data_9FEN
# 
_entry.id   9FEN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FEN         pdb_00009fen 10.2210/pdb9fen/pdb 
WWPDB D_1292132729 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FEN 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              brynda@uochb.cas.cz 
_pdbx_contact_author.name_first         Jiri 
_pdbx_contact_author.name_last          Brynda 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3675-6769 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Myskova, J.' 1 ? 
'Brynda, J.'  2 ? 
'Lazar, J.'   3 ? 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? ? ? ? primary 'To Be Published' ? 0353 ? ? ? ? ? ? ? 'Directionality of Optical Properties of Fluorescent Proteins' 
? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? 1       'To Be Published' ? 0353 ? ? ? ? ? ? ? 'Directional optical properties of fluorescent proteins'       
? ? ? ? ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Myskova, J.'   1 ? 
primary 'Brynda, J.'    2 ? 
primary 'Khoroshyy, P.' 3 ? 
primary 'Lazar, J.'     4 ? 
1       'Myskova, J.'   5 ? 
1       'Lazar, J.'     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 'nowGFP crystallized in Space Group C2' 27881.439 1   ? ? ? ? 
2 water   nat water                                   18.015    218 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MVSKGEKLFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKMSLKFICTTGKLPVPWPTLKTTLTWG(CRF)MQCFARY
PDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGVDFKEDGNILGHKLEYNAISGNANITA
DKQKNGIKAYFTIRHDVEDGSVLLADHYQQNTPIGDGPVLLPDNHYLSTQSKQSKDPNEKRDHMVLLEFVTAAGIPLGAD
ELYKHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVSKGEKLFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKMSLKFICTTGKLPVPWPTLKTTLTWGTWGMQCFARYPD
HMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGVDFKEDGNILGHKLEYNAISGNANITADK
QKNGIKAYFTIRHDVEDGSVLLADHYQQNTPIGDGPVLLPDNHYLSTQSKQSKDPNEKRDHMVLLEFVTAAGIPLGADEL
YKHHHHHH
;
_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   VAL n 
1 3   SER n 
1 4   LYS n 
1 5   GLY n 
1 6   GLU n 
1 7   LYS n 
1 8   LEU n 
1 9   PHE n 
1 10  THR n 
1 11  GLY n 
1 12  VAL n 
1 13  VAL n 
1 14  PRO n 
1 15  ILE n 
1 16  LEU n 
1 17  VAL n 
1 18  GLU n 
1 19  LEU n 
1 20  ASP n 
1 21  GLY n 
1 22  ASP n 
1 23  VAL n 
1 24  ASN n 
1 25  GLY n 
1 26  HIS n 
1 27  LYS n 
1 28  PHE n 
1 29  SER n 
1 30  VAL n 
1 31  SER n 
1 32  GLY n 
1 33  GLU n 
1 34  GLY n 
1 35  GLU n 
1 36  GLY n 
1 37  ASP n 
1 38  ALA n 
1 39  THR n 
1 40  TYR n 
1 41  GLY n 
1 42  LYS n 
1 43  MET n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  PHE n 
1 48  ILE n 
1 49  CYS n 
1 50  THR n 
1 51  THR n 
1 52  GLY n 
1 53  LYS n 
1 54  LEU n 
1 55  PRO n 
1 56  VAL n 
1 57  PRO n 
1 58  TRP n 
1 59  PRO n 
1 60  THR n 
1 61  LEU n 
1 62  LYS n 
1 63  THR n 
1 64  THR n 
1 65  LEU n 
1 66  THR n 
1 67  TRP n 
1 68  GLY n 
1 69  CRF n 
1 70  MET n 
1 71  GLN n 
1 72  CYS n 
1 73  PHE n 
1 74  ALA n 
1 75  ARG n 
1 76  TYR n 
1 77  PRO n 
1 78  ASP n 
1 79  HIS n 
1 80  MET n 
1 81  LYS n 
1 82  GLN n 
1 83  HIS n 
1 84  ASP n 
1 85  PHE n 
1 86  PHE n 
1 87  LYS n 
1 88  SER n 
1 89  ALA n 
1 90  MET n 
1 91  PRO n 
1 92  GLU n 
1 93  GLY n 
1 94  TYR n 
1 95  VAL n 
1 96  GLN n 
1 97  GLU n 
1 98  ARG n 
1 99  THR n 
1 100 ILE n 
1 101 PHE n 
1 102 PHE n 
1 103 LYS n 
1 104 ASP n 
1 105 ASP n 
1 106 GLY n 
1 107 ASN n 
1 108 TYR n 
1 109 LYS n 
1 110 THR n 
1 111 ARG n 
1 112 ALA n 
1 113 GLU n 
1 114 VAL n 
1 115 LYS n 
1 116 PHE n 
1 117 GLU n 
1 118 GLY n 
1 119 ASP n 
1 120 THR n 
1 121 LEU n 
1 122 VAL n 
1 123 ASN n 
1 124 ARG n 
1 125 ILE n 
1 126 GLU n 
1 127 LEU n 
1 128 LYS n 
1 129 GLY n 
1 130 VAL n 
1 131 ASP n 
1 132 PHE n 
1 133 LYS n 
1 134 GLU n 
1 135 ASP n 
1 136 GLY n 
1 137 ASN n 
1 138 ILE n 
1 139 LEU n 
1 140 GLY n 
1 141 HIS n 
1 142 LYS n 
1 143 LEU n 
1 144 GLU n 
1 145 TYR n 
1 146 ASN n 
1 147 ALA n 
1 148 ILE n 
1 149 SER n 
1 150 GLY n 
1 151 ASN n 
1 152 ALA n 
1 153 ASN n 
1 154 ILE n 
1 155 THR n 
1 156 ALA n 
1 157 ASP n 
1 158 LYS n 
1 159 GLN n 
1 160 LYS n 
1 161 ASN n 
1 162 GLY n 
1 163 ILE n 
1 164 LYS n 
1 165 ALA n 
1 166 TYR n 
1 167 PHE n 
1 168 THR n 
1 169 ILE n 
1 170 ARG n 
1 171 HIS n 
1 172 ASP n 
1 173 VAL n 
1 174 GLU n 
1 175 ASP n 
1 176 GLY n 
1 177 SER n 
1 178 VAL n 
1 179 LEU n 
1 180 LEU n 
1 181 ALA n 
1 182 ASP n 
1 183 HIS n 
1 184 TYR n 
1 185 GLN n 
1 186 GLN n 
1 187 ASN n 
1 188 THR n 
1 189 PRO n 
1 190 ILE n 
1 191 GLY n 
1 192 ASP n 
1 193 GLY n 
1 194 PRO n 
1 195 VAL n 
1 196 LEU n 
1 197 LEU n 
1 198 PRO n 
1 199 ASP n 
1 200 ASN n 
1 201 HIS n 
1 202 TYR n 
1 203 LEU n 
1 204 SER n 
1 205 THR n 
1 206 GLN n 
1 207 SER n 
1 208 LYS n 
1 209 GLN n 
1 210 SER n 
1 211 LYS n 
1 212 ASP n 
1 213 PRO n 
1 214 ASN n 
1 215 GLU n 
1 216 LYS n 
1 217 ARG n 
1 218 ASP n 
1 219 HIS n 
1 220 MET n 
1 221 VAL n 
1 222 LEU n 
1 223 LEU n 
1 224 GLU n 
1 225 PHE n 
1 226 VAL n 
1 227 THR n 
1 228 ALA n 
1 229 ALA n 
1 230 GLY n 
1 231 ILE n 
1 232 PRO n 
1 233 LEU n 
1 234 GLY n 
1 235 ALA n 
1 236 ASP n 
1 237 GLU n 
1 238 LEU n 
1 239 TYR n 
1 240 LYS n 
1 241 HIS n 
1 242 HIS n 
1 243 HIS n 
1 244 HIS n 
1 245 HIS n 
1 246 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   246 
_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      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CRF 'L-peptide linking' n 
'[(4Z)-2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid' ? 
'C17 H18 N4 O4'  342.349 
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   0   ?   ?   ?   A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   GLY 5   4   4   GLY GLY A . n 
A 1 6   GLU 6   5   5   GLU GLU A . n 
A 1 7   LYS 7   6   6   LYS LYS A . n 
A 1 8   LEU 8   7   7   LEU LEU A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  THR 10  9   9   THR THR A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  VAL 12  11  11  VAL VAL A . n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  ILE 15  14  14  ILE ILE A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  VAL 17  16  16  VAL VAL A . n 
A 1 18  GLU 18  17  17  GLU GLU A . n 
A 1 19  LEU 19  18  18  LEU LEU A . n 
A 1 20  ASP 20  19  19  ASP ASP A . n 
A 1 21  GLY 21  20  20  GLY GLY A . n 
A 1 22  ASP 22  21  21  ASP ASP A . n 
A 1 23  VAL 23  22  22  VAL VAL A . n 
A 1 24  ASN 24  23  23  ASN ASN A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  HIS 26  25  25  HIS HIS A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  SER 29  28  28  SER SER A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  SER 31  30  30  SER SER A . n 
A 1 32  GLY 32  31  31  GLY GLY A . n 
A 1 33  GLU 33  32  32  GLU GLU A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  GLU 35  34  34  GLU GLU A . n 
A 1 36  GLY 36  35  35  GLY GLY A . n 
A 1 37  ASP 37  36  36  ASP ASP A . n 
A 1 38  ALA 38  37  37  ALA ALA A . n 
A 1 39  THR 39  38  38  THR THR A . n 
A 1 40  TYR 40  39  39  TYR TYR A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  LYS 42  41  41  LYS LYS A . n 
A 1 43  MET 43  42  42  MET MET A . n 
A 1 44  SER 44  43  43  SER SER A . n 
A 1 45  LEU 45  44  44  LEU LEU A . n 
A 1 46  LYS 46  45  45  LYS LYS A . n 
A 1 47  PHE 47  46  46  PHE PHE A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  CYS 49  48  48  CYS CYS A . n 
A 1 50  THR 50  49  49  THR THR A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  LYS 53  52  52  LYS LYS A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  PRO 55  54  54  PRO PRO A . n 
A 1 56  VAL 56  55  55  VAL VAL A . n 
A 1 57  PRO 57  56  56  PRO PRO A . n 
A 1 58  TRP 58  57  57  TRP TRP A . n 
A 1 59  PRO 59  58  58  PRO PRO A . n 
A 1 60  THR 60  59  59  THR THR A . n 
A 1 61  LEU 61  60  60  LEU LEU A . n 
A 1 62  LYS 62  61  61  LYS LYS A . n 
A 1 63  THR 63  62  62  THR THR A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  THR 66  64  ?   ?   ?   A A n 
A 1 67  TRP 67  64  ?   ?   ?   A B n 
A 1 68  GLY 68  64  ?   ?   ?   A C n 
A 1 69  CRF 69  65  65  CRF CRF A . n 
A 1 70  MET 70  66  66  MET MET A . n 
A 1 71  GLN 71  67  67  GLN GLN A . n 
A 1 72  CYS 72  68  68  CYS CYS A . n 
A 1 73  PHE 73  69  69  PHE PHE A . n 
A 1 74  ALA 74  70  70  ALA ALA A . n 
A 1 75  ARG 75  71  71  ARG ARG A . n 
A 1 76  TYR 76  72  72  TYR TYR A . n 
A 1 77  PRO 77  73  73  PRO PRO A . n 
A 1 78  ASP 78  74  74  ASP ASP A . n 
A 1 79  HIS 79  75  75  HIS HIS A . n 
A 1 80  MET 80  76  76  MET MET A . n 
A 1 81  LYS 81  77  77  LYS LYS A . n 
A 1 82  GLN 82  78  78  GLN GLN A . n 
A 1 83  HIS 83  79  79  HIS HIS A . n 
A 1 84  ASP 84  80  80  ASP ASP A . n 
A 1 85  PHE 85  81  81  PHE PHE A . n 
A 1 86  PHE 86  82  82  PHE PHE A . n 
A 1 87  LYS 87  83  83  LYS LYS A . n 
A 1 88  SER 88  84  84  SER SER A . n 
A 1 89  ALA 89  85  85  ALA ALA A . n 
A 1 90  MET 90  86  86  MET MET A . n 
A 1 91  PRO 91  87  87  PRO PRO A . n 
A 1 92  GLU 92  88  88  GLU GLU A . n 
A 1 93  GLY 93  89  89  GLY GLY A . n 
A 1 94  TYR 94  90  90  TYR TYR A . n 
A 1 95  VAL 95  91  91  VAL VAL A . n 
A 1 96  GLN 96  92  92  GLN GLN A . n 
A 1 97  GLU 97  93  93  GLU GLU A . n 
A 1 98  ARG 98  94  94  ARG ARG A . n 
A 1 99  THR 99  95  95  THR THR A . n 
A 1 100 ILE 100 96  96  ILE ILE A . n 
A 1 101 PHE 101 97  97  PHE PHE A . n 
A 1 102 PHE 102 98  98  PHE PHE A . n 
A 1 103 LYS 103 99  99  LYS LYS A . n 
A 1 104 ASP 104 100 100 ASP ASP A . n 
A 1 105 ASP 105 101 101 ASP ASP A . n 
A 1 106 GLY 106 102 102 GLY GLY A . n 
A 1 107 ASN 107 103 103 ASN ASN A . n 
A 1 108 TYR 108 104 104 TYR TYR A . n 
A 1 109 LYS 109 105 105 LYS LYS A . n 
A 1 110 THR 110 106 106 THR THR A . n 
A 1 111 ARG 111 107 107 ARG ARG A . n 
A 1 112 ALA 112 108 108 ALA ALA A . n 
A 1 113 GLU 113 109 109 GLU GLU A . n 
A 1 114 VAL 114 110 110 VAL VAL A . n 
A 1 115 LYS 115 111 111 LYS LYS A . n 
A 1 116 PHE 116 112 112 PHE PHE A . n 
A 1 117 GLU 117 113 113 GLU GLU A . n 
A 1 118 GLY 118 114 114 GLY GLY A . n 
A 1 119 ASP 119 115 115 ASP ASP A . n 
A 1 120 THR 120 116 116 THR THR A . n 
A 1 121 LEU 121 117 117 LEU LEU A . n 
A 1 122 VAL 122 118 118 VAL VAL A . n 
A 1 123 ASN 123 119 119 ASN ASN A . n 
A 1 124 ARG 124 120 120 ARG ARG A . n 
A 1 125 ILE 125 121 121 ILE ILE A . n 
A 1 126 GLU 126 122 122 GLU GLU A . n 
A 1 127 LEU 127 123 123 LEU LEU A . n 
A 1 128 LYS 128 124 124 LYS LYS A . n 
A 1 129 GLY 129 125 125 GLY GLY A . n 
A 1 130 VAL 130 126 126 VAL VAL A . n 
A 1 131 ASP 131 127 127 ASP ASP A . n 
A 1 132 PHE 132 128 128 PHE PHE A . n 
A 1 133 LYS 133 129 129 LYS LYS A . n 
A 1 134 GLU 134 130 130 GLU GLU A . n 
A 1 135 ASP 135 131 131 ASP ASP A . n 
A 1 136 GLY 136 132 132 GLY GLY A . n 
A 1 137 ASN 137 133 133 ASN ASN A . n 
A 1 138 ILE 138 134 134 ILE ILE A . n 
A 1 139 LEU 139 135 135 LEU LEU A . n 
A 1 140 GLY 140 136 136 GLY GLY A . n 
A 1 141 HIS 141 137 137 HIS HIS A . n 
A 1 142 LYS 142 138 138 LYS LYS A . n 
A 1 143 LEU 143 139 139 LEU LEU A . n 
A 1 144 GLU 144 140 140 GLU GLU A . n 
A 1 145 TYR 145 141 141 TYR TYR A . n 
A 1 146 ASN 146 142 142 ASN ASN A . n 
A 1 147 ALA 147 143 143 ALA ALA A . n 
A 1 148 ILE 148 144 144 ILE ILE A . n 
A 1 149 SER 149 145 145 SER SER A . n 
A 1 150 GLY 150 146 146 GLY GLY A . n 
A 1 151 ASN 151 147 147 ASN ASN A . n 
A 1 152 ALA 152 148 148 ALA ALA A . n 
A 1 153 ASN 153 149 149 ASN ASN A . n 
A 1 154 ILE 154 150 150 ILE ILE A . n 
A 1 155 THR 155 151 151 THR THR A . n 
A 1 156 ALA 156 152 152 ALA ALA A . n 
A 1 157 ASP 157 153 153 ASP ASP A . n 
A 1 158 LYS 158 154 154 LYS LYS A . n 
A 1 159 GLN 159 155 155 GLN GLN A . n 
A 1 160 LYS 160 156 156 LYS LYS A . n 
A 1 161 ASN 161 157 157 ASN ASN A . n 
A 1 162 GLY 162 158 158 GLY GLY A . n 
A 1 163 ILE 163 159 159 ILE ILE A . n 
A 1 164 LYS 164 160 160 LYS LYS A . n 
A 1 165 ALA 165 161 161 ALA ALA A . n 
A 1 166 TYR 166 162 162 TYR TYR A . n 
A 1 167 PHE 167 163 163 PHE PHE A . n 
A 1 168 THR 168 164 164 THR THR A . n 
A 1 169 ILE 169 165 165 ILE ILE A . n 
A 1 170 ARG 170 166 166 ARG ARG A . n 
A 1 171 HIS 171 167 167 HIS HIS A . n 
A 1 172 ASP 172 168 168 ASP ASP A . n 
A 1 173 VAL 173 169 169 VAL VAL A . n 
A 1 174 GLU 174 170 170 GLU GLU A . n 
A 1 175 ASP 175 171 171 ASP ASP A . n 
A 1 176 GLY 176 172 172 GLY GLY A . n 
A 1 177 SER 177 173 173 SER SER A . n 
A 1 178 VAL 178 174 174 VAL VAL A . n 
A 1 179 LEU 179 175 175 LEU LEU A . n 
A 1 180 LEU 180 176 176 LEU LEU A . n 
A 1 181 ALA 181 177 177 ALA ALA A . n 
A 1 182 ASP 182 178 178 ASP ASP A . n 
A 1 183 HIS 183 179 179 HIS HIS A . n 
A 1 184 TYR 184 180 180 TYR TYR A . n 
A 1 185 GLN 185 181 181 GLN GLN A . n 
A 1 186 GLN 186 182 182 GLN GLN A . n 
A 1 187 ASN 187 183 183 ASN ASN A . n 
A 1 188 THR 188 184 184 THR THR A . n 
A 1 189 PRO 189 185 185 PRO PRO A . n 
A 1 190 ILE 190 186 186 ILE ILE A . n 
A 1 191 GLY 191 187 187 GLY GLY A . n 
A 1 192 ASP 192 188 188 ASP ASP A . n 
A 1 193 GLY 193 189 189 GLY GLY A . n 
A 1 194 PRO 194 190 190 PRO PRO A . n 
A 1 195 VAL 195 191 191 VAL VAL A . n 
A 1 196 LEU 196 192 192 LEU LEU A . n 
A 1 197 LEU 197 193 193 LEU LEU A . n 
A 1 198 PRO 198 194 194 PRO PRO A . n 
A 1 199 ASP 199 195 195 ASP ASP A . n 
A 1 200 ASN 200 196 196 ASN ASN A . n 
A 1 201 HIS 201 197 197 HIS HIS A . n 
A 1 202 TYR 202 198 198 TYR TYR A . n 
A 1 203 LEU 203 199 199 LEU LEU A . n 
A 1 204 SER 204 200 200 SER SER A . n 
A 1 205 THR 205 201 201 THR THR A . n 
A 1 206 GLN 206 202 202 GLN GLN A . n 
A 1 207 SER 207 203 203 SER SER A . n 
A 1 208 LYS 208 204 204 LYS LYS A . n 
A 1 209 GLN 209 205 205 GLN GLN A . n 
A 1 210 SER 210 206 206 SER SER A . n 
A 1 211 LYS 211 207 207 LYS LYS A . n 
A 1 212 ASP 212 208 208 ASP ASP A . n 
A 1 213 PRO 213 209 209 PRO PRO A . n 
A 1 214 ASN 214 210 210 ASN ASN A . n 
A 1 215 GLU 215 211 211 GLU GLU A . n 
A 1 216 LYS 216 212 212 LYS LYS A . n 
A 1 217 ARG 217 213 213 ARG ARG A . n 
A 1 218 ASP 218 214 214 ASP ASP A . n 
A 1 219 HIS 219 215 215 HIS HIS A . n 
A 1 220 MET 220 216 216 MET MET A . n 
A 1 221 VAL 221 217 217 VAL VAL A . n 
A 1 222 LEU 222 218 218 LEU LEU A . n 
A 1 223 LEU 223 219 219 LEU LEU A . n 
A 1 224 GLU 224 220 220 GLU GLU A . n 
A 1 225 PHE 225 221 221 PHE PHE A . n 
A 1 226 VAL 226 222 222 VAL VAL A . n 
A 1 227 THR 227 223 223 THR THR A . n 
A 1 228 ALA 228 224 224 ALA ALA A . n 
A 1 229 ALA 229 225 225 ALA ALA A . n 
A 1 230 GLY 230 226 226 GLY GLY A . n 
A 1 231 ILE 231 227 227 ILE ILE A . n 
A 1 232 PRO 232 228 228 PRO PRO A . n 
A 1 233 LEU 233 229 229 LEU LEU A . n 
A 1 234 GLY 234 230 ?   ?   ?   A . n 
A 1 235 ALA 235 231 ?   ?   ?   A . n 
A 1 236 ASP 236 232 ?   ?   ?   A . n 
A 1 237 GLU 237 233 ?   ?   ?   A . n 
A 1 238 LEU 238 234 ?   ?   ?   A . n 
A 1 239 TYR 239 235 ?   ?   ?   A . n 
A 1 240 LYS 240 236 ?   ?   ?   A . n 
A 1 241 HIS 241 237 ?   ?   ?   A . n 
A 1 242 HIS 242 238 ?   ?   ?   A . n 
A 1 243 HIS 243 239 ?   ?   ?   A . n 
A 1 244 HIS 244 240 ?   ?   ?   A . n 
A 1 245 HIS 245 241 ?   ?   ?   A . n 
A 1 246 HIS 246 242 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CRF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CRF 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   301 211 HOH HOH A . 
B 2 HOH 2   302 213 HOH HOH A . 
B 2 HOH 3   303 11  HOH HOH A . 
B 2 HOH 4   304 189 HOH HOH A . 
B 2 HOH 5   305 200 HOH HOH A . 
B 2 HOH 6   306 223 HOH HOH A . 
B 2 HOH 7   307 158 HOH HOH A . 
B 2 HOH 8   308 212 HOH HOH A . 
B 2 HOH 9   309 220 HOH HOH A . 
B 2 HOH 10  310 183 HOH HOH A . 
B 2 HOH 11  311 209 HOH HOH A . 
B 2 HOH 12  312 112 HOH HOH A . 
B 2 HOH 13  313 135 HOH HOH A . 
B 2 HOH 14  314 208 HOH HOH A . 
B 2 HOH 15  315 77  HOH HOH A . 
B 2 HOH 16  316 182 HOH HOH A . 
B 2 HOH 17  317 210 HOH HOH A . 
B 2 HOH 18  318 214 HOH HOH A . 
B 2 HOH 19  319 225 HOH HOH A . 
B 2 HOH 20  320 29  HOH HOH A . 
B 2 HOH 21  321 100 HOH HOH A . 
B 2 HOH 22  322 104 HOH HOH A . 
B 2 HOH 23  323 105 HOH HOH A . 
B 2 HOH 24  324 93  HOH HOH A . 
B 2 HOH 25  325 113 HOH HOH A . 
B 2 HOH 26  326 167 HOH HOH A . 
B 2 HOH 27  327 176 HOH HOH A . 
B 2 HOH 28  328 69  HOH HOH A . 
B 2 HOH 29  329 143 HOH HOH A . 
B 2 HOH 30  330 20  HOH HOH A . 
B 2 HOH 31  331 17  HOH HOH A . 
B 2 HOH 32  332 56  HOH HOH A . 
B 2 HOH 33  333 9   HOH HOH A . 
B 2 HOH 34  334 226 HOH HOH A . 
B 2 HOH 35  335 118 HOH HOH A . 
B 2 HOH 36  336 129 HOH HOH A . 
B 2 HOH 37  337 76  HOH HOH A . 
B 2 HOH 38  338 67  HOH HOH A . 
B 2 HOH 39  339 27  HOH HOH A . 
B 2 HOH 40  340 193 HOH HOH A . 
B 2 HOH 41  341 41  HOH HOH A . 
B 2 HOH 42  342 28  HOH HOH A . 
B 2 HOH 43  343 16  HOH HOH A . 
B 2 HOH 44  344 40  HOH HOH A . 
B 2 HOH 45  345 85  HOH HOH A . 
B 2 HOH 46  346 8   HOH HOH A . 
B 2 HOH 47  347 64  HOH HOH A . 
B 2 HOH 48  348 7   HOH HOH A . 
B 2 HOH 49  349 173 HOH HOH A . 
B 2 HOH 50  350 221 HOH HOH A . 
B 2 HOH 51  351 191 HOH HOH A . 
B 2 HOH 52  352 89  HOH HOH A . 
B 2 HOH 53  353 103 HOH HOH A . 
B 2 HOH 54  354 86  HOH HOH A . 
B 2 HOH 55  355 140 HOH HOH A . 
B 2 HOH 56  356 39  HOH HOH A . 
B 2 HOH 57  357 62  HOH HOH A . 
B 2 HOH 58  358 14  HOH HOH A . 
B 2 HOH 59  359 172 HOH HOH A . 
B 2 HOH 60  360 102 HOH HOH A . 
B 2 HOH 61  361 141 HOH HOH A . 
B 2 HOH 62  362 111 HOH HOH A . 
B 2 HOH 63  363 168 HOH HOH A . 
B 2 HOH 64  364 75  HOH HOH A . 
B 2 HOH 65  365 46  HOH HOH A . 
B 2 HOH 66  366 192 HOH HOH A . 
B 2 HOH 67  367 145 HOH HOH A . 
B 2 HOH 68  368 95  HOH HOH A . 
B 2 HOH 69  369 114 HOH HOH A . 
B 2 HOH 70  370 31  HOH HOH A . 
B 2 HOH 71  371 108 HOH HOH A . 
B 2 HOH 72  372 132 HOH HOH A . 
B 2 HOH 73  373 98  HOH HOH A . 
B 2 HOH 74  374 59  HOH HOH A . 
B 2 HOH 75  375 72  HOH HOH A . 
B 2 HOH 76  376 187 HOH HOH A . 
B 2 HOH 77  377 134 HOH HOH A . 
B 2 HOH 78  378 110 HOH HOH A . 
B 2 HOH 79  379 61  HOH HOH A . 
B 2 HOH 80  380 74  HOH HOH A . 
B 2 HOH 81  381 60  HOH HOH A . 
B 2 HOH 82  382 116 HOH HOH A . 
B 2 HOH 83  383 25  HOH HOH A . 
B 2 HOH 84  384 133 HOH HOH A . 
B 2 HOH 85  385 58  HOH HOH A . 
B 2 HOH 86  386 151 HOH HOH A . 
B 2 HOH 87  387 70  HOH HOH A . 
B 2 HOH 88  388 186 HOH HOH A . 
B 2 HOH 89  389 152 HOH HOH A . 
B 2 HOH 90  390 50  HOH HOH A . 
B 2 HOH 91  391 150 HOH HOH A . 
B 2 HOH 92  392 13  HOH HOH A . 
B 2 HOH 93  393 44  HOH HOH A . 
B 2 HOH 94  394 33  HOH HOH A . 
B 2 HOH 95  395 199 HOH HOH A . 
B 2 HOH 96  396 109 HOH HOH A . 
B 2 HOH 97  397 144 HOH HOH A . 
B 2 HOH 98  398 215 HOH HOH A . 
B 2 HOH 99  399 184 HOH HOH A . 
B 2 HOH 100 400 42  HOH HOH A . 
B 2 HOH 101 401 96  HOH HOH A . 
B 2 HOH 102 402 19  HOH HOH A . 
B 2 HOH 103 403 23  HOH HOH A . 
B 2 HOH 104 404 127 HOH HOH A . 
B 2 HOH 105 405 149 HOH HOH A . 
B 2 HOH 106 406 10  HOH HOH A . 
B 2 HOH 107 407 6   HOH HOH A . 
B 2 HOH 108 408 43  HOH HOH A . 
B 2 HOH 109 409 4   HOH HOH A . 
B 2 HOH 110 410 37  HOH HOH A . 
B 2 HOH 111 411 18  HOH HOH A . 
B 2 HOH 112 412 125 HOH HOH A . 
B 2 HOH 113 413 166 HOH HOH A . 
B 2 HOH 114 414 153 HOH HOH A . 
B 2 HOH 115 415 38  HOH HOH A . 
B 2 HOH 116 416 84  HOH HOH A . 
B 2 HOH 117 417 73  HOH HOH A . 
B 2 HOH 118 418 142 HOH HOH A . 
B 2 HOH 119 419 3   HOH HOH A . 
B 2 HOH 120 420 124 HOH HOH A . 
B 2 HOH 121 421 47  HOH HOH A . 
B 2 HOH 122 422 78  HOH HOH A . 
B 2 HOH 123 423 55  HOH HOH A . 
B 2 HOH 124 424 224 HOH HOH A . 
B 2 HOH 125 425 30  HOH HOH A . 
B 2 HOH 126 426 128 HOH HOH A . 
B 2 HOH 127 427 130 HOH HOH A . 
B 2 HOH 128 428 206 HOH HOH A . 
B 2 HOH 129 429 156 HOH HOH A . 
B 2 HOH 130 430 138 HOH HOH A . 
B 2 HOH 131 431 52  HOH HOH A . 
B 2 HOH 132 432 24  HOH HOH A . 
B 2 HOH 133 433 107 HOH HOH A . 
B 2 HOH 134 434 205 HOH HOH A . 
B 2 HOH 135 435 45  HOH HOH A . 
B 2 HOH 136 436 34  HOH HOH A . 
B 2 HOH 137 437 54  HOH HOH A . 
B 2 HOH 138 438 21  HOH HOH A . 
B 2 HOH 139 439 119 HOH HOH A . 
B 2 HOH 140 440 71  HOH HOH A . 
B 2 HOH 141 441 97  HOH HOH A . 
B 2 HOH 142 442 126 HOH HOH A . 
B 2 HOH 143 443 83  HOH HOH A . 
B 2 HOH 144 444 123 HOH HOH A . 
B 2 HOH 145 445 5   HOH HOH A . 
B 2 HOH 146 446 82  HOH HOH A . 
B 2 HOH 147 447 49  HOH HOH A . 
B 2 HOH 148 448 15  HOH HOH A . 
B 2 HOH 149 449 165 HOH HOH A . 
B 2 HOH 150 450 117 HOH HOH A . 
B 2 HOH 151 451 87  HOH HOH A . 
B 2 HOH 152 452 79  HOH HOH A . 
B 2 HOH 153 453 80  HOH HOH A . 
B 2 HOH 154 454 68  HOH HOH A . 
B 2 HOH 155 455 32  HOH HOH A . 
B 2 HOH 156 456 51  HOH HOH A . 
B 2 HOH 157 457 36  HOH HOH A . 
B 2 HOH 158 458 190 HOH HOH A . 
B 2 HOH 159 459 35  HOH HOH A . 
B 2 HOH 160 460 91  HOH HOH A . 
B 2 HOH 161 461 122 HOH HOH A . 
B 2 HOH 162 462 99  HOH HOH A . 
B 2 HOH 163 463 53  HOH HOH A . 
B 2 HOH 164 464 106 HOH HOH A . 
B 2 HOH 165 465 1   HOH HOH A . 
B 2 HOH 166 466 139 HOH HOH A . 
B 2 HOH 167 467 216 HOH HOH A . 
B 2 HOH 168 468 201 HOH HOH A . 
B 2 HOH 169 469 48  HOH HOH A . 
B 2 HOH 170 470 194 HOH HOH A . 
B 2 HOH 171 471 115 HOH HOH A . 
B 2 HOH 172 472 155 HOH HOH A . 
B 2 HOH 173 473 157 HOH HOH A . 
B 2 HOH 174 474 198 HOH HOH A . 
B 2 HOH 175 475 63  HOH HOH A . 
B 2 HOH 176 476 66  HOH HOH A . 
B 2 HOH 177 477 136 HOH HOH A . 
B 2 HOH 178 478 180 HOH HOH A . 
B 2 HOH 179 479 81  HOH HOH A . 
B 2 HOH 180 480 121 HOH HOH A . 
B 2 HOH 181 481 154 HOH HOH A . 
B 2 HOH 182 482 174 HOH HOH A . 
B 2 HOH 183 483 207 HOH HOH A . 
B 2 HOH 184 484 196 HOH HOH A . 
B 2 HOH 185 485 120 HOH HOH A . 
B 2 HOH 186 486 195 HOH HOH A . 
B 2 HOH 187 487 177 HOH HOH A . 
B 2 HOH 188 488 222 HOH HOH A . 
B 2 HOH 189 489 148 HOH HOH A . 
B 2 HOH 190 490 163 HOH HOH A . 
B 2 HOH 191 491 160 HOH HOH A . 
B 2 HOH 192 492 204 HOH HOH A . 
B 2 HOH 193 493 178 HOH HOH A . 
B 2 HOH 194 494 146 HOH HOH A . 
B 2 HOH 195 495 227 HOH HOH A . 
B 2 HOH 196 496 218 HOH HOH A . 
B 2 HOH 197 497 188 HOH HOH A . 
B 2 HOH 198 498 181 HOH HOH A . 
B 2 HOH 199 499 162 HOH HOH A . 
B 2 HOH 200 500 203 HOH HOH A . 
B 2 HOH 201 501 2   HOH HOH A . 
B 2 HOH 202 502 179 HOH HOH A . 
B 2 HOH 203 503 185 HOH HOH A . 
B 2 HOH 204 504 92  HOH HOH A . 
B 2 HOH 205 505 147 HOH HOH A . 
B 2 HOH 206 506 131 HOH HOH A . 
B 2 HOH 207 507 101 HOH HOH A . 
B 2 HOH 208 508 94  HOH HOH A . 
B 2 HOH 209 509 197 HOH HOH A . 
B 2 HOH 210 510 65  HOH HOH A . 
B 2 HOH 211 511 159 HOH HOH A . 
B 2 HOH 212 512 202 HOH HOH A . 
B 2 HOH 213 513 161 HOH HOH A . 
B 2 HOH 214 514 171 HOH HOH A . 
B 2 HOH 215 515 169 HOH HOH A . 
B 2 HOH 216 516 170 HOH HOH A . 
B 2 HOH 217 517 164 HOH HOH A . 
B 2 HOH 218 518 217 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A VAL 1  ? CG1 ? A VAL 2  CG1 
2 1 Y 1 A VAL 1  ? CG2 ? A VAL 2  CG2 
3 1 Y 1 A LYS 6  ? CD  ? A LYS 7  CD  
4 1 Y 1 A LYS 6  ? CE  ? A LYS 7  CE  
5 1 Y 1 A LYS 6  ? NZ  ? A LYS 7  NZ  
6 1 Y 1 A LYS 52 ? CE  ? A LYS 53 CE  
7 1 Y 1 A LYS 52 ? NZ  ? A LYS 53 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FEN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     111.900 
_cell.length_a_esd                 ? 
_cell.length_b                     51.480 
_cell.length_b_esd                 ? 
_cell.length_c                     55.630 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FEN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FEN 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;20 % w/v Polyethylene glycol 6,000
100 mM tri-Sodium citrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9184 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BESSY BEAMLINE 14.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_synchrotron_site       BESSY 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FEN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.56 
_reflns.d_resolution_low                               50.0 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     85128 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.98 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.081 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.069 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.56 1.65 ? ? ? ? ? ? 13653 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.8330000000000002   ? ? 1 1 0.27699999999999997 ? ? ? ? 1.551 ? ? ? ? ? 
? ? ? ? 
1.65 1.77 ? ? ? ? ? ? 12857 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.051                ? ? 2 1 0.523               ? ? ? ? 0.89 ? ? ? ? ? 
? ? ? ? 
1.77 1.91 ? ? ? ? ? ? 12061 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.53                 ? ? 3 1 0.825               ? ? ? ? 0.45 ? ? ? ? ? 
? ? ? ? 
1.91 2.09 ? ? ? ? ? ? 11023 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.27699999999999997  ? ? 4 1 0.935               ? ? ? ? 0.233 ? ? ? ? ? 
? ? ? ? 
2.09 2.34 ? ? ? ? ? ? 10109 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.16                 ? ? 5 1 0.978               ? ? ? ? 0.136 ? ? ? ? ? 
? ? ? ? 
2.34 2.7  ? ? ? ? ? ? 8925  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.09699999999999999  ? ? 6 1 0.991               ? ? ? ? 
0.08199999999999999  ? ? ? ? ? ? ? ? ? 
2.70 3.3  ? ? ? ? ? ? 7538  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.054000000000000006 ? ? 7 1 0.998               ? ? ? ? 0.046 ? ? ? ? ? 
? ? ? ? 
3.30 4.66 ? ? ? ? ? ? 5780  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.034                ? ? 8 1 0.9990000000000001  ? ? ? ? 
0.028999999999999998 ? ? ? ? ? ? ? ? ? 
4.66 50.0 ? ? ? ? ? ? 3182  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 9 1 0.9990000000000001  ? ? ? ? 0.024 ? ? ? ? ? 
? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.14 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.33 
_refine.aniso_B[2][2]                            -0.11 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.35 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.826 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.965 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FEN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             42.89 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     39620 
_refine.ls_number_reflns_R_free                  1003 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.51 
_refine.ls_percent_reflns_R_free                 2.5 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17116 
_refine.ls_R_factor_R_free                       0.19935 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17044 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.072 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_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_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.009 
_refine.overall_SU_ML                            0.066 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        42.89 
_refine_hist.number_atoms_solvent             218 
_refine_hist.number_atoms_total               2028 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1810 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.013  1947 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  1792 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.841  1.674  2657 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.388  1.605  4179 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.377  5.000  254  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.073 24.706 102  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.786 15.000 338  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.794 15.000 6    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200  253  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2255 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  428  ? r_gen_planes_other           ? ? 
'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' ? 2.350  3.523  938  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.348  3.520  937  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.023  5.275  1176 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.023  5.279  1177 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.789  3.879  1009 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.780  3.881  1009 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.658  5.670  1466 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.131  41.761 2160 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.064  41.050 2103 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.600 
_refine_ls_shell.d_res_low                        1.641 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             72 
_refine_ls_shell.number_reflns_R_work             2879 
_refine_ls_shell.percent_reflns_obs               97.81 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.338 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.302 
# 
_struct.entry_id                     9FEN 
_struct.title                        'LSSmOrange (P1) - Directionality of Optical Properties of Fluorescent Proteins' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9FEN 
_struct_keywords.text            'FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9FEN 
_struct_ref.pdbx_db_accession          9FEN 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FEN 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 246 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9FEN 
_struct_ref_seq.db_align_beg                  0 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  242 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       0 
_struct_ref_seq.pdbx_auth_seq_align_end       242 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 750   ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  10560 ? 
