data_9KP2
# 
_entry.id   9KP2 
# 
_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   9KP2         pdb_00009kp2 10.2210/pdb9kp2/pdb 
WWPDB D_1300053950 ?            ?                   
# 
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                        9KP2 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-22 
_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' 19880.469 1   ? E56F/R59F ? ? 
2 non-polymer syn 'CADMIUM ION'          112.411   9   ? ?         ? ? 
3 non-polymer syn 'CHLORIDE ION'         35.453    1   ? ?         ? ? 
4 non-polymer syn 'SULFATE ION'          96.063    2   ? ?         ? ? 
5 non-polymer syn 1,2-ETHANEDIOL         62.068    4   ? ?         ? ? 
6 non-polymer syn 'Nile Red'             318.369   1   ? ?         ? ? 
7 water       nat water                  18.015    222 ? ?         ? ? 
# 
_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       
;SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRELAFEKFEGAERLLKMQNQRGGRALFQD
LQKPSQDEWGTTLDAMKAAIVLEKSLNQALLDLHALGSAQADPHLCDFLESHFLDEEVKLIKKMGDHLTNIQRLVGSQAG
LGEYLFERLTLKHD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSQIRQNYSTEVEAAVNRLVNLYLRASYTYLSLGFYFDRDDVALEGVCHFFRELAFEKFEGAERLLKMQNQRGGRALFQD
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 'CHLORIDE ION' CL    
4 'SULFATE ION'  SO4   
5 1,2-ETHANEDIOL EDO   
6 'Nile Red'     A1L52 
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  GLU n 
1 54  LEU n 
1 55  ALA n 
1 56  PHE n 
1 57  GLU n 
1 58  LYS n 
1 59  PHE n 
1 60  GLU n 
1 61  GLY n 
1 62  ALA n 
1 63  GLU 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 
A1L52 non-polymer         . 'Nile Red'      '9-(diethylamino)benzo[a]phenoxazin-5-one; Nile Blue A Oxazone' 'C20 H18 N2 O2'  
318.369 
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  GLU 53  53  53  GLU GLU 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  GLU 57  57  57  GLU GLU 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  GLU 60  60  60  GLU GLU 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  GLU 63  63  63  GLU GLU 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        A1L52 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L52 
_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 2 CD    1   206 6    CD    CD  A . 
H 2 CD    1   207 7    CD    CD  A . 
I 2 CD    1   208 8    CD    CD  A . 
J 2 CD    1   209 9    CD    CD  A . 
K 3 CL    1   210 1    CL    CL  A . 
L 4 SO4   1   211 1    SO4   SO4 A . 
M 4 SO4   1   212 2    SO4   SO4 A . 
N 5 EDO   1   213 201  EDO   EDO A . 
O 5 EDO   1   214 501  EDO   EDO A . 
P 5 EDO   1   215 901  EDO   EDO A . 
Q 5 EDO   1   216 1501 EDO   EDO A . 
R 6 A1L52 1   217 1101 A1L52 NRE A . 
S 7 HOH   1   301 278  HOH   HOH A . 
S 7 HOH   2   302 282  HOH   HOH A . 
S 7 HOH   3   303 280  HOH   HOH A . 
S 7 HOH   4   304 283  HOH   HOH A . 
S 7 HOH   5   305 281  HOH   HOH A . 
S 7 HOH   6   306 279  HOH   HOH A . 
S 7 HOH   7   307 182  HOH   HOH A . 
S 7 HOH   8   308 284  HOH   HOH A . 
S 7 HOH   9   309 267  HOH   HOH A . 
S 7 HOH   10  310 261  HOH   HOH A . 
S 7 HOH   11  311 107  HOH   HOH A . 
S 7 HOH   12  312 289  HOH   HOH A . 
S 7 HOH   13  313 252  HOH   HOH A . 
S 7 HOH   14  314 71   HOH   HOH A . 
S 7 HOH   15  315 27   HOH   HOH A . 
S 7 HOH   16  316 259  HOH   HOH A . 
S 7 HOH   17  317 275  HOH   HOH A . 
S 7 HOH   18  318 137  HOH   HOH A . 
S 7 HOH   19  319 125  HOH   HOH A . 
S 7 HOH   20  320 50   HOH   HOH A . 
S 7 HOH   21  321 163  HOH   HOH A . 
S 7 HOH   22  322 130  HOH   HOH A . 
S 7 HOH   23  323 120  HOH   HOH A . 
S 7 HOH   24  324 48   HOH   HOH A . 
S 7 HOH   25  325 44   HOH   HOH A . 
S 7 HOH   26  326 264  HOH   HOH A . 
S 7 HOH   27  327 237  HOH   HOH A . 
S 7 HOH   28  328 51   HOH   HOH A . 
S 7 HOH   29  329 277  HOH   HOH A . 
S 7 HOH   30  330 7    HOH   HOH A . 
S 7 HOH   31  331 156  HOH   HOH A . 
S 7 HOH   32  332 263  HOH   HOH A . 
S 7 HOH   33  333 122  HOH   HOH A . 
S 7 HOH   34  334 218  HOH   HOH A . 
S 7 HOH   35  335 77   HOH   HOH A . 
S 7 HOH   36  336 8    HOH   HOH A . 
S 7 HOH   37  337 101  HOH   HOH A . 
S 7 HOH   38  338 40   HOH   HOH A . 
S 7 HOH   39  339 287  HOH   HOH A . 
S 7 HOH   40  340 201  HOH   HOH A . 
S 7 HOH   41  341 60   HOH   HOH A . 
S 7 HOH   42  342 134  HOH   HOH A . 
S 7 HOH   43  343 260  HOH   HOH A . 
S 7 HOH   44  344 61   HOH   HOH A . 
S 7 HOH   45  345 1    HOH   HOH A . 
S 7 HOH   46  346 6    HOH   HOH A . 
S 7 HOH   47  347 80   HOH   HOH A . 
S 7 HOH   48  348 69   HOH   HOH A . 
S 7 HOH   49  349 192  HOH   HOH A . 
S 7 HOH   50  350 16   HOH   HOH A . 
S 7 HOH   51  351 110  HOH   HOH A . 
S 7 HOH   52  352 9    HOH   HOH A . 
S 7 HOH   53  353 24   HOH   HOH A . 
S 7 HOH   54  354 65   HOH   HOH A . 
S 7 HOH   55  355 17   HOH   HOH A . 
S 7 HOH   56  356 203  HOH   HOH A . 
S 7 HOH   57  357 18   HOH   HOH A . 
S 7 HOH   58  358 274  HOH   HOH A . 
S 7 HOH   59  359 126  HOH   HOH A . 
S 7 HOH   60  360 47   HOH   HOH A . 
S 7 HOH   61  361 91   HOH   HOH A . 
S 7 HOH   62  362 21   HOH   HOH A . 
S 7 HOH   63  363 26   HOH   HOH A . 
S 7 HOH   64  364 173  HOH   HOH A . 
S 7 HOH   65  365 286  HOH   HOH A . 
S 7 HOH   66  366 256  HOH   HOH A . 
S 7 HOH   67  367 119  HOH   HOH A . 
S 7 HOH   68  368 43   HOH   HOH A . 
S 7 HOH   69  369 38   HOH   HOH A . 
S 7 HOH   70  370 176  HOH   HOH A . 
S 7 HOH   71  371 98   HOH   HOH A . 
S 7 HOH   72  372 66   HOH   HOH A . 
S 7 HOH   73  373 22   HOH   HOH A . 
S 7 HOH   74  374 13   HOH   HOH A . 
S 7 HOH   75  375 55   HOH   HOH A . 
S 7 HOH   76  376 82   HOH   HOH A . 
S 7 HOH   77  377 54   HOH   HOH A . 
S 7 HOH   78  378 86   HOH   HOH A . 
S 7 HOH   79  379 46   HOH   HOH A . 
S 7 HOH   80  380 10   HOH   HOH A . 
S 7 HOH   81  381 20   HOH   HOH A . 
S 7 HOH   82  382 223  HOH   HOH A . 
S 7 HOH   83  383 36   HOH   HOH A . 
S 7 HOH   84  384 169  HOH   HOH A . 
S 7 HOH   85  385 32   HOH   HOH A . 
S 7 HOH   86  386 215  HOH   HOH A . 
S 7 HOH   87  387 28   HOH   HOH A . 
S 7 HOH   88  388 56   HOH   HOH A . 
S 7 HOH   89  389 25   HOH   HOH A . 
S 7 HOH   90  390 132  HOH   HOH A . 
S 7 HOH   91  391 104  HOH   HOH A . 
S 7 HOH   92  392 262  HOH   HOH A . 
S 7 HOH   93  393 240  HOH   HOH A . 
S 7 HOH   94  394 19   HOH   HOH A . 
S 7 HOH   95  395 57   HOH   HOH A . 
S 7 HOH   96  396 221  HOH   HOH A . 
S 7 HOH   97  397 127  HOH   HOH A . 
S 7 HOH   98  398 159  HOH   HOH A . 
S 7 HOH   99  399 255  HOH   HOH A . 
S 7 HOH   100 400 4    HOH   HOH A . 
S 7 HOH   101 401 11   HOH   HOH A . 
S 7 HOH   102 402 225  HOH   HOH A . 
S 7 HOH   103 403 59   HOH   HOH A . 
S 7 HOH   104 404 114  HOH   HOH A . 
S 7 HOH   105 405 3    HOH   HOH A . 
S 7 HOH   106 406 231  HOH   HOH A . 
S 7 HOH   107 407 33   HOH   HOH A . 
S 7 HOH   108 408 30   HOH   HOH A . 
S 7 HOH   109 409 243  HOH   HOH A . 
S 7 HOH   110 410 135  HOH   HOH A . 
S 7 HOH   111 411 64   HOH   HOH A . 
S 7 HOH   112 412 273  HOH   HOH A . 
S 7 HOH   113 413 41   HOH   HOH A . 
S 7 HOH   114 414 200  HOH   HOH A . 
S 7 HOH   115 415 108  HOH   HOH A . 
S 7 HOH   116 416 70   HOH   HOH A . 
S 7 HOH   117 417 88   HOH   HOH A . 
S 7 HOH   118 418 2    HOH   HOH A . 
S 7 HOH   119 419 49   HOH   HOH A . 
S 7 HOH   120 420 97   HOH   HOH A . 
S 7 HOH   121 421 99   HOH   HOH A . 
S 7 HOH   122 422 269  HOH   HOH A . 
S 7 HOH   123 423 291  HOH   HOH A . 
S 7 HOH   124 424 39   HOH   HOH A . 
S 7 HOH   125 425 29   HOH   HOH A . 
S 7 HOH   126 426 268  HOH   HOH A . 
S 7 HOH   127 427 78   HOH   HOH A . 
S 7 HOH   128 428 229  HOH   HOH A . 
S 7 HOH   129 429 166  HOH   HOH A . 
S 7 HOH   130 430 189  HOH   HOH A . 
S 7 HOH   131 431 152  HOH   HOH A . 
S 7 HOH   132 432 144  HOH   HOH A . 
S 7 HOH   133 433 207  HOH   HOH A . 
S 7 HOH   134 434 285  HOH   HOH A . 
S 7 HOH   135 435 193  HOH   HOH A . 
S 7 HOH   136 436 145  HOH   HOH A . 
S 7 HOH   137 437 72   HOH   HOH A . 
S 7 HOH   138 438 131  HOH   HOH A . 
S 7 HOH   139 439 15   HOH   HOH A . 
S 7 HOH   140 440 272  HOH   HOH A . 
S 7 HOH   141 441 136  HOH   HOH A . 
S 7 HOH   142 442 116  HOH   HOH A . 
S 7 HOH   143 443 133  HOH   HOH A . 
S 7 HOH   144 444 141  HOH   HOH A . 
S 7 HOH   145 445 233  HOH   HOH A . 
S 7 HOH   146 446 111  HOH   HOH A . 
S 7 HOH   147 447 140  HOH   HOH A . 
S 7 HOH   148 448 213  HOH   HOH A . 
S 7 HOH   149 449 248  HOH   HOH A . 
S 7 HOH   150 450 157  HOH   HOH A . 
S 7 HOH   151 451 244  HOH   HOH A . 
S 7 HOH   152 452 37   HOH   HOH A . 
S 7 HOH   153 453 276  HOH   HOH A . 
S 7 HOH   154 454 172  HOH   HOH A . 
S 7 HOH   155 455 232  HOH   HOH A . 
S 7 HOH   156 456 270  HOH   HOH A . 
S 7 HOH   157 457 139  HOH   HOH A . 
S 7 HOH   158 458 239  HOH   HOH A . 
S 7 HOH   159 459 53   HOH   HOH A . 
S 7 HOH   160 460 63   HOH   HOH A . 
S 7 HOH   161 461 83   HOH   HOH A . 
S 7 HOH   162 462 210  HOH   HOH A . 
S 7 HOH   163 463 241  HOH   HOH A . 
S 7 HOH   164 464 58   HOH   HOH A . 
S 7 HOH   165 465 62   HOH   HOH A . 
S 7 HOH   166 466 146  HOH   HOH A . 
S 7 HOH   167 467 290  HOH   HOH A . 
S 7 HOH   168 468 112  HOH   HOH A . 
S 7 HOH   169 469 187  HOH   HOH A . 
S 7 HOH   170 470 158  HOH   HOH A . 
S 7 HOH   171 471 105  HOH   HOH A . 
S 7 HOH   172 472 150  HOH   HOH A . 
S 7 HOH   173 473 35   HOH   HOH A . 
S 7 HOH   174 474 202  HOH   HOH A . 
S 7 HOH   175 475 118  HOH   HOH A . 
S 7 HOH   176 476 247  HOH   HOH A . 
S 7 HOH   177 477 113  HOH   HOH A . 
S 7 HOH   178 478 230  HOH   HOH A . 
S 7 HOH   179 479 161  HOH   HOH A . 
S 7 HOH   180 480 153  HOH   HOH A . 
S 7 HOH   181 481 271  HOH   HOH A . 
S 7 HOH   182 482 246  HOH   HOH A . 
S 7 HOH   183 483 168  HOH   HOH A . 
S 7 HOH   184 484 214  HOH   HOH A . 
S 7 HOH   185 485 149  HOH   HOH A . 
S 7 HOH   186 486 167  HOH   HOH A . 
S 7 HOH   187 487 76   HOH   HOH A . 
S 7 HOH   188 488 81   HOH   HOH A . 
S 7 HOH   189 489 185  HOH   HOH A . 
S 7 HOH   190 490 265  HOH   HOH A . 
S 7 HOH   191 491 217  HOH   HOH A . 
S 7 HOH   192 492 115  HOH   HOH A . 
S 7 HOH   193 493 89   HOH   HOH A . 
S 7 HOH   194 494 179  HOH   HOH A . 
S 7 HOH   195 495 148  HOH   HOH A . 
S 7 HOH   196 496 234  HOH   HOH A . 
S 7 HOH   197 497 208  HOH   HOH A . 
S 7 HOH   198 498 199  HOH   HOH A . 
S 7 HOH   199 499 170  HOH   HOH A . 
S 7 HOH   200 500 75   HOH   HOH A . 
S 7 HOH   201 501 288  HOH   HOH A . 
S 7 HOH   202 502 236  HOH   HOH A . 
S 7 HOH   203 503 209  HOH   HOH A . 
S 7 HOH   204 504 68   HOH   HOH A . 
S 7 HOH   205 505 143  HOH   HOH A . 
S 7 HOH   206 506 219  HOH   HOH A . 
S 7 HOH   207 507 74   HOH   HOH A . 
S 7 HOH   208 508 188  HOH   HOH A . 
S 7 HOH   209 509 138  HOH   HOH A . 
S 7 HOH   210 510 102  HOH   HOH A . 
S 7 HOH   211 511 220  HOH   HOH A . 
S 7 HOH   212 512 196  HOH   HOH A . 
S 7 HOH   213 513 175  HOH   HOH A . 
S 7 HOH   214 514 180  HOH   HOH A . 
S 7 HOH   215 515 129  HOH   HOH A . 
S 7 HOH   216 516 184  HOH   HOH A . 
S 7 HOH   217 517 216  HOH   HOH A . 
S 7 HOH   218 518 198  HOH   HOH A . 
S 7 HOH   219 519 190  HOH   HOH A . 
S 7 HOH   220 520 183  HOH   HOH A . 
S 7 HOH   221 521 212  HOH   HOH A . 
S 7 HOH   222 522 238  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   ? N   ? A SER 1   N   
2  1 Y 1 A SER 1   ? CA  ? A SER 1   CA  
3  1 Y 1 A SER 1   ? CB  ? A SER 1   CB  
4  1 Y 1 A SER 1   ? OG  ? A SER 1   OG  
5  1 Y 1 A GLN 82  ? CD  ? A GLN 82  CD  
6  1 Y 1 A GLN 82  ? OE1 ? A GLN 82  OE1 
7  1 Y 1 A GLN 82  ? NE2 ? A GLN 82  NE2 
8  1 Y 1 A GLN 158 ? OE1 ? A GLN 158 OE1 
9  1 Y 1 A GLN 158 ? NE2 ? A GLN 158 NE2 
10 1 Y 1 A LYS 172 ? CD  ? A LYS 172 CD  
11 1 Y 1 A LYS 172 ? CE  ? A LYS 172 CE  
12 1 Y 1 A LYS 172 ? NZ  ? A LYS 172 NZ  
13 1 Y 1 A ASP 174 ? C   ? A ASP 174 C   
14 1 Y 1 A ASP 174 ? O   ? A ASP 174 O   
15 1 Y 1 A ASP 174 ? CB  ? A ASP 174 CB  
16 1 Y 1 A ASP 174 ? CG  ? A ASP 174 CG  
17 1 Y 1 A ASP 174 ? OD1 ? A ASP 174 OD1 
18 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                     9KP2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     180.915 
_cell.length_a_esd                 ? 
_cell.length_b                     180.915 
_cell.length_b_esd                 ? 
_cell.length_c                     180.915 
_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                         9KP2 
_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                   9KP2 
_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          60.36 
_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         2021-04-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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                                       9KP2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               18.97 
_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                                     41026 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          28.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.058 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.055 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1995 
_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                               6.8 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.545 
_reflns_shell.pdbx_Rpim_I_all                               0.207 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.911 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.503 
_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                                 9KP2 
_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                            1.50 
_refine.ls_d_res_low                             18.97 
_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                     40952 
_refine.ls_number_reflns_R_free                  2074 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1787 
_refine.ls_R_factor_R_free                       0.1903 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1780 
_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                          1.34 
_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                 18.69 
_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                            0.11 
_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        1381 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.number_atoms_solvent             222 
_refine_hist.number_atoms_total               1663 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        18.97 
# 
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' ? 0.016  ? 1602 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.651  ? 2181 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.596 ? 627  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.102  ? 231  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 284  ? 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' 1.50 1.53  . . 141 2553 100.00 . . . . 0.2096 . . . . . . . . . . . 0.2271 
'X-RAY DIFFRACTION' 1.54 1.57  . . 106 2558 100.00 . . . . 0.2001 . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 1.57 1.62  . . 148 2546 100.00 . . . . 0.1938 . . . . . . . . . . . 0.2305 
'X-RAY DIFFRACTION' 1.62 1.66  . . 134 2536 100.00 . . . . 0.1984 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 1.66 1.72  . . 139 2539 100.00 . . . . 0.1878 . . . . . . . . . . . 0.1858 
'X-RAY DIFFRACTION' 1.72 1.78  . . 124 2571 100.00 . . . . 0.1869 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 1.78 1.85  . . 135 2586 100.00 . . . . 0.1860 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 1.85 1.93  . . 129 2566 100.00 . . . . 0.1845 . . . . . . . . . . . 0.2025 
'X-RAY DIFFRACTION' 1.93 2.03  . . 123 2576 100.00 . . . . 0.1842 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 2.04 2.16  . . 149 2565 100.00 . . . . 0.1717 . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 2.16 2.33  . . 131 2613 100.00 . . . . 0.1635 . . . . . . . . . . . 0.1747 
'X-RAY DIFFRACTION' 2.33 2.56  . . 143 2581 100.00 . . . . 0.1708 . . . . . . . . . . . 0.1972 
'X-RAY DIFFRACTION' 2.56 2.93  . . 150 2617 100.00 . . . . 0.1692 . . . . . . . . . . . 0.1729 
'X-RAY DIFFRACTION' 2.93 3.69  . . 152 2671 100.00 . . . . 0.1694 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 3.69 18.97 . . 170 2800 99.00  . . . . 0.1773 . . . . . . . . . . . 0.1750 
# 
_struct.entry_id                     9KP2 
_struct.title                        'Crystal structure of Horse spleen L-ferritin mutant (E56F/R59F) with Nile Red' 
_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        9KP2 
_struct_keywords.text            '24mer cage, Phenyl Alanine mutant, Nile red, 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 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 6 ? 
S 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              9KP2 
_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 9KP2 PHE A 56 ? UNP P02791 GLU 57 'engineered mutation' 56 1 
1 9KP2 PHE A 59 ? UNP P02791 ARG 60 'engineered mutation' 59 2 
# 
_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)' 126070 ? 
1 MORE         -670   ? 
1 'SSA (A^2)'  134370 ? 
# 
_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,N,O,P,Q,R,S 
# 
_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 ? LEU A 154 ? PHE A 133 LEU A 154 1 ? 22 
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  ? ? ? ? ? ? ? 2.689 ? ? 
metalc2  metalc ? ? A CYS 48  SG  ? ? ? 1_555 B CD . CD ? ? A CYS 48  A CD 201 1_555  ? ? ? ? ? ? ? 2.710 ? ? 
metalc3  metalc ? ? A HIS 49  NE2 A ? ? 1_555 I CD . CD ? ? A HIS 49  A CD 208 1_555  ? ? ? ? ? ? ? 2.434 ? ? 
metalc4  metalc ? ? A HIS 49  NE2 B ? ? 1_555 I CD . CD ? ? A HIS 49  A CD 208 1_555  ? ? ? ? ? ? ? 2.468 ? ? 
metalc5  metalc ? ? A GLU 60  OE1 A ? ? 1_555 H CD . CD ? ? A GLU 60  A CD 207 1_555  ? ? ? ? ? ? ? 2.337 ? ? 
metalc6  metalc ? ? A GLU 63  OE1 B ? ? 1_555 H CD . CD ? ? A GLU 63  A CD 207 1_555  ? ? ? ? ? ? ? 2.294 ? ? 
metalc7  metalc ? ? A ASP 80  OD1 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 1_555  ? ? ? ? ? ? ? 2.331 ? ? 
metalc8  metalc ? ? A ASP 80  OD2 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 1_555  ? ? ? ? ? ? ? 2.329 ? ? 
metalc9  metalc ? ? A ASP 80  OD1 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 72_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc10 metalc ? ? A ASP 80  OD2 ? ? ? 1_555 C CD . CD ? ? A ASP 80  A CD 202 72_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc11 metalc ? ? A GLU 130 OE1 ? ? ? 1_555 E CD . CD ? ? A GLU 130 A CD 204 1_555  ? ? ? ? ? ? ? 2.324 ? ? 
metalc12 metalc ? ? A GLU 130 OE1 ? ? ? 1_555 E CD . CD ? ? A GLU 130 A CD 204 9_555  ? ? ? ? ? ? ? 2.332 ? ? 
metalc13 metalc ? ? A GLU 130 OE1 ? ? ? 1_555 F CD . CD ? ? A GLU 130 A CD 205 1_555  ? ? ? ? ? ? ? 2.494 ? ? 
metalc14 metalc ? ? A GLU 130 OE1 ? ? ? 1_555 F CD . CD ? ? A GLU 130 A CD 205 5_555  ? ? ? ? ? ? ? 2.486 ? ? 
metalc15 metalc ? ? A HIS 132 NE2 ? ? ? 1_555 G CD . CD ? ? A HIS 132 A CD 206 1_555  ? ? ? ? ? ? ? 2.379 ? ? 
# 
_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_555 124.3 ? 
2  NE2 A A HIS 49  ? A HIS 49  ? 1_555 CD ? I CD . ? A CD 208 ? 1_555 NE2 B A HIS 49  ? A HIS 49  ? 1_555 3.4   ? 
3  OE1 A A GLU 60  ? A GLU 60  ? 1_555 CD ? H CD . ? A CD 207 ? 1_555 OE1 B A GLU 63  ? A GLU 63  ? 1_555 111.0 ? 
4  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 55.4  ? 
5  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   ? 
6  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 55.4  ? 
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 55.4  ? 
8  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   ? 
9  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 55.4  ? 
10 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   ? 
11 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                   9KP2 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    VAL 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     42 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -126.05 
_pdbx_validate_torsion.psi             -63.06 
# 
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 A1L52 217 ? R A1L52 . 
5 1 A A1L52 217 ? R A1L52 . 
6 1 A HOH   472 ? S HOH   . 
7 1 A HOH   505 ? S HOH   . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 521 ? 6.41 . 
2 1 O ? A HOH 522 ? 6.57 . 
# 
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 
A1L52 C1   C  N N 1   
A1L52 O2   O  N N 2   
A1L52 C3   C  N N 3   
A1L52 C4   C  N N 4   
A1L52 C5   C  Y N 5   
A1L52 C6   C  Y N 6   
A1L52 C7   C  Y N 7   
A1L52 C8   C  Y N 8   
A1L52 C9   C  N N 9   
A1L52 C12  C  Y N 10  
A1L52 C13  C  Y N 11  
A1L52 C14  C  Y N 12  
A1L52 C15  C  Y N 13  
A1L52 C16  C  N N 14  
A1L52 C17  C  N N 15  
A1L52 C18  C  N N 16  
A1L52 C20  C  Y N 17  
A1L52 C2   C  N N 18  
A1L52 N1   N  N N 19  
A1L52 N2   N  N N 20  
A1L52 C10  C  Y N 21  
A1L52 C11  C  Y N 22  
A1L52 O1   O  N N 23  
A1L52 C19  C  Y N 24  
A1L52 H2   H  N N 25  
A1L52 H3   H  N N 26  
A1L52 H1   H  N N 27  
A1L52 H6   H  N N 28  
A1L52 H7   H  N N 29  
A1L52 H8   H  N N 30  
A1L52 H10  H  N N 31  
A1L52 H9   H  N N 32  
A1L52 H11  H  N N 33  
A1L52 H12  H  N N 34  
A1L52 H14  H  N N 35  
A1L52 H15  H  N N 36  
A1L52 H16  H  N N 37  
A1L52 H17  H  N N 38  
A1L52 H18  H  N N 39  
A1L52 H5   H  N N 40  
A1L52 H4   H  N N 41  
A1L52 H13  H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CD    CD   CD N N 116 
CL    CL   CL N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
EDO   C1   C  N N 132 
EDO   O1   O  N N 133 
EDO   C2   C  N N 134 
EDO   O2   O  N N 135 
EDO   H11  H  N N 136 
EDO   H12  H  N N 137 
EDO   HO1  H  N N 138 
EDO   H21  H  N N 139 
EDO   H22  H  N N 140 
EDO   HO2  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
SO4   S    S  N N 358 
SO4   O1   O  N N 359 
SO4   O2   O  N N 360 
SO4   O3   O  N N 361 
SO4   O4   O  N N 362 
THR   N    N  N N 363 
THR   CA   C  N S 364 
THR   C    C  N N 365 
THR   O    O  N N 366 
THR   CB   C  N R 367 
THR   OG1  O  N N 368 
THR   CG2  C  N N 369 
THR   OXT  O  N N 370 
THR   H    H  N N 371 
THR   H2   H  N N 372 
THR   HA   H  N N 373 
THR   HB   H  N N 374 
THR   HG1  H  N N 375 
THR   HG21 H  N N 376 
THR   HG22 H  N N 377 
THR   HG23 H  N N 378 
THR   HXT  H  N N 379 
TRP   N    N  N N 380 
TRP   CA   C  N S 381 
TRP   C    C  N N 382 
TRP   O    O  N N 383 
TRP   CB   C  N N 384 
TRP   CG   C  Y N 385 
TRP   CD1  C  Y N 386 
TRP   CD2  C  Y N 387 
TRP   NE1  N  Y N 388 
TRP   CE2  C  Y N 389 
TRP   CE3  C  Y N 390 
TRP   CZ2  C  Y N 391 
TRP   CZ3  C  Y N 392 
TRP   CH2  C  Y N 393 
TRP   OXT  O  N N 394 
TRP   H    H  N N 395 
TRP   H2   H  N N 396 
TRP   HA   H  N N 397 
TRP   HB2  H  N N 398 
TRP   HB3  H  N N 399 
TRP   HD1  H  N N 400 
TRP   HE1  H  N N 401 
TRP   HE3  H  N N 402 
TRP   HZ2  H  N N 403 
TRP   HZ3  H  N N 404 
TRP   HH2  H  N N 405 
TRP   HXT  H  N N 406 
TYR   N    N  N N 407 
TYR   CA   C  N S 408 
TYR   C    C  N N 409 
TYR   O    O  N N 410 
TYR   CB   C  N N 411 
TYR   CG   C  Y N 412 
TYR   CD1  C  Y N 413 
TYR   CD2  C  Y N 414 
TYR   CE1  C  Y N 415 
TYR   CE2  C  Y N 416 
TYR   CZ   C  Y N 417 
TYR   OH   O  N N 418 
TYR   OXT  O  N N 419 
TYR   H    H  N N 420 
TYR   H2   H  N N 421 
TYR   HA   H  N N 422 
TYR   HB2  H  N N 423 
TYR   HB3  H  N N 424 
TYR   HD1  H  N N 425 
TYR   HD2  H  N N 426 
TYR   HE1  H  N N 427 
TYR   HE2  H  N N 428 
TYR   HH   H  N N 429 
TYR   HXT  H  N N 430 
VAL   N    N  N N 431 
VAL   CA   C  N S 432 
VAL   C    C  N N 433 
VAL   O    O  N N 434 
VAL   CB   C  N N 435 
VAL   CG1  C  N N 436 
VAL   CG2  C  N N 437 
VAL   OXT  O  N N 438 
VAL   H    H  N N 439 
VAL   H2   H  N N 440 
VAL   HA   H  N N 441 
