data_2JKF
# 
_entry.id   2JKF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.391 
_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   2JKF         pdb_00002jkf 10.2210/pdb2jkf/pdb 
PDBE  EBI-37310    ?            ?                   
WWPDB D_1290037310 ?            ?                   
# 
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 
1 'Structure model' 1 0 2008-09-23 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2018-01-17 
4 'Structure model' 1 3 2024-05-08 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' Advisory                    
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Data collection'           
4 4 'Structure model' 'Data collection'           
5 4 'Structure model' 'Database references'       
6 4 'Structure model' Other                       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' diffrn_source        
2 4 'Structure model' chem_comp_atom       
3 4 'Structure model' chem_comp_bond       
4 4 'Structure model' database_2           
5 4 'Structure model' pdbx_database_status 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_pdbx_database_status.status_code_sf' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2JKF 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2008-08-28 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2JKG 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        'PLASMODIUM FALCIPARUM PROFILIN' 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kursula, I.'      1 
'Kursula, P.'      2 
'Ganter, M.'       3 
'Panjikar, S.'     4 
'Matuschewski, K.' 5 
'Schueler, H.'     6 
# 
_citation.id                        primary 
_citation.title                     
'Structural Basis for Parasite-Specific Functions of the Divergent Profilin of Plasmodium Falciparum' 
_citation.journal_abbrev            Structure 
_citation.journal_volume            16 
_citation.page_first                1638 
_citation.page_last                 ? 
_citation.year                      2008 
_citation.journal_id_ASTM           STRUE6 
_citation.country                   UK 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_id_CSD            2005 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   19000816 
_citation.pdbx_database_id_DOI      10.1016/J.STR.2008.09.008 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kursula, I.'      1 ? 
primary 'Kursula, P.'      2 ? 
primary 'Ganter, M.'       3 ? 
primary 'Panjikar, S.'     4 ? 
primary 'Matuschewski, K.' 5 ? 
primary 'Schueler, H.'     6 ? 
# 
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 PROFILIN 20102.010 1  ? ? ? ? 
2 water   nat water    18.015    83 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CONSERVED PROTEIN' 
# 
_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       
;MAEEYSWDSYLNDRLLATNQVSGAGLASEEDGVVYACVAQGEESDPNFDKWSLFYKEDYDIEVEDENGTKTTKTINEGQT
ILVVFNEGYAPDGVWLGGTKYQFINIERDLEFEGYNFDVATCAKLKGGLHLVKVPGGNILVVLYDEEKEQDRGNSKIAAL
TFAKELAESSQLQHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAEEYSWDSYLNDRLLATNQVSGAGLASEEDGVVYACVAQGEESDPNFDKWSLFYKEDYDIEVEDENGTKTTKTINEGQT
ILVVFNEGYAPDGVWLGGTKYQFINIERDLEFEGYNFDVATCAKLKGGLHLVKVPGGNILVVLYDEEKEQDRGNSKIAAL
TFAKELAESSQLQHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLU n 
1 4   GLU n 
1 5   TYR n 
1 6   SER n 
1 7   TRP n 
1 8   ASP n 
1 9   SER n 
1 10  TYR n 
1 11  LEU n 
1 12  ASN n 
1 13  ASP n 
1 14  ARG n 
1 15  LEU n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  ASN n 
1 20  GLN n 
1 21  VAL n 
1 22  SER n 
1 23  GLY n 
1 24  ALA n 
1 25  GLY n 
1 26  LEU n 
1 27  ALA n 
1 28  SER n 
1 29  GLU n 
1 30  GLU n 
1 31  ASP n 
1 32  GLY n 
1 33  VAL n 
1 34  VAL n 
1 35  TYR n 
1 36  ALA n 
1 37  CYS n 
1 38  VAL n 
1 39  ALA n 
1 40  GLN n 
1 41  GLY n 
1 42  GLU n 
1 43  GLU n 
1 44  SER n 
1 45  ASP n 
1 46  PRO n 
1 47  ASN n 
1 48  PHE n 
1 49  ASP n 
1 50  LYS n 
1 51  TRP n 
1 52  SER n 
1 53  LEU n 
1 54  PHE n 
1 55  TYR n 
1 56  LYS n 
1 57  GLU n 
1 58  ASP n 
1 59  TYR n 
1 60  ASP n 
1 61  ILE n 
1 62  GLU n 
1 63  VAL n 
1 64  GLU n 
1 65  ASP n 
1 66  GLU n 
1 67  ASN n 
1 68  GLY n 
1 69  THR n 
1 70  LYS n 
1 71  THR n 
1 72  THR n 
1 73  LYS n 
1 74  THR n 
1 75  ILE n 
1 76  ASN n 
1 77  GLU n 
1 78  GLY n 
1 79  GLN n 
1 80  THR n 
1 81  ILE n 
1 82  LEU n 
1 83  VAL n 
1 84  VAL n 
1 85  PHE n 
1 86  ASN n 
1 87  GLU n 
1 88  GLY n 
1 89  TYR n 
1 90  ALA n 
1 91  PRO n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  TRP n 
1 96  LEU n 
1 97  GLY n 
1 98  GLY n 
1 99  THR n 
1 100 LYS n 
1 101 TYR n 
1 102 GLN n 
1 103 PHE n 
1 104 ILE n 
1 105 ASN n 
1 106 ILE n 
1 107 GLU n 
1 108 ARG n 
1 109 ASP n 
1 110 LEU n 
1 111 GLU n 
1 112 PHE n 
1 113 GLU n 
1 114 GLY n 
1 115 TYR n 
1 116 ASN n 
1 117 PHE n 
1 118 ASP n 
1 119 VAL n 
1 120 ALA n 
1 121 THR n 
1 122 CYS n 
1 123 ALA n 
1 124 LYS n 
1 125 LEU n 
1 126 LYS n 
1 127 GLY n 
1 128 GLY n 
1 129 LEU n 
1 130 HIS n 
1 131 LEU n 
1 132 VAL n 
1 133 LYS n 
1 134 VAL n 
1 135 PRO n 
1 136 GLY n 
1 137 GLY n 
1 138 ASN n 
1 139 ILE n 
1 140 LEU n 
1 141 VAL n 
1 142 VAL n 
1 143 LEU n 
1 144 TYR n 
1 145 ASP n 
1 146 GLU n 
1 147 GLU n 
1 148 LYS n 
1 149 GLU n 
1 150 GLN n 
1 151 ASP n 
1 152 ARG n 
1 153 GLY n 
1 154 ASN n 
1 155 SER n 
1 156 LYS n 
1 157 ILE n 
1 158 ALA n 
1 159 ALA n 
1 160 LEU n 
1 161 THR n 
1 162 PHE n 
1 163 ALA n 
1 164 LYS n 
1 165 GLU n 
1 166 LEU n 
1 167 ALA n 
1 168 GLU n 
1 169 SER n 
1 170 SER n 
1 171 GLN n 
1 172 LEU n 
1 173 GLN n 
1 174 HIS n 
1 175 HIS n 
1 176 HIS n 
1 177 HIS n 
1 178 HIS n 
1 179 HIS 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'PLASMODIUM FALCIPARUM' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5833 
_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     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_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                   CODONPLUSRIPL 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   TYR 5   5   5   TYR TYR A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   SER 9   9   9   SER SER A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  ASN 47  47  47  ASN ASN A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  TRP 51  51  51  TRP TRP A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 CYS 122 122 122 CYS CYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 PHE 162 162 162 PHE PHE A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 GLN 171 171 171 GLN GLN A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 HIS 175 175 ?   ?   ?   A . n 
A 1 176 HIS 176 176 ?   ?   ?   A . n 
A 1 177 HIS 177 177 ?   ?   ?   A . n 
A 1 178 HIS 178 178 ?   ?   ?   A . n 
A 1 179 HIS 179 179 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1  2001 2001 HOH HOH A . 
B 2 HOH 2  2002 2002 HOH HOH A . 
B 2 HOH 3  2003 2003 HOH HOH A . 
B 2 HOH 4  2004 2004 HOH HOH A . 
B 2 HOH 5  2005 2005 HOH HOH A . 
B 2 HOH 6  2006 2006 HOH HOH A . 
B 2 HOH 7  2007 2007 HOH HOH A . 
B 2 HOH 8  2008 2008 HOH HOH A . 
B 2 HOH 9  2009 2009 HOH HOH A . 
B 2 HOH 10 2010 2010 HOH HOH A . 
B 2 HOH 11 2011 2011 HOH HOH A . 
B 2 HOH 12 2012 2012 HOH HOH A . 
B 2 HOH 13 2013 2013 HOH HOH A . 
B 2 HOH 14 2014 2014 HOH HOH A . 
B 2 HOH 15 2015 2015 HOH HOH A . 
B 2 HOH 16 2016 2016 HOH HOH A . 
B 2 HOH 17 2017 2017 HOH HOH A . 
B 2 HOH 18 2018 2018 HOH HOH A . 
B 2 HOH 19 2019 2019 HOH HOH A . 
B 2 HOH 20 2020 2020 HOH HOH A . 
B 2 HOH 21 2021 2021 HOH HOH A . 
B 2 HOH 22 2022 2022 HOH HOH A . 
B 2 HOH 23 2023 2023 HOH HOH A . 
B 2 HOH 24 2024 2024 HOH HOH A . 
B 2 HOH 25 2025 2025 HOH HOH A . 
B 2 HOH 26 2026 2026 HOH HOH A . 
B 2 HOH 27 2027 2027 HOH HOH A . 
B 2 HOH 28 2028 2028 HOH HOH A . 
B 2 HOH 29 2029 2029 HOH HOH A . 
B 2 HOH 30 2030 2030 HOH HOH A . 
B 2 HOH 31 2031 2031 HOH HOH A . 
B 2 HOH 32 2032 2032 HOH HOH A . 
B 2 HOH 33 2033 2033 HOH HOH A . 
B 2 HOH 34 2034 2034 HOH HOH A . 
B 2 HOH 35 2035 2035 HOH HOH A . 
B 2 HOH 36 2036 2036 HOH HOH A . 
B 2 HOH 37 2037 2037 HOH HOH A . 
B 2 HOH 38 2038 2038 HOH HOH A . 
B 2 HOH 39 2039 2039 HOH HOH A . 
B 2 HOH 40 2040 2040 HOH HOH A . 
B 2 HOH 41 2041 2041 HOH HOH A . 
B 2 HOH 42 2042 2042 HOH HOH A . 
B 2 HOH 43 2043 2043 HOH HOH A . 
B 2 HOH 44 2044 2044 HOH HOH A . 
B 2 HOH 45 2045 2045 HOH HOH A . 
B 2 HOH 46 2046 2046 HOH HOH A . 
B 2 HOH 47 2047 2047 HOH HOH A . 
B 2 HOH 48 2048 2048 HOH HOH A . 
B 2 HOH 49 2049 2049 HOH HOH A . 
B 2 HOH 50 2050 2050 HOH HOH A . 
B 2 HOH 51 2051 2051 HOH HOH A . 
B 2 HOH 52 2052 2052 HOH HOH A . 
B 2 HOH 53 2053 2053 HOH HOH A . 
B 2 HOH 54 2054 2054 HOH HOH A . 
B 2 HOH 55 2055 2055 HOH HOH A . 
B 2 HOH 56 2056 2056 HOH HOH A . 
B 2 HOH 57 2057 2057 HOH HOH A . 
B 2 HOH 58 2058 2058 HOH HOH A . 
B 2 HOH 59 2059 2059 HOH HOH A . 
B 2 HOH 60 2060 2060 HOH HOH A . 
B 2 HOH 61 2061 2061 HOH HOH A . 
B 2 HOH 62 2062 2062 HOH HOH A . 
B 2 HOH 63 2063 2063 HOH HOH A . 
B 2 HOH 64 2064 2064 HOH HOH A . 
B 2 HOH 65 2065 2065 HOH HOH A . 
B 2 HOH 66 2066 2066 HOH HOH A . 
B 2 HOH 67 2067 2067 HOH HOH A . 
B 2 HOH 68 2068 2068 HOH HOH A . 
B 2 HOH 69 2069 2069 HOH HOH A . 
B 2 HOH 70 2070 2070 HOH HOH A . 
B 2 HOH 71 2071 2071 HOH HOH A . 
B 2 HOH 72 2072 2072 HOH HOH A . 
B 2 HOH 73 2073 2073 HOH HOH A . 
B 2 HOH 74 2074 2074 HOH HOH A . 
B 2 HOH 75 2075 2075 HOH HOH A . 
B 2 HOH 76 2076 2076 HOH HOH A . 
B 2 HOH 77 2077 2077 HOH HOH A . 
B 2 HOH 78 2078 2078 HOH HOH A . 
B 2 HOH 79 2079 2079 HOH HOH A . 
B 2 HOH 80 2080 2080 HOH HOH A . 
B 2 HOH 81 2081 2081 HOH HOH A . 
B 2 HOH 82 2082 2082 HOH HOH A . 
B 2 HOH 83 2083 2083 HOH HOH A . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.4.0077 ? 1 
XDS    'data reduction' .        ? 2 
XSCALE 'data scaling'   .        ? 3 
MOLREP phasing          .        ? 4 
# 
_cell.entry_id           2JKF 
_cell.length_a           45.440 
_cell.length_b           50.330 
_cell.length_c           86.650 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2JKF 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          2JKF 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.5 
_exptl_crystal.density_percent_sol   50 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '2.2 M AMMONIUM SULFATE, PH 6' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                'RH-COATED SI MIRRORS' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI(111) DOUBLE CRYSTAL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I911-3' 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_wavelength             1.0 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2JKF 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20.00 
_reflns.d_resolution_high            2.31 
_reflns.number_obs                   8883 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.4 
_reflns.pdbx_Rmerge_I_obs            0.05 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        25.00 
_reflns.B_iso_Wilson_estimate        36.00 
_reflns.pdbx_redundancy              6.4 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.31 
_reflns_shell.d_res_low              2.37 
_reflns_shell.percent_possible_all   85.0 
_reflns_shell.Rmerge_I_obs           0.20 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    6.80 
_reflns_shell.pdbx_redundancy        4.6 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2JKF 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.ls_number_reflns_obs                     8436 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            2.31 
_refine.ls_percent_reflns_obs                    96.6 
_refine.ls_R_factor_obs                          0.204 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.200 
_refine.ls_R_factor_R_free                       0.269 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  446 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.933 
_refine.correlation_coeff_Fo_to_Fc_free          0.897 
_refine.B_iso_mean                               26.45 
_refine.aniso_B[1][1]                            -0.72000 
_refine.aniso_B[2][2]                            -0.27000 
_refine.aniso_B[3][3]                            0.99000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.341 
_refine.pdbx_overall_ESU_R_Free                  0.262 
_refine.overall_SU_ML                            0.190 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             17.058 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1337 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             83 
_refine_hist.number_atoms_total               1420 
_refine_hist.d_res_high                       2.31 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.012  0.022  ? 1363 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 885  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.392  1.948  ? 1847 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.027  3.000  ? 2169 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       11.310 5.000  ? 169  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.219 26.250 ? 72   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.787 15.000 ? 226  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       8.726  15.000 ? 3    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.078  0.200  ? 199  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 1556 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 268  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.804  2.000  ? 836  'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.453  3.000  ? 1335 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.107  4.000  ? 527  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.209  5.000  ? 512  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.31 
_refine_ls_shell.d_res_low                        2.37 
_refine_ls_shell.number_reflns_R_work             524 
_refine_ls_shell.R_factor_R_work                  0.1850 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.2380 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             30 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_database_PDB_matrix.entry_id          2JKF 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  2JKF 
_struct.title                     'Plasmodium falciparum profilin' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2JKF 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
_struct_keywords.text            
;PROLINE-RICH LIGAND, PLASMODIUM FALCIPARUM, MALARIA, PROFILIN, CYTOSKELETON, ACTIN FILAMENT STRUCTURAL PROTEIN, PROTEIN-BINDING, PROTEIN BINDING
;
# 
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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP Q8I2J4_PLAF7 1 ? ? Q8I2J4 ? 
2 PDB 2JKF         1 ? ? 2JKF   ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2JKF A 1   ? 171 ? Q8I2J4 1   ? 171 ? 1   171 
2 2 2JKF A 172 ? 179 ? 2JKF   172 ? 179 ? 172 179 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_struct_biol.id   1 
# 
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 1 SER A 6   ? LEU A 15  ? SER A 6   LEU A 15  1 ? 10 
HELX_P HELX_P2 2 LEU A 16  ? ASN A 19  ? LEU A 16  ASN A 19  5 ? 4  
HELX_P HELX_P3 3 ASP A 49  ? PHE A 54  ? ASP A 49  PHE A 54  5 ? 6  
HELX_P HELX_P4 4 ASN A 76  ? GLU A 87  ? ASN A 76  GLU A 87  1 ? 12 
HELX_P HELX_P5 5 GLU A 147 ? GLU A 149 ? GLU A 147 GLU A 149 5 ? 3  
HELX_P HELX_P6 6 ASP A 151 ? SER A 170 ? ASP A 151 SER A 170 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 7 ? 
AB ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AB 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1 VAL A 34  ? ALA A 39  ? VAL A 34  ALA A 39  
AA 2 GLY A 23  ? SER A 28  ? GLY A 23  SER A 28  
AA 3 ASN A 138 ? ASP A 145 ? ASN A 138 ASP A 145 
AA 4 GLY A 127 ? VAL A 134 ? GLY A 127 VAL A 134 
AA 5 TYR A 115 ? LYS A 124 ? TYR A 115 LYS A 124 
AA 6 THR A 99  ? PHE A 112 ? THR A 99  PHE A 112 
AA 7 VAL A 94  ? LEU A 96  ? VAL A 94  LEU A 96  
AB 1 TYR A 59  ? GLU A 64  ? TYR A 59  GLU A 64  
AB 2 LYS A 70  ? ILE A 75  ? LYS A 70  ILE A 75  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA 1 2 N VAL A 38  ? N VAL A 38  O ALA A 24  ? O ALA A 24  
AA 2 3 N ALA A 27  ? N ALA A 27  O ILE A 139 ? O ILE A 139 
AA 3 4 N TYR A 144 ? N TYR A 144 O GLY A 128 ? O GLY A 128 
AA 4 5 N LYS A 133 ? N LYS A 133 O ASP A 118 ? O ASP A 118 
AA 5 6 N ALA A 123 ? N ALA A 123 O GLN A 102 ? O GLN A 102 
AA 6 7 N TYR A 101 ? N TYR A 101 O VAL A 94  ? O VAL A 94  
AB 1 2 N VAL A 63  ? N VAL A 63  O THR A 71  ? O THR A 71  
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 42 ? ? 166.91 -53.36 
2 1 ASP A 45 ? ? 83.02  112.97 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 TYR A 5  ? ? SER A 6  ? ? 149.31 
2 1 GLU A 43 ? ? SER A 44 ? ? -77.12 
3 1 SER A 44 ? ? ASP A 45 ? ? -85.13 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined -14.0510 4.4980   10.7840 0.1303 0.2745 0.2127 0.0230  -0.0237 -0.0659 4.8104  9.4225  8.9746  
-2.8255 1.8815  -5.5976 0.0251  0.1278  0.5144  0.0439  -0.0385 0.9478  -0.5418 -0.4507 0.0133  
'X-RAY DIFFRACTION' 2  ? refined -2.7160  6.0030   5.3960  0.1344 0.1353 0.0718 0.0075  -0.0504 0.0429  10.4199 6.4446  4.9234  
-1.0657 -3.9464 4.7317  0.4351  0.3051  0.5167  -0.5733 -0.0923 0.1345  -0.5545 0.0633  -0.3429 
'X-RAY DIFFRACTION' 3  ? refined -8.1650  8.2900   25.2910 0.6106 0.5016 0.7742 -0.0854 0.0731  -0.0301 24.1731 15.9972 10.4095 
19.4711 15.5473 12.1647 1.2402  -0.0859 -0.4363 0.2795  -1.2697 2.2259  1.0816  -1.6265 0.0296  
'X-RAY DIFFRACTION' 4  ? refined 6.1890   4.9940   14.1090 0.1952 0.3100 0.1022 -0.0212 -0.0309 -0.0251 12.4063 5.0015  1.3084  
-3.7098 -2.8937 1.0924  -0.0510 -0.2945 0.6617  0.1824  0.2107  -0.6299 -0.1478 0.5589  -0.1598 
'X-RAY DIFFRACTION' 5  ? refined 21.9780  -10.1050 11.4680 0.3128 0.4441 0.3300 -0.0350 -0.0092 -0.0155 3.0091  15.0585 3.0141  
-6.5036 1.0367  -3.8549 -0.0726 -0.5101 -0.2941 0.2093  0.0793  0.9534  0.3393  -0.2383 -0.0068 
'X-RAY DIFFRACTION' 6  ? refined 5.9770   -5.5380  4.8300  0.0464 0.1748 0.0661 -0.0168 -0.0059 0.0199  2.5378  3.0864  4.4315  
-0.7963 -0.5160 2.1723  -0.0240 0.1497  -0.0587 -0.2177 0.0347  -0.3150 -0.0447 0.1995  -0.0108 
'X-RAY DIFFRACTION' 7  ? refined -9.7520  -10.9360 -3.7650 0.1865 0.2427 0.1303 -0.0073 -0.0136 0.0093  18.1500 1.9174  1.9392  
3.0362  -3.4122 0.7816  -0.2069 0.4869  -1.0194 -0.5676 0.0975  -0.1327 0.1465  -0.0422 0.1094  
'X-RAY DIFFRACTION' 8  ? refined -6.3480  -5.1270  3.2090  0.0360 0.1746 0.0184 0.0064  0.0086  -0.0197 3.7268  2.0948  7.5173  