# 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 3   ? LEU A 8   ? SER A 2   LEU A 7   1 ? 6 
HELX_P HELX_P2 AA2 ALA A 38  ? TYR A 40  ? ALA A 37  TYR A 39  5 ? 3 
HELX_P HELX_P3 AA3 PRO A 57  ? LYS A 62  ? PRO A 56  LYS A 61  5 ? 6 
HELX_P HELX_P4 AA4 MET A 70  ? ALA A 74  ? MET A 66  ALA A 70  5 ? 5 
HELX_P HELX_P5 AA5 PRO A 77  ? HIS A 83  ? PRO A 73  HIS A 79  5 ? 7 
HELX_P HELX_P6 AA6 ASP A 84  ? ALA A 89  ? ASP A 80  ALA A 85  1 ? 6 
HELX_P HELX_P7 AA7 LYS A 158 ? ASN A 161 ? LYS A 154 ASN A 157 5 ? 4 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A LEU 65 C  ? ? ? 1_555 A CRF 69 N1 ? ? A LEU 64 A CRF 65 1_555 ? ? ? ? ? ? ? 1.520 ? ? 
covale2 covale both ? A CRF 69 C3 ? ? ? 1_555 A MET 70 N  ? ? A CRF 65 A MET 66 1_555 ? ? ? ? ? ? ? 1.551 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CRF 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       69 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       CRF 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        65 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                'THR, TRP, GLY' 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        CRF 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           Chromophore/chromophore-like 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          MET 
_struct_mon_prot_cis.label_seq_id           90 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           MET 
_struct_mon_prot_cis.auth_seq_id            86 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    91 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     87 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       7.97 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   12 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 13  ? VAL A 23  ? VAL A 12  VAL A 22  
AA1 2  HIS A 26  ? ASP A 37  ? HIS A 25  ASP A 36  
AA1 3  LYS A 42  ? CYS A 49  ? LYS A 41  CYS A 48  
AA1 4  HIS A 219 ? ALA A 229 ? HIS A 215 ALA A 225 
AA1 5  HIS A 201 ? SER A 210 ? HIS A 197 SER A 206 
AA1 6  GLY A 150 ? ASP A 157 ? GLY A 146 ASP A 153 
AA1 7  GLY A 162 ? ASP A 172 ? GLY A 158 ASP A 168 
AA1 8  VAL A 178 ? PRO A 189 ? VAL A 174 PRO A 185 
AA1 9  TYR A 94  ? PHE A 102 ? TYR A 90  PHE A 98  
AA1 10 ASN A 107 ? GLU A 117 ? ASN A 103 GLU A 113 
AA1 11 THR A 120 ? VAL A 130 ? THR A 116 VAL A 126 
AA1 12 VAL A 13  ? VAL A 23  ? VAL A 12  VAL A 22  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N VAL A 13  ? N VAL A 12  O GLY A 36  ? O GLY A 35  
AA1 2  3  N ASP A 37  ? N ASP A 36  O LYS A 42  ? O LYS A 41  
AA1 3  4  N PHE A 47  ? N PHE A 46  O MET A 220 ? O MET A 216 
AA1 4  5  O THR A 227 ? O THR A 223 N SER A 204 ? N SER A 200 
AA1 5  6  O HIS A 201 ? O HIS A 197 N ILE A 154 ? N ILE A 150 
AA1 6  7  N ASP A 157 ? N ASP A 153 O GLY A 162 ? O GLY A 158 
AA1 7  8  N HIS A 171 ? N HIS A 167 O LEU A 179 ? O LEU A 175 
AA1 8  9  O THR A 188 ? O THR A 184 N VAL A 95  ? N VAL A 91  
AA1 9  10 N GLN A 96  ? N GLN A 92  O ALA A 112 ? O ALA A 108 
AA1 10 11 N LYS A 115 ? N LYS A 111 O VAL A 122 ? O VAL A 118 
AA1 11 12 O GLY A 129 ? O GLY A 125 N ASP A 22  ? N ASP A 21  
# 
_pdbx_entry_details.entry_id                   9FEN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 113 ? A O A HOH 302 ? ? 1.46 
2 1 NE  A ARG 120 ? ? O A HOH 302 ? ? 2.05 
3 1 O   A HOH 468 ? ? O A HOH 488 ? ? 2.11 
4 1 O   A HOH 319 ? ? O A HOH 334 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     17 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OH 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    TYR 
_pdbx_validate_symm_contact.auth_seq_id_2     39 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_556 
_pdbx_validate_symm_contact.dist              2.05 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ILE 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     134 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -91.44 
_pdbx_validate_torsion.psi             -67.51 
# 
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 0   ? A MET 1   
2  1 Y 1 A THR 64  A A THR 66  
3  1 Y 1 A TRP 64  B A TRP 67  
4  1 Y 1 A GLY 64  C A GLY 68  
5  1 Y 1 A GLY 230 ? A GLY 234 
6  1 Y 1 A ALA 231 ? A ALA 235 
7  1 Y 1 A ASP 232 ? A ASP 236 
8  1 Y 1 A GLU 233 ? A GLU 237 
9  1 Y 1 A LEU 234 ? A LEU 238 
10 1 Y 1 A TYR 235 ? A TYR 239 
11 1 Y 1 A LYS 236 ? A LYS 240 
12 1 Y 1 A HIS 237 ? A HIS 241 
13 1 Y 1 A HIS 238 ? A HIS 242 
14 1 Y 1 A HIS 239 ? A HIS 243 
15 1 Y 1 A HIS 240 ? A HIS 244 
16 1 Y 1 A HIS 241 ? A HIS 245 
17 1 Y 1 A HIS 242 ? A HIS 246 
# 
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  
CRF N1   N N N 74  
CRF CA1  C N R 75  
CRF CB1  C N R 76  
CRF CG1  C N N 77  
CRF OG1  O N N 78  
CRF C1   C N N 79  
CRF N2   N N N 80  
CRF N3   N N N 81  
CRF C2   C N N 82  
CRF O2   O N N 83  
CRF CA2  C N N 84  
CRF CA3  C N N 85  
CRF C3   C N N 86  
CRF O3   O N N 87  
CRF CB2  C N N 88  
CRF CG2  C Y N 89  
CRF CD1  C Y N 90  
CRF CD2  C Y N 91  
CRF CE2  C Y N 92  
CRF NE1  N Y N 93  
CRF CE3  C Y N 94  
CRF CZ2  C Y N 95  
CRF CZ3  C Y N 96  
CRF CH2  C Y N 97  
CRF H    H N N 98  
CRF H2   H N N 99  
CRF HA1  H N N 100 
CRF HB1  H N N 101 
CRF HG11 H N N 102 
CRF HG12 H N N 103 
CRF HG13 H N N 104 
CRF HOG  H N N 105 
CRF HA31 H N N 106 
CRF HA32 H N N 107 
CRF OXT  O N N 108 
CRF HB2  H N N 109 
CRF HD1  H N N 110 
CRF HE1  H N N 111 
CRF HE3  H N N 112 
CRF HZ2  H N N 113 
CRF HZ3  H N N 114 
CRF HH2  H N N 115 
CRF HXT  H N N 116 
CYS N    N N N 117 
CYS CA   C N R 118 
CYS C    C N N 119 
CYS O    O N N 120 
CYS CB   C N N 121 
CYS SG   S N N 122 
CYS OXT  O N N 123 
CYS H    H N N 124 
CYS H2   H N N 125 
CYS HA   H N N 126 
CYS HB2  H N N 127 
CYS HB3  H N N 128 
CYS HG   H N N 129 
CYS HXT  H N N 130 
GLN N    N N N 131 
GLN CA   C N S 132 
GLN C    C N N 133 
GLN O    O N N 134 
GLN CB   C N N 135 
GLN CG   C N N 136 
GLN CD   C N N 137 
GLN OE1  O N N 138 
GLN NE2  N N N 139 
GLN OXT  O N N 140 
GLN H    H N N 141 
GLN H2   H N N 142 
GLN HA   H N N 143 
GLN HB2  H N N 144 
GLN HB3  H N N 145 
GLN HG2  H N N 146 
GLN HG3  H N N 147 
GLN HE21 H N N 148 
GLN HE22 H N N 149 
GLN HXT  H N N 150 
GLU N    N N N 151 
GLU CA   C N S 152 
GLU C    C N N 153 
GLU O    O N N 154 
GLU CB   C N N 155 
GLU CG   C N N 156 
GLU CD   C N N 157 
GLU OE1  O N N 158 
GLU OE2  O N N 159 
GLU OXT  O N N 160 
GLU H    H N N 161 
GLU H2   H N N 162 
GLU HA   H N N 163 
GLU HB2  H N N 164 
GLU HB3  H N N 165 
GLU HG2  H N N 166 
GLU HG3  H N N 167 
GLU HE2  H N N 168 
GLU HXT  H N N 169 
GLY N    N N N 170 
GLY CA   C N N 171 
GLY C    C N N 172 
GLY O    O N N 173 
GLY OXT  O N N 174 
GLY H    H N N 175 
GLY H2   H N N 176 
GLY HA2  H N N 177 
GLY HA3  H N N 178 
GLY HXT  H N N 179 
HIS N    N N N 180 
HIS CA   C N S 181 
HIS C    C N N 182 
HIS O    O N N 183 
HIS CB   C N N 184 
HIS CG   C Y N 185 
HIS ND1  N Y N 186 
HIS CD2  C Y N 187 
HIS CE1  C Y N 188 
HIS NE2  N Y N 189 
HIS OXT  O N N 190 
HIS H    H N N 191 
HIS H2   H N N 192 
HIS HA   H N N 193 
HIS HB2  H N N 194 
HIS HB3  H N N 195 
HIS HD1  H N N 196 
HIS HD2  H N N 197 
HIS HE1  H N N 198 
HIS HE2  H N N 199 
HIS HXT  H N N 200 
HOH O    O N N 201 
HOH H1   H N N 202 
HOH H2   H N N 203 
ILE N    N N N 204 
ILE CA   C N S 205 
ILE C    C N N 206 
ILE O    O N N 207 
ILE CB   C N S 208 
ILE CG1  C N N 209 
ILE CG2  C N N 210 
ILE CD1  C N N 211 
ILE OXT  O N N 212 
ILE H    H N N 213 
ILE H2   H N N 214 
ILE HA   H N N 215 
ILE HB   H N N 216 
ILE HG12 H N N 217 
ILE HG13 H N N 218 
ILE HG21 H N N 219 
ILE HG22 H N N 220 
ILE HG23 H N N 221 
ILE HD11 H N N 222 
ILE HD12 H N N 223 
ILE HD13 H N N 224 
ILE HXT  H N N 225 
LEU N    N N N 226 
LEU CA   C N S 227 
LEU C    C N N 228 
LEU O    O N N 229 
LEU CB   C N N 230 
LEU CG   C N N 231 
LEU CD1  C N N 232 
LEU CD2  C N N 233 
LEU OXT  O N N 234 
LEU H    H N N 235 
LEU H2   H N N 236 
LEU HA   H N N 237 
LEU HB2  H N N 238 
LEU HB3  H N N 239 
LEU HG   H N N 240 
LEU HD11 H N N 241 
LEU HD12 H N N 242 
LEU HD13 H N N 243 
LEU HD21 H N N 244 
LEU HD22 H N N 245 
LEU HD23 H N N 246 
LEU HXT  H N N 247 
LYS N    N N N 248 
LYS CA   C N S 249 
LYS C    C N N 250 
LYS O    O N N 251 
LYS CB   C N N 252 
LYS CG   C N N 253 
LYS CD   C N N 254 
LYS CE   C N N 255 
LYS NZ   N N N 256 
LYS OXT  O N N 257 
LYS H    H N N 258 
LYS H2   H N N 259 
LYS HA   H N N 260 
LYS HB2  H N N 261 
LYS HB3  H N N 262 
LYS HG2  H N N 263 
LYS HG3  H N N 264 
LYS HD2  H N N 265 
LYS HD3  H N N 266 
LYS HE2  H N N 267 
LYS HE3  H N N 268 
LYS HZ1  H N N 269 
LYS HZ2  H N N 270 
LYS HZ3  H N N 271 
LYS HXT  H N N 272 
MET N    N N N 273 
MET CA   C N S 274 
MET C    C N N 275 
MET O    O N N 276 
MET CB   C N N 277 
MET CG   C N N 278 
MET SD   S N N 279 
MET CE   C N N 280 
MET OXT  O N N 281 
MET H    H N N 282 
MET H2   H N N 283 
MET HA   H N N 284 
MET HB2  H N N 285 
MET HB3  H N N 286 
MET HG2  H N N 287 
MET HG3  H N N 288 
MET HE1  H N N 289 
MET HE2  H N N 290 
MET HE3  H N N 291 
MET HXT  H N N 292 
PHE N    N N N 293 
PHE CA   C N S 294 
PHE C    C N N 295 
PHE O    O N N 296 
PHE CB   C N N 297 
PHE CG   C Y N 298 
PHE CD1  C Y N 299 
PHE CD2  C Y N 300 
PHE CE1  C Y N 301 
PHE CE2  C Y N 302 
PHE CZ   C Y N 303 
PHE OXT  O N N 304 
PHE H    H N N 305 
PHE H2   H N N 306 
PHE HA   H N N 307 
PHE HB2  H N N 308 
PHE HB3  H N N 309 
PHE HD1  H N N 310 
PHE HD2  H N N 311 
PHE HE1  H N N 312 
PHE HE2  H N N 313 
PHE HZ   H N N 314 
PHE HXT  H N N 315 
PRO N    N N N 316 
PRO CA   C N S 317 
PRO C    C N N 318 
PRO O    O N N 319 
PRO CB   C N N 320 
PRO CG   C N N 321 
PRO CD   C N N 322 
PRO OXT  O N N 323 
PRO H    H N N 324 
PRO HA   H N N 325 
PRO HB2  H N N 326 
PRO HB3  H N N 327 
PRO HG2  H N N 328 
PRO HG3  H N N 329 
PRO HD2  H N N 330 
PRO HD3  H N N 331 
PRO HXT  H N N 332 
SER N    N N N 333 
SER CA   C N S 334 
SER C    C N N 335 
SER O    O N N 336 
SER CB   C N N 337 
SER OG   O N N 338 
SER OXT  O N N 339 
SER H    H N N 340 
SER H2   H N N 341 
SER HA   H N N 342 
SER HB2  H N N 343 
SER HB3  H N N 344 
SER HG   H N N 345 
SER HXT  H N N 346 
THR N    N N N 347 
THR CA   C N S 348 
THR C    C N N 349 
THR O    O N N 350 
THR CB   C N R 351 
THR OG1  O N N 352 
THR CG2  C N N 353 
THR OXT  O N N 354 
THR H    H N N 355 
THR H2   H N N 356 
THR HA   H N N 357 
THR HB   H N N 358 
THR HG1  H N N 359 
THR HG21 H N N 360 
THR HG22 H N N 361 
THR HG23 H N N 362 
THR HXT  H N N 363 
TRP N    N N N 364 
TRP CA   C N S 365 
TRP C    C N N 366 
TRP O    O N N 367 
TRP CB   C N N 368 
TRP CG   C Y N 369 
TRP CD1  C Y N 370 
TRP CD2  C Y N 371 
TRP NE1  N Y N 372 
TRP CE2  C Y N 373 
TRP CE3  C Y N 374 
TRP CZ2  C Y N 375 
TRP CZ3  C Y N 376 
TRP CH2  C Y N 377 
TRP OXT  O N N 378 
TRP H    H N N 379 
TRP H2   H N N 380 
TRP HA   H N N 381 
TRP HB2  H N N 382 
TRP HB3  H N N 383 
TRP HD1  H N N 384 
TRP HE1  H N N 385 
TRP HE3  H N N 386 
TRP HZ2  H N N 387 
TRP HZ3  H N N 388 
TRP HH2  H N N 389 
TRP HXT  H N N 390 
TYR N    N N N 391 
TYR CA   C N S 392 
TYR C    C N N 393 
TYR O    O N N 394 
TYR CB   C N N 395 
TYR CG   C Y N 396 
TYR CD1  C Y N 397 
TYR CD2  C Y N 398 
TYR CE1  C Y N 399 
TYR CE2  C Y N 400 
TYR CZ   C Y N 401 
TYR OH   O N N 402 
TYR OXT  O N N 403 
TYR H    H N N 404 
TYR H2   H N N 405 
TYR HA   H N N 406 
TYR HB2  H N N 407 
TYR HB3  H N N 408 
TYR HD1  H N N 409 
TYR HD2  H N N 410 
TYR HE1  H N N 411 
TYR HE2  H N N 412 
TYR HH   H N N 413 
TYR HXT  H N N 414 
VAL N    N N N 415 
VAL CA   C N S 416 
VAL C    C N N 417 
VAL O    O N N 418 
VAL CB   C N N 419 
VAL CG1  C N N 420 
VAL CG2  C N N 421 
VAL OXT  O N N 422 
VAL H    H N N 423 
VAL H2   H N N 424 
VAL HA   H N N 425 
VAL HB   H N N 426 
VAL HG11 H N N 427 
VAL HG12 H N N 428 
VAL HG13 H N N 429 
VAL HG21 H N N 430 
VAL HG22 H N N 431 
VAL HG23 H N N 432 
VAL HXT  H N N 433 
# 
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  
CRF N1  CA1  sing N N 70  
CRF N1  H    sing N N 71  
CRF N1  H2   sing N N 72  
CRF CA1 CB1  sing N N 73  
CRF CA1 C1   sing N N 74  
CRF CA1 HA1  sing N N 75  
CRF CB1 CG1  sing N N 76  
CRF CB1 OG1  sing N N 77  
CRF CB1 HB1  sing N N 78  
CRF CG1 HG11 sing N N 79  
CRF CG1 HG12 sing N N 80  
CRF CG1 HG13 sing N N 81  
CRF OG1 HOG  sing N N 82  
CRF C1  N2   doub N N 83  
CRF C1  N3   sing N N 84  
CRF N2  CA2  sing N N 85  
CRF N3  C2   sing N N 86  
CRF N3  CA3  sing N N 87  
CRF C2  O2   doub N N 88  
CRF C2  CA2  sing N N 89  
CRF CA2 CB2  doub N Z 90  
CRF CA3 C3   sing N N 91  
CRF CA3 HA31 sing N N 92  
CRF CA3 HA32 sing N N 93  
CRF C3  O3   doub N N 94  
CRF C3  OXT  sing N N 95  
CRF CB2 CG2  sing N N 96  
CRF CB2 HB2  sing N N 97  
CRF CG2 CD1  doub Y N 98  
CRF CG2 CD2  sing Y N 99  
CRF CD1 NE1  sing Y N 100 
CRF CD1 HD1  sing N N 101 
CRF CD2 CE2  doub Y N 102 
CRF CD2 CE3  sing Y N 103 
CRF CE2 NE1  sing Y N 104 
CRF CE2 CZ2  sing Y N 105 
CRF NE1 HE1  sing N N 106 
CRF CE3 CZ3  doub Y N 107 
CRF CE3 HE3  sing N N 108 
CRF CZ2 CH2  doub Y N 109 
CRF CZ2 HZ2  sing N N 110 
CRF CZ3 CH2  sing Y N 111 
CRF CZ3 HZ3  sing N N 112 
CRF CH2 HH2  sing N N 113 
CRF OXT HXT  sing N N 114 
CYS N   CA   sing N N 115 
CYS N   H    sing N N 116 
CYS N   H2   sing N N 117 
CYS CA  C    sing N N 118 
CYS CA  CB   sing N N 119 
CYS CA  HA   sing N N 120 
CYS C   O    doub N N 121 
CYS C   OXT  sing N N 122 
CYS CB  SG   sing N N 123 
CYS CB  HB2  sing N N 124 
CYS CB  HB3  sing N N 125 
CYS SG  HG   sing N N 126 
CYS OXT HXT  sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Education, Youth and Sports of the Czech Republic' 'Czech Republic' CZ.02.1.01/0.0/0.0/16_019/0000729 1 
'Czech Science Foundation'                                      'Czech Republic' 23-05983S                         2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   4RYS 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4RYS 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FEN 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008937 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001656 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019425 
_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]   0.018282 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . VAL A 1 2   ? 26.517 -5.364  44.863 1.00 81.19 ? 1   VAL A N   1 
ATOM   2    C CA  . VAL A 1 2   ? 26.818 -4.650  43.599 1.00 71.54 ? 1   VAL A CA  1 
ATOM   3    C C   . VAL A 1 2   ? 27.632 -3.396  43.950 1.00 65.86 ? 1   VAL A C   1 
ATOM   4    O O   . VAL A 1 2   ? 27.305 -2.726  44.951 1.00 60.57 ? 1   VAL A O   1 
ATOM   5    C CB  . VAL A 1 2   ? 25.530 -4.302  42.819 1.00 59.45 ? 1   VAL A CB  1 
ATOM   6    N N   . SER A 1 3   ? 28.679 -3.117  43.171 1.00 56.07 ? 2   SER A N   1 
ATOM   7    C CA  . SER A 1 3   ? 29.475 -1.858  43.189 1.00 53.29 ? 2   SER A CA  1 
ATOM   8    C C   . SER A 1 3   ? 28.633 -0.674  42.684 1.00 52.91 ? 2   SER A C   1 
ATOM   9    O O   . SER A 1 3   ? 27.569 -0.898  41.992 1.00 44.98 ? 2   SER A O   1 
ATOM   10   C CB  . SER A 1 3   ? 30.727 -1.991  42.355 1.00 56.88 ? 2   SER A CB  1 
ATOM   11   O OG  . SER A 1 3   ? 30.420 -1.854  40.975 1.00 57.55 ? 2   SER A OG  1 
ATOM   12   N N   . LYS A 1 4   ? 29.125 0.546   42.934 1.00 46.95 ? 3   LYS A N   1 
ATOM   13   C CA  . LYS A 1 4   ? 28.449 1.785   42.468 1.00 54.22 ? 3   LYS A CA  1 
ATOM   14   C C   . LYS A 1 4   ? 28.413 1.726   40.937 1.00 37.91 ? 3   LYS A C   1 
ATOM   15   O O   . LYS A 1 4   ? 27.348 2.005   40.355 1.00 42.41 ? 3   LYS A O   1 
ATOM   16   C CB  . LYS A 1 4   ? 29.153 3.045   42.983 1.00 57.12 ? 3   LYS A CB  1 
ATOM   17   C CG  . LYS A 1 4   ? 28.453 3.743   44.144 1.00 69.09 ? 3   LYS A CG  1 
ATOM   18   C CD  . LYS A 1 4   ? 29.334 4.745   44.885 1.00 70.76 ? 3   LYS A CD  1 
ATOM   19   C CE  . LYS A 1 4   ? 28.535 5.753   45.684 1.00 76.26 ? 3   LYS A CE  1 
ATOM   20   N NZ  . LYS A 1 4   ? 27.382 5.118   46.363 1.00 81.69 ? 3   LYS A NZ  1 
ATOM   21   N N   . GLY A 1 5   ? 29.558 1.391   40.331 1.00 44.34 ? 4   GLY A N   1 
ATOM   22   C CA  . GLY A 1 5   ? 29.680 1.398   38.865 1.00 38.36 ? 4   GLY A CA  1 
ATOM   23   C C   . GLY A 1 5   ? 28.744 0.375   38.249 1.00 35.96 ? 4   GLY A C   1 
ATOM   24   O O   . GLY A 1 5   ? 27.978 0.744   37.320 1.00 36.78 ? 4   GLY A O   1 
ATOM   25   N N   . GLU A 1 6   ? 28.740 -0.868  38.753 1.00 36.81 ? 5   GLU A N   1 
ATOM   26   C CA  A GLU A 1 6   ? 27.872 -1.966  38.237 0.50 39.56 ? 5   GLU A CA  1 
ATOM   27   C CA  B GLU A 1 6   ? 27.873 -1.921  38.158 0.50 41.33 ? 5   GLU A CA  1 
ATOM   28   C C   . GLU A 1 6   ? 26.397 -1.548  38.382 1.00 40.22 ? 5   GLU A C   1 
ATOM   29   O O   . GLU A 1 6   ? 25.596 -1.816  37.475 1.00 37.31 ? 5   GLU A O   1 
ATOM   30   C CB  A GLU A 1 6   ? 28.241 -3.301  38.917 0.50 40.96 ? 5   GLU A CB  1 
ATOM   31   C CB  B GLU A 1 6   ? 28.274 -3.327  38.624 0.50 46.09 ? 5   GLU A CB  1 
ATOM   32   C CG  A GLU A 1 6   ? 29.544 -3.882  38.376 0.50 45.53 ? 5   GLU A CG  1 
ATOM   33   C CG  B GLU A 1 6   ? 27.955 -3.655  40.061 0.50 54.02 ? 5   GLU A CG  1 
ATOM   34   C CD  A GLU A 1 6   ? 30.110 -5.175  38.966 0.50 48.54 ? 5   GLU A CD  1 
ATOM   35   C CD  B GLU A 1 6   ? 28.596 -4.967  40.493 0.50 51.12 ? 5   GLU A CD  1 
ATOM   36   O OE1 A GLU A 1 6   ? 29.675 -5.576  40.066 0.50 41.17 ? 5   GLU A OE1 1 
ATOM   37   O OE1 B GLU A 1 6   ? 28.417 -5.958  39.771 0.50 56.48 ? 5   GLU A OE1 1 
ATOM   38   O OE2 A GLU A 1 6   ? 31.031 -5.773  38.316 0.50 44.92 ? 5   GLU A OE2 1 
ATOM   39   O OE2 B GLU A 1 6   ? 29.299 -4.980  41.522 0.50 52.33 ? 5   GLU A OE2 1 
ATOM   40   N N   . LYS A 1 7   ? 26.051 -0.856  39.471 1.00 37.05 ? 6   LYS A N   1 
ATOM   41   C CA  . LYS A 1 7   ? 24.647 -0.443  39.744 1.00 36.75 ? 6   LYS A CA  1 
ATOM   42   C C   . LYS A 1 7   ? 24.128 0.504   38.664 1.00 35.67 ? 6   LYS A C   1 
ATOM   43   O O   . LYS A 1 7   ? 22.916 0.517   38.445 1.00 34.64 ? 6   LYS A O   1 
ATOM   44   C CB  . LYS A 1 7   ? 24.500 0.230   41.114 1.00 38.38 ? 6   LYS A CB  1 
ATOM   45   C CG  . LYS A 1 7   ? 24.678 -0.714  42.301 1.00 47.60 ? 6   LYS A CG  1 
ATOM   46   N N   . LEU A 1 8   ? 24.999 1.270   37.997 1.00 31.05 ? 7   LEU A N   1 
ATOM   47   C CA  . LEU A 1 8   ? 24.551 2.187   36.919 1.00 31.67 ? 7   LEU A CA  1 
ATOM   48   C C   . LEU A 1 8   ? 24.028 1.437   35.703 1.00 28.86 ? 7   LEU A C   1 
ATOM   49   O O   . LEU A 1 8   ? 23.380 2.112   34.861 1.00 31.21 ? 7   LEU A O   1 
ATOM   50   C CB  . LEU A 1 8   ? 25.694 3.120   36.512 1.00 32.35 ? 7   LEU A CB  1 
ATOM   51   C CG  . LEU A 1 8   ? 26.167 4.101   37.591 1.00 35.25 ? 7   LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 8   ? 27.433 4.827   37.156 1.00 36.49 ? 7   LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 8   ? 25.066 5.098   37.891 1.00 40.60 ? 7   LEU A CD2 1 
ATOM   54   N N   . PHE A 1 9   ? 24.272 0.135   35.572 1.00 30.29 ? 8   PHE A N   1 
ATOM   55   C CA  . PHE A 1 9   ? 23.967 -0.612  34.321 1.00 30.65 ? 8   PHE A CA  1 
ATOM   56   C C   . PHE A 1 9   ? 22.869 -1.662  34.534 1.00 33.59 ? 8   PHE A C   1 
ATOM   57   O O   . PHE A 1 9   ? 22.711 -2.519  33.650 1.00 34.24 ? 8   PHE A O   1 
ATOM   58   C CB  . PHE A 1 9   ? 25.250 -1.265  33.814 1.00 30.64 ? 8   PHE A CB  1 
ATOM   59   C CG  . PHE A 1 9   ? 26.245 -0.256  33.295 1.00 28.41 ? 8   PHE A CG  1 
ATOM   60   C CD1 . PHE A 1 9   ? 26.191 0.145   31.981 1.00 29.19 ? 8   PHE A CD1 1 
ATOM   61   C CD2 . PHE A 1 9   ? 27.204 0.285   34.128 1.00 29.06 ? 8   PHE A CD2 1 
ATOM   62   C CE1 . PHE A 1 9   ? 27.105 1.053   31.480 1.00 30.71 ? 8   PHE A CE1 1 
ATOM   63   C CE2 . PHE A 1 9   ? 28.093 1.213   33.637 1.00 28.37 ? 8   PHE A CE2 1 
ATOM   64   C CZ  . PHE A 1 9   ? 28.046 1.585   32.318 1.00 29.16 ? 8   PHE A CZ  1 
ATOM   65   N N   . THR A 1 10  ? 22.209 -1.675  35.685 1.00 32.35 ? 9   THR A N   1 
ATOM   66   C CA  . THR A 1 10  ? 21.223 -2.760  35.986 1.00 35.45 ? 9   THR A CA  1 
ATOM   67   C C   . THR A 1 10  ? 19.961 -2.619  35.130 1.00 36.49 ? 9   THR A C   1 
ATOM   68   O O   . THR A 1 10  ? 19.219 -3.638  35.007 1.00 36.08 ? 9   THR A O   1 
ATOM   69   C CB  . THR A 1 10  ? 20.928 -2.818  37.485 1.00 38.04 ? 9   THR A CB  1 
ATOM   70   O OG1 . THR A 1 10  ? 20.389 -1.542  37.836 1.00 36.74 ? 9   THR A OG1 1 
ATOM   71   C CG2 . THR A 1 10  ? 22.150 -3.179  38.294 1.00 39.31 ? 9   THR A CG2 1 
ATOM   72   N N   . GLY A 1 11  ? 19.672 -1.428  34.618 1.00 36.55 ? 10  GLY A N   1 
ATOM   73   C CA  . GLY A 1 11  ? 18.511 -1.190  33.762 1.00 34.57 ? 10  GLY A CA  1 
ATOM   74   C C   . GLY A 1 11  ? 18.898 -0.833  32.363 1.00 34.39 ? 10  GLY A C   1 
ATOM   75   O O   . GLY A 1 11  ? 20.076 -1.085  31.939 1.00 33.30 ? 10  GLY A O   1 
ATOM   76   N N   . VAL A 1 12  ? 17.956 -0.216  31.669 1.00 34.03 ? 11  VAL A N   1 
ATOM   77   C CA  . VAL A 1 12  ? 18.173 0.217   30.264 1.00 34.54 ? 11  VAL A CA  1 
ATOM   78   C C   . VAL A 1 12  ? 18.771 1.615   30.324 1.00 34.56 ? 11  VAL A C   1 
ATOM   79   O O   . VAL A 1 12  ? 18.178 2.501   30.973 1.00 35.21 ? 11  VAL A O   1 
ATOM   80   C CB  . VAL A 1 12  ? 16.889 0.186   29.432 1.00 36.23 ? 11  VAL A CB  1 
ATOM   81   C CG1 . VAL A 1 12  ? 17.107 0.723   28.039 1.00 36.30 ? 11  VAL A CG1 1 
ATOM   82   C CG2 . VAL A 1 12  ? 16.346 -1.227  29.384 1.00 36.72 ? 11  VAL A CG2 1 
ATOM   83   N N   . VAL A 1 13  ? 19.891 1.798   29.647 1.00 29.15 ? 12  VAL A N   1 
ATOM   84   C CA  . VAL A 1 13  ? 20.706 3.049   29.699 1.00 29.79 ? 12  VAL A CA  1 
ATOM   85   C C   . VAL A 1 13  ? 20.708 3.709   28.329 1.00 28.14 ? 12  VAL A C   1 
ATOM   86   O O   . VAL A 1 13  ? 21.088 3.115   27.321 1.00 28.82 ? 12  VAL A O   1 
ATOM   87   C CB  . VAL A 1 13  ? 22.142 2.740   30.141 1.00 27.92 ? 12  VAL A CB  1 
ATOM   88   C CG1 . VAL A 1 13  ? 23.027 3.977   30.047 1.00 28.50 ? 12  VAL A CG1 1 
ATOM   89   C CG2 . VAL A 1 13  ? 22.161 2.159   31.536 1.00 30.63 ? 12  VAL A CG2 1 
ATOM   90   N N   . PRO A 1 14  ? 20.325 5.003   28.220 1.00 28.57 ? 13  PRO A N   1 
ATOM   91   C CA  . PRO A 1 14  ? 20.400 5.691   26.938 1.00 28.62 ? 13  PRO A CA  1 
ATOM   92   C C   . PRO A 1 14  ? 21.865 5.889   26.522 1.00 29.13 ? 13  PRO A C   1 
ATOM   93   O O   . PRO A 1 14  ? 22.697 6.180   27.390 1.00 29.44 ? 13  PRO A O   1 
ATOM   94   C CB  . PRO A 1 14  ? 19.750 7.055   27.178 1.00 31.01 ? 13  PRO A CB  1 
ATOM   95   C CG  . PRO A 1 14  ? 19.017 6.899   28.497 1.00 32.60 ? 13  PRO A CG  1 
ATOM   96   C CD  . PRO A 1 14  ? 19.746 5.838   29.277 1.00 31.18 ? 13  PRO A CD  1 
ATOM   97   N N   . ILE A 1 15  ? 22.118 5.743   25.230 1.00 27.81 ? 14  ILE A N   1 
ATOM   98   C CA  . ILE A 1 15  ? 23.470 5.860   24.600 1.00 27.76 ? 14  ILE A CA  1 
ATOM   99   C C   . ILE A 1 15  ? 23.486 7.026   23.614 1.00 29.47 ? 14  ILE A C   1 
ATOM   100  O O   . ILE A 1 15  ? 22.518 7.168   22.788 1.00 29.13 ? 14  ILE A O   1 
ATOM   101  C CB  . ILE A 1 15  ? 23.860 4.534   23.910 1.00 29.54 ? 14  ILE A CB  1 
ATOM   102  C CG1 . ILE A 1 15  ? 23.991 3.419   24.942 1.00 29.47 ? 14  ILE A CG1 1 
ATOM   103  C CG2 . ILE A 1 15  ? 25.121 4.697   23.062 1.00 29.83 ? 14  ILE A CG2 1 
ATOM   104  C CD1 . ILE A 1 15  ? 24.164 2.068   24.306 1.00 29.33 ? 14  ILE A CD1 1 
ATOM   105  N N   . LEU A 1 16  ? 24.557 7.818   23.673 1.00 27.37 ? 15  LEU A N   1 
ATOM   106  C CA  . LEU A 1 16  ? 24.857 8.844   22.677 1.00 27.93 ? 15  LEU A CA  1 
ATOM   107  C C   . LEU A 1 16  ? 26.289 8.637   22.221 1.00 29.59 ? 15  LEU A C   1 
ATOM   108  O O   . LEU A 1 16  ? 27.187 8.530   23.066 1.00 29.75 ? 15  LEU A O   1 
ATOM   109  C CB  . LEU A 1 16  ? 24.681 10.228  23.305 1.00 28.47 ? 15  LEU A CB  1 
ATOM   110  C CG  . LEU A 1 16  ? 24.923 11.389  22.356 1.00 29.69 ? 15  LEU A CG  1 
ATOM   111  C CD1 . LEU A 1 16  ? 23.832 11.435  21.284 1.00 34.98 ? 15  LEU A CD1 1 
ATOM   112  C CD2 . LEU A 1 16  ? 25.018 12.693  23.148 1.00 31.38 ? 15  LEU A CD2 1 
ATOM   113  N N   . VAL A 1 17  ? 26.493 8.586   20.924 1.00 28.30 ? 16  VAL A N   1 
ATOM   114  C CA  . VAL A 1 17  ? 27.846 8.464   20.337 1.00 28.20 ? 16  VAL A CA  1 
ATOM   115  C C   . VAL A 1 17  ? 28.111 9.643   19.401 1.00 30.75 ? 16  VAL A C   1 
ATOM   116  O O   . VAL A 1 17  ? 27.239 10.006  18.582 1.00 30.75 ? 16  VAL A O   1 
ATOM   117  C CB  . VAL A 1 17  ? 28.012 7.122   19.599 1.00 28.48 ? 16  VAL A CB  1 
ATOM   118  C CG1 . VAL A 1 17  ? 29.427 6.983   19.052 1.00 30.03 ? 16  VAL A CG1 1 
ATOM   119  C CG2 . VAL A 1 17  ? 27.606 5.974   20.510 1.00 28.62 ? 16  VAL A CG2 1 
ATOM   120  N N   . GLU A 1 18  ? 29.309 10.200  19.483 1.00 28.86 ? 17  GLU A N   1 
ATOM   121  C CA  A GLU A 1 18  ? 29.754 11.287  18.576 0.50 29.54 ? 17  GLU A CA  1 
ATOM   122  C CA  B GLU A 1 18  ? 29.763 11.268  18.565 0.50 30.55 ? 17  GLU A CA  1 
ATOM   123  C C   . GLU A 1 18  ? 31.144 10.903  18.059 1.00 30.95 ? 17  GLU A C   1 
ATOM   124  O O   . GLU A 1 18  ? 31.984 10.569  18.901 1.00 30.90 ? 17  GLU A O   1 
ATOM   125  C CB  A GLU A 1 18  ? 29.704 12.640  19.298 0.50 30.99 ? 17  GLU A CB  1 
ATOM   126  C CB  B GLU A 1 18  ? 29.811 12.604  19.287 0.50 33.37 ? 17  GLU A CB  1 
ATOM   127  C CG  A GLU A 1 18  ? 28.411 12.915  20.088 0.50 30.31 ? 17  GLU A CG  1 
ATOM   128  C CG  B GLU A 1 18  ? 28.436 13.137  19.609 0.50 34.52 ? 17  GLU A CG  1 
ATOM   129  C CD  A GLU A 1 18  ? 27.151 13.289  19.302 0.50 31.22 ? 17  GLU A CD  1 
ATOM   130  C CD  B GLU A 1 18  ? 28.532 14.488  20.273 0.50 39.38 ? 17  GLU A CD  1 
ATOM   131  O OE1 A GLU A 1 18  ? 27.232 13.433  18.063 0.50 29.83 ? 17  GLU A OE1 1 
ATOM   132  O OE1 B GLU A 1 18  ? 29.588 14.751  20.902 0.50 37.63 ? 17  GLU A OE1 1 
ATOM   133  O OE2 A GLU A 1 18  ? 26.058 13.440  19.937 0.50 31.54 ? 17  GLU A OE2 1 
ATOM   134  O OE2 B GLU A 1 18  ? 27.578 15.269  20.135 0.50 38.52 ? 17  GLU A OE2 1 