VAL   HB   H  N N 442 
VAL   HG11 H  N N 443 
VAL   HG12 H  N N 444 
VAL   HG13 H  N N 445 
VAL   HG21 H  N N 446 
VAL   HG22 H  N N 447 
VAL   HG23 H  N N 448 
VAL   HXT  H  N N 449 
# 
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 
A1L52 C1  C2   sing N N 1   
A1L52 C2  N1   sing N N 2   
A1L52 N1  C3   sing N N 3   
A1L52 C3  C4   sing N N 4   
A1L52 N1  C5   sing N N 5   
A1L52 C5  C6   doub Y N 6   
A1L52 C6  C7   sing Y N 7   
A1L52 C7  C8   doub Y N 8   
A1L52 C8  N2   sing N N 9   
A1L52 N2  C9   doub N N 10  
A1L52 C9  C10  sing N N 11  
A1L52 C10 C11  doub Y N 12  
A1L52 C11 C12  sing Y N 13  
A1L52 C12 C13  doub Y N 14  
A1L52 C13 C14  sing Y N 15  
A1L52 C14 C15  doub Y N 16  
A1L52 C15 C16  sing N N 17  
A1L52 C16 O1   doub N N 18  
A1L52 C16 C17  sing N N 19  
A1L52 C17 C18  doub N N 20  
A1L52 C18 O2   sing N N 21  
A1L52 O2  C19  sing N N 22  
A1L52 C19 C20  doub Y N 23  
A1L52 C5  C20  sing Y N 24  
A1L52 C8  C19  sing Y N 25  
A1L52 C9  C18  sing N N 26  
A1L52 C10 C15  sing Y N 27  
A1L52 C1  H2   sing N N 28  
A1L52 C1  H3   sing N N 29  
A1L52 C1  H1   sing N N 30  
A1L52 C3  H6   sing N N 31  
A1L52 C3  H7   sing N N 32  
A1L52 C4  H8   sing N N 33  
A1L52 C4  H10  sing N N 34  
A1L52 C4  H9   sing N N 35  
A1L52 C6  H11  sing N N 36  
A1L52 C7  H12  sing N N 37  
A1L52 C12 H14  sing N N 38  
A1L52 C13 H15  sing N N 39  
A1L52 C14 H16  sing N N 40  
A1L52 C17 H17  sing N N 41  
A1L52 C20 H18  sing N N 42  
A1L52 C2  H5   sing N N 43  
A1L52 C2  H4   sing N N 44  
A1L52 C11 H13  sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
EDO   C1  O1   sing N N 128 
EDO   C1  C2   sing N N 129 
EDO   C1  H11  sing N N 130 
EDO   C1  H12  sing N N 131 
EDO   O1  HO1  sing N N 132 
EDO   C2  O2   sing N N 133 
EDO   C2  H21  sing N N 134 
EDO   C2  H22  sing N N 135 
EDO   O2  HO2  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
SO4   S   O1   doub N N 344 
SO4   S   O2   doub N N 345 
SO4   S   O3   sing N N 346 
SO4   S   O4   sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_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                    9KP2 
_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]   0.005527 
_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]   0.005527 
_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]   0.005527 
_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 
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    C  C   . SER   A 1 1   ? 54.342 18.184  22.062 1.00 49.38 ? 1   SER   A C   1 
ATOM   2    O  O   . SER   A 1 1   ? 54.869 17.918  20.958 1.00 59.40 ? 1   SER   A O   1 
ATOM   3    N  N   . SER   A 1 2   ? 53.134 18.730  22.199 1.00 52.26 ? 2   SER   A N   1 
ATOM   4    C  CA  . SER   A 1 2   ? 51.973 18.359  21.339 1.00 35.30 ? 2   SER   A CA  1 
ATOM   5    C  C   . SER   A 1 2   ? 51.838 19.304  20.138 1.00 39.53 ? 2   SER   A C   1 
ATOM   6    O  O   . SER   A 1 2   ? 52.015 20.529  20.279 1.00 34.64 ? 2   SER   A O   1 
ATOM   7    C  CB  . SER   A 1 2   ? 50.599 18.096  22.063 1.00 29.98 ? 2   SER   A CB  1 
ATOM   8    O  OG  . SER   A 1 2   ? 49.487 18.089  21.194 1.00 25.06 ? 2   SER   A OG  1 
ATOM   9    N  N   . GLN   A 1 3   ? 51.440 18.741  19.020 1.00 29.09 ? 3   GLN   A N   1 
ATOM   10   C  CA  . GLN   A 1 3   ? 51.222 19.529  17.796 1.00 16.68 ? 3   GLN   A CA  1 
ATOM   11   C  C   . GLN   A 1 3   ? 49.867 20.247  17.849 1.00 18.45 ? 3   GLN   A C   1 
ATOM   12   O  O   . GLN   A 1 3   ? 49.651 21.098  17.032 1.00 17.48 ? 3   GLN   A O   1 
ATOM   13   C  CB  . GLN   A 1 3   ? 51.270 18.536  16.640 1.00 17.19 ? 3   GLN   A CB  1 
ATOM   14   C  CG  . GLN   A 1 3   ? 50.128 17.533  16.624 1.00 41.73 ? 3   GLN   A CG  1 
ATOM   15   C  CD  . GLN   A 1 3   ? 50.332 16.406  15.637 1.00 55.69 ? 3   GLN   A CD  1 
ATOM   16   O  OE1 . GLN   A 1 3   ? 49.621 15.404  15.665 1.00 42.60 ? 3   GLN   A OE1 1 
ATOM   17   N  NE2 . GLN   A 1 3   ? 51.305 16.571  14.753 1.00 31.58 ? 3   GLN   A NE2 1 
ATOM   18   N  N   . ILE   A 1 4   ? 48.986 19.869  18.782 1.00 12.07 ? 4   ILE   A N   1 
ATOM   19   C  CA  . ILE   A 1 4   ? 47.628 20.496  18.811 1.00 10.35 ? 4   ILE   A CA  1 
ATOM   20   C  C   . ILE   A 1 4   ? 47.380 21.281  20.112 1.00 9.24  ? 4   ILE   A C   1 
ATOM   21   O  O   . ILE   A 1 4   ? 46.496 22.110  20.134 1.00 11.11 ? 4   ILE   A O   1 
ATOM   22   C  CB  . ILE   A 1 4   ? 46.529 19.419  18.623 1.00 9.22  ? 4   ILE   A CB  1 
ATOM   23   C  CG1 . ILE   A 1 4   ? 46.403 18.510  19.849 1.00 9.48  ? 4   ILE   A CG1 1 
ATOM   24   C  CG2 . ILE   A 1 4   ? 46.755 18.617  17.354 1.00 11.11 ? 4   ILE   A CG2 1 
ATOM   25   C  CD1 . ILE   A 1 4   ? 45.175 17.630  19.836 1.00 12.60 ? 4   ILE   A CD1 1 
ATOM   26   N  N   . ARG   A 1 5   ? 48.137 20.979  21.147 1.00 8.12  ? 5   ARG   A N   1 
ATOM   27   C  CA  . ARG   A 1 5   ? 47.846 21.573  22.469 1.00 8.31  ? 5   ARG   A CA  1 
ATOM   28   C  C   . ARG   A 1 5   ? 47.907 23.097  22.426 1.00 9.63  ? 5   ARG   A C   1 
ATOM   29   O  O   . ARG   A 1 5   ? 48.902 23.625  21.993 1.00 11.46 ? 5   ARG   A O   1 
ATOM   30   C  CB  . ARG   A 1 5   ? 48.828 21.024  23.505 1.00 9.18  ? 5   ARG   A CB  1 
ATOM   31   C  CG  . ARG   A 1 5   ? 48.408 21.265  24.947 1.00 10.45 ? 5   ARG   A CG  1 
ATOM   32   C  CD  . ARG   A 1 5   ? 49.365 20.607  25.918 1.00 15.22 ? 5   ARG   A CD  1 
ATOM   33   N  NE  . ARG   A 1 5   ? 48.933 20.796  27.291 1.00 12.42 ? 5   ARG   A NE  1 
ATOM   34   C  CZ  . ARG   A 1 5   ? 49.130 19.911  28.250 1.00 9.40  ? 5   ARG   A CZ  1 
ATOM   35   N  NH1 . ARG   A 1 5   ? 49.753 18.779  27.979 1.00 10.58 ? 5   ARG   A NH1 1 
ATOM   36   N  NH2 . ARG   A 1 5   ? 48.695 20.157  29.470 1.00 9.56  ? 5   ARG   A NH2 1 
ATOM   37   N  N   . GLN   A 1 6   ? 46.860 23.723  22.951 1.00 7.96  ? 6   GLN   A N   1 
ATOM   38   C  CA  . GLN   A 1 6   ? 46.800 25.193  22.957 1.00 8.34  ? 6   GLN   A CA  1 
ATOM   39   C  C   . GLN   A 1 6   ? 45.900 25.634  24.110 1.00 8.95  ? 6   GLN   A C   1 
ATOM   40   O  O   . GLN   A 1 6   ? 44.779 25.198  24.159 1.00 8.28  ? 6   GLN   A O   1 
ATOM   41   C  CB  . GLN   A 1 6   ? 46.307 25.660  21.585 1.00 7.60  ? 6   GLN   A CB  1 
ATOM   42   C  CG  . GLN   A 1 6   ? 46.403 27.170  21.405 1.00 9.81  ? 6   GLN   A CG  1 
ATOM   43   C  CD  . GLN   A 1 6   ? 45.977 27.612  20.027 1.00 10.85 ? 6   GLN   A CD  1 
ATOM   44   O  OE1 . GLN   A 1 6   ? 45.192 26.952  19.363 1.00 11.13 ? 6   GLN   A OE1 1 
ATOM   45   N  NE2 . GLN   A 1 6   ? 46.492 28.751  19.600 1.00 12.01 ? 6   GLN   A NE2 1 
ATOM   46   N  N   . ASN   A 1 7   ? 46.438 26.492  24.977 1.00 7.84  ? 7   ASN   A N   1 
ATOM   47   C  CA  . ASN   A 1 7   ? 45.662 27.031  26.122 1.00 7.34  ? 7   ASN   A CA  1 
ATOM   48   C  C   . ASN   A 1 7   ? 45.212 25.918  27.059 1.00 8.24  ? 7   ASN   A C   1 
ATOM   49   O  O   . ASN   A 1 7   ? 44.197 26.087  27.691 1.00 8.84  ? 7   ASN   A O   1 
ATOM   50   C  CB  . ASN   A 1 7   ? 44.454 27.842  25.673 1.00 8.15  ? 7   ASN   A CB  1 
ATOM   51   C  CG  . ASN   A 1 7   ? 43.970 28.753  26.776 1.00 8.55  ? 7   ASN   A CG  1 
ATOM   52   O  OD1 . ASN   A 1 7   ? 44.777 29.285  27.525 1.00 10.72 ? 7   ASN   A OD1 1 
ATOM   53   N  ND2 . ASN   A 1 7   ? 42.665 28.904  26.897 1.00 8.57  ? 7   ASN   A ND2 1 
ATOM   54   N  N   . TYR   A 1 8   ? 46.020 24.875  27.153 1.00 7.95  ? 8   TYR   A N   1 
ATOM   55   C  CA  . TYR   A 1 8   ? 45.631 23.711  27.993 1.00 8.38  ? 8   TYR   A CA  1 
ATOM   56   C  C   . TYR   A 1 8   ? 46.707 23.478  29.056 1.00 9.16  ? 8   TYR   A C   1 
ATOM   57   O  O   . TYR   A 1 8   ? 47.739 22.922  28.759 1.00 10.75 ? 8   TYR   A O   1 
ATOM   58   C  CB  . TYR   A 1 8   ? 45.348 22.484  27.114 1.00 8.77  ? 8   TYR   A CB  1 
ATOM   59   C  CG  . TYR   A 1 8   ? 44.615 21.368  27.819 1.00 8.61  ? 8   TYR   A CG  1 
ATOM   60   C  CD1 . TYR   A 1 8   ? 43.338 21.557  28.311 1.00 9.06  ? 8   TYR   A CD1 1 
ATOM   61   C  CD2 . TYR   A 1 8   ? 45.197 20.126  27.998 1.00 8.18  ? 8   TYR   A CD2 1 
ATOM   62   C  CE1 . TYR   A 1 8   ? 42.646 20.543  28.947 1.00 7.69  ? 8   TYR   A CE1 1 
ATOM   63   C  CE2 . TYR   A 1 8   ? 44.520 19.099  28.634 1.00 9.17  ? 8   TYR   A CE2 1 
ATOM   64   C  CZ  . TYR   A 1 8   ? 43.240 19.309  29.115 1.00 8.11  ? 8   TYR   A CZ  1 
ATOM   65   O  OH  . TYR   A 1 8   ? 42.560 18.308  29.746 1.00 9.52  ? 8   TYR   A OH  1 
ATOM   66   N  N   . SER   A 1 9   ? 46.408 23.917  30.261 1.00 8.47  ? 9   SER   A N   1 
ATOM   67   C  CA  . SER   A 1 9   ? 47.430 23.874  31.323 1.00 8.77  ? 9   SER   A CA  1 
ATOM   68   C  C   . SER   A 1 9   ? 47.707 22.469  31.853 1.00 10.00 ? 9   SER   A C   1 
ATOM   69   O  O   . SER   A 1 9   ? 46.865 21.613  31.756 1.00 9.37  ? 9   SER   A O   1 
ATOM   70   C  CB  . SER   A 1 9   ? 47.014 24.785  32.448 1.00 8.97  ? 9   SER   A CB  1 
ATOM   71   O  OG  . SER   A 1 9   ? 45.910 24.253  33.159 1.00 11.19 ? 9   SER   A OG  1 
ATOM   72   N  N   . THR   A 1 10  ? 48.911 22.316  32.381 1.00 10.92 ? 10  THR   A N   1 
ATOM   73   C  CA  . THR   A 1 10  ? 49.270 21.037  33.035 1.00 9.12  ? 10  THR   A CA  1 
ATOM   74   C  C   . THR   A 1 10  ? 48.343 20.812  34.237 1.00 8.22  ? 10  THR   A C   1 
ATOM   75   O  O   . THR   A 1 10  ? 48.053 19.695  34.530 1.00 9.63  ? 10  THR   A O   1 
ATOM   76   C  CB  . THR   A 1 10  ? 50.753 21.075  33.428 1.00 13.42 ? 10  THR   A CB  1 
ATOM   77   O  OG1 . THR   A 1 10  ? 50.961 22.153  34.334 1.00 18.35 ? 10  THR   A OG1 1 
ATOM   78   C  CG2 . THR   A 1 10  ? 51.663 21.218  32.229 1.00 15.09 ? 10  THR   A CG2 1 
ATOM   79   N  N   . GLU   A 1 11  ? 47.939 21.893  34.887 1.00 9.49  ? 11  GLU   A N   1 
ATOM   80   C  CA  . GLU   A 1 11  ? 47.072 21.755  36.083 1.00 8.89  ? 11  GLU   A CA  1 
ATOM   81   C  C   . GLU   A 1 11  ? 45.702 21.188  35.690 1.00 7.79  ? 11  GLU   A C   1 
ATOM   82   O  O   . GLU   A 1 11  ? 45.210 20.319  36.365 1.00 10.08 ? 11  GLU   A O   1 
ATOM   83   C  CB  . GLU   A 1 11  ? 46.899 23.091  36.800 1.00 12.56 ? 11  GLU   A CB  1 
ATOM   84   C  CG  . GLU   A 1 11  ? 48.175 23.607  37.439 1.00 14.50 ? 11  GLU   A CG  1 
ATOM   85   C  CD  . GLU   A 1 11  ? 49.098 24.420  36.546 1.00 18.74 ? 11  GLU   A CD  1 
ATOM   86   O  OE1 . GLU   A 1 11  ? 48.781 24.610  35.368 1.00 13.36 ? 11  GLU   A OE1 1 
ATOM   87   O  OE2 . GLU   A 1 11  ? 50.147 24.846  37.043 1.00 23.26 ? 11  GLU   A OE2 1 
ATOM   88   N  N   . VAL   A 1 12  ? 45.154 21.722  34.613 1.00 8.09  ? 12  VAL   A N   1 
ATOM   89   C  CA  . VAL   A 1 12  ? 43.846 21.195  34.120 1.00 8.00  ? 12  VAL   A CA  1 
ATOM   90   C  C   . VAL   A 1 12  ? 44.018 19.746  33.645 1.00 8.88  ? 12  VAL   A C   1 
ATOM   91   O  O   . VAL   A 1 12  ? 43.197 18.933  33.957 1.00 8.44  ? 12  VAL   A O   1 
ATOM   92   C  CB  . VAL   A 1 12  ? 43.263 22.116  33.031 1.00 8.23  ? 12  VAL   A CB  1 
ATOM   93   C  CG1 . VAL   A 1 12  ? 42.168 21.423  32.240 1.00 9.42  ? 12  VAL   A CG1 1 
ATOM   94   C  CG2 . VAL   A 1 12  ? 42.730 23.403  33.642 1.00 10.05 ? 12  VAL   A CG2 1 
ATOM   95   N  N   . GLU   A 1 13  ? 45.088 19.489  32.907 1.00 7.22  ? 13  GLU   A N   1 
ATOM   96   C  CA  . GLU   A 1 13  ? 45.310 18.120  32.401 1.00 8.25  ? 13  GLU   A CA  1 
ATOM   97   C  C   . GLU   A 1 13  ? 45.307 17.136  33.578 1.00 8.72  ? 13  GLU   A C   1 
ATOM   98   O  O   . GLU   A 1 13  ? 44.695 16.099  33.485 1.00 8.46  ? 13  GLU   A O   1 
ATOM   99   C  CB  . GLU   A 1 13  ? 46.626 18.101  31.624 1.00 8.67  ? 13  GLU   A CB  1 
ATOM   100  C  CG  . GLU   A 1 13  ? 47.061 16.723  31.156 1.00 7.90  ? 13  GLU   A CG  1 
ATOM   101  C  CD  . GLU   A 1 13  ? 48.431 16.721  30.498 1.00 10.65 ? 13  GLU   A CD  1 
ATOM   102  O  OE1 . GLU   A 1 13  ? 49.156 17.708  30.661 1.00 13.03 ? 13  GLU   A OE1 1 
ATOM   103  O  OE2 . GLU   A 1 13  ? 48.769 15.734  29.843 1.00 11.27 ? 13  GLU   A OE2 1 
ATOM   104  N  N   . ALA   A 1 14  ? 46.025 17.486  34.640 1.00 8.62  ? 14  ALA   A N   1 
ATOM   105  C  CA  . ALA   A 1 14  ? 46.112 16.566  35.792 1.00 7.47  ? 14  ALA   A CA  1 
ATOM   106  C  C   . ALA   A 1 14  ? 44.764 16.438  36.502 1.00 7.96  ? 14  ALA   A C   1 
ATOM   107  O  O   . ALA   A 1 14  ? 44.411 15.350  36.919 1.00 8.70  ? 14  ALA   A O   1 
ATOM   108  C  CB  . ALA   A 1 14  ? 47.180 17.066  36.746 1.00 8.87  ? 14  ALA   A CB  1 
ATOM   109  N  N   . ALA   A 1 15  ? 44.070 17.560  36.645 1.00 8.09  ? 15  ALA   A N   1 
ATOM   110  C  CA  . ALA   A 1 15  ? 42.771 17.522  37.345 1.00 8.58  ? 15  ALA   A CA  1 
ATOM   111  C  C   . ALA   A 1 15  ? 41.764 16.701  36.534 1.00 8.19  ? 15  ALA   A C   1 
ATOM   112  O  O   . ALA   A 1 15  ? 40.897 16.113  37.130 1.00 9.35  ? 15  ALA   A O   1 
ATOM   113  C  CB  . ALA   A 1 15  ? 42.281 18.929  37.541 1.00 10.23 ? 15  ALA   A CB  1 
ATOM   114  N  N   . VAL   A 1 16  ? 41.877 16.793  35.204 1.00 7.73  ? 16  VAL   A N   1 
ATOM   115  C  CA  . VAL   A 1 16  ? 40.992 15.965  34.327 1.00 6.97  ? 16  VAL   A CA  1 
ATOM   116  C  C   . VAL   A 1 16  ? 41.260 14.474  34.611 1.00 8.63  ? 16  VAL   A C   1 
ATOM   117  O  O   . VAL   A 1 16  ? 40.329 13.719  34.733 1.00 8.40  ? 16  VAL   A O   1 
ATOM   118  C  CB  . VAL   A 1 16  ? 41.182 16.333  32.838 1.00 7.22  ? 16  VAL   A CB  1 
ATOM   119  C  CG1 . VAL   A 1 16  ? 40.517 15.324  31.911 1.00 8.34  ? 16  VAL   A CG1 1 
ATOM   120  C  CG2 . VAL   A 1 16  ? 40.612 17.721  32.578 1.00 9.55  ? 16  VAL   A CG2 1 
ATOM   121  N  N   . ASN   A 1 17  ? 42.526 14.100  34.684 1.00 8.08  ? 17  ASN   A N   1 
ATOM   122  C  CA  . ASN   A 1 17  ? 42.865 12.683  34.947 1.00 7.87  ? 17  ASN   A CA  1 
ATOM   123  C  C   . ASN   A 1 17  ? 42.324 12.275  36.321 1.00 9.01  ? 17  ASN   A C   1 
ATOM   124  O  O   . ASN   A 1 17  ? 41.845 11.181  36.473 1.00 8.79  ? 17  ASN   A O   1 
ATOM   125  C  CB  . ASN   A 1 17  ? 44.375 12.502  34.837 1.00 7.53  ? 17  ASN   A CB  1 
ATOM   126  C  CG  . ASN   A 1 17  ? 44.853 12.384  33.410 1.00 9.55  ? 17  ASN   A CG  1 
ATOM   127  O  OD1 . ASN   A 1 17  ? 44.119 11.914  32.555 1.00 8.26  ? 17  ASN   A OD1 1 
ATOM   128  N  ND2 . ASN   A 1 17  ? 46.070 12.827  33.159 1.00 9.40  ? 17  ASN   A ND2 1 
ATOM   129  N  N   . ARG   A 1 18  ? 42.430 13.187  37.276 1.00 8.28  ? 18  ARG   A N   1 
ATOM   130  C  CA  A ARG   A 1 18  ? 41.906 12.896  38.642 0.43 10.25 ? 18  ARG   A CA  1 
ATOM   131  C  CA  B ARG   A 1 18  ? 41.899 12.888  38.645 0.57 10.21 ? 18  ARG   A CA  1 
ATOM   132  C  C   . ARG   A 1 18  ? 40.363 12.686  38.641 1.00 9.95  ? 18  ARG   A C   1 
ATOM   133  O  O   . ARG   A 1 18  ? 39.717 11.770  39.230 1.00 10.25 ? 18  ARG   A O   1 
ATOM   134  C  CB  A ARG   A 1 18  ? 42.333 14.026  39.589 0.43 10.46 ? 18  ARG   A CB  1 
ATOM   135  C  CB  B ARG   A 1 18  ? 42.322 14.002  39.610 0.57 10.39 ? 18  ARG   A CB  1 
ATOM   136  C  CG  A ARG   A 1 18  ? 41.629 14.007  40.936 0.43 13.66 ? 18  ARG   A CG  1 
ATOM   137  C  CG  B ARG   A 1 18  ? 43.739 13.822  40.132 0.57 15.21 ? 18  ARG   A CG  1 
ATOM   138  C  CD  A ARG   A 1 18  ? 42.084 15.110  41.874 0.43 18.30 ? 18  ARG   A CD  1 
ATOM   139  C  CD  B ARG   A 1 18  ? 44.053 14.695  41.327 0.57 17.04 ? 18  ARG   A CD  1 
ATOM   140  N  NE  A ARG   A 1 18  ? 41.007 15.588  42.728 0.43 28.49 ? 18  ARG   A NE  1 
ATOM   141  N  NE  B ARG   A 1 18  ? 43.941 16.094  40.956 0.57 20.90 ? 18  ARG   A NE  1 
ATOM   142  C  CZ  A ARG   A 1 18  ? 40.312 14.830  43.569 0.43 21.43 ? 18  ARG   A CZ  1 
ATOM   143  C  CZ  B ARG   A 1 18  ? 44.923 16.810  40.429 0.57 13.69 ? 18  ARG   A CZ  1 
ATOM   144  N  NH1 A ARG   A 1 18  ? 40.577 13.540  43.678 0.43 23.64 ? 18  ARG   A NH1 1 
ATOM   145  N  NH1 B ARG   A 1 18  ? 46.111 16.265  40.230 0.57 19.40 ? 18  ARG   A NH1 1 
ATOM   146  N  NH2 A ARG   A 1 18  ? 39.353 15.368  44.302 0.43 26.94 ? 18  ARG   A NH2 1 
ATOM   147  N  NH2 B ARG   A 1 18  ? 44.713 18.073  40.119 0.57 13.31 ? 18  ARG   A NH2 1 
ATOM   148  N  N   . LEU   A 1 19  ? 39.748 13.515  37.807 1.00 8.59  ? 19  LEU   A N   1 
ATOM   149  C  CA  . LEU   A 1 19  ? 38.262 13.437  37.690 1.00 8.07  ? 19  LEU   A CA  1 
ATOM   150  C  C   . LEU   A 1 19  ? 37.837 12.142  36.980 1.00 8.40  ? 19  LEU   A C   1 
ATOM   151  O  O   . LEU   A 1 19  ? 36.789 11.620  37.291 1.00 8.66  ? 19  LEU   A O   1 
ATOM   152  C  CB  . LEU   A 1 19  ? 37.763 14.679  36.949 1.00 10.42 ? 19  LEU   A CB  1 
ATOM   153  C  CG  . LEU   A 1 19  ? 36.256 14.916  36.981 1.00 10.38 ? 19  LEU   A CG  1 
ATOM   154  C  CD1 . LEU   A 1 19  ? 35.757 15.022  38.411 1.00 10.70 ? 19  LEU   A CD1 1 
ATOM   155  C  CD2 . LEU   A 1 19  ? 35.886 16.159  36.190 1.00 12.60 ? 19  LEU   A CD2 1 
ATOM   156  N  N   . VAL   A 1 20  ? 38.630 11.699  36.018 1.00 8.00  ? 20  VAL   A N   1 
ATOM   157  C  CA  . VAL   A 1 20  ? 38.341 10.383  35.389 1.00 8.41  ? 20  VAL   A CA  1 
ATOM   158  C  C   . VAL   A 1 20  ? 38.368 9.299   36.471 1.00 8.98  ? 20  VAL   A C   1 
ATOM   159  O  O   . VAL   A 1 20  ? 37.507 8.464   36.481 1.00 8.64  ? 20  VAL   A O   1 
ATOM   160  C  CB  . VAL   A 1 20  ? 39.368 10.098  34.281 1.00 7.98  ? 20  VAL   A CB  1 
ATOM   161  C  CG1 . VAL   A 1 20  ? 39.301 8.651   33.817 1.00 8.80  ? 20  VAL   A CG1 1 
ATOM   162  C  CG2 . VAL   A 1 20  ? 39.159 11.033  33.098 1.00 8.88  ? 20  VAL   A CG2 1 
ATOM   163  N  N   . ASN   A 1 21  ? 39.371 9.360   37.325 1.00 8.38  ? 21  ASN   A N   1 
ATOM   164  C  CA  . ASN   A 1 21  ? 39.435 8.399   38.445 1.00 6.32  ? 21  ASN   A CA  1 
ATOM   165  C  C   . ASN   A 1 21  ? 38.163 8.524   39.311 1.00 8.23  ? 21  ASN   A C   1 
ATOM   166  O  O   . ASN   A 1 21  ? 37.668 7.476   39.661 1.00 8.64  ? 21  ASN   A O   1 
ATOM   167  C  CB  . ASN   A 1 21  ? 40.749 8.559   39.215 1.00 9.53  ? 21  ASN   A CB  1 
ATOM   168  C  CG  . ASN   A 1 21  ? 41.042 7.416   40.165 1.00 9.61  ? 21  ASN   A CG  1 
ATOM   169  O  OD1 . ASN   A 1 21  ? 40.668 7.461   41.328 1.00 15.15 ? 21  ASN   A OD1 1 
ATOM   170  N  ND2 . ASN   A 1 21  ? 41.724 6.397   39.677 1.00 9.54  ? 21  ASN   A ND2 1 
ATOM   171  N  N   A LEU   A 1 22  ? 37.758 9.664   39.603 0.77 8.94  ? 22  LEU   A N   1 
ATOM   172  N  N   B LEU   A 1 22  ? 37.725 9.734   39.624 0.23 8.91  ? 22  LEU   A N   1 
ATOM   173  C  CA  A LEU   A 1 22  ? 36.577 9.798   40.495 0.77 8.69  ? 22  LEU   A CA  1 
ATOM   174  C  CA  B LEU   A 1 22  ? 36.555 9.856   40.523 0.23 8.81  ? 22  LEU   A CA  1 
ATOM   175  C  C   A LEU   A 1 22  ? 35.319 9.225   39.833 0.77 8.62  ? 22  LEU   A C   1 
ATOM   176  C  C   B LEU   A 1 22  ? 35.331 9.238   39.839 0.23 8.67  ? 22  LEU   A C   1 
ATOM   177  O  O   A LEU   A 1 22  ? 34.530 8.628   40.502 0.77 9.29  ? 22  LEU   A O   1 
ATOM   178  O  O   B LEU   A 1 22  ? 34.525 8.607   40.530 0.23 9.31  ? 22  LEU   A O   1 
ATOM   179  C  CB  A LEU   A 1 22  ? 36.379 11.288  40.833 0.77 9.81  ? 22  LEU   A CB  1 
ATOM   180  C  CB  B LEU   A 1 22  ? 36.338 11.340  40.832 0.23 9.77  ? 22  LEU   A CB  1 
ATOM   181  C  CG  A LEU   A 1 22  ? 37.440 11.909  41.734 0.77 9.38  ? 22  LEU   A CG  1 
ATOM   182  C  CG  B LEU   A 1 22  ? 36.077 11.662  42.301 0.23 12.76 ? 22  LEU   A CG  1 
ATOM   183  C  CD1 A LEU   A 1 22  ? 37.170 13.390  41.921 0.77 12.38 ? 22  LEU   A CD1 1 
ATOM   184  C  CD1 B LEU   A 1 22  ? 37.270 11.270  43.157 0.23 14.73 ? 22  LEU   A CD1 1 
ATOM   185  C  CD2 A LEU   A 1 22  ? 37.468 11.220  43.088 0.77 14.92 ? 22  LEU   A CD2 1 
ATOM   186  C  CD2 B LEU   A 1 22  ? 35.752 13.137  42.477 0.23 12.18 ? 22  LEU   A CD2 1 
ATOM   187  N  N   . TYR   A 1 23  ? 35.176 9.485   38.537 1.00 8.22  ? 23  TYR   A N   1 
ATOM   188  C  CA  . TYR   A 1 23  ? 34.003 8.950   37.803 1.00 7.14  ? 23  TYR   A CA  1 
ATOM   189  C  C   . TYR   A 1 23  ? 34.048 7.414   37.679 1.00 9.41  ? 23  TYR   A C   1 
ATOM   190  O  O   . TYR   A 1 23  ? 33.033 6.808   37.797 1.00 9.27  ? 23  TYR   A O   1 
ATOM   191  C  CB  . TYR   A 1 23  ? 33.879 9.644   36.434 1.00 7.90  ? 23  TYR   A CB  1 
ATOM   192  C  CG  . TYR   A 1 23  ? 32.997 10.865  36.508 1.00 8.17  ? 23  TYR   A CG  1 
ATOM   193  C  CD1 . TYR   A 1 23  ? 33.455 12.044  37.071 1.00 9.78  ? 23  TYR   A CD1 1 
ATOM   194  C  CD2 . TYR   A 1 23  ? 31.682 10.823  36.080 1.00 9.58  ? 23  TYR   A CD2 1 
ATOM   195  C  CE1 . TYR   A 1 23  ? 32.640 13.156  37.183 1.00 10.39 ? 23  TYR   A CE1 1 
ATOM   196  C  CE2 . TYR   A 1 23  ? 30.850 11.922  36.192 1.00 9.80  ? 23  TYR   A CE2 1 
ATOM   197  C  CZ  . TYR   A 1 23  ? 31.330 13.093  36.746 1.00 9.19  ? 23  TYR   A CZ  1 
ATOM   198  O  OH  . TYR   A 1 23  ? 30.514 14.180  36.859 1.00 12.57 ? 23  TYR   A OH  1 
ATOM   199  N  N   . LEU   A 1 24  ? 35.234 6.866   37.430 1.00 9.26  ? 24  LEU   A N   1 
ATOM   200  C  CA  . LEU   A 1 24  ? 35.324 5.387   37.369 1.00 8.71  ? 24  LEU   A CA  1 
ATOM   201  C  C   . LEU   A 1 24  ? 35.114 4.774   38.761 1.00 9.96  ? 24  LEU   A C   1 
ATOM   202  O  O   . LEU   A 1 24  ? 34.555 3.718   38.840 1.00 8.85  ? 24  LEU   A O   1 
ATOM   203  C  CB  . LEU   A 1 24  ? 36.685 4.992   36.783 1.00 7.82  ? 24  LEU   A CB  1 
ATOM   204  C  CG  . LEU   A 1 24  ? 36.884 5.335   35.306 1.00 8.92  ? 24  LEU   A CG  1 
ATOM   205  C  CD1 . LEU   A 1 24  ? 38.298 4.992   34.859 1.00 10.93 ? 24  LEU   A CD1 1 
ATOM   206  C  CD2 . LEU   A 1 24  ? 35.866 4.618   34.434 1.00 10.54 ? 24  LEU   A CD2 1 
ATOM   207  N  N   . ARG   A 1 25  ? 35.562 5.467   39.798 1.00 7.60  ? 25  ARG   A N   1 
ATOM   208  C  CA  . ARG   A 1 25  ? 35.306 4.952   41.172 1.00 7.89  ? 25  ARG   A CA  1 
ATOM   209  C  C   . ARG   A 1 25  ? 33.804 4.975   41.452 1.00 8.86  ? 25  ARG   A C   1 
ATOM   210  O  O   . ARG   A 1 25  ? 33.295 4.075   42.065 1.00 8.98  ? 25  ARG   A O   1 
ATOM   211  C  CB  . ARG   A 1 25  ? 35.997 5.868   42.186 1.00 11.05 ? 25  ARG   A CB  1 
ATOM   212  C  CG  . ARG   A 1 25  ? 37.458 5.583   42.499 1.00 18.01 ? 25  ARG   A CG  1 
ATOM   213  C  CD  . ARG   A 1 25  ? 38.008 6.671   43.416 1.00 19.51 ? 25  ARG   A CD  1 
ATOM   214  N  NE  . ARG   A 1 25  ? 37.317 6.808   44.694 1.00 23.48 ? 25  ARG   A NE  1 
ATOM   215  C  CZ  . ARG   A 1 25  ? 37.550 7.766   45.592 1.00 36.52 ? 25  ARG   A CZ  1 
ATOM   216  N  NH1 . ARG   A 1 25  ? 38.464 8.687   45.358 1.00 21.39 ? 25  ARG   A NH1 1 
ATOM   217  N  NH2 . ARG   A 1 25  ? 36.875 7.788   46.730 1.00 30.63 ? 25  ARG   A NH2 1 
ATOM   218  N  N   . ALA   A 1 26  ? 33.174 6.041   40.978 1.00 9.62  ? 26  ALA   A N   1 
ATOM   219  C  CA  . ALA   A 1 26  ? 31.715 6.188   41.176 1.00 7.51  ? 26  ALA   A CA  1 
ATOM   220  C  C   . ALA   A 1 26  ? 30.988 5.090   40.392 1.00 7.90  ? 26  ALA   A C   1 
ATOM   221  O  O   . ALA   A 1 26  ? 30.070 4.502   40.907 1.00 8.43  ? 26  ALA   A O   1 
ATOM   222  C  CB  . ALA   A 1 26  ? 31.258 7.573   40.755 1.00 8.00  ? 26  ALA   A CB  1 
ATOM   223  N  N   . SER   A 1 27  ? 31.439 4.854   39.175 1.00 8.60  ? 27  SER   A N   1 
ATOM   224  C  CA  . SER   A 1 27  ? 30.840 3.760   38.368 1.00 7.41  ? 27  SER   A CA  1 
ATOM   225  C  C   . SER   A 1 27  ? 30.955 2.435   39.144 1.00 9.11  ? 27  SER   A C   1 
ATOM   226  O  O   . SER   A 1 27  ? 30.015 1.664   39.171 1.00 8.04  ? 27  SER   A O   1 
ATOM   227  C  CB  . SER   A 1 27  ? 31.548 3.695   37.023 1.00 8.91  ? 27  SER   A CB  1 
ATOM   228  O  OG  . SER   A 1 27  ? 31.007 2.692   36.190 1.00 9.96  ? 27  SER   A OG  1 
ATOM   229  N  N   . TYR   A 1 28  ? 32.121 2.213   39.727 1.00 7.78  ? 28  TYR   A N   1 
ATOM   230  C  CA  . TYR   A 1 28  ? 32.365 0.947   40.462 1.00 6.09  ? 28  TYR   A CA  1 
ATOM   231  C  C   . TYR   A 1 28  ? 31.455 0.869   41.688 1.00 8.41  ? 28  TYR   A C   1 
ATOM   232  O  O   . TYR   A 1 28  ? 30.961 -0.177  41.989 1.00 7.69  ? 28  TYR   A O   1 
ATOM   233  C  CB  . TYR   A 1 28  ? 33.844 0.970   40.880 1.00 6.62  ? 28  TYR   A CB  1 