-0.2737 1.8817  -0.5195 -0.0901 0.2410  0.0533  -0.1896 0.1165  0.0912  -0.1361 -0.0109 -0.0264 
'X-RAY DIFFRACTION' 9  ? refined -10.5220 -6.1580  11.2690 0.0248 0.1776 0.0067 0.0093  0.0067  -0.0269 3.7461  6.5997  1.7724  
-0.0554 1.7000  -0.8164 0.0431  -0.4199 -0.0962 0.3489  -0.0563 0.0316  0.1088  -0.3785 0.0132  
'X-RAY DIFFRACTION' 10 ? refined -17.9080 5.1590   -6.6160 0.3680 0.3980 0.4213 0.0002  -0.0199 0.0077  5.3259  16.0888 3.1760  
-9.1455 3.8499  -6.2223 0.2870  0.5161  0.8422  -1.0198 -0.4473 0.3522  0.0815  -0.5935 0.1604  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  A 6   ? ? A 23  ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 24  ? ? A 40  ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 41  ? ? A 47  ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 48  ? ? A 62  ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 63  ? ? A 74  ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 75  ? ? A 106 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  A 107 ? ? A 112 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  A 113 ? ? A 139 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  A 140 ? ? A 164 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 A 165 ? ? A 174 ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A ALA 2   ? A ALA 2   
3 1 Y 1 A GLU 3   ? A GLU 3   
4 1 Y 1 A GLU 4   ? A GLU 4   
5 1 Y 1 A HIS 175 ? A HIS 175 
6 1 Y 1 A HIS 176 ? A HIS 176 
7 1 Y 1 A HIS 177 ? A HIS 177 
8 1 Y 1 A HIS 178 ? A HIS 178 
9 1 Y 1 A HIS 179 ? A HIS 179 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_atom_sites.entry_id                    2JKF 
_atom_sites.fract_transf_matrix[1][1]   0.022007 
_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]   0.019869 
_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]   0.011541 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . TYR A 1 5   ? -11.283 15.011  1.370   1.00 46.94 ? 5    TYR A N   1 
ATOM   2    C CA  . TYR A 1 5   ? -11.978 14.929  2.691   1.00 47.03 ? 5    TYR A CA  1 
ATOM   3    C C   . TYR A 1 5   ? -11.047 15.167  3.861   1.00 46.80 ? 5    TYR A C   1 
ATOM   4    O O   . TYR A 1 5   ? -9.808  15.186  3.728   1.00 46.86 ? 5    TYR A O   1 
ATOM   5    C CB  . TYR A 1 5   ? -12.590 13.542  2.882   1.00 47.08 ? 5    TYR A CB  1 
ATOM   6    C CG  . TYR A 1 5   ? -12.952 12.880  1.593   1.00 48.87 ? 5    TYR A CG  1 
ATOM   7    C CD1 . TYR A 1 5   ? -14.082 12.078  1.491   1.00 49.80 ? 5    TYR A CD1 1 
ATOM   8    C CD2 . TYR A 1 5   ? -12.173 13.084  0.454   1.00 50.18 ? 5    TYR A CD2 1 
ATOM   9    C CE1 . TYR A 1 5   ? -14.420 11.480  0.287   1.00 50.47 ? 5    TYR A CE1 1 
ATOM   10   C CE2 . TYR A 1 5   ? -12.502 12.496  -0.755  1.00 50.31 ? 5    TYR A CE2 1 
ATOM   11   C CZ  . TYR A 1 5   ? -13.624 11.695  -0.832  1.00 50.75 ? 5    TYR A CZ  1 
ATOM   12   O OH  . TYR A 1 5   ? -13.953 11.106  -2.030  1.00 51.04 ? 5    TYR A OH  1 
ATOM   13   N N   . SER A 1 6   ? -11.688 15.364  5.013   1.00 45.84 ? 6    SER A N   1 
ATOM   14   C CA  . SER A 1 6   ? -11.109 14.970  6.297   1.00 44.11 ? 6    SER A CA  1 
ATOM   15   C C   . SER A 1 6   ? -11.553 13.538  6.490   1.00 42.50 ? 6    SER A C   1 
ATOM   16   O O   . SER A 1 6   ? -12.705 13.245  6.821   1.00 42.00 ? 6    SER A O   1 
ATOM   17   C CB  . SER A 1 6   ? -11.581 15.821  7.471   1.00 44.10 ? 6    SER A CB  1 
ATOM   18   O OG  . SER A 1 6   ? -11.348 15.113  8.680   1.00 44.06 ? 6    SER A OG  1 
ATOM   19   N N   . TRP A 1 7   ? -10.609 12.653  6.251   1.00 41.18 ? 7    TRP A N   1 
ATOM   20   C CA  . TRP A 1 7   ? -10.874 11.238  6.205   1.00 40.11 ? 7    TRP A CA  1 
ATOM   21   C C   . TRP A 1 7   ? -11.180 10.670  7.568   1.00 39.37 ? 7    TRP A C   1 
ATOM   22   O O   . TRP A 1 7   ? -11.761 9.593   7.664   1.00 39.99 ? 7    TRP A O   1 
ATOM   23   C CB  . TRP A 1 7   ? -9.686  10.504  5.600   1.00 40.15 ? 7    TRP A CB  1 
ATOM   24   C CG  . TRP A 1 7   ? -9.655  10.626  4.141   1.00 39.89 ? 7    TRP A CG  1 
ATOM   25   C CD1 . TRP A 1 7   ? -8.928  11.509  3.401   1.00 39.88 ? 7    TRP A CD1 1 
ATOM   26   C CD2 . TRP A 1 7   ? -10.395 9.829   3.219   1.00 40.60 ? 7    TRP A CD2 1 
ATOM   27   N NE1 . TRP A 1 7   ? -9.175  11.311  2.063   1.00 41.09 ? 7    TRP A NE1 1 
ATOM   28   C CE2 . TRP A 1 7   ? -10.070 10.280  1.926   1.00 41.60 ? 7    TRP A CE2 1 
ATOM   29   C CE3 . TRP A 1 7   ? -11.299 8.771   3.362   1.00 40.80 ? 7    TRP A CE3 1 
ATOM   30   C CZ2 . TRP A 1 7   ? -10.629 9.717   0.780   1.00 42.73 ? 7    TRP A CZ2 1 
ATOM   31   C CZ3 . TRP A 1 7   ? -11.849 8.211   2.226   1.00 42.09 ? 7    TRP A CZ3 1 
ATOM   32   C CH2 . TRP A 1 7   ? -11.513 8.683   0.951   1.00 42.36 ? 7    TRP A CH2 1 
ATOM   33   N N   . ASP A 1 8   ? -10.795 11.399  8.610   1.00 38.18 ? 8    ASP A N   1 
ATOM   34   C CA  . ASP A 1 8   ? -11.000 10.957  9.997   1.00 37.47 ? 8    ASP A CA  1 
ATOM   35   C C   . ASP A 1 8   ? -12.463 10.674  10.296  1.00 36.35 ? 8    ASP A C   1 
ATOM   36   O O   . ASP A 1 8   ? -12.801 9.632   10.829  1.00 35.80 ? 8    ASP A O   1 
ATOM   37   C CB  . ASP A 1 8   ? -10.522 12.014  10.990  1.00 37.70 ? 8    ASP A CB  1 
ATOM   38   C CG  . ASP A 1 8   ? -9.013  12.056  11.116  1.00 39.06 ? 8    ASP A CG  1 
ATOM   39   O OD1 . ASP A 1 8   ? -8.324  11.440  10.272  1.00 40.66 ? 8    ASP A OD1 1 
ATOM   40   O OD2 . ASP A 1 8   ? -8.515  12.707  12.063  1.00 41.72 ? 8    ASP A OD2 1 
ATOM   41   N N   . SER A 1 9   ? -13.307 11.647  9.984   1.00 35.92 ? 9    SER A N   1 
ATOM   42   C CA  . SER A 1 9   ? -14.771 11.533  10.141  1.00 35.99 ? 9    SER A CA  1 
ATOM   43   C C   . SER A 1 9   ? -15.250 10.238  9.540   1.00 35.15 ? 9    SER A C   1 
ATOM   44   O O   . SER A 1 9   ? -15.883 9.403   10.188  1.00 34.94 ? 9    SER A O   1 
ATOM   45   C CB  . SER A 1 9   ? -15.498 12.665  9.390   1.00 36.01 ? 9    SER A CB  1 
ATOM   46   O OG  . SER A 1 9   ? -14.725 13.854  9.325   1.00 36.44 ? 9    SER A OG  1 
ATOM   47   N N   . TYR A 1 10  ? -14.924 10.106  8.265   1.00 34.69 ? 10   TYR A N   1 
ATOM   48   C CA  . TYR A 1 10  ? -15.358 8.983   7.458   1.00 34.22 ? 10   TYR A CA  1 
ATOM   49   C C   . TYR A 1 10  ? -14.855 7.648   8.044   1.00 34.24 ? 10   TYR A C   1 
ATOM   50   O O   . TYR A 1 10  ? -15.633 6.712   8.223   1.00 34.05 ? 10   TYR A O   1 
ATOM   51   C CB  . TYR A 1 10  ? -14.918 9.165   5.998   1.00 34.21 ? 10   TYR A CB  1 
ATOM   52   C CG  . TYR A 1 10  ? -15.734 8.324   5.054   1.00 36.56 ? 10   TYR A CG  1 
ATOM   53   C CD1 . TYR A 1 10  ? -17.118 8.442   5.014   1.00 38.74 ? 10   TYR A CD1 1 
ATOM   54   C CD2 . TYR A 1 10  ? -15.132 7.397   4.216   1.00 38.43 ? 10   TYR A CD2 1 
ATOM   55   C CE1 . TYR A 1 10  ? -17.878 7.659   4.159   1.00 39.59 ? 10   TYR A CE1 1 
ATOM   56   C CE2 . TYR A 1 10  ? -15.880 6.616   3.362   1.00 39.06 ? 10   TYR A CE2 1 
ATOM   57   C CZ  . TYR A 1 10  ? -17.242 6.746   3.338   1.00 39.32 ? 10   TYR A CZ  1 
ATOM   58   O OH  . TYR A 1 10  ? -17.961 5.947   2.490   1.00 41.85 ? 10   TYR A OH  1 
ATOM   59   N N   . LEU A 1 11  ? -13.563 7.566   8.362   1.00 33.96 ? 11   LEU A N   1 
ATOM   60   C CA  . LEU A 1 11  ? -12.972 6.315   8.889   1.00 33.77 ? 11   LEU A CA  1 
ATOM   61   C C   . LEU A 1 11  ? -13.641 5.911   10.196  1.00 33.91 ? 11   LEU A C   1 
ATOM   62   O O   . LEU A 1 11  ? -13.911 4.745   10.432  1.00 34.41 ? 11   LEU A O   1 
ATOM   63   C CB  . LEU A 1 11  ? -11.459 6.450   9.111   1.00 32.75 ? 11   LEU A CB  1 
ATOM   64   C CG  . LEU A 1 11  ? -10.604 6.599   7.855   1.00 33.05 ? 11   LEU A CG  1 
ATOM   65   C CD1 . LEU A 1 11  ? -9.157  6.980   8.182   1.00 29.54 ? 11   LEU A CD1 1 
ATOM   66   C CD2 . LEU A 1 11  ? -10.661 5.319   7.010   1.00 32.73 ? 11   LEU A CD2 1 
ATOM   67   N N   . ASN A 1 12  ? -13.926 6.902   11.023  1.00 34.24 ? 12   ASN A N   1 
ATOM   68   C CA  . ASN A 1 12  ? -14.540 6.674   12.321  1.00 35.33 ? 12   ASN A CA  1 
ATOM   69   C C   . ASN A 1 12  ? -15.983 6.191   12.177  1.00 34.49 ? 12   ASN A C   1 
ATOM   70   O O   . ASN A 1 12  ? -16.392 5.202   12.781  1.00 34.24 ? 12   ASN A O   1 
ATOM   71   C CB  . ASN A 1 12  ? -14.517 7.961   13.134  1.00 36.76 ? 12   ASN A CB  1 
ATOM   72   C CG  . ASN A 1 12  ? -14.037 7.740   14.545  1.00 41.11 ? 12   ASN A CG  1 
ATOM   73   O OD1 . ASN A 1 12  ? -14.751 7.162   15.370  1.00 46.47 ? 12   ASN A OD1 1 
ATOM   74   N ND2 . ASN A 1 12  ? -12.816 8.202   14.840  1.00 43.32 ? 12   ASN A ND2 1 
ATOM   75   N N   . ASP A 1 13  ? -16.748 6.893   11.362  1.00 33.36 ? 13   ASP A N   1 
ATOM   76   C CA  . ASP A 1 13  ? -18.156 6.564   11.206  1.00 34.12 ? 13   ASP A CA  1 
ATOM   77   C C   . ASP A 1 13  ? -18.358 5.228   10.487  1.00 33.58 ? 13   ASP A C   1 
ATOM   78   O O   . ASP A 1 13  ? -19.154 4.406   10.922  1.00 32.27 ? 13   ASP A O   1 
ATOM   79   C CB  . ASP A 1 13  ? -18.895 7.700   10.509  1.00 34.94 ? 13   ASP A CB  1 
ATOM   80   C CG  . ASP A 1 13  ? -18.978 8.942   11.383  1.00 37.91 ? 13   ASP A CG  1 
ATOM   81   O OD1 . ASP A 1 13  ? -18.733 8.828   12.613  1.00 39.91 ? 13   ASP A OD1 1 
ATOM   82   O OD2 . ASP A 1 13  ? -19.276 10.033  10.848  1.00 42.51 ? 13   ASP A OD2 1 
ATOM   83   N N   . ARG A 1 14  ? -17.560 4.993   9.444   1.00 33.72 ? 14   ARG A N   1 
ATOM   84   C CA  . ARG A 1 14  ? -17.731 3.841   8.553   1.00 33.68 ? 14   ARG A CA  1 
ATOM   85   C C   . ARG A 1 14  ? -16.989 2.585   9.017   1.00 33.61 ? 14   ARG A C   1 
ATOM   86   O O   . ARG A 1 14  ? -17.353 1.469   8.654   1.00 33.78 ? 14   ARG A O   1 
ATOM   87   C CB  . ARG A 1 14  ? -17.252 4.182   7.131   1.00 33.92 ? 14   ARG A CB  1 
ATOM   88   C CG  . ARG A 1 14  ? -17.636 5.571   6.627   1.00 33.64 ? 14   ARG A CG  1 
ATOM   89   C CD  . ARG A 1 14  ? -19.117 5.723   6.654   1.00 33.56 ? 14   ARG A CD  1 
ATOM   90   N NE  . ARG A 1 14  ? -19.721 4.408   6.507   1.00 32.92 ? 14   ARG A NE  1 
ATOM   91   C CZ  . ARG A 1 14  ? -21.016 4.171   6.619   1.00 32.01 ? 14   ARG A CZ  1 
ATOM   92   N NH1 . ARG A 1 14  ? -21.847 5.167   6.876   1.00 32.23 ? 14   ARG A NH1 1 
ATOM   93   N NH2 . ARG A 1 14  ? -21.477 2.941   6.472   1.00 31.97 ? 14   ARG A NH2 1 
ATOM   94   N N   . LEU A 1 15  ? -15.934 2.754   9.796   1.00 33.26 ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? -15.076 1.618   10.115  1.00 33.26 ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? -14.864 1.433   11.624  1.00 32.91 ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? -15.015 0.330   12.140  1.00 32.79 ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? -13.732 1.761   9.359   1.00 34.39 ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? -12.827 0.535   9.128   1.00 34.42 ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? -13.594 -0.750  8.898   1.00 33.10 ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? -11.893 0.797   7.959   1.00 36.03 ? 15   LEU A CD2 1 
ATOM   102  N N   . LEU A 1 16  ? -14.543 2.506   12.336  1.00 32.00 ? 16   LEU A N   1 
ATOM   103  C CA  . LEU A 1 16  ? -14.183 2.381   13.749  1.00 31.68 ? 16   LEU A CA  1 
ATOM   104  C C   . LEU A 1 16  ? -15.469 2.143   14.552  1.00 30.76 ? 16   LEU A C   1 
ATOM   105  O O   . LEU A 1 16  ? -15.458 1.476   15.595  1.00 29.98 ? 16   LEU A O   1 
ATOM   106  C CB  . LEU A 1 16  ? -13.427 3.617   14.260  1.00 32.34 ? 16   LEU A CB  1 
ATOM   107  C CG  . LEU A 1 16  ? -12.164 3.328   15.079  1.00 33.92 ? 16   LEU A CG  1 
ATOM   108  C CD1 . LEU A 1 16  ? -11.108 2.786   14.132  1.00 38.82 ? 16   LEU A CD1 1 
ATOM   109  C CD2 . LEU A 1 16  ? -11.661 4.576   15.780  1.00 34.17 ? 16   LEU A CD2 1 
ATOM   110  N N   . ALA A 1 17  ? -16.582 2.644   14.016  1.00 29.49 ? 17   ALA A N   1 
ATOM   111  C CA  . ALA A 1 17  ? -17.900 2.506   14.664  1.00 28.53 ? 17   ALA A CA  1 
ATOM   112  C C   . ALA A 1 17  ? -18.363 1.048   14.745  1.00 27.48 ? 17   ALA A C   1 
ATOM   113  O O   . ALA A 1 17  ? -19.238 0.721   15.523  1.00 27.35 ? 17   ALA A O   1 
ATOM   114  C CB  . ALA A 1 17  ? -18.977 3.387   13.958  1.00 28.38 ? 17   ALA A CB  1 
ATOM   115  N N   . THR A 1 18  ? -17.741 0.178   13.961  1.00 27.46 ? 18   THR A N   1 
ATOM   116  C CA  . THR A 1 18  ? -18.068 -1.264  13.935  1.00 26.84 ? 18   THR A CA  1 
ATOM   117  C C   . THR A 1 18  ? -17.668 -2.008  15.236  1.00 26.57 ? 18   THR A C   1 
ATOM   118  O O   . THR A 1 18  ? -18.198 -3.070  15.555  1.00 25.83 ? 18   THR A O   1 
ATOM   119  C CB  . THR A 1 18  ? -17.351 -1.976  12.727  1.00 27.43 ? 18   THR A CB  1 
ATOM   120  O OG1 . THR A 1 18  ? -15.906 -1.890  12.872  1.00 26.11 ? 18   THR A OG1 1 
ATOM   121  C CG2 . THR A 1 18  ? -17.788 -1.356  11.396  1.00 25.99 ? 18   THR A CG2 1 
ATOM   122  N N   . ASN A 1 19  ? -16.725 -1.432  15.963  1.00 27.20 ? 19   ASN A N   1 
ATOM   123  C CA  . ASN A 1 19  ? -16.054 -2.083  17.116  1.00 27.92 ? 19   ASN A CA  1 
ATOM   124  C C   . ASN A 1 19  ? -15.219 -3.295  16.754  1.00 27.94 ? 19   ASN A C   1 
ATOM   125  O O   . ASN A 1 19  ? -14.822 -4.060  17.633  1.00 29.24 ? 19   ASN A O   1 
ATOM   126  C CB  . ASN A 1 19  ? -17.046 -2.509  18.194  1.00 28.47 ? 19   ASN A CB  1 
ATOM   127  C CG  . ASN A 1 19  ? -17.789 -1.360  18.777  1.00 29.60 ? 19   ASN A CG  1 
ATOM   128  O OD1 . ASN A 1 19  ? -18.996 -1.448  19.038  1.00 34.09 ? 19   ASN A OD1 1 
ATOM   129  N ND2 . ASN A 1 19  ? -17.090 -0.266  18.991  1.00 29.16 ? 19   ASN A ND2 1 
ATOM   130  N N   . GLN A 1 20  ? -14.941 -3.476  15.472  1.00 27.44 ? 20   GLN A N   1 
ATOM   131  C CA  . GLN A 1 20  ? -14.271 -4.689  15.021  1.00 27.82 ? 20   GLN A CA  1 
ATOM   132  C C   . GLN A 1 20  ? -12.801 -4.436  14.710  1.00 27.69 ? 20   GLN A C   1 
ATOM   133  O O   . GLN A 1 20  ? -12.036 -5.379  14.473  1.00 28.72 ? 20   GLN A O   1 
ATOM   134  C CB  . GLN A 1 20  ? -14.984 -5.289  13.793  1.00 27.87 ? 20   GLN A CB  1 
ATOM   135  C CG  . GLN A 1 20  ? -16.387 -5.822  14.083  1.00 27.58 ? 20   GLN A CG  1 
ATOM   136  C CD  . GLN A 1 20  ? -16.410 -6.891  15.189  1.00 29.12 ? 20   GLN A CD  1 
ATOM   137  O OE1 . GLN A 1 20  ? -15.498 -7.716  15.302  1.00 29.15 ? 20   GLN A OE1 1 
ATOM   138  N NE2 . GLN A 1 20  ? -17.465 -6.882  15.996  1.00 25.93 ? 20   GLN A NE2 1 
ATOM   139  N N   . VAL A 1 21  ? -12.416 -3.170  14.696  1.00 26.72 ? 21   VAL A N   1 
ATOM   140  C CA  . VAL A 1 21  ? -11.016 -2.802  14.469  1.00 26.80 ? 21   VAL A CA  1 
ATOM   141  C C   . VAL A 1 21  ? -10.537 -1.824  15.541  1.00 27.01 ? 21   VAL A C   1 
ATOM   142  O O   . VAL A 1 21  ? -11.332 -1.097  16.142  1.00 26.26 ? 21   VAL A O   1 
ATOM   143  C CB  . VAL A 1 21  ? -10.785 -2.188  13.048  1.00 28.16 ? 21   VAL A CB  1 
ATOM   144  C CG1 . VAL A 1 21  ? -11.418 -3.071  11.946  1.00 26.24 ? 21   VAL A CG1 1 
ATOM   145  C CG2 . VAL A 1 21  ? -11.330 -0.768  12.984  1.00 28.85 ? 21   VAL A CG2 1 
ATOM   146  N N   . SER A 1 22  ? -9.231  -1.836  15.793  1.00 26.67 ? 22   SER A N   1 
ATOM   147  C CA  . SER A 1 22  ? -8.628  -0.965  16.803  1.00 27.40 ? 22   SER A CA  1 
ATOM   148  C C   . SER A 1 22  ? -8.105  0.323   16.171  1.00 28.54 ? 22   SER A C   1 
ATOM   149  O O   . SER A 1 22  ? -7.775  1.296   16.852  1.00 29.93 ? 22   SER A O   1 
ATOM   150  C CB  . SER A 1 22  ? -7.497  -1.702  17.542  1.00 27.55 ? 22   SER A CB  1 
ATOM   151  O OG  . SER A 1 22  ? -6.536  -2.237  16.633  1.00 28.94 ? 22   SER A OG  1 
ATOM   152  N N   . GLY A 1 23  ? -8.014  0.308   14.854  1.00 29.38 ? 23   GLY A N   1 
ATOM   153  C CA  . GLY A 1 23  ? -7.448  1.424   14.102  1.00 30.08 ? 23   GLY A CA  1 
ATOM   154  C C   . GLY A 1 23  ? -7.622  1.243   12.617  1.00 29.99 ? 23   GLY A C   1 
ATOM   155  O O   . GLY A 1 23  ? -7.805  0.145   12.141  1.00 30.64 ? 23   GLY A O   1 
ATOM   156  N N   . ALA A 1 24  ? -7.568  2.345   11.891  1.00 30.80 ? 24   ALA A N   1 
ATOM   157  C CA  . ALA A 1 24  ? -7.718  2.318   10.435  1.00 30.91 ? 24   ALA A CA  1 
ATOM   158  C C   . ALA A 1 24  ? -7.047  3.535   9.863   1.00 31.16 ? 24   ALA A C   1 
ATOM   159  O O   . ALA A 1 24  ? -7.134  4.638   10.430  1.00 32.45 ? 24   ALA A O   1 
ATOM   160  C CB  . ALA A 1 24  ? -9.207  2.255   10.010  1.00 29.13 ? 24   ALA A CB  1 
ATOM   161  N N   . GLY A 1 25  ? -6.339  3.324   8.759   1.00 30.72 ? 25   GLY A N   1 
ATOM   162  C CA  . GLY A 1 25  ? -5.689  4.429   8.062   1.00 30.57 ? 25   GLY A CA  1 
ATOM   163  C C   . GLY A 1 25  ? -5.629  4.296   6.565   1.00 29.61 ? 25   GLY A C   1 
ATOM   164  O O   . GLY A 1 25  ? -5.825  3.230   6.000   1.00 29.93 ? 25   GLY A O   1 
ATOM   165  N N   . LEU A 1 26  ? -5.354  5.415   5.930   1.00 29.99 ? 26   LEU A N   1 
ATOM   166  C CA  . LEU A 1 26  ? -5.102  5.449   4.503   1.00 29.86 ? 26   LEU A CA  1 
ATOM   167  C C   . LEU A 1 26  ? -3.637  5.790   4.204   1.00 29.17 ? 26   LEU A C   1 
ATOM   168  O O   . LEU A 1 26  ? -3.096  6.767   4.704   1.00 29.79 ? 26   LEU A O   1 
ATOM   169  C CB  . LEU A 1 26  ? -6.043  6.427   3.821   1.00 29.05 ? 26   LEU A CB  1 
ATOM   170  C CG  . LEU A 1 26  ? -7.509  5.972   3.726   1.00 31.01 ? 26   LEU A CG  1 
ATOM   171  C CD1 . LEU A 1 26  ? -8.418  7.156   3.387   1.00 27.05 ? 26   LEU A CD1 1 
ATOM   172  C CD2 . LEU A 1 26  ? -7.686  4.832   2.723   1.00 29.93 ? 26   LEU A CD2 1 
ATOM   173  N N   . ALA A 1 27  ? -3.024  4.959   3.376   1.00 28.09 ? 27   ALA A N   1 
ATOM   174  C CA  . ALA A 1 27  ? -1.693  5.210   2.846   1.00 27.66 ? 27   ALA A CA  1 
ATOM   175  C C   . ALA A 1 27  ? -1.740  5.481   1.328   1.00 27.98 ? 27   ALA A C   1 
ATOM   176  O O   . ALA A 1 27  ? -2.624  5.003   0.622   1.00 27.75 ? 27   ALA A O   1 
ATOM   177  C CB  . ALA A 1 27  ? -0.793  4.019   3.143   1.00 26.89 ? 27   ALA A CB  1 
ATOM   178  N N   . SER A 1 28  ? -0.799  6.284   0.848   1.00 28.45 ? 28   SER A N   1 
ATOM   179  C CA  . SER A 1 28  ? -0.586  6.421   -0.582  1.00 28.81 ? 28   SER A CA  1 
ATOM   180  C C   . SER A 1 28  ? 0.169   5.218   -1.097  1.00 28.58 ? 28   SER A C   1 
ATOM   181  O O   . SER A 1 28  ? 1.060   4.656   -0.461  1.00 27.01 ? 28   SER A O   1 
ATOM   182  C CB  . SER A 1 28  ? 0.177   7.691   -0.956  1.00 29.28 ? 28   SER A CB  1 
ATOM   183  O OG  . SER A 1 28  ? 0.317   7.790   -2.368  1.00 29.86 ? 28   SER A OG  1 
ATOM   184  N N   . GLU A 1 29  ? -0.255  4.837   -2.276  1.00 28.52 ? 29   GLU A N   1 
ATOM   185  C CA  . GLU A 1 29  ? 0.325   3.737   -3.015  1.00 30.02 ? 29   GLU A CA  1 
