 
HETATM 1526 O  O   . HOH   M 7 .   ? 26.744 21.465  39.035 1.00 10.70 ? 331 HOH   A O   1 
HETATM 1527 O  O   . HOH   M 7 .   ? 49.631 5.613   35.716 1.00 19.00 ? 332 HOH   A O   1 
HETATM 1528 O  O   . HOH   M 7 .   ? 21.276 13.828  35.130 1.00 23.30 ? 333 HOH   A O   1 
HETATM 1529 O  O   . HOH   M 7 .   ? 24.757 2.222   52.631 1.00 29.43 ? 334 HOH   A O   1 
HETATM 1530 O  O   . HOH   M 7 .   ? 16.015 10.027  56.735 1.00 30.00 ? 335 HOH   A O   1 
HETATM 1531 O  O   . HOH   M 7 .   ? 49.975 14.871  25.688 0.64 15.45 ? 336 HOH   A O   1 
HETATM 1532 O  O   . HOH   M 7 .   ? 36.101 4.075   48.072 1.00 28.77 ? 337 HOH   A O   1 
HETATM 1533 O  O   . HOH   M 7 .   ? 44.398 22.260  23.546 1.00 10.91 ? 338 HOH   A O   1 
HETATM 1534 O  O   . HOH   M 7 .   ? 48.932 24.666  26.400 1.00 14.17 ? 339 HOH   A O   1 
HETATM 1535 O  O   . HOH   M 7 .   ? 11.458 8.826   57.894 1.00 30.00 ? 340 HOH   A O   1 
HETATM 1536 O  O   . HOH   M 7 .   ? 51.220 16.056  19.550 1.00 25.47 ? 341 HOH   A O   1 
HETATM 1537 O  O   . HOH   M 7 .   ? 27.689 -5.608  45.820 1.00 15.75 ? 342 HOH   A O   1 
HETATM 1538 O  O   . HOH   M 7 .   ? 35.010 16.553  45.975 1.00 21.39 ? 343 HOH   A O   1 
HETATM 1539 O  O   . HOH   M 7 .   ? 29.712 14.643  49.865 1.00 18.43 ? 344 HOH   A O   1 
HETATM 1540 O  O   . HOH   M 7 .   ? 50.755 22.780  20.148 1.00 22.97 ? 345 HOH   A O   1 
HETATM 1541 O  O   . HOH   M 7 .   ? 46.880 2.076   45.246 1.00 20.41 ? 346 HOH   A O   1 
HETATM 1542 O  O   . HOH   M 7 .   ? 10.389 -6.060  44.964 1.00 10.82 ? 347 HOH   A O   1 
HETATM 1543 O  O   . HOH   M 7 .   ? 32.488 -5.322  47.873 1.00 11.46 ? 348 HOH   A O   1 
HETATM 1544 O  O   . HOH   M 7 .   ? 47.820 4.299   41.121 1.00 20.86 ? 349 HOH   A O   1 
HETATM 1545 O  O   . HOH   M 7 .   ? 30.273 5.410   49.156 1.00 28.51 ? 350 HOH   A O   1 
HETATM 1546 O  O   . HOH   M 7 .   ? 42.524 8.807   35.555 1.00 14.29 ? 351 HOH   A O   1 
HETATM 1547 O  O   . HOH   M 7 .   ? 28.921 7.808   49.709 1.00 16.19 ? 352 HOH   A O   1 
HETATM 1548 O  O   . HOH   M 7 .   ? 40.355 27.211  26.263 1.00 9.60  ? 353 HOH   A O   1 
HETATM 1549 O  O   . HOH   M 7 .   ? 17.244 2.851   56.988 1.00 20.27 ? 354 HOH   A O   1 
HETATM 1550 O  O   . HOH   M 7 .   ? 44.134 25.345  31.220 1.00 11.78 ? 355 HOH   A O   1 
HETATM 1551 O  O   . HOH   M 7 .   ? 36.941 -6.568  42.114 1.00 13.16 ? 356 HOH   A O   1 
HETATM 1552 O  O   . HOH   M 7 .   ? 46.292 10.365  26.220 1.00 13.19 ? 357 HOH   A O   1 
HETATM 1553 O  O   . HOH   M 7 .   ? 3.478  4.146   39.975 1.00 28.93 ? 358 HOH   A O   1 