ATOM   234  C  CG  . TYR   A 1 28  ? 34.499 -0.347  41.204 1.00 7.10  ? 28  TYR   A CG  1 
ATOM   235  C  CD1 . TYR   A 1 28  ? 33.918 -1.552  40.859 1.00 9.96  ? 28  TYR   A CD1 1 
ATOM   236  C  CD2 . TYR   A 1 28  ? 35.721 -0.374  41.848 1.00 9.68  ? 28  TYR   A CD2 1 
ATOM   237  C  CE1 . TYR   A 1 28  ? 34.538 -2.754  41.151 1.00 9.51  ? 28  TYR   A CE1 1 
ATOM   238  C  CE2 . TYR   A 1 28  ? 36.352 -1.566  42.149 1.00 10.46 ? 28  TYR   A CE2 1 
ATOM   239  C  CZ  . TYR   A 1 28  ? 35.758 -2.762  41.796 1.00 8.78  ? 28  TYR   A CZ  1 
ATOM   240  O  OH  . TYR   A 1 28  ? 36.368 -3.945  42.090 1.00 9.52  ? 28  TYR   A OH  1 
ATOM   241  N  N   . THR   A 1 29  ? 31.294 2.008   42.368 1.00 7.81  ? 29  THR   A N   1 
ATOM   242  C  CA  . THR   A 1 29  ? 30.393 2.056   43.542 1.00 8.26  ? 29  THR   A CA  1 
ATOM   243  C  C   . THR   A 1 29  ? 28.970 1.689   43.109 1.00 6.71  ? 29  THR   A C   1 
ATOM   244  O  O   . THR   A 1 29  ? 28.307 0.925   43.782 1.00 7.77  ? 29  THR   A O   1 
ATOM   245  C  CB  . THR   A 1 29  ? 30.484 3.448   44.181 1.00 8.46  ? 29  THR   A CB  1 
ATOM   246  O  OG1 . THR   A 1 29  ? 31.793 3.636   44.723 1.00 9.45  ? 29  THR   A OG1 1 
ATOM   247  C  CG2 . THR   A 1 29  ? 29.452 3.641   45.269 1.00 8.83  ? 29  THR   A CG2 1 
ATOM   248  N  N   . TYR   A 1 30  ? 28.577 2.234   41.970 1.00 6.97  ? 30  TYR   A N   1 
ATOM   249  C  CA  . TYR   A 1 30  ? 27.198 1.954   41.501 1.00 7.83  ? 30  TYR   A CA  1 
ATOM   250  C  C   . TYR   A 1 30  ? 27.054 0.498   41.028 1.00 7.14  ? 30  TYR   A C   1 
ATOM   251  O  O   . TYR   A 1 30  ? 25.970 -0.045  41.160 1.00 7.88  ? 30  TYR   A O   1 
ATOM   252  C  CB  . TYR   A 1 30  ? 26.780 2.980   40.440 1.00 7.23  ? 30  TYR   A CB  1 
ATOM   253  C  CG  . TYR   A 1 30  ? 26.440 4.322   41.025 1.00 7.07  ? 30  TYR   A CG  1 
ATOM   254  C  CD1 . TYR   A 1 30  ? 25.549 4.424   42.074 1.00 9.71  ? 30  TYR   A CD1 1 
ATOM   255  C  CD2 . TYR   A 1 30  ? 27.027 5.480   40.553 1.00 7.78  ? 30  TYR   A CD2 1 
ATOM   256  C  CE1 . TYR   A 1 30  ? 25.241 5.645   42.643 1.00 9.96  ? 30  TYR   A CE1 1 
ATOM   257  C  CE2 . TYR   A 1 30  ? 26.724 6.712   41.104 1.00 9.01  ? 30  TYR   A CE2 1 
ATOM   258  C  CZ  . TYR   A 1 30  ? 25.826 6.794   42.151 1.00 9.24  ? 30  TYR   A CZ  1 
ATOM   259  O  OH  . TYR   A 1 30  ? 25.511 7.992   42.714 1.00 11.23 ? 30  TYR   A OH  1 
ATOM   260  N  N   . LEU   A 1 31  ? 28.128 -0.061  40.466 1.00 7.40  ? 31  LEU   A N   1 
ATOM   261  C  CA  . LEU   A 1 31  ? 28.073 -1.501  40.102 1.00 7.48  ? 31  LEU   A CA  1 
ATOM   262  C  C   . LEU   A 1 31  ? 27.844 -2.321  41.383 1.00 6.75  ? 31  LEU   A C   1 
ATOM   263  O  O   . LEU   A 1 31  ? 27.053 -3.256  41.342 1.00 9.04  ? 31  LEU   A O   1 
ATOM   264  C  CB  . LEU   A 1 31  ? 29.410 -1.873  39.447 1.00 7.82  ? 31  LEU   A CB  1 
ATOM   265  C  CG  . LEU   A 1 31  ? 29.553 -3.316  38.978 1.00 9.60  ? 31  LEU   A CG  1 
ATOM   266  C  CD1 . LEU   A 1 31  ? 28.641 -3.576  37.794 1.00 10.53 ? 31  LEU   A CD1 1 
ATOM   267  C  CD2 . LEU   A 1 31  ? 31.001 -3.605  38.610 1.00 9.60  ? 31  LEU   A CD2 1 
ATOM   268  N  N   . SER   A 1 32  ? 28.547 -1.976  42.456 1.00 8.10  ? 32  SER   A N   1 
ATOM   269  C  CA  . SER   A 1 32  ? 28.386 -2.709  43.737 1.00 6.70  ? 32  SER   A CA  1 
ATOM   270  C  C   . SER   A 1 32  ? 26.981 -2.505  44.318 1.00 7.93  ? 32  SER   A C   1 
ATOM   271  O  O   . SER   A 1 32  ? 26.377 -3.456  44.761 1.00 9.15  ? 32  SER   A O   1 
ATOM   272  C  CB  . SER   A 1 32  ? 29.438 -2.261  44.730 1.00 7.53  ? 32  SER   A CB  1 
ATOM   273  O  OG  . SER   A 1 32  ? 29.236 -2.865  45.991 1.00 8.38  ? 32  SER   A OG  1 
ATOM   274  N  N   . LEU   A 1 33  ? 26.507 -1.269  44.279 1.00 8.05  ? 33  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 33  ? 25.134 -1.017  44.770 1.00 7.94  ? 33  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 33  ? 24.117 -1.831  43.966 1.00 7.52  ? 33  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 33  ? 23.232 -2.426  44.551 1.00 8.51  ? 33  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 33  ? 24.886 0.481   44.587 1.00 8.12  ? 33  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 33  ? 25.311 1.343   45.773 1.00 8.69  ? 33  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 33  ? 25.495 2.794   45.344 1.00 8.93  ? 33  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 33  ? 24.279 1.247   46.884 1.00 9.95  ? 33  LEU   A CD2 1 
ATOM   282  N  N   . GLY   A 1 34  ? 24.276 -1.810  42.658 1.00 7.92  ? 34  GLY   A N   1 
ATOM   283  C  CA  . GLY   A 1 34  ? 23.282 -2.501  41.819 1.00 7.43  ? 34  GLY   A CA  1 
ATOM   284  C  C   . GLY   A 1 34  ? 23.211 -3.994  42.121 1.00 7.85  ? 34  GLY   A C   1 
ATOM   285  O  O   . GLY   A 1 34  ? 22.142 -4.516  42.267 1.00 9.78  ? 34  GLY   A O   1 
ATOM   286  N  N   . PHE   A 1 35  ? 24.363 -4.621  42.244 1.00 7.74  ? 35  PHE   A N   1 
ATOM   287  C  CA  . PHE   A 1 35  ? 24.379 -6.089  42.451 1.00 8.28  ? 35  PHE   A CA  1 
ATOM   288  C  C   . PHE   A 1 35  ? 23.965 -6.447  43.887 1.00 9.88  ? 35  PHE   A C   1 
ATOM   289  O  O   . PHE   A 1 35  ? 23.457 -7.524  44.075 1.00 10.32 ? 35  PHE   A O   1 
ATOM   290  C  CB  . PHE   A 1 35  ? 25.722 -6.663  41.964 1.00 8.58  ? 35  PHE   A CB  1 
ATOM   291  C  CG  . PHE   A 1 35  ? 25.674 -6.920  40.483 1.00 7.63  ? 35  PHE   A CG  1 
ATOM   292  C  CD1 . PHE   A 1 35  ? 24.990 -8.016  39.989 1.00 10.14 ? 35  PHE   A CD1 1 
ATOM   293  C  CD2 . PHE   A 1 35  ? 26.217 -6.019  39.586 1.00 10.30 ? 35  PHE   A CD2 1 
ATOM   294  C  CE1 . PHE   A 1 35  ? 24.894 -8.230  38.627 1.00 11.30 ? 35  PHE   A CE1 1 
ATOM   295  C  CE2 . PHE   A 1 35  ? 26.118 -6.232  38.222 1.00 14.40 ? 35  PHE   A CE2 1 
ATOM   296  C  CZ  . PHE   A 1 35  ? 25.457 -7.338  37.745 1.00 12.07 ? 35  PHE   A CZ  1 
ATOM   297  N  N   . TYR   A 1 36  ? 24.201 -5.527  44.825 1.00 8.52  ? 36  TYR   A N   1 
ATOM   298  C  CA  . TYR   A 1 36  ? 23.718 -5.762  46.200 1.00 7.00  ? 36  TYR   A CA  1 
ATOM   299  C  C   . TYR   A 1 36  ? 22.189 -5.903  46.170 1.00 7.52  ? 36  TYR   A C   1 
ATOM   300  O  O   . TYR   A 1 36  ? 21.658 -6.774  46.832 1.00 7.57  ? 36  TYR   A O   1 
ATOM   301  C  CB  . TYR   A 1 36  ? 24.193 -4.622  47.115 1.00 6.70  ? 36  TYR   A CB  1 
ATOM   302  C  CG  . TYR   A 1 36  ? 23.492 -4.565  48.445 1.00 7.35  ? 36  TYR   A CG  1 
ATOM   303  C  CD1 . TYR   A 1 36  ? 23.857 -5.415  49.472 1.00 8.09  ? 36  TYR   A CD1 1 
ATOM   304  C  CD2 . TYR   A 1 36  ? 22.456 -3.676  48.667 1.00 9.68  ? 36  TYR   A CD2 1 
ATOM   305  C  CE1 . TYR   A 1 36  ? 23.213 -5.384  50.695 1.00 7.53  ? 36  TYR   A CE1 1 
ATOM   306  C  CE2 . TYR   A 1 36  ? 21.801 -3.632  49.884 1.00 8.23  ? 36  TYR   A CE2 1 
ATOM   307  C  CZ  . TYR   A 1 36  ? 22.184 -4.486  50.901 1.00 9.12  ? 36  TYR   A CZ  1 
ATOM   308  O  OH  . TYR   A 1 36  ? 21.537 -4.442  52.097 1.00 10.31 ? 36  TYR   A OH  1 
ATOM   309  N  N   . PHE   A 1 37  ? 21.531 -5.052  45.383 1.00 8.50  ? 37  PHE   A N   1 
ATOM   310  C  CA  . PHE   A 1 37  ? 20.037 -5.042  45.368 1.00 6.94  ? 37  PHE   A CA  1 
ATOM   311  C  C   . PHE   A 1 37  ? 19.503 -6.212  44.536 1.00 7.81  ? 37  PHE   A C   1 
ATOM   312  O  O   . PHE   A 1 37  ? 18.322 -6.469  44.606 1.00 9.42  ? 37  PHE   A O   1 
ATOM   313  C  CB  . PHE   A 1 37  ? 19.491 -3.652  44.986 1.00 8.15  ? 37  PHE   A CB  1 
ATOM   314  C  CG  . PHE   A 1 37  ? 19.562 -2.663  46.121 1.00 7.10  ? 37  PHE   A CG  1 
ATOM   315  C  CD1 . PHE   A 1 37  ? 18.616 -2.674  47.131 1.00 7.81  ? 37  PHE   A CD1 1 
ATOM   316  C  CD2 . PHE   A 1 37  ? 20.597 -1.748  46.205 1.00 7.68  ? 37  PHE   A CD2 1 
ATOM   317  C  CE1 . PHE   A 1 37  ? 18.695 -1.784  48.188 1.00 6.55  ? 37  PHE   A CE1 1 
ATOM   318  C  CE2 . PHE   A 1 37  ? 20.671 -0.856  47.259 1.00 7.71  ? 37  PHE   A CE2 1 
ATOM   319  C  CZ  . PHE   A 1 37  ? 19.724 -0.878  48.254 1.00 7.14  ? 37  PHE   A CZ  1 
ATOM   320  N  N   . ASP   A 1 38  ? 20.379 -6.890  43.812 1.00 7.15  ? 38  ASP   A N   1 
ATOM   321  C  CA  . ASP   A 1 38  ? 20.007 -8.103  43.052 1.00 9.04  ? 38  ASP   A CA  1 
ATOM   322  C  C   . ASP   A 1 38  ? 20.202 -9.371  43.904 1.00 8.41  ? 38  ASP   A C   1 
ATOM   323  O  O   . ASP   A 1 38  ? 19.824 -10.438 43.462 1.00 9.86  ? 38  ASP   A O   1 
ATOM   324  C  CB  . ASP   A 1 38  ? 20.849 -8.143  41.784 1.00 8.68  ? 38  ASP   A CB  1 
ATOM   325  C  CG  . ASP   A 1 38  ? 20.596 -9.377  40.938 1.00 10.52 ? 38  ASP   A CG  1 
ATOM   326  O  OD1 . ASP   A 1 38  ? 19.443 -9.576  40.538 1.00 15.09 ? 38  ASP   A OD1 1 
ATOM   327  O  OD2 . ASP   A 1 38  ? 21.550 -10.125 40.714 1.00 10.80 ? 38  ASP   A OD2 1 
ATOM   328  N  N   . ARG   A 1 39  ? 20.764 -9.230  45.101 1.00 6.65  ? 39  ARG   A N   1 
ATOM   329  C  CA  . ARG   A 1 39  ? 20.912 -10.390 46.005 1.00 7.34  ? 39  ARG   A CA  1 
ATOM   330  C  C   . ARG   A 1 39  ? 19.530 -10.975 46.296 1.00 9.25  ? 39  ARG   A C   1 
ATOM   331  O  O   . ARG   A 1 39  ? 18.588 -10.230 46.460 1.00 8.57  ? 39  ARG   A O   1 
ATOM   332  C  CB  . ARG   A 1 39  ? 21.529 -9.986  47.343 1.00 7.31  ? 39  ARG   A CB  1 
ATOM   333  C  CG  . ARG   A 1 39  ? 23.021 -9.709  47.264 1.00 8.99  ? 39  ARG   A CG  1 
ATOM   334  C  CD  . ARG   A 1 39  ? 23.569 -9.082  48.527 1.00 9.07  ? 39  ARG   A CD  1 
ATOM   335  N  NE  . ARG   A 1 39  ? 23.154 -9.724  49.763 1.00 15.27 ? 39  ARG   A NE  1 
ATOM   336  C  CZ  . ARG   A 1 39  ? 23.758 -9.550  50.934 1.00 15.63 ? 39  ARG   A CZ  1 
ATOM   337  N  NH1 . ARG   A 1 39  ? 24.819 -8.769  51.028 1.00 18.05 ? 39  ARG   A NH1 1 
ATOM   338  N  NH2 . ARG   A 1 39  ? 23.310 -10.171 52.009 1.00 19.19 ? 39  ARG   A NH2 1 
ATOM   339  N  N   . ASP   A 1 40  ? 19.486 -12.297 46.426 1.00 7.97  ? 40  ASP   A N   1 
ATOM   340  C  CA  . ASP   A 1 40  ? 18.192 -12.961 46.690 1.00 7.91  ? 40  ASP   A CA  1 
ATOM   341  C  C   . ASP   A 1 40  ? 17.630 -12.518 48.040 1.00 7.38  ? 40  ASP   A C   1 
ATOM   342  O  O   . ASP   A 1 40  ? 16.424 -12.589 48.205 1.00 9.38  ? 40  ASP   A O   1 
ATOM   343  C  CB  . ASP   A 1 40  ? 18.293 -14.491 46.629 1.00 8.23  ? 40  ASP   A CB  1 
ATOM   344  C  CG  . ASP   A 1 40  ? 19.031 -15.111 47.801 1.00 9.95  ? 40  ASP   A CG  1 
ATOM   345  O  OD1 . ASP   A 1 40  ? 20.254 -15.270 47.701 1.00 11.06 ? 40  ASP   A OD1 1 
ATOM   346  O  OD2 . ASP   A 1 40  ? 18.369 -15.443 48.788 1.00 10.51 ? 40  ASP   A OD2 1 
ATOM   347  N  N   . ASP   A 1 41  ? 18.485 -12.053 48.938 1.00 7.86  ? 41  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 41  ? 18.025 -11.650 50.295 1.00 9.66  ? 41  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 41  ? 17.811 -10.134 50.381 1.00 8.30  ? 41  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 41  ? 17.650 -9.642  51.488 1.00 9.48  ? 41  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 41  ? 18.970 -12.175 51.370 1.00 7.95  ? 41  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 41  ? 20.405 -11.711 51.251 1.00 10.66 ? 41  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 41  ? 20.717 -11.024 50.279 1.00 11.70 ? 41  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 41  ? 21.185 -12.062 52.138 1.00 14.11 ? 41  ASP   A OD2 1 
ATOM   355  N  N   . VAL   A 1 42  ? 17.822 -9.459  49.240 1.00 7.74  ? 42  VAL   A N   1 
ATOM   356  C  CA  . VAL   A 1 42  ? 17.544 -7.990  49.180 1.00 8.44  ? 42  VAL   A CA  1 
ATOM   357  C  C   . VAL   A 1 42  ? 16.419 -7.863  48.156 1.00 8.84  ? 42  VAL   A C   1 
ATOM   358  O  O   . VAL   A 1 42  ? 15.353 -7.425  48.527 1.00 8.77  ? 42  VAL   A O   1 
ATOM   359  C  CB  . VAL   A 1 42  ? 18.828 -7.238  48.774 1.00 7.73  ? 42  VAL   A CB  1 
ATOM   360  C  CG1 . VAL   A 1 42  ? 18.558 -5.748  48.602 1.00 9.47  ? 42  VAL   A CG1 1 
ATOM   361  C  CG2 . VAL   A 1 42  ? 19.956 -7.449  49.774 1.00 8.34  ? 42  VAL   A CG2 1 
ATOM   362  N  N   . ALA   A 1 43  ? 16.682 -8.238  46.913 1.00 7.96  ? 43  ALA   A N   1 
ATOM   363  C  CA  . ALA   A 1 43  ? 15.623 -8.444  45.903 1.00 6.57  ? 43  ALA   A CA  1 
ATOM   364  C  C   . ALA   A 1 43  ? 14.738 -7.217  45.667 1.00 7.66  ? 43  ALA   A C   1 
ATOM   365  O  O   . ALA   A 1 43  ? 13.552 -7.314  45.805 1.00 8.79  ? 43  ALA   A O   1 
ATOM   366  C  CB  . ALA   A 1 43  ? 14.831 -9.691  46.279 1.00 9.09  ? 43  ALA   A CB  1 
ATOM   367  N  N   . LEU   A 1 44  ? 15.359 -6.131  45.246 1.00 8.03  ? 44  LEU   A N   1 
ATOM   368  C  CA  . LEU   A 1 44  ? 14.614 -4.892  44.912 1.00 7.78  ? 44  LEU   A CA  1 
ATOM   369  C  C   . LEU   A 1 44  ? 15.063 -4.528  43.500 1.00 6.90  ? 44  LEU   A C   1 
ATOM   370  O  O   . LEU   A 1 44  ? 16.003 -3.774  43.347 1.00 8.05  ? 44  LEU   A O   1 
ATOM   371  C  CB  . LEU   A 1 44  ? 14.921 -3.806  45.952 1.00 7.13  ? 44  LEU   A CB  1 
ATOM   372  C  CG  . LEU   A 1 44  ? 14.316 -4.092  47.323 1.00 7.33  ? 44  LEU   A CG  1 
ATOM   373  C  CD1 . LEU   A 1 44  ? 14.934 -3.211  48.392 1.00 8.98  ? 44  LEU   A CD1 1 
ATOM   374  C  CD2 . LEU   A 1 44  ? 12.804 -3.930  47.285 1.00 10.01 ? 44  LEU   A CD2 1 
ATOM   375  N  N   . GLU   A 1 45  ? 14.390 -5.096  42.510 1.00 7.74  ? 45  GLU   A N   1 
ATOM   376  C  CA  . GLU   A 1 45  ? 14.818 -4.935  41.098 1.00 8.40  ? 45  GLU   A CA  1 
ATOM   377  C  C   . GLU   A 1 45  ? 14.917 -3.470  40.671 1.00 8.49  ? 45  GLU   A C   1 
ATOM   378  O  O   . GLU   A 1 45  ? 15.825 -3.134  39.967 1.00 8.57  ? 45  GLU   A O   1 
ATOM   379  C  CB  . GLU   A 1 45  ? 13.834 -5.710  40.211 1.00 11.04 ? 45  GLU   A CB  1 
ATOM   380  C  CG  . GLU   A 1 45  ? 14.180 -5.659  38.737 1.00 15.79 ? 45  GLU   A CG  1 
ATOM   381  C  CD  . GLU   A 1 45  ? 13.231 -6.460  37.865 1.00 32.09 ? 45  GLU   A CD  1 
ATOM   382  O  OE1 . GLU   A 1 45  ? 12.760 -7.505  38.332 1.00 23.00 ? 45  GLU   A OE1 1 
ATOM   383  O  OE2 . GLU   A 1 45  ? 12.967 -6.028  36.731 1.00 37.53 ? 45  GLU   A OE2 1 
ATOM   384  N  N   . GLY   A 1 46  ? 13.927 -2.680  41.039 1.00 7.95  ? 46  GLY   A N   1 
ATOM   385  C  CA  . GLY   A 1 46  ? 13.973 -1.276  40.592 1.00 7.99  ? 46  GLY   A CA  1 
ATOM   386  C  C   . GLY   A 1 46  ? 15.179 -0.533  41.153 1.00 7.19  ? 46  GLY   A C   1 
ATOM   387  O  O   . GLY   A 1 46  ? 15.687 0.356   40.496 1.00 9.03  ? 46  GLY   A O   1 
ATOM   388  N  N   . VAL   A 1 47  ? 15.564 -0.901  42.353 1.00 7.40  ? 47  VAL   A N   1 
ATOM   389  C  CA  . VAL   A 1 47  ? 16.740 -0.241  42.969 1.00 5.66  ? 47  VAL   A CA  1 
ATOM   390  C  C   . VAL   A 1 47  ? 18.002 -0.738  42.261 1.00 9.03  ? 47  VAL   A C   1 
ATOM   391  O  O   . VAL   A 1 47  ? 18.884 0.042   41.956 1.00 8.15  ? 47  VAL   A O   1 
ATOM   392  C  CB  . VAL   A 1 47  ? 16.777 -0.555  44.473 1.00 7.09  ? 47  VAL   A CB  1 
ATOM   393  C  CG1 . VAL   A 1 47  ? 17.852 0.267   45.172 1.00 7.83  ? 47  VAL   A CG1 1 
ATOM   394  C  CG2 . VAL   A 1 47  ? 15.428 -0.290  45.128 1.00 8.48  ? 47  VAL   A CG2 1 
ATOM   395  N  N   . CYS   A 1 48  ? 18.059 -2.028  42.024 1.00 8.27  ? 48  CYS   A N   1 
ATOM   396  C  CA  . CYS   A 1 48  ? 19.202 -2.572  41.268 1.00 8.72  ? 48  CYS   A CA  1 
ATOM   397  C  C   . CYS   A 1 48  ? 19.320 -1.855  39.913 1.00 8.35  ? 48  CYS   A C   1 
ATOM   398  O  O   . CYS   A 1 48  ? 20.410 -1.480  39.546 1.00 8.93  ? 48  CYS   A O   1 
ATOM   399  C  CB  . CYS   A 1 48  ? 18.936 -4.066  41.146 1.00 7.69  ? 48  CYS   A CB  1 
ATOM   400  S  SG  . CYS   A 1 48  ? 19.962 -4.875  39.887 1.00 11.46 ? 48  CYS   A SG  1 
ATOM   401  N  N   . HIS   A 1 49  ? 18.210 -1.818  39.184 1.00 7.89  ? 49  HIS   A N   1 
ATOM   402  C  CA  A HIS   A 1 49  ? 18.265 -1.140  37.866 0.38 9.28  ? 49  HIS   A CA  1 
ATOM   403  C  CA  B HIS   A 1 49  ? 18.252 -1.140  37.862 0.62 9.21  ? 49  HIS   A CA  1 
ATOM   404  C  C   . HIS   A 1 49  ? 18.687 0.354   37.901 1.00 8.98  ? 49  HIS   A C   1 
ATOM   405  O  O   . HIS   A 1 49  ? 19.497 0.886   37.120 1.00 9.46  ? 49  HIS   A O   1 
ATOM   406  C  CB  A HIS   A 1 49  ? 16.942 -1.348  37.127 0.38 12.45 ? 49  HIS   A CB  1 
ATOM   407  C  CB  B HIS   A 1 49  ? 16.907 -1.298  37.148 0.62 12.34 ? 49  HIS   A CB  1 
ATOM   408  C  CG  A HIS   A 1 49  ? 16.874 -2.723  36.555 0.38 20.06 ? 49  HIS   A CG  1 
ATOM   409  C  CG  B HIS   A 1 49  ? 16.656 -2.692  36.682 0.62 21.04 ? 49  HIS   A CG  1 
ATOM   410  N  ND1 A HIS   A 1 49  ? 16.855 -2.961  35.197 0.38 23.83 ? 49  HIS   A ND1 1 
ATOM   411  N  ND1 B HIS   A 1 49  ? 15.514 -3.047  35.988 0.62 21.47 ? 49  HIS   A ND1 1 
ATOM   412  C  CD2 A HIS   A 1 49  ? 16.885 -3.933  37.152 0.38 21.00 ? 49  HIS   A CD2 1 
ATOM   413  C  CD2 B HIS   A 1 49  ? 17.387 -3.820  36.813 0.62 19.21 ? 49  HIS   A CD2 1 
ATOM   414  C  CE1 A HIS   A 1 49  ? 16.820 -4.261  34.984 0.38 23.24 ? 49  HIS   A CE1 1 
ATOM   415  C  CE1 B HIS   A 1 49  ? 15.560 -4.334  35.706 0.62 19.83 ? 49  HIS   A CE1 1 
ATOM   416  N  NE2 A HIS   A 1 49  ? 16.834 -4.878  36.168 0.38 24.29 ? 49  HIS   A NE2 1 
ATOM   417  N  NE2 B HIS   A 1 49  ? 16.698 -4.830  36.203 0.62 24.39 ? 49  HIS   A NE2 1 
ATOM   418  N  N   . PHE   A 1 50  ? 18.191 1.017   38.937 1.00 8.56  ? 50  PHE   A N   1 
ATOM   419  C  CA  . PHE   A 1 50  ? 18.567 2.441   39.120 1.00 8.50  ? 50  PHE   A CA  1 
ATOM   420  C  C   . PHE   A 1 50  ? 20.089 2.588   39.247 1.00 7.29  ? 50  PHE   A C   1 
ATOM   421  O  O   . PHE   A 1 50  ? 20.669 3.414   38.591 1.00 8.00  ? 50  PHE   A O   1 
ATOM   422  C  CB  . PHE   A 1 50  ? 17.836 2.986   40.348 1.00 7.73  ? 50  PHE   A CB  1 
ATOM   423  C  CG  . PHE   A 1 50  ? 18.138 4.420   40.697 1.00 8.23  ? 50  PHE   A CG  1 
ATOM   424  C  CD1 . PHE   A 1 50  ? 17.543 5.456   40.000 1.00 11.32 ? 50  PHE   A CD1 1 
ATOM   425  C  CD2 . PHE   A 1 50  ? 18.996 4.731   41.736 1.00 9.18  ? 50  PHE   A CD2 1 
ATOM   426  C  CE1 . PHE   A 1 50  ? 17.813 6.774   40.327 1.00 10.63 ? 50  PHE   A CE1 1 
ATOM   427  C  CE2 . PHE   A 1 50  ? 19.270 6.050   42.056 1.00 9.81  ? 50  PHE   A CE2 1 
ATOM   428  C  CZ  . PHE   A 1 50  ? 18.674 7.069   41.354 1.00 11.59 ? 50  PHE   A CZ  1 
ATOM   429  N  N   . PHE   A 1 51  ? 20.672 1.781   40.104 1.00 7.38  ? 51  PHE   A N   1 
ATOM   430  C  CA  . PHE   A 1 51  ? 22.127 1.929   40.353 1.00 7.04  ? 51  PHE   A CA  1 
ATOM   431  C  C   . PHE   A 1 51  ? 22.974 1.384   39.187 1.00 7.54  ? 51  PHE   A C   1 
ATOM   432  O  O   . PHE   A 1 51  ? 23.991 1.948   38.882 1.00 8.03  ? 51  PHE   A O   1 
ATOM   433  C  CB  . PHE   A 1 51  ? 22.473 1.302   41.712 1.00 5.78  ? 51  PHE   A CB  1 
ATOM   434  C  CG  . PHE   A 1 51  ? 21.979 2.111   42.883 1.00 6.48  ? 51  PHE   A CG  1 
ATOM   435  C  CD1 . PHE   A 1 51  ? 22.242 3.467   42.966 1.00 9.01  ? 51  PHE   A CD1 1 
ATOM   436  C  CD2 . PHE   A 1 51  ? 21.251 1.521   43.901 1.00 7.83  ? 51  PHE   A CD2 1 
ATOM   437  C  CE1 . PHE   A 1 51  ? 21.791 4.211   44.041 1.00 7.48  ? 51  PHE   A CE1 1 
ATOM   438  C  CE2 . PHE   A 1 51  ? 20.793 2.268   44.973 1.00 8.56  ? 51  PHE   A CE2 1 
ATOM   439  C  CZ  . PHE   A 1 51  ? 21.065 3.613   45.041 1.00 9.17  ? 51  PHE   A CZ  1 
ATOM   440  N  N   . ARG   A 1 52  ? 22.522 0.306   38.566 1.00 8.62  ? 52  ARG   A N   1 
ATOM   441  C  CA  . ARG   A 1 52  ? 23.275 -0.209  37.396 1.00 7.27  ? 52  ARG   A CA  1 
ATOM   442  C  C   . ARG   A 1 52  ? 23.271 0.832   36.275 1.00 8.59  ? 52  ARG   A C   1 
ATOM   443  O  O   . ARG   A 1 52  ? 24.259 0.979   35.601 1.00 10.29 ? 52  ARG   A O   1 
ATOM   444  C  CB  . ARG   A 1 52  ? 22.645 -1.518  36.912 1.00 10.17 ? 52  ARG   A CB  1 
ATOM   445  C  CG  . ARG   A 1 52  ? 22.984 -2.707  37.800 1.00 14.44 ? 52  ARG   A CG  1 
ATOM   446  C  CD  . ARG   A 1 52  ? 22.487 -4.039  37.271 1.00 18.06 ? 52  ARG   A CD  1 
ATOM   447  N  NE  . ARG   A 1 52  ? 23.106 -4.402  36.008 1.00 17.64 ? 52  ARG   A NE  1 
ATOM   448  C  CZ  . ARG   A 1 52  ? 22.518 -5.113  35.054 1.00 32.46 ? 52  ARG   A CZ  1 
ATOM   449  N  NH1 . ARG   A 1 52  ? 21.280 -5.547  35.213 1.00 35.42 ? 52  ARG   A NH1 1 
ATOM   450  N  NH2 . ARG   A 1 52  ? 23.171 -5.379  33.939 1.00 32.20 ? 52  ARG   A NH2 1 
ATOM   451  N  N   . GLU   A 1 53  ? 22.134 1.500   36.106 1.00 9.92  ? 53  GLU   A N   1 
ATOM   452  C  CA  A GLU   A 1 53  ? 22.080 2.583   35.092 0.52 9.48  ? 53  GLU   A CA  1 
ATOM   453  C  CA  B GLU   A 1 53  ? 22.075 2.587   35.094 0.48 9.49  ? 53  GLU   A CA  1 
ATOM   454  C  C   . GLU   A 1 53  ? 23.097 3.716   35.407 1.00 9.64  ? 53  GLU   A C   1 
ATOM   455  O  O   . GLU   A 1 53  ? 23.860 4.258   34.572 1.00 9.95  ? 53  GLU   A O   1 
ATOM   456  C  CB  A GLU   A 1 53  ? 20.662 3.144   34.998 0.52 9.01  ? 53  GLU   A CB  1 
ATOM   457  C  CB  B GLU   A 1 53  ? 20.659 3.160   35.024 0.48 9.02  ? 53  GLU   A CB  1 
ATOM   458  C  CG  A GLU   A 1 53  ? 20.569 4.376   34.119 0.52 12.58 ? 53  GLU   A CG  1 
ATOM   459  C  CG  B GLU   A 1 53  ? 19.669 2.238   34.340 0.48 10.69 ? 53  GLU   A CG  1 
ATOM   460  C  CD  A GLU   A 1 53  ? 20.973 4.186   32.668 0.52 22.47 ? 53  GLU   A CD  1 
ATOM   461  C  CD  B GLU   A 1 53  ? 18.218 2.448   34.743 0.48 16.38 ? 53  GLU   A CD  1 
ATOM   462  O  OE1 A GLU   A 1 53  ? 20.973 3.033   32.192 0.52 20.72 ? 53  GLU   A OE1 1 
ATOM   463  O  OE1 B GLU   A 1 53  ? 17.914 3.501   35.340 0.48 20.21 ? 53  GLU   A OE1 1 
ATOM   464  O  OE2 A GLU   A 1 53  ? 21.268 5.200   32.013 0.52 21.96 ? 53  GLU   A OE2 1 
ATOM   465  O  OE2 B GLU   A 1 53  ? 17.395 1.553   34.457 0.48 20.42 ? 53  GLU   A OE2 1 
ATOM   466  N  N   . LEU   A 1 54  ? 23.204 3.973   36.712 1.00 8.33  ? 54  LEU   A N   1 
ATOM   467  C  CA  . LEU   A 1 54  ? 24.155 5.037   37.144 1.00 8.05  ? 54  LEU   A CA  1 
ATOM   468  C  C   . LEU   A 1 54  ? 25.608 4.576   36.932 1.00 9.36  ? 54  LEU   A C   1 
ATOM   469  O  O   . LEU   A 1 54  ? 26.443 5.389   36.653 1.00 9.12  ? 54  LEU   A O   1 
ATOM   470  C  CB  . LEU   A 1 54  ? 23.847 5.432   38.596 1.00 7.35  ? 54  LEU   A CB  1 
ATOM   471  C  CG  . LEU   A 1 54  ? 22.699 6.419   38.760 1.00 10.85 ? 54  LEU   A CG  1 
ATOM   472  C  CD1 . LEU   A 1 54  ? 22.307 6.539   40.221 1.00 14.40 ? 54  LEU   A CD1 1 
ATOM   473  C  CD2 . LEU   A 1 54  ? 23.098 7.770   38.194 1.00 18.70 ? 54  LEU   A CD2 1 
ATOM   474  N  N   . ALA   A 1 55  ? 25.870 3.280   37.071 1.00 7.84  ? 55  ALA   A N   1 
ATOM   475  C  CA  . ALA   A 1 55  ? 27.236 2.781   36.796 1.00 8.73  ? 55  ALA   A CA  1 
ATOM   476  C  C   . ALA   A 1 55  ? 27.600 3.090   35.345 1.00 9.95  ? 55  ALA   A C   1 
ATOM   477  O  O   . ALA   A 1 55  ? 28.693 3.539   35.079 1.00 9.96  ? 55  ALA   A O   1 
ATOM   478  C  CB  . ALA   A 1 55  ? 27.304 1.290   37.097 1.00 8.59  ? 55  ALA   A CB  1 
ATOM   479  N  N   A PHE   A 1 56  ? 26.642 2.890   34.458 0.54 7.96  ? 56  PHE   A N   1 
ATOM   480  N  N   B PHE   A 1 56  ? 26.641 2.884   34.456 0.46 7.96  ? 56  PHE   A N   1 
ATOM   481  C  CA  A PHE   A 1 56  ? 26.910 3.149   33.030 0.54 9.40  ? 56  PHE   A CA  1 
ATOM   482  C  CA  B PHE   A 1 56  ? 26.910 3.151   33.029 0.46 9.43  ? 56  PHE   A CA  1 
ATOM   483  C  C   A PHE   A 1 56  ? 27.075 4.652   32.808 0.54 10.78 ? 56  PHE   A C   1 
ATOM   484  C  C   B PHE   A 1 56  ? 27.084 4.653   32.820 0.46 10.79 ? 56  PHE   A C   1 
ATOM   485  O  O   A PHE   A 1 56  ? 27.939 5.072   32.045 0.54 10.57 ? 56  PHE   A O   1 
ATOM   486  O  O   B PHE   A 1 56  ? 27.936 5.068   32.044 0.46 10.60 ? 56  PHE   A O   1 
ATOM   487  C  CB  A PHE   A 1 56  ? 25.738 2.605   32.216 0.54 10.74 ? 56  PHE   A CB  1 
ATOM   488  C  CB  B PHE   A 1 56  ? 25.736 2.674   32.177 0.46 10.86 ? 56  PHE   A CB  1 
ATOM   489  C  CG  A PHE   A 1 56  ? 25.796 2.951   30.752 0.54 13.35 ? 56  PHE   A CG  1 
ATOM   490  C  CG  B PHE   A 1 56  ? 25.344 1.227   32.316 0.46 13.50 ? 56  PHE   A CG  1 
ATOM   491  C  CD1 A PHE   A 1 56  ? 26.892 2.593   29.985 0.54 19.31 ? 56  PHE   A CD1 1 
ATOM   492  C  CD1 B PHE   A 1 56  ? 26.294 0.242   32.527 0.46 19.50 ? 56  PHE   A CD1 1 