ATOM   135  N N   . LEU A 1 19  ? 31.327 10.942  16.749 1.00 30.74 ? 18  LEU A N   1 
ATOM   136  C CA  . LEU A 1 19  ? 32.639 10.648  16.120 1.00 32.07 ? 18  LEU A CA  1 
ATOM   137  C C   . LEU A 1 19  ? 32.967 11.769  15.137 1.00 33.86 ? 18  LEU A C   1 
ATOM   138  O O   . LEU A 1 19  ? 32.146 12.070  14.239 1.00 34.52 ? 18  LEU A O   1 
ATOM   139  C CB  . LEU A 1 19  ? 32.609 9.302   15.411 1.00 31.93 ? 18  LEU A CB  1 
ATOM   140  C CG  . LEU A 1 19  ? 33.946 8.880   14.787 1.00 35.92 ? 18  LEU A CG  1 
ATOM   141  C CD1 . LEU A 1 19  ? 34.102 7.372   14.785 1.00 39.93 ? 18  LEU A CD1 1 
ATOM   142  C CD2 . LEU A 1 19  ? 34.070 9.423   13.390 1.00 39.93 ? 18  LEU A CD2 1 
ATOM   143  N N   . ASP A 1 20  ? 34.133 12.367  15.315 1.00 31.36 ? 19  ASP A N   1 
ATOM   144  C CA  . ASP A 1 20  ? 34.754 13.276  14.318 1.00 35.96 ? 19  ASP A CA  1 
ATOM   145  C C   . ASP A 1 20  ? 35.927 12.539  13.689 1.00 33.61 ? 19  ASP A C   1 
ATOM   146  O O   . ASP A 1 20  ? 36.794 12.060  14.442 1.00 34.20 ? 19  ASP A O   1 
ATOM   147  C CB  . ASP A 1 20  ? 35.204 14.584  14.960 1.00 40.49 ? 19  ASP A CB  1 
ATOM   148  C CG  . ASP A 1 20  ? 34.102 15.625  15.173 1.00 54.94 ? 19  ASP A CG  1 
ATOM   149  O OD1 . ASP A 1 20  ? 33.015 15.653  14.423 1.00 41.97 ? 19  ASP A OD1 1 
ATOM   150  O OD2 . ASP A 1 20  ? 34.313 16.418  16.108 1.00 64.17 ? 19  ASP A OD2 1 
ATOM   151  N N   . GLY A 1 21  ? 35.907 12.371  12.369 1.00 32.73 ? 20  GLY A N   1 
ATOM   152  C CA  . GLY A 1 21  ? 36.871 11.553  11.622 1.00 34.10 ? 20  GLY A CA  1 
ATOM   153  C C   . GLY A 1 21  ? 37.611 12.356  10.564 1.00 36.00 ? 20  GLY A C   1 
ATOM   154  O O   . GLY A 1 21  ? 37.063 13.343  10.046 1.00 36.14 ? 20  GLY A O   1 
ATOM   155  N N   . ASP A 1 22  ? 38.831 11.933  10.287 1.00 35.45 ? 21  ASP A N   1 
ATOM   156  C CA  . ASP A 1 22  ? 39.674 12.472  9.192  1.00 37.05 ? 21  ASP A CA  1 
ATOM   157  C C   . ASP A 1 22  ? 40.479 11.304  8.652  1.00 36.08 ? 21  ASP A C   1 
ATOM   158  O O   . ASP A 1 22  ? 41.333 10.771  9.403  1.00 40.40 ? 21  ASP A O   1 
ATOM   159  C CB  . ASP A 1 22  ? 40.527 13.635  9.688  1.00 38.84 ? 21  ASP A CB  1 
ATOM   160  C CG  . ASP A 1 22  ? 41.383 14.215  8.568  1.00 44.27 ? 21  ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 22  ? 41.783 13.438  7.653  1.00 47.57 ? 21  ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 22  ? 41.616 15.429  8.609  1.00 51.17 ? 21  ASP A OD2 1 
ATOM   163  N N   . VAL A 1 23  ? 40.180 10.861  7.428  1.00 35.90 ? 22  VAL A N   1 
ATOM   164  C CA  . VAL A 1 23  ? 40.886 9.731   6.777  1.00 37.77 ? 22  VAL A CA  1 
ATOM   165  C C   . VAL A 1 23  ? 41.458 10.285  5.464  1.00 38.23 ? 22  VAL A C   1 
ATOM   166  O O   . VAL A 1 23  ? 40.667 10.624  4.585  1.00 40.30 ? 22  VAL A O   1 
ATOM   167  C CB  . VAL A 1 23  ? 39.990 8.490   6.561  1.00 37.09 ? 22  VAL A CB  1 
ATOM   168  C CG1 . VAL A 1 23  ? 40.752 7.400   5.817  1.00 38.10 ? 22  VAL A CG1 1 
ATOM   169  C CG2 . VAL A 1 23  ? 39.449 7.930   7.882  1.00 40.57 ? 22  VAL A CG2 1 
ATOM   170  N N   . ASN A 1 24  ? 42.785 10.414  5.386  1.00 42.68 ? 23  ASN A N   1 
ATOM   171  C CA  . ASN A 1 24  ? 43.480 10.982  4.201  1.00 44.08 ? 23  ASN A CA  1 
ATOM   172  C C   . ASN A 1 24  ? 42.909 12.378  3.903  1.00 44.86 ? 23  ASN A C   1 
ATOM   173  O O   . ASN A 1 24  ? 42.756 12.698  2.726  1.00 47.67 ? 23  ASN A O   1 
ATOM   174  C CB  . ASN A 1 24  ? 43.361 10.038  3.004  1.00 44.13 ? 23  ASN A CB  1 
ATOM   175  C CG  . ASN A 1 24  ? 44.326 8.868   3.018  1.00 46.21 ? 23  ASN A CG  1 
ATOM   176  O OD1 . ASN A 1 24  ? 44.779 8.410   4.061  1.00 42.86 ? 23  ASN A OD1 1 
ATOM   177  N ND2 . ASN A 1 24  ? 44.620 8.324   1.847  1.00 48.12 ? 23  ASN A ND2 1 
ATOM   178  N N   . GLY A 1 25  ? 42.590 13.180  4.931  1.00 42.23 ? 24  GLY A N   1 
ATOM   179  C CA  . GLY A 1 25  ? 42.050 14.549  4.784  1.00 42.94 ? 24  GLY A CA  1 
ATOM   180  C C   . GLY A 1 25  ? 40.561 14.604  4.448  1.00 42.30 ? 24  GLY A C   1 
ATOM   181  O O   . GLY A 1 25  ? 40.030 15.726  4.342  1.00 44.47 ? 24  GLY A O   1 
ATOM   182  N N   . HIS A 1 26  ? 39.891 13.460  4.259  1.00 42.16 ? 25  HIS A N   1 
ATOM   183  C CA  . HIS A 1 26  ? 38.419 13.366  4.056  1.00 41.78 ? 25  HIS A CA  1 
ATOM   184  C C   . HIS A 1 26  ? 37.778 13.449  5.438  1.00 42.38 ? 25  HIS A C   1 
ATOM   185  O O   . HIS A 1 26  ? 37.937 12.489  6.199  1.00 40.02 ? 25  HIS A O   1 
ATOM   186  C CB  . HIS A 1 26  ? 38.012 12.079  3.337  1.00 45.22 ? 25  HIS A CB  1 
ATOM   187  C CG  . HIS A 1 26  ? 38.693 11.870  2.022  1.00 48.97 ? 25  HIS A CG  1 
ATOM   188  N ND1 . HIS A 1 26  ? 38.358 12.595  0.901  1.00 54.79 ? 25  HIS A ND1 1 
ATOM   189  C CD2 . HIS A 1 26  ? 39.679 11.026  1.643  1.00 53.09 ? 25  HIS A CD2 1 
ATOM   190  C CE1 . HIS A 1 26  ? 39.114 12.214  -0.109 1.00 53.97 ? 25  HIS A CE1 1 
ATOM   191  N NE2 . HIS A 1 26  ? 39.938 11.264  0.319  1.00 54.88 ? 25  HIS A NE2 1 
ATOM   192  N N   . LYS A 1 27  ? 37.185 14.588  5.769  1.00 41.38 ? 26  LYS A N   1 
ATOM   193  C CA  . LYS A 1 27  ? 36.597 14.837  7.101  1.00 42.10 ? 26  LYS A CA  1 
ATOM   194  C C   . LYS A 1 27  ? 35.152 14.359  7.078  1.00 40.06 ? 26  LYS A C   1 
ATOM   195  O O   . LYS A 1 27  ? 34.482 14.430  6.035  1.00 39.71 ? 26  LYS A O   1 
ATOM   196  C CB  . LYS A 1 27  ? 36.708 16.313  7.468  1.00 45.93 ? 26  LYS A CB  1 
ATOM   197  C CG  . LYS A 1 27  ? 38.133 16.772  7.715  1.00 52.22 ? 26  LYS A CG  1 
ATOM   198  C CD  . LYS A 1 27  ? 38.438 18.096  7.082  1.00 62.41 ? 26  LYS A CD  1 
ATOM   199  C CE  . LYS A 1 27  ? 39.924 18.376  7.060  1.00 70.04 ? 26  LYS A CE  1 
ATOM   200  N NZ  . LYS A 1 27  ? 40.458 18.369  8.440  1.00 76.78 ? 26  LYS A NZ  1 
ATOM   201  N N   . PHE A 1 28  ? 34.682 13.832  8.197  1.00 37.74 ? 27  PHE A N   1 
ATOM   202  C CA  . PHE A 1 28  ? 33.295 13.350  8.311  1.00 34.94 ? 27  PHE A CA  1 
ATOM   203  C C   . PHE A 1 28  ? 32.936 13.304  9.791  1.00 33.34 ? 27  PHE A C   1 
ATOM   204  O O   . PHE A 1 28  ? 33.827 13.249  10.626 1.00 34.60 ? 27  PHE A O   1 
ATOM   205  C CB  . PHE A 1 28  ? 33.132 11.970  7.674  1.00 35.17 ? 27  PHE A CB  1 
ATOM   206  C CG  . PHE A 1 28  ? 33.964 10.862  8.268  1.00 35.18 ? 27  PHE A CG  1 
ATOM   207  C CD1 . PHE A 1 28  ? 35.272 10.673  7.870  1.00 36.16 ? 27  PHE A CD1 1 
ATOM   208  C CD2 . PHE A 1 28  ? 33.448 10.007  9.237  1.00 34.55 ? 27  PHE A CD2 1 
ATOM   209  C CE1 . PHE A 1 28  ? 36.056 9.677   8.432  1.00 38.12 ? 27  PHE A CE1 1 
ATOM   210  C CE2 . PHE A 1 28  ? 34.228 9.000   9.785  1.00 33.81 ? 27  PHE A CE2 1 
ATOM   211  C CZ  . PHE A 1 28  ? 35.524 8.822   9.376  1.00 35.18 ? 27  PHE A CZ  1 
ATOM   212  N N   . SER A 1 29  ? 31.656 13.331  10.071 1.00 33.25 ? 28  SER A N   1 
ATOM   213  C CA  . SER A 1 29  ? 31.134 13.188  11.448 1.00 31.44 ? 28  SER A CA  1 
ATOM   214  C C   . SER A 1 29  ? 30.080 12.095  11.445 1.00 32.14 ? 28  SER A C   1 
ATOM   215  O O   . SER A 1 29  ? 29.334 12.003  10.463 1.00 34.63 ? 28  SER A O   1 
ATOM   216  C CB  . SER A 1 29  ? 30.586 14.467  12.003 1.00 34.55 ? 28  SER A CB  1 
ATOM   217  O OG  . SER A 1 29  ? 31.624 15.432  12.096 1.00 37.84 ? 28  SER A OG  1 
ATOM   218  N N   . VAL A 1 30  ? 30.001 11.357  12.557 1.00 30.77 ? 29  VAL A N   1 
ATOM   219  C CA  . VAL A 1 30  ? 28.948 10.326  12.773 1.00 31.01 ? 29  VAL A CA  1 
ATOM   220  C C   . VAL A 1 30  ? 28.312 10.620  14.127 1.00 30.65 ? 29  VAL A C   1 
ATOM   221  O O   . VAL A 1 30  ? 29.033 10.934  15.090 1.00 31.87 ? 29  VAL A O   1 
ATOM   222  C CB  . VAL A 1 30  ? 29.545 8.908   12.699 1.00 31.18 ? 29  VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 30  ? 28.593 7.843   13.217 1.00 29.64 ? 29  VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 30  ? 29.993 8.564   11.292 1.00 32.17 ? 29  VAL A CG2 1 
ATOM   225  N N   . SER A 1 31  ? 27.000 10.504  14.201 1.00 29.49 ? 30  SER A N   1 
ATOM   226  C CA  A SER A 1 31  ? 26.271 10.514  15.485 0.50 29.13 ? 30  SER A CA  1 
ATOM   227  C CA  B SER A 1 31  ? 26.243 10.532  15.471 0.50 31.49 ? 30  SER A CA  1 
ATOM   228  C C   . SER A 1 31  ? 25.584 9.157   15.642 1.00 30.94 ? 30  SER A C   1 
ATOM   229  O O   . SER A 1 31  ? 25.219 8.583   14.645 1.00 30.60 ? 30  SER A O   1 
ATOM   230  C CB  A SER A 1 31  ? 25.273 11.643  15.550 0.50 32.86 ? 30  SER A CB  1 
ATOM   231  C CB  B SER A 1 31  ? 25.221 11.662  15.458 0.50 38.19 ? 30  SER A CB  1 
ATOM   232  O OG  A SER A 1 31  ? 24.371 11.552  14.471 0.50 30.47 ? 30  SER A OG  1 
ATOM   233  O OG  B SER A 1 31  ? 24.644 11.868  16.740 0.50 46.87 ? 30  SER A OG  1 
ATOM   234  N N   . GLY A 1 32  ? 25.427 8.699   16.871 1.00 28.69 ? 31  GLY A N   1 
ATOM   235  C CA  . GLY A 1 32  ? 24.673 7.485   17.155 1.00 28.78 ? 31  GLY A CA  1 
ATOM   236  C C   . GLY A 1 32  ? 23.810 7.654   18.375 1.00 28.87 ? 31  GLY A C   1 
ATOM   237  O O   . GLY A 1 32  ? 24.168 8.415   19.306 1.00 30.42 ? 31  GLY A O   1 
ATOM   238  N N   . GLU A 1 33  ? 22.719 6.913   18.387 1.00 27.99 ? 32  GLU A N   1 
ATOM   239  C CA  A GLU A 1 33  ? 21.776 6.865   19.542 0.25 26.90 ? 32  GLU A CA  1 
ATOM   240  C CA  B GLU A 1 33  ? 21.843 6.835   19.577 0.25 25.98 ? 32  GLU A CA  1 
ATOM   241  C CA  C GLU A 1 33  ? 21.773 6.870   19.526 0.50 28.72 ? 32  GLU A CA  1 
ATOM   242  C C   . GLU A 1 33  ? 21.304 5.419   19.726 1.00 28.37 ? 32  GLU A C   1 
ATOM   243  O O   . GLU A 1 33  ? 21.272 4.676   18.752 1.00 31.31 ? 32  GLU A O   1 
ATOM   244  C CB  A GLU A 1 33  ? 20.583 7.843   19.429 0.25 26.73 ? 32  GLU A CB  1 
ATOM   245  C CB  B GLU A 1 33  ? 20.691 7.824   19.456 0.25 25.14 ? 32  GLU A CB  1 
ATOM   246  C CB  C GLU A 1 33  ? 20.642 7.881   19.255 0.50 34.55 ? 32  GLU A CB  1 
ATOM   247  C CG  A GLU A 1 33  ? 19.724 7.780   18.157 0.25 25.16 ? 32  GLU A CG  1 
ATOM   248  C CG  B GLU A 1 33  ? 21.177 9.254   19.388 0.25 22.24 ? 32  GLU A CG  1 
ATOM   249  C CG  C GLU A 1 33  ? 19.489 7.400   18.369 0.50 39.14 ? 32  GLU A CG  1 
ATOM   250  C CD  A GLU A 1 33  ? 18.257 8.221   18.324 0.25 24.52 ? 32  GLU A CD  1 
ATOM   251  C CD  B GLU A 1 33  ? 20.023 10.215  19.335 0.25 22.21 ? 32  GLU A CD  1 
ATOM   252  C CD  C GLU A 1 33  ? 19.473 7.567   16.845 0.50 46.45 ? 32  GLU A CD  1 
ATOM   253  O OE1 A GLU A 1 33  ? 17.728 8.048   19.410 0.25 24.97 ? 32  GLU A OE1 1 
ATOM   254  O OE1 B GLU A 1 33  ? 18.906 9.739   19.582 0.25 22.97 ? 32  GLU A OE1 1 
ATOM   255  O OE1 C GLU A 1 33  ? 20.570 7.735   16.204 0.50 44.49 ? 32  GLU A OE1 1 
ATOM   256  O OE2 A GLU A 1 33  ? 17.624 8.695   17.368 0.25 20.40 ? 32  GLU A OE2 1 
ATOM   257  O OE2 B GLU A 1 33  ? 20.263 11.412  19.075 0.25 18.06 ? 32  GLU A OE2 1 
ATOM   258  O OE2 C GLU A 1 33  ? 18.325 7.474   16.269 0.50 43.24 ? 32  GLU A OE2 1 
ATOM   259  N N   . GLY A 1 34  ? 20.916 5.097   20.936 1.00 29.05 ? 33  GLY A N   1 
ATOM   260  C CA  . GLY A 1 34  ? 20.321 3.791   21.206 1.00 30.23 ? 33  GLY A CA  1 
ATOM   261  C C   . GLY A 1 34  ? 20.211 3.560   22.668 1.00 30.43 ? 33  GLY A C   1 
ATOM   262  O O   . GLY A 1 34  ? 20.129 4.524   23.437 1.00 29.50 ? 33  GLY A O   1 
ATOM   263  N N   . GLU A 1 35  ? 20.221 2.283   23.036 1.00 29.07 ? 34  GLU A N   1 
ATOM   264  C CA  . GLU A 1 35  ? 19.991 1.860   24.432 1.00 29.78 ? 34  GLU A CA  1 
ATOM   265  C C   . GLU A 1 35  ? 20.891 0.673   24.719 1.00 30.80 ? 34  GLU A C   1 
ATOM   266  O O   . GLU A 1 35  ? 20.986 -0.203  23.860 1.00 31.57 ? 34  GLU A O   1 
ATOM   267  C CB  . GLU A 1 35  ? 18.549 1.388   24.664 1.00 35.09 ? 34  GLU A CB  1 
ATOM   268  C CG  . GLU A 1 35  ? 17.523 2.456   24.491 1.00 42.29 ? 34  GLU A CG  1 
ATOM   269  C CD  . GLU A 1 35  ? 16.153 1.973   24.933 1.00 46.69 ? 34  GLU A CD  1 
ATOM   270  O OE1 . GLU A 1 35  ? 15.835 0.761   24.735 1.00 45.31 ? 34  GLU A OE1 1 
ATOM   271  O OE2 . GLU A 1 35  ? 15.438 2.783   25.530 1.00 56.60 ? 34  GLU A OE2 1 
ATOM   272  N N   . GLY A 1 36  ? 21.443 0.635   25.920 1.00 28.17 ? 35  GLY A N   1 
ATOM   273  C CA  . GLY A 1 36  ? 22.204 -0.505  26.441 1.00 29.52 ? 35  GLY A CA  1 
ATOM   274  C C   . GLY A 1 36  ? 21.497 -1.172  27.594 1.00 31.40 ? 35  GLY A C   1 
ATOM   275  O O   . GLY A 1 36  ? 20.983 -0.486  28.505 1.00 29.48 ? 35  GLY A O   1 
ATOM   276  N N   . ASP A 1 37  ? 21.526 -2.495  27.608 1.00 30.51 ? 36  ASP A N   1 
ATOM   277  C CA  . ASP A 1 37  ? 20.901 -3.344  28.642 1.00 30.58 ? 36  ASP A CA  1 
ATOM   278  C C   . ASP A 1 37  ? 21.947 -4.392  29.030 1.00 30.28 ? 36  ASP A C   1 
ATOM   279  O O   . ASP A 1 37  ? 21.877 -5.527  28.508 1.00 30.44 ? 36  ASP A O   1 
ATOM   280  C CB  . ASP A 1 37  ? 19.595 -3.921  28.104 1.00 31.61 ? 36  ASP A CB  1 
ATOM   281  C CG  . ASP A 1 37  ? 18.586 -4.410  29.137 1.00 35.44 ? 36  ASP A CG  1 
ATOM   282  O OD1 . ASP A 1 37  ? 18.878 -4.385  30.365 1.00 35.52 ? 36  ASP A OD1 1 
ATOM   283  O OD2 . ASP A 1 37  ? 17.467 -4.808  28.679 1.00 36.08 ? 36  ASP A OD2 1 
ATOM   284  N N   . ALA A 1 38  ? 22.922 -4.002  29.835 1.00 28.03 ? 37  ALA A N   1 
ATOM   285  C CA  . ALA A 1 38  ? 24.121 -4.819  30.152 1.00 28.71 ? 37  ALA A CA  1 
ATOM   286  C C   . ALA A 1 38  ? 23.722 -6.122  30.859 1.00 29.85 ? 37  ALA A C   1 
ATOM   287  O O   . ALA A 1 38  ? 24.487 -7.102  30.794 1.00 30.16 ? 37  ALA A O   1 
ATOM   288  C CB  . ALA A 1 38  ? 25.080 -4.039  30.998 1.00 29.41 ? 37  ALA A CB  1 
ATOM   289  N N   . THR A 1 39  ? 22.556 -6.139  31.502 1.00 31.35 ? 38  THR A N   1 
ATOM   290  C CA  . THR A 1 39  ? 22.072 -7.353  32.181 1.00 33.28 ? 38  THR A CA  1 
ATOM   291  C C   . THR A 1 39  ? 22.028 -8.484  31.149 1.00 33.65 ? 38  THR A C   1 
ATOM   292  O O   . THR A 1 39  ? 22.302 -9.629  31.544 1.00 32.04 ? 38  THR A O   1 
ATOM   293  C CB  . THR A 1 39  ? 20.711 -7.125  32.855 1.00 37.49 ? 38  THR A CB  1 
ATOM   294  O OG1 . THR A 1 39  ? 20.916 -6.078  33.805 1.00 36.07 ? 38  THR A OG1 1 
ATOM   295  C CG2 . THR A 1 39  ? 20.246 -8.376  33.574 1.00 37.91 ? 38  THR A CG2 1 
ATOM   296  N N   . TYR A 1 40  ? 21.668 -8.172  29.903 1.00 30.24 ? 39  TYR A N   1 
ATOM   297  C CA  . TYR A 1 40  ? 21.566 -9.152  28.791 1.00 33.27 ? 39  TYR A CA  1 
ATOM   298  C C   . TYR A 1 40  ? 22.690 -8.968  27.780 1.00 32.52 ? 39  TYR A C   1 
ATOM   299  O O   . TYR A 1 40  ? 22.650 -9.609  26.711 1.00 33.82 ? 39  TYR A O   1 
ATOM   300  C CB  . TYR A 1 40  ? 20.175 -9.040  28.166 1.00 32.48 ? 39  TYR A CB  1 
ATOM   301  C CG  . TYR A 1 40  ? 19.144 -9.183  29.236 1.00 35.71 ? 39  TYR A CG  1 
ATOM   302  C CD1 . TYR A 1 40  ? 18.862 -10.432 29.768 1.00 34.87 ? 39  TYR A CD1 1 
ATOM   303  C CD2 . TYR A 1 40  ? 18.545 -8.070  29.792 1.00 36.78 ? 39  TYR A CD2 1 
ATOM   304  C CE1 . TYR A 1 40  ? 17.969 -10.570 30.810 1.00 36.98 ? 39  TYR A CE1 1 
ATOM   305  C CE2 . TYR A 1 40  ? 17.658 -8.183  30.844 1.00 39.03 ? 39  TYR A CE2 1 
ATOM   306  C CZ  . TYR A 1 40  ? 17.353 -9.441  31.334 1.00 40.51 ? 39  TYR A CZ  1 
ATOM   307  O OH  . TYR A 1 40  ? 16.463 -9.545  32.358 1.00 45.13 ? 39  TYR A OH  1 
ATOM   308  N N   . GLY A 1 41  ? 23.649 -8.072  28.057 1.00 29.89 ? 40  GLY A N   1 
ATOM   309  C CA  . GLY A 1 41  ? 24.770 -7.793  27.145 1.00 30.22 ? 40  GLY A CA  1 
ATOM   310  C C   . GLY A 1 41  ? 24.339 -7.084  25.878 1.00 28.45 ? 40  GLY A C   1 
ATOM   311  O O   . GLY A 1 41  ? 25.065 -7.164  24.888 1.00 29.53 ? 40  GLY A O   1 
ATOM   312  N N   . LYS A 1 42  ? 23.208 -6.396  25.899 1.00 27.66 ? 41  LYS A N   1 
ATOM   313  C CA  . LYS A 1 42  ? 22.513 -5.933  24.679 1.00 28.72 ? 41  LYS A CA  1 
ATOM   314  C C   . LYS A 1 42  ? 22.768 -4.451  24.412 1.00 28.41 ? 41  LYS A C   1 
ATOM   315  O O   . LYS A 1 42  ? 22.619 -3.633  25.339 1.00 29.97 ? 41  LYS A O   1 
ATOM   316  C CB  . LYS A 1 42  ? 21.003 -6.156  24.840 1.00 31.56 ? 41  LYS A CB  1 
ATOM   317  C CG  . LYS A 1 42  ? 20.178 -5.794  23.635 1.00 34.89 ? 41  LYS A CG  1 
ATOM   318  C CD  . LYS A 1 42  ? 18.715 -6.175  23.832 1.00 41.70 ? 41  LYS A CD  1 
ATOM   319  C CE  . LYS A 1 42  ? 17.834 -5.588  22.757 1.00 51.52 ? 41  LYS A CE  1 
ATOM   320  N NZ  . LYS A 1 42  ? 16.460 -5.341  23.250 1.00 57.56 ? 41  LYS A NZ  1 
ATOM   321  N N   . MET A 1 43  ? 23.086 -4.123  23.150 1.00 27.89 ? 42  MET A N   1 
ATOM   322  C CA  . MET A 1 43  ? 22.964 -2.728  22.672 1.00 28.72 ? 42  MET A CA  1 
ATOM   323  C C   . MET A 1 43  ? 22.160 -2.678  21.382 1.00 28.76 ? 42  MET A C   1 
ATOM   324  O O   . MET A 1 43  ? 22.373 -3.501  20.511 1.00 28.34 ? 42  MET A O   1 
ATOM   325  C CB  . MET A 1 43  ? 24.343 -2.133  22.410 1.00 27.53 ? 42  MET A CB  1 
ATOM   326  C CG  . MET A 1 43  ? 25.163 -1.981  23.669 1.00 28.82 ? 42  MET A CG  1 
ATOM   327  S SD  . MET A 1 43  ? 26.820 -1.311  23.278 1.00 32.06 ? 42  MET A SD  1 
ATOM   328  C CE  . MET A 1 43  ? 27.480 -2.708  22.371 1.00 33.97 ? 42  MET A CE  1 
ATOM   329  N N   . SER A 1 44  ? 21.253 -1.721  21.306 1.00 28.59 ? 43  SER A N   1 
ATOM   330  C CA  A SER A 1 44  ? 20.454 -1.403  20.103 0.50 29.03 ? 43  SER A CA  1 
ATOM   331  C CA  B SER A 1 44  ? 20.448 -1.406  20.105 0.50 29.19 ? 43  SER A CA  1 
ATOM   332  C C   . SER A 1 44  ? 20.874 0.007   19.684 1.00 29.84 ? 43  SER A C   1 
ATOM   333  O O   . SER A 1 44  ? 20.714 0.911   20.497 1.00 33.77 ? 43  SER A O   1 
ATOM   334  C CB  A SER A 1 44  ? 18.985 -1.493  20.396 0.50 32.25 ? 43  SER A CB  1 
ATOM   335  C CB  B SER A 1 44  ? 18.965 -1.505  20.398 0.50 32.59 ? 43  SER A CB  1 
ATOM   336  O OG  A SER A 1 44  ? 18.688 -2.765  20.922 0.50 33.09 ? 43  SER A OG  1 
ATOM   337  O OG  B SER A 1 44  ? 18.204 -1.136  19.257 0.50 34.07 ? 43  SER A OG  1 
ATOM   338  N N   . LEU A 1 45  ? 21.427 0.149   18.493 1.00 29.37 ? 44  LEU A N   1 
ATOM   339  C CA  . LEU A 1 45  ? 22.081 1.406   18.073 1.00 29.81 ? 44  LEU A CA  1 
ATOM   340  C C   . LEU A 1 45  ? 21.694 1.773   16.637 1.00 32.79 ? 44  LEU A C   1 
ATOM   341  O O   . LEU A 1 45  ? 21.577 0.875   15.785 1.00 32.85 ? 44  LEU A O   1 
ATOM   342  C CB  . LEU A 1 45  ? 23.587 1.188   18.152 1.00 32.59 ? 44  LEU A CB  1 
ATOM   343  C CG  . LEU A 1 45  ? 24.115 0.843   19.539 1.00 33.03 ? 44  LEU A CG  1 
ATOM   344  C CD1 . LEU A 1 45  ? 25.489 0.245   19.404 1.00 37.23 ? 44  LEU A CD1 1 
ATOM   345  C CD2 . LEU A 1 45  ? 24.129 2.073   20.412 1.00 38.31 ? 44  LEU A CD2 1 
ATOM   346  N N   . LYS A 1 46  ? 21.605 3.070   16.361 1.00 31.07 ? 45  LYS A N   1 
ATOM   347  C CA  . LYS A 1 46  ? 21.531 3.577   14.980 1.00 31.50 ? 45  LYS A CA  1 
ATOM   348  C C   . LYS A 1 46  ? 22.547 4.709   14.814 1.00 31.86 ? 45  LYS A C   1 
ATOM   349  O O   . LYS A 1 46  ? 22.540 5.607   15.650 1.00 31.26 ? 45  LYS A O   1 
ATOM   350  C CB  . LYS A 1 46  ? 20.118 4.060   14.674 1.00 30.56 ? 45  LYS A CB  1 
ATOM   351  C CG  . LYS A 1 46  ? 20.014 4.666   13.285 1.00 32.14 ? 45  LYS A CG  1 
ATOM   352  C CD  . LYS A 1 46  ? 18.626 5.047   12.881 1.00 32.90 ? 45  LYS A CD  1 
ATOM   353  C CE  . LYS A 1 46  ? 18.606 5.800   11.566 1.00 33.05 ? 45  LYS A CE  1 
ATOM   354  N NZ  . LYS A 1 46  ? 17.216 6.245   11.276 1.00 33.72 ? 45  LYS A NZ  1 
ATOM   355  N N   . PHE A 1 47  ? 23.378 4.629   13.789 1.00 29.05 ? 46  PHE A N   1 
ATOM   356  C CA  . PHE A 1 47  ? 24.431 5.615   13.472 1.00 30.56 ? 46  PHE A CA  1 
ATOM   357  C C   . PHE A 1 47  ? 24.093 6.304   12.157 1.00 32.81 ? 46  PHE A C   1 
ATOM   358  O O   . PHE A 1 47  ? 23.665 5.645   11.201 1.00 33.22 ? 46  PHE A O   1 
ATOM   359  C CB  . PHE A 1 47  ? 25.815 4.970   13.370 1.00 30.52 ? 46  PHE A CB  1 
ATOM   360  C CG  . PHE A 1 47  ? 26.258 4.343   14.661 1.00 29.37 ? 46  PHE A CG  1 
ATOM   361  C CD1 . PHE A 1 47  ? 26.825 5.091   15.669 1.00 30.06 ? 46  PHE A CD1 1 
ATOM   362  C CD2 . PHE A 1 47  ? 26.051 2.987   14.877 1.00 30.20 ? 46  PHE A CD2 1 
ATOM   363  C CE1 . PHE A 1 47  ? 27.216 4.518   16.873 1.00 29.59 ? 46  PHE A CE1 1 
ATOM   364  C CE2 . PHE A 1 47  ? 26.390 2.426   16.105 1.00 30.77 ? 46  PHE A CE2 1 
ATOM   365  C CZ  . PHE A 1 47  ? 26.991 3.177   17.088 1.00 30.70 ? 46  PHE A CZ  1 
ATOM   366  N N   . ILE A 1 48  ? 24.364 7.611   12.123 1.00 32.00 ? 47  ILE A N   1 
ATOM   367  C CA  A ILE A 1 48  ? 24.113 8.466   10.923 0.50 33.05 ? 47  ILE A CA  1 
ATOM   368  C CA  B ILE A 1 48  ? 24.113 8.463   10.923 0.50 33.16 ? 47  ILE A CA  1 
ATOM   369  C C   . ILE A 1 48  ? 25.406 9.205   10.588 1.00 32.15 ? 47  ILE A C   1 
ATOM   370  O O   . ILE A 1 48  ? 26.080 9.685   11.523 1.00 31.41 ? 47  ILE A O   1 
ATOM   371  C CB  A ILE A 1 48  ? 22.937 9.432   11.180 0.50 36.79 ? 47  ILE A CB  1 
ATOM   372  C CB  B ILE A 1 48  ? 22.916 9.416   11.154 0.50 36.94 ? 47  ILE A CB  1 
ATOM   373  C CG1 A ILE A 1 48  ? 21.602 8.686   11.202 0.50 38.67 ? 47  ILE A CG1 1 
ATOM   374  C CG1 B ILE A 1 48  ? 23.113 10.346  12.353 0.50 38.98 ? 47  ILE A CG1 1 
ATOM   375  C CG2 A ILE A 1 48  ? 22.909 10.577  10.173 0.50 37.42 ? 47  ILE A CG2 1 
ATOM   376  C CG2 B ILE A 1 48  ? 21.625 8.623   11.280 0.50 37.11 ? 47  ILE A CG2 1 
ATOM   377  C CD1 A ILE A 1 48  ? 20.632 9.253   12.204 0.50 41.62 ? 47  ILE A CD1 1 
ATOM   378  C CD1 B ILE A 1 48  ? 22.066 11.435  12.480 0.50 41.72 ? 47  ILE A CD1 1 
ATOM   379  N N   . CYS A 1 49  ? 25.740 9.293   9.313  1.00 32.43 ? 48  CYS A N   1 
ATOM   380  C CA  . CYS A 1 49  ? 26.796 10.243  8.881  1.00 32.70 ? 48  CYS A CA  1 
ATOM   381  C C   . CYS A 1 49  ? 26.155 11.624  8.724  1.00 37.03 ? 48  CYS A C   1 
ATOM   382  O O   . CYS A 1 49  ? 25.264 11.721  7.901  1.00 36.04 ? 48  CYS A O   1 
ATOM   383  C CB  . CYS A 1 49  ? 27.456 9.813   7.584  1.00 35.68 ? 48  CYS A CB  1 
ATOM   384  S SG  . CYS A 1 49  ? 28.742 11.000  7.132  1.00 36.75 ? 48  CYS A SG  1 
ATOM   385  N N   . THR A 1 50  ? 26.561 12.623  9.517  1.00 33.49 ? 49  THR A N   1 
ATOM   386  C CA  . THR A 1 50  ? 25.865 13.929  9.616  1.00 37.16 ? 49  THR A CA  1 
ATOM   387  C C   . THR A 1 50  ? 26.426 14.875  8.555  1.00 37.04 ? 49  THR A C   1 
ATOM   388  O O   . THR A 1 50  ? 25.816 15.918  8.359  1.00 39.98 ? 49  THR A O   1 
ATOM   389  C CB  . THR A 1 50  ? 25.940 14.504  11.034 1.00 38.08 ? 49  THR A CB  1 
ATOM   390  O OG1 . THR A 1 50  ? 27.308 14.679  11.395 1.00 37.15 ? 49  THR A OG1 1 
ATOM   391  C CG2 . THR A 1 50  ? 25.236 13.622  12.044 1.00 37.37 ? 49  THR A CG2 1 
ATOM   392  N N   . THR A 1 51  ? 27.523 14.504  7.909  1.00 35.74 ? 50  THR A N   1 
ATOM   393  C CA  . THR A 1 51  ? 28.263 15.348  6.935  1.00 38.61 ? 50  THR A CA  1 
ATOM   394  C C   . THR A 1 51  ? 28.008 14.924  5.490  1.00 41.40 ? 50  THR A C   1 
ATOM   395  O O   . THR A 1 51  ? 28.698 15.444  4.616  1.00 43.18 ? 50  THR A O   1 
ATOM   396  C CB  . THR A 1 51  ? 29.753 15.338  7.278  1.00 39.92 ? 50  THR A CB  1 
ATOM   397  O OG1 . THR A 1 51  ? 30.229 13.987  7.347  1.00 37.12 ? 50  THR A OG1 1 
ATOM   398  C CG2 . THR A 1 51  ? 29.995 16.102  8.562  1.00 41.20 ? 50  THR A CG2 1 
ATOM   399  N N   . GLY A 1 52  ? 27.012 14.077  5.235  1.00 38.67 ? 51  GLY A N   1 
ATOM   400  C CA  . GLY A 1 52  ? 26.678 13.592  3.885  1.00 39.62 ? 51  GLY A CA  1 
ATOM   401  C C   . GLY A 1 52  ? 27.158 12.167  3.695  1.00 41.71 ? 51  GLY A C   1 
ATOM   402  O O   . GLY A 1 52  ? 26.812 11.315  4.515  1.00 38.66 ? 51  GLY A O   1 
ATOM   403  N N   . LYS A 1 53  ? 27.935 11.896  2.650  1.00 38.14 ? 52  LYS A N   1 
ATOM   404  C CA  . LYS A 1 53  ? 28.373 10.522  2.303  1.00 40.51 ? 52  LYS A CA  1 
ATOM   405  C C   . LYS A 1 53  ? 29.552 10.127  3.209  1.00 37.00 ? 52  LYS A C   1 
ATOM   406  O O   . LYS A 1 53  ? 30.511 10.885  3.325  1.00 37.98 ? 52  LYS A O   1 
ATOM   407  C CB  . LYS A 1 53  ? 28.685 10.413  0.805  1.00 46.24 ? 52  LYS A CB  1 
ATOM   408  C CG  . LYS A 1 53  ? 27.448 10.510  -0.089 1.00 55.09 ? 52  LYS A CG  1 
ATOM   409  C CD  . LYS A 1 53  ? 26.546 9.282   -0.012 1.00 58.45 ? 52  LYS A CD  1 
ATOM   410  N N   . LEU A 1 54  ? 29.482 8.963   3.833  1.00 35.90 ? 53  LEU A N   1 
ATOM   411  C CA  . LEU A 1 54  ? 30.611 8.460   4.645  1.00 36.82 ? 53  LEU A CA  1 
ATOM   412  C C   . LEU A 1 54  ? 31.744 8.057   3.703  1.00 37.09 ? 53  LEU A C   1 
ATOM   413  O O   . LEU A 1 54  ? 31.510 7.249   2.807  1.00 39.74 ? 53  LEU A O   1 
ATOM   414  C CB  . LEU A 1 54  ? 30.114 7.285   5.489  1.00 37.08 ? 53  LEU A CB  1 
ATOM   415  C CG  . LEU A 1 54  ? 31.055 6.823   6.599  1.00 36.10 ? 53  LEU A CG  1 
ATOM   416  C CD1 . LEU A 1 54  ? 31.117 7.844   7.731  1.00 34.85 ? 53  LEU A CD1 1 
ATOM   417  C CD2 . LEU A 1 54  ? 30.614 5.467   7.109  1.00 34.94 ? 53  LEU A CD2 1 
ATOM   418  N N   . PRO A 1 55  ? 32.979 8.597   3.863  1.00 38.20 ? 54  PRO A N   1 
ATOM   419  C CA  . PRO A 1 55  ? 34.075 8.326   2.919  1.00 37.09 ? 54  PRO A CA  1 
ATOM   420  C C   . PRO A 1 55  ? 34.835 7.004   3.122  1.00 39.16 ? 54  PRO A C   1 
ATOM   421  O O   . PRO A 1 55  ? 35.784 6.714   2.380  1.00 40.92 ? 54  PRO A O   1 
ATOM   422  C CB  . PRO A 1 55  ? 35.026 9.509   3.160  1.00 39.58 ? 54  PRO A CB  1 
ATOM   423  C CG  . PRO A 1 55  ? 34.829 9.872   4.630  1.00 41.30 ? 54  PRO A CG  1 
ATOM   424  C CD  . PRO A 1 55  ? 33.372 9.556   4.911  1.00 39.18 ? 54  PRO A CD  1 
ATOM   425  N N   . VAL A 1 56  ? 34.432 6.224   4.128  1.00 34.60 ? 55  VAL A N   1 
ATOM   426  C CA  . VAL A 1 56  ? 34.984 4.873   4.415  1.00 34.36 ? 55  VAL A CA  1 
ATOM   427  C C   . VAL A 1 56  ? 33.810 3.933   4.617  1.00 33.71 ? 55  VAL A C   1 
ATOM   428  O O   . VAL A 1 56  ? 32.693 4.397   4.827  1.00 35.64 ? 55  VAL A O   1 
ATOM   429  C CB  . VAL A 1 56  ? 35.893 4.868   5.659  1.00 36.14 ? 55  VAL A CB  1 
ATOM   430  C CG1 . VAL A 1 56  ? 37.084 5.812   5.506  1.00 39.13 ? 55  VAL A CG1 1 
ATOM   431  C CG2 . VAL A 1 56  ? 35.102 5.180   6.913  1.00 34.40 ? 55  VAL A CG2 1 