ATOM   186  C C   . GLU A 1 29  ? 1.702   4.117   -3.575  1.00 29.99 ? 29   GLU A C   1 
ATOM   187  O O   . GLU A 1 29  ? 2.474   3.264   -4.001  1.00 31.03 ? 29   GLU A O   1 
ATOM   188  C CB  . GLU A 1 29  ? -0.658  3.403   -4.132  1.00 30.77 ? 29   GLU A CB  1 
ATOM   189  C CG  . GLU A 1 29  ? -0.359  2.228   -4.943  1.00 34.82 ? 29   GLU A CG  1 
ATOM   190  C CD  . GLU A 1 29  ? -1.486  1.987   -5.911  1.00 38.74 ? 29   GLU A CD  1 
ATOM   191  O OE1 . GLU A 1 29  ? -2.542  2.656   -5.742  1.00 43.89 ? 29   GLU A OE1 1 
ATOM   192  O OE2 . GLU A 1 29  ? -1.322  1.162   -6.835  1.00 40.50 ? 29   GLU A OE2 1 
ATOM   193  N N   . GLU A 1 30  ? 2.016   5.406   -3.541  1.00 29.61 ? 30   GLU A N   1 
ATOM   194  C CA  . GLU A 1 30  ? 3.277   5.894   -4.081  1.00 30.14 ? 30   GLU A CA  1 
ATOM   195  C C   . GLU A 1 30  ? 4.451   5.666   -3.134  1.00 29.82 ? 30   GLU A C   1 
ATOM   196  O O   . GLU A 1 30  ? 5.577   5.453   -3.575  1.00 28.76 ? 30   GLU A O   1 
ATOM   197  C CB  . GLU A 1 30  ? 3.198   7.384   -4.396  1.00 30.91 ? 30   GLU A CB  1 
ATOM   198  C CG  . GLU A 1 30  ? 2.632   7.683   -5.773  1.00 34.37 ? 30   GLU A CG  1 
ATOM   199  C CD  . GLU A 1 30  ? 1.200   7.193   -5.945  1.00 38.01 ? 30   GLU A CD  1 
ATOM   200  O OE1 . GLU A 1 30  ? 0.437   7.195   -4.935  1.00 41.20 ? 30   GLU A OE1 1 
ATOM   201  O OE2 . GLU A 1 30  ? 0.846   6.805   -7.088  1.00 38.41 ? 30   GLU A OE2 1 
ATOM   202  N N   . ASP A 1 31  ? 4.179   5.744   -1.837  1.00 28.77 ? 31   ASP A N   1 
ATOM   203  C CA  . ASP A 1 31  ? 5.233   5.679   -0.824  1.00 29.10 ? 31   ASP A CA  1 
ATOM   204  C C   . ASP A 1 31  ? 4.851   4.835   0.403   1.00 29.15 ? 31   ASP A C   1 
ATOM   205  O O   . ASP A 1 31  ? 5.714   4.471   1.199   1.00 28.89 ? 31   ASP A O   1 
ATOM   206  C CB  . ASP A 1 31  ? 5.626   7.088   -0.380  1.00 29.70 ? 31   ASP A CB  1 
ATOM   207  C CG  . ASP A 1 31  ? 4.459   7.877   0.246   1.00 31.64 ? 31   ASP A CG  1 
ATOM   208  O OD1 . ASP A 1 31  ? 3.437   7.283   0.681   1.00 32.05 ? 31   ASP A OD1 1 
ATOM   209  O OD2 . ASP A 1 31  ? 4.583   9.117   0.309   1.00 34.65 ? 31   ASP A OD2 1 
ATOM   210  N N   . GLY A 1 32  ? 3.558   4.532   0.532   1.00 28.22 ? 32   GLY A N   1 
ATOM   211  C CA  . GLY A 1 32  ? 3.068   3.553   1.499   1.00 28.38 ? 32   GLY A CA  1 
ATOM   212  C C   . GLY A 1 32  ? 2.980   4.165   2.884   1.00 28.21 ? 32   GLY A C   1 
ATOM   213  O O   . GLY A 1 32  ? 2.952   3.464   3.881   1.00 28.64 ? 32   GLY A O   1 
ATOM   214  N N   . VAL A 1 33  ? 3.013   5.492   2.916   1.00 28.46 ? 33   VAL A N   1 
ATOM   215  C CA  . VAL A 1 33  ? 2.994   6.269   4.163   1.00 28.16 ? 33   VAL A CA  1 
ATOM   216  C C   . VAL A 1 33  ? 1.566   6.702   4.521   1.00 29.37 ? 33   VAL A C   1 
ATOM   217  O O   . VAL A 1 33  ? 0.853   7.339   3.729   1.00 27.99 ? 33   VAL A O   1 
ATOM   218  C CB  . VAL A 1 33  ? 3.928   7.503   4.091   1.00 27.77 ? 33   VAL A CB  1 
ATOM   219  C CG1 . VAL A 1 33  ? 3.708   8.406   5.292   1.00 29.32 ? 33   VAL A CG1 1 
ATOM   220  C CG2 . VAL A 1 33  ? 5.406   7.082   4.010   1.00 25.21 ? 33   VAL A CG2 1 
ATOM   221  N N   . VAL A 1 34  ? 1.151   6.303   5.721   1.00 30.09 ? 34   VAL A N   1 
ATOM   222  C CA  . VAL A 1 34  ? -0.193  6.591   6.211   1.00 29.42 ? 34   VAL A CA  1 
ATOM   223  C C   . VAL A 1 34  ? -0.311  8.086   6.361   1.00 29.04 ? 34   VAL A C   1 
ATOM   224  O O   . VAL A 1 34  ? 0.518   8.721   7.016   1.00 29.79 ? 34   VAL A O   1 
ATOM   225  C CB  . VAL A 1 34  ? -0.486  5.829   7.552   1.00 30.42 ? 34   VAL A CB  1 
ATOM   226  C CG1 . VAL A 1 34  ? -1.775  6.330   8.213   1.00 29.69 ? 34   VAL A CG1 1 
ATOM   227  C CG2 . VAL A 1 34  ? -0.549  4.316   7.291   1.00 27.16 ? 34   VAL A CG2 1 
ATOM   228  N N   . TYR A 1 35  ? -1.331  8.666   5.737   1.00 28.36 ? 35   TYR A N   1 
ATOM   229  C CA  . TYR A 1 35  ? -1.521  10.124  5.796   1.00 28.27 ? 35   TYR A CA  1 
ATOM   230  C C   . TYR A 1 35  ? -2.814  10.505  6.525   1.00 27.92 ? 35   TYR A C   1 
ATOM   231  O O   . TYR A 1 35  ? -3.044  11.659  6.827   1.00 29.01 ? 35   TYR A O   1 
ATOM   232  C CB  . TYR A 1 35  ? -1.498  10.753  4.390   1.00 28.70 ? 35   TYR A CB  1 
ATOM   233  C CG  . TYR A 1 35  ? -2.622  10.261  3.503   1.00 31.00 ? 35   TYR A CG  1 
ATOM   234  C CD1 . TYR A 1 35  ? -3.893  10.815  3.591   1.00 31.74 ? 35   TYR A CD1 1 
ATOM   235  C CD2 . TYR A 1 35  ? -2.416  9.227   2.602   1.00 30.51 ? 35   TYR A CD2 1 
ATOM   236  C CE1 . TYR A 1 35  ? -4.918  10.358  2.801   1.00 32.53 ? 35   TYR A CE1 1 
ATOM   237  C CE2 . TYR A 1 35  ? -3.432  8.770   1.805   1.00 31.40 ? 35   TYR A CE2 1 
ATOM   238  C CZ  . TYR A 1 35  ? -4.681  9.329   1.918   1.00 32.28 ? 35   TYR A CZ  1 
ATOM   239  O OH  . TYR A 1 35  ? -5.699  8.859   1.140   1.00 34.40 ? 35   TYR A OH  1 
ATOM   240  N N   . ALA A 1 36  ? -3.668  9.543   6.806   1.00 28.17 ? 36   ALA A N   1 
ATOM   241  C CA  . ALA A 1 36  ? -4.843  9.824   7.624   1.00 29.00 ? 36   ALA A CA  1 
ATOM   242  C C   . ALA A 1 36  ? -5.139  8.581   8.435   1.00 30.17 ? 36   ALA A C   1 
ATOM   243  O O   . ALA A 1 36  ? -4.924  7.458   7.968   1.00 30.81 ? 36   ALA A O   1 
ATOM   244  C CB  . ALA A 1 36  ? -6.052  10.242  6.773   1.00 27.81 ? 36   ALA A CB  1 
ATOM   245  N N   . CYS A 1 37  ? -5.580  8.774   9.671   1.00 29.81 ? 37   CYS A N   1 
ATOM   246  C CA  . CYS A 1 37  ? -5.847  7.624   10.516  1.00 30.26 ? 37   CYS A CA  1 
ATOM   247  C C   . CYS A 1 37  ? -6.713  7.928   11.728  1.00 29.68 ? 37   CYS A C   1 
ATOM   248  O O   . CYS A 1 37  ? -6.828  9.070   12.172  1.00 29.02 ? 37   CYS A O   1 
ATOM   249  C CB  . CYS A 1 37  ? -4.529  7.009   10.974  1.00 30.26 ? 37   CYS A CB  1 
ATOM   250  S SG  . CYS A 1 37  ? -3.649  7.952   12.218  1.00 32.82 ? 37   CYS A SG  1 
ATOM   251  N N   . VAL A 1 38  ? -7.312  6.864   12.240  1.00 28.82 ? 38   VAL A N   1 
ATOM   252  C CA  . VAL A 1 38  ? -8.070  6.916   13.474  1.00 28.46 ? 38   VAL A CA  1 
ATOM   253  C C   . VAL A 1 38  ? -7.697  5.711   14.311  1.00 27.63 ? 38   VAL A C   1 
ATOM   254  O O   . VAL A 1 38  ? -7.323  4.672   13.781  1.00 26.44 ? 38   VAL A O   1 
ATOM   255  C CB  . VAL A 1 38  ? -9.627  6.976   13.214  1.00 28.84 ? 38   VAL A CB  1 
ATOM   256  C CG1 . VAL A 1 38  ? -9.985  8.197   12.380  1.00 29.54 ? 38   VAL A CG1 1 
ATOM   257  C CG2 . VAL A 1 38  ? -10.108 5.743   12.520  1.00 27.32 ? 38   VAL A CG2 1 
ATOM   258  N N   . ALA A 1 39  ? -7.770  5.869   15.629  1.00 27.88 ? 39   ALA A N   1 
ATOM   259  C CA  . ALA A 1 39  ? -7.528  4.749   16.543  1.00 28.58 ? 39   ALA A CA  1 
ATOM   260  C C   . ALA A 1 39  ? -8.644  4.699   17.562  1.00 29.11 ? 39   ALA A C   1 
ATOM   261  O O   . ALA A 1 39  ? -9.141  5.742   17.993  1.00 28.66 ? 39   ALA A O   1 
ATOM   262  C CB  . ALA A 1 39  ? -6.174  4.886   17.224  1.00 27.78 ? 39   ALA A CB  1 
ATOM   263  N N   . GLN A 1 40  ? -9.060  3.501   17.948  1.00 30.51 ? 40   GLN A N   1 
ATOM   264  C CA  . GLN A 1 40  ? -10.172 3.422   18.886  1.00 32.92 ? 40   GLN A CA  1 
ATOM   265  C C   . GLN A 1 40  ? -9.783  3.963   20.278  1.00 34.57 ? 40   GLN A C   1 
ATOM   266  O O   . GLN A 1 40  ? -10.658 4.326   21.038  1.00 35.93 ? 40   GLN A O   1 
ATOM   267  C CB  . GLN A 1 40  ? -10.853 2.041   18.907  1.00 33.03 ? 40   GLN A CB  1 
ATOM   268  C CG  . GLN A 1 40  ? -10.358 1.023   19.895  1.00 34.20 ? 40   GLN A CG  1 
ATOM   269  C CD  . GLN A 1 40  ? -10.922 -0.363  19.573  1.00 33.20 ? 40   GLN A CD  1 
ATOM   270  O OE1 . GLN A 1 40  ? -10.228 -1.376  19.689  1.00 30.17 ? 40   GLN A OE1 1 
ATOM   271  N NE2 . GLN A 1 40  ? -12.180 -0.402  19.135  1.00 33.51 ? 40   GLN A NE2 1 
ATOM   272  N N   . GLY A 1 41  ? -8.500  4.097   20.595  1.00 36.17 ? 41   GLY A N   1 
ATOM   273  C CA  . GLY A 1 41  ? -8.159  4.944   21.732  1.00 37.63 ? 41   GLY A CA  1 
ATOM   274  C C   . GLY A 1 41  ? -9.251  6.001   21.805  1.00 39.07 ? 41   GLY A C   1 
ATOM   275  O O   . GLY A 1 41  ? -9.670  6.539   20.783  1.00 39.31 ? 41   GLY A O   1 
ATOM   276  N N   . GLU A 1 42  ? -9.717  6.302   23.013  1.00 40.34 ? 42   GLU A N   1 
ATOM   277  C CA  . GLU A 1 42  ? -10.917 7.128   23.211  1.00 41.09 ? 42   GLU A CA  1 
ATOM   278  C C   . GLU A 1 42  ? -11.401 7.048   24.645  1.00 41.96 ? 42   GLU A C   1 
ATOM   279  O O   . GLU A 1 42  ? -11.633 8.076   25.297  1.00 42.14 ? 42   GLU A O   1 
ATOM   280  C CB  . GLU A 1 42  ? -12.081 6.688   22.320  1.00 40.89 ? 42   GLU A CB  1 
ATOM   281  C CG  . GLU A 1 42  ? -13.317 7.528   22.526  1.00 40.86 ? 42   GLU A CG  1 
ATOM   282  C CD  . GLU A 1 42  ? -13.054 9.002   22.282  1.00 41.06 ? 42   GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 42  ? -11.968 9.332   21.757  1.00 41.03 ? 42   GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 42  ? -13.926 9.833   22.615  1.00 40.89 ? 42   GLU A OE2 1 
ATOM   285  N N   . GLU A 1 43  ? -11.597 5.812   25.101  1.00 42.69 ? 43   GLU A N   1 
ATOM   286  C CA  . GLU A 1 43  ? -11.944 5.566   26.491  1.00 43.18 ? 43   GLU A CA  1 
ATOM   287  C C   . GLU A 1 43  ? -10.718 5.946   27.274  1.00 43.83 ? 43   GLU A C   1 
ATOM   288  O O   . GLU A 1 43  ? -10.823 6.326   28.444  1.00 44.19 ? 43   GLU A O   1 
ATOM   289  C CB  . GLU A 1 43  ? -12.350 4.138   26.790  1.00 43.32 ? 43   GLU A CB  1 
ATOM   290  C CG  . GLU A 1 43  ? -12.244 3.861   28.285  1.00 43.10 ? 43   GLU A CG  1 
ATOM   291  C CD  . GLU A 1 43  ? -13.353 2.957   28.800  1.00 42.52 ? 43   GLU A CD  1 
ATOM   292  O OE1 . GLU A 1 43  ? -13.877 3.231   29.898  1.00 42.10 ? 43   GLU A OE1 1 
ATOM   293  O OE2 . GLU A 1 43  ? -13.710 1.978   28.109  1.00 42.66 ? 43   GLU A OE2 1 
ATOM   294  N N   . SER A 1 44  ? -9.551  5.694   26.677  1.00 43.83 ? 44   SER A N   1 
ATOM   295  C CA  . SER A 1 44  ? -8.966  4.351   26.601  1.00 43.54 ? 44   SER A CA  1 
ATOM   296  C C   . SER A 1 44  ? -7.570  4.370   27.261  1.00 43.17 ? 44   SER A C   1 
ATOM   297  O O   . SER A 1 44  ? -6.813  3.429   27.060  1.00 43.56 ? 44   SER A O   1 
ATOM   298  C CB  . SER A 1 44  ? -8.924  3.699   25.206  1.00 43.48 ? 44   SER A CB  1 
ATOM   299  O OG  . SER A 1 44  ? -7.595  3.597   24.729  1.00 43.83 ? 44   SER A OG  1 
ATOM   300  N N   . ASP A 1 45  ? -7.110  5.480   27.856  1.00 42.38 ? 45   ASP A N   1 
ATOM   301  C CA  . ASP A 1 45  ? -6.416  6.583   27.141  1.00 41.34 ? 45   ASP A CA  1 
ATOM   302  C C   . ASP A 1 45  ? -7.102  7.737   26.377  1.00 40.02 ? 45   ASP A C   1 
ATOM   303  O O   . ASP A 1 45  ? -7.735  7.534   25.339  1.00 41.08 ? 45   ASP A O   1 
ATOM   304  C CB  . ASP A 1 45  ? -5.387  5.904   26.228  1.00 41.72 ? 45   ASP A CB  1 
ATOM   305  C CG  . ASP A 1 45  ? -3.942  6.162   26.678  1.00 41.56 ? 45   ASP A CG  1 
ATOM   306  O OD1 . ASP A 1 45  ? -3.630  7.301   27.110  1.00 40.92 ? 45   ASP A OD1 1 
ATOM   307  O OD2 . ASP A 1 45  ? -3.116  5.227   26.586  1.00 41.43 ? 45   ASP A OD2 1 
ATOM   308  N N   . PRO A 1 46  ? -6.960  8.961   26.891  1.00 37.86 ? 46   PRO A N   1 
ATOM   309  C CA  . PRO A 1 46  ? -7.469  10.110  26.170  1.00 35.91 ? 46   PRO A CA  1 
ATOM   310  C C   . PRO A 1 46  ? -6.305  10.910  25.611  1.00 33.58 ? 46   PRO A C   1 
ATOM   311  O O   . PRO A 1 46  ? -6.456  11.723  24.711  1.00 33.63 ? 46   PRO A O   1 
ATOM   312  C CB  . PRO A 1 46  ? -8.195  10.901  27.266  1.00 36.23 ? 46   PRO A CB  1 
ATOM   313  C CG  . PRO A 1 46  ? -7.522  10.465  28.590  1.00 36.86 ? 46   PRO A CG  1 
ATOM   314  C CD  . PRO A 1 46  ? -6.595  9.310   28.274  1.00 37.85 ? 46   PRO A CD  1 
ATOM   315  N N   . ASN A 1 47  ? -5.133  10.658  26.156  1.00 31.22 ? 47   ASN A N   1 
ATOM   316  C CA  . ASN A 1 47  ? -3.926  11.291  25.662  1.00 29.41 ? 47   ASN A CA  1 
ATOM   317  C C   . ASN A 1 47  ? -3.216  10.332  24.721  1.00 29.03 ? 47   ASN A C   1 
ATOM   318  O O   . ASN A 1 47  ? -2.068  10.522  24.355  1.00 29.02 ? 47   ASN A O   1 
ATOM   319  C CB  . ASN A 1 47  ? -3.025  11.672  26.819  1.00 28.61 ? 47   ASN A CB  1 
ATOM   320  C CG  . ASN A 1 47  ? -3.676  12.648  27.742  1.00 28.29 ? 47   ASN A CG  1 
ATOM   321  O OD1 . ASN A 1 47  ? -4.329  13.579  27.297  1.00 27.58 ? 47   ASN A OD1 1 
ATOM   322  N ND2 . ASN A 1 47  ? -3.522  12.438  29.044  1.00 28.92 ? 47   ASN A ND2 1 
ATOM   323  N N   . PHE A 1 48  ? -3.926  9.281   24.346  1.00 28.69 ? 48   PHE A N   1 
ATOM   324  C CA  . PHE A 1 48  ? -3.412  8.312   23.404  1.00 29.57 ? 48   PHE A CA  1 
ATOM   325  C C   . PHE A 1 48  ? -3.146  8.974   22.027  1.00 29.42 ? 48   PHE A C   1 
ATOM   326  O O   . PHE A 1 48  ? -3.938  9.788   21.530  1.00 27.46 ? 48   PHE A O   1 
ATOM   327  C CB  . PHE A 1 48  ? -4.354  7.095   23.294  1.00 30.04 ? 48   PHE A CB  1 
ATOM   328  C CG  . PHE A 1 48  ? -3.811  6.009   22.424  1.00 31.45 ? 48   PHE A CG  1 
ATOM   329  C CD1 . PHE A 1 48  ? -2.825  5.155   22.902  1.00 31.40 ? 48   PHE A CD1 1 
ATOM   330  C CD2 . PHE A 1 48  ? -4.230  5.885   21.095  1.00 32.47 ? 48   PHE A CD2 1 
ATOM   331  C CE1 . PHE A 1 48  ? -2.284  4.181   22.084  1.00 32.47 ? 48   PHE A CE1 1 
ATOM   332  C CE2 . PHE A 1 48  ? -3.706  4.910   20.277  1.00 29.79 ? 48   PHE A CE2 1 
ATOM   333  C CZ  . PHE A 1 48  ? -2.733  4.060   20.758  1.00 31.04 ? 48   PHE A CZ  1 
ATOM   334  N N   . ASP A 1 49  ? -1.992  8.629   21.459  1.00 30.29 ? 49   ASP A N   1 
ATOM   335  C CA  . ASP A 1 49  ? -1.518  9.152   20.154  1.00 31.50 ? 49   ASP A CA  1 
ATOM   336  C C   . ASP A 1 49  ? -1.774  8.146   19.041  1.00 29.84 ? 49   ASP A C   1 
ATOM   337  O O   . ASP A 1 49  ? -1.081  7.145   18.927  1.00 31.21 ? 49   ASP A O   1 
ATOM   338  C CB  . ASP A 1 49  ? -0.011  9.452   20.242  1.00 32.72 ? 49   ASP A CB  1 
ATOM   339  C CG  . ASP A 1 49  ? 0.530   10.183  19.015  1.00 34.60 ? 49   ASP A CG  1 
ATOM   340  O OD1 . ASP A 1 49  ? -0.263  10.612  18.147  1.00 34.13 ? 49   ASP A OD1 1 
ATOM   341  O OD2 . ASP A 1 49  ? 1.773   10.329  18.938  1.00 38.59 ? 49   ASP A OD2 1 
ATOM   342  N N   . LYS A 1 50  ? -2.800  8.392   18.245  1.00 28.69 ? 50   LYS A N   1 
ATOM   343  C CA  . LYS A 1 50  ? -3.139  7.476   17.157  1.00 28.60 ? 50   LYS A CA  1 
ATOM   344  C C   . LYS A 1 50  ? -1.970  7.314   16.183  1.00 27.87 ? 50   LYS A C   1 
ATOM   345  O O   . LYS A 1 50  ? -1.768  6.257   15.617  1.00 27.41 ? 50   LYS A O   1 
ATOM   346  C CB  . LYS A 1 50  ? -4.378  7.943   16.377  1.00 28.48 ? 50   LYS A CB  1 
ATOM   347  C CG  . LYS A 1 50  ? -4.338  9.374   15.907  1.00 28.81 ? 50   LYS A CG  1 
ATOM   348  C CD  . LYS A 1 50  ? -5.643  9.742   15.238  1.00 30.28 ? 50   LYS A CD  1 
ATOM   349  C CE  . LYS A 1 50  ? -5.532  11.074  14.530  1.00 30.37 ? 50   LYS A CE  1 
ATOM   350  N NZ  . LYS A 1 50  ? -6.616  11.212  13.518  1.00 33.43 ? 50   LYS A NZ  1 
ATOM   351  N N   . TRP A 1 51  ? -1.203  8.371   15.992  1.00 27.91 ? 51   TRP A N   1 
ATOM   352  C CA  . TRP A 1 51  ? -0.113  8.322   15.027  1.00 29.15 ? 51   TRP A CA  1 
ATOM   353  C C   . TRP A 1 51  ? 0.952   7.304   15.415  1.00 29.89 ? 51   TRP A C   1 
ATOM   354  O O   . TRP A 1 51  ? 1.636   6.768   14.539  1.00 29.58 ? 51   TRP A O   1 
ATOM   355  C CB  . TRP A 1 51  ? 0.459   9.704   14.774  1.00 28.74 ? 51   TRP A CB  1 
ATOM   356  C CG  . TRP A 1 51  ? -0.489  10.440  13.885  1.00 31.66 ? 51   TRP A CG  1 
ATOM   357  C CD1 . TRP A 1 51  ? -1.427  11.377  14.255  1.00 30.89 ? 51   TRP A CD1 1 
ATOM   358  C CD2 . TRP A 1 51  ? -0.655  10.238  12.467  1.00 31.66 ? 51   TRP A CD2 1 
ATOM   359  N NE1 . TRP A 1 51  ? -2.138  11.795  13.140  1.00 33.60 ? 51   TRP A NE1 1 
ATOM   360  C CE2 . TRP A 1 51  ? -1.680  11.117  12.035  1.00 32.81 ? 51   TRP A CE2 1 
ATOM   361  C CE3 . TRP A 1 51  ? -0.024  9.417   11.523  1.00 30.56 ? 51   TRP A CE3 1 
ATOM   362  C CZ2 . TRP A 1 51  ? -2.084  11.195  10.691  1.00 33.44 ? 51   TRP A CZ2 1 
ATOM   363  C CZ3 . TRP A 1 51  ? -0.425  9.501   10.183  1.00 31.69 ? 51   TRP A CZ3 1 
ATOM   364  C CH2 . TRP A 1 51  ? -1.443  10.379  9.786   1.00 31.96 ? 51   TRP A CH2 1 
ATOM   365  N N   . SER A 1 52  ? 1.020   6.990   16.715  1.00 29.36 ? 52   SER A N   1 
ATOM   366  C CA  . SER A 1 52  ? 2.037   6.073   17.254  1.00 29.77 ? 52   SER A CA  1 
ATOM   367  C C   . SER A 1 52  ? 1.838   4.678   16.690  1.00 29.35 ? 52   SER A C   1 
ATOM   368  O O   . SER A 1 52  ? 2.771   3.882   16.611  1.00 30.47 ? 52   SER A O   1 
ATOM   369  C CB  . SER A 1 52  ? 2.018   6.038   18.801  1.00 29.83 ? 52   SER A CB  1 
ATOM   370  O OG  . SER A 1 52  ? 0.764   5.585   19.318  1.00 30.50 ? 52   SER A OG  1 
ATOM   371  N N   . LEU A 1 53  ? 0.616   4.408   16.265  1.00 29.26 ? 53   LEU A N   1 
ATOM   372  C CA  . LEU A 1 53  ? 0.260   3.107   15.691  1.00 29.12 ? 53   LEU A CA  1 
ATOM   373  C C   . LEU A 1 53  ? 0.543   3.016   14.192  1.00 27.40 ? 53   LEU A C   1 
ATOM   374  O O   . LEU A 1 53  ? 0.604   1.933   13.635  1.00 27.60 ? 53   LEU A O   1 
ATOM   375  C CB  . LEU A 1 53  ? -1.229  2.802   15.923  1.00 29.91 ? 53   LEU A CB  1 
ATOM   376  C CG  . LEU A 1 53  ? -1.673  2.557   17.365  1.00 30.68 ? 53   LEU A CG  1 
ATOM   377  C CD1 . LEU A 1 53  ? -3.186  2.417   17.353  1.00 30.60 ? 53   LEU A CD1 1 
ATOM   378  C CD2 . LEU A 1 53  ? -0.971  1.316   18.006  1.00 29.66 ? 53   LEU A CD2 1 
ATOM   379  N N   . PHE A 1 54  ? 0.717   4.162   13.553  1.00 27.12 ? 54   PHE A N   1 
ATOM   380  C CA  . PHE A 1 54  ? 0.622   4.250   12.088  1.00 26.89 ? 54   PHE A CA  1 
ATOM   381  C C   . PHE A 1 54  ? 1.808   4.889   11.366  1.00 27.46 ? 54   PHE A C   1 
ATOM   382  O O   . PHE A 1 54  ? 1.961   4.728   10.137  1.00 27.77 ? 54   PHE A O   1 
ATOM   383  C CB  . PHE A 1 54  ? -0.652  5.026   11.693  1.00 26.09 ? 54   PHE A CB  1 
ATOM   384  C CG  . PHE A 1 54  ? -1.921  4.218   11.826  1.00 25.98 ? 54   PHE A CG  1 
ATOM   385  C CD1 . PHE A 1 54  ? -2.229  3.227   10.902  1.00 25.66 ? 54   PHE A CD1 1 
ATOM   386  C CD2 . PHE A 1 54  ? -2.789  4.428   12.883  1.00 25.32 ? 54   PHE A CD2 1 
ATOM   387  C CE1 . PHE A 1 54  ? -3.383  2.484   11.024  1.00 25.82 ? 54   PHE A CE1 1 
ATOM   388  C CE2 . PHE A 1 54  ? -3.965  3.681   13.005  1.00 24.38 ? 54   PHE A CE2 1 
ATOM   389  C CZ  . PHE A 1 54  ? -4.254  2.715   12.084  1.00 24.00 ? 54   PHE A CZ  1 
ATOM   390  N N   . TYR A 1 55  ? 2.597   5.646   12.121  1.00 26.98 ? 55   TYR A N   1 
ATOM   391  C CA  . TYR A 1 55  ? 3.722   6.396   11.588  1.00 27.00 ? 55   TYR A CA  1 