HETATM 1554 O  O   . HOH   M 7 .   ? 21.518 -12.494 39.684 1.00 15.81 ? 359 HOH   A O   1 
HETATM 1555 O  O   . HOH   M 7 .   ? 36.595 21.481  47.473 1.00 37.93 ? 360 HOH   A O   1 
HETATM 1556 O  O   . HOH   M 7 .   ? 33.844 28.629  38.559 1.00 14.60 ? 361 HOH   A O   1 
HETATM 1557 O  O   . HOH   M 7 .   ? 14.758 1.824   38.413 1.00 21.31 ? 362 HOH   A O   1 
HETATM 1558 O  O   . HOH   M 7 .   ? 23.625 -13.623 47.519 1.00 24.64 ? 363 HOH   A O   1 
HETATM 1559 O  O   . HOH   M 7 .   ? 16.747 -10.722 53.918 1.00 33.12 ? 364 HOH   A O   1 
HETATM 1560 O  O   . HOH   M 7 .   ? 10.983 13.381  40.960 1.00 23.70 ? 365 HOH   A O   1 
HETATM 1561 O  O   . HOH   M 7 .   ? 15.773 16.095  38.421 1.00 17.68 ? 366 HOH   A O   1 
HETATM 1562 O  O   . HOH   M 7 .   ? 12.707 -3.852  54.125 1.00 31.44 ? 367 HOH   A O   1 
HETATM 1563 O  O   . HOH   M 7 .   ? 47.714 6.119   29.884 1.00 10.89 ? 368 HOH   A O   1 
HETATM 1564 O  O   . HOH   M 7 .   ? 19.064 -7.829  53.901 1.00 37.81 ? 369 HOH   A O   1 
HETATM 1565 O  O   . HOH   M 7 .   ? 22.812 5.618   56.389 1.00 25.56 ? 370 HOH   A O   1 
HETATM 1566 O  O   . HOH   M 7 .   ? 11.990 8.792   38.767 1.00 42.41 ? 371 HOH   A O   1 
HETATM 1567 O  O   . HOH   M 7 .   ? 10.510 2.227   54.601 1.00 32.85 ? 372 HOH   A O   1 
HETATM 1568 O  O   . HOH   M 7 .   ? 46.224 13.631  38.273 1.00 26.06 ? 373 HOH   A O   1 
HETATM 1569 O  O   . HOH   M 7 .   ? 17.175 -3.996  55.748 1.00 30.58 ? 374 HOH   A O   1 
HETATM 1570 O  O   . HOH   M 7 .   ? 38.479 18.921  40.675 1.00 13.76 ? 375 HOH   A O   1 
HETATM 1571 O  O   . HOH   M 7 .   ? 35.124 2.483   53.916 1.00 35.54 ? 376 HOH   A O   1 
HETATM 1572 O  O   . HOH   M 7 .   ? 39.819 25.199  42.033 1.00 19.75 ? 377 HOH   A O   1 
HETATM 1573 O  O   . HOH   M 7 .   ? 49.196 13.571  31.901 1.00 16.89 ? 378 HOH   A O   1 
HETATM 1574 O  O   . HOH   M 7 .   ? 12.873 0.909   48.185 1.00 12.80 ? 379 HOH   A O   1 
HETATM 1575 O  O   . HOH   M 7 .   ? 5.102  2.295   55.613 1.00 27.70 ? 380 HOH   A O   1 
HETATM 1576 O  O   . HOH   M 7 .   ? 49.654 17.419  34.133 1.00 17.11 ? 381 HOH   A O   1 
HETATM 1577 O  O   . HOH   M 7 .   ? 13.616 15.306  39.770 1.00 19.37 ? 382 HOH   A O   1 
HETATM 1578 O  O   . HOH   M 7 .   ? 24.272 5.885   54.146 1.00 15.67 ? 383 HOH   A O   1 
HETATM 1579 O  O   . HOH   M 7 .   ? 9.140  -0.897  61.097 1.00 46.29 ? 384 HOH   A O   1 
HETATM 1580 O  O   . HOH   M 7 .   ? 44.558 5.857   42.856 1.00 24.24 ? 385 HOH   A O   1 
HETATM 1581 O  O   . HOH   M 7 .   ? 51.207 17.818  25.856 1.00 31.45 ? 386 HOH   A O   1 