ATOM   432  N N   . PRO A 1 57  ? 34.002 2.600   4.516  1.00 36.36 ? 56  PRO A N   1 
ATOM   433  C CA  . PRO A 1 57  ? 32.906 1.662   4.726  1.00 35.79 ? 56  PRO A CA  1 
ATOM   434  C C   . PRO A 1 57  ? 32.474 1.666   6.195  1.00 36.22 ? 56  PRO A C   1 
ATOM   435  O O   . PRO A 1 57  ? 33.331 1.697   7.087  1.00 33.59 ? 56  PRO A O   1 
ATOM   436  C CB  . PRO A 1 57  ? 33.493 0.309   4.303  1.00 37.07 ? 56  PRO A CB  1 
ATOM   437  C CG  . PRO A 1 57  ? 34.678 0.688   3.422  1.00 37.41 ? 56  PRO A CG  1 
ATOM   438  C CD  . PRO A 1 57  ? 35.242 1.914   4.103  1.00 39.24 ? 56  PRO A CD  1 
ATOM   439  N N   . TRP A 1 58  ? 31.168 1.593   6.431  1.00 33.39 ? 57  TRP A N   1 
ATOM   440  C CA  . TRP A 1 58  ? 30.636 1.435   7.809  1.00 33.64 ? 57  TRP A CA  1 
ATOM   441  C C   . TRP A 1 58  ? 31.344 0.302   8.544  1.00 32.45 ? 57  TRP A C   1 
ATOM   442  O O   . TRP A 1 58  ? 31.634 0.433   9.737  1.00 32.27 ? 57  TRP A O   1 
ATOM   443  C CB  . TRP A 1 58  ? 29.125 1.228   7.786  1.00 32.50 ? 57  TRP A CB  1 
ATOM   444  C CG  . TRP A 1 58  ? 28.361 2.492   7.581  1.00 32.99 ? 57  TRP A CG  1 
ATOM   445  C CD1 . TRP A 1 58  ? 27.674 2.861   6.464  1.00 33.62 ? 57  TRP A CD1 1 
ATOM   446  C CD2 . TRP A 1 58  ? 28.183 3.546   8.553  1.00 31.12 ? 57  TRP A CD2 1 
ATOM   447  N NE1 . TRP A 1 58  ? 27.049 4.055   6.687  1.00 32.42 ? 57  TRP A NE1 1 
ATOM   448  C CE2 . TRP A 1 58  ? 27.339 4.502   7.949  1.00 32.54 ? 57  TRP A CE2 1 
ATOM   449  C CE3 . TRP A 1 58  ? 28.644 3.774   9.859  1.00 32.04 ? 57  TRP A CE3 1 
ATOM   450  C CZ2 . TRP A 1 58  ? 26.977 5.676   8.600  1.00 34.23 ? 57  TRP A CZ2 1 
ATOM   451  C CZ3 . TRP A 1 58  ? 28.269 4.928   10.505 1.00 32.01 ? 57  TRP A CZ3 1 
ATOM   452  C CH2 . TRP A 1 58  ? 27.452 5.874   9.880  1.00 34.94 ? 57  TRP A CH2 1 
ATOM   453  N N   . PRO A 1 59  ? 31.586 -0.884  7.938  1.00 33.61 ? 58  PRO A N   1 
ATOM   454  C CA  . PRO A 1 59  ? 32.235 -1.967  8.684  1.00 34.47 ? 58  PRO A CA  1 
ATOM   455  C C   . PRO A 1 59  ? 33.559 -1.580  9.362  1.00 34.20 ? 58  PRO A C   1 
ATOM   456  O O   . PRO A 1 59  ? 33.819 -2.073  10.490 1.00 34.04 ? 58  PRO A O   1 
ATOM   457  C CB  . PRO A 1 59  ? 32.412 -3.063  7.621  1.00 35.04 ? 58  PRO A CB  1 
ATOM   458  C CG  . PRO A 1 59  ? 31.225 -2.836  6.704  1.00 35.73 ? 58  PRO A CG  1 
ATOM   459  C CD  . PRO A 1 59  ? 31.134 -1.319  6.600  1.00 35.90 ? 58  PRO A CD  1 
ATOM   460  N N   . THR A 1 60  ? 34.332 -0.682  8.755  1.00 31.96 ? 59  THR A N   1 
ATOM   461  C CA  . THR A 1 60  ? 35.645 -0.262  9.296  1.00 32.55 ? 59  THR A CA  1 
ATOM   462  C C   . THR A 1 60  ? 35.494 0.575   10.569 1.00 31.94 ? 59  THR A C   1 
ATOM   463  O O   . THR A 1 60  ? 36.504 0.698   11.256 1.00 33.26 ? 59  THR A O   1 
ATOM   464  C CB  . THR A 1 60  ? 36.493 0.511   8.297  1.00 34.24 ? 59  THR A CB  1 
ATOM   465  O OG1 . THR A 1 60  ? 35.980 1.814   8.028  1.00 33.58 ? 59  THR A OG1 1 
ATOM   466  C CG2 . THR A 1 60  ? 36.667 -0.278  7.017  1.00 37.34 ? 59  THR A CG2 1 
ATOM   467  N N   . LEU A 1 61  ? 34.306 1.137   10.834 1.00 31.07 ? 60  LEU A N   1 
ATOM   468  C CA  . LEU A 1 61  ? 34.070 2.030   12.004 1.00 29.43 ? 60  LEU A CA  1 
ATOM   469  C C   . LEU A 1 61  ? 33.357 1.296   13.141 1.00 31.24 ? 60  LEU A C   1 
ATOM   470  O O   . LEU A 1 61  ? 33.227 1.919   14.195 1.00 31.05 ? 60  LEU A O   1 
ATOM   471  C CB  . LEU A 1 61  ? 33.212 3.217   11.559 1.00 28.49 ? 60  LEU A CB  1 
ATOM   472  C CG  . LEU A 1 61  ? 33.833 4.170   10.544 1.00 34.38 ? 60  LEU A CG  1 
ATOM   473  C CD1 . LEU A 1 61  ? 32.874 5.344   10.334 1.00 34.90 ? 60  LEU A CD1 1 
ATOM   474  C CD2 . LEU A 1 61  ? 35.195 4.659   10.989 1.00 35.92 ? 60  LEU A CD2 1 
ATOM   475  N N   . LYS A 1 62  ? 32.861 0.071   12.939 1.00 30.18 ? 61  LYS A N   1 
ATOM   476  C CA  . LYS A 1 62  ? 31.986 -0.613  13.917 1.00 30.17 ? 61  LYS A CA  1 
ATOM   477  C C   . LYS A 1 62  ? 32.716 -0.687  15.250 1.00 30.38 ? 61  LYS A C   1 
ATOM   478  O O   . LYS A 1 62  ? 32.111 -0.383  16.290 1.00 29.98 ? 61  LYS A O   1 
ATOM   479  C CB  . LYS A 1 62  ? 31.536 -2.000  13.450 1.00 35.32 ? 61  LYS A CB  1 
ATOM   480  C CG  . LYS A 1 62  ? 30.503 -1.993  12.332 1.00 41.77 ? 61  LYS A CG  1 
ATOM   481  C CD  . LYS A 1 62  ? 30.152 -3.398  11.871 1.00 47.80 ? 61  LYS A CD  1 
ATOM   482  C CE  . LYS A 1 62  ? 29.106 -3.442  10.773 1.00 53.29 ? 61  LYS A CE  1 
ATOM   483  N NZ  . LYS A 1 62  ? 28.745 -4.840  10.445 1.00 53.19 ? 61  LYS A NZ  1 
ATOM   484  N N   . THR A 1 63  ? 33.946 -1.212  15.269 1.00 28.69 ? 62  THR A N   1 
ATOM   485  C CA  . THR A 1 63  ? 34.653 -1.440  16.562 1.00 26.89 ? 62  THR A CA  1 
ATOM   486  C C   . THR A 1 63  ? 34.914 -0.101  17.264 1.00 27.27 ? 62  THR A C   1 
ATOM   487  O O   . THR A 1 63  ? 34.978 -0.093  18.501 1.00 28.83 ? 62  THR A O   1 
ATOM   488  C CB  . THR A 1 63  ? 35.929 -2.281  16.367 1.00 30.31 ? 62  THR A CB  1 
ATOM   489  O OG1 . THR A 1 63  ? 36.773 -1.537  15.496 1.00 29.86 ? 62  THR A OG1 1 
ATOM   490  C CG2 . THR A 1 63  ? 35.637 -3.674  15.872 1.00 30.92 ? 62  THR A CG2 1 
ATOM   491  N N   . THR A 1 64  ? 35.085 0.986   16.529 1.00 28.68 ? 63  THR A N   1 
ATOM   492  C CA  . THR A 1 64  ? 35.364 2.324   17.111 1.00 27.25 ? 63  THR A CA  1 
ATOM   493  C C   . THR A 1 64  ? 34.077 2.871   17.769 1.00 28.95 ? 63  THR A C   1 
ATOM   494  O O   . THR A 1 64  ? 34.131 3.407   18.889 1.00 28.54 ? 63  THR A O   1 
ATOM   495  C CB  . THR A 1 64  ? 35.950 3.262   16.047 1.00 29.96 ? 63  THR A CB  1 
ATOM   496  O OG1 . THR A 1 64  ? 37.173 2.666   15.586 1.00 30.65 ? 63  THR A OG1 1 
ATOM   497  C CG2 . THR A 1 64  ? 36.200 4.645   16.582 1.00 32.03 ? 63  THR A CG2 1 
ATOM   498  N N   . LEU A 1 65  ? 32.978 2.791   17.040 1.00 29.19 ? 64  LEU A N   1 
ATOM   499  C CA  . LEU A 1 65  ? 31.655 3.330   17.460 1.00 28.48 ? 64  LEU A CA  1 
ATOM   500  C C   . LEU A 1 65  ? 31.092 2.570   18.663 1.00 26.61 ? 64  LEU A C   1 
ATOM   501  O O   . LEU A 1 65  ? 30.515 3.116   19.634 1.00 29.99 ? 64  LEU A O   1 
ATOM   502  C CB  . LEU A 1 65  ? 30.722 3.242   16.262 1.00 27.91 ? 64  LEU A CB  1 
ATOM   503  C CG  . LEU A 1 65  ? 31.008 4.255   15.171 1.00 29.70 ? 64  LEU A CG  1 
ATOM   504  C CD1 . LEU A 1 65  ? 30.174 3.927   13.943 1.00 31.34 ? 64  LEU A CD1 1 
ATOM   505  C CD2 . LEU A 1 65  ? 30.763 5.702   15.596 1.00 28.93 ? 64  LEU A CD2 1 
HETATM 506  N N1  . CRF A 1 69  ? 31.285 1.063   18.605 1.00 28.87 ? 65  CRF A N1  1 
HETATM 507  C CA1 A CRF A 1 69  ? 30.831 0.266   19.689 0.50 30.30 ? 65  CRF A CA1 1 
HETATM 508  C CA1 B CRF A 1 69  ? 30.830 0.231   19.692 0.50 31.34 ? 65  CRF A CA1 1 
HETATM 509  C CB1 A CRF A 1 69  ? 29.534 -0.410  19.247 0.50 29.88 ? 65  CRF A CB1 1 
HETATM 510  C CB1 B CRF A 1 69  ? 29.600 -0.645  19.399 0.50 31.64 ? 65  CRF A CB1 1 
HETATM 511  C CG1 A CRF A 1 69  ? 29.562 -1.082  17.863 0.50 29.41 ? 65  CRF A CG1 1 
HETATM 512  C CG1 B CRF A 1 69  ? 28.486 0.212   18.832 0.50 33.00 ? 65  CRF A CG1 1 
HETATM 513  O OG1 A CRF A 1 69  ? 29.217 -1.350  20.241 0.50 31.34 ? 65  CRF A OG1 1 
HETATM 514  O OG1 B CRF A 1 69  ? 29.852 -1.729  18.470 0.50 35.75 ? 65  CRF A OG1 1 
HETATM 515  C C1  . CRF A 1 69  ? 32.014 -0.582  20.052 1.00 30.81 ? 65  CRF A C1  1 
HETATM 516  N N2  . CRF A 1 69  ? 32.244 -1.819  19.606 1.00 30.50 ? 65  CRF A N2  1 
HETATM 517  N N3  . CRF A 1 69  ? 33.024 -0.130  20.874 1.00 27.93 ? 65  CRF A N3  1 
HETATM 518  C C2  . CRF A 1 69  ? 33.914 -1.123  20.969 1.00 29.96 ? 65  CRF A C2  1 
HETATM 519  O O2  . CRF A 1 69  ? 34.976 -1.043  21.676 1.00 29.29 ? 65  CRF A O2  1 
HETATM 520  C CA2 . CRF A 1 69  ? 33.443 -2.204  20.161 1.00 30.36 ? 65  CRF A CA2 1 
HETATM 521  C CA3 . CRF A 1 69  ? 33.104 1.208   21.513 1.00 27.91 ? 65  CRF A CA3 1 
HETATM 522  C C3  . CRF A 1 69  ? 32.780 1.484   22.951 1.00 26.39 ? 65  CRF A C3  1 
HETATM 523  O O3  . CRF A 1 69  ? 33.282 2.386   23.558 1.00 29.97 ? 65  CRF A O3  1 
HETATM 524  C CB2 . CRF A 1 69  ? 34.096 -3.503  19.912 1.00 32.67 ? 65  CRF A CB2 1 
HETATM 525  C CG2 . CRF A 1 69  ? 33.560 -4.566  19.017 1.00 33.80 ? 65  CRF A CG2 1 
HETATM 526  C CD1 . CRF A 1 69  ? 32.434 -4.469  18.142 1.00 34.79 ? 65  CRF A CD1 1 
HETATM 527  C CD2 . CRF A 1 69  ? 34.294 -5.809  18.733 1.00 35.86 ? 65  CRF A CD2 1 
HETATM 528  C CE2 . CRF A 1 69  ? 33.407 -6.440  17.721 1.00 36.95 ? 65  CRF A CE2 1 
HETATM 529  N NE1 . CRF A 1 69  ? 32.371 -5.627  17.434 1.00 44.17 ? 65  CRF A NE1 1 
HETATM 530  C CE3 . CRF A 1 69  ? 35.416 -6.417  19.216 1.00 38.69 ? 65  CRF A CE3 1 
HETATM 531  C CZ2 . CRF A 1 69  ? 33.774 -7.709  17.285 1.00 39.78 ? 65  CRF A CZ2 1 
HETATM 532  C CZ3 . CRF A 1 69  ? 35.759 -7.687  18.737 1.00 42.68 ? 65  CRF A CZ3 1 
HETATM 533  C CH2 . CRF A 1 69  ? 34.945 -8.315  17.790 1.00 41.02 ? 65  CRF A CH2 1 
ATOM   534  N N   . MET A 1 70  ? 31.730 0.417   23.356 1.00 26.68 ? 66  MET A N   1 
ATOM   535  C CA  . MET A 1 70  ? 31.112 0.686   24.626 1.00 28.55 ? 66  MET A CA  1 
ATOM   536  C C   . MET A 1 70  ? 31.077 -0.647  25.358 1.00 29.38 ? 66  MET A C   1 
ATOM   537  O O   . MET A 1 70  ? 30.011 -1.176  25.624 1.00 28.94 ? 66  MET A O   1 
ATOM   538  C CB  . MET A 1 70  ? 29.744 1.344   24.415 1.00 29.69 ? 66  MET A CB  1 
ATOM   539  C CG  . MET A 1 70  ? 29.861 2.681   23.787 1.00 32.22 ? 66  MET A CG  1 
ATOM   540  S SD  . MET A 1 70  ? 28.256 3.410   23.346 1.00 31.89 ? 66  MET A SD  1 
ATOM   541  C CE  . MET A 1 70  ? 27.897 2.512   21.827 1.00 28.61 ? 66  MET A CE  1 
ATOM   542  N N   . GLN A 1 71  ? 32.288 -1.167  25.662 1.00 28.49 ? 67  GLN A N   1 
ATOM   543  C CA  . GLN A 1 71  ? 32.461 -2.510  26.273 1.00 29.00 ? 67  GLN A CA  1 
ATOM   544  C C   . GLN A 1 71  ? 31.926 -2.517  27.706 1.00 28.96 ? 67  GLN A C   1 
ATOM   545  O O   . GLN A 1 71  ? 31.792 -3.589  28.249 1.00 28.93 ? 67  GLN A O   1 
ATOM   546  C CB  . GLN A 1 71  ? 33.935 -2.898  26.182 1.00 28.09 ? 67  GLN A CB  1 
ATOM   547  C CG  . GLN A 1 71  ? 34.340 -3.123  24.746 1.00 29.29 ? 67  GLN A CG  1 
ATOM   548  C CD  . GLN A 1 71  ? 35.830 -3.234  24.565 1.00 30.36 ? 67  GLN A CD  1 
ATOM   549  O OE1 . GLN A 1 71  ? 36.578 -2.452  25.119 1.00 30.52 ? 67  GLN A OE1 1 
ATOM   550  N NE2 . GLN A 1 71  ? 36.257 -4.196  23.755 1.00 33.52 ? 67  GLN A NE2 1 
ATOM   551  N N   . CYS A 1 72  ? 31.573 -1.369  28.272 1.00 26.83 ? 68  CYS A N   1 
ATOM   552  C CA  . CYS A 1 72  ? 30.813 -1.250  29.561 1.00 27.06 ? 68  CYS A CA  1 
ATOM   553  C C   . CYS A 1 72  ? 29.445 -1.939  29.491 1.00 26.10 ? 68  CYS A C   1 
ATOM   554  O O   . CYS A 1 72  ? 28.910 -2.216  30.563 1.00 29.31 ? 68  CYS A O   1 
ATOM   555  C CB  . CYS A 1 72  ? 30.696 0.215   29.982 1.00 27.58 ? 68  CYS A CB  1 
ATOM   556  S SG  . CYS A 1 72  ? 30.029 1.325   28.715 1.00 29.30 ? 68  CYS A SG  1 
ATOM   557  N N   . PHE A 1 73  ? 28.888 -2.204  28.306 1.00 26.81 ? 69  PHE A N   1 
ATOM   558  C CA  . PHE A 1 73  ? 27.563 -2.850  28.170 1.00 28.28 ? 69  PHE A CA  1 
ATOM   559  C C   . PHE A 1 73  ? 27.714 -4.363  28.065 1.00 30.05 ? 69  PHE A C   1 
ATOM   560  O O   . PHE A 1 73  ? 26.695 -5.062  27.884 1.00 29.26 ? 69  PHE A O   1 
ATOM   561  C CB  . PHE A 1 73  ? 26.776 -2.239  27.015 1.00 27.03 ? 69  PHE A CB  1 
ATOM   562  C CG  . PHE A 1 73  ? 26.259 -0.864  27.346 1.00 28.49 ? 69  PHE A CG  1 
ATOM   563  C CD1 . PHE A 1 73  ? 25.309 -0.689  28.352 1.00 30.46 ? 69  PHE A CD1 1 
ATOM   564  C CD2 . PHE A 1 73  ? 26.775 0.248   26.710 1.00 28.45 ? 69  PHE A CD2 1 
ATOM   565  C CE1 . PHE A 1 73  ? 24.855 0.572   28.670 1.00 30.42 ? 69  PHE A CE1 1 
ATOM   566  C CE2 . PHE A 1 73  ? 26.327 1.524   27.048 1.00 28.40 ? 69  PHE A CE2 1 
ATOM   567  C CZ  . PHE A 1 73  ? 25.361 1.677   28.010 1.00 28.10 ? 69  PHE A CZ  1 
ATOM   568  N N   . ALA A 1 74  ? 28.910 -4.897  28.228 1.00 29.80 ? 70  ALA A N   1 
ATOM   569  C CA  . ALA A 1 74  ? 29.083 -6.363  28.195 1.00 27.52 ? 70  ALA A CA  1 
ATOM   570  C C   . ALA A 1 74  ? 28.333 -7.000  29.366 1.00 28.35 ? 70  ALA A C   1 
ATOM   571  O O   . ALA A 1 74  ? 28.268 -6.430  30.455 1.00 29.59 ? 70  ALA A O   1 
ATOM   572  C CB  . ALA A 1 74  ? 30.528 -6.749  28.235 1.00 28.27 ? 70  ALA A CB  1 
ATOM   573  N N   . ARG A 1 75  ? 27.829 -8.211  29.155 1.00 29.07 ? 71  ARG A N   1 
ATOM   574  C CA  . ARG A 1 75  ? 27.347 -9.038  30.287 1.00 29.00 ? 71  ARG A CA  1 
ATOM   575  C C   . ARG A 1 75  ? 28.521 -9.830  30.856 1.00 29.52 ? 71  ARG A C   1 
ATOM   576  O O   . ARG A 1 75  ? 29.058 -10.728 30.152 1.00 29.18 ? 71  ARG A O   1 
ATOM   577  C CB  . ARG A 1 75  ? 26.248 -9.987  29.831 1.00 29.63 ? 71  ARG A CB  1 
ATOM   578  C CG  . ARG A 1 75  ? 25.669 -10.782 30.993 1.00 28.91 ? 71  ARG A CG  1 
ATOM   579  C CD  . ARG A 1 75  ? 24.536 -11.672 30.544 1.00 31.72 ? 71  ARG A CD  1 
ATOM   580  N NE  . ARG A 1 75  ? 24.925 -12.815 29.732 1.00 31.60 ? 71  ARG A NE  1 
ATOM   581  C CZ  . ARG A 1 75  ? 25.343 -13.991 30.202 1.00 31.86 ? 71  ARG A CZ  1 
ATOM   582  N NH1 . ARG A 1 75  ? 25.518 -14.192 31.498 1.00 32.31 ? 71  ARG A NH1 1 
ATOM   583  N NH2 . ARG A 1 75  ? 25.592 -14.966 29.352 1.00 32.79 ? 71  ARG A NH2 1 
ATOM   584  N N   . TYR A 1 76  ? 28.933 -9.500  32.074 1.00 29.89 ? 72  TYR A N   1 
ATOM   585  C CA  . TYR A 1 76  ? 29.877 -10.317 32.864 1.00 28.75 ? 72  TYR A CA  1 
ATOM   586  C C   . TYR A 1 76  ? 29.039 -11.326 33.648 1.00 31.90 ? 72  TYR A C   1 
ATOM   587  O O   . TYR A 1 76  ? 28.152 -10.932 34.396 1.00 32.81 ? 72  TYR A O   1 
ATOM   588  C CB  . TYR A 1 76  ? 30.740 -9.437  33.759 1.00 29.31 ? 72  TYR A CB  1 
ATOM   589  C CG  . TYR A 1 76  ? 31.923 -8.863  33.034 1.00 29.65 ? 72  TYR A CG  1 
ATOM   590  C CD1 . TYR A 1 76  ? 31.787 -7.871  32.084 1.00 30.36 ? 72  TYR A CD1 1 
ATOM   591  C CD2 . TYR A 1 76  ? 33.197 -9.357  33.267 1.00 31.37 ? 72  TYR A CD2 1 
ATOM   592  C CE1 . TYR A 1 76  ? 32.895 -7.390  31.401 1.00 27.39 ? 72  TYR A CE1 1 
ATOM   593  C CE2 . TYR A 1 76  ? 34.309 -8.889  32.596 1.00 31.54 ? 72  TYR A CE2 1 
ATOM   594  C CZ  . TYR A 1 76  ? 34.157 -7.881  31.662 1.00 30.25 ? 72  TYR A CZ  1 
ATOM   595  O OH  . TYR A 1 76  ? 35.215 -7.404  30.934 1.00 28.95 ? 72  TYR A OH  1 
ATOM   596  N N   . PRO A 1 77  ? 29.253 -12.635 33.425 1.00 33.27 ? 73  PRO A N   1 
ATOM   597  C CA  . PRO A 1 77  ? 28.671 -13.668 34.287 1.00 36.55 ? 73  PRO A CA  1 
ATOM   598  C C   . PRO A 1 77  ? 28.972 -13.345 35.752 1.00 32.42 ? 73  PRO A C   1 
ATOM   599  O O   . PRO A 1 77  ? 30.035 -12.768 36.068 1.00 34.37 ? 73  PRO A O   1 
ATOM   600  C CB  . PRO A 1 77  ? 29.428 -14.938 33.870 1.00 40.32 ? 73  PRO A CB  1 
ATOM   601  C CG  . PRO A 1 77  ? 29.776 -14.684 32.418 1.00 40.98 ? 73  PRO A CG  1 
ATOM   602  C CD  . PRO A 1 77  ? 30.098 -13.202 32.360 1.00 36.57 ? 73  PRO A CD  1 
ATOM   603  N N   . ASP A 1 78  ? 28.057 -13.712 36.638 1.00 34.44 ? 74  ASP A N   1 
ATOM   604  C CA  . ASP A 1 78  ? 28.249 -13.488 38.093 1.00 32.76 ? 74  ASP A CA  1 
ATOM   605  C C   . ASP A 1 78  ? 29.662 -13.899 38.546 1.00 32.03 ? 74  ASP A C   1 
ATOM   606  O O   . ASP A 1 78  ? 30.293 -13.150 39.337 1.00 34.17 ? 74  ASP A O   1 
ATOM   607  C CB  . ASP A 1 78  ? 27.132 -14.174 38.872 1.00 34.60 ? 74  ASP A CB  1 
ATOM   608  C CG  . ASP A 1 78  ? 27.358 -14.029 40.359 1.00 36.36 ? 74  ASP A CG  1 
ATOM   609  O OD1 . ASP A 1 78  ? 26.987 -12.982 40.877 1.00 35.79 ? 74  ASP A OD1 1 
ATOM   610  O OD2 . ASP A 1 78  ? 27.987 -14.923 40.949 1.00 36.66 ? 74  ASP A OD2 1 
ATOM   611  N N   . HIS A 1 79  ? 30.187 -15.064 38.129 1.00 32.87 ? 75  HIS A N   1 
ATOM   612  C CA  . HIS A 1 79  ? 31.496 -15.560 38.617 1.00 34.70 ? 75  HIS A CA  1 
ATOM   613  C C   . HIS A 1 79  ? 32.676 -14.726 38.101 1.00 33.77 ? 75  HIS A C   1 
ATOM   614  O O   . HIS A 1 79  ? 33.794 -14.945 38.586 1.00 36.91 ? 75  HIS A O   1 
ATOM   615  C CB  . HIS A 1 79  ? 31.670 -17.059 38.326 1.00 34.07 ? 75  HIS A CB  1 
ATOM   616  C CG  . HIS A 1 79  ? 31.957 -17.397 36.912 1.00 33.78 ? 75  HIS A CG  1 
ATOM   617  N ND1 . HIS A 1 79  ? 30.958 -17.531 35.974 1.00 37.23 ? 75  HIS A ND1 1 
ATOM   618  C CD2 . HIS A 1 79  ? 33.128 -17.597 36.264 1.00 36.34 ? 75  HIS A CD2 1 
ATOM   619  C CE1 . HIS A 1 79  ? 31.497 -17.847 34.810 1.00 35.80 ? 75  HIS A CE1 1 
ATOM   620  N NE2 . HIS A 1 79  ? 32.823 -17.905 34.970 1.00 33.79 ? 75  HIS A NE2 1 
ATOM   621  N N   . MET A 1 80  ? 32.454 -13.808 37.149 1.00 33.87 ? 76  MET A N   1 
ATOM   622  C CA  . MET A 1 80  ? 33.516 -12.952 36.566 1.00 32.75 ? 76  MET A CA  1 
ATOM   623  C C   . MET A 1 80  ? 33.313 -11.463 36.900 1.00 34.22 ? 76  MET A C   1 
ATOM   624  O O   . MET A 1 80  ? 34.066 -10.654 36.359 1.00 32.86 ? 76  MET A O   1 
ATOM   625  C CB  . MET A 1 80  ? 33.512 -13.104 35.040 1.00 34.80 ? 76  MET A CB  1 
ATOM   626  C CG  . MET A 1 80  ? 33.995 -14.438 34.563 1.00 35.00 ? 76  MET A CG  1 
ATOM   627  S SD  . MET A 1 80  ? 33.880 -14.620 32.765 1.00 37.14 ? 76  MET A SD  1 
ATOM   628  C CE  . MET A 1 80  ? 35.153 -13.461 32.283 1.00 36.36 ? 76  MET A CE  1 
ATOM   629  N N   . LYS A 1 81  ? 32.360 -11.091 37.760 1.00 31.60 ? 77  LYS A N   1 
ATOM   630  C CA  . LYS A 1 81  ? 32.056 -9.657  38.031 1.00 35.89 ? 77  LYS A CA  1 
ATOM   631  C C   . LYS A 1 81  ? 33.306 -8.911  38.529 1.00 34.24 ? 77  LYS A C   1 
ATOM   632  O O   . LYS A 1 81  ? 33.402 -7.703  38.279 1.00 35.24 ? 77  LYS A O   1 
ATOM   633  C CB  . LYS A 1 81  ? 30.943 -9.507  39.077 1.00 36.19 ? 77  LYS A CB  1 
ATOM   634  C CG  . LYS A 1 81  ? 29.558 -9.987  38.692 1.00 42.77 ? 77  LYS A CG  1 
ATOM   635  C CD  . LYS A 1 81  ? 28.984 -9.315  37.503 1.00 43.04 ? 77  LYS A CD  1 
ATOM   636  C CE  . LYS A 1 81  ? 27.529 -9.676  37.268 1.00 42.08 ? 77  LYS A CE  1 
ATOM   637  N NZ  . LYS A 1 81  ? 27.001 -8.752  36.247 1.00 42.39 ? 77  LYS A NZ  1 
ATOM   638  N N   . GLN A 1 82  ? 34.247 -9.579  39.202 1.00 35.14 ? 78  GLN A N   1 
ATOM   639  C CA  . GLN A 1 82  ? 35.471 -8.913  39.720 1.00 34.52 ? 78  GLN A CA  1 
ATOM   640  C C   . GLN A 1 82  ? 36.465 -8.550  38.591 1.00 33.43 ? 78  GLN A C   1 
ATOM   641  O O   . GLN A 1 82  ? 37.498 -7.925  38.911 1.00 33.08 ? 78  GLN A O   1 
ATOM   642  C CB  . GLN A 1 82  ? 36.152 -9.795  40.778 1.00 37.89 ? 78  GLN A CB  1 
ATOM   643  C CG  . GLN A 1 82  ? 36.729 -11.093 40.222 1.00 43.62 ? 78  GLN A CG  1 
ATOM   644  C CD  . GLN A 1 82  ? 35.828 -12.312 40.247 1.00 49.40 ? 78  GLN A CD  1 
ATOM   645  O OE1 . GLN A 1 82  ? 34.630 -12.289 39.914 1.00 39.05 ? 78  GLN A OE1 1 
ATOM   646  N NE2 . GLN A 1 82  ? 36.431 -13.426 40.648 1.00 50.32 ? 78  GLN A NE2 1 
ATOM   647  N N   . HIS A 1 83  ? 36.192 -8.912  37.338 1.00 30.77 ? 79  HIS A N   1 
ATOM   648  C CA  . HIS A 1 83  ? 37.070 -8.659  36.170 1.00 30.79 ? 79  HIS A CA  1 
ATOM   649  C C   . HIS A 1 83  ? 36.489 -7.585  35.246 1.00 31.13 ? 79  HIS A C   1 
ATOM   650  O O   . HIS A 1 83  ? 37.044 -7.418  34.151 1.00 31.75 ? 79  HIS A O   1 
ATOM   651  C CB  . HIS A 1 83  ? 37.256 -9.962  35.406 1.00 34.54 ? 79  HIS A CB  1 
ATOM   652  C CG  . HIS A 1 83  ? 37.903 -10.983 36.273 1.00 38.81 ? 79  HIS A CG  1 
ATOM   653  N ND1 . HIS A 1 83  ? 37.271 -12.149 36.695 1.00 43.12 ? 79  HIS A ND1 1 
ATOM   654  C CD2 . HIS A 1 83  ? 39.111 -10.955 36.854 1.00 35.73 ? 79  HIS A CD2 1 
ATOM   655  C CE1 . HIS A 1 83  ? 38.108 -12.810 37.480 1.00 39.38 ? 79  HIS A CE1 1 
ATOM   656  N NE2 . HIS A 1 83  ? 39.241 -12.084 37.614 1.00 42.23 ? 79  HIS A NE2 1 
ATOM   657  N N   . ASP A 1 84  ? 35.413 -6.900  35.641 1.00 30.08 ? 80  ASP A N   1 
ATOM   658  C CA  . ASP A 1 84  ? 34.734 -5.902  34.781 1.00 29.92 ? 80  ASP A CA  1 
ATOM   659  C C   . ASP A 1 84  ? 35.327 -4.509  35.032 1.00 28.42 ? 80  ASP A C   1 
ATOM   660  O O   . ASP A 1 84  ? 34.752 -3.709  35.799 1.00 29.31 ? 80  ASP A O   1 
ATOM   661  C CB  . ASP A 1 84  ? 33.225 -5.943  34.974 1.00 30.19 ? 80  ASP A CB  1 
ATOM   662  C CG  . ASP A 1 84  ? 32.470 -5.047  33.990 1.00 28.96 ? 80  ASP A CG  1 
ATOM   663  O OD1 . ASP A 1 84  ? 33.151 -4.287  33.244 1.00 29.14 ? 80  ASP A OD1 1 
ATOM   664  O OD2 . ASP A 1 84  ? 31.217 -5.117  34.015 1.00 30.78 ? 80  ASP A OD2 1 
ATOM   665  N N   . PHE A 1 85  ? 36.467 -4.217  34.423 1.00 29.10 ? 81  PHE A N   1 
ATOM   666  C CA  . PHE A 1 85  ? 37.110 -2.896  34.542 1.00 28.11 ? 81  PHE A CA  1 
ATOM   667  C C   . PHE A 1 85  ? 36.165 -1.789  34.076 1.00 27.13 ? 81  PHE A C   1 
ATOM   668  O O   . PHE A 1 85  ? 36.099 -0.709  34.689 1.00 28.00 ? 81  PHE A O   1 
ATOM   669  C CB  . PHE A 1 85  ? 38.373 -2.842  33.687 1.00 28.13 ? 81  PHE A CB  1 
ATOM   670  C CG  . PHE A 1 85  ? 38.843 -1.452  33.398 1.00 27.99 ? 81  PHE A CG  1 
ATOM   671  C CD1 . PHE A 1 85  ? 39.672 -0.818  34.284 1.00 28.99 ? 81  PHE A CD1 1 
ATOM   672  C CD2 . PHE A 1 85  ? 38.489 -0.792  32.235 1.00 27.54 ? 81  PHE A CD2 1 
ATOM   673  C CE1 . PHE A 1 85  ? 40.096 0.472   34.051 1.00 29.28 ? 81  PHE A CE1 1 
ATOM   674  C CE2 . PHE A 1 85  ? 38.888 0.517   32.030 1.00 26.90 ? 81  PHE A CE2 1 
ATOM   675  C CZ  . PHE A 1 85  ? 39.722 1.121   32.924 1.00 31.08 ? 81  PHE A CZ  1 
ATOM   676  N N   . PHE A 1 86  ? 35.468 -2.051  32.962 1.00 28.29 ? 82  PHE A N   1 
ATOM   677  C CA  . PHE A 1 86  ? 34.697 -1.006  32.253 1.00 27.81 ? 82  PHE A CA  1 
ATOM   678  C C   . PHE A 1 86  ? 33.631 -0.366  33.154 1.00 28.85 ? 82  PHE A C   1 
ATOM   679  O O   . PHE A 1 86  ? 33.585 0.882   33.221 1.00 28.64 ? 82  PHE A O   1 
ATOM   680  C CB  . PHE A 1 86  ? 34.070 -1.605  31.006 1.00 27.93 ? 82  PHE A CB  1 
ATOM   681  C CG  . PHE A 1 86  ? 35.051 -2.315  30.115 1.00 28.47 ? 82  PHE A CG  1 
ATOM   682  C CD1 . PHE A 1 86  ? 35.898 -1.589  29.285 1.00 27.87 ? 82  PHE A CD1 1 
ATOM   683  C CD2 . PHE A 1 86  ? 35.164 -3.691  30.122 1.00 27.79 ? 82  PHE A CD2 1 
ATOM   684  C CE1 . PHE A 1 86  ? 36.783 -2.218  28.430 1.00 29.65 ? 82  PHE A CE1 1 
ATOM   685  C CE2 . PHE A 1 86  ? 36.077 -4.325  29.290 1.00 31.16 ? 82  PHE A CE2 1 
ATOM   686  C CZ  . PHE A 1 86  ? 36.884 -3.594  28.445 1.00 32.55 ? 82  PHE A CZ  1 
ATOM   687  N N   . LYS A 1 87  ? 32.809 -1.168  33.827 1.00 27.58 ? 83  LYS A N   1 
ATOM   688  C CA  . LYS A 1 87  ? 31.786 -0.601  34.747 1.00 28.27 ? 83  LYS A CA  1 
ATOM   689  C C   . LYS A 1 87  ? 32.454 -0.014  35.988 1.00 28.66 ? 83  LYS A C   1 
ATOM   690  O O   . LYS A 1 87  ? 31.927 0.972   36.501 1.00 28.97 ? 83  LYS A O   1 
ATOM   691  C CB  . LYS A 1 87  ? 30.716 -1.630  35.105 1.00 27.44 ? 83  LYS A CB  1 
ATOM   692  C CG  . LYS A 1 87  ? 29.900 -2.107  33.906 1.00 27.88 ? 83  LYS A CG  1 
ATOM   693  C CD  . LYS A 1 87  ? 28.775 -3.081  34.305 1.00 29.83 ? 83  LYS A CD  1 
ATOM   694  C CE  . LYS A 1 87  ? 28.097 -3.721  33.118 1.00 28.81 ? 83  LYS A CE  1 
ATOM   695  N NZ  . LYS A 1 87  ? 29.043 -4.535  32.318 1.00 28.41 ? 83  LYS A NZ  1 
ATOM   696  N N   . SER A 1 88  ? 33.578 -0.563  36.423 1.00 29.12 ? 84  SER A N   1 
ATOM   697  C CA  . SER A 1 88  ? 34.242 -0.150  37.678 1.00 28.08 ? 84  SER A CA  1 
ATOM   698  C C   . SER A 1 88  ? 34.680 1.307   37.537 1.00 30.64 ? 84  SER A C   1 
ATOM   699  O O   . SER A 1 88  ? 34.787 1.976   38.554 1.00 31.49 ? 84  SER A O   1 
ATOM   700  C CB  . SER A 1 88  ? 35.388 -1.057  38.026 1.00 28.94 ? 84  SER A CB  1 
ATOM   701  O OG  . SER A 1 88  ? 36.575 -0.760  37.315 1.00 29.82 ? 84  SER A OG  1 
ATOM   702  N N   . ALA A 1 89  ? 34.990 1.750   36.314 1.00 27.39 ? 85  ALA A N   1 
ATOM   703  C CA  . ALA A 1 89  ? 35.487 3.122   36.033 1.00 28.31 ? 85  ALA A CA  1 
ATOM   704  C C   . ALA A 1 89  ? 34.351 4.130   36.025 1.00 30.21 ? 85  ALA A C   1 
ATOM   705  O O   . ALA A 1 89  ? 34.639 5.329   35.927 1.00 29.06 ? 85  ALA A O   1 
ATOM   706  C CB  . ALA A 1 89  ? 36.236 3.158   34.720 1.00 29.56 ? 85  ALA A CB  1 
ATOM   707  N N   . MET A 1 90  ? 33.099 3.689   36.068 1.00 29.67 ? 86  MET A N   1 
ATOM   708  C CA  . MET A 1 90  ? 31.933 4.589   35.898 1.00 29.88 ? 86  MET A CA  1 
ATOM   709  C C   . MET A 1 90  ? 31.498 5.123   37.263 1.00 30.14 ? 86  MET A C   1 
ATOM   710  O O   . MET A 1 90  ? 31.690 4.449   38.276 1.00 31.75 ? 86  MET A O   1 
ATOM   711  C CB  . MET A 1 90  ? 30.784 3.810   35.245 1.00 29.17 ? 86  MET A CB  1 
ATOM   712  C CG  . MET A 1 90  ? 31.121 3.410   33.827 1.00 29.61 ? 86  MET A CG  1 
ATOM   713  S SD  . MET A 1 90  ? 31.335 4.827   32.733 1.00 30.81 ? 86  MET A SD  1 
ATOM   714  C CE  . MET A 1 90  ? 32.075 4.049   31.306 1.00 30.63 ? 86  MET A CE  1 
ATOM   715  N N   . PRO A 1 91  ? 30.907 6.343   37.362 1.00 30.60 ? 87  PRO A N   1 
ATOM   716  C CA  . PRO A 1 91  ? 30.486 7.160   36.214 1.00 31.47 ? 87  PRO A CA  1 
ATOM   717  C C   . PRO A 1 91  ? 31.516 8.083   35.560 1.00 30.03 ? 87  PRO A C   1 
ATOM   718  O O   . PRO A 1 91  ? 31.255 8.597   34.508 1.00 30.93 ? 87  PRO A O   1 
ATOM   719  C CB  . PRO A 1 91  ? 29.386 8.020   36.852 1.00 32.84 ? 87  PRO A CB  1 
ATOM   720  C CG  . PRO A 1 91  ? 29.923 8.258   38.251 1.00 31.49 ? 87  PRO A CG  1 
ATOM   721  C CD  . PRO A 1 91  ? 30.462 6.911   38.652 1.00 32.95 ? 87  PRO A CD  1 
ATOM   722  N N   . GLU A 1 92  ? 32.696 8.234   36.156 1.00 30.57 ? 88  GLU A N   1 
ATOM   723  C CA  A GLU A 1 92  ? 33.734 9.200   35.705 0.50 30.29 ? 88  GLU A CA  1 
ATOM   724  C CA  B GLU A 1 92  ? 33.684 9.235   35.671 0.50 30.97 ? 88  GLU A CA  1 
ATOM   725  C C   . GLU A 1 92  ? 34.226 8.764   34.318 1.00 30.94 ? 88  GLU A C   1 
ATOM   726  O O   . GLU A 1 92  ? 34.559 9.623   33.491 1.00 30.80 ? 88  GLU A O   1 
ATOM   727  C CB  A GLU A 1 92  ? 34.848 9.244   36.756 0.50 32.35 ? 88  GLU A CB  1 
ATOM   728  C CB  B GLU A 1 92  ? 34.801 9.454   36.690 0.50 34.35 ? 88  GLU A CB  1 
ATOM   729  C CG  A GLU A 1 92  ? 34.339 9.657   38.127 0.50 36.13 ? 88  GLU A CG  1 
ATOM   730  C CG  B GLU A 1 92  ? 34.400 10.369  37.830 0.50 38.20 ? 88  GLU A CG  1 