ATOM   493  C  CD2 A PHE   A 1 56  ? 24.763 3.642   30.145 0.54 18.32 ? 56  PHE   A CD2 1 
ATOM   494  C  CD2 B PHE   A 1 56  ? 24.015 0.849   32.208 0.46 15.95 ? 56  PHE   A CD2 1 
ATOM   495  C  CE1 A PHE   A 1 56  ? 26.945 2.909   28.637 0.54 19.61 ? 56  PHE   A CE1 1 
ATOM   496  C  CE1 B PHE   A 1 56  ? 25.919 -1.086  32.638 0.46 19.28 ? 56  PHE   A CE1 1 
ATOM   497  C  CE2 A PHE   A 1 56  ? 24.813 3.949   28.796 0.54 17.22 ? 56  PHE   A CE2 1 
ATOM   498  C  CE2 B PHE   A 1 56  ? 23.642 -0.480  32.317 0.46 16.81 ? 56  PHE   A CE2 1 
ATOM   499  C  CZ  A PHE   A 1 56  ? 25.905 3.585   28.046 0.54 14.47 ? 56  PHE   A CZ  1 
ATOM   500  C  CZ  B PHE   A 1 56  ? 24.596 -1.445  32.536 0.46 20.89 ? 56  PHE   A CZ  1 
ATOM   501  N  N   . GLU   A 1 57  ? 26.201 5.421   33.443 1.00 10.21 ? 57  GLU   A N   1 
ATOM   502  C  CA  . GLU   A 1 57  ? 26.238 6.896   33.238 1.00 9.31  ? 57  GLU   A CA  1 
ATOM   503  C  C   . GLU   A 1 57  ? 27.589 7.463   33.705 1.00 8.40  ? 57  GLU   A C   1 
ATOM   504  O  O   . GLU   A 1 57  ? 28.129 8.353   33.078 1.00 10.02 ? 57  GLU   A O   1 
ATOM   505  C  CB  . GLU   A 1 57  ? 25.074 7.588   33.964 1.00 9.42  ? 57  GLU   A CB  1 
ATOM   506  C  CG  . GLU   A 1 57  ? 23.747 7.294   33.304 1.00 15.70 ? 57  GLU   A CG  1 
ATOM   507  C  CD  . GLU   A 1 57  ? 22.526 7.918   33.946 1.00 25.30 ? 57  GLU   A CD  1 
ATOM   508  O  OE1 . GLU   A 1 57  ? 22.693 8.817   34.785 1.00 27.75 ? 57  GLU   A OE1 1 
ATOM   509  O  OE2 . GLU   A 1 57  ? 21.415 7.517   33.574 1.00 27.54 ? 57  GLU   A OE2 1 
ATOM   510  N  N   . LYS   A 1 58  ? 28.081 6.943   34.809 1.00 7.91  ? 58  LYS   A N   1 
ATOM   511  C  CA  . LYS   A 1 58  ? 29.366 7.460   35.316 1.00 6.90  ? 58  LYS   A CA  1 
ATOM   512  C  C   . LYS   A 1 58  ? 30.517 6.991   34.428 1.00 9.74  ? 58  LYS   A C   1 
ATOM   513  O  O   . LYS   A 1 58  ? 31.470 7.731   34.268 1.00 9.53  ? 58  LYS   A O   1 
ATOM   514  C  CB  . LYS   A 1 58  ? 29.570 6.997   36.760 1.00 8.00  ? 58  LYS   A CB  1 
ATOM   515  C  CG  . LYS   A 1 58  ? 28.656 7.652   37.787 1.00 8.34  ? 58  LYS   A CG  1 
ATOM   516  C  CD  . LYS   A 1 58  ? 28.521 9.147   37.599 1.00 11.11 ? 58  LYS   A CD  1 
ATOM   517  C  CE  . LYS   A 1 58  ? 27.481 9.747   38.515 1.00 16.74 ? 58  LYS   A CE  1 
ATOM   518  N  NZ  . LYS   A 1 58  ? 27.233 11.175  38.211 1.00 15.60 ? 58  LYS   A NZ  1 
ATOM   519  N  N   . PHE   A 1 59  ? 30.422 5.778   33.900 1.00 8.25  ? 59  PHE   A N   1 
ATOM   520  C  CA  . PHE   A 1 59  ? 31.470 5.354   32.938 1.00 8.37  ? 59  PHE   A CA  1 
ATOM   521  C  C   . PHE   A 1 59  ? 31.463 6.296   31.721 1.00 8.82  ? 59  PHE   A C   1 
ATOM   522  O  O   . PHE   A 1 59  ? 32.488 6.693   31.223 1.00 9.56  ? 59  PHE   A O   1 
ATOM   523  C  CB  . PHE   A 1 59  ? 31.222 3.895   32.532 1.00 8.82  ? 59  PHE   A CB  1 
ATOM   524  C  CG  . PHE   A 1 59  ? 32.127 3.496   31.405 1.00 10.43 ? 59  PHE   A CG  1 
ATOM   525  C  CD1 . PHE   A 1 59  ? 33.454 3.204   31.652 1.00 11.35 ? 59  PHE   A CD1 1 
ATOM   526  C  CD2 . PHE   A 1 59  ? 31.681 3.524   30.098 1.00 17.52 ? 59  PHE   A CD2 1 
ATOM   527  C  CE1 . PHE   A 1 59  ? 34.303 2.878   30.609 1.00 14.16 ? 59  PHE   A CE1 1 
ATOM   528  C  CE2 . PHE   A 1 59  ? 32.536 3.212   29.056 1.00 27.32 ? 59  PHE   A CE2 1 
ATOM   529  C  CZ  . PHE   A 1 59  ? 33.842 2.885   29.316 1.00 21.50 ? 59  PHE   A CZ  1 
ATOM   530  N  N   . GLU   A 1 60  ? 30.255 6.574   31.261 1.00 9.27  ? 60  GLU   A N   1 
ATOM   531  C  CA  A GLU   A 1 60  ? 30.146 7.483   30.077 0.38 9.43  ? 60  GLU   A CA  1 
ATOM   532  C  CA  B GLU   A 1 60  ? 30.149 7.484   30.082 0.62 9.31  ? 60  GLU   A CA  1 
ATOM   533  C  C   . GLU   A 1 60  ? 30.796 8.868   30.349 1.00 8.99  ? 60  GLU   A C   1 
ATOM   534  O  O   . GLU   A 1 60  ? 31.452 9.541   29.517 1.00 10.91 ? 60  GLU   A O   1 
ATOM   535  C  CB  A GLU   A 1 60  ? 28.690 7.630   29.624 0.38 13.13 ? 60  GLU   A CB  1 
ATOM   536  C  CB  B GLU   A 1 60  ? 28.691 7.662   29.656 0.62 13.06 ? 60  GLU   A CB  1 
ATOM   537  C  CG  A GLU   A 1 60  ? 28.051 6.318   29.209 0.38 17.12 ? 60  GLU   A CG  1 
ATOM   538  C  CG  B GLU   A 1 60  ? 28.088 6.445   28.990 0.62 16.68 ? 60  GLU   A CG  1 
ATOM   539  C  CD  A GLU   A 1 60  ? 28.570 5.706   27.921 0.38 21.60 ? 60  GLU   A CD  1 
ATOM   540  C  CD  B GLU   A 1 60  ? 26.632 6.686   28.637 0.62 24.53 ? 60  GLU   A CD  1 
ATOM   541  O  OE1 A GLU   A 1 60  ? 28.221 6.219   26.842 0.38 27.55 ? 60  GLU   A OE1 1 
ATOM   542  O  OE1 B GLU   A 1 60  ? 25.803 6.740   29.565 0.62 26.28 ? 60  GLU   A OE1 1 
ATOM   543  O  OE2 A GLU   A 1 60  ? 29.307 4.707   27.997 0.38 21.71 ? 60  GLU   A OE2 1 
ATOM   544  O  OE2 B GLU   A 1 60  ? 26.339 6.855   27.439 0.62 27.34 ? 60  GLU   A OE2 1 
ATOM   545  N  N   . GLY   A 1 61  ? 30.574 9.320   31.574 1.00 7.82  ? 61  GLY   A N   1 
ATOM   546  C  CA  . GLY   A 1 61  ? 31.213 10.571  32.007 1.00 8.39  ? 61  GLY   A CA  1 
ATOM   547  C  C   . GLY   A 1 61  ? 32.724 10.484  31.916 1.00 8.74  ? 61  GLY   A C   1 
ATOM   548  O  O   . GLY   A 1 61  ? 33.349 11.396  31.433 1.00 9.33  ? 61  GLY   A O   1 
ATOM   549  N  N   . ALA   A 1 62  ? 33.275 9.395   32.424 1.00 8.75  ? 62  ALA   A N   1 
ATOM   550  C  CA  . ALA   A 1 62  ? 34.731 9.204   32.312 1.00 7.31  ? 62  ALA   A CA  1 
ATOM   551  C  C   . ALA   A 1 62  ? 35.179 9.158   30.845 1.00 8.64  ? 62  ALA   A C   1 
ATOM   552  O  O   . ALA   A 1 62  ? 36.200 9.727   30.530 1.00 8.64  ? 62  ALA   A O   1 
ATOM   553  C  CB  . ALA   A 1 62  ? 35.121 7.930   33.041 1.00 9.78  ? 62  ALA   A CB  1 
ATOM   554  N  N   . GLU   A 1 63  ? 34.412 8.425   30.046 1.00 7.86  ? 63  GLU   A N   1 
ATOM   555  C  CA  A GLU   A 1 63  ? 34.748 8.362   28.605 0.49 8.40  ? 63  GLU   A CA  1 
ATOM   556  C  CA  B GLU   A 1 63  ? 34.745 8.341   28.596 0.51 8.41  ? 63  GLU   A CA  1 
ATOM   557  C  C   . GLU   A 1 63  ? 34.805 9.741   27.898 1.00 8.14  ? 63  GLU   A C   1 
ATOM   558  O  O   . GLU   A 1 63  ? 35.641 10.115  27.053 1.00 10.30 ? 63  GLU   A O   1 
ATOM   559  C  CB  A GLU   A 1 63  ? 33.692 7.536   27.882 0.49 10.19 ? 63  GLU   A CB  1 
ATOM   560  C  CB  B GLU   A 1 63  ? 33.671 7.490   27.929 0.51 10.18 ? 63  GLU   A CB  1 
ATOM   561  C  CG  A GLU   A 1 63  ? 33.971 6.055   27.853 0.49 15.40 ? 63  GLU   A CG  1 
ATOM   562  C  CG  B GLU   A 1 63  ? 34.073 6.859   26.621 0.51 9.22  ? 63  GLU   A CG  1 
ATOM   563  C  CD  A GLU   A 1 63  ? 32.880 5.343   27.079 0.49 17.82 ? 63  GLU   A CD  1 
ATOM   564  C  CD  B GLU   A 1 63  ? 32.969 5.931   26.155 0.51 19.72 ? 63  GLU   A CD  1 
ATOM   565  O  OE1 A GLU   A 1 63  ? 31.703 5.569   27.402 0.49 14.75 ? 63  GLU   A OE1 1 
ATOM   566  O  OE1 B GLU   A 1 63  ? 31.889 6.449   25.814 0.51 20.12 ? 63  GLU   A OE1 1 
ATOM   567  O  OE2 A GLU   A 1 63  ? 33.206 4.585   26.159 0.49 20.97 ? 63  GLU   A OE2 1 
ATOM   568  O  OE2 B GLU   A 1 63  ? 33.173 4.704   26.190 0.51 20.97 ? 63  GLU   A OE2 1 
ATOM   569  N  N   . ARG   A 1 64  ? 33.808 10.533  28.272 1.00 8.57  ? 64  ARG   A N   1 
ATOM   570  C  CA  . ARG   A 1 64  ? 33.768 11.902  27.679 1.00 7.83  ? 64  ARG   A CA  1 
ATOM   571  C  C   . ARG   A 1 64  ? 34.976 12.785  28.104 1.00 7.83  ? 64  ARG   A C   1 
ATOM   572  O  O   . ARG   A 1 64  ? 35.605 13.578  27.375 1.00 9.37  ? 64  ARG   A O   1 
ATOM   573  C  CB  . ARG   A 1 64  ? 32.443 12.586  28.033 1.00 9.35  ? 64  ARG   A CB  1 
ATOM   574  C  CG  . ARG   A 1 64  ? 32.254 13.917  27.324 1.00 13.27 ? 64  ARG   A CG  1 
ATOM   575  C  CD  . ARG   A 1 64  ? 30.980 14.620  27.737 1.00 16.83 ? 64  ARG   A CD  1 
ATOM   576  N  NE  . ARG   A 1 64  ? 29.808 13.870  27.319 1.00 16.00 ? 64  ARG   A NE  1 
ATOM   577  C  CZ  . ARG   A 1 64  ? 29.198 14.024  26.150 1.00 19.22 ? 64  ARG   A CZ  1 
ATOM   578  N  NH1 . ARG   A 1 64  ? 29.653 14.903  25.275 1.00 22.92 ? 64  ARG   A NH1 1 
ATOM   579  N  NH2 . ARG   A 1 64  ? 28.137 13.297  25.857 1.00 27.39 ? 64  ARG   A NH2 1 
ATOM   580  N  N   . LEU   A 1 65  ? 35.305 12.619  29.376 1.00 7.95  ? 65  LEU   A N   1 
ATOM   581  C  CA  . LEU   A 1 65  ? 36.503 13.333  29.888 1.00 7.55  ? 65  LEU   A CA  1 
ATOM   582  C  C   . LEU   A 1 65  ? 37.756 12.870  29.140 1.00 7.33  ? 65  LEU   A C   1 
ATOM   583  O  O   . LEU   A 1 65  ? 38.590 13.707  28.838 1.00 7.84  ? 65  LEU   A O   1 
ATOM   584  C  CB  . LEU   A 1 65  ? 36.642 13.072  31.394 1.00 7.87  ? 65  LEU   A CB  1 
ATOM   585  C  CG  . LEU   A 1 65  ? 35.675 13.872  32.263 1.00 9.17  ? 65  LEU   A CG  1 
ATOM   586  C  CD1 . LEU   A 1 65  ? 35.508 13.216  33.622 1.00 9.97  ? 65  LEU   A CD1 1 
ATOM   587  C  CD2 . LEU   A 1 65  ? 36.149 15.306  32.413 1.00 11.56 ? 65  LEU   A CD2 1 
ATOM   588  N  N   . LEU   A 1 66  ? 37.882 11.554  28.949 1.00 7.90  ? 66  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 66  ? 39.077 11.000  28.241 1.00 7.38  ? 66  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 66  ? 39.108 11.450  26.771 1.00 7.24  ? 66  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 66  ? 40.160 11.755  26.264 1.00 7.84  ? 66  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 66  ? 39.038 9.464   28.353 1.00 7.80  ? 66  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 66  ? 39.327 8.915   29.748 1.00 6.97  ? 66  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 66  ? 38.939 7.449   29.840 1.00 8.80  ? 66  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 66  ? 40.795 9.104   30.096 1.00 8.05  ? 66  LEU   A CD2 1 
ATOM   596  N  N   . LYS   A 1 67  ? 37.946 11.510  26.141 1.00 7.51  ? 67  LYS   A N   1 
ATOM   597  C  CA  . LYS   A 1 67  ? 37.889 11.997  24.739 1.00 6.52  ? 67  LYS   A CA  1 
ATOM   598  C  C   . LYS   A 1 67  ? 38.360 13.453  24.692 1.00 9.03  ? 67  LYS   A C   1 
ATOM   599  O  O   . LYS   A 1 67  ? 39.115 13.826  23.827 1.00 8.77  ? 67  LYS   A O   1 
ATOM   600  C  CB  . LYS   A 1 67  ? 36.444 11.889  24.228 1.00 7.97  ? 67  LYS   A CB  1 
ATOM   601  C  CG  . LYS   A 1 67  ? 35.928 10.497  23.893 1.00 17.15 ? 67  LYS   A CG  1 
ATOM   602  C  CD  . LYS   A 1 67  ? 34.458 10.513  23.519 1.00 20.19 ? 67  LYS   A CD  1 
ATOM   603  C  CE  . LYS   A 1 67  ? 33.933 9.177   23.036 1.00 25.23 ? 67  LYS   A CE  1 
ATOM   604  N  NZ  . LYS   A 1 67  ? 32.500 9.261   22.664 1.00 29.98 ? 67  LYS   A NZ  1 
ATOM   605  N  N   . MET   A 1 68  ? 37.893 14.223  25.657 1.00 7.51  ? 68  MET   A N   1 
ATOM   606  C  CA  . MET   A 1 68  ? 38.248 15.657  25.670 1.00 7.86  ? 68  MET   A CA  1 
ATOM   607  C  C   . MET   A 1 68  ? 39.743 15.835  25.969 1.00 7.11  ? 68  MET   A C   1 
ATOM   608  O  O   . MET   A 1 68  ? 40.369 16.664  25.373 1.00 8.39  ? 68  MET   A O   1 
ATOM   609  C  CB  . MET   A 1 68  ? 37.392 16.338  26.742 1.00 7.35  ? 68  MET   A CB  1 
ATOM   610  C  CG  . MET   A 1 68  ? 37.644 17.828  26.873 1.00 7.32  ? 68  MET   A CG  1 
ATOM   611  S  SD  . MET   A 1 68  ? 39.034 18.194  27.990 1.00 8.60  ? 68  MET   A SD  1 
ATOM   612  C  CE  . MET   A 1 68  ? 38.292 17.775  29.569 1.00 8.88  ? 68  MET   A CE  1 
ATOM   613  N  N   . GLN   A 1 69  ? 40.250 15.033  26.887 1.00 6.73  ? 69  GLN   A N   1 
ATOM   614  C  CA  . GLN   A 1 69  ? 41.689 15.096  27.204 1.00 7.50  ? 69  GLN   A CA  1 
ATOM   615  C  C   . GLN   A 1 69  ? 42.498 14.961  25.907 1.00 6.62  ? 69  GLN   A C   1 
ATOM   616  O  O   . GLN   A 1 69  ? 43.404 15.749  25.675 1.00 7.88  ? 69  GLN   A O   1 
ATOM   617  C  CB  . GLN   A 1 69  ? 42.013 13.992  28.226 1.00 7.44  ? 69  GLN   A CB  1 
ATOM   618  C  CG  . GLN   A 1 69  ? 43.475 13.905  28.653 1.00 9.60  ? 69  GLN   A CG  1 
ATOM   619  C  CD  . GLN   A 1 69  ? 43.829 14.919  29.713 1.00 8.67  ? 69  GLN   A CD  1 
ATOM   620  O  OE1 . GLN   A 1 69  ? 43.945 16.104  29.442 1.00 10.24 ? 69  GLN   A OE1 1 
ATOM   621  N  NE2 . GLN   A 1 69  ? 43.994 14.452  30.940 1.00 9.26  ? 69  GLN   A NE2 1 
ATOM   622  N  N   . ASN   A 1 70  ? 42.116 14.011  25.084 1.00 6.79  ? 70  ASN   A N   1 
ATOM   623  C  CA  . ASN   A 1 70  ? 42.845 13.807  23.817 1.00 6.79  ? 70  ASN   A CA  1 
ATOM   624  C  C   . ASN   A 1 70  ? 42.557 14.939  22.823 1.00 6.58  ? 70  ASN   A C   1 
ATOM   625  O  O   . ASN   A 1 70  ? 43.443 15.346  22.113 1.00 7.97  ? 70  ASN   A O   1 
ATOM   626  C  CB  . ASN   A 1 70  ? 42.475 12.453  23.223 1.00 6.73  ? 70  ASN   A CB  1 
ATOM   627  C  CG  . ASN   A 1 70  ? 43.285 11.305  23.784 1.00 9.41  ? 70  ASN   A CG  1 
ATOM   628  O  OD1 . ASN   A 1 70  ? 44.290 11.514  24.446 1.00 11.30 ? 70  ASN   A OD1 1 
ATOM   629  N  ND2 . ASN   A 1 70  ? 42.850 10.091  23.510 1.00 8.29  ? 70  ASN   A ND2 1 
ATOM   630  N  N   A GLN   A 1 71  ? 41.318 15.413  22.796 0.58 7.26  ? 71  GLN   A N   1 
ATOM   631  N  N   B GLN   A 1 71  ? 41.313 15.409  22.786 0.42 7.27  ? 71  GLN   A N   1 
ATOM   632  C  CA  A GLN   A 1 71  ? 41.003 16.521  21.861 0.58 7.05  ? 71  GLN   A CA  1 
ATOM   633  C  CA  B GLN   A 1 71  ? 40.985 16.522  21.860 0.42 7.07  ? 71  GLN   A CA  1 
ATOM   634  C  C   A GLN   A 1 71  ? 41.894 17.717  22.187 0.58 8.66  ? 71  GLN   A C   1 
ATOM   635  C  C   B GLN   A 1 71  ? 41.878 17.717  22.188 0.42 8.65  ? 71  GLN   A C   1 
ATOM   636  O  O   A GLN   A 1 71  ? 42.148 18.523  21.305 0.58 8.88  ? 71  GLN   A O   1 
ATOM   637  O  O   B GLN   A 1 71  ? 42.145 18.520  21.296 0.42 8.83  ? 71  GLN   A O   1 
ATOM   638  C  CB  A GLN   A 1 71  ? 39.548 16.948  22.028 0.58 8.97  ? 71  GLN   A CB  1 
ATOM   639  C  CB  B GLN   A 1 71  ? 39.528 16.947  22.035 0.42 8.96  ? 71  GLN   A CB  1 
ATOM   640  C  CG  A GLN   A 1 71  ? 38.559 15.960  21.432 0.58 9.78  ? 71  GLN   A CG  1 
ATOM   641  C  CG  B GLN   A 1 71  ? 38.525 15.920  21.532 0.42 9.83  ? 71  GLN   A CG  1 
ATOM   642  C  CD  A GLN   A 1 71  ? 37.138 16.334  21.764 0.58 9.70  ? 71  GLN   A CD  1 
ATOM   643  C  CD  B GLN   A 1 71  ? 38.277 16.046  20.050 0.42 9.02  ? 71  GLN   A CD  1 
ATOM   644  O  OE1 A GLN   A 1 71  ? 36.831 16.744  22.878 0.58 15.01 ? 71  GLN   A OE1 1 
ATOM   645  O  OE1 B GLN   A 1 71  ? 38.340 15.074  19.302 0.42 13.52 ? 71  GLN   A OE1 1 
ATOM   646  N  NE2 A GLN   A 1 71  ? 36.258 16.208  20.786 0.58 19.08 ? 71  GLN   A NE2 1 
ATOM   647  N  NE2 B GLN   A 1 71  ? 37.983 17.257  19.610 0.42 9.69  ? 71  GLN   A NE2 1 
ATOM   648  N  N   . ARG   A 1 72  ? 42.205 17.869  23.461 1.00 8.28  ? 72  ARG   A N   1 
ATOM   649  C  CA  . ARG   A 1 72  ? 42.978 19.059  23.910 1.00 8.17  ? 72  ARG   A CA  1 
ATOM   650  C  C   . ARG   A 1 72  ? 44.498 18.836  23.821 1.00 9.25  ? 72  ARG   A C   1 
ATOM   651  O  O   . ARG   A 1 72  ? 45.236 19.789  23.960 1.00 10.27 ? 72  ARG   A O   1 
ATOM   652  C  CB  . ARG   A 1 72  ? 42.625 19.497  25.340 1.00 6.12  ? 72  ARG   A CB  1 
ATOM   653  C  CG  . ARG   A 1 72  ? 41.243 20.119  25.491 1.00 8.43  ? 72  ARG   A CG  1 
ATOM   654  C  CD  . ARG   A 1 72  ? 41.028 21.366  24.655 1.00 6.76  ? 72  ARG   A CD  1 
ATOM   655  N  NE  . ARG   A 1 72  ? 41.924 22.482  24.941 1.00 7.11  ? 72  ARG   A NE  1 
ATOM   656  C  CZ  . ARG   A 1 72  ? 41.744 23.383  25.900 1.00 7.62  ? 72  ARG   A CZ  1 
ATOM   657  N  NH1 . ARG   A 1 72  ? 40.710 23.299  26.720 1.00 8.03  ? 72  ARG   A NH1 1 
ATOM   658  N  NH2 . ARG   A 1 72  ? 42.609 24.367  26.039 1.00 7.60  ? 72  ARG   A NH2 1 
ATOM   659  N  N   . GLY   A 1 73  ? 44.904 17.603  23.584 1.00 9.52  ? 73  GLY   A N   1 
ATOM   660  C  CA  . GLY   A 1 73  ? 46.355 17.329  23.544 1.00 9.73  ? 73  GLY   A CA  1 
ATOM   661  C  C   . GLY   A 1 73  ? 46.962 16.910  24.869 1.00 10.04 ? 73  GLY   A C   1 
ATOM   662  O  O   . GLY   A 1 73  ? 48.166 16.835  24.954 1.00 11.01 ? 73  GLY   A O   1 
ATOM   663  N  N   . GLY   A 1 74  ? 46.121 16.715  25.870 1.00 8.67  ? 74  GLY   A N   1 
ATOM   664  C  CA  . GLY   A 1 74  ? 46.624 16.151  27.118 1.00 9.46  ? 74  GLY   A CA  1 
ATOM   665  C  C   . GLY   A 1 74  ? 46.756 14.637  27.013 1.00 7.59  ? 74  GLY   A C   1 
ATOM   666  O  O   . GLY   A 1 74  ? 46.382 14.049  26.027 1.00 10.23 ? 74  GLY   A O   1 
ATOM   667  N  N   . ARG   A 1 75  ? 47.335 14.100  28.067 1.00 9.06  ? 75  ARG   A N   1 
ATOM   668  C  CA  . ARG   A 1 75  ? 47.621 12.659  28.064 1.00 9.95  ? 75  ARG   A CA  1 
ATOM   669  C  C   . ARG   A 1 75  ? 46.879 12.004  29.219 1.00 8.51  ? 75  ARG   A C   1 
ATOM   670  O  O   . ARG   A 1 75  ? 47.091 12.369  30.357 1.00 9.35  ? 75  ARG   A O   1 
ATOM   671  C  CB  . ARG   A 1 75  ? 49.133 12.487  28.148 1.00 11.20 ? 75  ARG   A CB  1 
ATOM   672  C  CG  . ARG   A 1 75  ? 49.812 12.835  26.829 1.00 19.34 ? 75  ARG   A CG  1 
ATOM   673  C  CD  . ARG   A 1 75  ? 49.232 12.132  25.613 1.00 18.73 ? 75  ARG   A CD  1 
ATOM   674  N  NE  . ARG   A 1 75  ? 49.742 12.637  24.342 1.00 27.10 ? 75  ARG   A NE  1 
ATOM   675  C  CZ  . ARG   A 1 75  ? 48.984 13.202  23.416 1.00 21.29 ? 75  ARG   A CZ  1 
ATOM   676  N  NH1 . ARG   A 1 75  ? 47.679 13.320  23.612 1.00 15.54 ? 75  ARG   A NH1 1 
ATOM   677  N  NH2 . ARG   A 1 75  ? 49.528 13.634  22.297 1.00 25.59 ? 75  ARG   A NH2 1 
ATOM   678  N  N   . ALA   A 1 76  ? 46.021 11.081  28.844 1.00 8.05  ? 76  ALA   A N   1 
ATOM   679  C  CA  . ALA   A 1 76  ? 45.318 10.281  29.864 1.00 9.26  ? 76  ALA   A CA  1 
ATOM   680  C  C   . ALA   A 1 76  ? 46.307 9.520   30.737 1.00 10.05 ? 76  ALA   A C   1 
ATOM   681  O  O   . ALA   A 1 76  ? 47.189 8.827   30.219 1.00 12.20 ? 76  ALA   A O   1 
ATOM   682  C  CB  . ALA   A 1 76  ? 44.396 9.289   29.210 1.00 12.44 ? 76  ALA   A CB  1 
ATOM   683  N  N   . LEU   A 1 77  ? 46.090 9.608   32.027 1.00 8.71  ? 77  LEU   A N   1 
ATOM   684  C  CA  . LEU   A 1 77  ? 46.929 8.822   32.950 1.00 9.94  ? 77  LEU   A CA  1 
ATOM   685  C  C   . LEU   A 1 77  ? 45.973 8.162   33.934 1.00 12.81 ? 77  LEU   A C   1 
ATOM   686  O  O   . LEU   A 1 77  ? 45.193 8.856   34.552 1.00 13.94 ? 77  LEU   A O   1 
ATOM   687  C  CB  . LEU   A 1 77  ? 47.951 9.705   33.666 1.00 12.91 ? 77  LEU   A CB  1 
ATOM   688  C  CG  . LEU   A 1 77  ? 49.194 10.078  32.867 1.00 16.53 ? 77  LEU   A CG  1 
ATOM   689  C  CD1 . LEU   A 1 77  ? 50.118 10.933  33.716 1.00 16.65 ? 77  LEU   A CD1 1 
ATOM   690  C  CD2 . LEU   A 1 77  ? 49.921 8.831   32.387 1.00 14.11 ? 77  LEU   A CD2 1 
ATOM   691  N  N   . PHE   A 1 78  ? 46.078 6.852   34.018 1.00 9.45  ? 78  PHE   A N   1 
ATOM   692  C  CA  . PHE   A 1 78  ? 45.161 6.085   34.879 1.00 10.10 ? 78  PHE   A CA  1 
ATOM   693  C  C   . PHE   A 1 78  ? 45.849 5.666   36.176 1.00 11.57 ? 78  PHE   A C   1 
ATOM   694  O  O   . PHE   A 1 78  ? 47.029 5.373   36.193 1.00 13.96 ? 78  PHE   A O   1 
ATOM   695  C  CB  . PHE   A 1 78  ? 44.668 4.862   34.107 1.00 8.20  ? 78  PHE   A CB  1 
ATOM   696  C  CG  . PHE   A 1 78  ? 43.841 5.227   32.903 1.00 8.36  ? 78  PHE   A CG  1 
ATOM   697  C  CD1 . PHE   A 1 78  ? 42.519 5.607   33.049 1.00 11.60 ? 78  PHE   A CD1 1 
ATOM   698  C  CD2 . PHE   A 1 78  ? 44.392 5.228   31.634 1.00 9.51  ? 78  PHE   A CD2 1 
ATOM   699  C  CE1 . PHE   A 1 78  ? 41.755 5.954   31.947 1.00 12.30 ? 78  PHE   A CE1 1 
ATOM   700  C  CE2 . PHE   A 1 78  ? 43.627 5.582   30.535 1.00 8.85  ? 78  PHE   A CE2 1 
ATOM   701  C  CZ  . PHE   A 1 78  ? 42.312 5.938   30.693 1.00 11.11 ? 78  PHE   A CZ  1 
ATOM   702  N  N   . GLN   A 1 79  ? 45.066 5.700   37.227 1.00 10.44 ? 79  GLN   A N   1 
ATOM   703  C  CA  . GLN   A 1 79  ? 45.576 5.266   38.540 1.00 11.88 ? 79  GLN   A CA  1 
ATOM   704  C  C   . GLN   A 1 79  ? 44.743 4.085   39.026 1.00 10.37 ? 79  GLN   A C   1 
ATOM   705  O  O   . GLN   A 1 79  ? 43.729 3.766   38.439 1.00 11.74 ? 79  GLN   A O   1 
ATOM   706  C  CB  . GLN   A 1 79  ? 45.493 6.422   39.545 1.00 14.50 ? 79  GLN   A CB  1 
ATOM   707  C  CG  . GLN   A 1 79  ? 46.328 7.633   39.159 1.00 16.90 ? 79  GLN   A CG  1 
ATOM   708  C  CD  . GLN   A 1 79  ? 47.788 7.315   38.953 1.00 36.25 ? 79  GLN   A CD  1 
ATOM   709  O  OE1 . GLN   A 1 79  ? 48.325 6.354   39.502 1.00 25.91 ? 79  GLN   A OE1 1 
ATOM   710  N  NE2 . GLN   A 1 79  ? 48.450 8.140   38.158 1.00 30.42 ? 79  GLN   A NE2 1 
ATOM   711  N  N   . ASP   A 1 80  ? 45.211 3.487   40.111 1.00 10.63 ? 80  ASP   A N   1 
ATOM   712  C  CA  . ASP   A 1 80  ? 44.442 2.384   40.711 1.00 11.00 ? 80  ASP   A CA  1 
ATOM   713  C  C   . ASP   A 1 80  ? 43.037 2.910   41.014 1.00 11.79 ? 80  ASP   A C   1 
ATOM   714  O  O   . ASP   A 1 80  ? 42.888 4.086   41.321 1.00 13.61 ? 80  ASP   A O   1 
ATOM   715  C  CB  . ASP   A 1 80  ? 45.188 1.872   41.959 1.00 12.96 ? 80  ASP   A CB  1 
ATOM   716  C  CG  . ASP   A 1 80  ? 46.578 1.289   41.761 1.00 15.26 ? 80  ASP   A CG  1 
ATOM   717  O  OD1 . ASP   A 1 80  ? 46.818 0.686   40.723 1.00 10.23 ? 80  ASP   A OD1 1 
ATOM   718  O  OD2 . ASP   A 1 80  ? 47.393 1.425   42.678 1.00 16.27 ? 80  ASP   A OD2 1 
ATOM   719  N  N   . LEU   A 1 81  ? 42.057 2.034   40.884 1.00 11.17 ? 81  LEU   A N   1 
ATOM   720  C  CA  A LEU   A 1 81  ? 40.656 2.451   41.293 0.46 10.74 ? 81  LEU   A CA  1 
ATOM   721  C  CA  B LEU   A 1 81  ? 40.666 2.426   41.228 0.54 10.71 ? 81  LEU   A CA  1 
ATOM   722  C  C   . LEU   A 1 81  ? 40.296 1.837   42.643 1.00 12.78 ? 81  LEU   A C   1 
ATOM   723  O  O   . LEU   A 1 81  ? 40.303 0.578   42.855 1.00 13.69 ? 81  LEU   A O   1 
ATOM   724  C  CB  A LEU   A 1 81  ? 39.680 1.924   40.231 0.46 15.85 ? 81  LEU   A CB  1 
ATOM   725  C  CB  B LEU   A 1 81  ? 39.678 1.941   40.164 0.54 15.88 ? 81  LEU   A CB  1 
ATOM   726  C  CG  A LEU   A 1 81  ? 38.530 2.828   39.809 0.46 18.00 ? 81  LEU   A CG  1 
ATOM   727  C  CG  B LEU   A 1 81  ? 39.629 2.768   38.885 0.54 16.02 ? 81  LEU   A CG  1 
ATOM   728  C  CD1 A LEU   A 1 81  ? 39.083 4.097   39.187 0.46 15.00 ? 81  LEU   A CD1 1 
ATOM   729  C  CD1 B LEU   A 1 81  ? 38.736 2.092   37.859 0.54 15.47 ? 81  LEU   A CD1 1 
ATOM   730  C  CD2 A LEU   A 1 81  ? 37.652 2.087   38.810 0.46 11.97 ? 81  LEU   A CD2 1 
ATOM   731  C  CD2 B LEU   A 1 81  ? 39.131 4.170   39.184 0.54 15.06 ? 81  LEU   A CD2 1 
ATOM   732  N  N   A GLN   A 1 82  ? 40.015 2.664   43.642 0.52 10.70 ? 82  GLN   A N   1 
ATOM   733  N  N   B GLN   A 1 82  ? 40.022 2.676   43.647 0.28 10.79 ? 82  GLN   A N   1 
ATOM   734  N  N   C GLN   A 1 82  ? 40.013 2.724   43.593 0.20 10.85 ? 82  GLN   A N   1 
ATOM   735  C  CA  A GLN   A 1 82  ? 39.723 2.164   44.996 0.52 11.67 ? 82  GLN   A CA  1 
ATOM   736  C  CA  B GLN   A 1 82  ? 39.701 2.214   45.015 0.28 11.82 ? 82  GLN   A CA  1 
ATOM   737  C  CA  C GLN   A 1 82  ? 39.690 2.283   44.969 0.20 11.90 ? 82  GLN   A CA  1 
ATOM   738  C  C   A GLN   A 1 82  ? 38.350 1.506   45.011 0.52 11.96 ? 82  GLN   A C   1 
ATOM   739  C  C   B GLN   A 1 82  ? 38.348 1.519   45.021 0.28 12.03 ? 82  GLN   A C   1 
ATOM   740  C  C   C GLN   A 1 82  ? 38.351 1.550   44.972 0.20 12.05 ? 82  GLN   A C   1 
ATOM   741  O  O   A GLN   A 1 82  ? 37.516 1.862   44.168 0.52 14.23 ? 82  GLN   A O   1 
ATOM   742  O  O   B GLN   A 1 82  ? 37.517 1.853   44.157 0.28 14.18 ? 82  GLN   A O   1 
ATOM   743  O  O   C GLN   A 1 82  ? 37.491 1.895   44.147 0.20 14.14 ? 82  GLN   A O   1 
ATOM   744  C  CB  A GLN   A 1 82  ? 39.795 3.299   46.017 0.52 14.15 ? 82  GLN   A CB  1 
ATOM   745  C  CB  B GLN   A 1 82  ? 39.629 3.404   45.972 0.28 14.18 ? 82  GLN   A CB  1 
ATOM   746  C  CB  C GLN   A 1 82  ? 39.608 3.470   45.930 0.20 14.17 ? 82  GLN   A CB  1 
ATOM   747  C  CG  A GLN   A 1 82  ? 38.576 4.197   46.009 0.52 15.14 ? 82  GLN   A CG  1 
ATOM   748  C  CG  B GLN   A 1 82  ? 40.989 3.963   46.359 0.28 12.75 ? 82  GLN   A CG  1 
ATOM   749  C  CG  C GLN   A 1 82  ? 39.421 3.055   47.382 0.20 12.93 ? 82  GLN   A CG  1 
ATOM   750  N  N   . LYS   A 1 83  ? 38.295 0.445   45.697 1.00 11.99 ? 83  LYS   A N   1 
ATOM   751  C  CA  . LYS   A 1 83  ? 37.018 -0.292  45.846 1.00 11.22 ? 83  LYS   A CA  1 
ATOM   752  C  C   . LYS   A 1 83  ? 35.980 0.613   46.523 1.00 11.53 ? 83  LYS   A C   1 