HETATM 1582 O  O   . HOH   M 7 .   ? 42.873 24.844  22.426 1.00 8.92  ? 387 HOH   A O   1 
HETATM 1583 O  O   . HOH   M 7 .   ? 40.792 5.513   43.536 0.88 17.10 ? 388 HOH   A O   1 
HETATM 1584 O  O   . HOH   M 7 .   ? 34.166 -2.144  50.775 1.00 16.98 ? 389 HOH   A O   1 
HETATM 1585 O  O   . HOH   M 7 .   ? 32.173 4.188   47.611 1.00 15.44 ? 390 HOH   A O   1 
HETATM 1586 O  O   . HOH   M 7 .   ? 38.798 21.411  27.718 1.00 11.38 ? 391 HOH   A O   1 
HETATM 1587 O  O   . HOH   M 7 .   ? 33.075 26.763  40.273 1.00 11.12 ? 392 HOH   A O   1 
HETATM 1588 O  O   . HOH   M 7 .   ? 48.034 29.936  27.752 1.00 40.26 ? 393 HOH   A O   1 
HETATM 1589 O  O   . HOH   M 7 .   ? 26.915 -7.538  49.554 1.00 11.38 ? 394 HOH   A O   1 
HETATM 1590 O  O   . HOH   M 7 .   ? 11.689 18.110  39.878 1.00 27.35 ? 395 HOH   A O   1 
HETATM 1591 O  O   . HOH   M 7 .   ? 20.672 -13.378 54.612 1.00 31.47 ? 396 HOH   A O   1 
HETATM 1592 O  O   . HOH   M 7 .   ? 14.549 7.313   39.288 1.00 19.68 ? 397 HOH   A O   1 
HETATM 1593 O  O   . HOH   M 7 .   ? 34.002 8.738   43.518 1.00 16.89 ? 398 HOH   A O   1 
HETATM 1594 O  O   . HOH   M 7 .   ? 38.362 33.134  32.816 1.00 32.65 ? 399 HOH   A O   1 
HETATM 1595 O  O   . HOH   M 7 .   ? 10.609 10.169  44.085 1.00 14.19 ? 400 HOH   A O   1 
HETATM 1596 O  O   . HOH   M 7 .   ? 39.898 16.679  39.904 1.00 16.69 ? 401 HOH   A O   1 
HETATM 1597 O  O   . HOH   M 7 .   ? 38.509 32.916  37.894 1.00 28.11 ? 402 HOH   A O   1 
HETATM 1598 O  O   . HOH   M 7 .   ? 50.786 24.548  32.239 1.00 22.67 ? 403 HOH   A O   1 
HETATM 1599 O  O   . HOH   M 7 .   ? 38.547 -3.600  53.681 1.00 29.06 ? 404 HOH   A O   1 
HETATM 1600 O  O   . HOH   M 7 .   ? 7.306  1.994   39.051 1.00 26.52 ? 405 HOH   A O   1 
HETATM 1601 O  O   . HOH   M 7 .   ? 50.635 20.873  37.051 1.00 33.97 ? 406 HOH   A O   1 
HETATM 1602 O  O   . HOH   M 7 .   ? 12.292 -6.941  43.036 1.00 11.81 ? 407 HOH   A O   1 
HETATM 1603 O  O   . HOH   M 7 .   ? 25.403 19.733  31.972 1.00 23.11 ? 408 HOH   A O   1 
HETATM 1604 O  O   . HOH   M 7 .   ? 23.991 -4.013  54.778 1.00 22.82 ? 409 HOH   A O   1 
HETATM 1605 O  O   . HOH   M 7 .   ? 11.190 -7.802  40.864 1.00 30.96 ? 410 HOH   A O   1 
HETATM 1606 O  O   . HOH   M 7 .   ? 45.058 27.713  30.266 1.00 15.73 ? 411 HOH   A O   1 
HETATM 1607 O  O   . HOH   M 7 .   ? 42.867 32.557  27.328 1.00 17.41 ? 412 HOH   A O   1 
HETATM 1608 O  O   . HOH   M 7 .   ? 35.646 4.822   45.938 1.00 24.40 ? 413 HOH   A O   1 
HETATM 1609 O  O   . HOH   M 7 .   ? 24.451 14.676  51.665 1.00 35.67 ? 414 HOH   A O   1 