ATOM   731  C CD  A GLU A 1 92  ? 33.801 8.578   39.058 0.50 35.59 ? 88  GLU A CD  1 
ATOM   732  C CD  B GLU A 1 92  ? 35.416 10.303  38.959 0.50 43.63 ? 88  GLU A CD  1 
ATOM   733  O OE1 A GLU A 1 92  ? 33.765 7.379   38.685 0.50 27.95 ? 88  GLU A OE1 1 
ATOM   734  O OE1 B GLU A 1 92  ? 35.571 9.209   39.543 0.50 49.39 ? 88  GLU A OE1 1 
ATOM   735  O OE2 A GLU A 1 92  ? 33.392 8.966   40.182 0.50 45.04 ? 88  GLU A OE2 1 
ATOM   736  O OE2 B GLU A 1 92  ? 36.112 11.307  39.182 0.50 46.08 ? 88  GLU A OE2 1 
ATOM   737  N N   . GLY A 1 93  ? 34.288 7.448   34.107 1.00 31.69 ? 89  GLY A N   1 
ATOM   738  C CA  . GLY A 1 93  ? 34.537 6.920   32.759 1.00 29.53 ? 89  GLY A CA  1 
ATOM   739  C C   . GLY A 1 93  ? 35.952 6.476   32.498 1.00 30.55 ? 89  GLY A C   1 
ATOM   740  O O   . GLY A 1 93  ? 36.805 6.408   33.436 1.00 29.77 ? 89  GLY A O   1 
ATOM   741  N N   . TYR A 1 94  ? 36.206 6.190   31.232 1.00 29.19 ? 90  TYR A N   1 
ATOM   742  C CA  . TYR A 1 94  ? 37.571 5.802   30.793 1.00 28.98 ? 90  TYR A CA  1 
ATOM   743  C C   . TYR A 1 94  ? 37.872 6.404   29.440 1.00 29.41 ? 90  TYR A C   1 
ATOM   744  O O   . TYR A 1 94  ? 36.981 6.725   28.648 1.00 29.24 ? 90  TYR A O   1 
ATOM   745  C CB  . TYR A 1 94  ? 37.752 4.286   30.774 1.00 28.65 ? 90  TYR A CB  1 
ATOM   746  C CG  . TYR A 1 94  ? 36.717 3.502   29.999 1.00 27.47 ? 90  TYR A CG  1 
ATOM   747  C CD1 . TYR A 1 94  ? 36.772 3.334   28.620 1.00 27.79 ? 90  TYR A CD1 1 
ATOM   748  C CD2 . TYR A 1 94  ? 35.665 2.898   30.656 1.00 28.47 ? 90  TYR A CD2 1 
ATOM   749  C CE1 . TYR A 1 94  ? 35.792 2.615   27.930 1.00 28.10 ? 90  TYR A CE1 1 
ATOM   750  C CE2 . TYR A 1 94  ? 34.731 2.126   29.998 1.00 27.96 ? 90  TYR A CE2 1 
ATOM   751  C CZ  . TYR A 1 94  ? 34.757 2.011   28.623 1.00 28.75 ? 90  TYR A CZ  1 
ATOM   752  O OH  . TYR A 1 94  ? 33.834 1.250   27.954 1.00 30.09 ? 90  TYR A OH  1 
ATOM   753  N N   . VAL A 1 95  ? 39.163 6.510   29.178 1.00 28.10 ? 91  VAL A N   1 
ATOM   754  C CA  . VAL A 1 95  ? 39.684 6.832   27.835 1.00 29.11 ? 91  VAL A CA  1 
ATOM   755  C C   . VAL A 1 95  ? 39.924 5.508   27.100 1.00 31.39 ? 91  VAL A C   1 
ATOM   756  O O   . VAL A 1 95  ? 40.570 4.611   27.660 1.00 32.34 ? 91  VAL A O   1 
ATOM   757  C CB  . VAL A 1 95  ? 40.971 7.676   27.942 1.00 32.28 ? 91  VAL A CB  1 
ATOM   758  C CG1 . VAL A 1 95  ? 41.579 7.897   26.583 1.00 32.03 ? 91  VAL A CG1 1 
ATOM   759  C CG2 . VAL A 1 95  ? 40.716 9.002   28.616 1.00 32.83 ? 91  VAL A CG2 1 
ATOM   760  N N   . GLN A 1 96  ? 39.490 5.398   25.848 1.00 28.70 ? 92  GLN A N   1 
ATOM   761  C CA  . GLN A 1 96  ? 39.757 4.198   25.034 1.00 28.79 ? 92  GLN A CA  1 
ATOM   762  C C   . GLN A 1 96  ? 40.545 4.648   23.801 1.00 27.90 ? 92  GLN A C   1 
ATOM   763  O O   . GLN A 1 96  ? 40.018 5.462   23.011 1.00 28.30 ? 92  GLN A O   1 
ATOM   764  C CB  . GLN A 1 96  ? 38.460 3.497   24.667 1.00 29.61 ? 92  GLN A CB  1 
ATOM   765  C CG  . GLN A 1 96  ? 38.669 2.292   23.777 1.00 28.58 ? 92  GLN A CG  1 
ATOM   766  C CD  . GLN A 1 96  ? 37.482 1.345   23.812 1.00 30.50 ? 92  GLN A CD  1 
ATOM   767  O OE1 . GLN A 1 96  ? 37.092 0.851   24.857 1.00 30.01 ? 92  GLN A OE1 1 
ATOM   768  N NE2 . GLN A 1 96  ? 36.909 1.093   22.647 1.00 31.50 ? 92  GLN A NE2 1 
ATOM   769  N N   . GLU A 1 97  ? 41.798 4.174   23.681 1.00 28.98 ? 93  GLU A N   1 
ATOM   770  C CA  . GLU A 1 97  ? 42.662 4.476   22.518 1.00 29.13 ? 93  GLU A CA  1 
ATOM   771  C C   . GLU A 1 97  ? 42.924 3.203   21.732 1.00 28.03 ? 93  GLU A C   1 
ATOM   772  O O   . GLU A 1 97  ? 43.186 2.158   22.332 1.00 29.52 ? 93  GLU A O   1 
ATOM   773  C CB  . GLU A 1 97  ? 43.980 5.090   22.983 1.00 32.59 ? 93  GLU A CB  1 
ATOM   774  C CG  . GLU A 1 97  ? 43.825 6.461   23.549 1.00 36.78 ? 93  GLU A CG  1 
ATOM   775  C CD  . GLU A 1 97  ? 45.099 7.041   24.128 1.00 48.05 ? 93  GLU A CD  1 
ATOM   776  O OE1 . GLU A 1 97  ? 45.716 6.366   24.955 1.00 49.59 ? 93  GLU A OE1 1 
ATOM   777  O OE2 . GLU A 1 97  ? 45.413 8.183   23.785 1.00 49.93 ? 93  GLU A OE2 1 
ATOM   778  N N   . ARG A 1 98  ? 42.854 3.298   20.400 1.00 28.39 ? 94  ARG A N   1 
ATOM   779  C CA  . ARG A 1 98  ? 43.240 2.172   19.553 1.00 31.01 ? 94  ARG A CA  1 
ATOM   780  C C   . ARG A 1 98  ? 44.123 2.677   18.421 1.00 30.55 ? 94  ARG A C   1 
ATOM   781  O O   . ARG A 1 98  ? 43.998 3.822   18.015 1.00 29.74 ? 94  ARG A O   1 
ATOM   782  C CB  . ARG A 1 98  ? 42.022 1.472   18.955 1.00 28.93 ? 94  ARG A CB  1 
ATOM   783  C CG  . ARG A 1 98  ? 41.177 0.733   19.981 1.00 29.84 ? 94  ARG A CG  1 
ATOM   784  C CD  . ARG A 1 98  ? 40.507 -0.439  19.301 1.00 30.47 ? 94  ARG A CD  1 
ATOM   785  N NE  . ARG A 1 98  ? 39.580 -1.182  20.137 1.00 28.96 ? 94  ARG A NE  1 
ATOM   786  C CZ  . ARG A 1 98  ? 38.244 -1.015  20.155 1.00 32.65 ? 94  ARG A CZ  1 
ATOM   787  N NH1 . ARG A 1 98  ? 37.673 -0.108  19.383 1.00 31.34 ? 94  ARG A NH1 1 
ATOM   788  N NH2 . ARG A 1 98  ? 37.498 -1.814  20.900 1.00 29.39 ? 94  ARG A NH2 1 
ATOM   789  N N   . THR A 1 99  ? 44.981 1.792   17.977 1.00 29.73 ? 95  THR A N   1 
ATOM   790  C CA  . THR A 1 99  ? 45.466 1.794   16.575 1.00 29.76 ? 95  THR A CA  1 
ATOM   791  C C   . THR A 1 99  ? 44.916 0.547   15.916 1.00 29.65 ? 95  THR A C   1 
ATOM   792  O O   . THR A 1 99  ? 45.030 -0.537  16.467 1.00 30.53 ? 95  THR A O   1 
ATOM   793  C CB  . THR A 1 99  ? 46.997 1.852   16.469 1.00 30.85 ? 95  THR A CB  1 
ATOM   794  O OG1 . THR A 1 99  ? 47.453 2.976   17.216 1.00 32.75 ? 95  THR A OG1 1 
ATOM   795  C CG2 . THR A 1 99  ? 47.438 1.993   15.026 1.00 33.95 ? 95  THR A CG2 1 
ATOM   796  N N   . ILE A 1 100 ? 44.361 0.722   14.719 1.00 32.21 ? 96  ILE A N   1 
ATOM   797  C CA  . ILE A 1 100 ? 43.831 -0.364  13.878 1.00 29.80 ? 96  ILE A CA  1 
ATOM   798  C C   . ILE A 1 100 ? 44.658 -0.345  12.598 1.00 30.81 ? 96  ILE A C   1 
ATOM   799  O O   . ILE A 1 100 ? 44.615 0.635   11.894 1.00 32.91 ? 96  ILE A O   1 
ATOM   800  C CB  . ILE A 1 100 ? 42.333 -0.167  13.613 1.00 29.54 ? 96  ILE A CB  1 
ATOM   801  C CG1 . ILE A 1 100 ? 41.547 -0.025  14.923 1.00 30.71 ? 96  ILE A CG1 1 
ATOM   802  C CG2 . ILE A 1 100 ? 41.804 -1.324  12.757 1.00 30.94 ? 96  ILE A CG2 1 
ATOM   803  C CD1 . ILE A 1 100 ? 40.108 0.432   14.731 1.00 30.50 ? 96  ILE A CD1 1 
ATOM   804  N N   . PHE A 1 101 ? 45.452 -1.380  12.421 1.00 31.75 ? 97  PHE A N   1 
ATOM   805  C CA  . PHE A 1 101 ? 46.323 -1.551  11.233 1.00 33.01 ? 97  PHE A CA  1 
ATOM   806  C C   . PHE A 1 101 ? 45.567 -2.415  10.236 1.00 31.49 ? 97  PHE A C   1 
ATOM   807  O O   . PHE A 1 101 ? 45.345 -3.587  10.539 1.00 34.14 ? 97  PHE A O   1 
ATOM   808  C CB  . PHE A 1 101 ? 47.616 -2.242  11.669 1.00 34.43 ? 97  PHE A CB  1 
ATOM   809  C CG  . PHE A 1 101 ? 48.447 -1.434  12.621 1.00 34.83 ? 97  PHE A CG  1 
ATOM   810  C CD1 . PHE A 1 101 ? 49.339 -0.509  12.128 1.00 34.03 ? 97  PHE A CD1 1 
ATOM   811  C CD2 . PHE A 1 101 ? 48.377 -1.643  14.000 1.00 33.48 ? 97  PHE A CD2 1 
ATOM   812  C CE1 . PHE A 1 101 ? 50.127 0.247   12.977 1.00 37.28 ? 97  PHE A CE1 1 
ATOM   813  C CE2 . PHE A 1 101 ? 49.194 -0.905  14.841 1.00 36.15 ? 97  PHE A CE2 1 
ATOM   814  C CZ  . PHE A 1 101 ? 50.084 0.018   14.327 1.00 35.97 ? 97  PHE A CZ  1 
ATOM   815  N N   . PHE A 1 102 ? 45.173 -1.830  9.103  1.00 35.38 ? 98  PHE A N   1 
ATOM   816  C CA  . PHE A 1 102 ? 44.569 -2.551  7.957  1.00 33.97 ? 98  PHE A CA  1 
ATOM   817  C C   . PHE A 1 102 ? 45.698 -3.088  7.070  1.00 35.22 ? 98  PHE A C   1 
ATOM   818  O O   . PHE A 1 102 ? 46.472 -2.279  6.585  1.00 37.71 ? 98  PHE A O   1 
ATOM   819  C CB  . PHE A 1 102 ? 43.626 -1.622  7.203  1.00 33.24 ? 98  PHE A CB  1 
ATOM   820  C CG  . PHE A 1 102 ? 42.460 -1.126  8.017  1.00 33.99 ? 98  PHE A CG  1 
ATOM   821  C CD1 . PHE A 1 102 ? 41.321 -1.914  8.139  1.00 34.46 ? 98  PHE A CD1 1 
ATOM   822  C CD2 . PHE A 1 102 ? 42.478 0.123   8.621  1.00 34.34 ? 98  PHE A CD2 1 
ATOM   823  C CE1 . PHE A 1 102 ? 40.242 -1.480  8.898  1.00 33.57 ? 98  PHE A CE1 1 
ATOM   824  C CE2 . PHE A 1 102 ? 41.385 0.560   9.345  1.00 34.38 ? 98  PHE A CE2 1 
ATOM   825  C CZ  . PHE A 1 102 ? 40.283 -0.243  9.480  1.00 33.67 ? 98  PHE A CZ  1 
ATOM   826  N N   . LYS A 1 103 ? 45.794 -4.405  6.969  1.00 36.08 ? 99  LYS A N   1 
ATOM   827  C CA  . LYS A 1 103 ? 46.903 -5.116  6.274  1.00 40.62 ? 99  LYS A CA  1 
ATOM   828  C C   . LYS A 1 103 ? 47.005 -4.588  4.840  1.00 38.21 ? 99  LYS A C   1 
ATOM   829  O O   . LYS A 1 103 ? 45.967 -4.571  4.135  1.00 41.23 ? 99  LYS A O   1 
ATOM   830  C CB  . LYS A 1 103 ? 46.676 -6.624  6.292  1.00 45.36 ? 99  LYS A CB  1 
ATOM   831  C CG  . LYS A 1 103 ? 47.778 -7.419  5.595  1.00 50.08 ? 99  LYS A CG  1 
ATOM   832  C CD  . LYS A 1 103 ? 48.237 -8.640  6.363  1.00 61.86 ? 99  LYS A CD  1 
ATOM   833  C CE  . LYS A 1 103 ? 48.108 -9.934  5.579  1.00 73.72 ? 99  LYS A CE  1 
ATOM   834  N NZ  . LYS A 1 103 ? 48.948 -9.931  4.360  1.00 78.99 ? 99  LYS A NZ  1 
ATOM   835  N N   . ASP A 1 104 ? 48.179 -4.066  4.486  1.00 46.11 ? 100 ASP A N   1 
ATOM   836  C CA  . ASP A 1 104 ? 48.522 -3.558  3.125  1.00 44.42 ? 100 ASP A CA  1 
ATOM   837  C C   . ASP A 1 104 ? 47.711 -2.298  2.825  1.00 46.18 ? 100 ASP A C   1 
ATOM   838  O O   . ASP A 1 104 ? 47.467 -2.015  1.656  1.00 45.18 ? 100 ASP A O   1 
ATOM   839  C CB  . ASP A 1 104 ? 48.323 -4.650  2.068  1.00 48.30 ? 100 ASP A CB  1 
ATOM   840  C CG  . ASP A 1 104 ? 49.357 -5.762  2.170  1.00 50.19 ? 100 ASP A CG  1 
ATOM   841  O OD1 . ASP A 1 104 ? 50.538 -5.444  2.449  1.00 53.41 ? 100 ASP A OD1 1 
ATOM   842  O OD2 . ASP A 1 104 ? 48.963 -6.930  2.001  1.00 57.55 ? 100 ASP A OD2 1 
ATOM   843  N N   . ASP A 1 105 ? 47.280 -1.564  3.849  1.00 41.01 ? 101 ASP A N   1 
ATOM   844  C CA  . ASP A 1 105 ? 46.564 -0.283  3.664  1.00 42.86 ? 101 ASP A CA  1 
ATOM   845  C C   . ASP A 1 105 ? 46.917 0.608   4.863  1.00 41.56 ? 101 ASP A C   1 
ATOM   846  O O   . ASP A 1 105 ? 47.944 0.340   5.525  1.00 40.48 ? 101 ASP A O   1 
ATOM   847  C CB  . ASP A 1 105 ? 45.065 -0.529  3.452  1.00 39.42 ? 101 ASP A CB  1 
ATOM   848  C CG  . ASP A 1 105 ? 44.310 0.505   2.619  1.00 42.31 ? 101 ASP A CG  1 
ATOM   849  O OD1 . ASP A 1 105 ? 44.736 1.704   2.553  1.00 43.95 ? 101 ASP A OD1 1 
ATOM   850  O OD2 . ASP A 1 105 ? 43.259 0.117   2.076  1.00 43.65 ? 101 ASP A OD2 1 
ATOM   851  N N   . GLY A 1 106 ? 46.103 1.624   5.109  1.00 40.80 ? 102 GLY A N   1 
ATOM   852  C CA  . GLY A 1 106 ? 46.356 2.615   6.150  1.00 39.12 ? 102 GLY A CA  1 
ATOM   853  C C   . GLY A 1 106 ? 46.024 2.099   7.538  1.00 33.20 ? 102 GLY A C   1 
ATOM   854  O O   . GLY A 1 106 ? 45.790 0.895   7.739  1.00 34.14 ? 102 GLY A O   1 
ATOM   855  N N   . ASN A 1 107 ? 46.113 3.006   8.489  1.00 36.18 ? 103 ASN A N   1 
ATOM   856  C CA  . ASN A 1 107 ? 45.763 2.719   9.900  1.00 36.68 ? 103 ASN A CA  1 
ATOM   857  C C   . ASN A 1 107 ? 44.836 3.819   10.388 1.00 35.22 ? 103 ASN A C   1 
ATOM   858  O O   . ASN A 1 107 ? 44.967 4.988   9.960  1.00 35.51 ? 103 ASN A O   1 
ATOM   859  C CB  . ASN A 1 107 ? 47.006 2.541   10.781 1.00 37.78 ? 103 ASN A CB  1 
ATOM   860  C CG  . ASN A 1 107 ? 47.886 3.768   10.808 1.00 39.08 ? 103 ASN A CG  1 
ATOM   861  O OD1 . ASN A 1 107 ? 48.857 3.872   10.054 1.00 47.47 ? 103 ASN A OD1 1 
ATOM   862  N ND2 . ASN A 1 107 ? 47.552 4.713   11.648 1.00 36.95 ? 103 ASN A ND2 1 
ATOM   863  N N   . TYR A 1 108 ? 43.955 3.447   11.321 1.00 35.24 ? 104 TYR A N   1 
ATOM   864  C CA  . TYR A 1 108 ? 43.172 4.387   12.145 1.00 32.66 ? 104 TYR A CA  1 
ATOM   865  C C   . TYR A 1 108 ? 43.786 4.468   13.542 1.00 30.56 ? 104 TYR A C   1 
ATOM   866  O O   . TYR A 1 108 ? 44.192 3.453   14.097 1.00 33.15 ? 104 TYR A O   1 
ATOM   867  C CB  . TYR A 1 108 ? 41.729 3.905   12.351 1.00 32.53 ? 104 TYR A CB  1 
ATOM   868  C CG  . TYR A 1 108 ? 40.829 3.806   11.144 1.00 33.30 ? 104 TYR A CG  1 
ATOM   869  C CD1 . TYR A 1 108 ? 41.079 4.482   9.957  1.00 33.74 ? 104 TYR A CD1 1 
ATOM   870  C CD2 . TYR A 1 108 ? 39.643 3.091   11.242 1.00 30.39 ? 104 TYR A CD2 1 
ATOM   871  C CE1 . TYR A 1 108 ? 40.205 4.386   8.880  1.00 34.11 ? 104 TYR A CE1 1 
ATOM   872  C CE2 . TYR A 1 108 ? 38.748 3.007   10.188 1.00 30.82 ? 104 TYR A CE2 1 
ATOM   873  C CZ  . TYR A 1 108 ? 39.022 3.672   9.013  1.00 35.26 ? 104 TYR A CZ  1 
ATOM   874  O OH  . TYR A 1 108 ? 38.114 3.585   8.009  1.00 36.52 ? 104 TYR A OH  1 
ATOM   875  N N   . LYS A 1 109 ? 43.895 5.677   14.042 1.00 31.66 ? 105 LYS A N   1 
ATOM   876  C CA  . LYS A 1 109 ? 44.195 5.971   15.450 1.00 33.42 ? 105 LYS A CA  1 
ATOM   877  C C   . LYS A 1 109 ? 42.965 6.641   16.020 1.00 31.09 ? 105 LYS A C   1 
ATOM   878  O O   . LYS A 1 109 ? 42.531 7.678   15.500 1.00 32.33 ? 105 LYS A O   1 
ATOM   879  C CB  . LYS A 1 109 ? 45.453 6.835   15.597 1.00 36.17 ? 105 LYS A CB  1 
ATOM   880  C CG  . LYS A 1 109 ? 46.737 6.119   15.240 1.00 41.77 ? 105 LYS A CG  1 
ATOM   881  C CD  . LYS A 1 109 ? 47.935 7.010   15.449 1.00 47.40 ? 105 LYS A CD  1 
ATOM   882  C CE  . LYS A 1 109 ? 49.236 6.247   15.357 1.00 55.90 ? 105 LYS A CE  1 
ATOM   883  N NZ  . LYS A 1 109 ? 49.413 5.649   14.011 1.00 60.37 ? 105 LYS A NZ  1 
ATOM   884  N N   . THR A 1 110 ? 42.460 6.086   17.113 1.00 33.14 ? 106 THR A N   1 
ATOM   885  C CA  . THR A 1 110 ? 41.215 6.583   17.713 1.00 28.55 ? 106 THR A CA  1 
ATOM   886  C C   . THR A 1 110 ? 41.450 6.906   19.180 1.00 30.25 ? 106 THR A C   1 
ATOM   887  O O   . THR A 1 110 ? 42.255 6.241   19.833 1.00 29.86 ? 106 THR A O   1 
ATOM   888  C CB  . THR A 1 110 ? 40.078 5.570   17.550 1.00 28.62 ? 106 THR A CB  1 
ATOM   889  O OG1 . THR A 1 110 ? 40.320 4.431   18.374 1.00 29.77 ? 106 THR A OG1 1 
ATOM   890  C CG2 . THR A 1 110 ? 39.904 5.193   16.101 1.00 32.22 ? 106 THR A CG2 1 
ATOM   891  N N   . ARG A 1 111 ? 40.819 7.971   19.642 1.00 29.47 ? 107 ARG A N   1 
ATOM   892  C CA  . ARG A 1 111 ? 40.820 8.273   21.081 1.00 29.83 ? 107 ARG A CA  1 
ATOM   893  C C   . ARG A 1 111 ? 39.383 8.610   21.429 1.00 30.92 ? 107 ARG A C   1 
ATOM   894  O O   . ARG A 1 111 ? 38.799 9.541   20.791 1.00 30.81 ? 107 ARG A O   1 
ATOM   895  C CB  . ARG A 1 111 ? 41.746 9.436   21.398 1.00 31.84 ? 107 ARG A CB  1 
ATOM   896  C CG  . ARG A 1 111 ? 41.780 9.763   22.881 1.00 33.42 ? 107 ARG A CG  1 
ATOM   897  C CD  . ARG A 1 111 ? 42.645 10.987  23.168 1.00 36.93 ? 107 ARG A CD  1 
ATOM   898  N NE  . ARG A 1 111 ? 42.619 11.217  24.615 1.00 36.90 ? 107 ARG A NE  1 
ATOM   899  C CZ  . ARG A 1 111 ? 41.605 11.787  25.285 1.00 41.01 ? 107 ARG A CZ  1 
ATOM   900  N NH1 . ARG A 1 111 ? 40.527 12.230  24.657 1.00 45.18 ? 107 ARG A NH1 1 
ATOM   901  N NH2 . ARG A 1 111 ? 41.674 11.923  26.595 1.00 49.15 ? 107 ARG A NH2 1 
ATOM   902  N N   . ALA A 1 112 ? 38.842 7.925   22.415 1.00 29.28 ? 108 ALA A N   1 
ATOM   903  C CA  . ALA A 1 112 ? 37.458 8.134   22.860 1.00 28.77 ? 108 ALA A CA  1 
ATOM   904  C C   . ALA A 1 112 ? 37.419 8.336   24.371 1.00 29.01 ? 108 ALA A C   1 
ATOM   905  O O   . ALA A 1 112 ? 38.259 7.753   25.109 1.00 30.89 ? 108 ALA A O   1 
ATOM   906  C CB  . ALA A 1 112 ? 36.593 6.950   22.432 1.00 30.03 ? 108 ALA A CB  1 
ATOM   907  N N   . GLU A 1 113 ? 36.422 9.084   24.823 1.00 29.07 ? 109 GLU A N   1 
ATOM   908  C CA  . GLU A 1 113 ? 36.051 9.176   26.243 1.00 29.03 ? 109 GLU A CA  1 
ATOM   909  C C   . GLU A 1 113 ? 34.647 8.619   26.410 1.00 29.37 ? 109 GLU A C   1 
ATOM   910  O O   . GLU A 1 113 ? 33.760 9.026   25.661 1.00 29.88 ? 109 GLU A O   1 
ATOM   911  C CB  . GLU A 1 113 ? 36.099 10.630  26.723 1.00 32.65 ? 109 GLU A CB  1 
ATOM   912  C CG  . GLU A 1 113 ? 37.513 11.131  26.757 1.00 38.65 ? 109 GLU A CG  1 
ATOM   913  C CD  . GLU A 1 113 ? 37.714 12.436  27.491 1.00 46.63 ? 109 GLU A CD  1 
ATOM   914  O OE1 . GLU A 1 113 ? 36.760 12.891  28.188 1.00 42.90 ? 109 GLU A OE1 1 
ATOM   915  O OE2 . GLU A 1 113 ? 38.814 13.007  27.316 1.00 54.04 ? 109 GLU A OE2 1 
ATOM   916  N N   . VAL A 1 114 ? 34.509 7.635   27.284 1.00 29.27 ? 110 VAL A N   1 
ATOM   917  C CA  . VAL A 1 114 ? 33.234 6.934   27.538 1.00 28.26 ? 110 VAL A CA  1 
ATOM   918  C C   . VAL A 1 114 ? 32.888 7.229   28.990 1.00 29.42 ? 110 VAL A C   1 
ATOM   919  O O   . VAL A 1 114 ? 33.656 6.826   29.879 1.00 27.87 ? 110 VAL A O   1 
ATOM   920  C CB  . VAL A 1 114 ? 33.354 5.425   27.267 1.00 27.97 ? 110 VAL A CB  1 
ATOM   921  C CG1 . VAL A 1 114 ? 32.028 4.718   27.412 1.00 29.80 ? 110 VAL A CG1 1 
ATOM   922  C CG2 . VAL A 1 114 ? 33.981 5.149   25.894 1.00 29.17 ? 110 VAL A CG2 1 
ATOM   923  N N   . LYS A 1 115 ? 31.779 7.926   29.221 1.00 29.30 ? 111 LYS A N   1 
ATOM   924  C CA  . LYS A 1 115 ? 31.405 8.290   30.606 1.00 29.08 ? 111 LYS A CA  1 
ATOM   925  C C   . LYS A 1 115 ? 29.919 8.617   30.644 1.00 29.11 ? 111 LYS A C   1 
ATOM   926  O O   . LYS A 1 115 ? 29.331 8.821   29.569 1.00 29.35 ? 111 LYS A O   1 
ATOM   927  C CB  . LYS A 1 115 ? 32.227 9.508   31.039 1.00 29.52 ? 111 LYS A CB  1 
ATOM   928  C CG  . LYS A 1 115 ? 31.870 10.798  30.356 1.00 32.61 ? 111 LYS A CG  1 
ATOM   929  C CD  . LYS A 1 115 ? 32.756 11.939  30.814 1.00 40.79 ? 111 LYS A CD  1 
ATOM   930  C CE  . LYS A 1 115 ? 34.072 11.950  30.079 1.00 46.99 ? 111 LYS A CE  1 
ATOM   931  N NZ  . LYS A 1 115 ? 33.952 12.554  28.729 1.00 54.94 ? 111 LYS A NZ  1 
ATOM   932  N N   . PHE A 1 116 ? 29.357 8.698   31.843 1.00 30.72 ? 112 PHE A N   1 
ATOM   933  C CA  . PHE A 1 116 ? 27.983 9.202   32.042 1.00 29.96 ? 112 PHE A CA  1 
ATOM   934  C C   . PHE A 1 116 ? 28.002 10.735  32.005 1.00 32.04 ? 112 PHE A C   1 
ATOM   935  O O   . PHE A 1 116 ? 28.888 11.388  32.594 1.00 32.60 ? 112 PHE A O   1 
ATOM   936  C CB  . PHE A 1 116 ? 27.412 8.673   33.355 1.00 29.92 ? 112 PHE A CB  1 
ATOM   937  C CG  . PHE A 1 116 ? 26.884 7.270   33.209 1.00 30.91 ? 112 PHE A CG  1 
ATOM   938  C CD1 . PHE A 1 116 ? 25.574 7.055   32.802 1.00 33.79 ? 112 PHE A CD1 1 
ATOM   939  C CD2 . PHE A 1 116 ? 27.704 6.182   33.461 1.00 31.46 ? 112 PHE A CD2 1 
ATOM   940  C CE1 . PHE A 1 116 ? 25.086 5.759   32.687 1.00 34.35 ? 112 PHE A CE1 1 
ATOM   941  C CE2 . PHE A 1 116 ? 27.218 4.890   33.323 1.00 33.16 ? 112 PHE A CE2 1 
ATOM   942  C CZ  . PHE A 1 116 ? 25.906 4.684   32.946 1.00 33.53 ? 112 PHE A CZ  1 
ATOM   943  N N   . GLU A 1 117 ? 27.034 11.257  31.260 1.00 30.59 ? 113 GLU A N   1 
ATOM   944  C CA  A GLU A 1 117 ? 26.580 12.662  31.352 0.50 29.72 ? 113 GLU A CA  1 
ATOM   945  C CA  B GLU A 1 117 ? 26.548 12.659  31.300 0.50 31.07 ? 113 GLU A CA  1 
ATOM   946  C C   . GLU A 1 117 ? 25.117 12.574  31.808 1.00 27.82 ? 113 GLU A C   1 
ATOM   947  O O   . GLU A 1 117 ? 24.209 12.272  30.988 1.00 30.21 ? 113 GLU A O   1 
ATOM   948  C CB  A GLU A 1 117 ? 26.941 13.341  30.031 0.50 29.59 ? 113 GLU A CB  1 
ATOM   949  C CB  B GLU A 1 117 ? 26.518 13.304  29.915 0.50 33.37 ? 113 GLU A CB  1 
ATOM   950  C CG  A GLU A 1 117 ? 28.404 13.127  29.697 0.50 30.69 ? 113 GLU A CG  1 
ATOM   951  C CG  B GLU A 1 117 ? 27.885 13.508  29.321 0.50 33.55 ? 113 GLU A CG  1 
ATOM   952  C CD  A GLU A 1 117 ? 28.890 13.711  28.388 0.50 32.78 ? 113 GLU A CD  1 
ATOM   953  C CD  B GLU A 1 117 ? 28.715 14.584  29.997 0.50 39.03 ? 113 GLU A CD  1 
ATOM   954  O OE1 A GLU A 1 117 ? 28.156 14.494  27.783 0.50 33.50 ? 113 GLU A OE1 1 
ATOM   955  O OE1 B GLU A 1 117 ? 28.190 15.280  30.894 0.50 37.17 ? 113 GLU A OE1 1 
ATOM   956  O OE2 A GLU A 1 117 ? 30.009 13.357  27.991 0.50 31.37 ? 113 GLU A OE2 1 
ATOM   957  O OE2 B GLU A 1 117 ? 29.874 14.731  29.602 0.50 38.64 ? 113 GLU A OE2 1 
ATOM   958  N N   . GLY A 1 118 ? 24.938 12.778  33.101 1.00 29.59 ? 114 GLY A N   1 
ATOM   959  C CA  . GLY A 1 118 ? 23.679 12.480  33.783 1.00 31.18 ? 114 GLY A CA  1 
ATOM   960  C C   . GLY A 1 118 ? 23.387 11.006  33.630 1.00 32.64 ? 114 GLY A C   1 
ATOM   961  O O   . GLY A 1 118 ? 24.258 10.173  33.997 1.00 34.32 ? 114 GLY A O   1 
ATOM   962  N N   . ASP A 1 119 ? 22.246 10.708  33.048 1.00 30.14 ? 115 ASP A N   1 
ATOM   963  C CA  . ASP A 1 119 ? 21.789 9.299   32.897 1.00 30.04 ? 115 ASP A CA  1 
ATOM   964  C C   . ASP A 1 119 ? 22.257 8.710   31.557 1.00 29.69 ? 115 ASP A C   1 
ATOM   965  O O   . ASP A 1 119 ? 21.978 7.524   31.359 1.00 31.28 ? 115 ASP A O   1 
ATOM   966  C CB  . ASP A 1 119 ? 20.277 9.202   33.030 1.00 33.15 ? 115 ASP A CB  1 
ATOM   967  C CG  . ASP A 1 119 ? 19.767 9.366   34.450 1.00 40.31 ? 115 ASP A CG  1 
ATOM   968  O OD1 . ASP A 1 119 ? 20.518 9.049   35.397 1.00 38.57 ? 115 ASP A OD1 1 
ATOM   969  O OD2 . ASP A 1 119 ? 18.630 9.885   34.574 1.00 44.23 ? 115 ASP A OD2 1 
ATOM   970  N N   . THR A 1 120 ? 22.829 9.511   30.649 1.00 30.91 ? 116 THR A N   1 
ATOM   971  C CA  . THR A 1 120 ? 23.217 9.076   29.299 1.00 29.91 ? 116 THR A CA  1 
ATOM   972  C C   . THR A 1 120 ? 24.663 8.565   29.310 1.00 31.15 ? 116 THR A C   1 
ATOM   973  O O   . THR A 1 120 ? 25.519 9.242   29.828 1.00 29.24 ? 116 THR A O   1 
ATOM   974  C CB  . THR A 1 120 ? 23.025 10.178  28.256 1.00 32.13 ? 116 THR A CB  1 
ATOM   975  O OG1 . THR A 1 120 ? 21.639 10.478  28.291 1.00 33.41 ? 116 THR A OG1 1 
ATOM   976  C CG2 . THR A 1 120 ? 23.431 9.766   26.866 1.00 31.06 ? 116 THR A CG2 1 
ATOM   977  N N   . LEU A 1 121 ? 24.896 7.374   28.739 1.00 28.37 ? 117 LEU A N   1 
ATOM   978  C CA  . LEU A 1 121 ? 26.274 6.875   28.479 1.00 28.01 ? 117 LEU A CA  1 
ATOM   979  C C   . LEU A 1 121 ? 26.730 7.506   27.165 1.00 27.64 ? 117 LEU A C   1 
ATOM   980  O O   . LEU A 1 121 ? 26.097 7.269   26.122 1.00 27.71 ? 117 LEU A O   1 
ATOM   981  C CB  . LEU A 1 121 ? 26.296 5.339   28.467 1.00 26.45 ? 117 LEU A CB  1 
ATOM   982  C CG  . LEU A 1 121 ? 27.670 4.668   28.449 1.00 25.58 ? 117 LEU A CG  1 
ATOM   983  C CD1 . LEU A 1 121 ? 28.304 4.740   27.086 1.00 28.31 ? 117 LEU A CD1 1 
ATOM   984  C CD2 . LEU A 1 121 ? 28.592 5.203   29.516 1.00 29.68 ? 117 LEU A CD2 1 
ATOM   985  N N   . VAL A 1 122 ? 27.765 8.355   27.231 1.00 27.62 ? 118 VAL A N   1 
ATOM   986  C CA  . VAL A 1 122 ? 28.225 9.125   26.061 1.00 26.69 ? 118 VAL A CA  1 
ATOM   987  C C   . VAL A 1 122 ? 29.600 8.600   25.660 1.00 25.96 ? 118 VAL A C   1 
ATOM   988  O O   . VAL A 1 122 ? 30.501 8.536   26.534 1.00 27.98 ? 118 VAL A O   1 
ATOM   989  C CB  . VAL A 1 122 ? 28.274 10.642  26.376 1.00 29.88 ? 118 VAL A CB  1 
ATOM   990  C CG1 . VAL A 1 122 ? 28.721 11.422  25.164 1.00 29.92 ? 118 VAL A CG1 1 
ATOM   991  C CG2 . VAL A 1 122 ? 26.915 11.170  26.873 1.00 30.83 ? 118 VAL A CG2 1 
ATOM   992  N N   . ASN A 1 123 ? 29.753 8.361   24.373 1.00 27.87 ? 119 ASN A N   1 
ATOM   993  C CA  . ASN A 1 123 ? 31.018 7.900   23.755 1.00 27.41 ? 119 ASN A CA  1 
ATOM   994  C C   . ASN A 1 123 ? 31.432 8.978   22.762 1.00 27.50 ? 119 ASN A C   1 
ATOM   995  O O   . ASN A 1 123 ? 30.816 9.053   21.708 1.00 29.24 ? 119 ASN A O   1 
ATOM   996  C CB  . ASN A 1 123 ? 30.782 6.542   23.081 1.00 28.81 ? 119 ASN A CB  1 
ATOM   997  C CG  . ASN A 1 123 ? 32.027 5.943   22.480 1.00 28.70 ? 119 ASN A CG  1 
ATOM   998  O OD1 . ASN A 1 123 ? 33.131 6.397   22.762 1.00 28.83 ? 119 ASN A OD1 1 
ATOM   999  N ND2 . ASN A 1 123 ? 31.847 4.967   21.600 1.00 30.20 ? 119 ASN A ND2 1 
ATOM   1000 N N   . ARG A 1 124 ? 32.434 9.773   23.105 1.00 26.63 ? 120 ARG A N   1 
ATOM   1001 C CA  . ARG A 1 124 ? 32.923 10.884  22.257 1.00 27.99 ? 120 ARG A CA  1 
ATOM   1002 C C   . ARG A 1 124 ? 34.259 10.455  21.657 1.00 28.54 ? 120 ARG A C   1 
ATOM   1003 O O   . ARG A 1 124 ? 35.187 10.176  22.455 1.00 30.01 ? 120 ARG A O   1 
ATOM   1004 C CB  . ARG A 1 124 ? 33.116 12.167  23.078 1.00 31.43 ? 120 ARG A CB  1 
ATOM   1005 C CG  . ARG A 1 124 ? 31.881 12.686  23.786 1.00 37.06 ? 120 ARG A CG  1 
ATOM   1006 C CD  . ARG A 1 124 ? 32.239 14.006  24.466 1.00 42.85 ? 120 ARG A CD  1 
ATOM   1007 N NE  . ARG A 1 124 ? 31.190 14.499  25.351 1.00 45.55 ? 120 ARG A NE  1 
ATOM   1008 C CZ  . ARG A 1 124 ? 30.887 15.783  25.550 1.00 47.56 ? 120 ARG A CZ  1 
ATOM   1009 N NH1 . ARG A 1 124 ? 29.908 16.088  26.384 1.00 39.94 ? 120 ARG A NH1 1 
ATOM   1010 N NH2 . ARG A 1 124 ? 31.541 16.749  24.910 1.00 50.48 ? 120 ARG A NH2 1 
ATOM   1011 N N   . ILE A 1 125 ? 34.358 10.426  20.332 1.00 28.32 ? 121 ILE A N   1 
ATOM   1012 C CA  . ILE A 1 125 ? 35.477 9.770   19.610 1.00 30.43 ? 121 ILE A CA  1 
ATOM   1013 C C   . ILE A 1 125 ? 36.102 10.765  18.634 1.00 30.43 ? 121 ILE A C   1 
ATOM   1014 O O   . ILE A 1 125 ? 35.348 11.452  17.932 1.00 31.09 ? 121 ILE A O   1 
ATOM   1015 C CB  . ILE A 1 125 ? 35.004 8.522   18.843 1.00 29.20 ? 121 ILE A CB  1 
ATOM   1016 C CG1 . ILE A 1 125 ? 34.130 7.559   19.650 1.00 30.53 ? 121 ILE A CG1 1 
ATOM   1017 C CG2 . ILE A 1 125 ? 36.223 7.811   18.294 1.00 32.27 ? 121 ILE A CG2 1 
ATOM   1018 C CD1 . ILE A 1 125 ? 33.169 6.803   18.784 1.00 32.79 ? 121 ILE A CD1 1 
ATOM   1019 N N   . GLU A 1 126 ? 37.435 10.764  18.573 1.00 32.51 ? 122 GLU A N   1 
ATOM   1020 C CA  . GLU A 1 126 ? 38.229 11.367  17.472 1.00 35.39 ? 122 GLU A CA  1 
ATOM   1021 C C   . GLU A 1 126 ? 38.932 10.233  16.728 1.00 32.15 ? 122 GLU A C   1 
ATOM   1022 O O   . GLU A 1 126 ? 39.507 9.347   17.405 1.00 31.77 ? 122 GLU A O   1 
ATOM   1023 C CB  . GLU A 1 126 ? 39.286 12.342  18.003 1.00 38.24 ? 122 GLU A CB  1 
ATOM   1024 C CG  . GLU A 1 126 ? 38.709 13.514  18.757 1.00 50.90 ? 122 GLU A CG  1 
ATOM   1025 C CD  . GLU A 1 126 ? 39.784 14.435  19.320 1.00 67.08 ? 122 GLU A CD  1 
ATOM   1026 O OE1 . GLU A 1 126 ? 40.185 14.245  20.508 1.00 72.52 ? 122 GLU A OE1 1 
ATOM   1027 O OE2 . GLU A 1 126 ? 40.235 15.327  18.562 1.00 74.79 ? 122 GLU A OE2 1 
ATOM   1028 N N   . LEU A 1 127 ? 38.842 10.225  15.398 1.00 31.28 ? 123 LEU A N   1 