ATOM   392  C C   . TYR A 1 55  ? 4.959   6.306   12.478  1.00 26.68 ? 55   TYR A C   1 
ATOM   393  O O   . TYR A 1 55  ? 4.868   6.411   13.675  1.00 26.51 ? 55   TYR A O   1 
ATOM   394  C CB  . TYR A 1 55  ? 3.364   7.874   11.385  1.00 27.01 ? 55   TYR A CB  1 
ATOM   395  C CG  . TYR A 1 55  ? 4.510   8.608   10.729  1.00 28.04 ? 55   TYR A CG  1 
ATOM   396  C CD1 . TYR A 1 55  ? 4.910   8.272   9.443   1.00 30.31 ? 55   TYR A CD1 1 
ATOM   397  C CD2 . TYR A 1 55  ? 5.240   9.579   11.412  1.00 30.01 ? 55   TYR A CD2 1 
ATOM   398  C CE1 . TYR A 1 55  ? 5.989   8.895   8.826   1.00 30.92 ? 55   TYR A CE1 1 
ATOM   399  C CE2 . TYR A 1 55  ? 6.322   10.220  10.806  1.00 31.73 ? 55   TYR A CE2 1 
ATOM   400  C CZ  . TYR A 1 55  ? 6.690   9.871   9.509   1.00 32.64 ? 55   TYR A CZ  1 
ATOM   401  O OH  . TYR A 1 55  ? 7.754   10.490  8.889   1.00 32.84 ? 55   TYR A OH  1 
ATOM   402  N N   . LYS A 1 56  ? 6.110   6.094   11.854  1.00 27.04 ? 56   LYS A N   1 
ATOM   403  C CA  . LYS A 1 56  ? 7.401   6.274   12.508  1.00 27.17 ? 56   LYS A CA  1 
ATOM   404  C C   . LYS A 1 56  ? 8.493   6.565   11.480  1.00 27.71 ? 56   LYS A C   1 
ATOM   405  O O   . LYS A 1 56  ? 8.686   5.810   10.544  1.00 27.11 ? 56   LYS A O   1 
ATOM   406  C CB  . LYS A 1 56  ? 7.764   5.054   13.335  1.00 27.43 ? 56   LYS A CB  1 
ATOM   407  C CG  . LYS A 1 56  ? 8.969   5.289   14.208  1.00 27.23 ? 56   LYS A CG  1 
ATOM   408  C CD  . LYS A 1 56  ? 9.133   4.179   15.211  1.00 29.39 ? 56   LYS A CD  1 
ATOM   409  C CE  . LYS A 1 56  ? 10.440  4.317   16.004  1.00 29.28 ? 56   LYS A CE  1 
ATOM   410  N NZ  . LYS A 1 56  ? 10.861  2.981   16.520  1.00 30.02 ? 56   LYS A NZ  1 
ATOM   411  N N   . GLU A 1 57  ? 9.192   7.681   11.661  1.00 29.24 ? 57   GLU A N   1 
ATOM   412  C CA  . GLU A 1 57  ? 10.251  8.092   10.719  1.00 30.24 ? 57   GLU A CA  1 
ATOM   413  C C   . GLU A 1 57  ? 11.353  7.032   10.651  1.00 29.40 ? 57   GLU A C   1 
ATOM   414  O O   . GLU A 1 57  ? 11.518  6.232   11.565  1.00 29.86 ? 57   GLU A O   1 
ATOM   415  C CB  . GLU A 1 57  ? 10.834  9.472   11.079  1.00 30.98 ? 57   GLU A CB  1 
ATOM   416  C CG  . GLU A 1 57  ? 11.903  9.450   12.168  1.00 33.72 ? 57   GLU A CG  1 
ATOM   417  C CD  . GLU A 1 57  ? 12.626  10.807  12.335  1.00 36.68 ? 57   GLU A CD  1 
ATOM   418  O OE1 . GLU A 1 57  ? 12.114  11.830  11.824  1.00 40.18 ? 57   GLU A OE1 1 
ATOM   419  O OE2 . GLU A 1 57  ? 13.703  10.854  12.983  1.00 36.29 ? 57   GLU A OE2 1 
ATOM   420  N N   . ASP A 1 58  ? 12.078  7.013   9.542   1.00 28.81 ? 58   ASP A N   1 
ATOM   421  C CA  . ASP A 1 58  ? 13.132  6.004   9.322   1.00 28.79 ? 58   ASP A CA  1 
ATOM   422  C C   . ASP A 1 58  ? 13.986  5.730   10.559  1.00 27.31 ? 58   ASP A C   1 
ATOM   423  O O   . ASP A 1 58  ? 14.464  6.638   11.219  1.00 26.19 ? 58   ASP A O   1 
ATOM   424  C CB  . ASP A 1 58  ? 14.037  6.388   8.142   1.00 29.23 ? 58   ASP A CB  1 
ATOM   425  C CG  . ASP A 1 58  ? 13.480  5.917   6.798   1.00 30.88 ? 58   ASP A CG  1 
ATOM   426  O OD1 . ASP A 1 58  ? 12.239  5.775   6.672   1.00 32.98 ? 58   ASP A OD1 1 
ATOM   427  O OD2 . ASP A 1 58  ? 14.289  5.678   5.874   1.00 32.46 ? 58   ASP A OD2 1 
ATOM   428  N N   . TYR A 1 59  ? 14.155  4.449   10.840  1.00 26.87 ? 59   TYR A N   1 
ATOM   429  C CA  . TYR A 1 59  ? 14.970  3.970   11.954  1.00 27.34 ? 59   TYR A CA  1 
ATOM   430  C C   . TYR A 1 59  ? 15.765  2.724   11.535  1.00 27.10 ? 59   TYR A C   1 
ATOM   431  O O   . TYR A 1 59  ? 15.393  1.996   10.600  1.00 26.38 ? 59   TYR A O   1 
ATOM   432  C CB  . TYR A 1 59  ? 14.104  3.691   13.214  1.00 26.98 ? 59   TYR A CB  1 
ATOM   433  C CG  . TYR A 1 59  ? 12.883  2.813   12.958  1.00 29.05 ? 59   TYR A CG  1 
ATOM   434  C CD1 . TYR A 1 59  ? 12.841  1.496   13.396  1.00 29.21 ? 59   TYR A CD1 1 
ATOM   435  C CD2 . TYR A 1 59  ? 11.795  3.300   12.261  1.00 29.41 ? 59   TYR A CD2 1 
ATOM   436  C CE1 . TYR A 1 59  ? 11.753  0.702   13.158  1.00 29.27 ? 59   TYR A CE1 1 
ATOM   437  C CE2 . TYR A 1 59  ? 10.695  2.512   12.026  1.00 32.56 ? 59   TYR A CE2 1 
ATOM   438  C CZ  . TYR A 1 59  ? 10.681  1.211   12.473  1.00 32.05 ? 59   TYR A CZ  1 
ATOM   439  O OH  . TYR A 1 59  ? 9.580   0.424   12.220  1.00 34.99 ? 59   TYR A OH  1 
ATOM   440  N N   . ASP A 1 60  ? 16.883  2.519   12.220  1.00 26.64 ? 60   ASP A N   1 
ATOM   441  C CA  . ASP A 1 60  ? 17.701  1.335   12.039  1.00 27.03 ? 60   ASP A CA  1 
ATOM   442  C C   . ASP A 1 60  ? 17.304  0.296   13.059  1.00 26.79 ? 60   ASP A C   1 
ATOM   443  O O   . ASP A 1 60  ? 16.915  0.623   14.162  1.00 26.72 ? 60   ASP A O   1 
ATOM   444  C CB  . ASP A 1 60  ? 19.191  1.661   12.218  1.00 27.82 ? 60   ASP A CB  1 
ATOM   445  C CG  . ASP A 1 60  ? 19.724  2.573   11.132  1.00 30.42 ? 60   ASP A CG  1 
ATOM   446  O OD1 . ASP A 1 60  ? 18.963  2.869   10.180  1.00 33.74 ? 60   ASP A OD1 1 
ATOM   447  O OD2 . ASP A 1 60  ? 20.907  2.986   11.221  1.00 33.37 ? 60   ASP A OD2 1 
ATOM   448  N N   . ILE A 1 61  ? 17.413  -0.962  12.666  1.00 27.78 ? 61   ILE A N   1 
ATOM   449  C CA  . ILE A 1 61  ? 17.170  -2.098  13.547  1.00 28.47 ? 61   ILE A CA  1 
ATOM   450  C C   . ILE A 1 61  ? 18.373  -3.020  13.443  1.00 29.11 ? 61   ILE A C   1 
ATOM   451  O O   . ILE A 1 61  ? 19.099  -3.001  12.448  1.00 30.07 ? 61   ILE A O   1 
ATOM   452  C CB  . ILE A 1 61  ? 15.857  -2.867  13.171  1.00 29.00 ? 61   ILE A CB  1 
ATOM   453  C CG1 . ILE A 1 61  ? 15.975  -3.508  11.795  1.00 28.95 ? 61   ILE A CG1 1 
ATOM   454  C CG2 . ILE A 1 61  ? 14.642  -1.933  13.168  1.00 28.64 ? 61   ILE A CG2 1 
ATOM   455  C CD1 . ILE A 1 61  ? 14.973  -4.586  11.559  1.00 28.47 ? 61   ILE A CD1 1 
ATOM   456  N N   . GLU A 1 62  ? 18.624  -3.801  14.480  1.00 29.65 ? 62   GLU A N   1 
ATOM   457  C CA  . GLU A 1 62  ? 19.694  -4.769  14.401  1.00 29.98 ? 62   GLU A CA  1 
ATOM   458  C C   . GLU A 1 62  ? 19.132  -6.153  14.172  1.00 30.03 ? 62   GLU A C   1 
ATOM   459  O O   . GLU A 1 62  ? 18.192  -6.575  14.842  1.00 29.41 ? 62   GLU A O   1 
ATOM   460  C CB  . GLU A 1 62  ? 20.575  -4.723  15.640  1.00 30.43 ? 62   GLU A CB  1 
ATOM   461  C CG  . GLU A 1 62  ? 22.039  -4.774  15.264  1.00 32.08 ? 62   GLU A CG  1 
ATOM   462  C CD  . GLU A 1 62  ? 22.685  -6.099  15.573  1.00 33.78 ? 62   GLU A CD  1 
ATOM   463  O OE1 . GLU A 1 62  ? 22.169  -7.150  15.127  1.00 36.03 ? 62   GLU A OE1 1 
ATOM   464  O OE2 . GLU A 1 62  ? 23.725  -6.084  16.264  1.00 34.90 ? 62   GLU A OE2 1 
ATOM   465  N N   . VAL A 1 63  ? 19.711  -6.841  13.195  1.00 30.60 ? 63   VAL A N   1 
ATOM   466  C CA  . VAL A 1 63  ? 19.281  -8.191  12.838  1.00 31.25 ? 63   VAL A CA  1 
ATOM   467  C C   . VAL A 1 63  ? 20.403  -9.208  13.000  1.00 31.93 ? 63   VAL A C   1 
ATOM   468  O O   . VAL A 1 63  ? 21.570  -8.951  12.686  1.00 32.27 ? 63   VAL A O   1 
ATOM   469  C CB  . VAL A 1 63  ? 18.770  -8.250  11.396  1.00 31.64 ? 63   VAL A CB  1 
ATOM   470  C CG1 . VAL A 1 63  ? 18.231  -9.643  11.100  1.00 30.68 ? 63   VAL A CG1 1 
ATOM   471  C CG2 . VAL A 1 63  ? 17.701  -7.178  11.168  1.00 31.92 ? 63   VAL A CG2 1 
ATOM   472  N N   . GLU A 1 64  ? 20.039  -10.369 13.514  1.00 32.50 ? 64   GLU A N   1 
ATOM   473  C CA  . GLU A 1 64  ? 20.994  -11.454 13.666  1.00 33.10 ? 64   GLU A CA  1 
ATOM   474  C C   . GLU A 1 64  ? 20.534  -12.691 12.912  1.00 32.48 ? 64   GLU A C   1 
ATOM   475  O O   . GLU A 1 64  ? 19.530  -13.295 13.258  1.00 32.24 ? 64   GLU A O   1 
ATOM   476  C CB  . GLU A 1 64  ? 21.198  -11.791 15.143  1.00 33.40 ? 64   GLU A CB  1 
ATOM   477  C CG  . GLU A 1 64  ? 22.182  -12.940 15.365  1.00 35.59 ? 64   GLU A CG  1 
ATOM   478  C CD  . GLU A 1 64  ? 22.441  -13.219 16.832  1.00 37.78 ? 64   GLU A CD  1 
ATOM   479  O OE1 . GLU A 1 64  ? 21.912  -12.464 17.682  1.00 39.39 ? 64   GLU A OE1 1 
ATOM   480  O OE2 . GLU A 1 64  ? 23.174  -14.189 17.137  1.00 38.85 ? 64   GLU A OE2 1 
ATOM   481  N N   . ASP A 1 65  ? 21.281  -13.073 11.882  1.00 32.33 ? 65   ASP A N   1 
ATOM   482  C CA  . ASP A 1 65  ? 20.944  -14.297 11.147  1.00 32.51 ? 65   ASP A CA  1 
ATOM   483  C C   . ASP A 1 65  ? 21.317  -15.564 11.922  1.00 31.87 ? 65   ASP A C   1 
ATOM   484  O O   . ASP A 1 65  ? 21.804  -15.508 13.055  1.00 31.55 ? 65   ASP A O   1 
ATOM   485  C CB  . ASP A 1 65  ? 21.492  -14.294 9.699   1.00 33.12 ? 65   ASP A CB  1 
ATOM   486  C CG  . ASP A 1 65  ? 23.021  -14.387 9.607   1.00 34.61 ? 65   ASP A CG  1 
ATOM   487  O OD1 . ASP A 1 65  ? 23.656  -15.090 10.434  1.00 35.04 ? 65   ASP A OD1 1 
ATOM   488  O OD2 . ASP A 1 65  ? 23.579  -13.768 8.655   1.00 36.09 ? 65   ASP A OD2 1 
ATOM   489  N N   . GLU A 1 66  ? 21.063  -16.701 11.291  1.00 31.69 ? 66   GLU A N   1 
ATOM   490  C CA  . GLU A 1 66  ? 21.123  -17.996 11.954  1.00 31.68 ? 66   GLU A CA  1 
ATOM   491  C C   . GLU A 1 66  ? 22.581  -18.339 12.172  1.00 31.41 ? 66   GLU A C   1 
ATOM   492  O O   . GLU A 1 66  ? 22.930  -19.260 12.909  1.00 31.35 ? 66   GLU A O   1 
ATOM   493  C CB  . GLU A 1 66  ? 20.456  -19.081 11.096  1.00 32.29 ? 66   GLU A CB  1 
ATOM   494  C CG  . GLU A 1 66  ? 19.012  -18.776 10.650  1.00 33.43 ? 66   GLU A CG  1 
ATOM   495  C CD  . GLU A 1 66  ? 17.998  -18.853 11.781  1.00 34.13 ? 66   GLU A CD  1 
ATOM   496  O OE1 . GLU A 1 66  ? 18.284  -18.353 12.891  1.00 35.23 ? 66   GLU A OE1 1 
ATOM   497  O OE2 . GLU A 1 66  ? 16.908  -19.414 11.555  1.00 35.12 ? 66   GLU A OE2 1 
ATOM   498  N N   . ASN A 1 67  ? 23.435  -17.587 11.499  1.00 30.92 ? 67   ASN A N   1 
ATOM   499  C CA  . ASN A 1 67  ? 24.865  -17.865 11.547  1.00 30.33 ? 67   ASN A CA  1 
ATOM   500  C C   . ASN A 1 67  ? 25.454  -17.223 12.794  1.00 29.12 ? 67   ASN A C   1 
ATOM   501  O O   . ASN A 1 67  ? 26.514  -17.619 13.262  1.00 28.65 ? 67   ASN A O   1 
ATOM   502  C CB  . ASN A 1 67  ? 25.575  -17.337 10.291  1.00 30.29 ? 67   ASN A CB  1 
ATOM   503  C CG  . ASN A 1 67  ? 25.260  -18.164 9.044   1.00 30.58 ? 67   ASN A CG  1 
ATOM   504  O OD1 . ASN A 1 67  ? 24.894  -19.335 9.143   1.00 30.79 ? 67   ASN A OD1 1 
ATOM   505  N ND2 . ASN A 1 67  ? 25.405  -17.555 7.867   1.00 26.57 ? 67   ASN A ND2 1 
ATOM   506  N N   . GLY A 1 68  ? 24.750  -16.222 13.316  1.00 27.62 ? 68   GLY A N   1 
ATOM   507  C CA  . GLY A 1 68  ? 25.255  -15.424 14.434  1.00 26.18 ? 68   GLY A CA  1 
ATOM   508  C C   . GLY A 1 68  ? 25.720  -14.052 13.979  1.00 25.30 ? 68   GLY A C   1 
ATOM   509  O O   . GLY A 1 68  ? 26.156  -13.225 14.781  1.00 24.33 ? 68   GLY A O   1 
ATOM   510  N N   . THR A 1 69  ? 25.610  -13.824 12.675  1.00 24.89 ? 69   THR A N   1 
ATOM   511  C CA  . THR A 1 69  ? 25.975  -12.544 12.049  1.00 24.25 ? 69   THR A CA  1 
ATOM   512  C C   . THR A 1 69  ? 24.981  -11.424 12.321  1.00 24.06 ? 69   THR A C   1 
ATOM   513  O O   . THR A 1 69  ? 23.787  -11.574 12.129  1.00 24.32 ? 69   THR A O   1 
ATOM   514  C CB  . THR A 1 69  ? 26.099  -12.669 10.512  1.00 24.33 ? 69   THR A CB  1 
ATOM   515  O OG1 . THR A 1 69  ? 27.132  -13.605 10.192  1.00 24.78 ? 69   THR A OG1 1 
ATOM   516  C CG2 . THR A 1 69  ? 26.398  -11.301 9.881   1.00 22.03 ? 69   THR A CG2 1 
ATOM   517  N N   . LYS A 1 70  ? 25.510  -10.287 12.737  1.00 24.41 ? 70   LYS A N   1 
ATOM   518  C CA  . LYS A 1 70  ? 24.701  -9.138  13.105  1.00 25.65 ? 70   LYS A CA  1 
ATOM   519  C C   . LYS A 1 70  ? 24.853  -8.042  12.096  1.00 25.98 ? 70   LYS A C   1 
ATOM   520  O O   . LYS A 1 70  ? 25.956  -7.600  11.829  1.00 26.53 ? 70   LYS A O   1 
ATOM   521  C CB  . LYS A 1 70  ? 25.117  -8.614  14.485  1.00 25.76 ? 70   LYS A CB  1 
ATOM   522  C CG  . LYS A 1 70  ? 24.990  -9.640  15.597  1.00 26.01 ? 70   LYS A CG  1 
ATOM   523  C CD  . LYS A 1 70  ? 26.041  -9.373  16.668  1.00 29.52 ? 70   LYS A CD  1 
ATOM   524  C CE  . LYS A 1 70  ? 26.123  -10.483 17.729  1.00 30.85 ? 70   LYS A CE  1 
ATOM   525  N NZ  . LYS A 1 70  ? 25.560  -10.056 19.034  1.00 32.10 ? 70   LYS A NZ  1 
ATOM   526  N N   . THR A 1 71  ? 23.726  -7.627  11.532  1.00 27.06 ? 71   THR A N   1 
ATOM   527  C CA  . THR A 1 71  ? 23.662  -6.510  10.584  1.00 27.37 ? 71   THR A CA  1 
ATOM   528  C C   . THR A 1 71  ? 22.665  -5.449  11.087  1.00 27.56 ? 71   THR A C   1 
ATOM   529  O O   . THR A 1 71  ? 21.861  -5.696  11.990  1.00 27.26 ? 71   THR A O   1 
ATOM   530  C CB  . THR A 1 71  ? 23.277  -6.981  9.122   1.00 27.92 ? 71   THR A CB  1 
ATOM   531  O OG1 . THR A 1 71  ? 22.033  -7.698  9.134   1.00 28.74 ? 71   THR A OG1 1 
ATOM   532  C CG2 . THR A 1 71  ? 24.361  -7.874  8.502   1.00 28.09 ? 71   THR A CG2 1 
ATOM   533  N N   . THR A 1 72  ? 22.781  -4.252  10.526  1.00 28.27 ? 72   THR A N   1 
ATOM   534  C CA  . THR A 1 72  ? 21.800  -3.197  10.703  1.00 29.73 ? 72   THR A CA  1 
ATOM   535  C C   . THR A 1 72  ? 20.989  -3.024  9.425   1.00 30.25 ? 72   THR A C   1 
ATOM   536  O O   . THR A 1 72  ? 21.533  -2.988  8.325   1.00 31.11 ? 72   THR A O   1 
ATOM   537  C CB  . THR A 1 72  ? 22.448  -1.838  11.030  1.00 29.80 ? 72   THR A CB  1 
ATOM   538  O OG1 . THR A 1 72  ? 23.428  -1.999  12.055  1.00 31.07 ? 72   THR A OG1 1 
ATOM   539  C CG2 . THR A 1 72  ? 21.385  -0.843  11.519  1.00 32.49 ? 72   THR A CG2 1 
ATOM   540  N N   . LYS A 1 73  ? 19.678  -2.938  9.582   1.00 30.83 ? 73   LYS A N   1 
ATOM   541  C CA  . LYS A 1 73  ? 18.795  -2.560  8.481   1.00 30.95 ? 73   LYS A CA  1 
ATOM   542  C C   . LYS A 1 73  ? 18.099  -1.261  8.839   1.00 30.25 ? 73   LYS A C   1 
ATOM   543  O O   . LYS A 1 73  ? 17.721  -1.038  9.987   1.00 28.96 ? 73   LYS A O   1 
ATOM   544  C CB  . LYS A 1 73  ? 17.773  -3.660  8.192   1.00 31.70 ? 73   LYS A CB  1 
ATOM   545  C CG  . LYS A 1 73  ? 18.390  -5.029  7.958   1.00 34.36 ? 73   LYS A CG  1 
ATOM   546  C CD  . LYS A 1 73  ? 17.320  -6.062  7.727   1.00 37.74 ? 73   LYS A CD  1 
ATOM   547  C CE  . LYS A 1 73  ? 17.906  -7.357  7.185   1.00 39.55 ? 73   LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 73  ? 16.818  -8.331  6.862   1.00 39.93 ? 73   LYS A NZ  1 
ATOM   549  N N   . THR A 1 74  ? 17.981  -0.402  7.836   1.00 30.15 ? 74   THR A N   1 
ATOM   550  C CA  . THR A 1 74  ? 17.261  0.864   7.936   1.00 29.97 ? 74   THR A CA  1 
ATOM   551  C C   . THR A 1 74  ? 15.861  0.670   7.435   1.00 29.51 ? 74   THR A C   1 
ATOM   552  O O   . THR A 1 74  ? 15.638  0.437   6.256   1.00 29.09 ? 74   THR A O   1 
ATOM   553  C CB  . THR A 1 74  ? 17.900  1.974   7.089   1.00 29.65 ? 74   THR A CB  1 
ATOM   554  O OG1 . THR A 1 74  ? 19.098  2.415   7.729   1.00 31.99 ? 74   THR A OG1 1 
ATOM   555  C CG2 . THR A 1 74  ? 16.963  3.151   6.945   1.00 30.02 ? 74   THR A CG2 1 
ATOM   556  N N   . ILE A 1 75  ? 14.923  0.784   8.359   1.00 29.99 ? 75   ILE A N   1 
ATOM   557  C CA  . ILE A 1 75  ? 13.518  0.496   8.087   1.00 29.67 ? 75   ILE A CA  1 
ATOM   558  C C   . ILE A 1 75  ? 12.838  1.751   7.594   1.00 29.99 ? 75   ILE A C   1 
ATOM   559  O O   . ILE A 1 75  ? 12.785  2.760   8.293   1.00 30.11 ? 75   ILE A O   1 
ATOM   560  C CB  . ILE A 1 75  ? 12.793  -0.030  9.340   1.00 29.36 ? 75   ILE A CB  1 
ATOM   561  C CG1 . ILE A 1 75  ? 13.397  -1.363  9.795   1.00 29.64 ? 75   ILE A CG1 1 
ATOM   562  C CG2 . ILE A 1 75  ? 11.270  -0.142  9.101   1.00 31.22 ? 75   ILE A CG2 1 
ATOM   563  C CD1 . ILE A 1 75  ? 13.413  -2.464  8.754   1.00 31.09 ? 75   ILE A CD1 1 
ATOM   564  N N   . ASN A 1 76  ? 12.368  1.696   6.353   1.00 31.01 ? 76   ASN A N   1 
ATOM   565  C CA  . ASN A 1 76  ? 11.365  2.647   5.866   1.00 31.79 ? 76   ASN A CA  1 
ATOM   566  C C   . ASN A 1 76  ? 10.034  1.899   5.813   1.00 31.37 ? 76   ASN A C   1 
ATOM   567  O O   . ASN A 1 76  ? 9.838   0.983   4.999   1.00 30.13 ? 76   ASN A O   1 
ATOM   568  C CB  . ASN A 1 76  ? 11.740  3.215   4.502   1.00 32.78 ? 76   ASN A CB  1 
ATOM   569  C CG  . ASN A 1 76  ? 10.740  4.251   4.010   1.00 34.22 ? 76   ASN A CG  1 
ATOM   570  O OD1 . ASN A 1 76  ? 9.549   3.971   3.852   1.00 39.35 ? 76   ASN A OD1 1 
ATOM   571  N ND2 . ASN A 1 76  ? 11.217  5.445   3.783   1.00 35.68 ? 76   ASN A ND2 1 
ATOM   572  N N   . GLU A 1 77  ? 9.137   2.285   6.711   1.00 31.26 ? 77   GLU A N   1 
ATOM   573  C CA  . GLU A 1 77  ? 7.957   1.477   6.992   1.00 31.47 ? 77   GLU A CA  1 
ATOM   574  C C   . GLU A 1 77  ? 7.032   1.370   5.781   1.00 30.41 ? 77   GLU A C   1 
ATOM   575  O O   . GLU A 1 77  ? 6.477   0.303   5.498   1.00 29.58 ? 77   GLU A O   1 
ATOM   576  C CB  . GLU A 1 77  ? 7.200   2.019   8.215   1.00 32.37 ? 77   GLU A CB  1 
ATOM   577  C CG  . GLU A 1 77  ? 7.987   1.907   9.539   1.00 34.40 ? 77   GLU A CG  1 
ATOM   578  C CD  . GLU A 1 77  ? 7.125   2.068   10.778  1.00 36.88 ? 77   GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 77  ? 6.078   2.785   10.704  1.00 39.95 ? 77   GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 77  ? 7.501   1.475   11.828  1.00 37.37 ? 77   GLU A OE2 1 
ATOM   581  N N   . GLY A 1 78  ? 6.894   2.479   5.072   1.00 30.01 ? 78   GLY A N   1 
ATOM   582  C CA  . GLY A 1 78  ? 6.017   2.549   3.921   1.00 30.36 ? 78   GLY A CA  1 
ATOM   583  C C   . GLY A 1 78  ? 6.486   1.549   2.890   1.00 30.79 ? 78   GLY A C   1 
ATOM   584  O O   . GLY A 1 78  ? 5.668   0.865   2.259   1.00 31.82 ? 78   GLY A O   1 
ATOM   585  N N   . GLN A 1 79  ? 7.808   1.445   2.748   1.00 29.67 ? 79   GLN A N   1 
ATOM   586  C CA  . GLN A 1 79  ? 8.395   0.565   1.736   1.00 29.20 ? 79   GLN A CA  1 
ATOM   587  C C   . GLN A 1 79  ? 8.067   -0.878  2.030   1.00 28.50 ? 79   GLN A C   1 
ATOM   588  O O   . GLN A 1 79  ? 7.946   -1.676  1.118   1.00 26.80 ? 79   GLN A O   1 
ATOM   589  C CB  . GLN A 1 79  ? 9.916   0.719   1.638   1.00 29.84 ? 79   GLN A CB  1 
ATOM   590  C CG  . GLN A 1 79  ? 10.368  1.961   0.896   1.00 31.14 ? 79   GLN A CG  1 
ATOM   591  C CD  . GLN A 1 79  ? 9.699   2.118   -0.468  1.00 33.25 ? 79   GLN A CD  1 
ATOM   592  O OE1 . GLN A 1 79  ? 9.490   3.236   -0.932  1.00 35.87 ? 79   GLN A OE1 1 
ATOM   593  N NE2 . GLN A 1 79  ? 9.356   0.997   -1.109  1.00 34.68 ? 79   GLN A NE2 1 
ATOM   594  N N   . THR A 1 80  ? 7.917   -1.210  3.308   1.00 29.15 ? 80   THR A N   1 
ATOM   595  C CA  . THR A 1 80  ? 7.679   -2.610  3.711   1.00 29.55 ? 80   THR A CA  1 
ATOM   596  C C   . THR A 1 80  ? 6.229   -3.001  3.354   1.00 31.30 ? 80   THR A C   1 
ATOM   597  O O   . THR A 1 80  ? 5.892   -4.175  3.177   1.00 31.78 ? 80   THR A O   1 