HETATM 1610 O  O   . HOH   M 7 .   ? 10.805 3.678   52.254 1.00 25.31 ? 415 HOH   A O   1 
HETATM 1611 O  O   . HOH   M 7 .   ? 33.082 6.319   44.887 1.00 20.02 ? 416 HOH   A O   1 
HETATM 1612 O  O   . HOH   M 7 .   ? 21.013 3.517   59.206 1.00 40.39 ? 417 HOH   A O   1 
HETATM 1613 O  O   . HOH   M 7 .   ? 13.693 0.053   55.269 0.66 24.34 ? 418 HOH   A O   1 
HETATM 1614 O  O   . HOH   M 7 .   ? 34.066 14.396  25.187 0.71 21.14 ? 419 HOH   A O   1 
HETATM 1615 O  O   . HOH   M 7 .   ? 52.797 13.548  28.997 1.00 30.03 ? 420 HOH   A O   1 
HETATM 1616 O  O   . HOH   M 7 .   ? 46.951 30.493  32.516 1.00 38.76 ? 421 HOH   A O   1 
HETATM 1617 O  O   . HOH   M 7 .   ? 29.899 -3.192  54.377 1.00 17.55 ? 422 HOH   A O   1 
HETATM 1618 O  O   . HOH   M 7 .   ? 9.840  12.962  54.047 1.00 23.58 ? 423 HOH   A O   1 
HETATM 1619 O  O   . HOH   M 7 .   ? 43.775 22.640  20.923 1.00 12.49 ? 424 HOH   A O   1 
HETATM 1620 O  O   . HOH   M 7 .   ? 21.695 -15.108 52.098 1.00 26.98 ? 425 HOH   A O   1 
HETATM 1621 O  O   . HOH   M 7 .   ? 21.673 -6.471  37.205 1.00 30.00 ? 426 HOH   A O   1 
HETATM 1622 O  O   . HOH   M 7 .   ? 32.228 25.662  45.203 1.00 20.51 ? 427 HOH   A O   1 
HETATM 1623 O  O   . HOH   M 7 .   ? 6.417  -3.183  57.251 1.00 33.69 ? 428 HOH   A O   1 
HETATM 1624 O  O   . HOH   M 7 .   ? 40.995 11.329  42.133 0.62 27.26 ? 429 HOH   A O   1 
HETATM 1625 O  O   . HOH   M 7 .   ? 14.642 2.033   52.981 0.70 8.74  ? 430 HOH   A O   1 
HETATM 1626 O  O   . HOH   M 7 .   ? 25.083 -2.846  39.073 0.56 13.94 ? 431 HOH   A O   1 
HETATM 1627 O  O   . HOH   M 7 .   ? 37.044 1.265   50.579 1.00 29.11 ? 432 HOH   A O   1 
HETATM 1628 O  O   . HOH   M 7 .   ? 50.009 26.262  20.967 1.00 31.29 ? 433 HOH   A O   1 
HETATM 1629 O  O   . HOH   M 7 .   ? 38.617 18.717  43.559 1.00 22.51 ? 434 HOH   A O   1 
HETATM 1630 O  O   . HOH   M 7 .   ? 47.665 13.090  36.070 1.00 26.51 ? 435 HOH   A O   1 
HETATM 1631 O  O   . HOH   M 7 .   ? 14.040 4.540   38.143 1.00 27.94 ? 436 HOH   A O   1 
HETATM 1632 O  O   . HOH   M 7 .   ? 8.951  -3.891  58.810 1.00 39.88 ? 437 HOH   A O   1 
HETATM 1633 O  O   . HOH   M 7 .   ? 20.514 24.580  33.244 1.00 31.60 ? 438 HOH   A O   1 
HETATM 1634 O  O   . HOH   M 7 .   ? 14.581 -8.704  43.202 0.52 17.36 ? 439 HOH   A O   1 
HETATM 1635 O  O   . HOH   M 7 .   ? 30.719 17.065  48.865 1.00 27.29 ? 440 HOH   A O   1 
HETATM 1636 O  O   . HOH   M 7 .   ? 9.466  12.746  43.579 0.51 15.76 ? 441 HOH   A O   1 