ATOM   1029 C CA  . LEU A 1 127 ? 39.486 9.202   14.554 1.00 31.76 ? 123 LEU A CA  1 
ATOM   1030 C C   . LEU A 1 127 ? 40.350 9.924   13.522 1.00 34.75 ? 123 LEU A C   1 
ATOM   1031 O O   . LEU A 1 127 ? 39.851 10.869  12.891 1.00 34.43 ? 123 LEU A O   1 
ATOM   1032 C CB  . LEU A 1 127 ? 38.440 8.274   13.922 1.00 31.91 ? 123 LEU A CB  1 
ATOM   1033 C CG  . LEU A 1 127 ? 38.973 7.208   12.966 1.00 32.10 ? 123 LEU A CG  1 
ATOM   1034 C CD1 . LEU A 1 127 ? 38.003 6.023   12.886 1.00 32.39 ? 123 LEU A CD1 1 
ATOM   1035 C CD2 . LEU A 1 127 ? 39.204 7.783   11.585 1.00 34.40 ? 123 LEU A CD2 1 
ATOM   1036 N N   . LYS A 1 128 ? 41.591 9.479   13.386 1.00 34.59 ? 124 LYS A N   1 
ATOM   1037 C CA  . LYS A 1 128 ? 42.543 9.988   12.377 1.00 36.79 ? 124 LYS A CA  1 
ATOM   1038 C C   . LYS A 1 128 ? 43.050 8.788   11.594 1.00 35.29 ? 124 LYS A C   1 
ATOM   1039 O O   . LYS A 1 128 ? 43.550 7.847   12.199 1.00 34.75 ? 124 LYS A O   1 
ATOM   1040 C CB  . LYS A 1 128 ? 43.671 10.768  13.066 1.00 40.36 ? 124 LYS A CB  1 
ATOM   1041 C CG  . LYS A 1 128 ? 44.684 11.378  12.106 1.00 51.40 ? 124 LYS A CG  1 
ATOM   1042 C CD  . LYS A 1 128 ? 44.214 12.706  11.537 1.00 60.37 ? 124 LYS A CD  1 
ATOM   1043 C CE  . LYS A 1 128 ? 45.034 13.152  10.345 1.00 62.34 ? 124 LYS A CE  1 
ATOM   1044 N NZ  . LYS A 1 128 ? 46.460 13.315  10.695 1.00 68.83 ? 124 LYS A NZ  1 
ATOM   1045 N N   . GLY A 1 129 ? 42.884 8.802   10.275 1.00 36.40 ? 125 GLY A N   1 
ATOM   1046 C CA  . GLY A 1 129 ? 43.348 7.719   9.399  1.00 37.86 ? 125 GLY A CA  1 
ATOM   1047 C C   . GLY A 1 129 ? 44.391 8.256   8.424  1.00 40.24 ? 125 GLY A C   1 
ATOM   1048 O O   . GLY A 1 129 ? 44.180 9.365   7.900  1.00 38.81 ? 125 GLY A O   1 
ATOM   1049 N N   . VAL A 1 130 ? 45.494 7.538   8.246  1.00 41.76 ? 126 VAL A N   1 
ATOM   1050 C CA  . VAL A 1 130 ? 46.603 7.976   7.344  1.00 42.77 ? 126 VAL A CA  1 
ATOM   1051 C C   . VAL A 1 130 ? 47.055 6.805   6.477  1.00 44.77 ? 126 VAL A C   1 
ATOM   1052 O O   . VAL A 1 130 ? 46.866 5.616   6.860  1.00 41.02 ? 126 VAL A O   1 
ATOM   1053 C CB  . VAL A 1 130 ? 47.806 8.567   8.107  1.00 43.33 ? 126 VAL A CB  1 
ATOM   1054 C CG1 . VAL A 1 130 ? 47.440 9.831   8.875  1.00 45.57 ? 126 VAL A CG1 1 
ATOM   1055 C CG2 . VAL A 1 130 ? 48.462 7.526   9.011  1.00 45.87 ? 126 VAL A CG2 1 
ATOM   1056 N N   . ASP A 1 131 ? 47.681 7.153   5.352  1.00 45.11 ? 127 ASP A N   1 
ATOM   1057 C CA  . ASP A 1 131 ? 48.423 6.221   4.461  1.00 46.54 ? 127 ASP A CA  1 
ATOM   1058 C C   . ASP A 1 131 ? 47.455 5.253   3.789  1.00 43.24 ? 127 ASP A C   1 
ATOM   1059 O O   . ASP A 1 131 ? 47.899 4.145   3.444  1.00 46.98 ? 127 ASP A O   1 
ATOM   1060 C CB  . ASP A 1 131 ? 49.515 5.456   5.222  1.00 48.88 ? 127 ASP A CB  1 
ATOM   1061 C CG  . ASP A 1 131 ? 50.668 6.333   5.691  1.00 53.69 ? 127 ASP A CG  1 
ATOM   1062 O OD1 . ASP A 1 131 ? 50.699 7.524   5.332  1.00 59.00 ? 127 ASP A OD1 1 
ATOM   1063 O OD2 . ASP A 1 131 ? 51.531 5.818   6.411  1.00 64.40 ? 127 ASP A OD2 1 
ATOM   1064 N N   . PHE A 1 132 ? 46.190 5.634   3.589  1.00 42.79 ? 128 PHE A N   1 
ATOM   1065 C CA  . PHE A 1 132 ? 45.221 4.783   2.849  1.00 42.60 ? 128 PHE A CA  1 
ATOM   1066 C C   . PHE A 1 132 ? 45.405 4.974   1.325  1.00 42.05 ? 128 PHE A C   1 
ATOM   1067 O O   . PHE A 1 132 ? 45.684 6.091   0.877  1.00 45.58 ? 128 PHE A O   1 
ATOM   1068 C CB  . PHE A 1 132 ? 43.777 5.054   3.281  1.00 43.10 ? 128 PHE A CB  1 
ATOM   1069 C CG  . PHE A 1 132 ? 43.466 4.526   4.660  1.00 39.89 ? 128 PHE A CG  1 
ATOM   1070 C CD1 . PHE A 1 132 ? 43.712 5.305   5.785  1.00 40.83 ? 128 PHE A CD1 1 
ATOM   1071 C CD2 . PHE A 1 132 ? 43.016 3.223   4.827  1.00 41.08 ? 128 PHE A CD2 1 
ATOM   1072 C CE1 . PHE A 1 132 ? 43.490 4.789   7.052  1.00 37.93 ? 128 PHE A CE1 1 
ATOM   1073 C CE2 . PHE A 1 132 ? 42.782 2.713   6.098  1.00 40.13 ? 128 PHE A CE2 1 
ATOM   1074 C CZ  . PHE A 1 132 ? 43.025 3.503   7.199  1.00 36.44 ? 128 PHE A CZ  1 
ATOM   1075 N N   . LYS A 1 133 ? 45.217 3.887   0.578  1.00 46.88 ? 129 LYS A N   1 
ATOM   1076 C CA  . LYS A 1 133 ? 45.195 3.856   -0.912 1.00 49.29 ? 129 LYS A CA  1 
ATOM   1077 C C   . LYS A 1 133 ? 43.843 4.396   -1.404 1.00 54.58 ? 129 LYS A C   1 
ATOM   1078 O O   . LYS A 1 133 ? 42.786 3.843   -0.985 1.00 46.08 ? 129 LYS A O   1 
ATOM   1079 C CB  . LYS A 1 133 ? 45.422 2.416   -1.366 1.00 49.26 ? 129 LYS A CB  1 
ATOM   1080 C CG  . LYS A 1 133 ? 46.726 1.807   -0.897 1.00 51.74 ? 129 LYS A CG  1 
ATOM   1081 C CD  . LYS A 1 133 ? 46.795 0.321   -1.100 1.00 54.21 ? 129 LYS A CD  1 
ATOM   1082 C CE  . LYS A 1 133 ? 48.207 -0.193  -0.916 1.00 57.66 ? 129 LYS A CE  1 
ATOM   1083 N NZ  . LYS A 1 133 ? 48.245 -1.675  -0.979 1.00 64.94 ? 129 LYS A NZ  1 
ATOM   1084 N N   . GLU A 1 134 ? 43.835 5.442   -2.245 1.00 55.25 ? 130 GLU A N   1 
ATOM   1085 C CA  . GLU A 1 134 ? 42.579 6.165   -2.618 1.00 55.24 ? 130 GLU A CA  1 
ATOM   1086 C C   . GLU A 1 134 ? 41.615 5.230   -3.378 1.00 56.02 ? 130 GLU A C   1 
ATOM   1087 O O   . GLU A 1 134 ? 40.392 5.447   -3.274 1.00 54.64 ? 130 GLU A O   1 
ATOM   1088 C CB  . GLU A 1 134 ? 42.855 7.453   -3.395 1.00 56.54 ? 130 GLU A CB  1 
ATOM   1089 C CG  . GLU A 1 134 ? 43.422 8.586   -2.548 1.00 62.23 ? 130 GLU A CG  1 
ATOM   1090 C CD  . GLU A 1 134 ? 42.518 9.285   -1.528 1.00 64.88 ? 130 GLU A CD  1 
ATOM   1091 O OE1 . GLU A 1 134 ? 43.093 9.945   -0.615 1.00 62.67 ? 130 GLU A OE1 1 
ATOM   1092 O OE2 . GLU A 1 134 ? 41.256 9.216   -1.645 1.00 56.13 ? 130 GLU A OE2 1 
ATOM   1093 N N   . ASP A 1 135 ? 42.099 4.202   -4.077 1.00 54.55 ? 131 ASP A N   1 
ATOM   1094 C CA  . ASP A 1 135 ? 41.192 3.163   -4.631 1.00 61.99 ? 131 ASP A CA  1 
ATOM   1095 C C   . ASP A 1 135 ? 41.572 1.786   -4.067 1.00 57.51 ? 131 ASP A C   1 
ATOM   1096 O O   . ASP A 1 135 ? 41.434 0.781   -4.771 1.00 53.57 ? 131 ASP A O   1 
ATOM   1097 C CB  . ASP A 1 135 ? 41.117 3.218   -6.161 1.00 73.03 ? 131 ASP A CB  1 
ATOM   1098 C CG  . ASP A 1 135 ? 39.783 2.684   -6.675 1.00 81.11 ? 131 ASP A CG  1 
ATOM   1099 O OD1 . ASP A 1 135 ? 38.723 3.076   -6.115 1.00 73.03 ? 131 ASP A OD1 1 
ATOM   1100 O OD2 . ASP A 1 135 ? 39.802 1.851   -7.604 1.00 89.89 ? 131 ASP A OD2 1 
ATOM   1101 N N   . GLY A 1 136 ? 41.971 1.725   -2.798 1.00 53.22 ? 132 GLY A N   1 
ATOM   1102 C CA  . GLY A 1 136 ? 42.017 0.451   -2.063 1.00 47.30 ? 132 GLY A CA  1 
ATOM   1103 C C   . GLY A 1 136 ? 40.614 0.042   -1.651 1.00 45.35 ? 132 GLY A C   1 
ATOM   1104 O O   . GLY A 1 136 ? 39.648 0.666   -2.099 1.00 45.58 ? 132 GLY A O   1 
ATOM   1105 N N   . ASN A 1 137 ? 40.520 -0.964  -0.790 1.00 43.32 ? 133 ASN A N   1 
ATOM   1106 C CA  . ASN A 1 137 ? 39.260 -1.605  -0.346 1.00 43.54 ? 133 ASN A CA  1 
ATOM   1107 C C   . ASN A 1 137 ? 38.468 -0.689  0.598  1.00 43.48 ? 133 ASN A C   1 
ATOM   1108 O O   . ASN A 1 137 ? 37.255 -0.938  0.746  1.00 42.29 ? 133 ASN A O   1 
ATOM   1109 C CB  . ASN A 1 137 ? 39.549 -2.918  0.371  1.00 44.57 ? 133 ASN A CB  1 
ATOM   1110 C CG  . ASN A 1 137 ? 40.074 -3.969  -0.577 1.00 49.16 ? 133 ASN A CG  1 
ATOM   1111 O OD1 . ASN A 1 137 ? 40.927 -4.764  -0.206 1.00 56.32 ? 133 ASN A OD1 1 
ATOM   1112 N ND2 . ASN A 1 137 ? 39.585 -3.972  -1.802 1.00 49.42 ? 133 ASN A ND2 1 
ATOM   1113 N N   . ILE A 1 138 ? 39.138 0.267   1.247  1.00 39.95 ? 134 ILE A N   1 
ATOM   1114 C CA  . ILE A 1 138 ? 38.509 1.208   2.213  1.00 42.26 ? 134 ILE A CA  1 
ATOM   1115 C C   . ILE A 1 138 ? 38.062 2.454   1.459  1.00 40.68 ? 134 ILE A C   1 
ATOM   1116 O O   . ILE A 1 138 ? 36.836 2.642   1.327  1.00 41.59 ? 134 ILE A O   1 
ATOM   1117 C CB  . ILE A 1 138 ? 39.467 1.499   3.382  1.00 42.36 ? 134 ILE A CB  1 
ATOM   1118 C CG1 . ILE A 1 138 ? 39.609 0.237   4.227  1.00 43.35 ? 134 ILE A CG1 1 
ATOM   1119 C CG2 . ILE A 1 138 ? 38.999 2.694   4.193  1.00 40.99 ? 134 ILE A CG2 1 
ATOM   1120 C CD1 . ILE A 1 138 ? 40.742 0.263   5.184  1.00 45.88 ? 134 ILE A CD1 1 
ATOM   1121 N N   . LEU A 1 139 ? 38.998 3.264   0.940  1.00 42.18 ? 135 LEU A N   1 
ATOM   1122 C CA  . LEU A 1 139 ? 38.600 4.523   0.252  1.00 44.37 ? 135 LEU A CA  1 
ATOM   1123 C C   . LEU A 1 139 ? 37.845 4.193   -1.050 1.00 44.62 ? 135 LEU A C   1 
ATOM   1124 O O   . LEU A 1 139 ? 37.027 5.044   -1.490 1.00 44.77 ? 135 LEU A O   1 
ATOM   1125 C CB  . LEU A 1 139 ? 39.820 5.421   0.054  1.00 44.71 ? 135 LEU A CB  1 
ATOM   1126 C CG  . LEU A 1 139 ? 40.321 6.045   1.353  1.00 43.59 ? 135 LEU A CG  1 
ATOM   1127 C CD1 . LEU A 1 139 ? 41.488 6.980   1.096  1.00 47.94 ? 135 LEU A CD1 1 
ATOM   1128 C CD2 . LEU A 1 139 ? 39.198 6.793   2.079  1.00 49.91 ? 135 LEU A CD2 1 
ATOM   1129 N N   . GLY A 1 140 ? 38.016 2.977   -1.571 1.00 44.47 ? 136 GLY A N   1 
ATOM   1130 C CA  . GLY A 1 140 ? 37.318 2.490   -2.780 1.00 45.94 ? 136 GLY A CA  1 
ATOM   1131 C C   . GLY A 1 140 ? 35.957 1.884   -2.475 1.00 48.18 ? 136 GLY A C   1 
ATOM   1132 O O   . GLY A 1 140 ? 35.245 1.540   -3.423 1.00 47.10 ? 136 GLY A O   1 
ATOM   1133 N N   . HIS A 1 141 ? 35.581 1.734   -1.203 1.00 45.19 ? 137 HIS A N   1 
ATOM   1134 C CA  . HIS A 1 141 ? 34.281 1.129   -0.788 1.00 45.13 ? 137 HIS A CA  1 
ATOM   1135 C C   . HIS A 1 141 ? 34.090 -0.255  -1.419 1.00 43.39 ? 137 HIS A C   1 
ATOM   1136 O O   . HIS A 1 141 ? 33.060 -0.478  -2.086 1.00 44.93 ? 137 HIS A O   1 
ATOM   1137 C CB  . HIS A 1 141 ? 33.085 2.033   -1.145 1.00 43.64 ? 137 HIS A CB  1 
ATOM   1138 C CG  . HIS A 1 141 ? 33.081 3.361   -0.459 1.00 48.27 ? 137 HIS A CG  1 
ATOM   1139 N ND1 . HIS A 1 141 ? 32.486 3.545   0.778  1.00 47.29 ? 137 HIS A ND1 1 
ATOM   1140 C CD2 . HIS A 1 141 ? 33.570 4.565   -0.832 1.00 47.10 ? 137 HIS A CD2 1 
ATOM   1141 C CE1 . HIS A 1 141 ? 32.626 4.807   1.138  1.00 45.79 ? 137 HIS A CE1 1 
ATOM   1142 N NE2 . HIS A 1 141 ? 33.298 5.450   0.176  1.00 47.61 ? 137 HIS A NE2 1 
ATOM   1143 N N   . LYS A 1 142 ? 34.991 -1.195  -1.160 1.00 44.33 ? 138 LYS A N   1 
ATOM   1144 C CA  . LYS A 1 142 ? 34.910 -2.550  -1.765 1.00 43.70 ? 138 LYS A CA  1 
ATOM   1145 C C   . LYS A 1 142 ? 34.717 -3.620  -0.691 1.00 40.49 ? 138 LYS A C   1 
ATOM   1146 O O   . LYS A 1 142 ? 35.056 -4.798  -0.970 1.00 40.75 ? 138 LYS A O   1 
ATOM   1147 C CB  . LYS A 1 142 ? 36.184 -2.799  -2.579 1.00 48.01 ? 138 LYS A CB  1 
ATOM   1148 C CG  . LYS A 1 142 ? 36.385 -1.871  -3.771 1.00 54.14 ? 138 LYS A CG  1 
ATOM   1149 C CD  . LYS A 1 142 ? 37.721 -2.080  -4.422 1.00 55.19 ? 138 LYS A CD  1 
ATOM   1150 C CE  . LYS A 1 142 ? 38.151 -0.914  -5.278 1.00 59.71 ? 138 LYS A CE  1 
ATOM   1151 N NZ  . LYS A 1 142 ? 39.484 -1.176  -5.857 1.00 59.46 ? 138 LYS A NZ  1 
ATOM   1152 N N   . LEU A 1 143 ? 34.225 -3.239  0.503  1.00 39.26 ? 139 LEU A N   1 
ATOM   1153 C CA  . LEU A 1 143 ? 33.950 -4.191  1.601  1.00 40.30 ? 139 LEU A CA  1 
ATOM   1154 C C   . LEU A 1 143 ? 32.476 -4.577  1.589  1.00 40.61 ? 139 LEU A C   1 
ATOM   1155 O O   . LEU A 1 143 ? 31.602 -3.686  1.391  1.00 46.87 ? 139 LEU A O   1 
ATOM   1156 C CB  . LEU A 1 143 ? 34.353 -3.592  2.960  1.00 37.08 ? 139 LEU A CB  1 
ATOM   1157 C CG  . LEU A 1 143 ? 35.816 -3.203  3.088  1.00 39.61 ? 139 LEU A CG  1 
ATOM   1158 C CD1 . LEU A 1 143 ? 36.136 -2.677  4.492  1.00 39.83 ? 139 LEU A CD1 1 
ATOM   1159 C CD2 . LEU A 1 143 ? 36.712 -4.384  2.779  1.00 38.28 ? 139 LEU A CD2 1 
ATOM   1160 N N   . GLU A 1 144 ? 32.204 -5.834  1.910  1.00 43.34 ? 140 GLU A N   1 
ATOM   1161 C CA  . GLU A 1 144 ? 30.823 -6.318  2.139  1.00 45.27 ? 140 GLU A CA  1 
ATOM   1162 C C   . GLU A 1 144 ? 30.251 -5.593  3.366  1.00 49.26 ? 140 GLU A C   1 
ATOM   1163 O O   . GLU A 1 144 ? 30.992 -5.407  4.340  1.00 44.55 ? 140 GLU A O   1 
ATOM   1164 C CB  . GLU A 1 144 ? 30.817 -7.839  2.289  1.00 47.85 ? 140 GLU A CB  1 
ATOM   1165 C CG  . GLU A 1 144 ? 31.337 -8.568  1.052  1.00 50.41 ? 140 GLU A CG  1 
ATOM   1166 C CD  . GLU A 1 144 ? 30.312 -8.803  -0.041 1.00 60.13 ? 140 GLU A CD  1 
ATOM   1167 O OE1 . GLU A 1 144 ? 29.305 -8.078  -0.060 1.00 56.65 ? 140 GLU A OE1 1 
ATOM   1168 O OE2 . GLU A 1 144 ? 30.519 -9.723  -0.857 1.00 58.80 ? 140 GLU A OE2 1 
ATOM   1169 N N   . TYR A 1 145 ? 29.017 -5.089  3.258  1.00 52.33 ? 141 TYR A N   1 
ATOM   1170 C CA  A TYR A 1 145 ? 28.232 -4.534  4.400  0.60 51.86 ? 141 TYR A CA  1 
ATOM   1171 C CA  B TYR A 1 145 ? 28.248 -4.530  4.401  0.40 56.20 ? 141 TYR A CA  1 
ATOM   1172 C C   . TYR A 1 145 ? 27.664 -5.712  5.185  1.00 53.41 ? 141 TYR A C   1 
ATOM   1173 O O   . TYR A 1 145 ? 26.469 -6.002  5.065  1.00 52.48 ? 141 TYR A O   1 
ATOM   1174 C CB  A TYR A 1 145 ? 27.117 -3.588  3.934  0.60 49.47 ? 141 TYR A CB  1 
ATOM   1175 C CB  B TYR A 1 145 ? 27.218 -3.510  3.900  0.40 60.19 ? 141 TYR A CB  1 
ATOM   1176 C CG  A TYR A 1 145 ? 26.352 -2.891  5.037  0.60 45.39 ? 141 TYR A CG  1 
ATOM   1177 C CG  B TYR A 1 145 ? 27.804 -2.328  3.159  0.40 64.64 ? 141 TYR A CG  1 
ATOM   1178 C CD1 A TYR A 1 145 ? 26.865 -1.762  5.671  0.60 45.66 ? 141 TYR A CD1 1 
ATOM   1179 C CD1 B TYR A 1 145 ? 28.280 -1.212  3.837  0.40 67.07 ? 141 TYR A CD1 1 
ATOM   1180 C CD2 A TYR A 1 145 ? 25.090 -3.329  5.419  0.60 45.78 ? 141 TYR A CD2 1 
ATOM   1181 C CD2 B TYR A 1 145 ? 27.874 -2.320  1.772  0.40 63.68 ? 141 TYR A CD2 1 
ATOM   1182 C CE1 A TYR A 1 145 ? 26.168 -1.117  6.684  0.60 40.42 ? 141 TYR A CE1 1 
ATOM   1183 C CE1 B TYR A 1 145 ? 28.813 -0.126  3.160  0.40 68.04 ? 141 TYR A CE1 1 
ATOM   1184 C CE2 A TYR A 1 145 ? 24.378 -2.691  6.427  0.60 44.59 ? 141 TYR A CE2 1 
ATOM   1185 C CE2 B TYR A 1 145 ? 28.401 -1.243  1.080  0.40 62.57 ? 141 TYR A CE2 1 
ATOM   1186 C CZ  A TYR A 1 145 ? 24.917 -1.582  7.061  0.60 42.26 ? 141 TYR A CZ  1 
ATOM   1187 C CZ  B TYR A 1 145 ? 28.869 -0.143  1.775  0.40 66.58 ? 141 TYR A CZ  1 
ATOM   1188 O OH  A TYR A 1 145 ? 24.188 -0.951  8.026  0.60 39.17 ? 141 TYR A OH  1 
ATOM   1189 O OH  B TYR A 1 145 ? 29.389 0.908   1.077  0.40 66.78 ? 141 TYR A OH  1 
ATOM   1190 N N   . ASN A 1 146 ? 28.510 -6.391  5.958  1.00 51.24 ? 142 ASN A N   1 
ATOM   1191 C CA  . ASN A 1 146 ? 28.019 -7.517  6.787  1.00 53.18 ? 142 ASN A CA  1 
ATOM   1192 C C   . ASN A 1 146 ? 28.577 -7.385  8.219  1.00 53.24 ? 142 ASN A C   1 
ATOM   1193 O O   . ASN A 1 146 ? 29.566 -6.568  8.475  1.00 49.72 ? 142 ASN A O   1 
ATOM   1194 C CB  . ASN A 1 146 ? 28.283 -8.859  6.107  1.00 61.25 ? 142 ASN A CB  1 
ATOM   1195 C CG  . ASN A 1 146 ? 29.762 -9.093  5.946  1.00 56.99 ? 142 ASN A CG  1 
ATOM   1196 O OD1 . ASN A 1 146 ? 30.526 -8.712  6.824  1.00 64.60 ? 142 ASN A OD1 1 
ATOM   1197 N ND2 . ASN A 1 146 ? 30.164 -9.688  4.837  1.00 60.63 ? 142 ASN A ND2 1 
ATOM   1198 N N   . ALA A 1 147 ? 27.907 -8.128  9.102  1.00 54.15 ? 143 ALA A N   1 
ATOM   1199 C CA  . ALA A 1 147 ? 28.061 -8.120  10.576 1.00 59.14 ? 143 ALA A CA  1 
ATOM   1200 C C   . ALA A 1 147 ? 29.464 -8.623  10.920 1.00 58.73 ? 143 ALA A C   1 
ATOM   1201 O O   . ALA A 1 147 ? 29.971 -9.516  10.216 1.00 54.29 ? 143 ALA A O   1 
ATOM   1202 C CB  . ALA A 1 147 ? 26.971 -8.953  11.221 1.00 57.25 ? 143 ALA A CB  1 
ATOM   1203 N N   . ILE A 1 148 ? 30.080 -8.022  11.935 1.00 53.13 ? 144 ILE A N   1 
ATOM   1204 C CA  . ILE A 1 148 ? 31.390 -8.463  12.479 1.00 55.86 ? 144 ILE A CA  1 
ATOM   1205 C C   . ILE A 1 148 ? 31.118 -8.987  13.896 1.00 54.92 ? 144 ILE A C   1 
ATOM   1206 O O   . ILE A 1 148 ? 30.514 -8.260  14.712 1.00 54.48 ? 144 ILE A O   1 
ATOM   1207 C CB  . ILE A 1 148 ? 32.441 -7.333  12.383 1.00 58.04 ? 144 ILE A CB  1 
ATOM   1208 C CG1 . ILE A 1 148 ? 32.246 -6.244  13.433 1.00 62.34 ? 144 ILE A CG1 1 
ATOM   1209 C CG2 . ILE A 1 148 ? 32.479 -6.725  10.976 1.00 57.61 ? 144 ILE A CG2 1 
ATOM   1210 C CD1 . ILE A 1 148 ? 33.469 -5.372  13.609 1.00 64.16 ? 144 ILE A CD1 1 
ATOM   1211 N N   . SER A 1 149 ? 31.466 -10.248 14.127 1.00 49.09 ? 145 SER A N   1 
ATOM   1212 C CA  . SER A 1 149 ? 31.327 -10.955 15.421 1.00 47.13 ? 145 SER A CA  1 
ATOM   1213 C C   . SER A 1 149 ? 32.725 -11.400 15.856 1.00 44.64 ? 145 SER A C   1 
ATOM   1214 O O   . SER A 1 149 ? 33.675 -11.267 15.067 1.00 50.41 ? 145 SER A O   1 
ATOM   1215 C CB  . SER A 1 149 ? 30.343 -12.091 15.286 1.00 49.11 ? 145 SER A CB  1 
ATOM   1216 O OG  . SER A 1 149 ? 29.019 -11.573 15.051 1.00 52.05 ? 145 SER A OG  1 
ATOM   1217 N N   . GLY A 1 150 ? 32.878 -11.840 17.091 1.00 41.89 ? 146 GLY A N   1 
ATOM   1218 C CA  . GLY A 1 150 ? 34.136 -12.463 17.515 1.00 40.94 ? 146 GLY A CA  1 
ATOM   1219 C C   . GLY A 1 150 ? 34.619 -11.888 18.828 1.00 39.12 ? 146 GLY A C   1 
ATOM   1220 O O   . GLY A 1 150 ? 33.818 -11.221 19.542 1.00 35.44 ? 146 GLY A O   1 
ATOM   1221 N N   . ASN A 1 151 ? 35.886 -12.137 19.145 1.00 38.01 ? 147 ASN A N   1 
ATOM   1222 C CA  . ASN A 1 151 ? 36.387 -12.003 20.540 1.00 36.35 ? 147 ASN A CA  1 
ATOM   1223 C C   . ASN A 1 151 ? 37.343 -10.818 20.643 1.00 40.82 ? 147 ASN A C   1 
ATOM   1224 O O   . ASN A 1 151 ? 38.153 -10.606 19.717 1.00 40.90 ? 147 ASN A O   1 
ATOM   1225 C CB  . ASN A 1 151 ? 37.061 -13.286 21.003 1.00 38.26 ? 147 ASN A CB  1 
ATOM   1226 C CG  . ASN A 1 151 ? 36.091 -14.444 21.129 1.00 39.48 ? 147 ASN A CG  1 
ATOM   1227 O OD1 . ASN A 1 151 ? 34.867 -14.281 21.198 1.00 37.06 ? 147 ASN A OD1 1 
ATOM   1228 N ND2 . ASN A 1 151 ? 36.642 -15.637 21.205 1.00 43.97 ? 147 ASN A ND2 1 
ATOM   1229 N N   . ALA A 1 152 ? 37.234 -10.066 21.733 1.00 34.50 ? 148 ALA A N   1 
ATOM   1230 C CA  . ALA A 1 152 ? 38.248 -9.062  22.132 1.00 34.60 ? 148 ALA A CA  1 
ATOM   1231 C C   . ALA A 1 152 ? 38.979 -9.573  23.362 1.00 31.93 ? 148 ALA A C   1 
ATOM   1232 O O   . ALA A 1 152 ? 38.326 -9.761  24.384 1.00 31.49 ? 148 ALA A O   1 
ATOM   1233 C CB  . ALA A 1 152 ? 37.593 -7.729  22.399 1.00 35.39 ? 148 ALA A CB  1 
ATOM   1234 N N   . ASN A 1 153 ? 40.295 -9.786  23.262 1.00 31.66 ? 149 ASN A N   1 
ATOM   1235 C CA  . ASN A 1 153 ? 41.124 -10.365 24.351 1.00 32.04 ? 149 ASN A CA  1 
ATOM   1236 C C   . ASN A 1 153 ? 41.524 -9.244  25.295 1.00 32.72 ? 149 ASN A C   1 
ATOM   1237 O O   . ASN A 1 153 ? 42.111 -8.300  24.825 1.00 34.28 ? 149 ASN A O   1 
ATOM   1238 C CB  . ASN A 1 153 ? 42.352 -11.072 23.789 1.00 34.72 ? 149 ASN A CB  1 
ATOM   1239 C CG  . ASN A 1 153 ? 41.944 -12.183 22.857 1.00 36.36 ? 149 ASN A CG  1 
ATOM   1240 O OD1 . ASN A 1 153 ? 42.135 -12.081 21.628 1.00 42.83 ? 149 ASN A OD1 1 
ATOM   1241 N ND2 . ASN A 1 153 ? 41.291 -13.182 23.424 1.00 35.16 ? 149 ASN A ND2 1 
ATOM   1242 N N   . ILE A 1 154 ? 41.195 -9.378  26.573 1.00 31.22 ? 150 ILE A N   1 
ATOM   1243 C CA  . ILE A 1 154 ? 41.411 -8.335  27.610 1.00 30.07 ? 150 ILE A CA  1 
ATOM   1244 C C   . ILE A 1 154 ? 42.529 -8.783  28.536 1.00 32.19 ? 150 ILE A C   1 
ATOM   1245 O O   . ILE A 1 154 ? 42.504 -9.951  28.965 1.00 34.06 ? 150 ILE A O   1 
ATOM   1246 C CB  . ILE A 1 154 ? 40.123 -8.089  28.438 1.00 32.82 ? 150 ILE A CB  1 
ATOM   1247 C CG1 . ILE A 1 154 ? 38.893 -7.905  27.547 1.00 35.09 ? 150 ILE A CG1 1 
ATOM   1248 C CG2 . ILE A 1 154 ? 40.316 -6.893  29.380 1.00 35.29 ? 150 ILE A CG2 1 
ATOM   1249 C CD1 . ILE A 1 154 ? 38.964 -6.760  26.594 1.00 36.50 ? 150 ILE A CD1 1 
ATOM   1250 N N   . THR A 1 155 ? 43.429 -7.866  28.874 1.00 33.16 ? 151 THR A N   1 
ATOM   1251 C CA  . THR A 1 155 ? 44.505 -8.145  29.857 1.00 33.82 ? 151 THR A CA  1 
ATOM   1252 C C   . THR A 1 155 ? 44.675 -6.913  30.732 1.00 36.22 ? 151 THR A C   1 
ATOM   1253 O O   . THR A 1 155 ? 44.408 -5.826  30.262 1.00 34.26 ? 151 THR A O   1 
ATOM   1254 C CB  . THR A 1 155 ? 45.785 -8.553  29.103 1.00 37.74 ? 151 THR A CB  1 
ATOM   1255 O OG1 . THR A 1 155 ? 46.653 -9.148  30.064 1.00 48.74 ? 151 THR A OG1 1 
ATOM   1256 C CG2 . THR A 1 155 ? 46.416 -7.381  28.379 1.00 34.29 ? 151 THR A CG2 1 
ATOM   1257 N N   . ALA A 1 156 ? 45.146 -7.087  31.967 1.00 34.73 ? 152 ALA A N   1 
ATOM   1258 C CA  . ALA A 1 156 ? 45.382 -5.961  32.877 1.00 30.91 ? 152 ALA A CA  1 
ATOM   1259 C C   . ALA A 1 156 ? 46.558 -5.131  32.384 1.00 32.10 ? 152 ALA A C   1 
ATOM   1260 O O   . ALA A 1 156 ? 47.468 -5.687  31.716 1.00 35.73 ? 152 ALA A O   1 
ATOM   1261 C CB  . ALA A 1 156 ? 45.607 -6.443  34.279 1.00 32.99 ? 152 ALA A CB  1 
ATOM   1262 N N   . ASP A 1 157 ? 46.533 -3.849  32.695 1.00 31.20 ? 153 ASP A N   1 
ATOM   1263 C CA  . ASP A 1 157 ? 47.646 -2.907  32.418 1.00 32.72 ? 153 ASP A CA  1 
ATOM   1264 C C   . ASP A 1 157 ? 47.895 -2.139  33.707 1.00 31.09 ? 153 ASP A C   1 
ATOM   1265 O O   . ASP A 1 157 ? 47.508 -0.958  33.804 1.00 32.63 ? 153 ASP A O   1 
ATOM   1266 C CB  . ASP A 1 157 ? 47.366 -2.038  31.202 1.00 35.20 ? 153 ASP A CB  1 
ATOM   1267 C CG  . ASP A 1 157 ? 48.556 -1.195  30.776 1.00 42.98 ? 153 ASP A CG  1 
ATOM   1268 O OD1 . ASP A 1 157 ? 49.645 -1.299  31.430 1.00 41.06 ? 153 ASP A OD1 1 
ATOM   1269 O OD2 . ASP A 1 157 ? 48.359 -0.366  29.867 1.00 40.90 ? 153 ASP A OD2 1 
ATOM   1270 N N   . LYS A 1 158 ? 48.512 -2.799  34.673 1.00 31.83 ? 154 LYS A N   1 
ATOM   1271 C CA  . LYS A 1 158 ? 48.688 -2.220  36.024 1.00 32.04 ? 154 LYS A CA  1 
ATOM   1272 C C   . LYS A 1 158 ? 49.460 -0.909  35.935 1.00 30.67 ? 154 LYS A C   1 
ATOM   1273 O O   . LYS A 1 158 ? 49.156 -0.026  36.696 1.00 31.00 ? 154 LYS A O   1 
ATOM   1274 C CB  . LYS A 1 158 ? 49.348 -3.202  36.990 1.00 35.22 ? 154 LYS A CB  1 
ATOM   1275 C CG  . LYS A 1 158 ? 49.344 -2.712  38.424 1.00 34.81 ? 154 LYS A CG  1 
ATOM   1276 C CD  . LYS A 1 158 ? 49.680 -3.728  39.469 1.00 40.24 ? 154 LYS A CD  1 
ATOM   1277 C CE  . LYS A 1 158 ? 49.620 -3.052  40.833 1.00 43.19 ? 154 LYS A CE  1 
ATOM   1278 N NZ  . LYS A 1 158 ? 49.807 -4.012  41.939 1.00 48.26 ? 154 LYS A NZ  1 
ATOM   1279 N N   . GLN A 1 159 ? 50.453 -0.787  35.043 1.00 32.94 ? 155 GLN A N   1 
ATOM   1280 C CA  . GLN A 1 159 ? 51.282 0.446   34.986 1.00 31.54 ? 155 GLN A CA  1 
ATOM   1281 C C   . GLN A 1 159 ? 50.378 1.647   34.728 1.00 33.62 ? 155 GLN A C   1 
ATOM   1282 O O   . GLN A 1 159 ? 50.697 2.770   35.194 1.00 34.51 ? 155 GLN A O   1 
ATOM   1283 C CB  . GLN A 1 159 ? 52.369 0.366   33.912 1.00 32.24 ? 155 GLN A CB  1 
ATOM   1284 C CG  . GLN A 1 159 ? 53.433 1.431   34.091 1.00 33.96 ? 155 GLN A CG  1 
ATOM   1285 C CD  . GLN A 1 159 ? 54.619 1.208   33.175 1.00 32.61 ? 155 GLN A CD  1 
ATOM   1286 O OE1 . GLN A 1 159 ? 54.730 0.190   32.516 1.00 33.45 ? 155 GLN A OE1 1 
ATOM   1287 N NE2 . GLN A 1 159 ? 55.525 2.163   33.143 1.00 35.80 ? 155 GLN A NE2 1 
ATOM   1288 N N   . LYS A 1 160 ? 49.320 1.445   33.944 1.00 32.67 ? 156 LYS A N   1 
ATOM   1289 C CA  . LYS A 1 160 ? 48.383 2.534   33.528 1.00 34.68 ? 156 LYS A CA  1 
ATOM   1290 C C   . LYS A 1 160 ? 47.076 2.482   34.336 1.00 34.35 ? 156 LYS A C   1 
ATOM   1291 O O   . LYS A 1 160 ? 46.172 3.304   34.045 1.00 35.60 ? 156 LYS A O   1 
ATOM   1292 C CB  . LYS A 1 160 ? 48.120 2.427   32.024 1.00 38.29 ? 156 LYS A CB  1 
ATOM   1293 C CG  . LYS A 1 160 ? 49.337 2.745   31.162 1.00 49.26 ? 156 LYS A CG  1 
ATOM   1294 C CD  . LYS A 1 160 ? 49.636 4.226   31.148 1.00 58.14 ? 156 LYS A CD  1 
ATOM   1295 C CE  . LYS A 1 160 ? 51.001 4.585   31.699 1.00 67.45 ? 156 LYS A CE  1 
ATOM   1296 N NZ  . LYS A 1 160 ? 52.106 4.078   30.851 1.00 70.08 ? 156 LYS A NZ  1 
ATOM   1297 N N   . ASN A 1 161 ? 47.001 1.610   35.342 1.00 32.36 ? 157 ASN A N   1 
ATOM   1298 C CA  . ASN A 1 161 ? 45.790 1.404   36.179 1.00 32.10 ? 157 ASN A CA  1 
ATOM   1299 C C   . ASN A 1 161 ? 44.607 1.135   35.246 1.00 34.83 ? 157 ASN A C   1 
ATOM   1300 O O   . ASN A 1 161 ? 43.502 1.647   35.507 1.00 30.85 ? 157 ASN A O   1 
ATOM   1301 C CB  . ASN A 1 161 ? 45.509 2.614   37.069 1.00 33.72 ? 157 ASN A CB  1 
ATOM   1302 C CG  . ASN A 1 161 ? 44.591 2.270   38.227 1.00 36.08 ? 157 ASN A CG  1 
ATOM   1303 O OD1 . ASN A 1 161 ? 44.629 1.162   38.767 1.00 39.63 ? 157 ASN A OD1 1 
ATOM   1304 N ND2 . ASN A 1 161 ? 43.735 3.206   38.574 1.00 40.45 ? 157 ASN A ND2 1 
ATOM   1305 N N   . GLY A 1 162 ? 44.824 0.340   34.214 1.00 30.79 ? 158 GLY A N   1 
ATOM   1306 C CA  . GLY A 1 162 ? 43.745 0.062   33.240 1.00 31.63 ? 158 GLY A CA  1 
ATOM   1307 C C   . GLY A 1 162 ? 43.869 -1.293  32.620 1.00 29.37 ? 158 GLY A C   1 
ATOM   1308 O O   . GLY A 1 162 ? 44.302 -2.252  33.285 1.00 31.04 ? 158 GLY A O   1 
ATOM   1309 N N   . ILE A 1 163 ? 43.484 -1.388  31.344 1.00 29.12 ? 159 ILE A N   1 
ATOM   1310 C CA  . ILE A 1 163 ? 43.492 -2.656  30.588 1.00 31.49 ? 159 ILE A CA  1 
ATOM   1311 C C   . ILE A 1 163 ? 44.087 -2.382  29.208 1.00 29.82 ? 159 ILE A C   1 
ATOM   1312 O O   . ILE A 1 163 ? 44.134 -1.215  28.758 1.00 29.36 ? 159 ILE A O   1 
ATOM   1313 C CB  . ILE A 1 163 ? 42.088 -3.301  30.502 1.00 30.59 ? 159 ILE A CB  1 
ATOM   1314 C CG1 . ILE A 1 163 ? 41.053 -2.431  29.756 1.00 34.26 ? 159 ILE A CG1 1 
ATOM   1315 C CG2 . ILE A 1 163 ? 41.566 -3.653  31.890 1.00 31.80 ? 159 ILE A CG2 1 
ATOM   1316 C CD1 . ILE A 1 163 ? 40.960 -2.652  28.249 1.00 39.89 ? 159 ILE A CD1 1 
ATOM   1317 N N   . LYS A 1 164 ? 44.534 -3.458  28.589 1.00 29.02 ? 160 LYS A N   1 
ATOM   1318 C CA  . LYS A 1 164 ? 44.857 -3.515  27.152 1.00 31.45 ? 160 LYS A CA  1 
ATOM   1319 C C   . LYS A 1 164 ? 43.906 -4.524  26.512 1.00 30.84 ? 160 LYS A C   1 
ATOM   1320 O O   . LYS A 1 164 ? 43.433 -5.443  27.220 1.00 32.92 ? 160 LYS A O   1 
ATOM   1321 C CB  . LYS A 1 164 ? 46.324 -3.924  26.951 1.00 35.55 ? 160 LYS A CB  1 
ATOM   1322 C CG  . LYS A 1 164 ? 47.302 -2.773  27.161 1.00 44.30 ? 160 LYS A CG  1 
ATOM   1323 C CD  . LYS A 1 164 ? 48.686 -3.044  26.601 1.00 58.28 ? 160 LYS A CD  1 
ATOM   1324 C CE  . LYS A 1 164 ? 49.548 -1.796  26.517 1.00 71.27 ? 160 LYS A CE  1 
ATOM   1325 N NZ  . LYS A 1 164 ? 49.424 -1.086  25.215 1.00 76.47 ? 160 LYS A NZ  1 
ATOM   1326 N N   . ALA A 1 165 ? 43.662 -4.406  25.212 1.00 31.64 ? 161 ALA A N   1 