ATOM   598  C CB  . THR A 1 80  ? 7.939   -2.846  5.218   1.00 30.00 ? 80   THR A CB  1 
ATOM   599  O OG1 . THR A 1 80  ? 6.936   -2.157  5.995   1.00 27.98 ? 80   THR A OG1 1 
ATOM   600  C CG2 . THR A 1 80  ? 9.417   -2.400  5.620   1.00 26.37 ? 80   THR A CG2 1 
ATOM   601  N N   . ILE A 1 81  ? 5.383   -1.991  3.228   1.00 32.39 ? 81   ILE A N   1 
ATOM   602  C CA  . ILE A 1 81  ? 4.012   -2.212  2.791   1.00 34.15 ? 81   ILE A CA  1 
ATOM   603  C C   . ILE A 1 81  ? 3.961   -2.334  1.260   1.00 34.03 ? 81   ILE A C   1 
ATOM   604  O O   . ILE A 1 81  ? 3.257   -3.166  0.721   1.00 35.20 ? 81   ILE A O   1 
ATOM   605  C CB  . ILE A 1 81  ? 3.070   -1.095  3.266   1.00 35.01 ? 81   ILE A CB  1 
ATOM   606  C CG1 . ILE A 1 81  ? 2.711   -1.341  4.736   1.00 35.44 ? 81   ILE A CG1 1 
ATOM   607  C CG2 . ILE A 1 81  ? 1.823   -1.043  2.372   1.00 35.45 ? 81   ILE A CG2 1 
ATOM   608  C CD1 . ILE A 1 81  ? 1.758   -0.350  5.278   1.00 36.91 ? 81   ILE A CD1 1 
ATOM   609  N N   . LEU A 1 82  ? 4.744   -1.534  0.560   1.00 34.28 ? 82   LEU A N   1 
ATOM   610  C CA  . LEU A 1 82  ? 4.737   -1.604  -0.903  1.00 34.68 ? 82   LEU A CA  1 
ATOM   611  C C   . LEU A 1 82  ? 5.334   -2.904  -1.440  1.00 34.54 ? 82   LEU A C   1 
ATOM   612  O O   . LEU A 1 82  ? 4.937   -3.361  -2.513  1.00 36.25 ? 82   LEU A O   1 
ATOM   613  C CB  . LEU A 1 82  ? 5.451   -0.411  -1.536  1.00 34.16 ? 82   LEU A CB  1 
ATOM   614  C CG  . LEU A 1 82  ? 4.808   0.943   -1.303  1.00 32.98 ? 82   LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 82  ? 5.518   1.948   -2.161  1.00 31.75 ? 82   LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 82  ? 3.323   0.917   -1.603  1.00 33.52 ? 82   LEU A CD2 1 
ATOM   617  N N   . VAL A 1 83  ? 6.259   -3.503  -0.699  1.00 33.74 ? 83   VAL A N   1 
ATOM   618  C CA  . VAL A 1 83  ? 6.994   -4.661  -1.213  1.00 33.16 ? 83   VAL A CA  1 
ATOM   619  C C   . VAL A 1 83  ? 6.075   -5.871  -1.290  1.00 32.63 ? 83   VAL A C   1 
ATOM   620  O O   . VAL A 1 83  ? 6.188   -6.729  -2.174  1.00 31.61 ? 83   VAL A O   1 
ATOM   621  C CB  . VAL A 1 83  ? 8.288   -4.991  -0.384  1.00 33.84 ? 83   VAL A CB  1 
ATOM   622  C CG1 . VAL A 1 83  ? 7.940   -5.471  1.031   1.00 31.70 ? 83   VAL A CG1 1 
ATOM   623  C CG2 . VAL A 1 83  ? 9.142   -6.033  -1.139  1.00 30.74 ? 83   VAL A CG2 1 
ATOM   624  N N   . VAL A 1 84  ? 5.135   -5.918  -0.362  1.00 33.13 ? 84   VAL A N   1 
ATOM   625  C CA  . VAL A 1 84  ? 4.209   -7.043  -0.272  1.00 33.03 ? 84   VAL A CA  1 
ATOM   626  C C   . VAL A 1 84  ? 3.271   -7.062  -1.500  1.00 32.63 ? 84   VAL A C   1 
ATOM   627  O O   . VAL A 1 84  ? 3.011   -8.110  -2.081  1.00 32.49 ? 84   VAL A O   1 
ATOM   628  C CB  . VAL A 1 84  ? 3.431   -7.035  1.075   1.00 34.41 ? 84   VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 84  ? 2.164   -7.893  0.971   1.00 34.83 ? 84   VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 84  ? 4.372   -7.485  2.235   1.00 31.24 ? 84   VAL A CG2 1 
ATOM   631  N N   . PHE A 1 85  ? 2.809   -5.897  -1.923  1.00 32.49 ? 85   PHE A N   1 
ATOM   632  C CA  . PHE A 1 85  ? 1.935   -5.821  -3.099  1.00 33.48 ? 85   PHE A CA  1 
ATOM   633  C C   . PHE A 1 85  ? 2.746   -5.904  -4.389  1.00 33.20 ? 85   PHE A C   1 
ATOM   634  O O   . PHE A 1 85  ? 2.337   -6.569  -5.330  1.00 32.93 ? 85   PHE A O   1 
ATOM   635  C CB  . PHE A 1 85  ? 1.131   -4.522  -3.120  1.00 33.35 ? 85   PHE A CB  1 
ATOM   636  C CG  . PHE A 1 85  ? 0.041   -4.452  -2.081  1.00 35.83 ? 85   PHE A CG  1 
ATOM   637  C CD1 . PHE A 1 85  ? -1.209  -5.001  -2.328  1.00 36.23 ? 85   PHE A CD1 1 
ATOM   638  C CD2 . PHE A 1 85  ? 0.252   -3.793  -0.879  1.00 34.73 ? 85   PHE A CD2 1 
ATOM   639  C CE1 . PHE A 1 85  ? -2.229  -4.911  -1.385  1.00 37.71 ? 85   PHE A CE1 1 
ATOM   640  C CE2 . PHE A 1 85  ? -0.767  -3.708  0.064   1.00 38.06 ? 85   PHE A CE2 1 
ATOM   641  C CZ  . PHE A 1 85  ? -2.017  -4.262  -0.205  1.00 37.50 ? 85   PHE A CZ  1 
ATOM   642  N N   . ASN A 1 86  ? 3.895   -5.229  -4.407  1.00 32.96 ? 86   ASN A N   1 
ATOM   643  C CA  . ASN A 1 86  ? 4.768   -5.195  -5.595  1.00 33.56 ? 86   ASN A CA  1 
ATOM   644  C C   . ASN A 1 86  ? 5.451   -6.543  -5.872  1.00 33.28 ? 86   ASN A C   1 
ATOM   645  O O   . ASN A 1 86  ? 5.560   -6.939  -7.018  1.00 33.66 ? 86   ASN A O   1 
ATOM   646  C CB  . ASN A 1 86  ? 5.831   -4.080  -5.501  1.00 32.76 ? 86   ASN A CB  1 
ATOM   647  C CG  . ASN A 1 86  ? 5.232   -2.683  -5.569  1.00 34.41 ? 86   ASN A CG  1 
ATOM   648  O OD1 . ASN A 1 86  ? 4.073   -2.499  -5.949  1.00 35.84 ? 86   ASN A OD1 1 
ATOM   649  N ND2 . ASN A 1 86  ? 6.024   -1.687  -5.198  1.00 34.90 ? 86   ASN A ND2 1 
ATOM   650  N N   . GLU A 1 87  ? 5.880   -7.243  -4.824  1.00 33.60 ? 87   GLU A N   1 
ATOM   651  C CA  . GLU A 1 87  ? 6.713   -8.462  -4.971  1.00 34.18 ? 87   GLU A CA  1 
ATOM   652  C C   . GLU A 1 87  ? 6.047   -9.724  -4.443  1.00 33.41 ? 87   GLU A C   1 
ATOM   653  O O   . GLU A 1 87  ? 6.307   -10.810 -4.929  1.00 33.24 ? 87   GLU A O   1 
ATOM   654  C CB  . GLU A 1 87  ? 8.042   -8.294  -4.228  1.00 35.23 ? 87   GLU A CB  1 
ATOM   655  C CG  . GLU A 1 87  ? 8.734   -6.967  -4.465  1.00 37.54 ? 87   GLU A CG  1 
ATOM   656  C CD  . GLU A 1 87  ? 9.186   -6.824  -5.896  1.00 41.33 ? 87   GLU A CD  1 
ATOM   657  O OE1 . GLU A 1 87  ? 9.297   -7.869  -6.574  1.00 45.89 ? 87   GLU A OE1 1 
ATOM   658  O OE2 . GLU A 1 87  ? 9.428   -5.682  -6.350  1.00 44.24 ? 87   GLU A OE2 1 
ATOM   659  N N   . GLY A 1 88  ? 5.216   -9.584  -3.414  1.00 33.13 ? 88   GLY A N   1 
ATOM   660  C CA  . GLY A 1 88  ? 4.484   -10.730 -2.873  1.00 32.57 ? 88   GLY A CA  1 
ATOM   661  C C   . GLY A 1 88  ? 5.239   -11.437 -1.762  1.00 32.08 ? 88   GLY A C   1 
ATOM   662  O O   . GLY A 1 88  ? 4.900   -12.538 -1.375  1.00 32.60 ? 88   GLY A O   1 
ATOM   663  N N   . TYR A 1 89  ? 6.292   -10.792 -1.284  1.00 32.25 ? 89   TYR A N   1 
ATOM   664  C CA  . TYR A 1 89  ? 7.025   -11.234 -0.101  1.00 31.58 ? 89   TYR A CA  1 
ATOM   665  C C   . TYR A 1 89  ? 7.554   -10.034 0.693   1.00 31.41 ? 89   TYR A C   1 
ATOM   666  O O   . TYR A 1 89  ? 7.471   -8.891  0.253   1.00 32.33 ? 89   TYR A O   1 
ATOM   667  C CB  . TYR A 1 89  ? 8.173   -12.173 -0.486  1.00 32.45 ? 89   TYR A CB  1 
ATOM   668  C CG  . TYR A 1 89  ? 9.134   -11.609 -1.513  1.00 33.03 ? 89   TYR A CG  1 
ATOM   669  C CD1 . TYR A 1 89  ? 10.172  -10.768 -1.129  1.00 32.76 ? 89   TYR A CD1 1 
ATOM   670  C CD2 . TYR A 1 89  ? 9.001   -11.927 -2.870  1.00 33.45 ? 89   TYR A CD2 1 
ATOM   671  C CE1 . TYR A 1 89  ? 11.047  -10.244 -2.061  1.00 33.78 ? 89   TYR A CE1 1 
ATOM   672  C CE2 . TYR A 1 89  ? 9.875   -11.417 -3.803  1.00 32.53 ? 89   TYR A CE2 1 
ATOM   673  C CZ  . TYR A 1 89  ? 10.893  -10.571 -3.389  1.00 33.47 ? 89   TYR A CZ  1 
ATOM   674  O OH  . TYR A 1 89  ? 11.759  -10.045 -4.305  1.00 35.18 ? 89   TYR A OH  1 
ATOM   675  N N   . ALA A 1 90  ? 8.078   -10.295 1.877   1.00 31.22 ? 90   ALA A N   1 
ATOM   676  C CA  . ALA A 1 90  ? 8.535   -9.215  2.762   1.00 31.97 ? 90   ALA A CA  1 
ATOM   677  C C   . ALA A 1 90  ? 9.974   -9.491  3.225   1.00 32.07 ? 90   ALA A C   1 
ATOM   678  O O   . ALA A 1 90  ? 10.178  -10.261 4.148   1.00 31.73 ? 90   ALA A O   1 
ATOM   679  C CB  . ALA A 1 90  ? 7.584   -9.081  3.964   1.00 30.57 ? 90   ALA A CB  1 
ATOM   680  N N   . PRO A 1 91  ? 10.981  -8.898  2.561   1.00 33.37 ? 91   PRO A N   1 
ATOM   681  C CA  . PRO A 1 91  ? 12.306  -9.359  2.985   1.00 34.88 ? 91   PRO A CA  1 
ATOM   682  C C   . PRO A 1 91  ? 12.654  -9.027  4.451   1.00 35.56 ? 91   PRO A C   1 
ATOM   683  O O   . PRO A 1 91  ? 13.466  -9.723  5.037   1.00 34.72 ? 91   PRO A O   1 
ATOM   684  C CB  . PRO A 1 91  ? 13.273  -8.655  2.008   1.00 34.75 ? 91   PRO A CB  1 
ATOM   685  C CG  . PRO A 1 91  ? 12.415  -8.080  0.914   1.00 34.65 ? 91   PRO A CG  1 
ATOM   686  C CD  . PRO A 1 91  ? 11.067  -7.827  1.552   1.00 33.50 ? 91   PRO A CD  1 
ATOM   687  N N   . ASP A 1 92  ? 12.010  -8.003  5.023   1.00 37.03 ? 92   ASP A N   1 
ATOM   688  C CA  . ASP A 1 92  ? 12.327  -7.513  6.389   1.00 38.51 ? 92   ASP A CA  1 
ATOM   689  C C   . ASP A 1 92  ? 11.168  -7.612  7.377   1.00 37.69 ? 92   ASP A C   1 
ATOM   690  O O   . ASP A 1 92  ? 11.268  -7.073  8.483   1.00 38.17 ? 92   ASP A O   1 
ATOM   691  C CB  . ASP A 1 92  ? 12.702  -6.018  6.401   1.00 39.68 ? 92   ASP A CB  1 
ATOM   692  C CG  . ASP A 1 92  ? 13.780  -5.650  5.415   1.00 42.02 ? 92   ASP A CG  1 
ATOM   693  O OD1 . ASP A 1 92  ? 14.942  -6.073  5.588   1.00 46.00 ? 92   ASP A OD1 1 
ATOM   694  O OD2 . ASP A 1 92  ? 13.462  -4.875  4.483   1.00 48.22 ? 92   ASP A OD2 1 
ATOM   695  N N   . GLY A 1 93  ? 10.077  -8.264  6.986   1.00 36.60 ? 93   GLY A N   1 
ATOM   696  C CA  . GLY A 1 93  ? 8.810   -8.141  7.719   1.00 35.36 ? 93   GLY A CA  1 
ATOM   697  C C   . GLY A 1 93  ? 8.047   -6.906  7.263   1.00 34.17 ? 93   GLY A C   1 
ATOM   698  O O   . GLY A 1 93  ? 8.553   -6.120  6.497   1.00 33.02 ? 93   GLY A O   1 
ATOM   699  N N   . VAL A 1 94  ? 6.814   -6.757  7.729   1.00 34.05 ? 94   VAL A N   1 
ATOM   700  C CA  . VAL A 1 94  ? 6.073   -5.511  7.615   1.00 32.52 ? 94   VAL A CA  1 
ATOM   701  C C   . VAL A 1 94  ? 6.149   -4.733  8.917   1.00 32.82 ? 94   VAL A C   1 
ATOM   702  O O   . VAL A 1 94  ? 5.906   -5.261  9.997   1.00 35.24 ? 94   VAL A O   1 
ATOM   703  C CB  . VAL A 1 94  ? 4.595   -5.776  7.241   1.00 33.54 ? 94   VAL A CB  1 
ATOM   704  C CG1 . VAL A 1 94  ? 3.804   -4.460  7.133   1.00 28.19 ? 94   VAL A CG1 1 
ATOM   705  C CG2 . VAL A 1 94  ? 4.539   -6.563  5.935   1.00 33.00 ? 94   VAL A CG2 1 
ATOM   706  N N   . TRP A 1 95  ? 6.539   -3.474  8.817   1.00 32.35 ? 95   TRP A N   1 
ATOM   707  C CA  . TRP A 1 95  ? 6.746   -2.665  9.987   1.00 32.13 ? 95   TRP A CA  1 
ATOM   708  C C   . TRP A 1 95  ? 5.780   -1.534  9.898   1.00 32.69 ? 95   TRP A C   1 
ATOM   709  O O   . TRP A 1 95  ? 5.655   -0.887  8.855   1.00 33.10 ? 95   TRP A O   1 
ATOM   710  C CB  . TRP A 1 95  ? 8.180   -2.123  10.061  1.00 31.98 ? 95   TRP A CB  1 
ATOM   711  C CG  . TRP A 1 95  ? 9.226   -3.141  10.387  1.00 33.03 ? 95   TRP A CG  1 
ATOM   712  C CD1 . TRP A 1 95  ? 9.769   -4.058  9.536   1.00 32.89 ? 95   TRP A CD1 1 
ATOM   713  C CD2 . TRP A 1 95  ? 9.877   -3.337  11.658  1.00 34.25 ? 95   TRP A CD2 1 
ATOM   714  N NE1 . TRP A 1 95  ? 10.715  -4.812  10.200  1.00 35.19 ? 95   TRP A NE1 1 
ATOM   715  C CE2 . TRP A 1 95  ? 10.794  -4.391  11.501  1.00 33.02 ? 95   TRP A CE2 1 
ATOM   716  C CE3 . TRP A 1 95  ? 9.756   -2.731  12.914  1.00 35.95 ? 95   TRP A CE3 1 
ATOM   717  C CZ2 . TRP A 1 95  ? 11.578  -4.859  12.546  1.00 34.84 ? 95   TRP A CZ2 1 
ATOM   718  C CZ3 . TRP A 1 95  ? 10.555  -3.188  13.958  1.00 35.30 ? 95   TRP A CZ3 1 
ATOM   719  C CH2 . TRP A 1 95  ? 11.449  -4.244  13.767  1.00 35.34 ? 95   TRP A CH2 1 
ATOM   720  N N   . LEU A 1 96  ? 5.076   -1.311  10.996  1.00 32.53 ? 96   LEU A N   1 
ATOM   721  C CA  . LEU A 1 96  ? 4.144   -0.197  11.081  1.00 33.05 ? 96   LEU A CA  1 
ATOM   722  C C   . LEU A 1 96  ? 4.108   0.381   12.491  1.00 32.90 ? 96   LEU A C   1 
ATOM   723  O O   . LEU A 1 96  ? 3.891   -0.323  13.473  1.00 32.69 ? 96   LEU A O   1 
ATOM   724  C CB  . LEU A 1 96  ? 2.744   -0.648  10.660  1.00 32.68 ? 96   LEU A CB  1 
ATOM   725  C CG  . LEU A 1 96  ? 1.722   0.484   10.592  1.00 31.79 ? 96   LEU A CG  1 
ATOM   726  C CD1 . LEU A 1 96  ? 2.056   1.360   9.415   1.00 31.98 ? 96   LEU A CD1 1 
ATOM   727  C CD2 . LEU A 1 96  ? 0.256   -0.031  10.533  1.00 28.17 ? 96   LEU A CD2 1 
ATOM   728  N N   . GLY A 1 97  ? 4.335   1.679   12.569  1.00 33.27 ? 97   GLY A N   1 
ATOM   729  C CA  . GLY A 1 97  ? 4.347   2.364   13.831  1.00 33.66 ? 97   GLY A CA  1 
ATOM   730  C C   . GLY A 1 97  ? 5.442   1.890   14.770  1.00 34.03 ? 97   GLY A C   1 
ATOM   731  O O   . GLY A 1 97  ? 5.352   2.124   15.959  1.00 34.70 ? 97   GLY A O   1 
ATOM   732  N N   . GLY A 1 98  ? 6.467   1.215   14.247  1.00 34.08 ? 98   GLY A N   1 
ATOM   733  C CA  . GLY A 1 98  ? 7.620   0.806   15.071  1.00 32.78 ? 98   GLY A CA  1 
ATOM   734  C C   . GLY A 1 98  ? 7.474   -0.649  15.470  1.00 32.36 ? 98   GLY A C   1 
ATOM   735  O O   . GLY A 1 98  ? 8.350   -1.236  16.069  1.00 32.20 ? 98   GLY A O   1 
ATOM   736  N N   . THR A 1 99  ? 6.334   -1.222  15.113  1.00 32.20 ? 99   THR A N   1 
ATOM   737  C CA  . THR A 1 99  ? 6.011   -2.611  15.431  1.00 31.55 ? 99   THR A CA  1 
ATOM   738  C C   . THR A 1 99  ? 6.262   -3.481  14.220  1.00 31.97 ? 99   THR A C   1 
ATOM   739  O O   . THR A 1 99  ? 5.920   -3.135  13.089  1.00 30.61 ? 99   THR A O   1 
ATOM   740  C CB  . THR A 1 99  ? 4.495   -2.800  15.828  1.00 32.19 ? 99   THR A CB  1 
ATOM   741  O OG1 . THR A 1 99  ? 4.175   -1.999  16.967  1.00 33.74 ? 99   THR A OG1 1 
ATOM   742  C CG2 . THR A 1 99  ? 4.159   -4.262  16.128  1.00 28.21 ? 99   THR A CG2 1 
ATOM   743  N N   . LYS A 1 100 ? 6.827   -4.643  14.494  1.00 32.63 ? 100  LYS A N   1 
ATOM   744  C CA  . LYS A 1 100 ? 7.033   -5.644  13.484  1.00 33.93 ? 100  LYS A CA  1 
ATOM   745  C C   . LYS A 1 100 ? 5.842   -6.577  13.372  1.00 32.84 ? 100  LYS A C   1 
ATOM   746  O O   . LYS A 1 100 ? 5.442   -7.219  14.340  1.00 32.98 ? 100  LYS A O   1 
ATOM   747  C CB  . LYS A 1 100 ? 8.263   -6.479  13.785  1.00 34.11 ? 100  LYS A CB  1 
ATOM   748  C CG  . LYS A 1 100 ? 8.730   -7.259  12.579  1.00 36.27 ? 100  LYS A CG  1 
ATOM   749  C CD  . LYS A 1 100 ? 9.804   -8.257  12.969  1.00 39.19 ? 100  LYS A CD  1 
ATOM   750  C CE  . LYS A 1 100 ? 10.269  -9.038  11.743  1.00 42.33 ? 100  LYS A CE  1 
ATOM   751  N NZ  . LYS A 1 100 ? 11.269  -10.104 12.084  1.00 43.01 ? 100  LYS A NZ  1 
ATOM   752  N N   . TYR A 1 101 ? 5.302   -6.672  12.169  1.00 30.95 ? 101  TYR A N   1 
ATOM   753  C CA  . TYR A 1 101 ? 4.350   -7.730  11.876  1.00 30.67 ? 101  TYR A CA  1 
ATOM   754  C C   . TYR A 1 101 ? 4.952   -8.742  10.929  1.00 30.81 ? 101  TYR A C   1 
ATOM   755  O O   . TYR A 1 101 ? 5.764   -8.405  10.055  1.00 32.22 ? 101  TYR A O   1 
ATOM   756  C CB  . TYR A 1 101 ? 3.093   -7.183  11.227  1.00 29.59 ? 101  TYR A CB  1 
ATOM   757  C CG  . TYR A 1 101 ? 2.377   -6.112  12.003  1.00 27.25 ? 101  TYR A CG  1 
ATOM   758  C CD1 . TYR A 1 101 ? 1.107   -6.342  12.518  1.00 27.43 ? 101  TYR A CD1 1 
ATOM   759  C CD2 . TYR A 1 101 ? 2.939   -4.872  12.186  1.00 25.06 ? 101  TYR A CD2 1 
ATOM   760  C CE1 . TYR A 1 101 ? 0.416   -5.362  13.200  1.00 26.31 ? 101  TYR A CE1 1 
ATOM   761  C CE2 . TYR A 1 101 ? 2.274   -3.886  12.871  1.00 25.68 ? 101  TYR A CE2 1 
ATOM   762  C CZ  . TYR A 1 101 ? 0.998   -4.143  13.372  1.00 26.28 ? 101  TYR A CZ  1 
ATOM   763  O OH  . TYR A 1 101 ? 0.313   -3.179  14.037  1.00 24.71 ? 101  TYR A OH  1 
ATOM   764  N N   . GLN A 1 102 ? 4.503   -9.970  11.111  1.00 29.76 ? 102  GLN A N   1 
ATOM   765  C CA  . GLN A 1 102 ? 4.772   -11.070 10.221  1.00 30.30 ? 102  GLN A CA  1 
ATOM   766  C C   . GLN A 1 102 ? 3.744   -11.169 9.071   1.00 29.98 ? 102  GLN A C   1 
ATOM   767  O O   . GLN A 1 102 ? 2.527   -11.277 9.272   1.00 29.26 ? 102  GLN A O   1 
ATOM   768  C CB  . GLN A 1 102 ? 4.808   -12.388 11.008  1.00 29.81 ? 102  GLN A CB  1 
ATOM   769  C CG  . GLN A 1 102 ? 5.272   -13.550 10.168  1.00 33.73 ? 102  GLN A CG  1 
ATOM   770  C CD  . GLN A 1 102 ? 4.806   -14.903 10.671  1.00 36.96 ? 102  GLN A CD  1 
ATOM   771  O OE1 . GLN A 1 102 ? 4.314   -15.035 11.785  1.00 41.16 ? 102  GLN A OE1 1 
ATOM   772  N NE2 . GLN A 1 102 ? 4.962   -15.923 9.834   1.00 42.84 ? 102  GLN A NE2 1 
ATOM   773  N N   . PHE A 1 103 ? 4.277   -11.168 7.858   1.00 30.51 ? 103  PHE A N   1 
ATOM   774  C CA  . PHE A 1 103 ? 3.494   -11.368 6.617   1.00 30.67 ? 103  PHE A CA  1 
ATOM   775  C C   . PHE A 1 103 ? 2.949   -12.783 6.554   1.00 29.52 ? 103  PHE A C   1 
ATOM   776  O O   . PHE A 1 103 ? 3.690   -13.751 6.496   1.00 29.03 ? 103  PHE A O   1 
ATOM   777  C CB  . PHE A 1 103 ? 4.362   -11.026 5.386   1.00 31.59 ? 103  PHE A CB  1 
ATOM   778  C CG  . PHE A 1 103 ? 3.689   -11.277 4.035   1.00 32.90 ? 103  PHE A CG  1 
ATOM   779  C CD1 . PHE A 1 103 ? 2.426   -10.770 3.753   1.00 32.24 ? 103  PHE A CD1 1 
ATOM   780  C CD2 . PHE A 1 103 ? 4.366   -11.982 3.032   1.00 32.70 ? 103  PHE A CD2 1 
ATOM   781  C CE1 . PHE A 1 103 ? 1.833   -10.984 2.491   1.00 35.73 ? 103  PHE A CE1 1 
ATOM   782  C CE2 . PHE A 1 103 ? 3.791   -12.197 1.789   1.00 32.86 ? 103  PHE A CE2 1 
ATOM   783  C CZ  . PHE A 1 103 ? 2.509   -11.702 1.515   1.00 32.73 ? 103  PHE A CZ  1 
ATOM   784  N N   . ILE A 1 104 ? 1.628   -12.899 6.581   1.00 29.61 ? 104  ILE A N   1 
ATOM   785  C CA  . ILE A 1 104 ? 0.981   -14.207 6.617   1.00 29.64 ? 104  ILE A CA  1 
ATOM   786  C C   . ILE A 1 104 ? 0.416   -14.609 5.254   1.00 29.96 ? 104  ILE A C   1 
ATOM   787  O O   . ILE A 1 104 ? 0.479   -15.774 4.846   1.00 29.42 ? 104  ILE A O   1 
ATOM   788  C CB  . ILE A 1 104 ? -0.155  -14.206 7.653   1.00 30.78 ? 104  ILE A CB  1 
ATOM   789  C CG1 . ILE A 1 104 ? 0.426   -13.977 9.059   1.00 32.01 ? 104  ILE A CG1 1 
ATOM   790  C CG2 . ILE A 1 104 ? -0.975  -15.514 7.562   1.00 30.66 ? 104  ILE A CG2 1 
ATOM   791  C CD1 . ILE A 1 104 ? 1.391   -15.079 9.528   1.00 28.02 ? 104  ILE A CD1 1 
ATOM   792  N N   . ASN A 1 105 ? -0.142  -13.641 4.546   1.00 31.18 ? 105  ASN A N   1 
ATOM   793  C CA  . ASN A 1 105 ? -0.905  -13.959 3.338   1.00 32.07 ? 105  ASN A CA  1 
ATOM   794  C C   . ASN A 1 105 ? -1.238  -12.769 2.441   1.00 31.56 ? 105  ASN A C   1 
ATOM   795  O O   . ASN A 1 105 ? -1.477  -11.651 2.892   1.00 29.44 ? 105  ASN A O   1 
ATOM   796  C CB  . ASN A 1 105 ? -2.200  -14.672 3.727   1.00 33.47 ? 105  ASN A CB  1 
ATOM   797  C CG  . ASN A 1 105 ? -2.723  -15.556 2.617   1.00 37.22 ? 105  ASN A CG  1 
ATOM   798  O OD1 . ASN A 1 105 ? -1.996  -15.848 1.655   1.00 43.65 ? 105  ASN A OD1 1 
ATOM   799  N ND2 . ASN A 1 105 ? -3.994  -15.952 2.709   1.00 39.09 ? 105  ASN A ND2 1 
ATOM   800  N N   . ILE A 1 106 ? -1.248  -13.034 1.145   1.00 32.18 ? 106  ILE A N   1 
ATOM   801  C CA  . ILE A 1 106 ? -1.794  -12.074 0.220   1.00 32.91 ? 106  ILE A CA  1 
ATOM   802  C C   . ILE A 1 106 ? -2.789  -12.747 -0.698  1.00 32.69 ? 106  ILE A C   1 