ATOM   753  O  O   . LYS   A 1 83  ? 36.350 1.540   47.220 1.00 11.91 ? 83  LYS   A O   1 
ATOM   754  C  CB  . LYS   A 1 83  ? 37.206 -1.594  46.634 1.00 11.15 ? 83  LYS   A CB  1 
ATOM   755  C  CG  . LYS   A 1 83  ? 37.428 -1.449  48.130 1.00 12.03 ? 83  LYS   A CG  1 
ATOM   756  C  CD  . LYS   A 1 83  ? 37.578 -2.793  48.803 1.00 14.45 ? 83  LYS   A CD  1 
ATOM   757  C  CE  . LYS   A 1 83  ? 37.562 -2.712  50.311 1.00 15.88 ? 83  LYS   A CE  1 
ATOM   758  N  NZ  . LYS   A 1 83  ? 37.833 -4.034  50.923 1.00 20.78 ? 83  LYS   A NZ  1 
ATOM   759  N  N   . PRO   A 1 84  ? 34.693 0.293   46.352 1.00 8.35  ? 84  PRO   A N   1 
ATOM   760  C  CA  . PRO   A 1 84  ? 33.661 1.075   46.995 1.00 8.70  ? 84  PRO   A CA  1 
ATOM   761  C  C   . PRO   A 1 84  ? 33.806 1.073   48.523 1.00 10.32 ? 84  PRO   A C   1 
ATOM   762  O  O   . PRO   A 1 84  ? 34.398 0.174   49.058 1.00 11.79 ? 84  PRO   A O   1 
ATOM   763  C  CB  . PRO   A 1 84  ? 32.355 0.426   46.491 1.00 9.43  ? 84  PRO   A CB  1 
ATOM   764  C  CG  . PRO   A 1 84  ? 32.753 -0.192  45.182 1.00 8.72  ? 84  PRO   A CG  1 
ATOM   765  C  CD  . PRO   A 1 84  ? 34.124 -0.753  45.483 1.00 9.54  ? 84  PRO   A CD  1 
ATOM   766  N  N   . SER   A 1 85  ? 33.151 2.030   49.164 1.00 10.54 ? 85  SER   A N   1 
ATOM   767  C  CA  . SER   A 1 85  ? 33.313 2.263   50.621 1.00 11.19 ? 85  SER   A CA  1 
ATOM   768  C  C   . SER   A 1 85  ? 32.662 1.176   51.471 1.00 12.31 ? 85  SER   A C   1 
ATOM   769  O  O   . SER   A 1 85  ? 33.060 1.010   52.599 1.00 15.32 ? 85  SER   A O   1 
ATOM   770  C  CB  . SER   A 1 85  ? 32.742 3.622   50.948 1.00 13.59 ? 85  SER   A CB  1 
ATOM   771  O  OG  . SER   A 1 85  ? 31.341 3.655   50.760 1.00 20.63 ? 85  SER   A OG  1 
ATOM   772  N  N   . GLN   A 1 86  ? 31.695 0.470   50.882 1.00 9.71  ? 86  GLN   A N   1 
ATOM   773  C  CA  A GLN   A 1 86  ? 30.964 -0.577  51.621 0.61 9.11  ? 86  GLN   A CA  1 
ATOM   774  C  CA  B GLN   A 1 86  ? 31.064 -0.577  51.621 0.39 9.22  ? 86  GLN   A CA  1 
ATOM   775  C  C   . GLN   A 1 86  ? 30.831 -1.835  50.764 1.00 8.59  ? 86  GLN   A C   1 
ATOM   776  O  O   . GLN   A 1 86  ? 30.896 -1.724  49.566 1.00 10.35 ? 86  GLN   A O   1 
ATOM   777  C  CB  A GLN   A 1 86  ? 29.540 -0.112  51.957 0.61 11.04 ? 86  GLN   A CB  1 
ATOM   778  C  CB  B GLN   A 1 86  ? 29.640 -0.112  51.957 0.39 11.36 ? 86  GLN   A CB  1 
ATOM   779  C  CG  A GLN   A 1 86  ? 29.533 1.122   52.847 0.61 11.47 ? 86  GLN   A CG  1 
ATOM   780  C  CG  B GLN   A 1 86  ? 29.632 1.074   52.910 0.39 11.78 ? 86  GLN   A CG  1 
ATOM   781  C  CD  A GLN   A 1 86  ? 28.161 1.725   52.998 0.61 15.36 ? 86  GLN   A CD  1 
ATOM   782  C  CD  B GLN   A 1 86  ? 30.299 0.771   54.226 0.39 16.18 ? 86  GLN   A CD  1 
ATOM   783  O  OE1 A GLN   A 1 86  ? 27.995 2.941   53.019 0.61 19.61 ? 86  GLN   A OE1 1 
ATOM   784  O  OE1 B GLN   A 1 86  ? 30.146 -0.311  54.786 0.39 21.04 ? 86  GLN   A OE1 1 
ATOM   785  N  NE2 A GLN   A 1 86  ? 27.165 0.864   53.108 0.61 15.18 ? 86  GLN   A NE2 1 
ATOM   786  N  NE2 B GLN   A 1 86  ? 31.045 1.738   54.727 0.39 27.76 ? 86  GLN   A NE2 1 
ATOM   787  N  N   . ASP   A 1 87  ? 30.714 -2.976  51.416 1.00 8.51  ? 87  ASP   A N   1 
ATOM   788  C  CA  . ASP   A 1 87  ? 30.405 -4.261  50.732 1.00 9.61  ? 87  ASP   A CA  1 
ATOM   789  C  C   . ASP   A 1 87  ? 28.899 -4.547  50.727 1.00 11.43 ? 87  ASP   A C   1 
ATOM   790  O  O   . ASP   A 1 87  ? 28.431 -5.235  49.836 1.00 12.68 ? 87  ASP   A O   1 
ATOM   791  C  CB  . ASP   A 1 87  ? 31.115 -5.429  51.418 1.00 9.25  ? 87  ASP   A CB  1 
ATOM   792  C  CG  . ASP   A 1 87  ? 32.627 -5.289  51.399 1.00 11.56 ? 87  ASP   A CG  1 
ATOM   793  O  OD1 . ASP   A 1 87  ? 33.150 -4.830  50.376 1.00 11.83 ? 87  ASP   A OD1 1 
ATOM   794  O  OD2 . ASP   A 1 87  ? 33.256 -5.642  52.406 1.00 14.67 ? 87  ASP   A OD2 1 
ATOM   795  N  N   . GLU   A 1 88  ? 28.216 -4.051  51.749 1.00 10.11 ? 88  GLU   A N   1 
ATOM   796  C  CA  . GLU   A 1 88  ? 26.747 -4.219  51.909 1.00 11.03 ? 88  GLU   A CA  1 
ATOM   797  C  C   . GLU   A 1 88  ? 26.211 -2.798  52.086 1.00 11.52 ? 88  GLU   A C   1 
ATOM   798  O  O   . GLU   A 1 88  ? 26.823 -2.038  52.786 1.00 13.39 ? 88  GLU   A O   1 
ATOM   799  C  CB  . GLU   A 1 88  ? 26.430 -5.151  53.078 1.00 14.20 ? 88  GLU   A CB  1 
ATOM   800  C  CG  . GLU   A 1 88  ? 27.043 -6.516  52.897 1.00 20.49 ? 88  GLU   A CG  1 
ATOM   801  C  CD  . GLU   A 1 88  ? 26.661 -7.473  54.005 1.00 43.40 ? 88  GLU   A CD  1 
ATOM   802  O  OE1 . GLU   A 1 88  ? 26.933 -7.152  55.165 1.00 35.77 ? 88  GLU   A OE1 1 
ATOM   803  O  OE2 . GLU   A 1 88  ? 26.100 -8.528  53.695 1.00 31.88 ? 88  GLU   A OE2 1 
ATOM   804  N  N   . TRP   A 1 89  ? 25.043 -2.511  51.540 1.00 9.35  ? 89  TRP   A N   1 
ATOM   805  C  CA  . TRP   A 1 89  ? 24.627 -1.087  51.405 1.00 8.44  ? 89  TRP   A CA  1 
ATOM   806  C  C   . TRP   A 1 89  ? 23.375 -0.759  52.222 1.00 9.91  ? 89  TRP   A C   1 
ATOM   807  O  O   . TRP   A 1 89  ? 22.881 0.342   52.105 1.00 10.97 ? 89  TRP   A O   1 
ATOM   808  C  CB  . TRP   A 1 89  ? 24.463 -0.732  49.930 1.00 8.42  ? 89  TRP   A CB  1 
ATOM   809  C  CG  . TRP   A 1 89  ? 25.757 -0.792  49.180 1.00 9.40  ? 89  TRP   A CG  1 
ATOM   810  C  CD1 . TRP   A 1 89  ? 26.220 -1.822  48.413 1.00 8.70  ? 89  TRP   A CD1 1 
ATOM   811  C  CD2 . TRP   A 1 89  ? 26.773 0.224   49.140 1.00 8.12  ? 89  TRP   A CD2 1 
ATOM   812  N  NE1 . TRP   A 1 89  ? 27.441 -1.509  47.885 1.00 7.89  ? 89  TRP   A NE1 1 
ATOM   813  C  CE2 . TRP   A 1 89  ? 27.804 -0.261  48.310 1.00 8.59  ? 89  TRP   A CE2 1 
ATOM   814  C  CE3 . TRP   A 1 89  ? 26.897 1.500   49.696 1.00 8.38  ? 89  TRP   A CE3 1 
ATOM   815  C  CZ2 . TRP   A 1 89  ? 28.953 0.475   48.046 1.00 9.30  ? 89  TRP   A CZ2 1 
ATOM   816  C  CZ3 . TRP   A 1 89  ? 28.034 2.226   49.435 1.00 10.18 ? 89  TRP   A CZ3 1 
ATOM   817  C  CH2 . TRP   A 1 89  ? 29.045 1.719   48.622 1.00 9.21  ? 89  TRP   A CH2 1 
ATOM   818  N  N   . GLY   A 1 90  ? 22.932 -1.711  53.022 1.00 9.53  ? 90  GLY   A N   1 
ATOM   819  C  CA  . GLY   A 1 90  ? 21.786 -1.452  53.915 1.00 9.07  ? 90  GLY   A CA  1 
ATOM   820  C  C   . GLY   A 1 90  ? 20.446 -1.382  53.214 1.00 9.10  ? 90  GLY   A C   1 
ATOM   821  O  O   . GLY   A 1 90  ? 20.181 -2.182  52.357 1.00 9.58  ? 90  GLY   A O   1 
ATOM   822  N  N   . THR   A 1 91  ? 19.651 -0.435  53.664 1.00 8.52  ? 91  THR   A N   1 
ATOM   823  C  CA  . THR   A 1 91  ? 18.324 -0.249  53.059 1.00 9.45  ? 91  THR   A CA  1 
ATOM   824  C  C   . THR   A 1 91  ? 18.401 0.640   51.819 1.00 9.07  ? 91  THR   A C   1 
ATOM   825  O  O   . THR   A 1 91  ? 19.434 1.197   51.555 1.00 9.39  ? 91  THR   A O   1 
ATOM   826  C  CB  . THR   A 1 91  ? 17.378 0.409   54.067 1.00 9.80  ? 91  THR   A CB  1 
ATOM   827  O  OG1 . THR   A 1 91  ? 17.888 1.698   54.392 1.00 9.54  ? 91  THR   A OG1 1 
ATOM   828  C  CG2 . THR   A 1 91  ? 17.259 -0.400  55.336 1.00 12.45 ? 91  THR   A CG2 1 
ATOM   829  N  N   . THR   A 1 92  ? 17.294 0.691   51.095 1.00 9.26  ? 92  THR   A N   1 
ATOM   830  C  CA  . THR   A 1 92  ? 17.224 1.619   49.942 1.00 8.56  ? 92  THR   A CA  1 
ATOM   831  C  C   . THR   A 1 92  ? 17.551 3.034   50.418 1.00 8.22  ? 92  THR   A C   1 
ATOM   832  O  O   . THR   A 1 92  ? 18.225 3.728   49.718 1.00 9.39  ? 92  THR   A O   1 
ATOM   833  C  CB  . THR   A 1 92  ? 15.827 1.579   49.309 1.00 9.37  ? 92  THR   A CB  1 
ATOM   834  O  OG1 . THR   A 1 92  ? 15.527 0.246   48.905 1.00 8.93  ? 92  THR   A OG1 1 
ATOM   835  C  CG2 . THR   A 1 92  ? 15.722 2.477   48.096 1.00 8.70  ? 92  THR   A CG2 1 
ATOM   836  N  N   . LEU   A 1 93  ? 17.057 3.375   51.607 1.00 8.76  ? 93  LEU   A N   1 
ATOM   837  C  CA  . LEU   A 1 93  ? 17.346 4.722   52.170 1.00 8.06  ? 93  LEU   A CA  1 
ATOM   838  C  C   . LEU   A 1 93  ? 18.852 4.915   52.380 1.00 8.92  ? 93  LEU   A C   1 
ATOM   839  O  O   . LEU   A 1 93  ? 19.371 5.935   52.009 1.00 10.39 ? 93  LEU   A O   1 
ATOM   840  C  CB  . LEU   A 1 93  ? 16.565 4.870   53.483 1.00 8.63  ? 93  LEU   A CB  1 
ATOM   841  C  CG  . LEU   A 1 93  ? 16.751 6.193   54.221 1.00 12.72 ? 93  LEU   A CG  1 
ATOM   842  C  CD1 . LEU   A 1 93  ? 16.473 7.365   53.299 1.00 17.60 ? 93  LEU   A CD1 1 
ATOM   843  C  CD2 . LEU   A 1 93  ? 15.840 6.256   55.435 1.00 17.44 ? 93  LEU   A CD2 1 
ATOM   844  N  N   . ASP   A 1 94  ? 19.466 3.931   53.002 1.00 8.94  ? 94  ASP   A N   1 
ATOM   845  C  CA  . ASP   A 1 94  ? 20.923 4.032   53.250 1.00 8.07  ? 94  ASP   A CA  1 
ATOM   846  C  C   . ASP   A 1 94  ? 21.651 4.192   51.918 1.00 10.73 ? 94  ASP   A C   1 
ATOM   847  O  O   . ASP   A 1 94  ? 22.570 4.972   51.821 1.00 9.31  ? 94  ASP   A O   1 
ATOM   848  C  CB  . ASP   A 1 94  ? 21.438 2.761   53.920 1.00 8.60  ? 94  ASP   A CB  1 
ATOM   849  C  CG  . ASP   A 1 94  ? 20.977 2.550   55.351 1.00 12.34 ? 94  ASP   A CG  1 
ATOM   850  O  OD1 . ASP   A 1 94  ? 20.869 3.540   56.079 1.00 15.02 ? 94  ASP   A OD1 1 
ATOM   851  O  OD2 . ASP   A 1 94  ? 20.769 1.393   55.720 1.00 13.03 ? 94  ASP   A OD2 1 
ATOM   852  N  N   . ALA   A 1 95  ? 21.213 3.426   50.934 1.00 7.27  ? 95  ALA   A N   1 
ATOM   853  C  CA  . ALA   A 1 95  ? 21.904 3.450   49.635 1.00 7.95  ? 95  ALA   A CA  1 
ATOM   854  C  C   . ALA   A 1 95  ? 21.700 4.791   48.927 1.00 9.13  ? 95  ALA   A C   1 
ATOM   855  O  O   . ALA   A 1 95  ? 22.628 5.296   48.348 1.00 8.75  ? 95  ALA   A O   1 
ATOM   856  C  CB  . ALA   A 1 95  ? 21.362 2.302   48.813 1.00 8.24  ? 95  ALA   A CB  1 
ATOM   857  N  N   . MET   A 1 96  ? 20.476 5.284   48.996 1.00 8.63  ? 96  MET   A N   1 
ATOM   858  C  CA  . MET   A 1 96  ? 20.190 6.557   48.308 1.00 8.13  ? 96  MET   A CA  1 
ATOM   859  C  C   . MET   A 1 96  ? 20.944 7.700   49.011 1.00 8.47  ? 96  MET   A C   1 
ATOM   860  O  O   . MET   A 1 96  ? 21.388 8.604   48.334 1.00 9.67  ? 96  MET   A O   1 
ATOM   861  C  CB  . MET   A 1 96  ? 18.677 6.814   48.271 1.00 7.17  ? 96  MET   A CB  1 
ATOM   862  C  CG  . MET   A 1 96  ? 18.258 7.895   47.282 1.00 7.90  ? 96  MET   A CG  1 
ATOM   863  S  SD  . MET   A 1 96  ? 18.575 7.427   45.556 1.00 10.65 ? 96  MET   A SD  1 
ATOM   864  C  CE  . MET   A 1 96  ? 17.362 6.125   45.333 1.00 11.16 ? 96  MET   A CE  1 
ATOM   865  N  N   . LYS   A 1 97  ? 21.067 7.623   50.329 1.00 8.10  ? 97  LYS   A N   1 
ATOM   866  C  CA  . LYS   A 1 97  ? 21.877 8.644   51.046 1.00 9.97  ? 97  LYS   A CA  1 
ATOM   867  C  C   . LYS   A 1 97  ? 23.347 8.560   50.612 1.00 11.69 ? 97  LYS   A C   1 
ATOM   868  O  O   . LYS   A 1 97  ? 23.944 9.602   50.412 1.00 11.40 ? 97  LYS   A O   1 
ATOM   869  C  CB  . LYS   A 1 97  ? 21.777 8.437   52.557 1.00 9.68  ? 97  LYS   A CB  1 
ATOM   870  C  CG  . LYS   A 1 97  ? 20.470 8.872   53.202 1.00 13.54 ? 97  LYS   A CG  1 
ATOM   871  C  CD  . LYS   A 1 97  ? 20.435 8.524   54.668 1.00 18.35 ? 97  LYS   A CD  1 
ATOM   872  C  CE  . LYS   A 1 97  ? 19.166 8.965   55.362 1.00 40.35 ? 97  LYS   A CE  1 
ATOM   873  N  NZ  . LYS   A 1 97  ? 18.973 8.253   56.650 1.00 41.37 ? 97  LYS   A NZ  1 
ATOM   874  N  N   . ALA   A 1 98  ? 23.875 7.343   50.512 1.00 8.69  ? 98  ALA   A N   1 
ATOM   875  C  CA  . ALA   A 1 98  ? 25.282 7.172   50.082 1.00 8.01  ? 98  ALA   A CA  1 
ATOM   876  C  C   . ALA   A 1 98  ? 25.468 7.710   48.663 1.00 10.22 ? 98  ALA   A C   1 
ATOM   877  O  O   . ALA   A 1 98  ? 26.494 8.290   48.387 1.00 9.75  ? 98  ALA   A O   1 
ATOM   878  C  CB  . ALA   A 1 98  ? 25.650 5.712   50.169 1.00 11.28 ? 98  ALA   A CB  1 
ATOM   879  N  N   . ALA   A 1 99  ? 24.465 7.514   47.823 1.00 8.43  ? 99  ALA   A N   1 
ATOM   880  C  CA  . ALA   A 1 99  ? 24.568 7.985   46.426 1.00 8.65  ? 99  ALA   A CA  1 
ATOM   881  C  C   . ALA   A 1 99  ? 24.564 9.525   46.348 1.00 9.05  ? 99  ALA   A C   1 
ATOM   882  O  O   . ALA   A 1 99  ? 25.296 10.077  45.576 1.00 10.60 ? 99  ALA   A O   1 
ATOM   883  C  CB  . ALA   A 1 99  ? 23.419 7.387   45.645 1.00 12.44 ? 99  ALA   A CB  1 
ATOM   884  N  N   . ILE   A 1 100 ? 23.705 10.138  47.160 1.00 9.81  ? 100 ILE   A N   1 
ATOM   885  C  CA  A ILE   A 1 100 ? 23.685 11.635  47.162 0.57 8.84  ? 100 ILE   A CA  1 
ATOM   886  C  CA  B ILE   A 1 100 ? 23.685 11.636  47.186 0.43 8.89  ? 100 ILE   A CA  1 
ATOM   887  C  C   . ILE   A 1 100 ? 25.023 12.239  47.685 1.00 7.59  ? 100 ILE   A C   1 
ATOM   888  O  O   . ILE   A 1 100 ? 25.608 13.239  47.189 1.00 11.63 ? 100 ILE   A O   1 
ATOM   889  C  CB  A ILE   A 1 100 ? 22.447 12.173  47.907 0.57 9.20  ? 100 ILE   A CB  1 
ATOM   890  C  CB  B ILE   A 1 100 ? 22.503 12.137  48.033 0.43 9.14  ? 100 ILE   A CB  1 
ATOM   891  C  CG1 A ILE   A 1 100 ? 22.155 13.619  47.496 0.57 15.79 ? 100 ILE   A CG1 1 
ATOM   892  C  CG1 B ILE   A 1 100 ? 21.174 11.865  47.330 0.43 7.64  ? 100 ILE   A CG1 1 
ATOM   893  C  CG2 A ILE   A 1 100 ? 22.601 12.048  49.408 0.57 9.23  ? 100 ILE   A CG2 1 
ATOM   894  C  CG2 B ILE   A 1 100 ? 22.674 13.610  48.366 0.43 14.42 ? 100 ILE   A CG2 1 
ATOM   895  C  CD1 A ILE   A 1 100 ? 20.687 13.968  47.423 0.57 12.56 ? 100 ILE   A CD1 1 
ATOM   896  C  CD1 B ILE   A 1 100 ? 19.964 12.144  48.181 0.43 11.62 ? 100 ILE   A CD1 1 
ATOM   897  N  N   . VAL   A 1 101 ? 25.555 11.548  48.684 1.00 7.97  ? 101 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 101 ? 26.907 11.928  49.190 1.00 8.53  ? 101 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 101 ? 27.926 11.774  48.051 1.00 10.09 ? 101 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 101 ? 28.716 12.689  47.832 1.00 10.43 ? 101 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 101 ? 27.301 11.106  50.428 1.00 9.89  ? 101 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 101 ? 28.776 11.271  50.759 1.00 11.27 ? 101 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 101 ? 26.446 11.456  51.636 1.00 12.11 ? 101 VAL   A CG2 1 
ATOM   904  N  N   . LEU   A 1 102 ? 27.877 10.665  47.337 1.00 9.45  ? 102 LEU   A N   1 
ATOM   905  C  CA  . LEU   A 1 102 ? 28.816 10.450  46.212 1.00 9.37  ? 102 LEU   A CA  1 
ATOM   906  C  C   . LEU   A 1 102 ? 28.624 11.544  45.162 1.00 9.37  ? 102 LEU   A C   1 
ATOM   907  O  O   . LEU   A 1 102 ? 29.587 12.096  44.694 1.00 10.26 ? 102 LEU   A O   1 
ATOM   908  C  CB  . LEU   A 1 102 ? 28.555 9.048   45.642 1.00 9.73  ? 102 LEU   A CB  1 
ATOM   909  C  CG  . LEU   A 1 102 ? 29.364 8.637   44.418 1.00 11.11 ? 102 LEU   A CG  1 
ATOM   910  C  CD1 . LEU   A 1 102 ? 30.848 8.820   44.679 1.00 15.53 ? 102 LEU   A CD1 1 
ATOM   911  C  CD2 . LEU   A 1 102 ? 29.062 7.193   44.044 1.00 13.33 ? 102 LEU   A CD2 1 
ATOM   912  N  N   . GLU   A 1 103 ? 27.378 11.786  44.800 1.00 10.10 ? 103 GLU   A N   1 
ATOM   913  C  CA  . GLU   A 1 103 ? 27.132 12.772  43.721 1.00 8.88  ? 103 GLU   A CA  1 
ATOM   914  C  C   . GLU   A 1 103 ? 27.578 14.187  44.117 1.00 8.85  ? 103 GLU   A C   1 
ATOM   915  O  O   . GLU   A 1 103 ? 28.098 14.885  43.264 1.00 10.81 ? 103 GLU   A O   1 
ATOM   916  C  CB  . GLU   A 1 103 ? 25.653 12.791  43.352 1.00 9.07  ? 103 GLU   A CB  1 
ATOM   917  C  CG  . GLU   A 1 103 ? 25.231 11.539  42.602 1.00 10.91 ? 103 GLU   A CG  1 
ATOM   918  C  CD  . GLU   A 1 103 ? 26.108 11.153  41.424 1.00 12.74 ? 103 GLU   A CD  1 
ATOM   919  O  OE1 . GLU   A 1 103 ? 26.522 12.039  40.683 1.00 10.81 ? 103 GLU   A OE1 1 
ATOM   920  O  OE2 . GLU   A 1 103 ? 26.347 9.965   41.241 1.00 12.40 ? 103 GLU   A OE2 1 
ATOM   921  N  N   . LYS   A 1 104 ? 27.346 14.565  45.361 1.00 10.04 ? 104 LYS   A N   1 
ATOM   922  C  CA  . LYS   A 1 104 ? 27.808 15.906  45.818 1.00 9.24  ? 104 LYS   A CA  1 
ATOM   923  C  C   . LYS   A 1 104 ? 29.336 16.013  45.731 1.00 10.67 ? 104 LYS   A C   1 
ATOM   924  O  O   . LYS   A 1 104 ? 29.847 17.068  45.502 1.00 10.02 ? 104 LYS   A O   1 
ATOM   925  C  CB  . LYS   A 1 104 ? 27.334 16.169  47.248 1.00 10.41 ? 104 LYS   A CB  1 
ATOM   926  C  CG  . LYS   A 1 104 ? 25.872 16.567  47.367 1.00 14.74 ? 104 LYS   A CG  1 
ATOM   927  C  CD  . LYS   A 1 104 ? 25.409 16.558  48.801 1.00 20.50 ? 104 LYS   A CD  1 
ATOM   928  C  CE  . LYS   A 1 104 ? 24.011 17.103  48.973 1.00 26.82 ? 104 LYS   A CE  1 
ATOM   929  N  NZ  . LYS   A 1 104 ? 23.642 17.153  50.406 1.00 25.01 ? 104 LYS   A NZ  1 
ATOM   930  N  N   A SER   A 1 105 ? 29.990 14.892  45.995 0.68 10.28 ? 105 SER   A N   1 
ATOM   931  N  N   B SER   A 1 105 ? 30.007 14.895  45.995 0.32 10.34 ? 105 SER   A N   1 
ATOM   932  C  CA  A SER   A 1 105 ? 31.470 14.896  45.915 0.68 11.01 ? 105 SER   A CA  1 
ATOM   933  C  CA  B SER   A 1 105 ? 31.489 14.886  45.914 0.32 11.01 ? 105 SER   A CA  1 
ATOM   934  C  C   A SER   A 1 105 ? 31.914 15.048  44.452 0.68 9.65  ? 105 SER   A C   1 
ATOM   935  C  C   B SER   A 1 105 ? 31.932 15.036  44.454 0.32 9.73  ? 105 SER   A C   1 
ATOM   936  O  O   A SER   A 1 105 ? 32.851 15.780  44.208 0.68 10.28 ? 105 SER   A O   1 
ATOM   937  O  O   B SER   A 1 105 ? 32.855 15.816  44.204 0.32 10.29 ? 105 SER   A O   1 
ATOM   938  C  CB  A SER   A 1 105 ? 32.044 13.660  46.597 0.68 10.33 ? 105 SER   A CB  1 
ATOM   939  C  CB  B SER   A 1 105 ? 32.051 13.637  46.547 0.32 10.52 ? 105 SER   A CB  1 
ATOM   940  O  OG  A SER   A 1 105 ? 31.988 12.530  45.740 0.68 11.64 ? 105 SER   A OG  1 
ATOM   941  O  OG  B SER   A 1 105 ? 31.803 13.627  47.943 0.32 14.94 ? 105 SER   A OG  1 
ATOM   942  N  N   . LEU   A 1 106 ? 31.238 14.412  43.534 1.00 9.44  ? 106 LEU   A N   1 
ATOM   943  C  CA  . LEU   A 1 106 ? 31.569 14.570  42.090 1.00 8.14  ? 106 LEU   A CA  1 
ATOM   944  C  C   . LEU   A 1 106 ? 31.254 16.012  41.663 1.00 8.89  ? 106 LEU   A C   1 
ATOM   945  O  O   . LEU   A 1 106 ? 32.019 16.581  40.945 1.00 9.86  ? 106 LEU   A O   1 
ATOM   946  C  CB  . LEU   A 1 106 ? 30.780 13.571  41.230 1.00 11.81 ? 106 LEU   A CB  1 
ATOM   947  C  CG  . LEU   A 1 106 ? 31.140 12.092  41.364 1.00 12.82 ? 106 LEU   A CG  1 
ATOM   948  C  CD1 . LEU   A 1 106 ? 30.230 11.263  40.476 1.00 14.53 ? 106 LEU   A CD1 1 
ATOM   949  C  CD2 . LEU   A 1 106 ? 32.594 11.842  40.991 1.00 14.29 ? 106 LEU   A CD2 1 
ATOM   950  N  N   . ASN   A 1 107 ? 30.103 16.509  42.120 1.00 9.54  ? 107 ASN   A N   1 
ATOM   951  C  CA  . ASN   A 1 107 ? 29.708 17.889  41.774 1.00 8.61  ? 107 ASN   A CA  1 
ATOM   952  C  C   . ASN   A 1 107 ? 30.772 18.882  42.273 1.00 8.50  ? 107 ASN   A C   1 
ATOM   953  O  O   . ASN   A 1 107 ? 31.111 19.778  41.562 1.00 7.87  ? 107 ASN   A O   1 
ATOM   954  C  CB  . ASN   A 1 107 ? 28.317 18.172  42.343 1.00 9.22  ? 107 ASN   A CB  1 
ATOM   955  C  CG  . ASN   A 1 107 ? 27.640 19.311  41.621 1.00 8.91  ? 107 ASN   A CG  1 
ATOM   956  O  OD1 . ASN   A 1 107 ? 27.829 19.470  40.425 1.00 10.64 ? 107 ASN   A OD1 1 
ATOM   957  N  ND2 . ASN   A 1 107 ? 26.880 20.106  42.349 1.00 9.92  ? 107 ASN   A ND2 1 
ATOM   958  N  N   . GLN   A 1 108 ? 31.213 18.664  43.503 1.00 9.00  ? 108 GLN   A N   1 
ATOM   959  C  CA  . GLN   A 1 108 ? 32.234 19.595  44.031 1.00 7.30  ? 108 GLN   A CA  1 
ATOM   960  C  C   . GLN   A 1 108 ? 33.506 19.521  43.169 1.00 8.18  ? 108 GLN   A C   1 
ATOM   961  O  O   . GLN   A 1 108 ? 34.118 20.535  42.923 1.00 7.89  ? 108 GLN   A O   1 
ATOM   962  C  CB  . GLN   A 1 108 ? 32.541 19.318  45.507 1.00 8.76  ? 108 GLN   A CB  1 
ATOM   963  C  CG  . GLN   A 1 108 ? 33.350 20.438  46.150 1.00 10.01 ? 108 GLN   A CG  1 
ATOM   964  C  CD  . GLN   A 1 108 ? 32.666 21.777  46.024 1.00 12.28 ? 108 GLN   A CD  1 
ATOM   965  O  OE1 . GLN   A 1 108 ? 31.554 21.969  46.495 1.00 13.91 ? 108 GLN   A OE1 1 
ATOM   966  N  NE2 . GLN   A 1 108 ? 33.331 22.717  45.376 1.00 11.53 ? 108 GLN   A NE2 1 
ATOM   967  N  N   . ALA   A 1 109 ? 33.859 18.308  42.760 1.00 8.06  ? 109 ALA   A N   1 
ATOM   968  C  CA  . ALA   A 1 109 ? 35.057 18.147  41.906 1.00 7.13  ? 109 ALA   A CA  1 
ATOM   969  C  C   . ALA   A 1 109 ? 34.846 18.853  40.549 1.00 7.95  ? 109 ALA   A C   1 
ATOM   970  O  O   . ALA   A 1 109 ? 35.780 19.426  40.032 1.00 9.35  ? 109 ALA   A O   1 
ATOM   971  C  CB  . ALA   A 1 109 ? 35.374 16.667  41.745 1.00 7.48  ? 109 ALA   A CB  1 
ATOM   972  N  N   . LEU   A 1 110 ? 33.623 18.768  40.020 1.00 8.60  ? 110 LEU   A N   1 
ATOM   973  C  CA  . LEU   A 1 110 ? 33.341 19.490  38.757 1.00 7.94  ? 110 LEU   A CA  1 
ATOM   974  C  C   . LEU   A 1 110 ? 33.476 20.998  38.979 1.00 7.95  ? 110 LEU   A C   1 
ATOM   975  O  O   . LEU   A 1 110 ? 33.995 21.685  38.131 1.00 9.18  ? 110 LEU   A O   1 
ATOM   976  C  CB  . LEU   A 1 110 ? 31.899 19.189  38.350 1.00 9.28  ? 110 LEU   A CB  1 
ATOM   977  C  CG  . LEU   A 1 110 ? 31.578 17.776  37.869 1.00 10.91 ? 110 LEU   A CG  1 
ATOM   978  C  CD1 . LEU   A 1 110 ? 30.079 17.632  37.662 1.00 11.51 ? 110 LEU   A CD1 1 
ATOM   979  C  CD2 . LEU   A 1 110 ? 32.315 17.465  36.576 1.00 11.28 ? 110 LEU   A CD2 1 
ATOM   980  N  N   . LEU   A 1 111 ? 32.878 21.470  40.066 1.00 7.81  ? 111 LEU   A N   1 
ATOM   981  C  CA  . LEU   A 1 111 ? 32.935 22.922  40.372 1.00 8.50  ? 111 LEU   A CA  1 
ATOM   982  C  C   . LEU   A 1 111 ? 34.385 23.379  40.581 1.00 9.00  ? 111 LEU   A C   1 
ATOM   983  O  O   . LEU   A 1 111 ? 34.731 24.460  40.149 1.00 9.56  ? 111 LEU   A O   1 
ATOM   984  C  CB  . LEU   A 1 111 ? 32.085 23.182  41.622 1.00 7.68  ? 111 LEU   A CB  1 
ATOM   985  C  CG  . LEU   A 1 111 ? 30.591 22.940  41.445 1.00 7.39  ? 111 LEU   A CG  1 
ATOM   986  C  CD1 . LEU   A 1 111 ? 29.866 23.066  42.773 1.00 10.77 ? 111 LEU   A CD1 1 
ATOM   987  C  CD2 . LEU   A 1 111 ? 30.013 23.894  40.413 1.00 10.39 ? 111 LEU   A CD2 1 
ATOM   988  N  N   . ASP   A 1 112 ? 35.161 22.557  41.259 1.00 7.88  ? 112 ASP   A N   1 
ATOM   989  C  CA  . ASP   A 1 112 ? 36.578 22.907  41.507 1.00 7.79  ? 112 ASP   A CA  1 
ATOM   990  C  C   . ASP   A 1 112 ? 37.328 22.980  40.170 1.00 9.43  ? 112 ASP   A C   1 
ATOM   991  O  O   . ASP   A 1 112 ? 38.122 23.877  39.990 1.00 10.84 ? 112 ASP   A O   1 
ATOM   992  C  CB  . ASP   A 1 112 ? 37.219 21.885  42.444 1.00 9.86  ? 112 ASP   A CB  1 
ATOM   993  C  CG  . ASP   A 1 112 ? 36.748 21.921  43.885 1.00 11.04 ? 112 ASP   A CG  1 
ATOM   994  O  OD1 . ASP   A 1 112 ? 36.084 22.888  44.265 1.00 12.75 ? 112 ASP   A OD1 1 
ATOM   995  O  OD2 . ASP   A 1 112 ? 37.070 20.971  44.602 1.00 14.72 ? 112 ASP   A OD2 1 
ATOM   996  N  N   . LEU   A 1 113 ? 37.062 22.024  39.290 1.00 8.44  ? 113 LEU   A N   1 
ATOM   997  C  CA  . LEU   A 1 113 ? 37.740 22.045  37.973 1.00 9.23  ? 113 LEU   A CA  1 
ATOM   998  C  C   . LEU   A 1 113 ? 37.268 23.254  37.151 1.00 9.46  ? 113 LEU   A C   1 
ATOM   999  O  O   . LEU   A 1 113 ? 38.050 23.840  36.454 1.00 10.72 ? 113 LEU   A O   1 
ATOM   1000 C  CB  . LEU   A 1 113 ? 37.478 20.716  37.258 1.00 9.70  ? 113 LEU   A CB  1 
ATOM   1001 C  CG  . LEU   A 1 113 ? 38.101 20.576  35.872 1.00 10.82 ? 113 LEU   A CG  1 
ATOM   1002 C  CD1 . LEU   A 1 113 ? 39.602 20.813  35.928 1.00 11.70 ? 113 LEU   A CD1 1 
ATOM   1003 C  CD2 . LEU   A 1 113 ? 37.793 19.209  35.286 1.00 12.06 ? 113 LEU   A CD2 1 
ATOM   1004 N  N   . HIS   A 1 114 ? 35.976 23.553  37.226 1.00 8.96  ? 114 HIS   A N   1 
ATOM   1005 C  CA  . HIS   A 1 114 ? 35.493 24.755  36.510 1.00 8.68  ? 114 HIS   A CA  1 
ATOM   1006 C  C   . HIS   A 1 114 ? 36.231 25.999  37.020 1.00 10.42 ? 114 HIS   A C   1 
ATOM   1007 O  O   . HIS   A 1 114 ? 36.599 26.831  36.240 1.00 10.71 ? 114 HIS   A O   1 
ATOM   1008 C  CB  . HIS   A 1 114 ? 33.965 24.859  36.666 1.00 9.04  ? 114 HIS   A CB  1 
ATOM   1009 C  CG  . HIS   A 1 114 ? 33.366 25.874  35.760 1.00 10.79 ? 114 HIS   A CG  1 
ATOM   1010 N  ND1 . HIS   A 1 114 ? 33.468 27.224  36.002 1.00 12.68 ? 114 HIS   A ND1 1 
ATOM   1011 C  CD2 . HIS   A 1 114 ? 32.696 25.745  34.600 1.00 9.85  ? 114 HIS   A CD2 1 