ATOM   1327 C CA  . ALA A 1 165 ? 42.935 -5.445  24.473 1.00 30.63 ? 161 ALA A CA  1 
ATOM   1328 C C   . ALA A 1 165 ? 43.592 -5.616  23.119 1.00 31.50 ? 161 ALA A C   1 
ATOM   1329 O O   . ALA A 1 165 ? 44.308 -4.681  22.648 1.00 31.17 ? 161 ALA A O   1 
ATOM   1330 C CB  . ALA A 1 165 ? 41.470 -5.104  24.328 1.00 31.22 ? 161 ALA A CB  1 
ATOM   1331 N N   . TYR A 1 166 ? 43.382 -6.796  22.549 1.00 31.92 ? 162 TYR A N   1 
ATOM   1332 C CA  . TYR A 1 166 ? 43.907 -7.092  21.200 1.00 31.27 ? 162 TYR A CA  1 
ATOM   1333 C C   . TYR A 1 166 ? 42.967 -8.073  20.531 1.00 31.22 ? 162 TYR A C   1 
ATOM   1334 O O   . TYR A 1 166 ? 42.373 -8.956  21.185 1.00 32.43 ? 162 TYR A O   1 
ATOM   1335 C CB  . TYR A 1 166 ? 45.340 -7.612  21.265 1.00 35.93 ? 162 TYR A CB  1 
ATOM   1336 C CG  . TYR A 1 166 ? 45.487 -8.896  22.030 1.00 36.92 ? 162 TYR A CG  1 
ATOM   1337 C CD1 . TYR A 1 166 ? 45.646 -8.899  23.407 1.00 41.97 ? 162 TYR A CD1 1 
ATOM   1338 C CD2 . TYR A 1 166 ? 45.472 -10.115 21.371 1.00 41.42 ? 162 TYR A CD2 1 
ATOM   1339 C CE1 . TYR A 1 166 ? 45.786 -10.083 24.114 1.00 41.30 ? 162 TYR A CE1 1 
ATOM   1340 C CE2 . TYR A 1 166 ? 45.598 -11.305 22.064 1.00 41.20 ? 162 TYR A CE2 1 
ATOM   1341 C CZ  . TYR A 1 166 ? 45.777 -11.287 23.436 1.00 42.37 ? 162 TYR A CZ  1 
ATOM   1342 O OH  . TYR A 1 166 ? 45.893 -12.453 24.124 1.00 47.66 ? 162 TYR A OH  1 
ATOM   1343 N N   . PHE A 1 167 ? 42.832 -7.897  19.226 1.00 32.62 ? 163 PHE A N   1 
ATOM   1344 C CA  . PHE A 1 167 ? 42.009 -8.799  18.394 1.00 32.04 ? 163 PHE A CA  1 
ATOM   1345 C C   . PHE A 1 167 ? 42.181 -8.385  16.936 1.00 32.30 ? 163 PHE A C   1 
ATOM   1346 O O   . PHE A 1 167 ? 42.603 -7.266  16.670 1.00 30.30 ? 163 PHE A O   1 
ATOM   1347 C CB  . PHE A 1 167 ? 40.543 -8.757  18.804 1.00 31.79 ? 163 PHE A CB  1 
ATOM   1348 C CG  . PHE A 1 167 ? 39.929 -7.374  18.863 1.00 33.21 ? 163 PHE A CG  1 
ATOM   1349 C CD1 . PHE A 1 167 ? 40.045 -6.593  19.993 1.00 31.80 ? 163 PHE A CD1 1 
ATOM   1350 C CD2 . PHE A 1 167 ? 39.216 -6.873  17.786 1.00 35.12 ? 163 PHE A CD2 1 
ATOM   1351 C CE1 . PHE A 1 167 ? 39.487 -5.324  20.048 1.00 32.94 ? 163 PHE A CE1 1 
ATOM   1352 C CE2 . PHE A 1 167 ? 38.661 -5.603  17.835 1.00 36.28 ? 163 PHE A CE2 1 
ATOM   1353 C CZ  . PHE A 1 167 ? 38.788 -4.843  18.973 1.00 33.20 ? 163 PHE A CZ  1 
ATOM   1354 N N   . THR A 1 168 ? 41.833 -9.302  16.026 1.00 32.48 ? 164 THR A N   1 
ATOM   1355 C CA  . THR A 1 168 ? 41.850 -9.048  14.576 1.00 33.00 ? 164 THR A CA  1 
ATOM   1356 C C   . THR A 1 168 ? 40.439 -9.235  14.030 1.00 31.93 ? 164 THR A C   1 
ATOM   1357 O O   . THR A 1 168 ? 39.827 -10.284 14.258 1.00 36.44 ? 164 THR A O   1 
ATOM   1358 C CB  . THR A 1 168 ? 42.917 -9.901  13.879 1.00 37.99 ? 164 THR A CB  1 
ATOM   1359 O OG1 . THR A 1 168 ? 44.204 -9.550  14.402 1.00 38.64 ? 164 THR A OG1 1 
ATOM   1360 C CG2 . THR A 1 168 ? 42.882 -9.698  12.377 1.00 38.45 ? 164 THR A CG2 1 
ATOM   1361 N N   . ILE A 1 169 ? 39.949 -8.227  13.317 1.00 32.90 ? 165 ILE A N   1 
ATOM   1362 C CA  . ILE A 1 169 ? 38.679 -8.326  12.551 1.00 32.83 ? 165 ILE A CA  1 
ATOM   1363 C C   . ILE A 1 169 ? 39.011 -8.710  11.115 1.00 34.20 ? 165 ILE A C   1 
ATOM   1364 O O   . ILE A 1 169 ? 39.934 -8.112  10.556 1.00 37.22 ? 165 ILE A O   1 
ATOM   1365 C CB  . ILE A 1 169 ? 37.880 -7.019  12.586 1.00 34.42 ? 165 ILE A CB  1 
ATOM   1366 C CG1 . ILE A 1 169 ? 37.606 -6.573  14.028 1.00 32.17 ? 165 ILE A CG1 1 
ATOM   1367 C CG2 . ILE A 1 169 ? 36.598 -7.127  11.739 1.00 35.16 ? 165 ILE A CG2 1 
ATOM   1368 C CD1 . ILE A 1 169 ? 36.824 -7.548  14.862 1.00 32.09 ? 165 ILE A CD1 1 
ATOM   1369 N N   . ARG A 1 170 ? 38.258 -9.659  10.568 1.00 37.38 ? 166 ARG A N   1 
ATOM   1370 C CA  . ARG A 1 170 ? 38.433 -10.110 9.162  1.00 38.13 ? 166 ARG A CA  1 
ATOM   1371 C C   . ARG A 1 170 ? 37.270 -9.525  8.366  1.00 36.44 ? 166 ARG A C   1 
ATOM   1372 O O   . ARG A 1 170 ? 36.182 -10.080 8.445  1.00 40.15 ? 166 ARG A O   1 
ATOM   1373 C CB  . ARG A 1 170 ? 38.460 -11.643 9.114  1.00 43.78 ? 166 ARG A CB  1 
ATOM   1374 C CG  . ARG A 1 170 ? 39.533 -12.280 9.984  1.00 46.61 ? 166 ARG A CG  1 
ATOM   1375 C CD  . ARG A 1 170 ? 39.310 -13.765 10.213 1.00 50.46 ? 166 ARG A CD  1 
ATOM   1376 N NE  . ARG A 1 170 ? 39.217 -14.512 8.960  1.00 58.67 ? 166 ARG A NE  1 
ATOM   1377 C CZ  . ARG A 1 170 ? 40.234 -14.806 8.155  1.00 60.58 ? 166 ARG A CZ  1 
ATOM   1378 N NH1 . ARG A 1 170 ? 41.464 -14.405 8.437  1.00 62.99 ? 166 ARG A NH1 1 
ATOM   1379 N NH2 . ARG A 1 170 ? 40.012 -15.504 7.055  1.00 68.35 ? 166 ARG A NH2 1 
ATOM   1380 N N   . HIS A 1 171 ? 37.492 -8.439  7.652  1.00 36.80 ? 167 HIS A N   1 
ATOM   1381 C CA  . HIS A 1 171 ? 36.455 -7.788  6.814  1.00 36.53 ? 167 HIS A CA  1 
ATOM   1382 C C   . HIS A 1 171 ? 36.392 -8.520  5.469  1.00 41.76 ? 167 HIS A C   1 
ATOM   1383 O O   . HIS A 1 171 ? 37.428 -8.613  4.790  1.00 40.53 ? 167 HIS A O   1 
ATOM   1384 C CB  . HIS A 1 171 ? 36.794 -6.324  6.594  1.00 35.97 ? 167 HIS A CB  1 
ATOM   1385 C CG  . HIS A 1 171 ? 36.772 -5.500  7.834  1.00 37.25 ? 167 HIS A CG  1 
ATOM   1386 N ND1 . HIS A 1 171 ? 35.610 -5.246  8.513  1.00 38.21 ? 167 HIS A ND1 1 
ATOM   1387 C CD2 . HIS A 1 171 ? 37.737 -4.770  8.443  1.00 36.64 ? 167 HIS A CD2 1 
ATOM   1388 C CE1 . HIS A 1 171 ? 35.873 -4.447  9.529  1.00 34.57 ? 167 HIS A CE1 1 
ATOM   1389 N NE2 . HIS A 1 171 ? 37.164 -4.150  9.531  1.00 35.23 ? 167 HIS A NE2 1 
ATOM   1390 N N   . ASP A 1 172 ? 35.209 -8.964  5.075  1.00 40.79 ? 168 ASP A N   1 
ATOM   1391 C CA  . ASP A 1 172 ? 35.009 -9.586  3.743  1.00 41.05 ? 168 ASP A CA  1 
ATOM   1392 C C   . ASP A 1 172 ? 35.099 -8.499  2.667  1.00 41.58 ? 168 ASP A C   1 
ATOM   1393 O O   . ASP A 1 172 ? 34.498 -7.376  2.791  1.00 37.96 ? 168 ASP A O   1 
ATOM   1394 C CB  . ASP A 1 172 ? 33.713 -10.388 3.671  1.00 43.14 ? 168 ASP A CB  1 
ATOM   1395 C CG  . ASP A 1 172 ? 33.706 -11.657 4.499  1.00 48.37 ? 168 ASP A CG  1 
ATOM   1396 O OD1 . ASP A 1 172 ? 34.763 -12.287 4.647  1.00 45.40 ? 168 ASP A OD1 1 
ATOM   1397 O OD2 . ASP A 1 172 ? 32.621 -12.017 4.972  1.00 54.72 ? 168 ASP A OD2 1 
ATOM   1398 N N   . VAL A 1 173 ? 35.867 -8.814  1.638  1.00 39.01 ? 169 VAL A N   1 
ATOM   1399 C CA  . VAL A 1 173 ? 36.055 -7.957  0.448  1.00 38.11 ? 169 VAL A CA  1 
ATOM   1400 C C   . VAL A 1 173 ? 35.137 -8.504  -0.656 1.00 37.58 ? 169 VAL A C   1 
ATOM   1401 O O   . VAL A 1 173 ? 34.899 -9.709  -0.676 1.00 41.54 ? 169 VAL A O   1 
ATOM   1402 C CB  . VAL A 1 173 ? 37.525 -7.881  0.030  1.00 40.67 ? 169 VAL A CB  1 
ATOM   1403 C CG1 . VAL A 1 173 ? 37.710 -6.829  -1.039 1.00 39.16 ? 169 VAL A CG1 1 
ATOM   1404 C CG2 . VAL A 1 173 ? 38.427 -7.584  1.227  1.00 41.47 ? 169 VAL A CG2 1 
ATOM   1405 N N   . GLU A 1 174 ? 34.637 -7.611  -1.498 1.00 41.32 ? 170 GLU A N   1 
ATOM   1406 C CA  A GLU A 1 174 ? 33.634 -7.927  -2.557 0.50 45.29 ? 170 GLU A CA  1 
ATOM   1407 C CA  B GLU A 1 174 ? 33.627 -7.937  -2.547 0.50 47.20 ? 170 GLU A CA  1 
ATOM   1408 C C   . GLU A 1 174 ? 34.195 -8.950  -3.557 1.00 46.78 ? 170 GLU A C   1 
ATOM   1409 O O   . GLU A 1 174 ? 33.388 -9.491  -4.335 1.00 52.21 ? 170 GLU A O   1 
ATOM   1410 C CB  A GLU A 1 174 ? 33.191 -6.654  -3.284 0.50 43.04 ? 170 GLU A CB  1 
ATOM   1411 C CB  B GLU A 1 174 ? 33.139 -6.654  -3.227 0.50 47.52 ? 170 GLU A CB  1 
ATOM   1412 C CG  A GLU A 1 174 ? 34.292 -5.971  -4.078 0.50 43.16 ? 170 GLU A CG  1 
ATOM   1413 C CG  B GLU A 1 174 ? 32.188 -5.842  -2.353 0.50 50.47 ? 170 GLU A CG  1 
ATOM   1414 C CD  A GLU A 1 174 ? 33.879 -4.686  -4.776 0.50 41.76 ? 170 GLU A CD  1 
ATOM   1415 C CD  B GLU A 1 174 ? 31.683 -4.543  -2.959 0.50 50.72 ? 170 GLU A CD  1 
ATOM   1416 O OE1 A GLU A 1 174 ? 32.836 -4.127  -4.427 0.50 43.38 ? 170 GLU A OE1 1 
ATOM   1417 O OE1 B GLU A 1 174 ? 31.978 -4.291  -4.143 0.50 55.51 ? 170 GLU A OE1 1 
ATOM   1418 O OE2 A GLU A 1 174 ? 34.615 -4.247  -5.658 0.50 43.68 ? 170 GLU A OE2 1 
ATOM   1419 O OE2 B GLU A 1 174 ? 31.024 -3.776  -2.236 0.50 48.66 ? 170 GLU A OE2 1 
ATOM   1420 N N   . ASP A 1 175 ? 35.513 -9.205  -3.553 1.00 45.54 ? 171 ASP A N   1 
ATOM   1421 C CA  . ASP A 1 175 ? 36.149 -10.197 -4.474 1.00 42.48 ? 171 ASP A CA  1 
ATOM   1422 C C   . ASP A 1 175 ? 36.387 -11.535 -3.756 1.00 45.02 ? 171 ASP A C   1 
ATOM   1423 O O   . ASP A 1 175 ? 37.069 -12.421 -4.345 1.00 44.46 ? 171 ASP A O   1 
ATOM   1424 C CB  . ASP A 1 175 ? 37.413 -9.608  -5.101 1.00 44.77 ? 171 ASP A CB  1 
ATOM   1425 C CG  . ASP A 1 175 ? 38.533 -9.351  -4.109 1.00 43.17 ? 171 ASP A CG  1 
ATOM   1426 O OD1 . ASP A 1 175 ? 38.353 -9.661  -2.931 1.00 44.00 ? 171 ASP A OD1 1 
ATOM   1427 O OD2 . ASP A 1 175 ? 39.582 -8.875  -4.535 1.00 51.12 ? 171 ASP A OD2 1 
ATOM   1428 N N   . GLY A 1 176 ? 35.866 -11.704 -2.535 1.00 41.00 ? 172 GLY A N   1 
ATOM   1429 C CA  . GLY A 1 176 ? 36.045 -12.919 -1.724 1.00 42.82 ? 172 GLY A CA  1 
ATOM   1430 C C   . GLY A 1 176 ? 37.339 -12.925 -0.914 1.00 37.60 ? 172 GLY A C   1 
ATOM   1431 O O   . GLY A 1 176 ? 37.524 -13.882 -0.170 1.00 41.09 ? 172 GLY A O   1 
ATOM   1432 N N   . SER A 1 177 ? 38.223 -11.940 -1.087 1.00 40.82 ? 173 SER A N   1 
ATOM   1433 C CA  . SER A 1 177 ? 39.425 -11.768 -0.220 1.00 42.79 ? 173 SER A CA  1 
ATOM   1434 C C   . SER A 1 177 ? 38.964 -11.293 1.169  1.00 40.46 ? 173 SER A C   1 
ATOM   1435 O O   . SER A 1 177 ? 37.762 -11.078 1.366  1.00 37.47 ? 173 SER A O   1 
ATOM   1436 C CB  . SER A 1 177 ? 40.508 -10.871 -0.798 1.00 39.62 ? 173 SER A CB  1 
ATOM   1437 O OG  . SER A 1 177 ? 40.079 -9.538  -1.079 1.00 42.36 ? 173 SER A OG  1 
ATOM   1438 N N   . VAL A 1 178 ? 39.908 -11.176 2.092  1.00 39.96 ? 174 VAL A N   1 
ATOM   1439 C CA  . VAL A 1 178 ? 39.657 -10.735 3.498  1.00 43.44 ? 174 VAL A CA  1 
ATOM   1440 C C   . VAL A 1 178 ? 40.603 -9.571  3.746  1.00 44.03 ? 174 VAL A C   1 
ATOM   1441 O O   . VAL A 1 178 ? 41.764 -9.677  3.336  1.00 43.34 ? 174 VAL A O   1 
ATOM   1442 C CB  . VAL A 1 178 ? 39.869 -11.891 4.494  1.00 48.46 ? 174 VAL A CB  1 
ATOM   1443 C CG1 . VAL A 1 178 ? 39.861 -11.406 5.928  1.00 55.24 ? 174 VAL A CG1 1 
ATOM   1444 C CG2 . VAL A 1 178 ? 38.847 -13.000 4.319  1.00 52.16 ? 174 VAL A CG2 1 
ATOM   1445 N N   . LEU A 1 179 ? 40.123 -8.484  4.355  1.00 40.99 ? 175 LEU A N   1 
ATOM   1446 C CA  . LEU A 1 179 ? 40.997 -7.380  4.813  1.00 36.28 ? 175 LEU A CA  1 
ATOM   1447 C C   . LEU A 1 179 ? 41.144 -7.497  6.338  1.00 39.09 ? 175 LEU A C   1 
ATOM   1448 O O   . LEU A 1 179 ? 40.113 -7.425  7.044  1.00 36.63 ? 175 LEU A O   1 
ATOM   1449 C CB  . LEU A 1 179 ? 40.378 -6.040  4.408  1.00 41.23 ? 175 LEU A CB  1 
ATOM   1450 C CG  . LEU A 1 179 ? 41.046 -4.775  4.966  1.00 40.14 ? 175 LEU A CG  1 
ATOM   1451 C CD1 . LEU A 1 179 ? 42.484 -4.603  4.471  1.00 44.77 ? 175 LEU A CD1 1 
ATOM   1452 C CD2 . LEU A 1 179 ? 40.217 -3.559  4.624  1.00 45.96 ? 175 LEU A CD2 1 
ATOM   1453 N N   . LEU A 1 180 ? 42.351 -7.805  6.815  1.00 38.86 ? 176 LEU A N   1 
ATOM   1454 C CA  . LEU A 1 180 ? 42.629 -7.974  8.261  1.00 38.55 ? 176 LEU A CA  1 
ATOM   1455 C C   . LEU A 1 180 ? 42.810 -6.597  8.881  1.00 36.78 ? 176 LEU A C   1 
ATOM   1456 O O   . LEU A 1 180 ? 43.580 -5.777  8.341  1.00 36.97 ? 176 LEU A O   1 
ATOM   1457 C CB  . LEU A 1 180 ? 43.873 -8.841  8.484  1.00 38.63 ? 176 LEU A CB  1 
ATOM   1458 C CG  . LEU A 1 180 ? 43.799 -10.249 7.912  1.00 44.49 ? 176 LEU A CG  1 
ATOM   1459 C CD1 . LEU A 1 180 ? 45.078 -10.995 8.263  1.00 45.88 ? 176 LEU A CD1 1 
ATOM   1460 C CD2 . LEU A 1 180 ? 42.577 -11.019 8.392  1.00 45.11 ? 176 LEU A CD2 1 
ATOM   1461 N N   . ALA A 1 181 ? 42.101 -6.371  9.997  1.00 34.76 ? 177 ALA A N   1 
ATOM   1462 C CA  . ALA A 1 181 ? 42.168 -5.122  10.773 1.00 34.54 ? 177 ALA A CA  1 
ATOM   1463 C C   . ALA A 1 181 ? 42.689 -5.498  12.161 1.00 31.82 ? 177 ALA A C   1 
ATOM   1464 O O   . ALA A 1 181 ? 41.940 -6.032  12.960 1.00 31.34 ? 177 ALA A O   1 
ATOM   1465 C CB  . ALA A 1 181 ? 40.817 -4.445  10.802 1.00 34.63 ? 177 ALA A CB  1 
ATOM   1466 N N   . ASP A 1 182 ? 43.988 -5.304  12.375 1.00 33.91 ? 178 ASP A N   1 
ATOM   1467 C CA  A ASP A 1 182 ? 44.684 -5.713  13.614 0.50 31.62 ? 178 ASP A CA  1 
ATOM   1468 C CA  B ASP A 1 182 ? 44.678 -5.717  13.626 0.50 33.38 ? 178 ASP A CA  1 
ATOM   1469 C C   . ASP A 1 182 ? 44.514 -4.589  14.640 1.00 30.75 ? 178 ASP A C   1 
ATOM   1470 O O   . ASP A 1 182 ? 45.027 -3.513  14.406 1.00 31.16 ? 178 ASP A O   1 
ATOM   1471 C CB  A ASP A 1 182 ? 46.141 -6.006  13.251 0.50 31.73 ? 178 ASP A CB  1 
ATOM   1472 C CB  B ASP A 1 182 ? 46.174 -5.988  13.415 0.50 36.45 ? 178 ASP A CB  1 
ATOM   1473 C CG  A ASP A 1 182 ? 46.929 -6.720  14.321 0.50 32.59 ? 178 ASP A CG  1 
ATOM   1474 C CG  B ASP A 1 182 ? 46.512 -7.330  12.791 0.50 40.29 ? 178 ASP A CG  1 
ATOM   1475 O OD1 A ASP A 1 182 ? 46.318 -7.172  15.301 0.50 33.27 ? 178 ASP A OD1 1 
ATOM   1476 O OD1 B ASP A 1 182 ? 45.642 -8.218  12.773 0.50 46.42 ? 178 ASP A OD1 1 
ATOM   1477 O OD2 A ASP A 1 182 ? 48.157 -6.820  14.144 0.50 31.49 ? 178 ASP A OD2 1 
ATOM   1478 O OD2 B ASP A 1 182 ? 47.667 -7.471  12.302 0.50 45.31 ? 178 ASP A OD2 1 
ATOM   1479 N N   . HIS A 1 183 ? 43.788 -4.853  15.724 1.00 31.75 ? 179 HIS A N   1 
ATOM   1480 C CA  . HIS A 1 183 ? 43.412 -3.837  16.719 1.00 29.43 ? 179 HIS A CA  1 
ATOM   1481 C C   . HIS A 1 183 ? 44.337 -3.955  17.927 1.00 29.53 ? 179 HIS A C   1 
ATOM   1482 O O   . HIS A 1 183 ? 44.468 -5.067  18.486 1.00 31.45 ? 179 HIS A O   1 
ATOM   1483 C CB  . HIS A 1 183 ? 41.969 -4.042  17.188 1.00 29.48 ? 179 HIS A CB  1 
ATOM   1484 C CG  . HIS A 1 183 ? 40.906 -3.656  16.237 1.00 30.89 ? 179 HIS A CG  1 
ATOM   1485 N ND1 . HIS A 1 183 ? 40.763 -4.239  14.992 1.00 32.41 ? 179 HIS A ND1 1 
ATOM   1486 C CD2 . HIS A 1 183 ? 39.873 -2.781  16.375 1.00 33.11 ? 179 HIS A CD2 1 
ATOM   1487 C CE1 . HIS A 1 183 ? 39.670 -3.732  14.401 1.00 33.08 ? 179 HIS A CE1 1 
ATOM   1488 N NE2 . HIS A 1 183 ? 39.103 -2.832  15.218 1.00 30.97 ? 179 HIS A NE2 1 
ATOM   1489 N N   . TYR A 1 184 ? 44.905 -2.828  18.320 1.00 30.68 ? 180 TYR A N   1 
ATOM   1490 C CA  . TYR A 1 184 ? 45.628 -2.657  19.608 1.00 30.22 ? 180 TYR A CA  1 
ATOM   1491 C C   . TYR A 1 184 ? 44.872 -1.611  20.406 1.00 28.62 ? 180 TYR A C   1 
ATOM   1492 O O   . TYR A 1 184 ? 44.610 -0.534  19.875 1.00 30.32 ? 180 TYR A O   1 
ATOM   1493 C CB  . TYR A 1 184 ? 47.091 -2.265  19.345 1.00 30.13 ? 180 TYR A CB  1 
ATOM   1494 C CG  . TYR A 1 184 ? 47.808 -3.321  18.550 1.00 32.11 ? 180 TYR A CG  1 
ATOM   1495 C CD1 . TYR A 1 184 ? 47.684 -3.400  17.168 1.00 36.08 ? 180 TYR A CD1 1 
ATOM   1496 C CD2 . TYR A 1 184 ? 48.576 -4.283  19.190 1.00 33.62 ? 180 TYR A CD2 1 
ATOM   1497 C CE1 . TYR A 1 184 ? 48.295 -4.414  16.443 1.00 33.84 ? 180 TYR A CE1 1 
ATOM   1498 C CE2 . TYR A 1 184 ? 49.210 -5.288  18.476 1.00 33.72 ? 180 TYR A CE2 1 
ATOM   1499 C CZ  . TYR A 1 184 ? 49.052 -5.368  17.100 1.00 36.01 ? 180 TYR A CZ  1 
ATOM   1500 O OH  . TYR A 1 184 ? 49.640 -6.378  16.384 1.00 37.07 ? 180 TYR A OH  1 
ATOM   1501 N N   . GLN A 1 185 ? 44.575 -1.925  21.665 1.00 29.12 ? 181 GLN A N   1 
ATOM   1502 C CA  . GLN A 1 185 ? 43.666 -1.094  22.477 1.00 28.78 ? 181 GLN A CA  1 
ATOM   1503 C C   . GLN A 1 185 ? 44.249 -0.881  23.861 1.00 27.95 ? 181 GLN A C   1 
ATOM   1504 O O   . GLN A 1 185 ? 44.832 -1.823  24.450 1.00 30.17 ? 181 GLN A O   1 
ATOM   1505 C CB  . GLN A 1 185 ? 42.321 -1.795  22.578 1.00 30.95 ? 181 GLN A CB  1 
ATOM   1506 C CG  . GLN A 1 185 ? 41.315 -1.078  23.460 1.00 30.25 ? 181 GLN A CG  1 
ATOM   1507 C CD  . GLN A 1 185 ? 39.999 -1.816  23.505 1.00 30.43 ? 181 GLN A CD  1 
ATOM   1508 O OE1 . GLN A 1 185 ? 39.641 -2.608  22.620 1.00 29.18 ? 181 GLN A OE1 1 
ATOM   1509 N NE2 . GLN A 1 185 ? 39.284 -1.596  24.599 1.00 30.74 ? 181 GLN A NE2 1 
ATOM   1510 N N   . GLN A 1 186 ? 44.112 0.335   24.367 1.00 28.51 ? 182 GLN A N   1 
ATOM   1511 C CA  . GLN A 1 186 ? 44.496 0.664   25.747 1.00 31.58 ? 182 GLN A CA  1 
ATOM   1512 C C   . GLN A 1 186 ? 43.356 1.457   26.376 1.00 31.54 ? 182 GLN A C   1 
ATOM   1513 O O   . GLN A 1 186 ? 42.909 2.426   25.745 1.00 33.33 ? 182 GLN A O   1 
ATOM   1514 C CB  . GLN A 1 186 ? 45.808 1.467   25.745 1.00 37.38 ? 182 GLN A CB  1 
ATOM   1515 C CG  . GLN A 1 186 ? 45.997 2.303   27.018 1.00 51.31 ? 182 GLN A CG  1 
ATOM   1516 C CD  . GLN A 1 186 ? 46.669 1.544   28.139 1.00 63.85 ? 182 GLN A CD  1 
ATOM   1517 O OE1 . GLN A 1 186 ? 46.166 1.418   29.286 1.00 49.45 ? 182 GLN A OE1 1 
ATOM   1518 N NE2 . GLN A 1 186 ? 47.848 1.032   27.806 1.00 73.25 ? 182 GLN A NE2 1 
ATOM   1519 N N   . ASN A 1 187 ? 42.949 1.100   27.594 1.00 30.35 ? 183 ASN A N   1 
ATOM   1520 C CA  . ASN A 1 187 ? 41.913 1.880   28.326 1.00 27.95 ? 183 ASN A CA  1 
ATOM   1521 C C   . ASN A 1 187 ? 42.518 2.360   29.650 1.00 28.71 ? 183 ASN A C   1 
ATOM   1522 O O   . ASN A 1 187 ? 43.161 1.583   30.329 1.00 32.23 ? 183 ASN A O   1 
ATOM   1523 C CB  . ASN A 1 187 ? 40.631 1.089   28.601 1.00 29.38 ? 183 ASN A CB  1 
ATOM   1524 C CG  . ASN A 1 187 ? 39.892 0.782   27.318 1.00 33.56 ? 183 ASN A CG  1 
ATOM   1525 O OD1 . ASN A 1 187 ? 40.515 0.417   26.330 1.00 33.71 ? 183 ASN A OD1 1 
ATOM   1526 N ND2 . ASN A 1 187 ? 38.586 0.961   27.308 1.00 30.20 ? 183 ASN A ND2 1 
ATOM   1527 N N   . THR A 1 188 ? 42.236 3.610   29.988 1.00 29.49 ? 184 THR A N   1 
ATOM   1528 C CA  A THR A 1 188 ? 42.662 4.172   31.293 0.50 29.45 ? 184 THR A CA  1 
ATOM   1529 C CA  B THR A 1 188 ? 42.690 4.244   31.253 0.50 31.04 ? 184 THR A CA  1 
ATOM   1530 C C   . THR A 1 188 ? 41.495 4.904   31.934 1.00 33.47 ? 184 THR A C   1 
ATOM   1531 O O   . THR A 1 188 ? 40.742 5.616   31.275 1.00 31.47 ? 184 THR A O   1 
ATOM   1532 C CB  A THR A 1 188 ? 43.890 5.067   31.117 0.50 32.49 ? 184 THR A CB  1 
ATOM   1533 C CB  B THR A 1 188 ? 43.785 5.280   30.957 0.50 34.92 ? 184 THR A CB  1 
ATOM   1534 O OG1 A THR A 1 188 ? 43.523 6.100   30.208 0.50 29.60 ? 184 THR A OG1 1 
ATOM   1535 O OG1 B THR A 1 188 ? 44.775 4.725   30.083 0.50 38.46 ? 184 THR A OG1 1 
ATOM   1536 C CG2 A THR A 1 188 ? 45.094 4.308   30.594 0.50 31.18 ? 184 THR A CG2 1 
ATOM   1537 C CG2 B THR A 1 188 ? 44.493 5.747   32.206 0.50 34.95 ? 184 THR A CG2 1 
ATOM   1538 N N   . PRO A 1 189 ? 41.338 4.784   33.257 1.00 29.73 ? 185 PRO A N   1 
ATOM   1539 C CA  . PRO A 1 189 ? 40.252 5.471   33.938 1.00 28.95 ? 185 PRO A CA  1 
ATOM   1540 C C   . PRO A 1 189 ? 40.441 6.984   33.879 1.00 29.87 ? 185 PRO A C   1 
ATOM   1541 O O   . PRO A 1 189 ? 41.585 7.481   33.955 1.00 32.68 ? 185 PRO A O   1 
ATOM   1542 C CB  . PRO A 1 189 ? 40.320 4.955   35.383 1.00 30.78 ? 185 PRO A CB  1 
ATOM   1543 C CG  . PRO A 1 189 ? 41.722 4.481   35.555 1.00 33.29 ? 185 PRO A CG  1 
ATOM   1544 C CD  . PRO A 1 189 ? 42.218 4.061   34.187 1.00 30.24 ? 185 PRO A CD  1 
ATOM   1545 N N   . ILE A 1 190 ? 39.326 7.708   33.813 1.00 30.66 ? 186 ILE A N   1 
ATOM   1546 C CA  . ILE A 1 190 ? 39.356 9.197   33.891 1.00 31.70 ? 186 ILE A CA  1 
ATOM   1547 C C   . ILE A 1 190 ? 39.431 9.659   35.353 1.00 37.45 ? 186 ILE A C   1 
ATOM   1548 O O   . ILE A 1 190 ? 40.126 10.670  35.608 1.00 40.62 ? 186 ILE A O   1 
ATOM   1549 C CB  . ILE A 1 190 ? 38.167 9.809   33.142 1.00 32.87 ? 186 ILE A CB  1 
ATOM   1550 C CG1 . ILE A 1 190 ? 38.276 9.522   31.642 1.00 31.41 ? 186 ILE A CG1 1 
ATOM   1551 C CG2 . ILE A 1 190 ? 38.109 11.306  33.384 1.00 33.70 ? 186 ILE A CG2 1 
ATOM   1552 C CD1 . ILE A 1 190 ? 37.072 9.818   30.828 1.00 30.39 ? 186 ILE A CD1 1 
ATOM   1553 N N   . GLY A 1 191 ? 38.735 8.987   36.255 1.00 36.13 ? 187 GLY A N   1 
ATOM   1554 C CA  . GLY A 1 191 ? 38.656 9.358   37.681 1.00 40.48 ? 187 GLY A CA  1 
ATOM   1555 C C   . GLY A 1 191 ? 39.820 8.793   38.473 1.00 41.09 ? 187 GLY A C   1 
ATOM   1556 O O   . GLY A 1 191 ? 40.645 8.034   37.904 1.00 37.15 ? 187 GLY A O   1 
ATOM   1557 N N   . ASP A 1 192 ? 39.879 9.127   39.766 1.00 48.12 ? 188 ASP A N   1 
ATOM   1558 C CA  . ASP A 1 192 ? 40.987 8.707   40.666 1.00 53.67 ? 188 ASP A CA  1 
ATOM   1559 C C   . ASP A 1 192 ? 40.540 7.565   41.569 1.00 52.27 ? 188 ASP A C   1 
ATOM   1560 O O   . ASP A 1 192 ? 41.410 7.047   42.282 1.00 59.81 ? 188 ASP A O   1 
ATOM   1561 C CB  . ASP A 1 192 ? 41.477 9.859   41.546 1.00 62.67 ? 188 ASP A CB  1 
ATOM   1562 C CG  . ASP A 1 192 ? 41.959 11.030  40.720 1.00 73.25 ? 188 ASP A CG  1 
ATOM   1563 O OD1 . ASP A 1 192 ? 42.770 10.797  39.787 1.00 75.26 ? 188 ASP A OD1 1 
ATOM   1564 O OD2 . ASP A 1 192 ? 41.490 12.155  40.990 1.00 87.08 ? 188 ASP A OD2 1 
ATOM   1565 N N   . GLY A 1 193 ? 39.256 7.206   41.524 1.00 51.15 ? 189 GLY A N   1 
ATOM   1566 C CA  . GLY A 1 193 ? 38.656 6.142   42.353 1.00 51.74 ? 189 GLY A CA  1 
ATOM   1567 C C   . GLY A 1 193 ? 39.186 4.768   41.951 1.00 51.83 ? 189 GLY A C   1 
ATOM   1568 O O   . GLY A 1 193 ? 39.642 4.594   40.824 1.00 48.56 ? 189 GLY A O   1 
ATOM   1569 N N   . PRO A 1 194 ? 39.133 3.759   42.851 1.00 47.92 ? 190 PRO A N   1 
ATOM   1570 C CA  . PRO A 1 194 ? 39.671 2.433   42.552 1.00 48.68 ? 190 PRO A CA  1 
ATOM   1571 C C   . PRO A 1 194 ? 38.918 1.783   41.380 1.00 40.86 ? 190 PRO A C   1 
ATOM   1572 O O   . PRO A 1 194 ? 37.731 1.967   41.244 1.00 41.39 ? 190 PRO A O   1 
ATOM   1573 C CB  . PRO A 1 194 ? 39.443 1.638   43.846 1.00 51.13 ? 190 PRO A CB  1 
ATOM   1574 C CG  . PRO A 1 194 ? 38.259 2.342   44.499 1.00 53.56 ? 190 PRO A CG  1 
ATOM   1575 C CD  . PRO A 1 194 ? 38.474 3.808   44.173 1.00 55.01 ? 190 PRO A CD  1 
ATOM   1576 N N   . VAL A 1 195 ? 39.646 1.044   40.553 1.00 37.83 ? 191 VAL A N   1 
ATOM   1577 C CA  . VAL A 1 195 ? 39.052 0.266   39.441 1.00 34.26 ? 191 VAL A CA  1 
ATOM   1578 C C   . VAL A 1 195 ? 39.450 -1.190  39.608 1.00 34.94 ? 191 VAL A C   1 
ATOM   1579 O O   . VAL A 1 195 ? 40.368 -1.517  40.395 1.00 36.06 ? 191 VAL A O   1 
ATOM   1580 C CB  . VAL A 1 195 ? 39.503 0.793   38.066 1.00 36.10 ? 191 VAL A CB  1 
ATOM   1581 C CG1 . VAL A 1 195 ? 38.963 2.181   37.834 1.00 38.64 ? 191 VAL A CG1 1 
ATOM   1582 C CG2 . VAL A 1 195 ? 41.009 0.727   37.887 1.00 40.37 ? 191 VAL A CG2 1 
ATOM   1583 N N   . LEU A 1 196 ? 38.807 -2.041  38.842 1.00 29.94 ? 192 LEU A N   1 
ATOM   1584 C CA  . LEU A 1 196 ? 39.071 -3.493  38.892 1.00 30.68 ? 192 LEU A CA  1 
ATOM   1585 C C   . LEU A 1 196 ? 40.085 -3.836  37.808 1.00 36.09 ? 192 LEU A C   1 
ATOM   1586 O O   . LEU A 1 196 ? 39.821 -3.540  36.629 1.00 38.55 ? 192 LEU A O   1 
ATOM   1587 C CB  . LEU A 1 196 ? 37.782 -4.267  38.659 1.00 32.35 ? 192 LEU A CB  1 
ATOM   1588 C CG  . LEU A 1 196 ? 36.718 -4.136  39.743 1.00 33.50 ? 192 LEU A CG  1 
ATOM   1589 C CD1 . LEU A 1 196 ? 35.449 -4.847  39.300 1.00 32.05 ? 192 LEU A CD1 1 
ATOM   1590 C CD2 . LEU A 1 196 ? 37.198 -4.619  41.108 1.00 35.80 ? 192 LEU A CD2 1 
ATOM   1591 N N   . LEU A 1 197 ? 41.177 -4.496  38.181 1.00 32.48 ? 193 LEU A N   1 
ATOM   1592 C CA  . LEU A 1 197 ? 42.170 -4.912  37.176 1.00 34.58 ? 193 LEU A CA  1 
ATOM   1593 C C   . LEU A 1 197 ? 42.002 -6.404  36.957 1.00 34.73 ? 193 LEU A C   1 
ATOM   1594 O O   . LEU A 1 197 ? 42.098 -7.214  37.874 1.00 37.67 ? 193 LEU A O   1 
ATOM   1595 C CB  . LEU A 1 197 ? 43.577 -4.513  37.622 1.00 40.66 ? 193 LEU A CB  1 
ATOM   1596 C CG  . LEU A 1 197 ? 43.788 -3.002  37.768 1.00 41.71 ? 193 LEU A CG  1 
ATOM   1597 C CD1 . LEU A 1 197 ? 45.227 -2.745  38.217 1.00 48.35 ? 193 LEU A CD1 1 
ATOM   1598 C CD2 . LEU A 1 197 ? 43.440 -2.212  36.489 1.00 40.71 ? 193 LEU A CD2 1 
ATOM   1599 N N   . PRO A 1 198 ? 41.555 -6.792  35.753 1.00 29.99 ? 194 PRO A N   1 
ATOM   1600 C CA  . PRO A 1 198 ? 41.095 -8.148  35.537 1.00 30.17 ? 194 PRO A CA  1 
ATOM   1601 C C   . PRO A 1 198 ? 42.197 -9.186  35.302 1.00 30.98 ? 194 PRO A C   1 
ATOM   1602 O O   . PRO A 1 198 ? 43.261 -8.869  34.807 1.00 33.67 ? 194 PRO A O   1 
ATOM   1603 C CB  . PRO A 1 198 ? 40.260 -7.989  34.251 1.00 32.06 ? 194 PRO A CB  1 
ATOM   1604 C CG  . PRO A 1 198 ? 40.970 -6.927  33.496 1.00 32.15 ? 194 PRO A CG  1 
ATOM   1605 C CD  . PRO A 1 198 ? 41.383 -5.933  34.557 1.00 33.83 ? 194 PRO A CD  1 
ATOM   1606 N N   . ASP A 1 199 ? 41.862 -10.430 35.588 1.00 32.23 ? 195 ASP A N   1 
ATOM   1607 C CA  . ASP A 1 199 ? 42.603 -11.570 35.011 1.00 35.32 ? 195 ASP A CA  1 
ATOM   1608 C C   . ASP A 1 199 ? 42.296 -11.611 33.513 1.00 35.98 ? 195 ASP A C   1 
ATOM   1609 O O   . ASP A 1 199 ? 41.283 -11.021 33.062 1.00 35.36 ? 195 ASP A O   1 
ATOM   1610 C CB  . ASP A 1 199 ? 42.210 -12.872 35.693 1.00 36.65 ? 195 ASP A CB  1 
ATOM   1611 C CG  . ASP A 1 199 ? 42.666 -12.968 37.140 1.00 39.85 ? 195 ASP A CG  1 
ATOM   1612 O OD1 . ASP A 1 199 ? 43.518 -12.170 37.551 1.00 40.50 ? 195 ASP A OD1 1 
ATOM   1613 O OD2 . ASP A 1 199 ? 42.165 -13.857 37.815 1.00 42.61 ? 195 ASP A OD2 1 
ATOM   1614 N N   . ASN A 1 200 ? 43.129 -12.297 32.758 1.00 32.28 ? 196 ASN A N   1 
ATOM   1615 C CA  . ASN A 1 200 ? 42.927 -12.434 31.296 1.00 32.45 ? 196 ASN A CA  1 
ATOM   1616 C C   . ASN A 1 200 ? 41.554 -13.037 31.027 1.00 33.96 ? 196 ASN A C   1 
ATOM   1617 O O   . ASN A 1 200 ? 41.126 -14.028 31.707 1.00 35.13 ? 196 ASN A O   1 
ATOM   1618 C CB  . ASN A 1 200 ? 44.047 -13.278 30.679 1.00 34.30 ? 196 ASN A CB  1 
ATOM   1619 C CG  . ASN A 1 200 ? 45.370 -12.548 30.691 1.00 41.25 ? 196 ASN A CG  1 
ATOM   1620 O OD1 . ASN A 1 200 ? 45.495 -11.454 31.227 1.00 40.26 ? 196 ASN A OD1 1 
ATOM   1621 N ND2 . ASN A 1 200 ? 46.374 -13.135 30.060 1.00 44.17 ? 196 ASN A ND2 1 
ATOM   1622 N N   . HIS A 1 201 ? 40.843 -12.474 30.050 1.00 31.47 ? 197 HIS A N   1 
ATOM   1623 C CA  . HIS A 1 201 ? 39.561 -13.027 29.576 1.00 32.53 ? 197 HIS A CA  1 
ATOM   1624 C C   . HIS A 1 201 ? 39.276 -12.399 28.220 1.00 30.79 ? 197 HIS A C   1 
ATOM   1625 O O   . HIS A 1 201 ? 40.137 -11.621 27.714 1.00 31.86 ? 197 HIS A O   1 