ATOM   803  O O   . ILE A 1 106 ? -2.556  -13.822 -1.228  1.00 33.65 ? 106  ILE A O   1 
ATOM   804  C CB  . ILE A 1 106 ? -0.724  -11.299 -0.583  1.00 33.54 ? 106  ILE A CB  1 
ATOM   805  C CG1 . ILE A 1 106 ? -1.453  -10.319 -1.516  1.00 35.53 ? 106  ILE A CG1 1 
ATOM   806  C CG2 . ILE A 1 106 ? 0.163   -12.271 -1.356  1.00 33.07 ? 106  ILE A CG2 1 
ATOM   807  C CD1 . ILE A 1 106 ? -0.917  -8.903  -1.538  1.00 35.45 ? 106  ILE A CD1 1 
ATOM   808  N N   . GLU A 1 107 ? -3.937  -12.116 -0.854  1.00 32.77 ? 107  GLU A N   1 
ATOM   809  C CA  . GLU A 1 107 ? -4.937  -12.635 -1.769  1.00 32.07 ? 107  GLU A CA  1 
ATOM   810  C C   . GLU A 1 107 ? -5.244  -11.590 -2.817  1.00 30.90 ? 107  GLU A C   1 
ATOM   811  O O   . GLU A 1 107 ? -5.852  -10.569 -2.537  1.00 31.91 ? 107  GLU A O   1 
ATOM   812  C CB  . GLU A 1 107 ? -6.183  -13.075 -1.013  1.00 32.94 ? 107  GLU A CB  1 
ATOM   813  C CG  . GLU A 1 107 ? -6.069  -14.486 -0.447  1.00 33.86 ? 107  GLU A CG  1 
ATOM   814  C CD  . GLU A 1 107 ? -6.972  -14.711 0.757   1.00 36.11 ? 107  GLU A CD  1 
ATOM   815  O OE1 . GLU A 1 107 ? -7.516  -13.717 1.286   1.00 38.08 ? 107  GLU A OE1 1 
ATOM   816  O OE2 . GLU A 1 107 ? -7.134  -15.878 1.182   1.00 37.38 ? 107  GLU A OE2 1 
ATOM   817  N N   . ARG A 1 108 ? -4.799  -11.865 -4.034  1.00 30.09 ? 108  ARG A N   1 
ATOM   818  C CA  . ARG A 1 108 ? -4.983  -10.952 -5.167  1.00 29.31 ? 108  ARG A CA  1 
ATOM   819  C C   . ARG A 1 108 ? -6.296  -11.227 -5.895  1.00 28.27 ? 108  ARG A C   1 
ATOM   820  O O   . ARG A 1 108 ? -6.692  -12.361 -6.068  1.00 25.78 ? 108  ARG A O   1 
ATOM   821  C CB  . ARG A 1 108 ? -3.780  -11.046 -6.111  1.00 29.54 ? 108  ARG A CB  1 
ATOM   822  C CG  . ARG A 1 108 ? -2.446  -10.820 -5.376  1.00 30.13 ? 108  ARG A CG  1 
ATOM   823  C CD  . ARG A 1 108 ? -1.319  -10.565 -6.307  1.00 29.92 ? 108  ARG A CD  1 
ATOM   824  N NE  . ARG A 1 108 ? -0.019  -10.544 -5.638  1.00 29.61 ? 108  ARG A NE  1 
ATOM   825  C CZ  . ARG A 1 108 ? 0.638   -9.428  -5.324  1.00 27.07 ? 108  ARG A CZ  1 
ATOM   826  N NH1 . ARG A 1 108 ? 1.831   -9.492  -4.753  1.00 27.43 ? 108  ARG A NH1 1 
ATOM   827  N NH2 . ARG A 1 108 ? 0.111   -8.246  -5.595  1.00 24.21 ? 108  ARG A NH2 1 
ATOM   828  N N   . ASP A 1 109 ? -6.968  -10.159 -6.291  1.00 29.01 ? 109  ASP A N   1 
ATOM   829  C CA  . ASP A 1 109 ? -8.298  -10.246 -6.929  1.00 30.40 ? 109  ASP A CA  1 
ATOM   830  C C   . ASP A 1 109 ? -9.266  -11.117 -6.136  1.00 28.23 ? 109  ASP A C   1 
ATOM   831  O O   . ASP A 1 109 ? -10.030 -11.881 -6.693  1.00 27.97 ? 109  ASP A O   1 
ATOM   832  C CB  . ASP A 1 109 ? -8.203  -10.730 -8.382  1.00 31.18 ? 109  ASP A CB  1 
ATOM   833  C CG  . ASP A 1 109 ? -8.237  -9.569  -9.384  1.00 36.86 ? 109  ASP A CG  1 
ATOM   834  O OD1 . ASP A 1 109 ? -7.800  -8.447  -9.013  1.00 40.78 ? 109  ASP A OD1 1 
ATOM   835  O OD2 . ASP A 1 109 ? -8.714  -9.768  -10.540 1.00 43.58 ? 109  ASP A OD2 1 
ATOM   836  N N   . LEU A 1 110 ? -9.186  -11.003 -4.824  1.00 27.25 ? 110  LEU A N   1 
ATOM   837  C CA  . LEU A 1 110 ? -10.193 -11.578 -3.942  1.00 26.98 ? 110  LEU A CA  1 
ATOM   838  C C   . LEU A 1 110 ? -11.552 -10.964 -4.272  1.00 25.64 ? 110  LEU A C   1 
ATOM   839  O O   . LEU A 1 110 ? -11.686 -9.749  -4.422  1.00 25.63 ? 110  LEU A O   1 
ATOM   840  C CB  . LEU A 1 110 ? -9.806  -11.337 -2.474  1.00 27.33 ? 110  LEU A CB  1 
ATOM   841  C CG  . LEU A 1 110 ? -10.760 -11.810 -1.376  1.00 29.28 ? 110  LEU A CG  1 
ATOM   842  C CD1 . LEU A 1 110 ? -10.020 -12.313 -0.131  1.00 30.10 ? 110  LEU A CD1 1 
ATOM   843  C CD2 . LEU A 1 110 ? -11.702 -10.653 -1.045  1.00 31.17 ? 110  LEU A CD2 1 
ATOM   844  N N   . GLU A 1 111 ? -12.545 -11.821 -4.440  1.00 25.65 ? 111  GLU A N   1 
ATOM   845  C CA  . GLU A 1 111 ? -13.921 -11.373 -4.778  1.00 26.65 ? 111  GLU A CA  1 
ATOM   846  C C   . GLU A 1 111 ? -14.791 -11.161 -3.533  1.00 26.94 ? 111  GLU A C   1 
ATOM   847  O O   . GLU A 1 111 ? -15.161 -12.114 -2.835  1.00 26.39 ? 111  GLU A O   1 
ATOM   848  C CB  . GLU A 1 111 ? -14.594 -12.369 -5.737  1.00 26.39 ? 111  GLU A CB  1 
ATOM   849  C CG  . GLU A 1 111 ? -13.710 -12.718 -6.931  1.00 27.88 ? 111  GLU A CG  1 
ATOM   850  C CD  . GLU A 1 111 ? -14.410 -13.516 -8.024  1.00 29.01 ? 111  GLU A CD  1 
ATOM   851  O OE1 . GLU A 1 111 ? -15.570 -13.971 -7.846  1.00 29.24 ? 111  GLU A OE1 1 
ATOM   852  O OE2 . GLU A 1 111 ? -13.766 -13.716 -9.071  1.00 31.12 ? 111  GLU A OE2 1 
ATOM   853  N N   . PHE A 1 112 ? -15.093 -9.897  -3.262  1.00 27.30 ? 112  PHE A N   1 
ATOM   854  C CA  . PHE A 1 112 ? -16.013 -9.532  -2.180  1.00 27.66 ? 112  PHE A CA  1 
ATOM   855  C C   . PHE A 1 112 ? -17.245 -8.772  -2.698  1.00 27.21 ? 112  PHE A C   1 
ATOM   856  O O   . PHE A 1 112 ? -17.187 -7.588  -3.051  1.00 28.12 ? 112  PHE A O   1 
ATOM   857  C CB  . PHE A 1 112 ? -15.292 -8.725  -1.082  1.00 27.67 ? 112  PHE A CB  1 
ATOM   858  C CG  . PHE A 1 112 ? -16.186 -8.341  0.079   1.00 26.09 ? 112  PHE A CG  1 
ATOM   859  C CD1 . PHE A 1 112 ? -16.374 -9.203  1.137   1.00 28.55 ? 112  PHE A CD1 1 
ATOM   860  C CD2 . PHE A 1 112 ? -16.826 -7.121  0.097   1.00 25.77 ? 112  PHE A CD2 1 
ATOM   861  C CE1 . PHE A 1 112 ? -17.177 -8.850  2.205   1.00 28.23 ? 112  PHE A CE1 1 
ATOM   862  C CE2 . PHE A 1 112 ? -17.643 -6.755  1.152   1.00 26.41 ? 112  PHE A CE2 1 
ATOM   863  C CZ  . PHE A 1 112 ? -17.829 -7.626  2.199   1.00 27.10 ? 112  PHE A CZ  1 
ATOM   864  N N   . GLU A 1 113 ? -18.347 -9.500  -2.761  1.00 27.56 ? 113  GLU A N   1 
ATOM   865  C CA  . GLU A 1 113 ? -19.648 -8.948  -3.133  1.00 27.91 ? 113  GLU A CA  1 
ATOM   866  C C   . GLU A 1 113 ? -19.631 -7.991  -4.324  1.00 26.44 ? 113  GLU A C   1 
ATOM   867  O O   . GLU A 1 113 ? -20.028 -6.835  -4.216  1.00 24.76 ? 113  GLU A O   1 
ATOM   868  C CB  . GLU A 1 113 ? -20.253 -8.256  -1.920  1.00 29.15 ? 113  GLU A CB  1 
ATOM   869  C CG  . GLU A 1 113 ? -20.124 -9.101  -0.672  1.00 33.35 ? 113  GLU A CG  1 
ATOM   870  C CD  . GLU A 1 113 ? -20.961 -8.587  0.474   1.00 37.59 ? 113  GLU A CD  1 
ATOM   871  O OE1 . GLU A 1 113 ? -21.441 -7.433  0.374   1.00 42.15 ? 113  GLU A OE1 1 
ATOM   872  O OE2 . GLU A 1 113 ? -21.142 -9.338  1.466   1.00 40.40 ? 113  GLU A OE2 1 
ATOM   873  N N   . GLY A 1 114 ? -19.195 -8.497  -5.467  1.00 26.10 ? 114  GLY A N   1 
ATOM   874  C CA  . GLY A 1 114 ? -19.284 -7.755  -6.726  1.00 26.02 ? 114  GLY A CA  1 
ATOM   875  C C   . GLY A 1 114 ? -17.978 -7.102  -7.141  1.00 26.11 ? 114  GLY A C   1 
ATOM   876  O O   . GLY A 1 114 ? -17.829 -6.732  -8.287  1.00 25.64 ? 114  GLY A O   1 
ATOM   877  N N   . TYR A 1 115 ? -17.043 -6.972  -6.196  1.00 27.45 ? 115  TYR A N   1 
ATOM   878  C CA  . TYR A 1 115 ? -15.753 -6.268  -6.412  1.00 29.08 ? 115  TYR A CA  1 
ATOM   879  C C   . TYR A 1 115 ? -14.550 -7.124  -6.089  1.00 29.76 ? 115  TYR A C   1 
ATOM   880  O O   . TYR A 1 115 ? -14.586 -7.950  -5.175  1.00 30.45 ? 115  TYR A O   1 
ATOM   881  C CB  . TYR A 1 115 ? -15.674 -4.968  -5.576  1.00 29.68 ? 115  TYR A CB  1 
ATOM   882  C CG  . TYR A 1 115 ? -16.739 -3.991  -5.977  1.00 29.87 ? 115  TYR A CG  1 
ATOM   883  C CD1 . TYR A 1 115 ? -16.514 -3.064  -6.972  1.00 32.78 ? 115  TYR A CD1 1 
ATOM   884  C CD2 . TYR A 1 115 ? -17.999 -4.050  -5.408  1.00 34.08 ? 115  TYR A CD2 1 
ATOM   885  C CE1 . TYR A 1 115 ? -17.523 -2.196  -7.392  1.00 33.63 ? 115  TYR A CE1 1 
ATOM   886  C CE2 . TYR A 1 115 ? -19.010 -3.195  -5.808  1.00 35.16 ? 115  TYR A CE2 1 
ATOM   887  C CZ  . TYR A 1 115 ? -18.760 -2.265  -6.802  1.00 34.96 ? 115  TYR A CZ  1 
ATOM   888  O OH  . TYR A 1 115 ? -19.762 -1.410  -7.194  1.00 37.88 ? 115  TYR A OH  1 
ATOM   889  N N   . ASN A 1 116 ? -13.474 -6.895  -6.836  1.00 30.52 ? 116  ASN A N   1 
ATOM   890  C CA  . ASN A 1 116 ? -12.181 -7.543  -6.574  1.00 31.18 ? 116  ASN A CA  1 
ATOM   891  C C   . ASN A 1 116 ? -11.202 -6.677  -5.802  1.00 30.92 ? 116  ASN A C   1 
ATOM   892  O O   . ASN A 1 116 ? -11.130 -5.456  -5.982  1.00 30.50 ? 116  ASN A O   1 
ATOM   893  C CB  . ASN A 1 116 ? -11.529 -8.011  -7.869  1.00 31.65 ? 116  ASN A CB  1 
ATOM   894  C CG  . ASN A 1 116 ? -12.283 -9.145  -8.504  1.00 34.18 ? 116  ASN A CG  1 
ATOM   895  O OD1 . ASN A 1 116 ? -13.502 -9.230  -8.391  1.00 38.40 ? 116  ASN A OD1 1 
ATOM   896  N ND2 . ASN A 1 116 ? -11.567 -10.035 -9.171  1.00 38.91 ? 116  ASN A ND2 1 
ATOM   897  N N   . PHE A 1 117 ? -10.444 -7.346  -4.943  1.00 30.50 ? 117  PHE A N   1 
ATOM   898  C CA  . PHE A 1 117 ? -9.499  -6.677  -4.053  1.00 30.76 ? 117  PHE A CA  1 
ATOM   899  C C   . PHE A 1 117 ? -8.208  -7.443  -3.848  1.00 30.29 ? 117  PHE A C   1 
ATOM   900  O O   . PHE A 1 117 ? -8.206  -8.668  -3.746  1.00 29.62 ? 117  PHE A O   1 
ATOM   901  C CB  . PHE A 1 117 ? -10.140 -6.444  -2.676  1.00 30.44 ? 117  PHE A CB  1 
ATOM   902  C CG  . PHE A 1 117 ? -11.306 -5.495  -2.708  1.00 30.89 ? 117  PHE A CG  1 
ATOM   903  C CD1 . PHE A 1 117 ? -11.105 -4.141  -2.896  1.00 30.59 ? 117  PHE A CD1 1 
ATOM   904  C CD2 . PHE A 1 117 ? -12.603 -5.961  -2.550  1.00 29.93 ? 117  PHE A CD2 1 
ATOM   905  C CE1 . PHE A 1 117 ? -12.176 -3.275  -2.923  1.00 31.22 ? 117  PHE A CE1 1 
ATOM   906  C CE2 . PHE A 1 117 ? -13.670 -5.091  -2.550  1.00 29.88 ? 117  PHE A CE2 1 
ATOM   907  C CZ  . PHE A 1 117 ? -13.453 -3.751  -2.749  1.00 30.16 ? 117  PHE A CZ  1 
ATOM   908  N N   . ASP A 1 118 ? -7.116  -6.687  -3.804  1.00 30.52 ? 118  ASP A N   1 
ATOM   909  C CA  . ASP A 1 118 ? -5.830  -7.214  -3.379  1.00 32.54 ? 118  ASP A CA  1 
ATOM   910  C C   . ASP A 1 118 ? -5.770  -6.929  -1.890  1.00 31.11 ? 118  ASP A C   1 
ATOM   911  O O   . ASP A 1 118 ? -5.816  -5.779  -1.479  1.00 29.45 ? 118  ASP A O   1 
ATOM   912  C CB  . ASP A 1 118 ? -4.652  -6.508  -4.049  1.00 33.82 ? 118  ASP A CB  1 
ATOM   913  C CG  . ASP A 1 118 ? -4.506  -6.843  -5.518  1.00 38.30 ? 118  ASP A CG  1 
ATOM   914  O OD1 . ASP A 1 118 ? -5.237  -7.721  -6.057  1.00 41.61 ? 118  ASP A OD1 1 
ATOM   915  O OD2 . ASP A 1 118 ? -3.607  -6.214  -6.134  1.00 43.09 ? 118  ASP A OD2 1 
ATOM   916  N N   . VAL A 1 119 ? -5.669  -7.986  -1.103  1.00 30.92 ? 119  VAL A N   1 
ATOM   917  C CA  . VAL A 1 119 ? -5.732  -7.873  0.360   1.00 31.60 ? 119  VAL A CA  1 
ATOM   918  C C   . VAL A 1 119 ? -4.668  -8.739  0.985   1.00 31.12 ? 119  VAL A C   1 
ATOM   919  O O   . VAL A 1 119 ? -4.581  -9.935  0.697   1.00 30.35 ? 119  VAL A O   1 
ATOM   920  C CB  . VAL A 1 119 ? -7.118  -8.299  0.933   1.00 31.17 ? 119  VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 119 ? -7.539  -9.590  0.334   1.00 34.24 ? 119  VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 119 ? -7.079  -8.406  2.488   1.00 30.30 ? 119  VAL A CG2 1 
ATOM   923  N N   . ALA A 1 120 ? -3.878  -8.110  1.856   1.00 30.88 ? 120  ALA A N   1 
ATOM   924  C CA  . ALA A 1 120 ? -2.775  -8.772  2.555   1.00 31.64 ? 120  ALA A CA  1 
ATOM   925  C C   . ALA A 1 120 ? -3.053  -8.763  4.048   1.00 32.14 ? 120  ALA A C   1 
ATOM   926  O O   . ALA A 1 120 ? -3.701  -7.860  4.571   1.00 32.47 ? 120  ALA A O   1 
ATOM   927  C CB  . ALA A 1 120 ? -1.417  -8.086  2.225   1.00 29.68 ? 120  ALA A CB  1 
ATOM   928  N N   . THR A 1 121 ? -2.580  -9.798  4.722   1.00 33.65 ? 121  THR A N   1 
ATOM   929  C CA  . THR A 1 121 ? -2.751  -9.923  6.174   1.00 34.95 ? 121  THR A CA  1 
ATOM   930  C C   . THR A 1 121 ? -1.417  -10.230 6.849   1.00 34.05 ? 121  THR A C   1 
ATOM   931  O O   . THR A 1 121 ? -0.652  -11.053 6.373   1.00 33.19 ? 121  THR A O   1 
ATOM   932  C CB  . THR A 1 121 ? -3.790  -11.013 6.523   1.00 35.89 ? 121  THR A CB  1 
ATOM   933  O OG1 . THR A 1 121 ? -5.124  -10.475 6.377   1.00 41.28 ? 121  THR A OG1 1 
ATOM   934  C CG2 . THR A 1 121 ? -3.612  -11.493 7.954   1.00 37.86 ? 121  THR A CG2 1 
ATOM   935  N N   . CYS A 1 122 ? -1.156  -9.503  7.932   1.00 34.18 ? 122  CYS A N   1 
ATOM   936  C CA  . CYS A 1 122 ? 0.042   -9.661  8.774   1.00 33.95 ? 122  CYS A CA  1 
ATOM   937  C C   . CYS A 1 122 ? -0.341  -9.783  10.254  1.00 32.68 ? 122  CYS A C   1 
ATOM   938  O O   . CYS A 1 122 ? -1.357  -9.234  10.701  1.00 32.32 ? 122  CYS A O   1 
ATOM   939  C CB  . CYS A 1 122 ? 0.974   -8.451  8.635   1.00 33.65 ? 122  CYS A CB  1 
ATOM   940  S SG  . CYS A 1 122 ? 1.482   -8.001  6.969   1.00 40.10 ? 122  CYS A SG  1 
ATOM   941  N N   . ALA A 1 123 ? 0.521   -10.460 11.006  1.00 31.63 ? 123  ALA A N   1 
ATOM   942  C CA  . ALA A 1 123 ? 0.272   -10.774 12.407  1.00 31.60 ? 123  ALA A CA  1 
ATOM   943  C C   . ALA A 1 123 ? 1.317   -10.200 13.372  1.00 31.27 ? 123  ALA A C   1 
ATOM   944  O O   . ALA A 1 123 ? 2.526   -10.169 13.101  1.00 31.35 ? 123  ALA A O   1 
ATOM   945  C CB  . ALA A 1 123 ? 0.162   -12.293 12.583  1.00 30.81 ? 123  ALA A CB  1 
ATOM   946  N N   . LYS A 1 124 ? 0.823   -9.751  14.514  1.00 30.58 ? 124  LYS A N   1 
ATOM   947  C CA  . LYS A 1 124 ? 1.683   -9.511  15.675  1.00 30.13 ? 124  LYS A CA  1 
ATOM   948  C C   . LYS A 1 124 ? 1.242   -10.369 16.851  1.00 30.57 ? 124  LYS A C   1 
ATOM   949  O O   . LYS A 1 124 ? 0.376   -11.232 16.704  1.00 32.03 ? 124  LYS A O   1 
ATOM   950  C CB  . LYS A 1 124 ? 1.706   -8.034  16.086  1.00 29.45 ? 124  LYS A CB  1 
ATOM   951  C CG  . LYS A 1 124 ? 0.371   -7.320  16.147  1.00 28.84 ? 124  LYS A CG  1 
ATOM   952  C CD  . LYS A 1 124 ? 0.451   -6.148  17.076  1.00 32.20 ? 124  LYS A CD  1 
ATOM   953  C CE  . LYS A 1 124 ? 0.408   -6.663  18.517  1.00 35.91 ? 124  LYS A CE  1 
ATOM   954  N NZ  . LYS A 1 124 ? 0.961   -5.716  19.525  1.00 39.39 ? 124  LYS A NZ  1 
ATOM   955  N N   . LEU A 1 125 ? 1.831   -10.106 18.018  1.00 30.35 ? 125  LEU A N   1 
ATOM   956  C CA  . LEU A 1 125 ? 1.400   -10.738 19.244  1.00 30.28 ? 125  LEU A CA  1 
ATOM   957  C C   . LEU A 1 125 ? -0.020  -10.241 19.517  1.00 29.68 ? 125  LEU A C   1 
ATOM   958  O O   . LEU A 1 125 ? -0.263  -9.041  19.615  1.00 30.26 ? 125  LEU A O   1 
ATOM   959  C CB  . LEU A 1 125 ? 2.353   -10.403 20.405  1.00 30.89 ? 125  LEU A CB  1 
ATOM   960  C CG  . LEU A 1 125 ? 1.937   -10.945 21.782  1.00 31.92 ? 125  LEU A CG  1 
ATOM   961  C CD1 . LEU A 1 125 ? 1.730   -12.440 21.731  1.00 32.75 ? 125  LEU A CD1 1 
ATOM   962  C CD2 . LEU A 1 125 ? 2.953   -10.596 22.855  1.00 32.58 ? 125  LEU A CD2 1 
ATOM   963  N N   . LYS A 1 126 ? -0.967  -11.168 19.590  1.00 29.68 ? 126  LYS A N   1 
ATOM   964  C CA  . LYS A 1 126 ? -2.347  -10.845 20.021  1.00 28.89 ? 126  LYS A CA  1 
ATOM   965  C C   . LYS A 1 126 ? -2.968  -9.736  19.178  1.00 28.28 ? 126  LYS A C   1 
ATOM   966  O O   . LYS A 1 126 ? -3.658  -8.850  19.683  1.00 27.45 ? 126  LYS A O   1 
ATOM   967  C CB  . LYS A 1 126 ? -2.361  -10.477 21.502  1.00 28.55 ? 126  LYS A CB  1 
ATOM   968  C CG  . LYS A 1 126 ? -1.796  -11.587 22.375  1.00 29.74 ? 126  LYS A CG  1 
ATOM   969  C CD  . LYS A 1 126 ? -1.894  -11.266 23.871  1.00 31.28 ? 126  LYS A CD  1 
ATOM   970  C CE  . LYS A 1 126 ? -3.249  -11.686 24.389  1.00 33.52 ? 126  LYS A CE  1 
ATOM   971  N NZ  . LYS A 1 126 ? -3.314  -11.742 25.886  1.00 34.90 ? 126  LYS A NZ  1 
ATOM   972  N N   . GLY A 1 127 ? -2.700  -9.802  17.875  1.00 27.49 ? 127  GLY A N   1 
ATOM   973  C CA  . GLY A 1 127 ? -3.239  -8.848  16.935  1.00 27.30 ? 127  GLY A CA  1 
ATOM   974  C C   . GLY A 1 127 ? -2.684  -8.962  15.538  1.00 26.84 ? 127  GLY A C   1 
ATOM   975  O O   . GLY A 1 127 ? -1.938  -9.872  15.208  1.00 26.32 ? 127  GLY A O   1 
ATOM   976  N N   . GLY A 1 128 ? -3.040  -7.997  14.720  1.00 27.89 ? 128  GLY A N   1 
ATOM   977  C CA  . GLY A 1 128 ? -2.551  -7.967  13.347  1.00 30.06 ? 128  GLY A CA  1 
ATOM   978  C C   . GLY A 1 128 ? -3.043  -6.780  12.566  1.00 30.15 ? 128  GLY A C   1 
ATOM   979  O O   . GLY A 1 128 ? -3.590  -5.828  13.116  1.00 28.79 ? 128  GLY A O   1 
ATOM   980  N N   . LEU A 1 129 ? -2.869  -6.872  11.256  1.00 31.16 ? 129  LEU A N   1 
ATOM   981  C CA  . LEU A 1 129 ? -3.389  -5.858  10.365  1.00 31.82 ? 129  LEU A CA  1 
ATOM   982  C C   . LEU A 1 129 ? -3.776  -6.430  9.007   1.00 30.78 ? 129  LEU A C   1 
ATOM   983  O O   . LEU A 1 129 ? -3.319  -7.491  8.607   1.00 30.96 ? 129  LEU A O   1 
ATOM   984  C CB  . LEU A 1 129 ? -2.383  -4.715  10.232  1.00 32.95 ? 129  LEU A CB  1 
ATOM   985  C CG  . LEU A 1 129 ? -1.046  -5.056  9.601   1.00 33.65 ? 129  LEU A CG  1 
ATOM   986  C CD1 . LEU A 1 129 ? -1.298  -5.462  8.136   1.00 34.63 ? 129  LEU A CD1 1 
ATOM   987  C CD2 . LEU A 1 129 ? -0.080  -3.873  9.721   1.00 34.58 ? 129  LEU A CD2 1 
ATOM   988  N N   . HIS A 1 130 ? -4.666  -5.722  8.334   1.00 29.67 ? 130  HIS A N   1 
ATOM   989  C CA  . HIS A 1 130 ? -5.016  -6.040  6.956   1.00 29.36 ? 130  HIS A CA  1 
ATOM   990  C C   . HIS A 1 130 ? -4.694  -4.830  6.135   1.00 28.46 ? 130  HIS A C   1 
ATOM   991  O O   . HIS A 1 130 ? -4.857  -3.699  6.597   1.00 26.33 ? 130  HIS A O   1 
ATOM   992  C CB  . HIS A 1 130 ? -6.510  -6.363  6.820   1.00 29.69 ? 130  HIS A CB  1 
ATOM   993  C CG  . HIS A 1 130 ? -6.956  -7.475  7.718   1.00 29.49 ? 130  HIS A CG  1 
ATOM   994  N ND1 . HIS A 1 130 ? -6.672  -8.795  7.456   1.00 29.00 ? 130  HIS A ND1 1 
ATOM   995  C CD2 . HIS A 1 130 ? -7.633  -7.461  8.890   1.00 26.76 ? 130  HIS A CD2 1 
ATOM   996  C CE1 . HIS A 1 130 ? -7.190  -9.552  8.409   1.00 27.43 ? 130  HIS A CE1 1 
ATOM   997  N NE2 . HIS A 1 130 ? -7.774  -8.766  9.290   1.00 27.22 ? 130  HIS A NE2 1 
ATOM   998  N N   . LEU A 1 131 ? -4.214  -5.100  4.932   1.00 28.35 ? 131  LEU A N   1 
ATOM   999  C CA  . LEU A 1 131 ? -3.926  -4.072  3.924   1.00 29.18 ? 131  LEU A CA  1 
ATOM   1000 C C   . LEU A 1 131 ? -4.715  -4.376  2.661   1.00 29.06 ? 131  LEU A C   1 
ATOM   1001 O O   . LEU A 1 131 ? -4.640  -5.495  2.115   1.00 29.43 ? 131  LEU A O   1 
ATOM   1002 C CB  . LEU A 1 131 ? -2.448  -4.099  3.544   1.00 28.31 ? 131  LEU A CB  1 
ATOM   1003 C CG  . LEU A 1 131 ? -1.433  -3.957  4.666   1.00 28.70 ? 131  LEU A CG  1 
ATOM   1004 C CD1 . LEU A 1 131 ? -0.052  -4.414  4.184   1.00 25.46 ? 131  LEU A CD1 1 
ATOM   1005 C CD2 . LEU A 1 131 ? -1.407  -2.508  5.177   1.00 26.14 ? 131  LEU A CD2 1 
ATOM   1006 N N   . VAL A 1 132 ? -5.444  -3.367  2.200   1.00 28.68 ? 132  VAL A N   1 
ATOM   1007 C CA  . VAL A 1 132 ? -6.317  -3.487  1.041   1.00 28.50 ? 132  VAL A CA  1 
ATOM   1008 C C   . VAL A 1 132 ? -6.097  -2.315  0.095   1.00 28.82 ? 132  VAL A C   1 