ATOM   1012 C  CE1 . HIS   A 1 114 ? 32.866 27.883  35.041 1.00 8.39  ? 114 HIS   A CE1 1 
ATOM   1013 N  NE2 . HIS   A 1 114 ? 32.388 27.003  34.172 1.00 11.22 ? 114 HIS   A NE2 1 
ATOM   1014 N  N   . ALA   A 1 115 ? 36.369 26.077  38.325 1.00 10.80 ? 115 ALA   A N   1 
ATOM   1015 C  CA  . ALA   A 1 115 ? 37.020 27.269  38.889 1.00 9.19  ? 115 ALA   A CA  1 
ATOM   1016 C  C   . ALA   A 1 115 ? 38.484 27.335  38.438 1.00 9.56  ? 115 ALA   A C   1 
ATOM   1017 O  O   . ALA   A 1 115 ? 38.972 28.429  38.233 1.00 11.58 ? 115 ALA   A O   1 
ATOM   1018 C  CB  . ALA   A 1 115 ? 36.891 27.208  40.393 1.00 9.67  ? 115 ALA   A CB  1 
ATOM   1019 N  N   . LEU   A 1 116 ? 39.146 26.190  38.356 1.00 9.94  ? 116 LEU   A N   1 
ATOM   1020 C  CA  . LEU   A 1 116 ? 40.545 26.167  37.877 1.00 10.05 ? 116 LEU   A CA  1 
ATOM   1021 C  C   . LEU   A 1 116 ? 40.576 26.634  36.416 1.00 10.30 ? 116 LEU   A C   1 
ATOM   1022 O  O   . LEU   A 1 116 ? 41.398 27.448  36.056 1.00 11.65 ? 116 LEU   A O   1 
ATOM   1023 C  CB  . LEU   A 1 116 ? 41.068 24.731  38.035 1.00 11.18 ? 116 LEU   A CB  1 
ATOM   1024 C  CG  . LEU   A 1 116 ? 42.449 24.455  37.446 1.00 13.46 ? 116 LEU   A CG  1 
ATOM   1025 C  CD1 . LEU   A 1 116 ? 43.502 25.340  38.088 1.00 12.97 ? 116 LEU   A CD1 1 
ATOM   1026 C  CD2 . LEU   A 1 116 ? 42.821 22.992  37.603 1.00 15.46 ? 116 LEU   A CD2 1 
ATOM   1027 N  N   . GLY   A 1 117 ? 39.644 26.115  35.633 1.00 10.93 ? 117 GLY   A N   1 
ATOM   1028 C  CA  . GLY   A 1 117 ? 39.601 26.536  34.226 1.00 9.89  ? 117 GLY   A CA  1 
ATOM   1029 C  C   . GLY   A 1 117 ? 39.366 28.027  34.066 1.00 10.09 ? 117 GLY   A C   1 
ATOM   1030 O  O   . GLY   A 1 117 ? 39.956 28.640  33.190 1.00 12.00 ? 117 GLY   A O   1 
ATOM   1031 N  N   . SER   A 1 118 ? 38.450 28.545  34.872 1.00 10.85 ? 118 SER   A N   1 
ATOM   1032 C  CA  A SER   A 1 118 ? 38.196 30.013  34.867 0.33 10.62 ? 118 SER   A CA  1 
ATOM   1033 C  CA  B SER   A 1 118 ? 38.197 30.008  34.863 0.67 10.49 ? 118 SER   A CA  1 
ATOM   1034 C  C   . SER   A 1 118 ? 39.477 30.816  35.232 1.00 13.30 ? 118 SER   A C   1 
ATOM   1035 O  O   . SER   A 1 118 ? 39.943 31.807  34.603 1.00 14.20 ? 118 SER   A O   1 
ATOM   1036 C  CB  A SER   A 1 118 ? 37.080 30.360  35.814 0.33 14.11 ? 118 SER   A CB  1 
ATOM   1037 C  CB  B SER   A 1 118 ? 37.066 30.333  35.796 0.67 14.10 ? 118 SER   A CB  1 
ATOM   1038 O  OG  A SER   A 1 118 ? 35.996 29.456  35.694 0.33 13.71 ? 118 SER   A OG  1 
ATOM   1039 O  OG  B SER   A 1 118 ? 36.756 31.715  35.741 0.67 16.33 ? 118 SER   A OG  1 
ATOM   1040 N  N   . ALA   A 1 119 ? 40.105 30.323  36.286 1.00 12.45 ? 119 ALA   A N   1 
ATOM   1041 C  CA  . ALA   A 1 119 ? 41.351 30.989  36.753 1.00 14.99 ? 119 ALA   A CA  1 
ATOM   1042 C  C   . ALA   A 1 119 ? 42.422 30.946  35.656 1.00 18.01 ? 119 ALA   A C   1 
ATOM   1043 O  O   . ALA   A 1 119 ? 43.224 31.875  35.551 1.00 18.91 ? 119 ALA   A O   1 
ATOM   1044 C  CB  . ALA   A 1 119 ? 41.866 30.334  37.998 1.00 15.91 ? 119 ALA   A CB  1 
ATOM   1045 N  N   . GLN   A 1 120 ? 42.452 29.856  34.896 1.00 13.09 ? 120 GLN   A N   1 
ATOM   1046 C  CA  . GLN   A 1 120 ? 43.482 29.669  33.832 1.00 12.41 ? 120 GLN   A CA  1 
ATOM   1047 C  C   . GLN   A 1 120 ? 43.008 30.236  32.485 1.00 12.99 ? 120 GLN   A C   1 
ATOM   1048 O  O   . GLN   A 1 120 ? 43.694 30.015  31.507 1.00 14.91 ? 120 GLN   A O   1 
ATOM   1049 C  CB  . GLN   A 1 120 ? 43.798 28.191  33.692 1.00 12.19 ? 120 GLN   A CB  1 
ATOM   1050 C  CG  . GLN   A 1 120 ? 44.441 27.575  34.925 1.00 16.49 ? 120 GLN   A CG  1 
ATOM   1051 C  CD  . GLN   A 1 120 ? 45.942 27.519  34.812 1.00 25.38 ? 120 GLN   A CD  1 
ATOM   1052 O  OE1 . GLN   A 1 120 ? 46.536 28.053  33.883 1.00 22.10 ? 120 GLN   A OE1 1 
ATOM   1053 N  NE2 . GLN   A 1 120 ? 46.567 26.862  35.765 1.00 28.58 ? 120 GLN   A NE2 1 
ATOM   1054 N  N   . ALA   A 1 121 ? 41.848 30.863  32.450 1.00 10.64 ? 121 ALA   A N   1 
ATOM   1055 C  CA  . ALA   A 1 121 ? 41.262 31.404  31.202 1.00 9.59  ? 121 ALA   A CA  1 
ATOM   1056 C  C   . ALA   A 1 121 ? 41.193 30.294  30.155 1.00 11.32 ? 121 ALA   A C   1 
ATOM   1057 O  O   . ALA   A 1 121 ? 41.691 30.495  29.063 1.00 9.64  ? 121 ALA   A O   1 
ATOM   1058 C  CB  . ALA   A 1 121 ? 42.029 32.609  30.706 1.00 13.35 ? 121 ALA   A CB  1 
ATOM   1059 N  N   . ASP   A 1 122 ? 40.537 29.193  30.518 1.00 9.15  ? 122 ASP   A N   1 
ATOM   1060 C  CA  . ASP   A 1 122 ? 40.360 28.026  29.615 1.00 9.26  ? 122 ASP   A CA  1 
ATOM   1061 C  C   . ASP   A 1 122 ? 38.864 27.883  29.360 1.00 9.42  ? 122 ASP   A C   1 
ATOM   1062 O  O   . ASP   A 1 122 ? 38.225 27.081  29.980 1.00 8.41  ? 122 ASP   A O   1 
ATOM   1063 C  CB  . ASP   A 1 122 ? 40.923 26.767  30.275 1.00 8.68  ? 122 ASP   A CB  1 
ATOM   1064 C  CG  . ASP   A 1 122 ? 41.041 25.585  29.334 1.00 7.93  ? 122 ASP   A CG  1 
ATOM   1065 O  OD1 . ASP   A 1 122 ? 40.363 25.600  28.297 1.00 8.54  ? 122 ASP   A OD1 1 
ATOM   1066 O  OD2 . ASP   A 1 122 ? 41.799 24.670  29.661 1.00 9.54  ? 122 ASP   A OD2 1 
ATOM   1067 N  N   . PRO   A 1 123 ? 38.300 28.682  28.442 1.00 7.80  ? 123 PRO   A N   1 
ATOM   1068 C  CA  . PRO   A 1 123 ? 36.857 28.648  28.249 1.00 8.76  ? 123 PRO   A CA  1 
ATOM   1069 C  C   . PRO   A 1 123 ? 36.331 27.369  27.584 1.00 7.85  ? 123 PRO   A C   1 
ATOM   1070 O  O   . PRO   A 1 123 ? 35.218 27.049  27.777 1.00 9.26  ? 123 PRO   A O   1 
ATOM   1071 C  CB  . PRO   A 1 123 ? 36.591 29.879  27.361 1.00 9.22  ? 123 PRO   A CB  1 
ATOM   1072 C  CG  . PRO   A 1 123 ? 37.879 30.090  26.614 1.00 10.13 ? 123 PRO   A CG  1 
ATOM   1073 C  CD  . PRO   A 1 123 ? 38.954 29.703  27.602 1.00 9.40  ? 123 PRO   A CD  1 
ATOM   1074 N  N   . HIS   A 1 124 ? 37.199 26.683  26.848 1.00 7.54  ? 124 HIS   A N   1 
ATOM   1075 C  CA  . HIS   A 1 124 ? 36.730 25.402  26.270 1.00 6.46  ? 124 HIS   A CA  1 
ATOM   1076 C  C   . HIS   A 1 124 ? 36.422 24.418  27.406 1.00 9.36  ? 124 HIS   A C   1 
ATOM   1077 O  O   . HIS   A 1 124 ? 35.418 23.756  27.357 1.00 8.88  ? 124 HIS   A O   1 
ATOM   1078 C  CB  . HIS   A 1 124 ? 37.762 24.811  25.309 1.00 7.94  ? 124 HIS   A CB  1 
ATOM   1079 C  CG  . HIS   A 1 124 ? 37.256 23.579  24.646 1.00 8.75  ? 124 HIS   A CG  1 
ATOM   1080 N  ND1 . HIS   A 1 124 ? 37.409 22.331  25.204 1.00 10.07 ? 124 HIS   A ND1 1 
ATOM   1081 C  CD2 . HIS   A 1 124 ? 36.572 23.403  23.498 1.00 11.05 ? 124 HIS   A CD2 1 
ATOM   1082 C  CE1 . HIS   A 1 124 ? 36.854 21.437  24.417 1.00 8.59  ? 124 HIS   A CE1 1 
ATOM   1083 N  NE2 . HIS   A 1 124 ? 36.335 22.067  23.366 1.00 9.98  ? 124 HIS   A NE2 1 
ATOM   1084 N  N   . LEU   A 1 125 ? 37.325 24.375  28.368 1.00 8.55  ? 125 LEU   A N   1 
ATOM   1085 C  CA  A LEU   A 1 125 ? 37.119 23.446  29.518 0.49 9.34  ? 125 LEU   A CA  1 
ATOM   1086 C  CA  B LEU   A 1 125 ? 37.106 23.446  29.507 0.51 9.34  ? 125 LEU   A CA  1 
ATOM   1087 C  C   . LEU   A 1 125 ? 35.814 23.797  30.289 1.00 9.09  ? 125 LEU   A C   1 
ATOM   1088 O  O   . LEU   A 1 125 ? 34.948 23.004  30.684 1.00 9.61  ? 125 LEU   A O   1 
ATOM   1089 C  CB  A LEU   A 1 125 ? 38.361 23.553  30.412 0.49 9.66  ? 125 LEU   A CB  1 
ATOM   1090 C  CB  B LEU   A 1 125 ? 38.326 23.498  30.432 0.51 9.74  ? 125 LEU   A CB  1 
ATOM   1091 C  CG  A LEU   A 1 125 ? 38.458 22.650  31.641 0.49 10.66 ? 125 LEU   A CG  1 
ATOM   1092 C  CG  B LEU   A 1 125 ? 38.179 22.684  31.716 0.51 10.78 ? 125 LEU   A CG  1 
ATOM   1093 C  CD1 A LEU   A 1 125 ? 37.680 23.210  32.818 0.49 10.91 ? 125 LEU   A CD1 1 
ATOM   1094 C  CD1 B LEU   A 1 125 ? 38.338 21.201  31.433 0.51 9.14  ? 125 LEU   A CD1 1 
ATOM   1095 C  CD2 A LEU   A 1 125 ? 38.055 21.219  31.333 0.49 11.08 ? 125 LEU   A CD2 1 
ATOM   1096 C  CD2 B LEU   A 1 125 ? 39.165 23.137  32.776 0.51 10.99 ? 125 LEU   A CD2 1 
ATOM   1097 N  N   . CYS   A 1 126 ? 35.707 25.097  30.513 1.00 9.33  ? 126 CYS   A N   1 
ATOM   1098 C  CA  . CYS   A 1 126 ? 34.535 25.575  31.284 1.00 9.83  ? 126 CYS   A CA  1 
ATOM   1099 C  C   . CYS   A 1 126 ? 33.238 25.237  30.546 1.00 10.52 ? 126 CYS   A C   1 
ATOM   1100 O  O   . CYS   A 1 126 ? 32.318 24.745  31.165 1.00 12.43 ? 126 CYS   A O   1 
ATOM   1101 C  CB  . CYS   A 1 126 ? 34.658 27.075  31.517 1.00 9.85  ? 126 CYS   A CB  1 
ATOM   1102 S  SG  . CYS   A 1 126 ? 35.962 27.496  32.714 1.00 12.91 ? 126 CYS   A SG  1 
ATOM   1103 N  N   . ASP   A 1 127 ? 33.203 25.501  29.250 1.00 9.73  ? 127 ASP   A N   1 
ATOM   1104 C  CA  . ASP   A 1 127 ? 32.002 25.187  28.437 1.00 12.14 ? 127 ASP   A CA  1 
ATOM   1105 C  C   . ASP   A 1 127 ? 31.745 23.676  28.420 1.00 12.13 ? 127 ASP   A C   1 
ATOM   1106 O  O   . ASP   A 1 127 ? 30.614 23.268  28.464 1.00 13.09 ? 127 ASP   A O   1 
ATOM   1107 C  CB  . ASP   A 1 127 ? 32.178 25.749  27.025 1.00 16.73 ? 127 ASP   A CB  1 
ATOM   1108 C  CG  . ASP   A 1 127 ? 31.203 25.165  26.010 1.00 20.49 ? 127 ASP   A CG  1 
ATOM   1109 O  OD1 . ASP   A 1 127 ? 30.090 25.672  25.932 1.00 21.25 ? 127 ASP   A OD1 1 
ATOM   1110 O  OD2 . ASP   A 1 127 ? 31.575 24.207  25.308 1.00 25.82 ? 127 ASP   A OD2 1 
ATOM   1111 N  N   . PHE   A 1 128 ? 32.811 22.915  28.292 1.00 10.65 ? 128 PHE   A N   1 
ATOM   1112 C  CA  . PHE   A 1 128 ? 32.679 21.440  28.264 1.00 8.33  ? 128 PHE   A CA  1 
ATOM   1113 C  C   . PHE   A 1 128 ? 31.959 20.955  29.534 1.00 9.83  ? 128 PHE   A C   1 
ATOM   1114 O  O   . PHE   A 1 128 ? 31.069 20.135  29.459 1.00 8.68  ? 128 PHE   A O   1 
ATOM   1115 C  CB  . PHE   A 1 128 ? 34.076 20.821  28.129 1.00 8.17  ? 128 PHE   A CB  1 
ATOM   1116 C  CG  . PHE   A 1 128 ? 34.136 19.334  28.365 1.00 8.57  ? 128 PHE   A CG  1 
ATOM   1117 C  CD1 . PHE   A 1 128 ? 33.889 18.443  27.337 1.00 10.26 ? 128 PHE   A CD1 1 
ATOM   1118 C  CD2 . PHE   A 1 128 ? 34.431 18.829  29.617 1.00 10.89 ? 128 PHE   A CD2 1 
ATOM   1119 C  CE1 . PHE   A 1 128 ? 33.941 17.075  27.553 1.00 10.65 ? 128 PHE   A CE1 1 
ATOM   1120 C  CE2 . PHE   A 1 128 ? 34.491 17.461  29.831 1.00 13.68 ? 128 PHE   A CE2 1 
ATOM   1121 C  CZ  . PHE   A 1 128 ? 34.250 16.589  28.799 1.00 10.33 ? 128 PHE   A CZ  1 
ATOM   1122 N  N   . LEU   A 1 129 ? 32.393 21.470  30.675 1.00 8.92  ? 129 LEU   A N   1 
ATOM   1123 C  CA  . LEU   A 1 129 ? 31.805 21.020  31.952 1.00 7.29  ? 129 LEU   A CA  1 
ATOM   1124 C  C   . LEU   A 1 129 ? 30.365 21.530  32.046 1.00 11.40 ? 129 LEU   A C   1 
ATOM   1125 O  O   . LEU   A 1 129 ? 29.499 20.809  32.492 1.00 10.96 ? 129 LEU   A O   1 
ATOM   1126 C  CB  . LEU   A 1 129 ? 32.670 21.565  33.094 1.00 9.99  ? 129 LEU   A CB  1 
ATOM   1127 C  CG  . LEU   A 1 129 ? 34.065 20.969  33.228 1.00 11.20 ? 129 LEU   A CG  1 
ATOM   1128 C  CD1 . LEU   A 1 129 ? 34.829 21.687  34.330 1.00 12.46 ? 129 LEU   A CD1 1 
ATOM   1129 C  CD2 . LEU   A 1 129 ? 33.995 19.477  33.514 1.00 13.29 ? 129 LEU   A CD2 1 
ATOM   1130 N  N   . GLU   A 1 130 ? 30.161 22.754  31.610 1.00 11.33 ? 130 GLU   A N   1 
ATOM   1131 C  CA  . GLU   A 1 130 ? 28.813 23.333  31.738 1.00 15.36 ? 130 GLU   A CA  1 
ATOM   1132 C  C   . GLU   A 1 130 ? 27.865 22.569  30.826 1.00 14.78 ? 130 GLU   A C   1 
ATOM   1133 O  O   . GLU   A 1 130 ? 26.748 22.257  31.250 1.00 20.79 ? 130 GLU   A O   1 
ATOM   1134 C  CB  . GLU   A 1 130 ? 28.848 24.791  31.290 1.00 14.76 ? 130 GLU   A CB  1 
ATOM   1135 C  CG  . GLU   A 1 130 ? 29.510 25.726  32.279 1.00 15.81 ? 130 GLU   A CG  1 
ATOM   1136 C  CD  . GLU   A 1 130 ? 29.953 27.046  31.671 1.00 26.20 ? 130 GLU   A CD  1 
ATOM   1137 O  OE1 . GLU   A 1 130 ? 29.538 27.344  30.537 1.00 25.28 ? 130 GLU   A OE1 1 
ATOM   1138 O  OE2 . GLU   A 1 130 ? 30.709 27.758  32.321 1.00 14.29 ? 130 GLU   A OE2 1 
ATOM   1139 N  N   . SER   A 1 131 ? 28.318 22.246  29.617 1.00 12.27 ? 131 SER   A N   1 
ATOM   1140 C  CA  . SER   A 1 131 ? 27.443 21.617  28.597 1.00 13.29 ? 131 SER   A CA  1 
ATOM   1141 C  C   . SER   A 1 131 ? 27.177 20.123  28.822 1.00 14.54 ? 131 SER   A C   1 
ATOM   1142 O  O   . SER   A 1 131 ? 26.136 19.651  28.401 1.00 17.62 ? 131 SER   A O   1 
ATOM   1143 C  CB  . SER   A 1 131 ? 28.030 21.846  27.226 1.00 19.95 ? 131 SER   A CB  1 
ATOM   1144 O  OG  . SER   A 1 131 ? 28.066 23.237  26.957 1.00 19.10 ? 131 SER   A OG  1 
ATOM   1145 N  N   . HIS   A 1 132 ? 28.112 19.410  29.425 1.00 13.08 ? 132 HIS   A N   1 
ATOM   1146 C  CA  . HIS   A 1 132 ? 27.950 17.943  29.543 1.00 14.82 ? 132 HIS   A CA  1 
ATOM   1147 C  C   . HIS   A 1 132 ? 27.930 17.410  30.988 1.00 13.11 ? 132 HIS   A C   1 
ATOM   1148 O  O   . HIS   A 1 132 ? 27.663 16.227  31.159 1.00 14.23 ? 132 HIS   A O   1 
ATOM   1149 C  CB  . HIS   A 1 132 ? 29.081 17.267  28.764 1.00 16.41 ? 132 HIS   A CB  1 
ATOM   1150 C  CG  . HIS   A 1 132 ? 29.080 17.644  27.334 1.00 18.57 ? 132 HIS   A CG  1 
ATOM   1151 N  ND1 . HIS   A 1 132 ? 27.992 17.398  26.529 1.00 24.97 ? 132 HIS   A ND1 1 
ATOM   1152 C  CD2 . HIS   A 1 132 ? 29.988 18.245  26.572 1.00 23.83 ? 132 HIS   A CD2 1 
ATOM   1153 C  CE1 . HIS   A 1 132 ? 28.252 17.845  25.312 1.00 27.62 ? 132 HIS   A CE1 1 
ATOM   1154 N  NE2 . HIS   A 1 132 ? 29.456 18.363  25.317 1.00 29.13 ? 132 HIS   A NE2 1 
ATOM   1155 N  N   . PHE   A 1 133 ? 28.233 18.241  31.987 1.00 10.30 ? 133 PHE   A N   1 
ATOM   1156 C  CA  . PHE   A 1 133 ? 28.335 17.689  33.364 1.00 8.01  ? 133 PHE   A CA  1 
ATOM   1157 C  C   . PHE   A 1 133 ? 27.541 18.449  34.434 1.00 10.32 ? 133 PHE   A C   1 
ATOM   1158 O  O   . PHE   A 1 133 ? 26.880 17.819  35.212 1.00 10.67 ? 133 PHE   A O   1 
ATOM   1159 C  CB  . PHE   A 1 133 ? 29.807 17.673  33.801 1.00 9.66  ? 133 PHE   A CB  1 
ATOM   1160 C  CG  . PHE   A 1 133 ? 30.600 16.603  33.099 1.00 7.31  ? 133 PHE   A CG  1 
ATOM   1161 C  CD1 . PHE   A 1 133 ? 31.111 16.812  31.830 1.00 12.08 ? 133 PHE   A CD1 1 
ATOM   1162 C  CD2 . PHE   A 1 133 ? 30.777 15.363  33.686 1.00 11.82 ? 133 PHE   A CD2 1 
ATOM   1163 C  CE1 . PHE   A 1 133 ? 31.803 15.807  31.176 1.00 11.11 ? 133 PHE   A CE1 1 
ATOM   1164 C  CE2 . PHE   A 1 133 ? 31.483 14.367  33.038 1.00 11.97 ? 133 PHE   A CE2 1 
ATOM   1165 C  CZ  . PHE   A 1 133 ? 31.985 14.588  31.782 1.00 10.69 ? 133 PHE   A CZ  1 
ATOM   1166 N  N   . LEU   A 1 134 ? 27.626 19.773  34.427 1.00 11.78 ? 134 LEU   A N   1 
ATOM   1167 C  CA  . LEU   A 1 134 ? 27.049 20.529  35.583 1.00 8.18  ? 134 LEU   A CA  1 
ATOM   1168 C  C   . LEU   A 1 134 ? 25.525 20.351  35.692 1.00 9.45  ? 134 LEU   A C   1 
ATOM   1169 O  O   . LEU   A 1 134 ? 25.052 20.168  36.796 1.00 8.49  ? 134 LEU   A O   1 
ATOM   1170 C  CB  . LEU   A 1 134 ? 27.452 22.010  35.494 1.00 9.25  ? 134 LEU   A CB  1 
ATOM   1171 C  CG  . LEU   A 1 134 ? 28.941 22.338  35.532 1.00 12.52 ? 134 LEU   A CG  1 
ATOM   1172 C  CD1 . LEU   A 1 134 ? 29.127 23.843  35.595 1.00 12.89 ? 134 LEU   A CD1 1 
ATOM   1173 C  CD2 . LEU   A 1 134 ? 29.616 21.680  36.717 1.00 10.89 ? 134 LEU   A CD2 1 
ATOM   1174 N  N   . ASP   A 1 135 ? 24.812 20.522  34.586 1.00 11.79 ? 135 ASP   A N   1 
ATOM   1175 C  CA  . ASP   A 1 135 ? 23.340 20.390  34.692 1.00 11.32 ? 135 ASP   A CA  1 
ATOM   1176 C  C   . ASP   A 1 135 ? 22.942 18.913  34.855 1.00 10.69 ? 135 ASP   A C   1 
ATOM   1177 O  O   . ASP   A 1 135 ? 21.997 18.630  35.543 1.00 10.74 ? 135 ASP   A O   1 
ATOM   1178 C  CB  . ASP   A 1 135 ? 22.628 21.039  33.498 1.00 13.34 ? 135 ASP   A CB  1 
ATOM   1179 C  CG  . ASP   A 1 135 ? 21.124 21.051  33.667 1.00 16.46 ? 135 ASP   A CG  1 
ATOM   1180 O  OD1 . ASP   A 1 135 ? 20.666 21.515  34.711 1.00 14.78 ? 135 ASP   A OD1 1 
ATOM   1181 O  OD2 . ASP   A 1 135 ? 20.444 20.568  32.762 1.00 21.34 ? 135 ASP   A OD2 1 
ATOM   1182 N  N   . GLU   A 1 136 ? 23.692 18.026  34.219 1.00 10.26 ? 136 GLU   A N   1 
ATOM   1183 C  CA  . GLU   A 1 136 ? 23.403 16.591  34.427 1.00 12.11 ? 136 GLU   A CA  1 
ATOM   1184 C  C   . GLU   A 1 136 ? 23.523 16.258  35.919 1.00 11.94 ? 136 GLU   A C   1 
ATOM   1185 O  O   . GLU   A 1 136 ? 22.677 15.530  36.395 1.00 11.81 ? 136 GLU   A O   1 
ATOM   1186 C  CB  . GLU   A 1 136 ? 24.352 15.746  33.573 1.00 14.20 ? 136 GLU   A CB  1 
ATOM   1187 C  CG  . GLU   A 1 136 ? 24.175 15.975  32.081 1.00 20.42 ? 136 GLU   A CG  1 
ATOM   1188 C  CD  . GLU   A 1 136 ? 22.767 15.724  31.573 1.00 32.08 ? 136 GLU   A CD  1 
ATOM   1189 O  OE1 . GLU   A 1 136 ? 22.280 14.590  31.721 1.00 37.28 ? 136 GLU   A OE1 1 
ATOM   1190 O  OE2 . GLU   A 1 136 ? 22.161 16.663  31.036 1.00 42.42 ? 136 GLU   A OE2 1 
ATOM   1191 N  N   A GLU   A 1 137 ? 24.531 16.796  36.563 0.74 9.79  ? 137 GLU   A N   1 
ATOM   1192 N  N   B GLU   A 1 137 ? 24.564 16.758  36.569 0.26 9.80  ? 137 GLU   A N   1 
ATOM   1193 C  CA  A GLU   A 1 137 ? 24.714 16.494  37.986 0.74 9.18  ? 137 GLU   A CA  1 
ATOM   1194 C  CA  B GLU   A 1 137 ? 24.734 16.495  38.012 0.26 9.30  ? 137 GLU   A CA  1 
ATOM   1195 C  C   A GLU   A 1 137 ? 23.554 17.121  38.764 0.74 8.81  ? 137 GLU   A C   1 
ATOM   1196 C  C   B GLU   A 1 137 ? 23.548 17.113  38.752 0.26 8.88  ? 137 GLU   A C   1 
ATOM   1197 O  O   A GLU   A 1 137 ? 23.036 16.497  39.668 0.74 9.92  ? 137 GLU   A O   1 
ATOM   1198 O  O   B GLU   A 1 137 ? 23.037 16.483  39.677 0.26 9.89  ? 137 GLU   A O   1 
ATOM   1199 C  CB  A GLU   A 1 137 ? 26.106 16.995  38.393 0.74 10.79 ? 137 GLU   A CB  1 
ATOM   1200 C  CB  B GLU   A 1 137 ? 26.062 17.079  38.501 0.26 10.73 ? 137 GLU   A CB  1 
ATOM   1201 C  CG  A GLU   A 1 137 ? 26.584 16.490  39.722 0.74 9.31  ? 137 GLU   A CG  1 
ATOM   1202 C  CG  B GLU   A 1 137 ? 27.183 16.077  38.656 0.26 10.86 ? 137 GLU   A CG  1 
ATOM   1203 C  CD  A GLU   A 1 137 ? 26.577 14.980  39.791 0.74 8.45  ? 137 GLU   A CD  1 
ATOM   1204 C  CD  B GLU   A 1 137 ? 26.752 14.732  39.204 0.26 10.76 ? 137 GLU   A CD  1 
ATOM   1205 O  OE1 A GLU   A 1 137 ? 26.876 14.331  38.773 0.74 12.22 ? 137 GLU   A OE1 1 
ATOM   1206 O  OE1 B GLU   A 1 137 ? 26.382 14.664  40.392 0.26 11.56 ? 137 GLU   A OE1 1 
ATOM   1207 O  OE2 A GLU   A 1 137 ? 26.247 14.482  40.849 0.74 14.85 ? 137 GLU   A OE2 1 
ATOM   1208 O  OE2 B GLU   A 1 137 ? 26.789 13.767  38.436 0.26 14.21 ? 137 GLU   A OE2 1 
ATOM   1209 N  N   . VAL   A 1 138 ? 23.252 18.380  38.462 1.00 7.74  ? 138 VAL   A N   1 
ATOM   1210 C  CA  . VAL   A 1 138 ? 22.162 19.036  39.232 1.00 9.06  ? 138 VAL   A CA  1 
ATOM   1211 C  C   . VAL   A 1 138 ? 20.852 18.242  39.078 1.00 9.45  ? 138 VAL   A C   1 
ATOM   1212 O  O   . VAL   A 1 138 ? 20.168 18.067  40.056 1.00 8.75  ? 138 VAL   A O   1 
ATOM   1213 C  CB  . VAL   A 1 138 ? 22.016 20.513  38.808 1.00 6.57  ? 138 VAL   A CB  1 
ATOM   1214 C  CG1 . VAL   A 1 138 ? 20.626 21.054  39.123 1.00 10.21 ? 138 VAL   A CG1 1 
ATOM   1215 C  CG2 . VAL   A 1 138 ? 23.061 21.384  39.488 1.00 8.16  ? 138 VAL   A CG2 1 
ATOM   1216 N  N   . LYS   A 1 139 ? 20.553 17.824  37.862 1.00 7.67  ? 139 LYS   A N   1 
ATOM   1217 C  CA  . LYS   A 1 139 ? 19.301 17.064  37.607 1.00 8.32  ? 139 LYS   A CA  1 
ATOM   1218 C  C   . LYS   A 1 139 ? 19.324 15.749  38.403 1.00 8.77  ? 139 LYS   A C   1 
ATOM   1219 O  O   . LYS   A 1 139 ? 18.305 15.366  38.939 1.00 10.20 ? 139 LYS   A O   1 
ATOM   1220 C  CB  . LYS   A 1 139 ? 19.129 16.851  36.100 1.00 9.79  ? 139 LYS   A CB  1 
ATOM   1221 C  CG  . LYS   A 1 139 ? 18.675 18.070  35.316 1.00 14.28 ? 139 LYS   A CG  1 
ATOM   1222 C  CD  . LYS   A 1 139 ? 18.521 17.782  33.845 1.00 20.65 ? 139 LYS   A CD  1 
ATOM   1223 C  CE  . LYS   A 1 139 ? 19.714 17.085  33.231 1.00 26.25 ? 139 LYS   A CE  1 
ATOM   1224 N  NZ  . LYS   A 1 139 ? 19.387 16.515  31.901 1.00 35.46 ? 139 LYS   A NZ  1 
ATOM   1225 N  N   . LEU   A 1 140 ? 20.476 15.094  38.436 1.00 9.70  ? 140 LEU   A N   1 
ATOM   1226 C  CA  . LEU   A 1 140 ? 20.530 13.785  39.131 1.00 8.96  ? 140 LEU   A CA  1 
ATOM   1227 C  C   . LEU   A 1 140 ? 20.389 13.959  40.646 1.00 10.32 ? 140 LEU   A C   1 
ATOM   1228 O  O   . LEU   A 1 140 ? 19.719 13.171  41.264 1.00 10.01 ? 140 LEU   A O   1 
ATOM   1229 C  CB  . LEU   A 1 140 ? 21.849 13.106  38.759 1.00 9.64  ? 140 LEU   A CB  1 
ATOM   1230 C  CG  . LEU   A 1 140 ? 22.115 11.772  39.452 1.00 9.10  ? 140 LEU   A CG  1 
ATOM   1231 C  CD1 . LEU   A 1 140 ? 21.022 10.766  39.125 1.00 10.77 ? 140 LEU   A CD1 1 
ATOM   1232 C  CD2 . LEU   A 1 140 ? 23.476 11.233  39.052 1.00 11.86 ? 140 LEU   A CD2 1 
ATOM   1233 N  N   . ILE   A 1 141 ? 21.051 14.974  41.189 1.00 8.00  ? 141 ILE   A N   1 
ATOM   1234 C  CA  . ILE   A 1 141 ? 20.968 15.213  42.651 1.00 8.09  ? 141 ILE   A CA  1 
ATOM   1235 C  C   . ILE   A 1 141 ? 19.516 15.579  43.022 1.00 9.25  ? 141 ILE   A C   1 
ATOM   1236 O  O   . ILE   A 1 141 ? 19.050 15.153  44.046 1.00 9.65  ? 141 ILE   A O   1 
ATOM   1237 C  CB  . ILE   A 1 141 ? 22.020 16.252  43.084 1.00 9.48  ? 141 ILE   A CB  1 
ATOM   1238 C  CG1 . ILE   A 1 141 ? 23.427 15.678  42.880 1.00 9.20  ? 141 ILE   A CG1 1 
ATOM   1239 C  CG2 . ILE   A 1 141 ? 21.790 16.696  44.517 1.00 12.73 ? 141 ILE   A CG2 1 
ATOM   1240 C  CD1 . ILE   A 1 141 ? 24.560 16.659  43.081 1.00 9.26  ? 141 ILE   A CD1 1 
ATOM   1241 N  N   . LYS   A 1 142 ? 18.864 16.318  42.135 1.00 8.06  ? 142 LYS   A N   1 
ATOM   1242 C  CA  . LYS   A 1 142 ? 17.454 16.672  42.424 1.00 9.15  ? 142 LYS   A CA  1 
ATOM   1243 C  C   . LYS   A 1 142 ? 16.592 15.402  42.433 1.00 8.46  ? 142 LYS   A C   1 
ATOM   1244 O  O   . LYS   A 1 142 ? 15.762 15.259  43.292 1.00 9.53  ? 142 LYS   A O   1 
ATOM   1245 C  CB  . LYS   A 1 142 ? 16.956 17.712  41.418 1.00 8.17  ? 142 LYS   A CB  1 
ATOM   1246 C  CG  . LYS   A 1 142 ? 15.457 17.993  41.470 1.00 7.14  ? 142 LYS   A CG  1 
ATOM   1247 C  CD  . LYS   A 1 142 ? 15.005 18.574  42.790 1.00 7.95  ? 142 LYS   A CD  1 
ATOM   1248 C  CE  . LYS   A 1 142 ? 13.655 19.254  42.710 1.00 8.24  ? 142 LYS   A CE  1 
ATOM   1249 N  NZ  . LYS   A 1 142 ? 12.560 18.284  42.467 1.00 8.02  ? 142 LYS   A NZ  1 
ATOM   1250 N  N   . LYS   A 1 143 ? 16.840 14.533  41.482 1.00 9.26  ? 143 LYS   A N   1 
ATOM   1251 C  CA  . LYS   A 1 143 ? 16.068 13.267  41.420 1.00 8.97  ? 143 LYS   A CA  1 
ATOM   1252 C  C   . LYS   A 1 143 ? 16.305 12.455  42.692 1.00 9.71  ? 143 LYS   A C   1 
ATOM   1253 O  O   . LYS   A 1 143 ? 15.391 11.872  43.225 1.00 9.53  ? 143 LYS   A O   1 
ATOM   1254 C  CB  . LYS   A 1 143 ? 16.515 12.506  40.168 1.00 9.98  ? 143 LYS   A CB  1 
ATOM   1255 C  CG  . LYS   A 1 143 ? 15.885 11.136  39.985 1.00 12.50 ? 143 LYS   A CG  1 
ATOM   1256 C  CD  . LYS   A 1 143 ? 14.388 11.201  40.025 1.00 24.18 ? 143 LYS   A CD  1 
ATOM   1257 C  CE  . LYS   A 1 143 ? 13.791 11.780  38.765 1.00 31.87 ? 143 LYS   A CE  1 
ATOM   1258 N  NZ  . LYS   A 1 143 ? 12.314 11.828  38.858 1.00 32.32 ? 143 LYS   A NZ  1 
ATOM   1259 N  N   . MET   A 1 144 ? 17.555 12.407  43.086 1.00 10.01 ? 144 MET   A N   1 
ATOM   1260 C  CA  . MET   A 1 144 ? 17.904 11.599  44.285 1.00 8.71  ? 144 MET   A CA  1 
ATOM   1261 C  C   . MET   A 1 144 ? 17.303 12.220  45.548 1.00 9.32  ? 144 MET   A C   1 
ATOM   1262 O  O   . MET   A 1 144 ? 16.919 11.490  46.428 1.00 11.16 ? 144 MET   A O   1 
ATOM   1263 C  CB  . MET   A 1 144 ? 19.427 11.471  44.447 1.00 9.13  ? 144 MET   A CB  1 
ATOM   1264 C  CG  . MET   A 1 144 ? 20.065 10.525  43.474 1.00 9.63  ? 144 MET   A CG  1 
ATOM   1265 S  SD  . MET   A 1 144 ? 21.855 10.521  43.747 1.00 10.60 ? 144 MET   A SD  1 
ATOM   1266 C  CE  . MET   A 1 144 ? 22.331 9.239   42.589 1.00 10.43 ? 144 MET   A CE  1 
ATOM   1267 N  N   . GLY   A 1 145 ? 17.301 13.543  45.625 1.00 8.92  ? 145 GLY   A N   1 
ATOM   1268 C  CA  . GLY   A 1 145 ? 16.620 14.157  46.776 1.00 8.40  ? 145 GLY   A CA  1 
ATOM   1269 C  C   . GLY   A 1 145 ? 15.113 13.854  46.781 1.00 7.07  ? 145 GLY   A C   1 
ATOM   1270 O  O   . GLY   A 1 145 ? 14.578 13.666  47.839 1.00 8.52  ? 145 GLY   A O   1 
ATOM   1271 N  N   . ASP   A 1 146 ? 14.503 13.897  45.602 1.00 8.10  ? 146 ASP   A N   1 