HETATM 1637 O  O   . HOH   M 7 .   ? 43.561 4.349   44.671 1.00 25.79 ? 442 HOH   A O   1 
HETATM 1638 O  O   . HOH   M 7 .   ? 45.160 28.504  39.007 1.00 37.73 ? 443 HOH   A O   1 
HETATM 1639 O  O   . HOH   M 7 .   ? 34.723 -1.881  53.397 1.00 27.48 ? 444 HOH   A O   1 
HETATM 1640 O  O   . HOH   M 7 .   ? 16.847 -7.553  41.246 1.00 32.62 ? 445 HOH   A O   1 
HETATM 1641 O  O   . HOH   M 7 .   ? 41.095 27.487  41.077 1.00 34.54 ? 446 HOH   A O   1 
HETATM 1642 O  O   . HOH   M 7 .   ? 25.568 8.251   53.612 1.00 23.47 ? 447 HOH   A O   1 
HETATM 1643 O  O   . HOH   M 7 .   ? 23.010 11.876  53.065 1.00 41.56 ? 448 HOH   A O   1 
HETATM 1644 O  O   . HOH   M 7 .   ? 46.794 7.885   26.737 1.00 17.16 ? 449 HOH   A O   1 
HETATM 1645 O  O   . HOH   M 7 .   ? 51.154 23.566  27.954 1.00 39.27 ? 450 HOH   A O   1 
HETATM 1646 O  O   . HOH   M 7 .   ? 40.363 20.894  40.316 1.00 26.76 ? 451 HOH   A O   1 
HETATM 1647 O  O   . HOH   M 7 .   ? 52.299 21.671  28.609 1.00 32.41 ? 452 HOH   A O   1 
HETATM 1648 O  O   . HOH   M 7 .   ? 53.447 15.075  17.546 1.00 26.20 ? 453 HOH   A O   1 
HETATM 1649 O  O   . HOH   M 7 .   ? 18.458 -7.749  37.071 1.00 37.27 ? 454 HOH   A O   1 
HETATM 1650 O  O   . HOH   M 7 .   ? 48.847 14.855  34.321 1.00 24.66 ? 455 HOH   A O   1 
HETATM 1651 O  O   . HOH   M 7 .   ? 40.596 26.012  23.741 1.00 10.07 ? 456 HOH   A O   1 
HETATM 1652 O  O   . HOH   M 7 .   ? 47.832 27.417  29.900 1.00 34.36 ? 457 HOH   A O   1 
HETATM 1653 O  O   . HOH   M 7 .   ? 55.981 11.721  23.435 1.00 36.81 ? 458 HOH   A O   1 
HETATM 1654 O  O   . HOH   M 7 .   ? 38.063 31.889  30.729 1.00 24.45 ? 459 HOH   A O   1 
HETATM 1655 O  O   . HOH   M 7 .   ? 43.814 5.559   47.368 1.00 31.21 ? 460 HOH   A O   1 
HETATM 1656 O  O   . HOH   M 7 .   ? 31.101 9.135   48.760 1.00 24.74 ? 461 HOH   A O   1 
HETATM 1657 O  O   . HOH   M 7 .   ? 40.347 29.760  41.689 1.00 35.97 ? 462 HOH   A O   1 
HETATM 1658 O  O   . HOH   M 7 .   ? 34.825 22.416  49.034 1.00 42.87 ? 463 HOH   A O   1 
HETATM 1659 O  O   . HOH   M 7 .   ? 19.713 -3.579  56.036 1.00 34.47 ? 464 HOH   A O   1 
HETATM 1660 O  O   . HOH   M 7 .   ? 24.549 0.499   56.074 1.00 42.89 ? 465 HOH   A O   1 
HETATM 1661 O  O   . HOH   M 7 .   ? 12.850 2.522   50.664 1.00 16.59 ? 466 HOH   A O   1 
HETATM 1662 O  O   . HOH   M 7 .   ? 23.190 -5.058  38.710 1.00 30.00 ? 467 HOH   A O   1 
HETATM 1663 O  O   . HOH   M 7 .   ? 43.758 9.805   40.740 1.00 31.95 ? 468 HOH   A O   1 
HETATM 1664 O  O   . HOH   M 7 .   ? 38.672 26.096  44.076 1.00 34.09 ? 469 HOH   A O   1 