ATOM   1009 O O   . VAL A 1 132 ? -6.215  -1.155  0.488   1.00 28.75 ? 132  VAL A O   1 
ATOM   1010 C CB  . VAL A 1 132 ? -7.812  -3.495  1.453   1.00 29.60 ? 132  VAL A CB  1 
ATOM   1011 C CG1 . VAL A 1 132 ? -8.715  -3.943  0.251   1.00 28.13 ? 132  VAL A CG1 1 
ATOM   1012 C CG2 . VAL A 1 132 ? -8.026  -4.349  2.678   1.00 27.54 ? 132  VAL A CG2 1 
ATOM   1013 N N   . LYS A 1 133 ? -5.765  -2.615  -1.158  1.00 29.55 ? 133  LYS A N   1 
ATOM   1014 C CA  . LYS A 1 133 ? -5.678  -1.561  -2.169  1.00 30.42 ? 133  LYS A CA  1 
ATOM   1015 C C   . LYS A 1 133 ? -7.087  -1.095  -2.548  1.00 30.03 ? 133  LYS A C   1 
ATOM   1016 O O   . LYS A 1 133 ? -7.922  -1.898  -2.909  1.00 30.95 ? 133  LYS A O   1 
ATOM   1017 C CB  . LYS A 1 133 ? -4.897  -2.022  -3.403  1.00 30.98 ? 133  LYS A CB  1 
ATOM   1018 C CG  . LYS A 1 133 ? -3.434  -1.930  -3.194  1.00 33.15 ? 133  LYS A CG  1 
ATOM   1019 C CD  . LYS A 1 133 ? -2.683  -1.934  -4.479  1.00 35.94 ? 133  LYS A CD  1 
ATOM   1020 C CE  . LYS A 1 133 ? -1.239  -1.575  -4.248  1.00 37.96 ? 133  LYS A CE  1 
ATOM   1021 N NZ  . LYS A 1 133 ? -0.463  -1.617  -5.524  1.00 40.11 ? 133  LYS A NZ  1 
ATOM   1022 N N   . VAL A 1 134 ? -7.332  0.202   -2.429  1.00 30.51 ? 134  VAL A N   1 
ATOM   1023 C CA  . VAL A 1 134 ? -8.651  0.812   -2.678  1.00 31.45 ? 134  VAL A CA  1 
ATOM   1024 C C   . VAL A 1 134 ? -8.433  1.949   -3.686  1.00 33.03 ? 134  VAL A C   1 
ATOM   1025 O O   . VAL A 1 134 ? -7.294  2.282   -3.973  1.00 34.20 ? 134  VAL A O   1 
ATOM   1026 C CB  . VAL A 1 134 ? -9.306  1.314   -1.344  1.00 31.15 ? 134  VAL A CB  1 
ATOM   1027 C CG1 . VAL A 1 134 ? -9.388  0.171   -0.342  1.00 29.68 ? 134  VAL A CG1 1 
ATOM   1028 C CG2 . VAL A 1 134 ? -8.512  2.472   -0.717  1.00 29.43 ? 134  VAL A CG2 1 
ATOM   1029 N N   . PRO A 1 135 ? -9.503  2.555   -4.236  1.00 34.90 ? 135  PRO A N   1 
ATOM   1030 C CA  . PRO A 1 135 ? -9.223  3.471   -5.362  1.00 35.68 ? 135  PRO A CA  1 
ATOM   1031 C C   . PRO A 1 135 ? -8.560  4.768   -4.966  1.00 36.08 ? 135  PRO A C   1 
ATOM   1032 O O   . PRO A 1 135 ? -8.486  5.107   -3.786  1.00 37.33 ? 135  PRO A O   1 
ATOM   1033 C CB  . PRO A 1 135 ? -10.607 3.768   -5.945  1.00 35.96 ? 135  PRO A CB  1 
ATOM   1034 C CG  . PRO A 1 135 ? -11.552 3.545   -4.810  1.00 36.80 ? 135  PRO A CG  1 
ATOM   1035 C CD  . PRO A 1 135 ? -10.938 2.485   -3.911  1.00 35.22 ? 135  PRO A CD  1 
ATOM   1036 N N   . GLY A 1 136 ? -8.104  5.487   -5.981  1.00 35.89 ? 136  GLY A N   1 
ATOM   1037 C CA  . GLY A 1 136 ? -7.403  6.747   -5.798  1.00 35.07 ? 136  GLY A CA  1 
ATOM   1038 C C   . GLY A 1 136 ? -5.924  6.466   -5.624  1.00 34.02 ? 136  GLY A C   1 
ATOM   1039 O O   . GLY A 1 136 ? -5.133  7.376   -5.388  1.00 34.90 ? 136  GLY A O   1 
ATOM   1040 N N   . GLY A 1 137 ? -5.567  5.193   -5.759  1.00 32.48 ? 137  GLY A N   1 
ATOM   1041 C CA  . GLY A 1 137 ? -4.184  4.743   -5.572  1.00 31.45 ? 137  GLY A CA  1 
ATOM   1042 C C   . GLY A 1 137 ? -3.859  4.775   -4.087  1.00 30.15 ? 137  GLY A C   1 
ATOM   1043 O O   . GLY A 1 137 ? -2.824  5.297   -3.676  1.00 27.87 ? 137  GLY A O   1 
ATOM   1044 N N   . ASN A 1 138 ? -4.788  4.247   -3.293  1.00 29.68 ? 138  ASN A N   1 
ATOM   1045 C CA  . ASN A 1 138 ? -4.655  4.207   -1.835  1.00 29.89 ? 138  ASN A CA  1 
ATOM   1046 C C   . ASN A 1 138 ? -4.538  2.789   -1.317  1.00 29.72 ? 138  ASN A C   1 
ATOM   1047 O O   . ASN A 1 138 ? -5.040  1.851   -1.925  1.00 28.75 ? 138  ASN A O   1 
ATOM   1048 C CB  . ASN A 1 138 ? -5.869  4.843   -1.159  1.00 30.48 ? 138  ASN A CB  1 
ATOM   1049 C CG  . ASN A 1 138 ? -5.867  6.346   -1.239  1.00 31.98 ? 138  ASN A CG  1 
ATOM   1050 O OD1 . ASN A 1 138 ? -6.756  6.951   -1.856  1.00 36.28 ? 138  ASN A OD1 1 
ATOM   1051 N ND2 . ASN A 1 138 ? -4.879  6.964   -0.627  1.00 30.49 ? 138  ASN A ND2 1 
ATOM   1052 N N   . ILE A 1 139 ? -3.868  2.660   -0.174  1.00 29.89 ? 139  ILE A N   1 
ATOM   1053 C CA  . ILE A 1 139 ? -3.875  1.436   0.600   1.00 29.86 ? 139  ILE A CA  1 
ATOM   1054 C C   . ILE A 1 139 ? -4.610  1.709   1.925   1.00 31.59 ? 139  ILE A C   1 
ATOM   1055 O O   . ILE A 1 139 ? -4.358  2.718   2.622   1.00 31.67 ? 139  ILE A O   1 
ATOM   1056 C CB  . ILE A 1 139 ? -2.433  0.907   0.852   1.00 29.64 ? 139  ILE A CB  1 
ATOM   1057 C CG1 . ILE A 1 139 ? -1.691  0.719   -0.477  1.00 28.83 ? 139  ILE A CG1 1 
ATOM   1058 C CG2 . ILE A 1 139 ? -2.466  -0.405  1.626   1.00 27.17 ? 139  ILE A CG2 1 
ATOM   1059 C CD1 . ILE A 1 139 ? -0.208  0.435   -0.313  1.00 27.78 ? 139  ILE A CD1 1 
ATOM   1060 N N   . LEU A 1 140 ? -5.550  0.823   2.238   1.00 32.32 ? 140  LEU A N   1 
ATOM   1061 C CA  . LEU A 1 140 ? -6.307  0.904   3.493   1.00 33.29 ? 140  LEU A CA  1 
ATOM   1062 C C   . LEU A 1 140 ? -5.599  0.003   4.499   1.00 32.63 ? 140  LEU A C   1 
ATOM   1063 O O   . LEU A 1 140 ? -5.297  -1.147  4.198   1.00 32.08 ? 140  LEU A O   1 
ATOM   1064 C CB  . LEU A 1 140 ? -7.768  0.459   3.307   1.00 33.10 ? 140  LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 140 ? -8.565  0.252   4.607   1.00 33.39 ? 140  LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 140 ? -8.926  1.610   5.220   1.00 33.05 ? 140  LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 140 ? -9.826  -0.596  4.354   1.00 32.20 ? 140  LEU A CD2 1 
ATOM   1068 N N   . VAL A 1 141 ? -5.290  0.557   5.662   1.00 32.30 ? 141  VAL A N   1 
ATOM   1069 C CA  . VAL A 1 141 ? -4.614  -0.200  6.724   1.00 32.32 ? 141  VAL A CA  1 
ATOM   1070 C C   . VAL A 1 141 ? -5.589  -0.371  7.870   1.00 32.28 ? 141  VAL A C   1 
ATOM   1071 O O   . VAL A 1 141 ? -6.116  0.599   8.409   1.00 31.42 ? 141  VAL A O   1 
ATOM   1072 C CB  . VAL A 1 141 ? -3.398  0.541   7.285   1.00 33.05 ? 141  VAL A CB  1 
ATOM   1073 C CG1 . VAL A 1 141 ? -2.476  -0.464  8.104   1.00 33.08 ? 141  VAL A CG1 1 
ATOM   1074 C CG2 . VAL A 1 141 ? -2.659  1.303   6.162   1.00 32.96 ? 141  VAL A CG2 1 
ATOM   1075 N N   . VAL A 1 142 ? -5.849  -1.610  8.226   1.00 32.29 ? 142  VAL A N   1 
ATOM   1076 C CA  . VAL A 1 142 ? -6.758  -1.869  9.311   1.00 33.00 ? 142  VAL A CA  1 
ATOM   1077 C C   . VAL A 1 142 ? -6.059  -2.712  10.370  1.00 32.37 ? 142  VAL A C   1 
ATOM   1078 O O   . VAL A 1 142 ? -5.425  -3.737  10.046  1.00 32.16 ? 142  VAL A O   1 
ATOM   1079 C CB  . VAL A 1 142 ? -8.043  -2.531  8.779   1.00 33.82 ? 142  VAL A CB  1 
ATOM   1080 C CG1 . VAL A 1 142 ? -8.868  -3.064  9.905   1.00 34.34 ? 142  VAL A CG1 1 
ATOM   1081 C CG2 . VAL A 1 142 ? -8.825  -1.532  7.900   1.00 33.13 ? 142  VAL A CG2 1 
ATOM   1082 N N   . LEU A 1 143 ? -6.141  -2.236  11.620  1.00 30.72 ? 143  LEU A N   1 
ATOM   1083 C CA  . LEU A 1 143 ? -5.583  -2.957  12.776  1.00 30.97 ? 143  LEU A CA  1 
ATOM   1084 C C   . LEU A 1 143 ? -6.662  -3.711  13.548  1.00 30.96 ? 143  LEU A C   1 
ATOM   1085 O O   . LEU A 1 143 ? -7.826  -3.293  13.593  1.00 31.02 ? 143  LEU A O   1 
ATOM   1086 C CB  . LEU A 1 143 ? -4.852  -2.008  13.734  1.00 30.47 ? 143  LEU A CB  1 
ATOM   1087 C CG  . LEU A 1 143 ? -3.851  -1.030  13.104  1.00 31.39 ? 143  LEU A CG  1 
ATOM   1088 C CD1 . LEU A 1 143 ? -3.080  -0.353  14.189  1.00 29.87 ? 143  LEU A CD1 1 
ATOM   1089 C CD2 . LEU A 1 143 ? -2.911  -1.766  12.160  1.00 29.08 ? 143  LEU A CD2 1 
ATOM   1090 N N   . TYR A 1 144 ? -6.254  -4.842  14.112  1.00 30.80 ? 144  TYR A N   1 
ATOM   1091 C CA  . TYR A 1 144 ? -7.072  -5.595  15.061  1.00 30.59 ? 144  TYR A CA  1 
ATOM   1092 C C   . TYR A 1 144 ? -6.287  -6.080  16.290  1.00 30.22 ? 144  TYR A C   1 
ATOM   1093 O O   . TYR A 1 144 ? -5.072  -6.348  16.251  1.00 27.43 ? 144  TYR A O   1 
ATOM   1094 C CB  . TYR A 1 144 ? -7.818  -6.760  14.382  1.00 30.84 ? 144  TYR A CB  1 
ATOM   1095 C CG  . TYR A 1 144 ? -6.955  -7.926  13.988  1.00 29.30 ? 144  TYR A CG  1 
ATOM   1096 C CD1 . TYR A 1 144 ? -6.718  -8.969  14.870  1.00 30.85 ? 144  TYR A CD1 1 
ATOM   1097 C CD2 . TYR A 1 144 ? -6.404  -8.003  12.719  1.00 31.08 ? 144  TYR A CD2 1 
ATOM   1098 C CE1 . TYR A 1 144 ? -5.920  -10.045 14.512  1.00 30.00 ? 144  TYR A CE1 1 
ATOM   1099 C CE2 . TYR A 1 144 ? -5.595  -9.082  12.345  1.00 31.70 ? 144  TYR A CE2 1 
ATOM   1100 C CZ  . TYR A 1 144 ? -5.355  -10.084 13.246  1.00 31.02 ? 144  TYR A CZ  1 
ATOM   1101 O OH  . TYR A 1 144 ? -4.585  -11.150 12.864  1.00 32.39 ? 144  TYR A OH  1 
ATOM   1102 N N   . ASP A 1 145 ? -7.024  -6.158  17.395  1.00 30.82 ? 145  ASP A N   1 
ATOM   1103 C CA  . ASP A 1 145 ? -6.440  -6.374  18.724  1.00 31.37 ? 145  ASP A CA  1 
ATOM   1104 C C   . ASP A 1 145 ? -7.256  -7.419  19.464  1.00 31.80 ? 145  ASP A C   1 
ATOM   1105 O O   . ASP A 1 145 ? -8.398  -7.164  19.880  1.00 31.06 ? 145  ASP A O   1 
ATOM   1106 C CB  . ASP A 1 145 ? -6.408  -5.047  19.476  1.00 31.69 ? 145  ASP A CB  1 
ATOM   1107 C CG  . ASP A 1 145 ? -5.836  -5.159  20.897  1.00 33.37 ? 145  ASP A CG  1 
ATOM   1108 O OD1 . ASP A 1 145 ? -5.722  -6.268  21.469  1.00 34.72 ? 145  ASP A OD1 1 
ATOM   1109 O OD2 . ASP A 1 145 ? -5.492  -4.100  21.448  1.00 34.19 ? 145  ASP A OD2 1 
ATOM   1110 N N   . GLU A 1 146 ? -6.648  -8.591  19.616  1.00 32.16 ? 146  GLU A N   1 
ATOM   1111 C CA  . GLU A 1 146 ? -7.336  -9.767  20.165  1.00 33.33 ? 146  GLU A CA  1 
ATOM   1112 C C   . GLU A 1 146 ? -7.710  -9.646  21.625  1.00 32.95 ? 146  GLU A C   1 
ATOM   1113 O O   . GLU A 1 146 ? -8.566  -10.372 22.102  1.00 34.28 ? 146  GLU A O   1 
ATOM   1114 C CB  . GLU A 1 146 ? -6.523  -11.034 19.932  1.00 33.51 ? 146  GLU A CB  1 
ATOM   1115 C CG  . GLU A 1 146 ? -6.509  -11.367 18.453  1.00 35.87 ? 146  GLU A CG  1 
ATOM   1116 C CD  . GLU A 1 146 ? -5.666  -12.558 18.085  1.00 36.26 ? 146  GLU A CD  1 
ATOM   1117 O OE1 . GLU A 1 146 ? -5.010  -13.157 18.963  1.00 39.89 ? 146  GLU A OE1 1 
ATOM   1118 O OE2 . GLU A 1 146 ? -5.662  -12.891 16.888  1.00 38.71 ? 146  GLU A OE2 1 
ATOM   1119 N N   . GLU A 1 147 ? -7.087  -8.714  22.322  1.00 32.48 ? 147  GLU A N   1 
ATOM   1120 C CA  . GLU A 1 147 ? -7.442  -8.433  23.712  1.00 32.46 ? 147  GLU A CA  1 
ATOM   1121 C C   . GLU A 1 147 ? -8.723  -7.590  23.789  1.00 31.89 ? 147  GLU A C   1 
ATOM   1122 O O   . GLU A 1 147 ? -9.290  -7.413  24.852  1.00 30.71 ? 147  GLU A O   1 
ATOM   1123 C CB  . GLU A 1 147 ? -6.281  -7.733  24.419  1.00 32.41 ? 147  GLU A CB  1 
ATOM   1124 C CG  . GLU A 1 147 ? -5.033  -8.599  24.440  1.00 35.36 ? 147  GLU A CG  1 
ATOM   1125 C CD  . GLU A 1 147 ? -3.862  -7.957  25.148  1.00 38.56 ? 147  GLU A CD  1 
ATOM   1126 O OE1 . GLU A 1 147 ? -3.368  -6.925  24.664  1.00 41.05 ? 147  GLU A OE1 1 
ATOM   1127 O OE2 . GLU A 1 147 ? -3.411  -8.498  26.182  1.00 42.02 ? 147  GLU A OE2 1 
ATOM   1128 N N   . LYS A 1 148 ? -9.185  -7.085  22.652  1.00 32.19 ? 148  LYS A N   1 
ATOM   1129 C CA  . LYS A 1 148 ? -10.385 -6.237  22.631  1.00 32.49 ? 148  LYS A CA  1 
ATOM   1130 C C   . LYS A 1 148 ? -11.580 -6.904  21.968  1.00 31.84 ? 148  LYS A C   1 
ATOM   1131 O O   . LYS A 1 148 ? -12.427 -6.234  21.383  1.00 31.13 ? 148  LYS A O   1 
ATOM   1132 C CB  . LYS A 1 148 ? -10.105 -4.901  21.943  1.00 33.12 ? 148  LYS A CB  1 
ATOM   1133 C CG  . LYS A 1 148 ? -9.038  -4.058  22.623  1.00 36.04 ? 148  LYS A CG  1 
ATOM   1134 C CD  . LYS A 1 148 ? -9.449  -2.592  22.698  1.00 38.08 ? 148  LYS A CD  1 
ATOM   1135 C CE  . LYS A 1 148 ? -8.325  -1.709  23.214  1.00 39.18 ? 148  LYS A CE  1 
ATOM   1136 N NZ  . LYS A 1 148 ? -7.604  -2.345  24.349  1.00 40.50 ? 148  LYS A NZ  1 
ATOM   1137 N N   . GLU A 1 149 ? -11.663 -8.220  22.070  1.00 32.61 ? 149  GLU A N   1 
ATOM   1138 C CA  . GLU A 1 149 ? -12.798 -8.950  21.480  1.00 33.90 ? 149  GLU A CA  1 
ATOM   1139 C C   . GLU A 1 149 ? -12.797 -8.790  19.962  1.00 33.88 ? 149  GLU A C   1 
ATOM   1140 O O   . GLU A 1 149 ? -13.842 -8.805  19.314  1.00 34.38 ? 149  GLU A O   1 
ATOM   1141 C CB  . GLU A 1 149 ? -14.131 -8.423  22.004  1.00 34.55 ? 149  GLU A CB  1 
ATOM   1142 C CG  . GLU A 1 149 ? -14.599 -8.988  23.356  1.00 36.35 ? 149  GLU A CG  1 
ATOM   1143 C CD  . GLU A 1 149 ? -16.128 -8.980  23.481  1.00 38.72 ? 149  GLU A CD  1 
ATOM   1144 O OE1 . GLU A 1 149 ? -16.648 -8.824  24.609  1.00 41.77 ? 149  GLU A OE1 1 
ATOM   1145 O OE2 . GLU A 1 149 ? -16.825 -9.125  22.449  1.00 41.04 ? 149  GLU A OE2 1 
ATOM   1146 N N   . GLN A 1 150 ? -11.622 -8.583  19.403  1.00 33.53 ? 150  GLN A N   1 
ATOM   1147 C CA  . GLN A 1 150 ? -11.484 -8.562  17.951  1.00 33.78 ? 150  GLN A CA  1 
ATOM   1148 C C   . GLN A 1 150 ? -10.717 -9.789  17.496  1.00 33.64 ? 150  GLN A C   1 
ATOM   1149 O O   . GLN A 1 150 ? -10.059 -10.480 18.279  1.00 34.77 ? 150  GLN A O   1 
ATOM   1150 C CB  . GLN A 1 150 ? -10.797 -7.273  17.493  1.00 33.96 ? 150  GLN A CB  1 
ATOM   1151 C CG  . GLN A 1 150 ? -11.515 -5.990  17.913  1.00 33.08 ? 150  GLN A CG  1 
ATOM   1152 C CD  . GLN A 1 150 ? -10.592 -4.795  17.900  1.00 32.95 ? 150  GLN A CD  1 
ATOM   1153 O OE1 . GLN A 1 150 ? -9.474  -4.880  17.399  1.00 31.02 ? 150  GLN A OE1 1 
ATOM   1154 N NE2 . GLN A 1 150 ? -11.055 -3.668  18.437  1.00 29.61 ? 150  GLN A NE2 1 
ATOM   1155 N N   . ASP A 1 151 ? -10.866 -10.092 16.228  1.00 33.94 ? 151  ASP A N   1 
ATOM   1156 C CA  . ASP A 1 151 ? -10.185 -11.225 15.609  1.00 34.61 ? 151  ASP A CA  1 
ATOM   1157 C C   . ASP A 1 151 ? -9.921  -10.997 14.133  1.00 33.28 ? 151  ASP A C   1 
ATOM   1158 O O   . ASP A 1 151 ? -10.464 -10.086 13.528  1.00 31.74 ? 151  ASP A O   1 
ATOM   1159 C CB  . ASP A 1 151 ? -10.949 -12.533 15.810  1.00 35.70 ? 151  ASP A CB  1 
ATOM   1160 C CG  . ASP A 1 151 ? -12.326 -12.523 15.200  1.00 38.79 ? 151  ASP A CG  1 
ATOM   1161 O OD1 . ASP A 1 151 ? -13.253 -13.034 15.860  1.00 44.81 ? 151  ASP A OD1 1 
ATOM   1162 O OD2 . ASP A 1 151 ? -12.504 -12.031 14.065  1.00 45.61 ? 151  ASP A OD2 1 
ATOM   1163 N N   . ARG A 1 152 ? -9.082  -11.862 13.582  1.00 33.37 ? 152  ARG A N   1 
ATOM   1164 C CA  . ARG A 1 152 ? -8.530  -11.683 12.231  1.00 34.33 ? 152  ARG A CA  1 
ATOM   1165 C C   . ARG A 1 152 ? -9.620  -11.742 11.152  1.00 32.95 ? 152  ARG A C   1 
ATOM   1166 O O   . ARG A 1 152 ? -9.649  -10.904 10.253  1.00 31.80 ? 152  ARG A O   1 
ATOM   1167 C CB  . ARG A 1 152 ? -7.425  -12.715 11.960  1.00 34.92 ? 152  ARG A CB  1 
ATOM   1168 C CG  . ARG A 1 152 ? -6.847  -12.705 10.549  1.00 36.95 ? 152  ARG A CG  1 
ATOM   1169 C CD  . ARG A 1 152 ? -5.776  -13.804 10.405  1.00 39.42 ? 152  ARG A CD  1 
ATOM   1170 N NE  . ARG A 1 152 ? -4.610  -13.566 11.274  1.00 42.81 ? 152  ARG A NE  1 
ATOM   1171 C CZ  . ARG A 1 152 ? -3.602  -14.426 11.450  1.00 43.66 ? 152  ARG A CZ  1 
ATOM   1172 N NH1 . ARG A 1 152 ? -3.601  -15.594 10.823  1.00 44.39 ? 152  ARG A NH1 1 
ATOM   1173 N NH2 . ARG A 1 152 ? -2.599  -14.130 12.266  1.00 43.95 ? 152  ARG A NH2 1 
ATOM   1174 N N   . GLY A 1 153 ? -10.532 -12.697 11.293  1.00 32.84 ? 153  GLY A N   1 
ATOM   1175 C CA  . GLY A 1 153 ? -11.655 -12.884 10.344  1.00 33.08 ? 153  GLY A CA  1 
ATOM   1176 C C   . GLY A 1 153 ? -12.608 -11.700 10.271  1.00 33.00 ? 153  GLY A C   1 
ATOM   1177 O O   . GLY A 1 153 ? -12.860 -11.138 9.197   1.00 32.88 ? 153  GLY A O   1 
ATOM   1178 N N   . ASN A 1 154 ? -13.105 -11.278 11.425  1.00 31.72 ? 154  ASN A N   1 
ATOM   1179 C CA  . ASN A 1 154 ? -14.100 -10.195 11.457  1.00 31.05 ? 154  ASN A CA  1 
ATOM   1180 C C   . ASN A 1 154 ? -13.516 -8.816  11.080  1.00 30.57 ? 154  ASN A C   1 
ATOM   1181 O O   . ASN A 1 154 ? -14.177 -8.007  10.426  1.00 30.95 ? 154  ASN A O   1 
ATOM   1182 C CB  . ASN A 1 154 ? -14.799 -10.143 12.818  1.00 30.59 ? 154  ASN A CB  1 
ATOM   1183 C CG  . ASN A 1 154 ? -16.254 -9.764  12.708  1.00 31.19 ? 154  ASN A CG  1 
ATOM   1184 O OD1 . ASN A 1 154 ? -16.662 -9.017  11.814  1.00 34.61 ? 154  ASN A OD1 1 
ATOM   1185 N ND2 . ASN A 1 154 ? -17.041 -10.261 13.618  1.00 26.15 ? 154  ASN A ND2 1 
ATOM   1186 N N   . SER A 1 155 ? -12.274 -8.542  11.468  1.00 30.25 ? 155  SER A N   1 
ATOM   1187 C CA  . SER A 1 155 ? -11.662 -7.254  11.100  1.00 30.60 ? 155  SER A CA  1 
ATOM   1188 C C   . SER A 1 155 ? -11.453 -7.193  9.570   1.00 30.79 ? 155  SER A C   1 
ATOM   1189 O O   . SER A 1 155 ? -11.546 -6.139  8.967   1.00 31.49 ? 155  SER A O   1 
ATOM   1190 C CB  . SER A 1 155 ? -10.353 -6.972  11.857  1.00 29.91 ? 155  SER A CB  1 
ATOM   1191 O OG  . SER A 1 155 ? -9.352  -7.953  11.631  1.00 31.64 ? 155  SER A OG  1 
ATOM   1192 N N   . LYS A 1 156 ? -11.213 -8.342  8.966   1.00 30.82 ? 156  LYS A N   1 
ATOM   1193 C CA  . LYS A 1 156 ? -10.999 -8.430  7.523   1.00 32.04 ? 156  LYS A CA  1 
ATOM   1194 C C   . LYS A 1 156 ? -12.316 -8.202  6.763   1.00 32.46 ? 156  LYS A C   1 
ATOM   1195 O O   . LYS A 1 156 ? -12.342 -7.511  5.752   1.00 32.30 ? 156  LYS A O   1 
ATOM   1196 C CB  . LYS A 1 156 ? -10.379 -9.762  7.162   1.00 30.99 ? 156  LYS A CB  1 
ATOM   1197 C CG  . LYS A 1 156 ? -10.162 -9.991  5.671   1.00 35.09 ? 156  LYS A CG  1 
ATOM   1198 C CD  . LYS A 1 156 ? -9.677  -11.413 5.439   1.00 33.79 ? 156  LYS A CD  1 
ATOM   1199 C CE  . LYS A 1 156 ? -9.108  -11.588 4.077   1.00 35.97 ? 156  LYS A CE  1 
ATOM   1200 N NZ  . LYS A 1 156 ? -8.631  -12.984 3.929   1.00 32.99 ? 156  LYS A NZ  1 
ATOM   1201 N N   . ILE A 1 157 ? -13.414 -8.743  7.281   1.00 33.40 ? 157  ILE A N   1 
ATOM   1202 C CA  . ILE A 1 157 ? -14.733 -8.519  6.663   1.00 33.49 ? 157  ILE A CA  1 
ATOM   1203 C C   . ILE A 1 157 ? -15.033 -7.043  6.779   1.00 33.76 ? 157  ILE A C   1 
ATOM   1204 O O   . ILE A 1 157 ? -15.480 -6.421  5.821   1.00 33.72 ? 157  ILE A O   1 
ATOM   1205 C CB  . ILE A 1 157 ? -15.843 -9.385  7.309   1.00 34.09 ? 157  ILE A CB  1 
ATOM   1206 C CG1 . ILE A 1 157 ? -15.683 -10.821 6.841   1.00 34.72 ? 157  ILE A CG1 1 
ATOM   1207 C CG2 . ILE A 1 157 ? -17.256 -8.893  6.925   1.00 35.07 ? 157  ILE A CG2 1 
ATOM   1208 C CD1 . ILE A 1 157 ? -15.975 -11.002 5.334   1.00 34.54 ? 157  ILE A CD1 1 
ATOM   1209 N N   . ALA A 1 158 ? -14.708 -6.473  7.943   1.00 33.40 ? 158  ALA A N   1 
ATOM   1210 C CA  . ALA A 1 158 ? -14.855 -5.027  8.178   1.00 32.76 ? 158  ALA A CA  1 
ATOM   1211 C C   . ALA A 1 158 ? -13.995 -4.168  7.224   1.00 32.59 ? 158  ALA A C   1 
ATOM   1212 O O   . ALA A 1 158 ? -14.462 -3.148  6.713   1.00 34.48 ? 158  ALA A O   1 
ATOM   1213 C CB  . ALA A 1 158 ? -14.547 -4.672  9.666   1.00 32.42 ? 158  ALA A CB  1 
ATOM   1214 N N   . ALA A 1 159 ? -12.749 -4.571  6.991   1.00 30.60 ? 159  ALA A N   1 