ATOM   1272 C  CA  . ASP   A 1 146 ? 13.063 13.581  45.490 1.00 8.35  ? 146 ASP   A CA  1 
ATOM   1273 C  C   . ASP   A 1 146 ? 12.865 12.150  45.986 1.00 8.46  ? 146 ASP   A C   1 
ATOM   1274 O  O   . ASP   A 1 146 ? 11.949 11.901  46.741 1.00 8.29  ? 146 ASP   A O   1 
ATOM   1275 C  CB  . ASP   A 1 146 ? 12.625 13.711  44.032 1.00 7.27  ? 146 ASP   A CB  1 
ATOM   1276 C  CG  . ASP   A 1 146 ? 12.593 15.118  43.447 1.00 8.86  ? 146 ASP   A CG  1 
ATOM   1277 O  OD1 . ASP   A 1 146 ? 12.725 16.085  44.197 1.00 8.21  ? 146 ASP   A OD1 1 
ATOM   1278 O  OD2 . ASP   A 1 146 ? 12.436 15.217  42.225 1.00 11.94 ? 146 ASP   A OD2 1 
ATOM   1279 N  N   . HIS   A 1 147 ? 13.749 11.264  45.544 1.00 9.49  ? 147 HIS   A N   1 
ATOM   1280 C  CA  . HIS   A 1 147 ? 13.650 9.846   45.980 1.00 8.74  ? 147 HIS   A CA  1 
ATOM   1281 C  C   . HIS   A 1 147 ? 13.806 9.746   47.505 1.00 9.81  ? 147 HIS   A C   1 
ATOM   1282 O  O   . HIS   A 1 147 ? 13.023 9.045   48.113 1.00 8.81  ? 147 HIS   A O   1 
ATOM   1283 C  CB  . HIS   A 1 147 ? 14.673 8.943   45.249 1.00 7.87  ? 147 HIS   A CB  1 
ATOM   1284 C  CG  . HIS   A 1 147 ? 14.387 8.675   43.814 1.00 9.61  ? 147 HIS   A CG  1 
ATOM   1285 N  ND1 . HIS   A 1 147 ? 13.156 8.895   43.246 1.00 10.00 ? 147 HIS   A ND1 1 
ATOM   1286 C  CD2 . HIS   A 1 147 ? 15.180 8.188   42.837 1.00 9.78  ? 147 HIS   A CD2 1 
ATOM   1287 C  CE1 . HIS   A 1 147 ? 13.203 8.556   41.978 1.00 9.84  ? 147 HIS   A CE1 1 
ATOM   1288 N  NE2 . HIS   A 1 147 ? 14.436 8.118   41.701 1.00 10.22 ? 147 HIS   A NE2 1 
ATOM   1289 N  N   A LEU   A 1 148 ? 14.821 10.421  48.055 0.64 9.39  ? 148 LEU   A N   1 
ATOM   1290 N  N   B LEU   A 1 148 ? 14.824 10.410  48.054 0.36 9.41  ? 148 LEU   A N   1 
ATOM   1291 C  CA  A LEU   A 1 148 ? 15.050 10.339  49.516 0.64 7.82  ? 148 LEU   A CA  1 
ATOM   1292 C  CA  B LEU   A 1 148 ? 15.062 10.332  49.515 0.36 7.91  ? 148 LEU   A CA  1 
ATOM   1293 C  C   A LEU   A 1 148 ? 13.779 10.759  50.257 0.64 10.35 ? 148 LEU   A C   1 
ATOM   1294 C  C   B LEU   A 1 148 ? 13.784 10.745  50.241 0.36 10.37 ? 148 LEU   A C   1 
ATOM   1295 O  O   A LEU   A 1 148 ? 13.410 10.120  51.219 0.64 10.36 ? 148 LEU   A O   1 
ATOM   1296 O  O   B LEU   A 1 148 ? 13.425 10.096  51.228 0.36 10.43 ? 148 LEU   A O   1 
ATOM   1297 C  CB  A LEU   A 1 148 ? 16.240 11.238  49.901 0.64 11.26 ? 148 LEU   A CB  1 
ATOM   1298 C  CB  B LEU   A 1 148 ? 16.221 11.267  49.874 0.36 11.32 ? 148 LEU   A CB  1 
ATOM   1299 C  CG  A LEU   A 1 148 ? 17.629 10.635  49.711 0.64 13.69 ? 148 LEU   A CG  1 
ATOM   1300 C  CG  B LEU   A 1 148 ? 17.129 10.788  51.002 0.36 19.30 ? 148 LEU   A CG  1 
ATOM   1301 C  CD1 A LEU   A 1 148 ? 18.705 11.681  49.964 0.64 16.20 ? 148 LEU   A CD1 1 
ATOM   1302 C  CD1 B LEU   A 1 148 ? 17.796 9.475   50.631 0.36 17.59 ? 148 LEU   A CD1 1 
ATOM   1303 C  CD2 A LEU   A 1 148 ? 17.823 9.447   50.634 0.64 17.74 ? 148 LEU   A CD2 1 
ATOM   1304 C  CD2 B LEU   A 1 148 ? 18.177 11.840  51.327 0.36 16.52 ? 148 LEU   A CD2 1 
ATOM   1305 N  N   . THR   A 1 149 ? 13.184 11.842  49.795 1.00 8.21  ? 149 THR   A N   1 
ATOM   1306 C  CA  . THR   A 1 149 ? 11.989 12.359  50.494 1.00 9.19  ? 149 THR   A CA  1 
ATOM   1307 C  C   . THR   A 1 149 ? 10.857 11.323  50.454 1.00 8.75  ? 149 THR   A C   1 
ATOM   1308 O  O   . THR   A 1 149 ? 10.173 11.153  51.440 1.00 10.88 ? 149 THR   A O   1 
ATOM   1309 C  CB  . THR   A 1 149 ? 11.582 13.691  49.856 1.00 8.39  ? 149 THR   A CB  1 
ATOM   1310 O  OG1 . THR   A 1 149 ? 12.597 14.650  50.136 1.00 8.22  ? 149 THR   A OG1 1 
ATOM   1311 C  CG2 . THR   A 1 149 ? 10.240 14.187  50.350 1.00 8.93  ? 149 THR   A CG2 1 
ATOM   1312 N  N   . ASN   A 1 150 ? 10.679 10.692  49.309 1.00 9.23  ? 150 ASN   A N   1 
ATOM   1313 C  CA  . ASN   A 1 150 ? 9.603  9.687   49.181 1.00 8.40  ? 150 ASN   A CA  1 
ATOM   1314 C  C   . ASN   A 1 150 ? 9.947  8.437   50.006 1.00 8.19  ? 150 ASN   A C   1 
ATOM   1315 O  O   . ASN   A 1 150 ? 9.073  7.881   50.629 1.00 8.86  ? 150 ASN   A O   1 
ATOM   1316 C  CB  . ASN   A 1 150 ? 9.352  9.363   47.708 1.00 7.46  ? 150 ASN   A CB  1 
ATOM   1317 C  CG  . ASN   A 1 150 ? 8.455  10.402  47.073 1.00 7.61  ? 150 ASN   A CG  1 
ATOM   1318 O  OD1 . ASN   A 1 150 ? 7.253  10.380  47.278 1.00 8.18  ? 150 ASN   A OD1 1 
ATOM   1319 N  ND2 . ASN   A 1 150 ? 9.039  11.330  46.341 1.00 8.88  ? 150 ASN   A ND2 1 
ATOM   1320 N  N   . ILE   A 1 151 ? 11.209 8.030   49.965 1.00 8.57  ? 151 ILE   A N   1 
ATOM   1321 C  CA  . ILE   A 1 151 ? 11.604 6.859   50.785 1.00 9.22  ? 151 ILE   A CA  1 
ATOM   1322 C  C   . ILE   A 1 151 ? 11.343 7.183   52.254 1.00 10.85 ? 151 ILE   A C   1 
ATOM   1323 O  O   . ILE   A 1 151 ? 10.805 6.350   52.950 1.00 10.93 ? 151 ILE   A O   1 
ATOM   1324 C  CB  . ILE   A 1 151 ? 13.089 6.537   50.502 1.00 8.99  ? 151 ILE   A CB  1 
ATOM   1325 C  CG1 . ILE   A 1 151 ? 13.305 5.986   49.092 1.00 10.73 ? 151 ILE   A CG1 1 
ATOM   1326 C  CG2 . ILE   A 1 151 ? 13.635 5.597   51.568 1.00 10.82 ? 151 ILE   A CG2 1 
ATOM   1327 C  CD1 . ILE   A 1 151 ? 14.733 6.092   48.612 1.00 12.58 ? 151 ILE   A CD1 1 
ATOM   1328 N  N   . GLN   A 1 152 ? 11.711 8.386   52.668 1.00 10.38 ? 152 GLN   A N   1 
ATOM   1329 C  CA  . GLN   A 1 152 ? 11.587 8.762   54.104 1.00 10.14 ? 152 GLN   A CA  1 
ATOM   1330 C  C   . GLN   A 1 152 ? 10.107 8.827   54.527 1.00 13.86 ? 152 GLN   A C   1 
ATOM   1331 O  O   . GLN   A 1 152 ? 9.765  8.373   55.610 1.00 16.33 ? 152 GLN   A O   1 
ATOM   1332 C  CB  . GLN   A 1 152 ? 12.327 10.079  54.361 1.00 13.77 ? 152 GLN   A CB  1 
ATOM   1333 C  CG  . GLN   A 1 152 ? 13.835 10.002  54.145 1.00 20.90 ? 152 GLN   A CG  1 
ATOM   1334 C  CD  . GLN   A 1 152 ? 14.528 11.342  54.052 1.00 28.19 ? 152 GLN   A CD  1 
ATOM   1335 O  OE1 . GLN   A 1 152 ? 15.666 11.501  54.481 1.00 30.78 ? 152 GLN   A OE1 1 
ATOM   1336 N  NE2 . GLN   A 1 152 ? 13.853 12.320  53.475 1.00 24.96 ? 152 GLN   A NE2 1 
ATOM   1337 N  N   . ARG   A 1 153 ? 9.277  9.379   53.662 1.00 12.25 ? 153 ARG   A N   1 
ATOM   1338 C  CA  A ARG   A 1 153 ? 7.818  9.432   53.955 0.54 12.68 ? 153 ARG   A CA  1 
ATOM   1339 C  CA  B ARG   A 1 153 ? 7.821  9.432   53.977 0.46 12.70 ? 153 ARG   A CA  1 
ATOM   1340 C  C   . ARG   A 1 153 ? 7.164  8.031   54.116 1.00 15.74 ? 153 ARG   A C   1 
ATOM   1341 O  O   . ARG   A 1 153 ? 6.221  7.750   54.909 1.00 16.87 ? 153 ARG   A O   1 
ATOM   1342 C  CB  A ARG   A 1 153 ? 7.112  10.176  52.817 0.54 16.14 ? 153 ARG   A CB  1 
ATOM   1343 C  CB  B ARG   A 1 153 ? 7.103  10.303  52.938 0.46 16.16 ? 153 ARG   A CB  1 
ATOM   1344 C  CG  A ARG   A 1 153 ? 5.782  10.805  53.207 0.54 17.49 ? 153 ARG   A CG  1 
ATOM   1345 C  CG  B ARG   A 1 153 ? 6.716  9.622   51.636 0.46 13.83 ? 153 ARG   A CG  1 
ATOM   1346 C  CD  A ARG   A 1 153 ? 5.267  11.866  52.249 0.54 19.21 ? 153 ARG   A CD  1 
ATOM   1347 C  CD  B ARG   A 1 153 ? 5.730  10.479  50.854 0.46 10.84 ? 153 ARG   A CD  1 
ATOM   1348 N  NE  A ARG   A 1 153 ? 5.903  11.807  50.947 0.54 17.14 ? 153 ARG   A NE  1 
ATOM   1349 N  NE  B ARG   A 1 153 ? 5.750  11.900  51.182 0.46 15.21 ? 153 ARG   A NE  1 
ATOM   1350 C  CZ  A ARG   A 1 153 ? 6.380  12.853  50.288 0.54 14.34 ? 153 ARG   A CZ  1 
ATOM   1351 C  CZ  B ARG   A 1 153 ? 6.295  12.848  50.425 0.46 14.14 ? 153 ARG   A CZ  1 
ATOM   1352 N  NH1 A ARG   A 1 153 ? 6.286  14.066  50.806 0.54 16.08 ? 153 ARG   A NH1 1 
ATOM   1353 N  NH1 B ARG   A 1 153 ? 6.884  12.536  49.281 0.46 11.46 ? 153 ARG   A NH1 1 
ATOM   1354 N  NH2 A ARG   A 1 153 ? 6.952  12.677  49.110 0.54 9.21  ? 153 ARG   A NH2 1 
ATOM   1355 N  NH2 B ARG   A 1 153 ? 6.257  14.108  50.820 0.46 15.91 ? 153 ARG   A NH2 1 
ATOM   1356 N  N   . LEU   A 1 154 ? 7.811  7.070   53.467 1.00 14.00 ? 154 LEU   A N   1 
ATOM   1357 C  CA  . LEU   A 1 154 ? 7.279  5.676   53.432 1.00 14.26 ? 154 LEU   A CA  1 
ATOM   1358 C  C   . LEU   A 1 154 ? 7.785  4.808   54.599 1.00 20.00 ? 154 LEU   A C   1 
ATOM   1359 O  O   . LEU   A 1 154 ? 7.287  3.700   54.748 1.00 21.51 ? 154 LEU   A O   1 
ATOM   1360 C  CB  . LEU   A 1 154 ? 7.630  5.023   52.095 1.00 13.80 ? 154 LEU   A CB  1 
ATOM   1361 C  CG  . LEU   A 1 154 ? 6.714  5.363   50.922 1.00 9.58  ? 154 LEU   A CG  1 
ATOM   1362 C  CD1 . LEU   A 1 154 ? 7.328  4.916   49.606 1.00 12.51 ? 154 LEU   A CD1 1 
ATOM   1363 C  CD2 . LEU   A 1 154 ? 5.340  4.739   51.106 1.00 15.12 ? 154 LEU   A CD2 1 
ATOM   1364 N  N   . VAL   A 1 155 ? 8.709  5.303   55.396 1.00 19.31 ? 155 VAL   A N   1 
ATOM   1365 C  CA  . VAL   A 1 155 ? 9.295  4.477   56.489 1.00 21.71 ? 155 VAL   A CA  1 
ATOM   1366 C  C   . VAL   A 1 155 ? 8.239  4.264   57.569 1.00 38.33 ? 155 VAL   A C   1 
ATOM   1367 O  O   . VAL   A 1 155 ? 7.850  3.113   57.825 1.00 31.58 ? 155 VAL   A O   1 
ATOM   1368 C  CB  . VAL   A 1 155 ? 10.507 5.178   57.101 1.00 25.01 ? 155 VAL   A CB  1 
ATOM   1369 C  CG1 . VAL   A 1 155 ? 10.966 4.434   58.345 1.00 27.70 ? 155 VAL   A CG1 1 
ATOM   1370 C  CG2 . VAL   A 1 155 ? 11.652 5.281   56.101 1.00 22.26 ? 155 VAL   A CG2 1 
ATOM   1371 N  N   . GLY   A 1 156 ? 7.784  5.377   58.137 1.00 33.15 ? 156 GLY   A N   1 
ATOM   1372 C  CA  . GLY   A 1 156 ? 6.740  5.287   59.165 1.00 47.93 ? 156 GLY   A CA  1 
ATOM   1373 C  C   . GLY   A 1 156 ? 6.985  4.152   60.141 1.00 45.79 ? 156 GLY   A C   1 
ATOM   1374 O  O   . GLY   A 1 156 ? 8.085  4.101   60.678 1.00 44.99 ? 156 GLY   A O   1 
ATOM   1375 N  N   . SER   A 1 157 ? 5.968  3.317   60.362 1.00 57.17 ? 157 SER   A N   1 
ATOM   1376 C  CA  . SER   A 1 157 ? 6.041  2.176   61.306 1.00 62.46 ? 157 SER   A CA  1 
ATOM   1377 C  C   . SER   A 1 157 ? 6.044  0.861   60.527 1.00 62.12 ? 157 SER   A C   1 
ATOM   1378 O  O   . SER   A 1 157 ? 6.046  -0.194  61.170 1.00 59.85 ? 157 SER   A O   1 
ATOM   1379 C  CB  . SER   A 1 157 ? 4.851  2.236   62.211 1.00 62.35 ? 157 SER   A CB  1 
ATOM   1380 O  OG  . SER   A 1 157 ? 3.652  2.210   61.452 1.00 59.20 ? 157 SER   A OG  1 
ATOM   1381 N  N   . GLN   A 1 158 ? 6.073  0.937   59.195 1.00 42.80 ? 158 GLN   A N   1 
ATOM   1382 C  CA  . GLN   A 1 158 ? 6.037  -0.263  58.325 1.00 38.83 ? 158 GLN   A CA  1 
ATOM   1383 C  C   . GLN   A 1 158 ? 7.160  -0.117  57.291 1.00 25.21 ? 158 GLN   A C   1 
ATOM   1384 O  O   . GLN   A 1 158 ? 6.843  0.123   56.127 1.00 19.75 ? 158 GLN   A O   1 
ATOM   1385 C  CB  . GLN   A 1 158 ? 4.648  -0.369  57.702 1.00 35.92 ? 158 GLN   A CB  1 
ATOM   1386 C  CG  . GLN   A 1 158 ? 3.514  -0.325  58.714 1.00 46.99 ? 158 GLN   A CG  1 
ATOM   1387 C  CD  . GLN   A 1 158 ? 2.211  -0.810  58.127 1.00 42.59 ? 158 GLN   A CD  1 
ATOM   1388 N  N   . ALA   A 1 159 ? 8.409  -0.316  57.690 1.00 26.52 ? 159 ALA   A N   1 
ATOM   1389 C  CA  . ALA   A 1 159 ? 9.557  -0.019  56.787 1.00 20.33 ? 159 ALA   A CA  1 
ATOM   1390 C  C   . ALA   A 1 159 ? 9.626  -0.954  55.569 1.00 15.13 ? 159 ALA   A C   1 
ATOM   1391 O  O   . ALA   A 1 159 ? 9.937  -0.471  54.506 1.00 13.92 ? 159 ALA   A O   1 
ATOM   1392 C  CB  . ALA   A 1 159 ? 10.837 -0.079  57.578 1.00 19.79 ? 159 ALA   A CB  1 
ATOM   1393 N  N   . GLY   A 1 160 ? 9.369  -2.242  55.781 1.00 16.62 ? 160 GLY   A N   1 
ATOM   1394 C  CA  . GLY   A 1 160 ? 9.456  -3.195  54.660 1.00 13.63 ? 160 GLY   A CA  1 
ATOM   1395 C  C   . GLY   A 1 160 ? 8.391  -2.892  53.617 1.00 10.41 ? 160 GLY   A C   1 
ATOM   1396 O  O   . GLY   A 1 160 ? 8.683  -2.920  52.466 1.00 12.44 ? 160 GLY   A O   1 
ATOM   1397 N  N   . LEU   A 1 161 ? 7.193  -2.625  54.104 1.00 11.96 ? 161 LEU   A N   1 
ATOM   1398 C  CA  . LEU   A 1 161 ? 6.077  -2.265  53.198 1.00 11.39 ? 161 LEU   A CA  1 
ATOM   1399 C  C   . LEU   A 1 161 ? 6.450  -1.021  52.375 1.00 10.13 ? 161 LEU   A C   1 
ATOM   1400 O  O   . LEU   A 1 161 ? 6.250  -1.029  51.185 1.00 10.90 ? 161 LEU   A O   1 
ATOM   1401 C  CB  . LEU   A 1 161 ? 4.839  -2.014  54.064 1.00 13.77 ? 161 LEU   A CB  1 
ATOM   1402 C  CG  . LEU   A 1 161 ? 3.658  -1.341  53.374 1.00 13.33 ? 161 LEU   A CG  1 
ATOM   1403 C  CD1 . LEU   A 1 161 ? 3.084  -2.257  52.309 1.00 14.15 ? 161 LEU   A CD1 1 
ATOM   1404 C  CD2 . LEU   A 1 161 ? 2.588  -0.976  54.392 1.00 18.20 ? 161 LEU   A CD2 1 
ATOM   1405 N  N   . GLY   A 1 162 ? 6.983  -0.008  53.048 1.00 11.33 ? 162 GLY   A N   1 
ATOM   1406 C  CA  . GLY   A 1 162 ? 7.352  1.218   52.316 1.00 10.17 ? 162 GLY   A CA  1 
ATOM   1407 C  C   . GLY   A 1 162 ? 8.471  0.985   51.311 1.00 10.31 ? 162 GLY   A C   1 
ATOM   1408 O  O   . GLY   A 1 162 ? 8.462  1.583   50.274 1.00 12.11 ? 162 GLY   A O   1 
ATOM   1409 N  N   . GLU   A 1 163 ? 9.411  0.130   51.676 1.00 8.56  ? 163 GLU   A N   1 
ATOM   1410 C  CA  . GLU   A 1 163 ? 10.562 -0.122  50.774 1.00 8.92  ? 163 GLU   A CA  1 
ATOM   1411 C  C   . GLU   A 1 163 ? 10.083 -0.875  49.527 1.00 8.96  ? 163 GLU   A C   1 
ATOM   1412 O  O   . GLU   A 1 163 ? 10.523 -0.583  48.441 1.00 9.47  ? 163 GLU   A O   1 
ATOM   1413 C  CB  . GLU   A 1 163 ? 11.635 -0.862  51.572 1.00 13.68 ? 163 GLU   A CB  1 
ATOM   1414 C  CG  . GLU   A 1 163 ? 12.949 -0.976  50.829 1.00 12.92 ? 163 GLU   A CG  1 
ATOM   1415 C  CD  . GLU   A 1 163 ? 14.160 -1.399  51.642 1.00 13.56 ? 163 GLU   A CD  1 
ATOM   1416 O  OE1 . GLU   A 1 163 ? 13.979 -1.966  52.727 1.00 18.80 ? 163 GLU   A OE1 1 
ATOM   1417 O  OE2 . GLU   A 1 163 ? 15.266 -1.202  51.155 1.00 12.24 ? 163 GLU   A OE2 1 
ATOM   1418 N  N   . TYR   A 1 164 ? 9.208  -1.843  49.731 1.00 9.12  ? 164 TYR   A N   1 
ATOM   1419 C  CA  . TYR   A 1 164 ? 8.604  -2.544  48.579 1.00 8.00  ? 164 TYR   A CA  1 
ATOM   1420 C  C   . TYR   A 1 164 ? 7.811  -1.581  47.683 1.00 7.16  ? 164 TYR   A C   1 
ATOM   1421 O  O   . TYR   A 1 164 ? 7.964  -1.609  46.500 1.00 8.45  ? 164 TYR   A O   1 
ATOM   1422 C  CB  . TYR   A 1 164 ? 7.677  -3.634  49.141 1.00 8.83  ? 164 TYR   A CB  1 
ATOM   1423 C  CG  . TYR   A 1 164 ? 6.897  -4.394  48.096 1.00 8.78  ? 164 TYR   A CG  1 
ATOM   1424 C  CD1 . TYR   A 1 164 ? 7.510  -5.367  47.330 1.00 10.64 ? 164 TYR   A CD1 1 
ATOM   1425 C  CD2 . TYR   A 1 164 ? 5.555  -4.139  47.866 1.00 8.55  ? 164 TYR   A CD2 1 
ATOM   1426 C  CE1 . TYR   A 1 164 ? 6.812  -6.079  46.371 1.00 8.57  ? 164 TYR   A CE1 1 
ATOM   1427 C  CE2 . TYR   A 1 164 ? 4.841  -4.842  46.910 1.00 9.78  ? 164 TYR   A CE2 1 
ATOM   1428 C  CZ  . TYR   A 1 164 ? 5.473  -5.816  46.161 1.00 9.52  ? 164 TYR   A CZ  1 
ATOM   1429 O  OH  . TYR   A 1 164 ? 4.800  -6.514  45.209 1.00 9.32  ? 164 TYR   A OH  1 
ATOM   1430 N  N   . LEU   A 1 165 ? 6.945  -0.783  48.308 1.00 8.21  ? 165 LEU   A N   1 
ATOM   1431 C  CA  . LEU   A 1 165 ? 6.080  0.121   47.511 1.00 8.02  ? 165 LEU   A CA  1 
ATOM   1432 C  C   . LEU   A 1 165 ? 6.893  1.157   46.710 1.00 7.22  ? 165 LEU   A C   1 
ATOM   1433 O  O   . LEU   A 1 165 ? 6.535  1.431   45.595 1.00 8.83  ? 165 LEU   A O   1 
ATOM   1434 C  CB  . LEU   A 1 165 ? 5.086  0.799   48.457 1.00 9.35  ? 165 LEU   A CB  1 
ATOM   1435 C  CG  . LEU   A 1 165 ? 3.936  -0.088  48.923 1.00 9.99  ? 165 LEU   A CG  1 
ATOM   1436 C  CD1 . LEU   A 1 165 ? 3.142  0.599   50.017 1.00 13.30 ? 165 LEU   A CD1 1 
ATOM   1437 C  CD2 . LEU   A 1 165 ? 3.037  -0.454  47.757 1.00 11.35 ? 165 LEU   A CD2 1 
ATOM   1438 N  N   . PHE   A 1 166 ? 7.955  1.662   47.323 1.00 9.76  ? 166 PHE   A N   1 
ATOM   1439 C  CA  . PHE   A 1 166 ? 8.808  2.631   46.597 1.00 8.86  ? 166 PHE   A CA  1 
ATOM   1440 C  C   . PHE   A 1 166 ? 9.404  1.955   45.358 1.00 8.98  ? 166 PHE   A C   1 
ATOM   1441 O  O   . PHE   A 1 166 ? 9.418  2.524   44.301 1.00 8.38  ? 166 PHE   A O   1 
ATOM   1442 C  CB  . PHE   A 1 166 ? 9.885  3.224   47.513 1.00 10.06 ? 166 PHE   A CB  1 
ATOM   1443 C  CG  . PHE   A 1 166 ? 10.723 4.251   46.802 1.00 8.27  ? 166 PHE   A CG  1 
ATOM   1444 C  CD1 . PHE   A 1 166 ? 10.219 5.516   46.554 1.00 10.55 ? 166 PHE   A CD1 1 
ATOM   1445 C  CD2 . PHE   A 1 166 ? 11.986 3.939   46.329 1.00 10.39 ? 166 PHE   A CD2 1 
ATOM   1446 C  CE1 . PHE   A 1 166 ? 10.977 6.461   45.886 1.00 10.40 ? 166 PHE   A CE1 1 
ATOM   1447 C  CE2 . PHE   A 1 166 ? 12.734 4.884   45.649 1.00 12.03 ? 166 PHE   A CE2 1 
ATOM   1448 C  CZ  . PHE   A 1 166 ? 12.227 6.138   45.423 1.00 9.72  ? 166 PHE   A CZ  1 
ATOM   1449 N  N   . GLU   A 1 167 ? 9.948  0.767   45.565 1.00 7.13  ? 167 GLU   A N   1 
ATOM   1450 C  CA  . GLU   A 1 167 ? 10.600 0.060   44.440 1.00 7.90  ? 167 GLU   A CA  1 
ATOM   1451 C  C   . GLU   A 1 167 ? 9.584  -0.276  43.341 1.00 8.13  ? 167 GLU   A C   1 
ATOM   1452 O  O   . GLU   A 1 167 ? 9.899  -0.151  42.182 1.00 9.55  ? 167 GLU   A O   1 
ATOM   1453 C  CB  . GLU   A 1 167 ? 11.289 -1.200  44.978 1.00 8.31  ? 167 GLU   A CB  1 
ATOM   1454 C  CG  . GLU   A 1 167 ? 11.981 -2.023  43.906 1.00 9.26  ? 167 GLU   A CG  1 
ATOM   1455 C  CD  . GLU   A 1 167 ? 11.111 -3.087  43.257 1.00 7.32  ? 167 GLU   A CD  1 
ATOM   1456 O  OE1 . GLU   A 1 167 ? 10.146 -3.521  43.899 1.00 9.34  ? 167 GLU   A OE1 1 
ATOM   1457 O  OE2 . GLU   A 1 167 ? 11.400 -3.457  42.118 1.00 9.41  ? 167 GLU   A OE2 1 
ATOM   1458 N  N   . ARG   A 1 168 ? 8.383  -0.656  43.751 1.00 7.82  ? 168 ARG   A N   1 
ATOM   1459 C  CA  . ARG   A 1 168 ? 7.345  -1.045  42.779 1.00 7.42  ? 168 ARG   A CA  1 
ATOM   1460 C  C   . ARG   A 1 168 ? 6.707  0.150   42.067 1.00 8.38  ? 168 ARG   A C   1 
ATOM   1461 O  O   . ARG   A 1 168 ? 6.464  0.047   40.880 1.00 10.21 ? 168 ARG   A O   1 
ATOM   1462 C  CB  . ARG   A 1 168 ? 6.189  -1.745  43.504 1.00 9.29  ? 168 ARG   A CB  1 
ATOM   1463 C  CG  . ARG   A 1 168 ? 6.501  -3.149  44.004 1.00 8.35  ? 168 ARG   A CG  1 
ATOM   1464 C  CD  . ARG   A 1 168 ? 6.565  -4.181  42.894 1.00 9.33  ? 168 ARG   A CD  1 
ATOM   1465 N  NE  . ARG   A 1 168 ? 7.920  -4.341  42.387 1.00 8.41  ? 168 ARG   A NE  1 
ATOM   1466 C  CZ  . ARG   A 1 168 ? 8.242  -5.122  41.371 1.00 8.60  ? 168 ARG   A CZ  1 
ATOM   1467 N  NH1 . ARG   A 1 168 ? 7.310  -5.824  40.754 1.00 11.58 ? 168 ARG   A NH1 1 
ATOM   1468 N  NH2 . ARG   A 1 168 ? 9.497  -5.203  40.975 1.00 11.51 ? 168 ARG   A NH2 1 
ATOM   1469 N  N   . LEU   A 1 169 ? 6.460  1.235   42.800 1.00 7.97  ? 169 LEU   A N   1 
ATOM   1470 C  CA  . LEU   A 1 169 ? 5.640  2.332   42.204 1.00 9.47  ? 169 LEU   A CA  1 
ATOM   1471 C  C   . LEU   A 1 169 ? 6.456  3.558   41.756 1.00 10.93 ? 169 LEU   A C   1 
ATOM   1472 O  O   . LEU   A 1 169 ? 5.919  4.357   41.042 1.00 10.46 ? 169 LEU   A O   1 
ATOM   1473 C  CB  . LEU   A 1 169 ? 4.557  2.739   43.214 1.00 9.49  ? 169 LEU   A CB  1 
ATOM   1474 C  CG  . LEU   A 1 169 ? 3.610  1.614   43.634 1.00 9.42  ? 169 LEU   A CG  1 
ATOM   1475 C  CD1 . LEU   A 1 169 ? 2.545  2.130   44.590 1.00 11.66 ? 169 LEU   A CD1 1 
ATOM   1476 C  CD2 . LEU   A 1 169 ? 2.962  0.975   42.418 1.00 12.71 ? 169 LEU   A CD2 1 
ATOM   1477 N  N   . THR   A 1 170 ? 7.681  3.694   42.231 1.00 10.32 ? 170 THR   A N   1 
ATOM   1478 C  CA  . THR   A 1 170 ? 8.502  4.812   41.709 1.00 10.13 ? 170 THR   A CA  1 
ATOM   1479 C  C   . THR   A 1 170 ? 9.616  4.315   40.786 1.00 10.41 ? 170 THR   A C   1 
ATOM   1480 O  O   . THR   A 1 170 ? 9.778  4.865   39.731 1.00 12.79 ? 170 THR   A O   1 
ATOM   1481 C  CB  . THR   A 1 170 ? 9.118  5.585   42.877 1.00 8.37  ? 170 THR   A CB  1 
ATOM   1482 O  OG1 . THR   A 1 170 ? 8.057  6.190   43.611 1.00 10.02 ? 170 THR   A OG1 1 
ATOM   1483 C  CG2 . THR   A 1 170 ? 10.103 6.642   42.425 1.00 10.19 ? 170 THR   A CG2 1 
ATOM   1484 N  N   . LEU   A 1 171 ? 10.298 3.245   41.195 1.00 10.19 ? 171 LEU   A N   1 
ATOM   1485 C  CA  . LEU   A 1 171 ? 11.485 2.863   40.388 1.00 13.57 ? 171 LEU   A CA  1 
ATOM   1486 C  C   . LEU   A 1 171 ? 11.121 1.960   39.205 1.00 20.46 ? 171 LEU   A C   1 
ATOM   1487 O  O   . LEU   A 1 171 ? 10.165 1.215   39.285 1.00 22.00 ? 171 LEU   A O   1 
ATOM   1488 C  CB  . LEU   A 1 171 ? 12.582 2.292   41.285 1.00 11.18 ? 171 LEU   A CB  1 
ATOM   1489 C  CG  . LEU   A 1 171 ? 13.099 3.228   42.375 1.00 14.06 ? 171 LEU   A CG  1 
ATOM   1490 C  CD1 . LEU   A 1 171 ? 14.133 2.517   43.231 1.00 15.23 ? 171 LEU   A CD1 1 
ATOM   1491 C  CD2 . LEU   A 1 171 ? 13.696 4.486   41.770 1.00 14.05 ? 171 LEU   A CD2 1 
ATOM   1492 N  N   . LYS   A 1 172 ? 11.842 2.153   38.109 1.00 21.99 ? 172 LYS   A N   1 
ATOM   1493 C  CA  . LYS   A 1 172 ? 11.451 1.450   36.851 1.00 43.20 ? 172 LYS   A CA  1 
ATOM   1494 C  C   . LYS   A 1 172 ? 11.821 -0.017  37.010 1.00 45.53 ? 172 LYS   A C   1 
ATOM   1495 O  O   . LYS   A 1 172 ? 12.927 -0.292  37.496 1.00 37.26 ? 172 LYS   A O   1 
ATOM   1496 C  CB  . LYS   A 1 172 ? 12.127 2.081   35.633 1.00 39.67 ? 172 LYS   A CB  1 
ATOM   1497 C  CG  . LYS   A 1 172 ? 11.828 1.389   34.311 1.00 31.72 ? 172 LYS   A CG  1 
ATOM   1498 N  N   . HIS   A 1 173 ? 10.911 -0.901  36.638 1.00 32.09 ? 173 HIS   A N   1 
ATOM   1499 C  CA  . HIS   A 1 173 ? 11.197 -2.363  36.756 1.00 39.74 ? 173 HIS   A CA  1 
ATOM   1500 C  C   . HIS   A 1 173 ? 10.455 -3.148  35.679 1.00 40.38 ? 173 HIS   A C   1 
ATOM   1501 O  O   . HIS   A 1 173 ? 9.596  -2.556  35.024 1.00 48.18 ? 173 HIS   A O   1 
ATOM   1502 C  CB  . HIS   A 1 173 ? 10.872 -2.960  38.135 1.00 27.19 ? 173 HIS   A CB  1 
ATOM   1503 C  CG  . HIS   A 1 173 ? 9.504  -2.636  38.611 1.00 25.64 ? 173 HIS   A CG  1 
ATOM   1504 N  ND1 . HIS   A 1 173 ? 8.401  -3.348  38.206 1.00 30.68 ? 173 HIS   A ND1 1 
ATOM   1505 C  CD2 . HIS   A 1 173 ? 9.064  -1.686  39.460 1.00 22.84 ? 173 HIS   A CD2 1 
ATOM   1506 C  CE1 . HIS   A 1 173 ? 7.328  -2.847  38.776 1.00 35.54 ? 173 HIS   A CE1 1 
ATOM   1507 N  NE2 . HIS   A 1 173 ? 7.708  -1.832  39.549 1.00 34.87 ? 173 HIS   A NE2 1 
ATOM   1508 N  N   . ASP   A 1 174 ? 10.780 -4.432  35.545 1.00 37.49 ? 174 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 174 ? 10.165 -5.264  34.477 1.00 41.99 ? 174 ASP   A CA  1 
HETATM 1510 CD CD  . CD    B 2 .   ? 18.723 -7.239  39.419 0.14 16.55 ? 201 CD    A CD  1 
HETATM 1511 CD CD  . CD    C 2 .   ? 48.862 -0.020  41.592 0.41 11.38 ? 202 CD    A CD  1 
HETATM 1512 CD CD  . CD    D 2 .   ? 27.016 26.995  27.008 0.15 22.37 ? 203 CD    A CD  1 
HETATM 1513 CD CD  . CD    E 2 .   ? 29.353 29.329  29.342 0.07 16.85 ? 204 CD    A CD  1 
HETATM 1514 CD CD  . CD    F 2 .   ? 29.227 29.780  30.973 0.30 19.96 ? 205 CD    A CD  1 
HETATM 1515 CD CD  . CD    G 2 .   ? 30.146 18.294  23.041 0.17 24.55 ? 206 CD    A CD  1 
HETATM 1516 CD CD  . CD    H 2 .   ? 29.866 5.467   25.362 0.17 24.97 ? 207 CD    A CD  1 
HETATM 1517 CD CD  . CD    I 2 .   ? 16.445 -7.260  35.854 0.19 41.15 ? 208 CD    A CD  1 
HETATM 1518 CD CD  . CD    J 2 .   ? 32.812 29.760  33.329 0.12 23.88 ? 209 CD    A CD  1 
HETATM 1519 CL CL  . CL    K 3 .   ? 49.455 -1.742  40.006 1.00 25.22 ? 210 CL    A CL  1 
HETATM 1520 S  S   . SO4   L 4 .   ? 49.662 28.138  24.449 1.00 25.13 ? 211 SO4   A S   1 
HETATM 1521 O  O1  . SO4   L 4 .   ? 49.877 28.513  23.091 1.00 31.15 ? 211 SO4   A O1  1 
HETATM 1522 O  O2  . SO4   L 4 .   ? 48.657 28.971  25.026 1.00 29.84 ? 211 SO4   A O2  1 
HETATM 1523 O  O3  . SO4   L 4 .   ? 49.247 26.774  24.510 1.00 29.66 ? 211 SO4   A O3  1 
HETATM 1524 O  O4  . SO4   L 4 .   ? 50.877 28.289  25.190 1.00 34.31 ? 211 SO4   A O4  1 
HETATM 1525 S  S   . SO4   M 4 .   ? 30.802 -2.931  54.972 0.46 24.33 ? 212 SO4   A S   1 
HETATM 1526 O  O1  . SO4   M 4 .   ? 31.973 -2.906  54.139 0.46 15.35 ? 212 SO4   A O1  1 
HETATM 1527 O  O2  . SO4   M 4 .   ? 29.648 -3.179  54.162 0.46 8.19  ? 212 SO4   A O2  1 
HETATM 1528 O  O3  . SO4   M 4 .   ? 30.933 -3.971  55.950 0.46 27.51 ? 212 SO4   A O3  1 
HETATM 1529 O  O4  . SO4   M 4 .   ? 30.660 -1.666  55.635 0.46 25.73 ? 212 SO4   A O4  1 
HETATM 1530 C  C1  . EDO   N 5 .   ? 18.079 -4.730  52.251 1.00 18.76 ? 213 EDO   A C1  1 
HETATM 1531 O  O1  . EDO   N 5 .   ? 17.406 -5.813  52.840 1.00 25.29 ? 213 EDO   A O1  1 