HETATM 1665 O  O   . HOH   M 7 .   ? 14.907 -8.375  54.596 1.00 44.72 ? 470 HOH   A O   1 
HETATM 1666 O  O   . HOH   M 7 .   ? 36.222 6.417   50.716 1.00 42.11 ? 471 HOH   A O   1 
HETATM 1667 O  O   . HOH   M 7 .   ? 32.273 11.317  49.789 1.00 37.26 ? 472 HOH   A O   1 
HETATM 1668 O  O   . HOH   M 7 .   ? 51.976 12.706  31.385 1.00 26.96 ? 473 HOH   A O   1 
HETATM 1669 O  O   . HOH   M 7 .   ? 23.590 -2.580  57.228 1.00 49.83 ? 474 HOH   A O   1 
HETATM 1670 O  O   . HOH   M 7 .   ? 13.682 1.913   54.870 0.74 28.21 ? 475 HOH   A O   1 
HETATM 1671 O  O   . HOH   M 7 .   ? 31.973 13.489  50.760 1.00 30.12 ? 476 HOH   A O   1 
HETATM 1672 O  O   . HOH   M 7 .   ? 17.984 1.183   58.995 1.00 36.61 ? 477 HOH   A O   1 
HETATM 1673 O  O   . HOH   M 7 .   ? 35.635 30.535  39.879 1.00 24.62 ? 478 HOH   A O   1 
HETATM 1674 O  O   . HOH   M 7 .   ? 35.553 30.849  31.013 1.00 29.06 ? 479 HOH   A O   1 
HETATM 1675 O  O   . HOH   M 7 .   ? 28.493 7.655   52.377 1.00 24.63 ? 480 HOH   A O   1 
HETATM 1676 O  O   . HOH   M 7 .   ? 48.690 20.055  39.242 1.00 28.28 ? 481 HOH   A O   1 
HETATM 1677 O  O   . HOH   M 7 .   ? 32.765 6.916   47.528 1.00 32.91 ? 482 HOH   A O   1 
HETATM 1678 O  O   . HOH   M 7 .   ? 24.540 10.573  54.807 1.00 26.67 ? 483 HOH   A O   1 
HETATM 1679 O  O   . HOH   M 7 .   ? 33.717 17.119  48.537 1.00 35.84 ? 484 HOH   A O   1 
HETATM 1680 O  O   . HOH   M 7 .   ? 36.690 14.239  46.168 1.00 37.41 ? 485 HOH   A O   1 
HETATM 1681 O  O   . HOH   M 7 .   ? 27.624 15.323  51.761 1.00 30.96 ? 486 HOH   A O   1 
HETATM 1682 O  O   . HOH   M 7 .   ? 52.494 21.278  13.512 1.00 38.70 ? 487 HOH   A O   1 
HETATM 1683 O  O   . HOH   M 7 .   ? 50.390 15.971  38.547 1.00 42.11 ? 488 HOH   A O   1 
HETATM 1684 O  O   . HOH   M 7 .   ? 28.004 17.929  52.151 1.00 45.63 ? 489 HOH   A O   1 
HETATM 1685 O  O   . HOH   M 7 .   ? 43.716 34.790  28.083 1.00 28.05 ? 490 HOH   A O   1 
HETATM 1686 O  O   . HOH   M 7 .   ? 14.631 3.324   57.575 1.00 28.03 ? 491 HOH   A O   1 
HETATM 1687 O  O   . HOH   M 7 .   ? 43.764 35.705  32.661 1.00 45.93 ? 492 HOH   A O   1 
HETATM 1688 O  O   . HOH   M 7 .   ? 45.913 33.842  29.334 1.00 37.94 ? 493 HOH   A O   1 
HETATM 1689 O  O   . HOH   M 7 .   ? 33.959 14.948  49.993 1.00 35.23 ? 494 HOH   A O   1 
HETATM 1690 O  O   . HOH   M 7 .   ? 38.707 29.433  43.441 1.00 36.80 ? 495 HOH   A O   1 
HETATM 1691 O  O   . HOH   M 7 .   ? 42.882 35.943  30.013 1.00 27.15 ? 496 HOH   A O   1 
HETATM 1692 O  O   . HOH   M 7 .   ? 14.622 5.767   58.804 1.00 33.27 ? 497 HOH   A O   1 
# 