ATOM   1215 C CA  . ALA A 1 159 ? -11.885 -3.876  6.030   1.00 30.73 ? 159  ALA A CA  1 
ATOM   1216 C C   . ALA A 1 159 ? -12.461 -3.969  4.593   1.00 28.83 ? 159  ALA A C   1 
ATOM   1217 O O   . ALA A 1 159 ? -12.514 -3.000  3.884   1.00 26.86 ? 159  ALA A O   1 
ATOM   1218 C CB  . ALA A 1 159 ? -10.419 -4.449  6.062   1.00 29.73 ? 159  ALA A CB  1 
ATOM   1219 N N   . LEU A 1 160 ? -12.878 -5.161  4.203   1.00 29.99 ? 160  LEU A N   1 
ATOM   1220 C CA  . LEU A 1 160 ? -13.449 -5.427  2.860   1.00 30.78 ? 160  LEU A CA  1 
ATOM   1221 C C   . LEU A 1 160 ? -14.760 -4.673  2.620   1.00 30.96 ? 160  LEU A C   1 
ATOM   1222 O O   . LEU A 1 160 ? -15.017 -4.183  1.525   1.00 30.76 ? 160  LEU A O   1 
ATOM   1223 C CB  . LEU A 1 160 ? -13.661 -6.916  2.651   1.00 30.82 ? 160  LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 160 ? -12.356 -7.712  2.475   1.00 32.08 ? 160  LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 160 ? -12.654 -9.196  2.347   1.00 30.91 ? 160  LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 160 ? -11.566 -7.211  1.264   1.00 32.23 ? 160  LEU A CD2 1 
ATOM   1227 N N   . THR A 1 161 ? -15.542 -4.528  3.681   1.00 31.12 ? 161  THR A N   1 
ATOM   1228 C CA  . THR A 1 161 ? -16.830 -3.845  3.608   1.00 30.40 ? 161  THR A CA  1 
ATOM   1229 C C   . THR A 1 161 ? -16.588 -2.357  3.370   1.00 31.27 ? 161  THR A C   1 
ATOM   1230 O O   . THR A 1 161 ? -17.279 -1.723  2.539   1.00 29.62 ? 161  THR A O   1 
ATOM   1231 C CB  . THR A 1 161 ? -17.656 -4.104  4.884   1.00 30.37 ? 161  THR A CB  1 
ATOM   1232 O OG1 . THR A 1 161 ? -17.970 -5.501  4.944   1.00 30.17 ? 161  THR A OG1 1 
ATOM   1233 C CG2 . THR A 1 161 ? -18.953 -3.259  4.926   1.00 28.43 ? 161  THR A CG2 1 
ATOM   1234 N N   . PHE A 1 162 ? -15.590 -1.811  4.071   1.00 31.11 ? 162  PHE A N   1 
ATOM   1235 C CA  . PHE A 1 162 ? -15.193 -0.405  3.863   1.00 32.29 ? 162  PHE A CA  1 
ATOM   1236 C C   . PHE A 1 162 ? -14.601 -0.191  2.449   1.00 32.19 ? 162  PHE A C   1 
ATOM   1237 O O   . PHE A 1 162 ? -14.973 0.745   1.745   1.00 32.33 ? 162  PHE A O   1 
ATOM   1238 C CB  . PHE A 1 162 ? -14.196 0.091   4.917   1.00 32.98 ? 162  PHE A CB  1 
ATOM   1239 C CG  . PHE A 1 162 ? -13.936 1.569   4.842   1.00 33.52 ? 162  PHE A CG  1 
ATOM   1240 C CD1 . PHE A 1 162 ? -14.915 2.468   5.199   1.00 39.02 ? 162  PHE A CD1 1 
ATOM   1241 C CD2 . PHE A 1 162 ? -12.735 2.058   4.366   1.00 38.05 ? 162  PHE A CD2 1 
ATOM   1242 C CE1 . PHE A 1 162 ? -14.683 3.845   5.112   1.00 39.46 ? 162  PHE A CE1 1 
ATOM   1243 C CE2 . PHE A 1 162 ? -12.484 3.429   4.286   1.00 35.78 ? 162  PHE A CE2 1 
ATOM   1244 C CZ  . PHE A 1 162 ? -13.453 4.315   4.661   1.00 39.09 ? 162  PHE A CZ  1 
ATOM   1245 N N   . ALA A 1 163 ? -13.717 -1.086  2.034   1.00 31.31 ? 163  ALA A N   1 
ATOM   1246 C CA  . ALA A 1 163 ? -13.145 -1.027  0.671   1.00 31.60 ? 163  ALA A CA  1 
ATOM   1247 C C   . ALA A 1 163 ? -14.254 -1.036  -0.419  1.00 31.41 ? 163  ALA A C   1 
ATOM   1248 O O   . ALA A 1 163 ? -14.199 -0.266  -1.366  1.00 30.44 ? 163  ALA A O   1 
ATOM   1249 C CB  . ALA A 1 163 ? -12.152 -2.169  0.441   1.00 29.26 ? 163  ALA A CB  1 
ATOM   1250 N N   . LYS A 1 164 ? -15.248 -1.899  -0.258  1.00 31.52 ? 164  LYS A N   1 
ATOM   1251 C CA  . LYS A 1 164 ? -16.376 -1.977  -1.196  1.00 32.45 ? 164  LYS A CA  1 
ATOM   1252 C C   . LYS A 1 164 ? -17.125 -0.641  -1.286  1.00 32.02 ? 164  LYS A C   1 
ATOM   1253 O O   . LYS A 1 164 ? -17.509 -0.231  -2.368  1.00 33.53 ? 164  LYS A O   1 
ATOM   1254 C CB  . LYS A 1 164 ? -17.329 -3.097  -0.791  1.00 32.97 ? 164  LYS A CB  1 
ATOM   1255 C CG  . LYS A 1 164 ? -18.503 -3.329  -1.724  1.00 35.73 ? 164  LYS A CG  1 
ATOM   1256 C CD  . LYS A 1 164 ? -19.632 -3.990  -0.954  1.00 37.47 ? 164  LYS A CD  1 
ATOM   1257 C CE  . LYS A 1 164 ? -20.693 -4.552  -1.874  1.00 38.62 ? 164  LYS A CE  1 
ATOM   1258 N NZ  . LYS A 1 164 ? -20.731 -3.764  -3.127  1.00 40.89 ? 164  LYS A NZ  1 
ATOM   1259 N N   . GLU A 1 165 ? -17.279 0.062   -0.169  1.00 31.32 ? 165  GLU A N   1 
ATOM   1260 C CA  . GLU A 1 165 ? -17.990 1.347   -0.175  1.00 30.93 ? 165  GLU A CA  1 
ATOM   1261 C C   . GLU A 1 165 ? -17.217 2.355   -1.011  1.00 30.37 ? 165  GLU A C   1 
ATOM   1262 O O   . GLU A 1 165 ? -17.792 3.151   -1.752  1.00 29.52 ? 165  GLU A O   1 
ATOM   1263 C CB  . GLU A 1 165 ? -18.128 1.948   1.224   1.00 31.22 ? 165  GLU A CB  1 
ATOM   1264 C CG  . GLU A 1 165 ? -18.797 1.099   2.255   1.00 33.29 ? 165  GLU A CG  1 
ATOM   1265 C CD  . GLU A 1 165 ? -18.719 1.736   3.639   1.00 34.63 ? 165  GLU A CD  1 
ATOM   1266 O OE1 . GLU A 1 165 ? -18.637 2.984   3.727   1.00 36.52 ? 165  GLU A OE1 1 
ATOM   1267 O OE2 . GLU A 1 165 ? -18.733 0.988   4.637   1.00 35.65 ? 165  GLU A OE2 1 
ATOM   1268 N N   . LEU A 1 166 ? -15.899 2.329   -0.842  1.00 29.91 ? 166  LEU A N   1 
ATOM   1269 C CA  . LEU A 1 166 ? -15.000 3.211   -1.576  1.00 29.28 ? 166  LEU A CA  1 
ATOM   1270 C C   . LEU A 1 166 ? -15.015 2.868   -3.075  1.00 28.75 ? 166  LEU A C   1 
ATOM   1271 O O   . LEU A 1 166 ? -14.994 3.761   -3.918  1.00 28.47 ? 166  LEU A O   1 
ATOM   1272 C CB  . LEU A 1 166 ? -13.575 3.099   -1.035  1.00 29.10 ? 166  LEU A CB  1 
ATOM   1273 C CG  . LEU A 1 166 ? -13.367 3.519   0.422   1.00 29.65 ? 166  LEU A CG  1 
ATOM   1274 C CD1 . LEU A 1 166 ? -11.946 3.147   0.897   1.00 29.45 ? 166  LEU A CD1 1 
ATOM   1275 C CD2 . LEU A 1 166 ? -13.657 5.003   0.593   1.00 25.95 ? 166  LEU A CD2 1 
ATOM   1276 N N   . ALA A 1 167 ? -15.041 1.578   -3.387  1.00 28.28 ? 167  ALA A N   1 
ATOM   1277 C CA  . ALA A 1 167 ? -15.018 1.107   -4.782  1.00 29.87 ? 167  ALA A CA  1 
ATOM   1278 C C   . ALA A 1 167 ? -16.344 1.397   -5.495  1.00 30.97 ? 167  ALA A C   1 
ATOM   1279 O O   . ALA A 1 167 ? -16.397 1.520   -6.715  1.00 31.42 ? 167  ALA A O   1 
ATOM   1280 C CB  . ALA A 1 167 ? -14.714 -0.376  -4.854  1.00 29.01 ? 167  ALA A CB  1 
ATOM   1281 N N   . GLU A 1 168 ? -17.410 1.521   -4.723  1.00 32.07 ? 168  GLU A N   1 
ATOM   1282 C CA  . GLU A 1 168 ? -18.718 1.772   -5.312  1.00 33.23 ? 168  GLU A CA  1 
ATOM   1283 C C   . GLU A 1 168 ? -18.932 3.226   -5.675  1.00 33.77 ? 168  GLU A C   1 
ATOM   1284 O O   . GLU A 1 168 ? -19.496 3.530   -6.723  1.00 34.37 ? 168  GLU A O   1 
ATOM   1285 C CB  . GLU A 1 168 ? -19.829 1.345   -4.379  1.00 33.78 ? 168  GLU A CB  1 
ATOM   1286 C CG  . GLU A 1 168 ? -20.291 -0.064  -4.600  1.00 35.00 ? 168  GLU A CG  1 
ATOM   1287 C CD  . GLU A 1 168 ? -21.191 -0.505  -3.482  1.00 36.65 ? 168  GLU A CD  1 
ATOM   1288 O OE1 . GLU A 1 168 ? -21.099 0.130   -2.403  1.00 37.75 ? 168  GLU A OE1 1 
ATOM   1289 O OE2 . GLU A 1 168 ? -21.976 -1.463  -3.676  1.00 37.48 ? 168  GLU A OE2 1 
ATOM   1290 N N   . SER A 1 169 ? -18.493 4.126   -4.805  1.00 34.08 ? 169  SER A N   1 
ATOM   1291 C CA  . SER A 1 169 ? -18.773 5.543   -4.994  1.00 34.38 ? 169  SER A CA  1 
ATOM   1292 C C   . SER A 1 169 ? -17.681 6.123   -5.856  1.00 34.81 ? 169  SER A C   1 
ATOM   1293 O O   . SER A 1 169 ? -17.792 7.219   -6.393  1.00 35.53 ? 169  SER A O   1 
ATOM   1294 C CB  . SER A 1 169 ? -18.872 6.275   -3.656  1.00 34.24 ? 169  SER A CB  1 
ATOM   1295 O OG  . SER A 1 169 ? -17.616 6.343   -3.027  1.00 33.39 ? 169  SER A OG  1 
ATOM   1296 N N   . SER A 1 170 ? -16.617 5.358   -5.980  1.00 35.17 ? 170  SER A N   1 
ATOM   1297 C CA  . SER A 1 170 ? -15.542 5.696   -6.892  1.00 35.91 ? 170  SER A CA  1 
ATOM   1298 C C   . SER A 1 170 ? -16.040 5.484   -8.318  1.00 36.52 ? 170  SER A C   1 
ATOM   1299 O O   . SER A 1 170 ? -15.418 5.903   -9.289  1.00 37.01 ? 170  SER A O   1 
ATOM   1300 C CB  . SER A 1 170 ? -14.308 4.829   -6.630  1.00 35.82 ? 170  SER A CB  1 
ATOM   1301 O OG  . SER A 1 170 ? -13.627 4.563   -7.838  1.00 36.08 ? 170  SER A OG  1 
ATOM   1302 N N   . GLN A 1 171 ? -17.192 4.853   -8.440  1.00 37.41 ? 171  GLN A N   1 
ATOM   1303 C CA  . GLN A 1 171 ? -17.722 4.557   -9.766  1.00 38.28 ? 171  GLN A CA  1 
ATOM   1304 C C   . GLN A 1 171 ? -18.926 5.428   -10.129 1.00 38.34 ? 171  GLN A C   1 
ATOM   1305 O O   . GLN A 1 171 ? -19.426 5.364   -11.247 1.00 38.16 ? 171  GLN A O   1 
ATOM   1306 C CB  . GLN A 1 171 ? -17.946 3.067   -9.937  1.00 38.33 ? 171  GLN A CB  1 
ATOM   1307 C CG  . GLN A 1 171 ? -16.610 2.429   -10.235 1.00 39.28 ? 171  GLN A CG  1 
ATOM   1308 C CD  . GLN A 1 171 ? -16.583 0.946   -10.007 1.00 40.68 ? 171  GLN A CD  1 
ATOM   1309 O OE1 . GLN A 1 171 ? -17.498 0.228   -10.405 1.00 42.32 ? 171  GLN A OE1 1 
ATOM   1310 N NE2 . GLN A 1 171 ? -15.524 0.469   -9.363  1.00 42.32 ? 171  GLN A NE2 1 
ATOM   1311 N N   . LEU A 1 172 ? -19.359 6.249   -9.172  1.00 38.41 ? 172  LEU A N   1 
ATOM   1312 C CA  . LEU A 1 172 ? -20.013 7.513   -9.507  1.00 38.28 ? 172  LEU A CA  1 
ATOM   1313 C C   . LEU A 1 172 ? -18.826 8.442   -9.689  1.00 38.66 ? 172  LEU A C   1 
ATOM   1314 O O   . LEU A 1 172 ? -18.089 8.695   -8.741  1.00 38.56 ? 172  LEU A O   1 
ATOM   1315 C CB  . LEU A 1 172 ? -20.935 8.041   -8.396  1.00 38.00 ? 172  LEU A CB  1 
ATOM   1316 C CG  . LEU A 1 172 ? -21.428 7.094   -7.308  1.00 37.00 ? 172  LEU A CG  1 
ATOM   1317 C CD1 . LEU A 1 172 ? -22.615 7.714   -6.593  1.00 35.50 ? 172  LEU A CD1 1 
ATOM   1318 C CD2 . LEU A 1 172 ? -21.781 5.734   -7.902  1.00 37.16 ? 172  LEU A CD2 1 
ATOM   1319 N N   . GLN A 1 173 ? -18.592 8.892   -10.917 1.00 39.22 ? 173  GLN A N   1 
ATOM   1320 C CA  . GLN A 1 173 ? -17.382 9.678   -11.208 1.00 39.21 ? 173  GLN A CA  1 
ATOM   1321 C C   . GLN A 1 173 ? -17.723 10.930  -11.992 1.00 39.15 ? 173  GLN A C   1 
ATOM   1322 O O   . GLN A 1 173 ? -16.856 11.620  -12.542 1.00 39.60 ? 173  GLN A O   1 
ATOM   1323 C CB  . GLN A 1 173 ? -16.330 8.833   -11.937 1.00 39.35 ? 173  GLN A CB  1 
ATOM   1324 C CG  . GLN A 1 173 ? -16.811 8.065   -13.177 1.00 39.77 ? 173  GLN A CG  1 
ATOM   1325 C CD  . GLN A 1 173 ? -15.811 6.992   -13.611 1.00 39.64 ? 173  GLN A CD  1 
ATOM   1326 O OE1 . GLN A 1 173 ? -15.137 6.387   -12.778 1.00 38.23 ? 173  GLN A OE1 1 
ATOM   1327 N NE2 . GLN A 1 173 ? -15.717 6.755   -14.915 1.00 39.54 ? 173  GLN A NE2 1 
ATOM   1328 N N   . HIS A 1 174 ? -19.015 11.215  -11.993 1.00 38.80 ? 174  HIS A N   1 
ATOM   1329 C CA  . HIS A 1 174 ? -19.601 12.332  -12.723 1.00 38.06 ? 174  HIS A CA  1 
ATOM   1330 C C   . HIS A 1 174 ? -19.938 13.425  -11.732 1.00 37.82 ? 174  HIS A C   1 
ATOM   1331 O O   . HIS A 1 174 ? -20.592 13.160  -10.723 1.00 37.34 ? 174  HIS A O   1 
ATOM   1332 C CB  . HIS A 1 174 ? -20.890 11.890  -13.416 1.00 37.96 ? 174  HIS A CB  1 
ATOM   1333 C CG  . HIS A 1 174 ? -21.861 11.219  -12.494 1.00 37.05 ? 174  HIS A CG  1 
ATOM   1334 N ND1 . HIS A 1 174 ? -21.942 11.529  -11.153 1.00 35.44 ? 174  HIS A ND1 1 
ATOM   1335 C CD2 . HIS A 1 174 ? -22.779 10.247  -12.711 1.00 37.46 ? 174  HIS A CD2 1 
ATOM   1336 C CE1 . HIS A 1 174 ? -22.867 10.776  -10.585 1.00 36.56 ? 174  HIS A CE1 1 
ATOM   1337 N NE2 . HIS A 1 174 ? -23.393 9.992   -11.508 1.00 36.94 ? 174  HIS A NE2 1 
HETATM 1338 O O   . HOH B 2 .   ? -13.654 17.338  1.584   1.00 35.03 ? 2001 HOH A O   1 
HETATM 1339 O O   . HOH B 2 .   ? -5.723  11.712  10.281  1.00 23.33 ? 2002 HOH A O   1 
HETATM 1340 O O   . HOH B 2 .   ? -16.542 5.429   16.016  1.00 35.25 ? 2003 HOH A O   1 
HETATM 1341 O O   . HOH B 2 .   ? -21.352 5.493   11.766  1.00 33.82 ? 2004 HOH A O   1 
HETATM 1342 O O   . HOH B 2 .   ? -20.454 8.650   7.655   1.00 55.34 ? 2005 HOH A O   1 
HETATM 1343 O O   . HOH B 2 .   ? -12.751 -8.011  14.849  1.00 24.41 ? 2006 HOH A O   1 
HETATM 1344 O O   . HOH B 2 .   ? -6.318  1.740   19.086  1.00 31.56 ? 2007 HOH A O   1 
HETATM 1345 O O   . HOH B 2 .   ? 3.356   1.326   -5.265  1.00 38.37 ? 2008 HOH A O   1 
HETATM 1346 O O   . HOH B 2 .   ? -4.688  1.314   -4.992  1.00 39.34 ? 2009 HOH A O   1 
HETATM 1347 O O   . HOH B 2 .   ? -1.858  8.219   -4.570  1.00 41.43 ? 2010 HOH A O   1 
HETATM 1348 O O   . HOH B 2 .   ? 3.614   3.112   6.381   1.00 36.57 ? 2011 HOH A O   1 
HETATM 1349 O O   . HOH B 2 .   ? 0.937   8.604   1.754   1.00 42.10 ? 2012 HOH A O   1 
HETATM 1350 O O   . HOH B 2 .   ? -8.915  8.463   16.599  1.00 34.00 ? 2013 HOH A O   1 
HETATM 1351 O O   . HOH B 2 .   ? 11.625  -6.868  16.200  1.00 62.20 ? 2014 HOH A O   1 
HETATM 1352 O O   . HOH B 2 .   ? -11.970 7.288   18.722  1.00 45.16 ? 2015 HOH A O   1 
HETATM 1353 O O   . HOH B 2 .   ? -3.008  -18.373 5.775   1.00 44.63 ? 2016 HOH A O   1 
HETATM 1354 O O   . HOH B 2 .   ? -3.010  -14.599 -7.994  1.00 37.76 ? 2017 HOH A O   1 
HETATM 1355 O O   . HOH B 2 .   ? -5.677  15.080  28.950  1.00 43.21 ? 2018 HOH A O   1 
HETATM 1356 O O   . HOH B 2 .   ? 0.455   11.257  24.364  1.00 25.58 ? 2019 HOH A O   1 
HETATM 1357 O O   . HOH B 2 .   ? -4.323  10.695  18.961  1.00 30.01 ? 2020 HOH A O   1 
HETATM 1358 O O   . HOH B 2 .   ? 3.516   9.378   20.860  1.00 40.30 ? 2021 HOH A O   1 
HETATM 1359 O O   . HOH B 2 .   ? -0.009  7.472   23.111  1.00 38.29 ? 2022 HOH A O   1 
HETATM 1360 O O   . HOH B 2 .   ? -4.559  14.285  12.849  1.00 38.97 ? 2023 HOH A O   1 
HETATM 1361 O O   . HOH B 2 .   ? 5.406   4.603   17.319  1.00 44.30 ? 2024 HOH A O   1 
HETATM 1362 O O   . HOH B 2 .   ? 1.187   -0.434  14.624  1.00 29.18 ? 2025 HOH A O   1 
HETATM 1363 O O   . HOH B 2 .   ? 3.159   5.254   7.921   1.00 29.23 ? 2026 HOH A O   1 
HETATM 1364 O O   . HOH B 2 .   ? 3.960   9.156   15.087  1.00 43.74 ? 2027 HOH A O   1 
HETATM 1365 O O   . HOH B 2 .   ? 5.827   5.413   8.792   1.00 33.12 ? 2028 HOH A O   1 
HETATM 1366 O O   . HOH B 2 .   ? 9.664   4.758   8.233   1.00 26.43 ? 2029 HOH A O   1 
HETATM 1367 O O   . HOH B 2 .   ? 8.746   9.245   13.932  1.00 36.15 ? 2030 HOH A O   1 
HETATM 1368 O O   . HOH B 2 .   ? 11.415  8.607   7.077   1.00 42.38 ? 2031 HOH A O   1 
HETATM 1369 O O   . HOH B 2 .   ? -18.010 -4.088  8.610   1.00 56.84 ? 2032 HOH A O   1 
HETATM 1370 O O   . HOH B 2 .   ? 17.849  4.707   14.271  1.00 29.13 ? 2033 HOH A O   1 
HETATM 1371 O O   . HOH B 2 .   ? 15.795  -6.996  14.441  1.00 40.03 ? 2034 HOH A O   1 
HETATM 1372 O O   . HOH B 2 .   ? 17.237  -3.031  17.061  1.00 29.75 ? 2035 HOH A O   1 
HETATM 1373 O O   . HOH B 2 .   ? 25.837  -15.030 8.137   1.00 32.35 ? 2036 HOH A O   1 
HETATM 1374 O O   . HOH B 2 .   ? 29.849  -13.343 10.492  1.00 28.58 ? 2037 HOH A O   1 
HETATM 1375 O O   . HOH B 2 .   ? 19.582  -2.607  5.228   1.00 44.64 ? 2038 HOH A O   1 
HETATM 1376 O O   . HOH B 2 .   ? 8.166   5.132   2.015   1.00 33.26 ? 2039 HOH A O   1 
HETATM 1377 O O   . HOH B 2 .   ? 4.199   0.425   6.952   1.00 37.14 ? 2040 HOH A O   1 
HETATM 1378 O O   . HOH B 2 .   ? 7.601   5.547   6.507   1.00 31.31 ? 2041 HOH A O   1 
HETATM 1379 O O   . HOH B 2 .   ? 9.333   -1.568  -1.268  1.00 24.92 ? 2042 HOH A O   1 
HETATM 1380 O O   . HOH B 2 .   ? 5.669   -5.109  -9.131  1.00 38.26 ? 2043 HOH A O   1 
HETATM 1381 O O   . HOH B 2 .   ? 8.298   -2.498  -3.758  1.00 34.32 ? 2044 HOH A O   1 
HETATM 1382 O O   . HOH B 2 .   ? 4.378   -11.831 -6.518  1.00 34.84 ? 2045 HOH A O   1 
HETATM 1383 O O   . HOH B 2 .   ? 8.441   -10.634 -6.747  1.00 38.17 ? 2046 HOH A O   1 
HETATM 1384 O O   . HOH B 2 .   ? 2.960   -13.734 -2.441  1.00 34.65 ? 2047 HOH A O   1 
HETATM 1385 O O   . HOH B 2 .   ? 11.110  -10.283 -7.058  1.00 35.09 ? 2048 HOH A O   1 
HETATM 1386 O O   . HOH B 2 .   ? 15.493  -10.741 4.084   1.00 28.67 ? 2049 HOH A O   1 
HETATM 1387 O O   . HOH B 2 .   ? 13.658  -7.146  10.315  1.00 40.55 ? 2050 HOH A O   1 
HETATM 1388 O O   . HOH B 2 .   ? 10.265  -6.007  4.363   1.00 41.02 ? 2051 HOH A O   1 
HETATM 1389 O O   . HOH B 2 .   ? 11.269  -4.076  2.876   1.00 50.61 ? 2052 HOH A O   1 
HETATM 1390 O O   . HOH B 2 .   ? 2.518   -0.139  16.738  1.00 40.24 ? 2053 HOH A O   1 
HETATM 1391 O O   . HOH B 2 .   ? 8.214   -5.055  16.948  1.00 44.54 ? 2054 HOH A O   1 
HETATM 1392 O O   . HOH B 2 .   ? 13.654  -7.961  12.632  1.00 49.29 ? 2055 HOH A O   1 
HETATM 1393 O O   . HOH B 2 .   ? 2.462   -14.780 13.122  1.00 39.70 ? 2056 HOH A O   1 
HETATM 1394 O O   . HOH B 2 .   ? -0.450  -18.208 5.095   1.00 44.18 ? 2057 HOH A O   1 
HETATM 1395 O O   . HOH B 2 .   ? -3.381  -14.407 -4.552  1.00 41.68 ? 2058 HOH A O   1 
HETATM 1396 O O   . HOH B 2 .   ? 1.977   -12.544 -4.315  1.00 53.72 ? 2059 HOH A O   1 
HETATM 1397 O O   . HOH B 2 .   ? -8.505  -6.467  -7.643  1.00 44.24 ? 2060 HOH A O   1 
HETATM 1398 O O   . HOH B 2 .   ? -20.767 -5.231  2.656   1.00 65.74 ? 2061 HOH A O   1 
HETATM 1399 O O   . HOH B 2 .   ? -13.532 -4.896  -9.018  1.00 32.19 ? 2062 HOH A O   1 
HETATM 1400 O O   . HOH B 2 .   ? -5.070  -11.855 2.983   1.00 39.55 ? 2063 HOH A O   1 
HETATM 1401 O O   . HOH B 2 .   ? -1.217  -13.145 16.158  1.00 29.07 ? 2064 HOH A O   1 
HETATM 1402 O O   . HOH B 2 .   ? 4.092   -8.447  18.479  1.00 45.88 ? 2065 HOH A O   1 
HETATM 1403 O O   . HOH B 2 .   ? -2.289  -4.574  15.084  1.00 51.91 ? 2066 HOH A O   1 
HETATM 1404 O O   . HOH B 2 .   ? 1.922   -1.055  -3.881  1.00 48.33 ? 2067 HOH A O   1 
HETATM 1405 O O   . HOH B 2 .   ? -7.583  -3.721  -4.370  1.00 46.12 ? 2068 HOH A O   1 
HETATM 1406 O O   . HOH B 2 .   ? -3.535  -4.670  17.592  1.00 41.31 ? 2069 HOH A O   1 
HETATM 1407 O O   . HOH B 2 .   ? -3.537  -7.071  22.049  1.00 49.31 ? 2070 HOH A O   1 
HETATM 1408 O O   . HOH B 2 .   ? -7.798  -13.450 15.575  1.00 27.93 ? 2071 HOH A O   1 
HETATM 1409 O O   . HOH B 2 .   ? -8.551  -5.288  26.047  1.00 37.36 ? 2072 HOH A O   1 
HETATM 1410 O O   . HOH B 2 .   ? -8.616  -0.047  26.495  1.00 2.00  ? 2073 HOH A O   1 
HETATM 1411 O O   . HOH B 2 .   ? -9.591  -13.427 18.565  1.00 49.40 ? 2074 HOH A O   1 
HETATM 1412 O O   . HOH B 2 .   ? -10.370 -11.521 20.581  1.00 40.62 ? 2075 HOH A O   1 
HETATM 1413 O O   . HOH B 2 .   ? -10.641 -15.302 12.846  1.00 35.32 ? 2076 HOH A O   1 
HETATM 1414 O O   . HOH B 2 .   ? -12.782 -12.712 6.948   1.00 39.02 ? 2077 HOH A O   1 
HETATM 1415 O O   . HOH B 2 .   ? -17.492 -11.583 15.577  1.00 47.07 ? 2078 HOH A O   1 
HETATM 1416 O O   . HOH B 2 .   ? -16.600 -2.070  7.716   1.00 24.46 ? 2079 HOH A O   1 
HETATM 1417 O O   . HOH B 2 .   ? -19.813 -2.332  1.965   1.00 39.75 ? 2080 HOH A O   1 
HETATM 1418 O O   . HOH B 2 .   ? -18.029 0.004   6.672   1.00 34.86 ? 2081 HOH A O   1 
HETATM 1419 O O   . HOH B 2 .   ? -20.440 8.552   -13.731 1.00 30.15 ? 2082 HOH A O   1 
HETATM 1420 O O   . HOH B 2 .   ? -17.112 4.185   -13.271 1.00 28.21 ? 2083 HOH A O   1 
# 