HETATM 1532 C  C2  . EDO   N 5 .   ? 17.149 -3.633  51.938 1.00 17.55 ? 213 EDO   A C2  1 
HETATM 1533 O  O2  . EDO   N 5 .   ? 16.470 -3.210  53.096 1.00 19.05 ? 213 EDO   A O2  1 
HETATM 1534 C  C1  . EDO   O 5 .   ? 52.283 22.726  29.039 1.00 38.25 ? 214 EDO   A C1  1 
HETATM 1535 O  O1  . EDO   O 5 .   ? 52.420 21.433  28.491 1.00 41.85 ? 214 EDO   A O1  1 
HETATM 1536 C  C2  . EDO   O 5 .   ? 51.047 23.415  28.608 1.00 29.98 ? 214 EDO   A C2  1 
HETATM 1537 O  O2  . EDO   O 5 .   ? 50.911 23.430  27.203 1.00 34.58 ? 214 EDO   A O2  1 
HETATM 1538 C  C1  . EDO   P 5 .   ? 20.984 -7.876  37.694 1.00 28.03 ? 215 EDO   A C1  1 
HETATM 1539 O  O1  . EDO   P 5 .   ? 20.094 -6.942  37.123 1.00 38.03 ? 215 EDO   A O1  1 
HETATM 1540 C  C2  . EDO   P 5 .   ? 20.607 -9.266  37.351 1.00 29.80 ? 215 EDO   A C2  1 
HETATM 1541 O  O2  . EDO   P 5 .   ? 20.609 -9.488  35.962 1.00 38.47 ? 215 EDO   A O2  1 
HETATM 1542 C  C1  . EDO   Q 5 .   ? 19.663 7.654   37.186 1.00 27.68 ? 216 EDO   A C1  1 
HETATM 1543 O  O1  . EDO   Q 5 .   ? 20.039 8.411   36.056 1.00 36.45 ? 216 EDO   A O1  1 
HETATM 1544 C  C2  . EDO   Q 5 .   ? 19.413 6.224   36.874 1.00 22.00 ? 216 EDO   A C2  1 
HETATM 1545 O  O2  . EDO   Q 5 .   ? 18.357 6.085   35.953 1.00 33.70 ? 216 EDO   A O2  1 
HETATM 1546 C  C1  . A1L52 R 6 .   ? 37.192 0.194   34.079 0.40 18.87 ? 217 A1L52 A C1  1 
HETATM 1547 O  O2  . A1L52 R 6 .   ? 33.267 -0.094  30.723 0.40 12.80 ? 217 A1L52 A O2  1 
HETATM 1548 C  C3  . A1L52 R 6 .   ? 34.908 0.411   36.519 0.40 16.92 ? 217 A1L52 A C3  1 
HETATM 1549 C  C4  . A1L52 R 6 .   ? 34.154 -0.478  37.468 0.40 21.64 ? 217 A1L52 A C4  1 
HETATM 1550 C  C5  . A1L52 R 6 .   ? 33.945 -0.010  34.289 0.40 16.25 ? 217 A1L52 A C5  1 
HETATM 1551 C  C6  . A1L52 R 6 .   ? 32.633 0.263   34.763 0.40 11.41 ? 217 A1L52 A C6  1 
HETATM 1552 C  C7  . A1L52 R 6 .   ? 31.576 0.406   33.912 0.40 11.88 ? 217 A1L52 A C7  1 
HETATM 1553 C  C8  . A1L52 R 6 .   ? 31.759 0.290   32.535 0.40 10.99 ? 217 A1L52 A C8  1 
HETATM 1554 C  C9  . A1L52 R 6 .   ? 30.914 0.321   30.369 0.40 18.21 ? 217 A1L52 A C9  1 
HETATM 1555 C  C12 . A1L52 R 6 .   ? 27.472 0.877   29.028 0.40 21.29 ? 217 A1L52 A C12 1 
HETATM 1556 C  C13 . A1L52 R 6 .   ? 27.691 0.759   27.648 0.40 18.22 ? 217 A1L52 A C13 1 
HETATM 1557 C  C14 . A1L52 R 6 .   ? 28.955 0.503   27.171 0.40 22.98 ? 217 A1L52 A C14 1 
HETATM 1558 C  C15 . A1L52 R 6 .   ? 30.040 0.354   28.071 0.40 17.92 ? 217 A1L52 A C15 1 
HETATM 1559 C  C16 . A1L52 R 6 .   ? 31.341 0.092   27.593 0.40 20.71 ? 217 A1L52 A C16 1 
HETATM 1560 C  C17 . A1L52 R 6 .   ? 32.432 -0.057  28.508 0.40 12.83 ? 217 A1L52 A C17 1 
HETATM 1561 C  C18 . A1L52 R 6 .   ? 32.213 0.052   29.866 0.40 12.74 ? 217 A1L52 A C18 1 
HETATM 1562 C  C20 . A1L52 R 6 .   ? 34.137 -0.121  32.915 0.40 15.22 ? 217 A1L52 A C20 1 
HETATM 1563 C  C2  . A1L52 R 6 .   ? 36.254 -0.755  34.773 0.40 16.29 ? 217 A1L52 A C2  1 
HETATM 1564 N  N1  . A1L52 R 6 .   ? 34.988 -0.129  35.161 0.40 18.12 ? 217 A1L52 A N1  1 
HETATM 1565 N  N2  . A1L52 R 6 .   ? 30.685 0.439   31.672 0.40 14.14 ? 217 A1L52 A N2  1 
HETATM 1566 C  C10 . A1L52 R 6 .   ? 29.814 0.476   29.463 0.40 20.36 ? 217 A1L52 A C10 1 
HETATM 1567 C  C11 . A1L52 R 6 .   ? 28.512 0.735   29.913 0.40 18.71 ? 217 A1L52 A C11 1 
HETATM 1568 O  O1  . A1L52 R 6 .   ? 31.530 -0.008  26.367 0.40 25.58 ? 217 A1L52 A O1  1 
HETATM 1569 C  C19 . A1L52 R 6 .   ? 33.055 0.022   32.067 0.40 12.74 ? 217 A1L52 A C19 1 
HETATM 1570 O  O   . HOH   S 7 .   ? 37.270 15.148  18.289 0.61 19.24 ? 301 HOH   A O   1 
HETATM 1571 O  O   . HOH   S 7 .   ? 34.261 16.309  20.142 0.42 20.42 ? 302 HOH   A O   1 
HETATM 1572 O  O   . HOH   S 7 .   ? 35.956 18.306  21.189 0.44 14.19 ? 303 HOH   A O   1 
HETATM 1573 O  O   . HOH   S 7 .   ? 23.832 10.613  35.295 0.53 20.86 ? 304 HOH   A O   1 
HETATM 1574 O  O   . HOH   S 7 .   ? 35.476 18.281  23.854 0.60 21.23 ? 305 HOH   A O   1 
HETATM 1575 O  O   . HOH   S 7 .   ? 37.907 12.838  19.422 0.59 18.97 ? 306 HOH   A O   1 
HETATM 1576 O  O   . HOH   S 7 .   ? 27.091 14.347  29.779 1.00 35.85 ? 307 HOH   A O   1 
HETATM 1577 O  O   . HOH   S 7 .   ? 27.848 13.883  36.263 0.85 18.36 ? 308 HOH   A O   1 
HETATM 1578 O  O   . HOH   S 7 .   ? 50.611 26.057  34.713 1.00 27.29 ? 309 HOH   A O   1 
HETATM 1579 O  O   . HOH   S 7 .   ? 33.676 23.005  25.126 1.00 15.90 ? 310 HOH   A O   1 
HETATM 1580 O  O   . HOH   S 7 .   ? 24.181 -9.558  54.878 1.00 34.98 ? 311 HOH   A O   1 
HETATM 1581 O  O   . HOH   S 7 .   ? 53.719 17.105  14.294 1.00 30.00 ? 312 HOH   A O   1 
HETATM 1582 O  O   . HOH   S 7 .   ? 18.569 10.407  35.596 1.00 38.41 ? 313 HOH   A O   1 
HETATM 1583 O  O   . HOH   S 7 .   ? 35.499 3.660   25.661 1.00 19.93 ? 314 HOH   A O   1 
HETATM 1584 O  O   . HOH   S 7 .   ? 45.840 20.037  39.001 1.00 19.13 ? 315 HOH   A O   1 
HETATM 1585 O  O   . HOH   S 7 .   ? 20.332 0.230   57.937 1.00 30.67 ? 316 HOH   A O   1 
HETATM 1586 O  O   . HOH   S 7 .   ? 18.009 -0.763  33.603 1.00 35.71 ? 317 HOH   A O   1 
HETATM 1587 O  O   . HOH   S 7 .   ? 29.582 4.838   52.335 1.00 28.59 ? 318 HOH   A O   1 
HETATM 1588 O  O   . HOH   S 7 .   ? 25.910 11.231  36.004 1.00 26.17 ? 319 HOH   A O   1 
HETATM 1589 O  O   . HOH   S 7 .   ? 46.467 30.089  24.253 1.00 17.67 ? 320 HOH   A O   1 
HETATM 1590 O  O   . HOH   S 7 .   ? 26.269 24.932  27.710 1.00 29.97 ? 321 HOH   A O   1 
HETATM 1591 O  O   . HOH   S 7 .   ? 29.614 -6.044  55.148 1.00 36.28 ? 322 HOH   A O   1 
HETATM 1592 O  O   . HOH   S 7 .   ? 40.032 9.231   43.104 1.00 27.45 ? 323 HOH   A O   1 
HETATM 1593 O  O   . HOH   S 7 .   ? 8.260  8.710   44.166 1.00 15.96 ? 324 HOH   A O   1 
HETATM 1594 O  O   . HOH   S 7 .   ? 48.843 24.637  26.218 1.00 14.51 ? 325 HOH   A O   1 
HETATM 1595 O  O   . HOH   S 7 .   ? 18.912 5.164   56.696 1.00 33.38 ? 326 HOH   A O   1 
HETATM 1596 O  O   . HOH   S 7 .   ? 12.334 -8.942  36.184 1.00 45.08 ? 327 HOH   A O   1 
HETATM 1597 O  O   . HOH   S 7 .   ? 38.395 30.592  39.595 1.00 19.98 ? 328 HOH   A O   1 
HETATM 1598 O  O   . HOH   S 7 .   ? 17.756 14.463  31.839 1.00 43.31 ? 329 HOH   A O   1 
HETATM 1599 O  O   . HOH   S 7 .   ? 45.703 14.100  21.609 1.00 9.85  ? 330 HOH   A O   1 
HETATM 1600 O  O   . HOH   S 7 .   ? 14.873 -6.104  53.493 1.00 32.64 ? 331 HOH   A O   1 
HETATM 1601 O  O   . HOH   S 7 .   ? 30.105 5.190   49.011 1.00 23.79 ? 332 HOH   A O   1 
HETATM 1602 O  O   . HOH   S 7 .   ? 31.847 13.351  50.565 1.00 27.50 ? 333 HOH   A O   1 
HETATM 1603 O  O   . HOH   S 7 .   ? 18.798 7.206   33.353 1.00 35.07 ? 334 HOH   A O   1 
HETATM 1604 O  O   . HOH   S 7 .   ? 51.044 15.693  28.495 1.00 19.11 ? 335 HOH   A O   1 
HETATM 1605 O  O   . HOH   S 7 .   ? 31.603 -2.869  47.171 1.00 9.57  ? 336 HOH   A O   1 
HETATM 1606 O  O   . HOH   S 7 .   ? 5.192  2.212   55.397 1.00 24.40 ? 337 HOH   A O   1 
HETATM 1607 O  O   . HOH   S 7 .   ? 30.185 21.151  48.612 1.00 17.04 ? 338 HOH   A O   1 
HETATM 1608 O  O   . HOH   S 7 .   ? 11.132 -7.756  40.411 1.00 19.64 ? 339 HOH   A O   1 
HETATM 1609 O  O   . HOH   S 7 .   ? 8.172  7.985   57.791 1.00 34.18 ? 340 HOH   A O   1 
HETATM 1610 O  O   . HOH   S 7 .   ? 44.956 31.255  29.308 1.00 22.79 ? 341 HOH   A O   1 
HETATM 1611 O  O   . HOH   S 7 .   ? 51.694 17.585  31.463 1.00 36.02 ? 342 HOH   A O   1 
HETATM 1612 O  O   . HOH   S 7 .   ? 25.467 23.485  33.245 1.00 27.03 ? 343 HOH   A O   1 
HETATM 1613 O  O   . HOH   S 7 .   ? 14.743 1.545   38.195 1.00 19.35 ? 344 HOH   A O   1 
HETATM 1614 O  O   . HOH   S 7 .   ? 44.322 22.234  23.370 1.00 9.11  ? 345 HOH   A O   1 
HETATM 1615 O  O   . HOH   S 7 .   ? 42.460 20.470  19.484 1.00 9.25  ? 346 HOH   A O   1 
HETATM 1616 O  O   . HOH   S 7 .   ? 46.903 1.897   45.273 1.00 22.00 ? 347 HOH   A O   1 
HETATM 1617 O  O   . HOH   S 7 .   ? 17.168 2.713   56.769 1.00 18.26 ? 348 HOH   A O   1 
HETATM 1618 O  O   . HOH   S 7 .   ? 34.942 2.553   53.743 1.00 27.87 ? 349 HOH   A O   1 
HETATM 1619 O  O   . HOH   S 7 .   ? 32.391 -5.358  47.849 1.00 9.31  ? 350 HOH   A O   1 
HETATM 1620 O  O   . HOH   S 7 .   ? 21.074 13.965  34.903 1.00 26.62 ? 351 HOH   A O   1 
HETATM 1621 O  O   . HOH   S 7 .   ? 44.036 25.297  31.024 1.00 10.87 ? 352 HOH   A O   1 
HETATM 1622 O  O   . HOH   S 7 .   ? 21.354 -12.527 39.508 1.00 12.36 ? 353 HOH   A O   1 
HETATM 1623 O  O   . HOH   S 7 .   ? 34.998 16.324  45.762 1.00 21.29 ? 354 HOH   A O   1 
HETATM 1624 O  O   . HOH   S 7 .   ? 26.669 21.384  38.911 1.00 9.49  ? 355 HOH   A O   1 
HETATM 1625 O  O   . HOH   S 7 .   ? 12.912 15.437  52.702 1.00 26.50 ? 356 HOH   A O   1 
HETATM 1626 O  O   . HOH   S 7 .   ? 42.544 8.785   35.433 1.00 11.52 ? 357 HOH   A O   1 
HETATM 1627 O  O   . HOH   S 7 .   ? 35.994 4.086   48.063 1.00 27.31 ? 358 HOH   A O   1 
HETATM 1628 O  O   . HOH   S 7 .   ? 24.563 2.456   52.268 1.00 24.84 ? 359 HOH   A O   1 
HETATM 1629 O  O   . HOH   S 7 .   ? 36.900 -6.598  42.230 1.00 12.46 ? 360 HOH   A O   1 
HETATM 1630 O  O   . HOH   S 7 .   ? 51.201 16.099  19.574 1.00 28.02 ? 361 HOH   A O   1 
HETATM 1631 O  O   . HOH   S 7 .   ? 10.328 -6.103  44.706 1.00 9.55  ? 362 HOH   A O   1 
HETATM 1632 O  O   . HOH   S 7 .   ? 33.713 28.509  38.378 1.00 14.36 ? 363 HOH   A O   1 
HETATM 1633 O  O   . HOH   S 7 .   ? 36.290 25.582  44.027 1.00 27.58 ? 364 HOH   A O   1 
HETATM 1634 O  O   . HOH   S 7 .   ? 40.243 27.144  26.067 1.00 10.27 ? 365 HOH   A O   1 
HETATM 1635 O  O   . HOH   S 7 .   ? 34.931 2.797   44.228 1.00 17.81 ? 366 HOH   A O   1 
HETATM 1636 O  O   . HOH   S 7 .   ? 50.639 22.852  19.965 1.00 25.88 ? 367 HOH   A O   1 
HETATM 1637 O  O   . HOH   S 7 .   ? 28.913 7.715   49.486 1.00 14.03 ? 368 HOH   A O   1 
HETATM 1638 O  O   . HOH   S 7 .   ? 46.003 10.274  26.156 1.00 15.34 ? 369 HOH   A O   1 
HETATM 1639 O  O   . HOH   S 7 .   ? 42.447 10.516  27.071 1.00 21.87 ? 370 HOH   A O   1 
HETATM 1640 O  O   . HOH   S 7 .   ? 11.038 13.286  40.907 1.00 23.26 ? 371 HOH   A O   1 
HETATM 1641 O  O   . HOH   S 7 .   ? 39.784 25.013  41.837 1.00 21.45 ? 372 HOH   A O   1 
HETATM 1642 O  O   . HOH   S 7 .   ? 27.683 -5.706  45.619 1.00 11.59 ? 373 HOH   A O   1 
HETATM 1643 O  O   . HOH   S 7 .   ? 29.785 -6.119  47.624 1.00 10.38 ? 374 HOH   A O   1 
HETATM 1644 O  O   . HOH   S 7 .   ? 35.698 -5.613  49.741 1.00 14.90 ? 375 HOH   A O   1 
HETATM 1645 O  O   . HOH   S 7 .   ? 46.305 13.734  38.066 1.00 25.05 ? 376 HOH   A O   1 
HETATM 1646 O  O   . HOH   S 7 .   ? 35.784 -4.706  52.907 1.00 22.27 ? 377 HOH   A O   1 
HETATM 1647 O  O   . HOH   S 7 .   ? 20.453 -13.183 54.535 1.00 29.36 ? 378 HOH   A O   1 
HETATM 1648 O  O   . HOH   S 7 .   ? 12.817 0.824   47.888 1.00 12.14 ? 379 HOH   A O   1 
HETATM 1649 O  O   . HOH   S 7 .   ? 15.734 16.007  38.201 1.00 15.21 ? 380 HOH   A O   1 
HETATM 1650 O  O   . HOH   S 7 .   ? 32.143 4.115   47.411 1.00 12.07 ? 381 HOH   A O   1 
HETATM 1651 O  O   . HOH   S 7 .   ? 26.734 10.287  31.699 1.00 31.25 ? 382 HOH   A O   1 
HETATM 1652 O  O   . HOH   S 7 .   ? 24.150 5.818   53.913 1.00 16.50 ? 383 HOH   A O   1 
HETATM 1653 O  O   . HOH   S 7 .   ? 16.568 -10.686 53.798 1.00 30.51 ? 384 HOH   A O   1 
HETATM 1654 O  O   . HOH   S 7 .   ? 29.673 14.579  49.601 1.00 16.24 ? 385 HOH   A O   1 
HETATM 1655 O  O   . HOH   S 7 .   ? 43.272 33.985  37.333 1.00 40.92 ? 386 HOH   A O   1 
HETATM 1656 O  O   . HOH   S 7 .   ? 33.987 8.631   43.242 1.00 16.61 ? 387 HOH   A O   1 
HETATM 1657 O  O   . HOH   S 7 .   ? 47.829 4.188   41.182 1.00 17.01 ? 388 HOH   A O   1 
HETATM 1658 O  O   . HOH   S 7 .   ? 38.456 18.819  40.519 1.00 14.49 ? 389 HOH   A O   1 
HETATM 1659 O  O   . HOH   S 7 .   ? 44.507 5.862   42.734 1.00 24.91 ? 390 HOH   A O   1 
HETATM 1660 O  O   . HOH   S 7 .   ? 22.801 5.551   56.162 1.00 25.65 ? 391 HOH   A O   1 
HETATM 1661 O  O   . HOH   S 7 .   ? 3.570  3.892   39.605 1.00 27.80 ? 392 HOH   A O   1 
HETATM 1662 O  O   . HOH   S 7 .   ? 25.908 -1.067  34.645 0.52 13.10 ? 393 HOH   A O   1 
HETATM 1663 O  O   . HOH   S 7 .   ? 49.258 13.560  31.676 1.00 15.10 ? 394 HOH   A O   1 
HETATM 1664 O  O   . HOH   S 7 .   ? 13.654 15.107  39.703 1.00 17.47 ? 395 HOH   A O   1 
HETATM 1665 O  O   . HOH   S 7 .   ? 24.275 20.137  26.362 1.00 45.54 ? 396 HOH   A O   1 
HETATM 1666 O  O   . HOH   S 7 .   ? 38.220 33.096  32.804 1.00 29.96 ? 397 HOH   A O   1 
HETATM 1667 O  O   . HOH   S 7 .   ? 33.002 26.669  40.161 1.00 11.40 ? 398 HOH   A O   1 
HETATM 1668 O  O   . HOH   S 7 .   ? 7.372  1.851   38.923 1.00 24.06 ? 399 HOH   A O   1 
HETATM 1669 O  O   . HOH   S 7 .   ? 42.706 24.856  22.287 1.00 7.76  ? 400 HOH   A O   1 
HETATM 1670 O  O   . HOH   S 7 .   ? 26.854 -7.535  49.420 1.00 11.19 ? 401 HOH   A O   1 
HETATM 1671 O  O   . HOH   S 7 .   ? 34.780 13.983  21.705 1.00 32.24 ? 402 HOH   A O   1 
HETATM 1672 O  O   . HOH   S 7 .   ? 49.587 17.386  33.986 1.00 18.47 ? 403 HOH   A O   1 
HETATM 1673 O  O   . HOH   S 7 .   ? 17.012 -4.125  55.729 1.00 27.90 ? 404 HOH   A O   1 
HETATM 1674 O  O   . HOH   S 7 .   ? 38.696 21.437  27.579 1.00 8.98  ? 405 HOH   A O   1 
HETATM 1675 O  O   . HOH   S 7 .   ? 14.464 7.236   38.992 1.00 16.83 ? 406 HOH   A O   1 
HETATM 1676 O  O   . HOH   S 7 .   ? 34.089 -2.133  50.706 1.00 14.95 ? 407 HOH   A O   1 
HETATM 1677 O  O   . HOH   S 7 .   ? 10.649 10.105  43.873 1.00 14.10 ? 408 HOH   A O   1 
HETATM 1678 O  O   . HOH   S 7 .   ? 39.842 16.643  39.729 1.00 14.86 ? 409 HOH   A O   1 
HETATM 1679 O  O   . HOH   S 7 .   ? 34.079 10.600  45.462 1.00 28.41 ? 410 HOH   A O   1 
HETATM 1680 O  O   . HOH   S 7 .   ? 42.686 32.419  27.190 1.00 15.61 ? 411 HOH   A O   1 
HETATM 1681 O  O   . HOH   S 7 .   ? 35.556 4.862   45.845 1.00 23.19 ? 412 HOH   A O   1 
HETATM 1682 O  O   . HOH   S 7 .   ? 12.053 18.087  39.648 1.00 18.72 ? 413 HOH   A O   1 
HETATM 1683 O  O   . HOH   S 7 .   ? 11.594 8.884   57.767 1.00 35.35 ? 414 HOH   A O   1 
HETATM 1684 O  O   . HOH   S 7 .   ? 50.559 20.910  36.894 1.00 30.21 ? 415 HOH   A O   1 
HETATM 1685 O  O   . HOH   S 7 .   ? 40.964 5.433   43.398 1.00 18.44 ? 416 HOH   A O   1 
HETATM 1686 O  O   . HOH   S 7 .   ? 49.791 8.972   28.995 1.00 23.01 ? 417 HOH   A O   1 
HETATM 1687 O  O   . HOH   S 7 .   ? 12.258 -6.998  42.921 1.00 9.39  ? 418 HOH   A O   1 
HETATM 1688 O  O   . HOH   S 7 .   ? 50.654 24.613  32.145 1.00 21.16 ? 419 HOH   A O   1 
HETATM 1689 O  O   . HOH   S 7 .   ? 38.552 -3.496  53.677 1.00 24.96 ? 420 HOH   A O   1 
HETATM 1690 O  O   . HOH   S 7 .   ? 38.436 32.940  37.763 1.00 32.14 ? 421 HOH   A O   1 
HETATM 1691 O  O   . HOH   S 7 .   ? 10.734 3.564   52.135 1.00 23.42 ? 422 HOH   A O   1 
HETATM 1692 O  O   . HOH   S 7 .   ? 17.184 -7.776  40.923 1.00 30.00 ? 423 HOH   A O   1 
HETATM 1693 O  O   . HOH   S 7 .   ? 44.832 27.724  30.102 1.00 14.43 ? 424 HOH   A O   1 
HETATM 1694 O  O   . HOH   S 7 .   ? 25.341 19.753  31.799 1.00 19.27 ? 425 HOH   A O   1 
HETATM 1695 O  O   . HOH   S 7 .   ? 8.876  -0.900  60.862 1.00 42.74 ? 426 HOH   A O   1 
HETATM 1696 O  O   . HOH   S 7 .   ? 33.063 6.284   44.697 1.00 17.94 ? 427 HOH   A O   1 
HETATM 1697 O  O   . HOH   S 7 .   ? 21.208 3.190   58.977 1.00 40.57 ? 428 HOH   A O   1 
HETATM 1698 O  O   . HOH   S 7 .   ? 24.472 14.561  51.515 1.00 32.71 ? 429 HOH   A O   1 
HETATM 1699 O  O   . HOH   S 7 .   ? 32.241 11.182  49.517 1.00 34.45 ? 430 HOH   A O   1 
HETATM 1700 O  O   . HOH   S 7 .   ? 49.832 26.183  20.854 1.00 27.48 ? 431 HOH   A O   1 
HETATM 1701 O  O   . HOH   S 7 .   ? 25.570 16.072  27.570 1.00 36.16 ? 432 HOH   A O   1 
HETATM 1702 O  O   . HOH   S 7 .   ? 52.600 13.337  24.706 1.00 25.40 ? 433 HOH   A O   1 
HETATM 1703 O  O   . HOH   S 7 .   ? 41.128 11.261  41.851 0.58 24.23 ? 434 HOH   A O   1 
HETATM 1704 O  O   . HOH   S 7 .   ? 47.732 30.082  27.624 1.00 37.10 ? 435 HOH   A O   1 
HETATM 1705 O  O   . HOH   S 7 .   ? 8.784  -3.729  58.293 1.00 33.73 ? 436 HOH   A O   1 
HETATM 1706 O  O   . HOH   S 7 .   ? 9.898  12.850  53.873 1.00 22.95 ? 437 HOH   A O   1 
HETATM 1707 O  O   . HOH   S 7 .   ? 6.332  -3.481  56.831 1.00 32.44 ? 438 HOH   A O   1 
HETATM 1708 O  O   . HOH   S 7 .   ? 43.606 22.576  20.753 1.00 10.75 ? 439 HOH   A O   1 
HETATM 1709 O  O   . HOH   S 7 .   ? 28.193 11.043  34.393 1.00 26.77 ? 440 HOH   A O   1 
HETATM 1710 O  O   . HOH   S 7 .   ? 38.563 18.658  43.421 1.00 24.29 ? 441 HOH   A O   1 
HETATM 1711 O  O   . HOH   S 7 .   ? 30.636 9.069   26.551 1.00 26.22 ? 442 HOH   A O   1 
HETATM 1712 O  O   . HOH   S 7 .   ? 46.530 10.141  36.986 1.00 26.15 ? 443 HOH   A O   1 
HETATM 1713 O  O   . HOH   S 7 .   ? 48.857 17.489  39.994 1.00 40.24 ? 444 HOH   A O   1 
HETATM 1714 O  O   . HOH   S 7 .   ? 16.185 9.775   56.905 1.00 36.95 ? 445 HOH   A O   1 
HETATM 1715 O  O   . HOH   S 7 .   ? 20.159 24.313  33.691 1.00 26.52 ? 446 HOH   A O   1 
HETATM 1716 O  O   . HOH   S 7 .   ? 34.692 -1.858  53.341 1.00 31.18 ? 447 HOH   A O   1 
HETATM 1717 O  O   . HOH   S 7 .   ? 39.303 10.927  47.210 1.00 39.79 ? 448 HOH   A O   1 
HETATM 1718 O  O   . HOH   S 7 .   ? 14.558 2.018   52.653 1.00 14.13 ? 449 HOH   A O   1 
HETATM 1719 O  O   . HOH   S 7 .   ? 52.071 15.148  21.603 1.00 30.54 ? 450 HOH   A O   1 
HETATM 1720 O  O   . HOH   S 7 .   ? 32.374 15.948  24.350 1.00 38.90 ? 451 HOH   A O   1 
HETATM 1721 O  O   . HOH   S 7 .   ? 32.148 25.537  45.033 1.00 16.70 ? 452 HOH   A O   1 
HETATM 1722 O  O   . HOH   S 7 .   ? 16.063 7.852   37.008 1.00 37.47 ? 453 HOH   A O   1 
HETATM 1723 O  O   . HOH   S 7 .   ? 37.018 1.176   50.501 1.00 28.58 ? 454 HOH   A O   1 
HETATM 1724 O  O   . HOH   S 7 .   ? 12.055 8.682   38.683 1.00 33.16 ? 455 HOH   A O   1 
HETATM 1725 O  O   . HOH   S 7 .   ? 34.058 14.929  49.887 1.00 31.43 ? 456 HOH   A O   1 
HETATM 1726 O  O   . HOH   S 7 .   ? 43.483 4.290   44.553 1.00 29.26 ? 457 HOH   A O   1 
HETATM 1727 O  O   . HOH   S 7 .   ? 14.123 4.571   37.969 1.00 27.54 ? 458 HOH   A O   1 
HETATM 1728 O  O   . HOH   S 7 .   ? 30.735 16.995  48.709 1.00 26.39 ? 459 HOH   A O   1 
HETATM 1729 O  O   . HOH   S 7 .   ? 47.688 12.966  36.120 1.00 27.34 ? 460 HOH   A O   1 
HETATM 1730 O  O   . HOH   S 7 .   ? 9.681  12.603  43.272 1.00 17.13 ? 461 HOH   A O   1 
HETATM 1731 O  O   . HOH   S 7 .   ? 36.537 14.239  45.875 1.00 37.92 ? 462 HOH   A O   1 
HETATM 1732 O  O   . HOH   S 7 .   ? 22.953 11.869  52.796 0.55 28.79 ? 463 HOH   A O   1 
HETATM 1733 O  O   . HOH   S 7 .   ? 48.721 14.841  34.070 1.00 21.89 ? 464 HOH   A O   1 
HETATM 1734 O  O   . HOH   S 7 .   ? 25.545 8.182   53.423 1.00 22.27 ? 465 HOH   A O   1 
HETATM 1735 O  O   . HOH   S 7 .   ? 44.858 11.107  38.760 1.00 30.89 ? 466 HOH   A O   1 
HETATM 1736 O  O   . HOH   S 7 .   ? 28.301 12.487  30.201 1.00 30.00 ? 467 HOH   A O   1 
HETATM 1737 O  O   . HOH   S 7 .   ? 41.173 27.498  40.946 1.00 30.37 ? 468 HOH   A O   1 
HETATM 1738 O  O   . HOH   S 7 .   ? 41.035 22.765  41.674 1.00 38.13 ? 469 HOH   A O   1 
HETATM 1739 O  O   . HOH   S 7 .   ? 40.480 25.969  23.626 1.00 9.54  ? 470 HOH   A O   1 
HETATM 1740 O  O   . HOH   S 7 .   ? 40.379 20.862  40.159 1.00 29.00 ? 471 HOH   A O   1 
HETATM 1741 O  O   . HOH   S 7 .   ? 45.227 0.006   45.226 0.18 25.63 ? 472 HOH   A O   1 
HETATM 1742 O  O   . HOH   S 7 .   ? 26.354 -7.812  46.692 1.00 14.34 ? 473 HOH   A O   1 
HETATM 1743 O  O   . HOH   S 7 .   ? 9.007  12.068  56.122 1.00 40.50 ? 474 HOH   A O   1 
HETATM 1744 O  O   . HOH   S 7 .   ? 53.237 15.050  17.511 1.00 29.19 ? 475 HOH   A O   1 
HETATM 1745 O  O   . HOH   S 7 .   ? 37.832 31.770  30.469 1.00 25.02 ? 476 HOH   A O   1 
HETATM 1746 O  O   . HOH   S 7 .   ? 31.061 9.090   48.546 1.00 25.46 ? 477 HOH   A O   1 
HETATM 1747 O  O   . HOH   S 7 .   ? 23.782 -2.106  56.684 1.00 44.69 ? 478 HOH   A O   1 
HETATM 1748 O  O   . HOH   S 7 .   ? 19.782 -3.838  55.733 1.00 31.75 ? 479 HOH   A O   1 
HETATM 1749 O  O   . HOH   S 7 .   ? 47.842 27.367  29.596 1.00 29.28 ? 480 HOH   A O   1 
HETATM 1750 O  O   . HOH   S 7 .   ? 33.579 16.959  48.403 1.00 31.06 ? 481 HOH   A O   1 
HETATM 1751 O  O   . HOH   S 7 .   ? 3.572  3.168   57.339 1.00 45.89 ? 482 HOH   A O   1 
HETATM 1752 O  O   . HOH   S 7 .   ? 34.330 14.839  17.724 1.00 29.67 ? 483 HOH   A O   1 
HETATM 1753 O  O   . HOH   S 7 .   ? 40.345 29.705  41.621 1.00 36.57 ? 484 HOH   A O   1 
HETATM 1754 O  O   . HOH   S 7 .   ? 43.615 9.946   40.939 1.00 32.61 ? 485 HOH   A O   1 
HETATM 1755 O  O   . HOH   S 7 .   ? 18.599 12.688  36.031 1.00 32.77 ? 486 HOH   A O   1 
HETATM 1756 O  O   . HOH   S 7 .   ? 12.786 2.552   50.450 1.00 16.37 ? 487 HOH   A O   1 
HETATM 1757 O  O   . HOH   S 7 .   ? 35.311 30.508  39.390 1.00 27.44 ? 488 HOH   A O   1 
HETATM 1758 O  O   . HOH   S 7 .   ? 50.911 17.571  36.347 1.00 37.49 ? 489 HOH   A O   1 
HETATM 1759 O  O   . HOH   S 7 .   ? 24.597 0.172   56.177 1.00 41.70 ? 490 HOH   A O   1 
HETATM 1760 O  O   . HOH   S 7 .   ? 46.790 5.622   43.333 1.00 27.42 ? 491 HOH   A O   1 
HETATM 1761 O  O   . HOH   S 7 .   ? 48.477 19.705  39.213 1.00 30.64 ? 492 HOH   A O   1 
HETATM 1762 O  O   . HOH   S 7 .   ? 17.898 1.150   58.788 1.00 37.44 ? 493 HOH   A O   1 
HETATM 1763 O  O   . HOH   S 7 .   ? 38.660 26.215  43.856 1.00 30.22 ? 494 HOH   A O   1 
HETATM 1764 O  O   . HOH   S 7 .   ? 44.601 8.269   42.676 1.00 35.30 ? 495 HOH   A O   1 
HETATM 1765 O  O   . HOH   S 7 .   ? 35.386 30.678  30.784 1.00 28.69 ? 496 HOH   A O   1 
HETATM 1766 O  O   . HOH   S 7 .   ? 32.760 6.868   47.332 1.00 30.44 ? 497 HOH   A O   1 
HETATM 1767 O  O   . HOH   S 7 .   ? 13.803 8.492   57.061 1.00 32.55 ? 498 HOH   A O   1 
HETATM 1768 O  O   . HOH   S 7 .   ? 23.119 -11.628 56.063 1.00 38.38 ? 499 HOH   A O   1 
HETATM 1769 O  O   . HOH   S 7 .   ? 24.483 10.524  54.596 1.00 25.64 ? 500 HOH   A O   1 
HETATM 1770 O  O   . HOH   S 7 .   ? 52.377 21.418  13.680 0.76 36.75 ? 501 HOH   A O   1 
HETATM 1771 O  O   . HOH   S 7 .   ? 45.378 22.340  40.528 1.00 37.66 ? 502 HOH   A O   1 
HETATM 1772 O  O   . HOH   S 7 .   ? 35.945 5.945   50.546 1.00 39.75 ? 503 HOH   A O   1 
HETATM 1773 O  O   . HOH   S 7 .   ? 28.409 7.630   52.262 1.00 23.22 ? 504 HOH   A O   1 
HETATM 1774 O  O   . HOH   S 7 .   ? 37.276 -0.003  53.179 0.50 32.83 ? 505 HOH   A O   1 
HETATM 1775 O  O   . HOH   S 7 .   ? 29.791 -10.158 51.827 1.00 37.36 ? 506 HOH   A O   1 
HETATM 1776 O  O   . HOH   S 7 .   ? 27.720 15.164  51.489 1.00 25.27 ? 507 HOH   A O   1 
HETATM 1777 O  O   . HOH   S 7 .   ? 27.897 17.738  51.938 1.00 41.51 ? 508 HOH   A O   1 
HETATM 1778 O  O   . HOH   S 7 .   ? 51.801 12.561  31.138 1.00 27.90 ? 509 HOH   A O   1 
HETATM 1779 O  O   . HOH   S 7 .   ? 52.981 13.656  28.885 1.00 28.84 ? 510 HOH   A O   1 
HETATM 1780 O  O   . HOH   S 7 .   ? 49.607 21.855  40.783 1.00 38.75 ? 511 HOH   A O   1 
HETATM 1781 O  O   . HOH   S 7 .   ? 16.376 -2.648  57.885 1.00 37.47 ? 512 HOH   A O   1 
HETATM 1782 O  O   . HOH   S 7 .   ? 34.814 27.855  43.575 1.00 26.40 ? 513 HOH   A O   1 
HETATM 1783 O  O   . HOH   S 7 .   ? 45.920 33.672  29.222 1.00 33.87 ? 514 HOH   A O   1 
HETATM 1784 O  O   . HOH   S 7 .   ? 14.469 3.174   57.492 1.00 31.58 ? 515 HOH   A O   1 
HETATM 1785 O  O   . HOH   S 7 .   ? 49.912 14.054  36.230 1.00 34.91 ? 516 HOH   A O   1 
HETATM 1786 O  O   . HOH   S 7 .   ? 38.561 29.173  43.567 1.00 39.98 ? 517 HOH   A O   1 
HETATM 1787 O  O   . HOH   S 7 .   ? 14.637 5.716   58.775 1.00 36.51 ? 518 HOH   A O   1 
HETATM 1788 O  O   . HOH   S 7 .   ? 31.159 12.571  53.400 1.00 47.93 ? 519 HOH   A O   1 
HETATM 1789 O  O   . HOH   S 7 .   ? 36.012 29.886  42.817 1.00 28.17 ? 520 HOH   A O   1 
HETATM 1790 O  O   . HOH   S 7 .   ? 30.139 9.190   53.760 1.00 37.73 ? 521 HOH   A O   1 
HETATM 1791 O  O   . HOH   S 7 .   ? 52.205 13.237  35.468 1.00 38.33 ? 522 HOH   A O   1 
# 