ATOM   1626 C CB  . HIS A 1 201 ? 38.463 -12.758 30.603 1.00 33.05 ? 197 HIS A CB  1 
ATOM   1627 C CG  . HIS A 1 201 ? 38.127 -11.318 30.775 1.00 29.49 ? 197 HIS A CG  1 
ATOM   1628 N ND1 . HIS A 1 201 ? 38.946 -10.460 31.492 1.00 31.20 ? 197 HIS A ND1 1 
ATOM   1629 C CD2 . HIS A 1 201 ? 37.095 -10.579 30.297 1.00 31.20 ? 197 HIS A CD2 1 
ATOM   1630 C CE1 . HIS A 1 201 ? 38.401 -9.250  31.477 1.00 32.78 ? 197 HIS A CE1 1 
ATOM   1631 N NE2 . HIS A 1 201 ? 37.266 -9.302  30.739 1.00 29.35 ? 197 HIS A NE2 1 
ATOM   1632 N N   . TYR A 1 202 ? 38.135 -12.716 27.648 1.00 30.10 ? 198 TYR A N   1 
ATOM   1633 C CA  . TYR A 1 202 ? 37.700 -12.065 26.407 1.00 33.43 ? 198 TYR A CA  1 
ATOM   1634 C C   . TYR A 1 202 ? 36.221 -11.667 26.493 1.00 30.30 ? 198 TYR A C   1 
ATOM   1635 O O   . TYR A 1 202 ? 35.423 -12.164 27.320 1.00 31.34 ? 198 TYR A O   1 
ATOM   1636 C CB  . TYR A 1 202 ? 38.054 -12.945 25.212 1.00 33.10 ? 198 TYR A CB  1 
ATOM   1637 C CG  . TYR A 1 202 ? 37.329 -14.257 25.201 1.00 34.39 ? 198 TYR A CG  1 
ATOM   1638 C CD1 . TYR A 1 202 ? 36.080 -14.350 24.616 1.00 35.27 ? 198 TYR A CD1 1 
ATOM   1639 C CD2 . TYR A 1 202 ? 37.922 -15.396 25.721 1.00 35.93 ? 198 TYR A CD2 1 
ATOM   1640 C CE1 . TYR A 1 202 ? 35.417 -15.554 24.558 1.00 39.65 ? 198 TYR A CE1 1 
ATOM   1641 C CE2 . TYR A 1 202 ? 37.258 -16.608 25.696 1.00 37.09 ? 198 TYR A CE2 1 
ATOM   1642 C CZ  . TYR A 1 202 ? 36.007 -16.675 25.113 1.00 38.63 ? 198 TYR A CZ  1 
ATOM   1643 O OH  . TYR A 1 202 ? 35.281 -17.827 25.064 1.00 42.61 ? 198 TYR A OH  1 
ATOM   1644 N N   . LEU A 1 203 ? 35.880 -10.764 25.581 1.00 30.68 ? 199 LEU A N   1 
ATOM   1645 C CA  . LEU A 1 203 ? 34.497 -10.393 25.279 1.00 28.52 ? 199 LEU A CA  1 
ATOM   1646 C C   . LEU A 1 203 ? 34.141 -10.973 23.912 1.00 28.92 ? 199 LEU A C   1 
ATOM   1647 O O   . LEU A 1 203 ? 34.848 -10.718 22.914 1.00 32.68 ? 199 LEU A O   1 
ATOM   1648 C CB  . LEU A 1 203 ? 34.337 -8.874  25.287 1.00 28.00 ? 199 LEU A CB  1 
ATOM   1649 C CG  . LEU A 1 203 ? 34.758 -8.142  26.543 1.00 29.08 ? 199 LEU A CG  1 
ATOM   1650 C CD1 . LEU A 1 203 ? 34.450 -6.652  26.370 1.00 30.30 ? 199 LEU A CD1 1 
ATOM   1651 C CD2 . LEU A 1 203 ? 34.033 -8.681  27.762 1.00 30.87 ? 199 LEU A CD2 1 
ATOM   1652 N N   . SER A 1 204 ? 33.010 -11.654 23.880 1.00 30.93 ? 200 SER A N   1 
ATOM   1653 C CA  . SER A 1 204 ? 32.453 -12.294 22.679 1.00 31.45 ? 200 SER A CA  1 
ATOM   1654 C C   . SER A 1 204 ? 31.311 -11.408 22.168 1.00 31.93 ? 200 SER A C   1 
ATOM   1655 O O   . SER A 1 204 ? 30.364 -11.202 22.916 1.00 29.80 ? 200 SER A O   1 
ATOM   1656 C CB  . SER A 1 204 ? 31.973 -13.674 23.025 1.00 33.90 ? 200 SER A CB  1 
ATOM   1657 O OG  . SER A 1 204 ? 31.360 -14.253 21.890 1.00 38.48 ? 200 SER A OG  1 
ATOM   1658 N N   . THR A 1 205 ? 31.384 -10.930 20.935 1.00 31.43 ? 201 THR A N   1 
ATOM   1659 C CA  . THR A 1 205 ? 30.337 -10.057 20.341 1.00 34.27 ? 201 THR A CA  1 
ATOM   1660 C C   . THR A 1 205 ? 29.581 -10.808 19.237 1.00 35.30 ? 201 THR A C   1 
ATOM   1661 O O   . THR A 1 205 ? 30.273 -11.380 18.338 1.00 34.96 ? 201 THR A O   1 
ATOM   1662 C CB  . THR A 1 205 ? 30.912 -8.744  19.768 1.00 34.48 ? 201 THR A CB  1 
ATOM   1663 O OG1 . THR A 1 205 ? 31.555 -8.001  20.813 1.00 34.99 ? 201 THR A OG1 1 
ATOM   1664 C CG2 . THR A 1 205 ? 29.830 -7.897  19.127 1.00 35.89 ? 201 THR A CG2 1 
ATOM   1665 N N   . GLN A 1 206 ? 28.247 -10.832 19.344 1.00 30.48 ? 202 GLN A N   1 
ATOM   1666 C CA  . GLN A 1 206 ? 27.314 -11.366 18.329 1.00 35.10 ? 202 GLN A CA  1 
ATOM   1667 C C   . GLN A 1 206 ? 26.619 -10.117 17.782 1.00 39.72 ? 202 GLN A C   1 
ATOM   1668 O O   . GLN A 1 206 ? 26.118 -9.321  18.575 1.00 36.40 ? 202 GLN A O   1 
ATOM   1669 C CB  . GLN A 1 206 ? 26.417 -12.423 18.983 1.00 41.75 ? 202 GLN A CB  1 
ATOM   1670 C CG  . GLN A 1 206 ? 25.413 -13.101 18.065 1.00 46.73 ? 202 GLN A CG  1 
ATOM   1671 C CD  . GLN A 1 206 ? 24.184 -12.262 17.797 1.00 57.57 ? 202 GLN A CD  1 
ATOM   1672 O OE1 . GLN A 1 206 ? 23.755 -11.451 18.623 1.00 63.25 ? 202 GLN A OE1 1 
ATOM   1673 N NE2 . GLN A 1 206 ? 23.633 -12.404 16.600 1.00 63.55 ? 202 GLN A NE2 1 
ATOM   1674 N N   . SER A 1 207 ? 26.707 -9.880  16.479 1.00 36.44 ? 203 SER A N   1 
ATOM   1675 C CA  . SER A 1 207 ? 26.211 -8.618  15.874 1.00 37.18 ? 203 SER A CA  1 
ATOM   1676 C C   . SER A 1 207 ? 25.225 -8.914  14.736 1.00 44.25 ? 203 SER A C   1 
ATOM   1677 O O   . SER A 1 207 ? 25.426 -9.915  14.027 1.00 40.71 ? 203 SER A O   1 
ATOM   1678 C CB  . SER A 1 207 ? 27.367 -7.808  15.393 1.00 37.93 ? 203 SER A CB  1 
ATOM   1679 O OG  . SER A 1 207 ? 26.887 -6.708  14.636 1.00 45.76 ? 203 SER A OG  1 
ATOM   1680 N N   . LYS A 1 208 ? 24.181 -8.099  14.617 1.00 41.16 ? 204 LYS A N   1 
ATOM   1681 C CA  . LYS A 1 208 ? 23.231 -8.113  13.468 1.00 42.73 ? 204 LYS A CA  1 
ATOM   1682 C C   . LYS A 1 208 ? 23.176 -6.684  12.935 1.00 44.56 ? 204 LYS A C   1 
ATOM   1683 O O   . LYS A 1 208 ? 22.810 -5.766  13.705 1.00 39.74 ? 204 LYS A O   1 
ATOM   1684 C CB  . LYS A 1 208 ? 21.866 -8.663  13.882 1.00 48.07 ? 204 LYS A CB  1 
ATOM   1685 C CG  . LYS A 1 208 ? 20.970 -8.993  12.695 1.00 57.81 ? 204 LYS A CG  1 
ATOM   1686 C CD  . LYS A 1 208 ? 19.556 -9.389  13.070 1.00 67.12 ? 204 LYS A CD  1 
ATOM   1687 C CE  . LYS A 1 208 ? 18.564 -9.084  11.967 1.00 73.06 ? 204 LYS A CE  1 
ATOM   1688 N NZ  . LYS A 1 208 ? 18.304 -7.624  11.870 1.00 80.35 ? 204 LYS A NZ  1 
ATOM   1689 N N   . GLN A 1 209 ? 23.571 -6.498  11.678 1.00 41.29 ? 205 GLN A N   1 
ATOM   1690 C CA  . GLN A 1 209 ? 23.690 -5.172  11.029 1.00 43.42 ? 205 GLN A CA  1 
ATOM   1691 C C   . GLN A 1 209 ? 22.552 -5.038  10.016 1.00 42.40 ? 205 GLN A C   1 
ATOM   1692 O O   . GLN A 1 209 ? 22.300 -6.010  9.270  1.00 43.40 ? 205 GLN A O   1 
ATOM   1693 C CB  . GLN A 1 209 ? 25.043 -5.038  10.357 1.00 46.65 ? 205 GLN A CB  1 
ATOM   1694 C CG  . GLN A 1 209 ? 25.231 -3.722  9.626  1.00 52.77 ? 205 GLN A CG  1 
ATOM   1695 C CD  . GLN A 1 209 ? 26.440 -3.759  8.716  1.00 62.87 ? 205 GLN A CD  1 
ATOM   1696 O OE1 . GLN A 1 209 ? 26.773 -4.786  8.131  1.00 80.22 ? 205 GLN A OE1 1 
ATOM   1697 N NE2 . GLN A 1 209 ? 27.118 -2.638  8.582  1.00 67.39 ? 205 GLN A NE2 1 
ATOM   1698 N N   . SER A 1 210 ? 21.856 -3.905  9.994  1.00 40.71 ? 206 SER A N   1 
ATOM   1699 C CA  . SER A 1 210 ? 20.729 -3.674  9.053  1.00 41.54 ? 206 SER A CA  1 
ATOM   1700 C C   . SER A 1 210 ? 20.682 -2.216  8.564  1.00 42.41 ? 206 SER A C   1 
ATOM   1701 O O   . SER A 1 210 ? 21.588 -1.374  8.902  1.00 39.88 ? 206 SER A O   1 
ATOM   1702 C CB  . SER A 1 210 ? 19.443 -4.116  9.679  1.00 37.49 ? 206 SER A CB  1 
ATOM   1703 O OG  . SER A 1 210 ? 19.180 -3.418  10.886 1.00 40.92 ? 206 SER A OG  1 
ATOM   1704 N N   . LYS A 1 211 ? 19.721 -1.951  7.677  1.00 43.59 ? 207 LYS A N   1 
ATOM   1705 C CA  . LYS A 1 211 ? 19.382 -0.589  7.209  1.00 41.02 ? 207 LYS A CA  1 
ATOM   1706 C C   . LYS A 1 211 ? 17.958 -0.255  7.642  1.00 41.30 ? 207 LYS A C   1 
ATOM   1707 O O   . LYS A 1 211 ? 17.085 -1.161  7.803  1.00 41.85 ? 207 LYS A O   1 
ATOM   1708 C CB  . LYS A 1 211 ? 19.566 -0.446  5.693  1.00 40.42 ? 207 LYS A CB  1 
ATOM   1709 C CG  . LYS A 1 211 ? 20.984 -0.658  5.173  1.00 45.44 ? 207 LYS A CG  1 
ATOM   1710 C CD  . LYS A 1 211 ? 22.001 0.406   5.583  1.00 49.27 ? 207 LYS A CD  1 
ATOM   1711 C CE  . LYS A 1 211 ? 23.223 0.405   4.695  1.00 47.50 ? 207 LYS A CE  1 
ATOM   1712 N NZ  . LYS A 1 211 ? 24.271 1.362   5.132  1.00 46.76 ? 207 LYS A NZ  1 
ATOM   1713 N N   . ASP A 1 212 ? 17.733 1.029   7.863  1.00 41.71 ? 208 ASP A N   1 
ATOM   1714 C CA  . ASP A 1 212 ? 16.414 1.619   8.179  1.00 41.05 ? 208 ASP A CA  1 
ATOM   1715 C C   . ASP A 1 212 ? 15.820 2.011   6.827  1.00 43.11 ? 208 ASP A C   1 
ATOM   1716 O O   . ASP A 1 212 ? 16.381 2.867   6.168  1.00 36.56 ? 208 ASP A O   1 
ATOM   1717 C CB  . ASP A 1 212 ? 16.615 2.790   9.136  1.00 40.18 ? 208 ASP A CB  1 
ATOM   1718 C CG  . ASP A 1 212 ? 15.353 3.567   9.441  1.00 43.13 ? 208 ASP A CG  1 
ATOM   1719 O OD1 . ASP A 1 212 ? 14.301 3.243   8.859  1.00 40.09 ? 208 ASP A OD1 1 
ATOM   1720 O OD2 . ASP A 1 212 ? 15.426 4.485   10.271 1.00 41.74 ? 208 ASP A OD2 1 
ATOM   1721 N N   . PRO A 1 213 ? 14.714 1.401   6.341  1.00 47.38 ? 209 PRO A N   1 
ATOM   1722 C CA  . PRO A 1 213 ? 14.214 1.718   4.996  1.00 49.54 ? 209 PRO A CA  1 
ATOM   1723 C C   . PRO A 1 213 ? 13.659 3.158   4.879  1.00 45.09 ? 209 PRO A C   1 
ATOM   1724 O O   . PRO A 1 213 ? 13.535 3.649   3.789  1.00 50.16 ? 209 PRO A O   1 
ATOM   1725 C CB  . PRO A 1 213 ? 13.124 0.660   4.723  1.00 47.85 ? 209 PRO A CB  1 
ATOM   1726 C CG  . PRO A 1 213 ? 12.743 0.093   6.098  1.00 52.79 ? 209 PRO A CG  1 
ATOM   1727 C CD  . PRO A 1 213 ? 13.882 0.419   7.052  1.00 49.75 ? 209 PRO A CD  1 
ATOM   1728 N N   . ASN A 1 214 ? 13.331 3.804   5.993  1.00 45.76 ? 210 ASN A N   1 
ATOM   1729 C CA  . ASN A 1 214 ? 12.831 5.208   6.030  1.00 45.50 ? 210 ASN A CA  1 
ATOM   1730 C C   . ASN A 1 214 ? 13.962 6.220   6.239  1.00 41.90 ? 210 ASN A C   1 
ATOM   1731 O O   . ASN A 1 214 ? 13.645 7.396   6.356  1.00 45.18 ? 210 ASN A O   1 
ATOM   1732 C CB  . ASN A 1 214 ? 11.815 5.396   7.150  1.00 50.96 ? 210 ASN A CB  1 
ATOM   1733 C CG  . ASN A 1 214 ? 10.636 4.460   7.009  1.00 59.76 ? 210 ASN A CG  1 
ATOM   1734 O OD1 . ASN A 1 214 ? 10.134 3.939   7.998  1.00 64.65 ? 210 ASN A OD1 1 
ATOM   1735 N ND2 . ASN A 1 214 ? 10.203 4.234   5.780  1.00 58.07 ? 210 ASN A ND2 1 
ATOM   1736 N N   . GLU A 1 215 ? 15.221 5.801   6.304  1.00 35.88 ? 211 GLU A N   1 
ATOM   1737 C CA  . GLU A 1 215 ? 16.366 6.712   6.567  1.00 35.96 ? 211 GLU A CA  1 
ATOM   1738 C C   . GLU A 1 215 ? 17.078 7.063   5.265  1.00 34.83 ? 211 GLU A C   1 
ATOM   1739 O O   . GLU A 1 215 ? 17.647 6.163   4.661  1.00 35.68 ? 211 GLU A O   1 
ATOM   1740 C CB  . GLU A 1 215 ? 17.382 6.039   7.492  1.00 33.85 ? 211 GLU A CB  1 
ATOM   1741 C CG  . GLU A 1 215 ? 18.530 6.953   7.871  1.00 32.88 ? 211 GLU A CG  1 
ATOM   1742 C CD  . GLU A 1 215 ? 18.071 8.310   8.379  1.00 34.59 ? 211 GLU A CD  1 
ATOM   1743 O OE1 . GLU A 1 215 ? 17.514 8.332   9.513  1.00 32.35 ? 211 GLU A OE1 1 
ATOM   1744 O OE2 . GLU A 1 215 ? 18.246 9.328   7.651  1.00 33.40 ? 211 GLU A OE2 1 
ATOM   1745 N N   . LYS A 1 216 ? 17.083 8.331   4.868  1.00 34.37 ? 212 LYS A N   1 
ATOM   1746 C CA  . LYS A 1 216 ? 17.755 8.774   3.611  1.00 36.24 ? 212 LYS A CA  1 
ATOM   1747 C C   . LYS A 1 216 ? 19.221 9.145   3.826  1.00 34.16 ? 212 LYS A C   1 
ATOM   1748 O O   . LYS A 1 216 ? 19.987 9.174   2.858  1.00 33.54 ? 212 LYS A O   1 
ATOM   1749 C CB  . LYS A 1 216 ? 16.969 9.951   3.070  1.00 36.54 ? 212 LYS A CB  1 
ATOM   1750 C CG  . LYS A 1 216 ? 15.608 9.542   2.557  1.00 40.84 ? 212 LYS A CG  1 
ATOM   1751 C CD  . LYS A 1 216 ? 14.769 10.757  2.269  1.00 49.13 ? 212 LYS A CD  1 
ATOM   1752 C CE  . LYS A 1 216 ? 13.419 10.442  1.672  1.00 52.41 ? 212 LYS A CE  1 
ATOM   1753 N NZ  . LYS A 1 216 ? 12.829 11.699  1.160  1.00 59.28 ? 212 LYS A NZ  1 
ATOM   1754 N N   . ARG A 1 217 ? 19.611 9.399   5.066  1.00 32.06 ? 213 ARG A N   1 
ATOM   1755 C CA  . ARG A 1 217 ? 21.019 9.670   5.416  1.00 31.67 ? 213 ARG A CA  1 
ATOM   1756 C C   . ARG A 1 217 ? 21.821 8.361   5.384  1.00 32.06 ? 213 ARG A C   1 
ATOM   1757 O O   . ARG A 1 217 ? 21.254 7.248   5.508  1.00 31.92 ? 213 ARG A O   1 
ATOM   1758 C CB  . ARG A 1 217 ? 21.127 10.365  6.777  1.00 32.03 ? 213 ARG A CB  1 
ATOM   1759 C CG  . ARG A 1 217 ? 20.457 11.739  6.811  1.00 32.80 ? 213 ARG A CG  1 
ATOM   1760 C CD  . ARG A 1 217 ? 20.321 12.268  8.208  1.00 34.00 ? 213 ARG A CD  1 
ATOM   1761 N NE  . ARG A 1 217 ? 19.370 11.462  8.963  1.00 33.91 ? 213 ARG A NE  1 
ATOM   1762 C CZ  . ARG A 1 217 ? 19.046 11.684  10.231 1.00 35.13 ? 213 ARG A CZ  1 
ATOM   1763 N NH1 . ARG A 1 217 ? 19.581 12.698  10.895 1.00 36.69 ? 213 ARG A NH1 1 
ATOM   1764 N NH2 . ARG A 1 217 ? 18.174 10.893  10.825 1.00 36.22 ? 213 ARG A NH2 1 
ATOM   1765 N N   . ASP A 1 218 ? 23.111 8.491   5.083  1.00 32.14 ? 214 ASP A N   1 
ATOM   1766 C CA  A ASP A 1 218 ? 24.068 7.362   5.159  0.50 32.73 ? 214 ASP A CA  1 
ATOM   1767 C CA  B ASP A 1 218 ? 24.071 7.361   5.162  0.50 36.02 ? 214 ASP A CA  1 
ATOM   1768 C C   . ASP A 1 218 ? 24.037 6.875   6.606  1.00 33.66 ? 214 ASP A C   1 
ATOM   1769 O O   . ASP A 1 218 ? 24.203 7.733   7.502  1.00 33.88 ? 214 ASP A O   1 
ATOM   1770 C CB  A ASP A 1 218 ? 25.468 7.789   4.734  0.50 32.27 ? 214 ASP A CB  1 
ATOM   1771 C CB  B ASP A 1 218 ? 25.492 7.759   4.771  0.50 40.38 ? 214 ASP A CB  1 
ATOM   1772 C CG  A ASP A 1 218 ? 26.316 6.672   4.164  0.50 29.32 ? 214 ASP A CG  1 
ATOM   1773 C CG  B ASP A 1 218 ? 25.725 7.822   3.276  0.50 45.87 ? 214 ASP A CG  1 
ATOM   1774 O OD1 A ASP A 1 218 ? 25.952 5.509   4.339  0.50 28.63 ? 214 ASP A OD1 1 
ATOM   1775 O OD1 B ASP A 1 218 ? 24.719 7.802   2.524  0.50 46.78 ? 214 ASP A OD1 1 
ATOM   1776 O OD2 A ASP A 1 218 ? 27.332 7.010   3.537  0.50 30.33 ? 214 ASP A OD2 1 
ATOM   1777 O OD2 B ASP A 1 218 ? 26.917 7.862   2.880  0.50 48.50 ? 214 ASP A OD2 1 
ATOM   1778 N N   . HIS A 1 219 ? 23.775 5.590   6.821  1.00 31.09 ? 215 HIS A N   1 
ATOM   1779 C CA  . HIS A 1 219 ? 23.501 5.126   8.214  1.00 32.40 ? 215 HIS A CA  1 
ATOM   1780 C C   . HIS A 1 219 ? 23.823 3.644   8.396  1.00 32.35 ? 215 HIS A C   1 
ATOM   1781 O O   . HIS A 1 219 ? 24.024 2.927   7.402  1.00 33.13 ? 215 HIS A O   1 
ATOM   1782 C CB  . HIS A 1 219 ? 22.046 5.427   8.594  1.00 31.30 ? 215 HIS A CB  1 
ATOM   1783 C CG  . HIS A 1 219 ? 21.104 4.533   7.892  1.00 33.09 ? 215 HIS A CG  1 
ATOM   1784 N ND1 . HIS A 1 219 ? 20.785 4.710   6.548  1.00 32.48 ? 215 HIS A ND1 1 
ATOM   1785 C CD2 . HIS A 1 219 ? 20.458 3.430   8.306  1.00 36.49 ? 215 HIS A CD2 1 
ATOM   1786 C CE1 . HIS A 1 219 ? 19.974 3.732   6.179  1.00 36.72 ? 215 HIS A CE1 1 
ATOM   1787 N NE2 . HIS A 1 219 ? 19.748 2.946   7.239  1.00 37.35 ? 215 HIS A NE2 1 
ATOM   1788 N N   . MET A 1 220 ? 23.773 3.197   9.655  1.00 31.53 ? 216 MET A N   1 
ATOM   1789 C CA  . MET A 1 220 ? 24.026 1.785   10.027 1.00 32.50 ? 216 MET A CA  1 
ATOM   1790 C C   . MET A 1 220 ? 23.167 1.509   11.260 1.00 34.50 ? 216 MET A C   1 
ATOM   1791 O O   . MET A 1 220 ? 23.228 2.305   12.220 1.00 32.29 ? 216 MET A O   1 
ATOM   1792 C CB  . MET A 1 220 ? 25.509 1.575   10.345 1.00 34.96 ? 216 MET A CB  1 
ATOM   1793 C CG  . MET A 1 220 ? 25.819 0.232   10.944 1.00 35.49 ? 216 MET A CG  1 
ATOM   1794 S SD  . MET A 1 220 ? 27.561 -0.085  11.050 1.00 36.51 ? 216 MET A SD  1 
ATOM   1795 C CE  . MET A 1 220 ? 28.060 1.030   12.361 1.00 35.16 ? 216 MET A CE  1 
ATOM   1796 N N   . VAL A 1 221 ? 22.404 0.416   11.250 1.00 32.22 ? 217 VAL A N   1 
ATOM   1797 C CA  . VAL A 1 221 ? 21.604 -0.020  12.421 1.00 30.95 ? 217 VAL A CA  1 
ATOM   1798 C C   . VAL A 1 221 ? 22.266 -1.302  12.926 1.00 30.60 ? 217 VAL A C   1 
ATOM   1799 O O   . VAL A 1 221 ? 22.571 -2.171  12.096 1.00 34.84 ? 217 VAL A O   1 
ATOM   1800 C CB  . VAL A 1 221 ? 20.127 -0.268  12.057 1.00 32.91 ? 217 VAL A CB  1 
ATOM   1801 C CG1 . VAL A 1 221 ? 19.373 -0.814  13.258 1.00 34.28 ? 217 VAL A CG1 1 
ATOM   1802 C CG2 . VAL A 1 221 ? 19.449 0.999   11.546 1.00 33.31 ? 217 VAL A CG2 1 
ATOM   1803 N N   . LEU A 1 222 ? 22.498 -1.390  14.235 1.00 30.57 ? 218 LEU A N   1 
ATOM   1804 C CA  . LEU A 1 222 ? 23.135 -2.569  14.862 1.00 31.33 ? 218 LEU A CA  1 
ATOM   1805 C C   . LEU A 1 222 ? 22.296 -3.061  16.025 1.00 33.17 ? 218 LEU A C   1 
ATOM   1806 O O   . LEU A 1 222 ? 21.730 -2.254  16.808 1.00 34.04 ? 218 LEU A O   1 
ATOM   1807 C CB  . LEU A 1 222 ? 24.512 -2.268  15.450 1.00 32.36 ? 218 LEU A CB  1 
ATOM   1808 C CG  . LEU A 1 222 ? 25.596 -1.833  14.485 1.00 38.15 ? 218 LEU A CG  1 
ATOM   1809 C CD1 . LEU A 1 222 ? 26.848 -1.487  15.262 1.00 38.23 ? 218 LEU A CD1 1 
ATOM   1810 C CD2 . LEU A 1 222 ? 25.862 -2.912  13.448 1.00 38.80 ? 218 LEU A CD2 1 
ATOM   1811 N N   . LEU A 1 223 ? 22.334 -4.375  16.187 1.00 29.91 ? 219 LEU A N   1 
ATOM   1812 C CA  . LEU A 1 223 ? 21.826 -5.043  17.398 1.00 31.02 ? 219 LEU A CA  1 
ATOM   1813 C C   . LEU A 1 223 ? 22.961 -5.939  17.855 1.00 31.91 ? 219 LEU A C   1 
ATOM   1814 O O   . LEU A 1 223 ? 23.291 -6.899  17.132 1.00 34.31 ? 219 LEU A O   1 
ATOM   1815 C CB  . LEU A 1 223 ? 20.575 -5.874  17.087 1.00 34.22 ? 219 LEU A CB  1 
ATOM   1816 C CG  . LEU A 1 223 ? 20.019 -6.684  18.257 1.00 37.80 ? 219 LEU A CG  1 
ATOM   1817 C CD1 . LEU A 1 223 ? 19.656 -5.792  19.438 1.00 40.39 ? 219 LEU A CD1 1 
ATOM   1818 C CD2 . LEU A 1 223 ? 18.796 -7.495  17.810 1.00 40.21 ? 219 LEU A CD2 1 
ATOM   1819 N N   . GLU A 1 224 ? 23.545 -5.624  18.994 1.00 28.14 ? 220 GLU A N   1 
ATOM   1820 C CA  . GLU A 1 224 ? 24.793 -6.261  19.468 1.00 29.40 ? 220 GLU A CA  1 
ATOM   1821 C C   . GLU A 1 224 ? 24.509 -6.979  20.783 1.00 29.98 ? 220 GLU A C   1 
ATOM   1822 O O   . GLU A 1 224 ? 23.776 -6.427  21.652 1.00 29.67 ? 220 GLU A O   1 
ATOM   1823 C CB  . GLU A 1 224 ? 25.838 -5.206  19.787 1.00 33.15 ? 220 GLU A CB  1 
ATOM   1824 C CG  . GLU A 1 224 ? 26.072 -4.270  18.667 1.00 35.28 ? 220 GLU A CG  1 
ATOM   1825 C CD  . GLU A 1 224 ? 26.711 -4.977  17.509 1.00 36.84 ? 220 GLU A CD  1 
ATOM   1826 O OE1 . GLU A 1 224 ? 27.871 -5.379  17.682 1.00 41.08 ? 220 GLU A OE1 1 
ATOM   1827 O OE2 . GLU A 1 224 ? 26.026 -5.136  16.456 1.00 40.54 ? 220 GLU A OE2 1 
ATOM   1828 N N   . PHE A 1 225 ? 25.112 -8.172  20.944 1.00 29.30 ? 221 PHE A N   1 
ATOM   1829 C CA  . PHE A 1 225 ? 25.113 -8.905  22.228 1.00 29.12 ? 221 PHE A CA  1 
ATOM   1830 C C   . PHE A 1 225 ? 26.564 -9.199  22.588 1.00 31.19 ? 221 PHE A C   1 
ATOM   1831 O O   . PHE A 1 225 ? 27.298 -9.774  21.773 1.00 31.45 ? 221 PHE A O   1 
ATOM   1832 C CB  . PHE A 1 225 ? 24.252 -10.161 22.121 1.00 31.59 ? 221 PHE A CB  1 
ATOM   1833 C CG  . PHE A 1 225 ? 22.782 -9.867  22.025 1.00 28.80 ? 221 PHE A CG  1 
ATOM   1834 C CD1 . PHE A 1 225 ? 22.044 -9.670  23.174 1.00 31.49 ? 221 PHE A CD1 1 
ATOM   1835 C CD2 . PHE A 1 225 ? 22.170 -9.726  20.794 1.00 32.92 ? 221 PHE A CD2 1 
ATOM   1836 C CE1 . PHE A 1 225 ? 20.684 -9.401  23.097 1.00 31.58 ? 221 PHE A CE1 1 
ATOM   1837 C CE2 . PHE A 1 225 ? 20.814 -9.462  20.720 1.00 30.55 ? 221 PHE A CE2 1 
ATOM   1838 C CZ  . PHE A 1 225 ? 20.094 -9.272  21.865 1.00 31.07 ? 221 PHE A CZ  1 
ATOM   1839 N N   . VAL A 1 226 ? 26.989 -8.761  23.766 1.00 30.21 ? 222 VAL A N   1 
ATOM   1840 C CA  . VAL A 1 226 ? 28.409 -8.883  24.192 1.00 29.93 ? 222 VAL A CA  1 
ATOM   1841 C C   . VAL A 1 226 ? 28.478 -9.565  25.549 1.00 27.98 ? 222 VAL A C   1 
ATOM   1842 O O   . VAL A 1 226 ? 27.764 -9.157  26.499 1.00 30.16 ? 222 VAL A O   1 
ATOM   1843 C CB  . VAL A 1 226 ? 29.099 -7.511  24.210 1.00 28.55 ? 222 VAL A CB  1 
ATOM   1844 C CG1 . VAL A 1 226 ? 30.542 -7.600  24.596 1.00 30.70 ? 222 VAL A CG1 1 
ATOM   1845 C CG2 . VAL A 1 226 ? 28.897 -6.795  22.894 1.00 29.44 ? 222 VAL A CG2 1 
ATOM   1846 N N   . THR A 1 227 ? 29.244 -10.659 25.590 1.00 30.22 ? 223 THR A N   1 
ATOM   1847 C CA  . THR A 1 227 ? 29.347 -11.535 26.773 1.00 29.16 ? 223 THR A CA  1 
ATOM   1848 C C   . THR A 1 227 ? 30.810 -11.736 27.146 1.00 28.16 ? 223 THR A C   1 
ATOM   1849 O O   . THR A 1 227 ? 31.643 -12.110 26.253 1.00 30.34 ? 223 THR A O   1 
ATOM   1850 C CB  . THR A 1 227 ? 28.720 -12.906 26.500 1.00 32.80 ? 223 THR A CB  1 
ATOM   1851 O OG1 . THR A 1 227 ? 27.423 -12.695 25.934 1.00 34.12 ? 223 THR A OG1 1 
ATOM   1852 C CG2 . THR A 1 227 ? 28.687 -13.742 27.765 1.00 33.92 ? 223 THR A CG2 1 
ATOM   1853 N N   . ALA A 1 228 ? 31.149 -11.531 28.413 1.00 28.46 ? 224 ALA A N   1 
ATOM   1854 C CA  . ALA A 1 228 ? 32.490 -11.876 28.931 1.00 29.43 ? 224 ALA A CA  1 
ATOM   1855 C C   . ALA A 1 228 ? 32.603 -13.401 29.113 1.00 32.17 ? 224 ALA A C   1 
ATOM   1856 O O   . ALA A 1 228 ? 31.645 -14.062 29.540 1.00 30.74 ? 224 ALA A O   1 
ATOM   1857 C CB  . ALA A 1 228 ? 32.800 -11.136 30.203 1.00 31.44 ? 224 ALA A CB  1 
ATOM   1858 N N   . ALA A 1 229 ? 33.786 -13.937 28.831 1.00 32.64 ? 225 ALA A N   1 
ATOM   1859 C CA  . ALA A 1 229 ? 34.048 -15.391 28.858 1.00 32.68 ? 225 ALA A CA  1 
ATOM   1860 C C   . ALA A 1 229 ? 35.535 -15.645 29.041 1.00 36.26 ? 225 ALA A C   1 
ATOM   1861 O O   . ALA A 1 229 ? 36.336 -14.689 29.075 1.00 31.59 ? 225 ALA A O   1 
ATOM   1862 C CB  . ALA A 1 229 ? 33.528 -16.001 27.581 1.00 33.36 ? 225 ALA A CB  1 
ATOM   1863 N N   . GLY A 1 230 ? 35.906 -16.924 29.170 1.00 36.29 ? 226 GLY A N   1 
ATOM   1864 C CA  . GLY A 1 230 ? 37.327 -17.309 29.232 1.00 37.48 ? 226 GLY A CA  1 
ATOM   1865 C C   . GLY A 1 230 ? 37.799 -17.645 30.634 1.00 42.28 ? 226 GLY A C   1 
ATOM   1866 O O   . GLY A 1 230 ? 38.960 -18.015 30.766 1.00 40.81 ? 226 GLY A O   1 
ATOM   1867 N N   . ILE A 1 231 ? 36.957 -17.518 31.655 1.00 41.02 ? 227 ILE A N   1 
ATOM   1868 C CA  . ILE A 1 231 ? 37.225 -17.999 33.044 1.00 47.16 ? 227 ILE A CA  1 
ATOM   1869 C C   . ILE A 1 231 ? 36.082 -18.942 33.428 1.00 49.88 ? 227 ILE A C   1 
ATOM   1870 O O   . ILE A 1 231 ? 34.916 -18.545 33.455 1.00 47.48 ? 227 ILE A O   1 
ATOM   1871 C CB  . ILE A 1 231 ? 37.375 -16.816 34.020 1.00 48.04 ? 227 ILE A CB  1 
ATOM   1872 C CG1 . ILE A 1 231 ? 38.413 -15.800 33.535 1.00 46.79 ? 227 ILE A CG1 1 
ATOM   1873 C CG2 . ILE A 1 231 ? 37.686 -17.323 35.417 1.00 52.47 ? 227 ILE A CG2 1 
ATOM   1874 C CD1 . ILE A 1 231 ? 38.475 -14.529 34.348 1.00 44.42 ? 227 ILE A CD1 1 
ATOM   1875 N N   . PRO A 1 232 ? 36.354 -20.248 33.667 1.00 59.96 ? 228 PRO A N   1 
ATOM   1876 C CA  . PRO A 1 232 ? 35.273 -21.243 33.764 1.00 63.46 ? 228 PRO A CA  1 
ATOM   1877 C C   . PRO A 1 232 ? 34.462 -21.118 35.073 1.00 56.79 ? 228 PRO A C   1 
ATOM   1878 O O   . PRO A 1 232 ? 35.030 -20.679 36.044 1.00 52.67 ? 228 PRO A O   1 
ATOM   1879 C CB  . PRO A 1 232 ? 36.051 -22.569 33.630 1.00 62.69 ? 228 PRO A CB  1 
ATOM   1880 C CG  . PRO A 1 232 ? 37.404 -22.258 34.256 1.00 63.70 ? 228 PRO A CG  1 
ATOM   1881 C CD  . PRO A 1 232 ? 37.697 -20.827 33.857 1.00 63.32 ? 228 PRO A CD  1 
ATOM   1882 N N   . LEU A 1 233 ? 33.150 -21.426 35.056 1.00 59.13 ? 229 LEU A N   1 
ATOM   1883 C CA  . LEU A 1 233 ? 32.265 -21.358 36.262 1.00 63.13 ? 229 LEU A CA  1 
ATOM   1884 C C   . LEU A 1 233 ? 32.793 -22.359 37.291 1.00 60.78 ? 229 LEU A C   1 
ATOM   1885 O O   . LEU A 1 233 ? 33.010 -22.032 38.438 1.00 63.82 ? 229 LEU A O   1 
ATOM   1886 C CB  . LEU A 1 233 ? 30.798 -21.636 35.878 1.00 72.95 ? 229 LEU A CB  1 
ATOM   1887 C CG  . LEU A 1 233 ? 29.761 -21.620 37.015 1.00 81.95 ? 229 LEU A CG  1 
ATOM   1888 C CD1 . LEU A 1 233 ? 29.996 -20.472 37.990 1.00 81.87 ? 229 LEU A CD1 1 
ATOM   1889 C CD2 . LEU A 1 233 ? 28.329 -21.548 36.476 1.00 79.65 ? 229 LEU A CD2 1 
HETATM 1890 O O   . HOH B 2 .   ? 31.609 -5.927  38.321 0.50 30.37 ? 301 HOH A O   1 
HETATM 1891 O O   . HOH B 2 .   ? 31.204 13.618  27.198 1.00 59.30 ? 302 HOH A O   1 
HETATM 1892 O O   . HOH B 2 .   ? 21.112 7.947   14.808 0.50 28.69 ? 303 HOH A O   1 
HETATM 1893 O O   . HOH B 2 .   ? 31.039 1.391   1.633  0.50 37.81 ? 304 HOH A O   1 
HETATM 1894 O O   . HOH B 2 .   ? 18.475 8.207   14.568 0.50 31.86 ? 305 HOH A O   1 
HETATM 1895 O O   . HOH B 2 .   ? 50.083 1.063   28.353 1.00 52.32 ? 306 HOH A O   1 
HETATM 1896 O O   . HOH B 2 .   ? 42.699 -1.972  1.246  1.00 54.68 ? 307 HOH A O   1 
HETATM 1897 O O   . HOH B 2 .   ? 21.992 11.971  17.575 1.00 49.22 ? 308 HOH A O   1 
HETATM 1898 O O   . HOH B 2 .   ? 32.533 -2.309  40.005 1.00 45.92 ? 309 HOH A O   1 
HETATM 1899 O O   . HOH B 2 .   ? 29.420 17.295  31.141 1.00 51.21 ? 310 HOH A O   1 
HETATM 1900 O O   . HOH B 2 .   ? 28.370 -5.665  13.051 1.00 50.97 ? 311 HOH A O   1 
HETATM 1901 O O   . HOH B 2 .   ? 17.318 3.037   3.952  1.00 51.31 ? 312 HOH A O   1 
HETATM 1902 O O   . HOH B 2 .   ? 45.852 -12.409 26.551 1.00 46.61 ? 313 HOH A O   1 
HETATM 1903 O O   . HOH B 2 .   ? 46.121 -7.324  17.716 1.00 38.07 ? 314 HOH A O   1 
HETATM 1904 O O   . HOH B 2 .   ? 32.897 -9.311  6.914  1.00 50.81 ? 315 HOH A O   1 
HETATM 1905 O O   . HOH B 2 .   ? 28.027 16.885  29.006 1.00 47.69 ? 316 HOH A O   1 
HETATM 1906 O O   . HOH B 2 .   ? 30.536 11.303  34.459 1.00 60.10 ? 317 HOH A O   1 
HETATM 1907 O O   . HOH B 2 .   ? 38.187 11.169  40.585 1.00 50.71 ? 318 HOH A O   1 
HETATM 1908 O O   . HOH B 2 .   ? 32.404 14.487  29.154 1.00 56.08 ? 319 HOH A O   1 
HETATM 1909 O O   . HOH B 2 .   ? 48.165 -1.921  23.201 1.00 37.14 ? 320 HOH A O   1 
HETATM 1910 O O   . HOH B 2 .   ? 39.692 -7.866  40.164 1.00 50.93 ? 321 HOH A O   1 
HETATM 1911 O O   . HOH B 2 .   ? 16.950 -2.211  10.801 1.00 52.17 ? 322 HOH A O   1 
HETATM 1912 O O   . HOH B 2 .   ? 29.131 5.762   2.235  1.00 50.21 ? 323 HOH A O   1 
HETATM 1913 O O   . HOH B 2 .   ? 33.275 -6.131  5.212  1.00 43.68 ? 324 HOH A O   1 
HETATM 1914 O O   . HOH B 2 .   ? 46.190 5.798   34.606 1.00 47.90 ? 325 HOH A O   1 
HETATM 1915 O O   . HOH B 2 .   ? 32.440 11.859  1.954  1.00 53.27 ? 326 HOH A O   1 
HETATM 1916 O O   . HOH B 2 .   ? 39.206 -12.847 -5.691 1.00 43.34 ? 327 HOH A O   1 
HETATM 1917 O O   . HOH B 2 .   ? 17.603 -4.618  32.577 1.00 46.97 ? 328 HOH A O   1 
HETATM 1918 O O   . HOH B 2 .   ? 25.865 3.788   41.449 1.00 46.49 ? 329 HOH A O   1 
HETATM 1919 O O   . HOH B 2 .   ? 51.284 -2.684  32.839 1.00 35.74 ? 330 HOH A O   1 
HETATM 1920 O O   . HOH B 2 .   ? 38.934 4.619   20.532 1.00 33.81 ? 331 HOH A O   1 
HETATM 1921 O O   . HOH B 2 .   ? 49.985 3.333   16.932 1.00 41.84 ? 332 HOH A O   1 
HETATM 1922 O O   . HOH B 2 .   ? 36.513 0.788   13.938 1.00 29.58 ? 333 HOH A O   1 
HETATM 1923 O O   . HOH B 2 .   ? 31.877 15.873  30.771 1.00 50.68 ? 334 HOH A O   1 
HETATM 1924 O O   . HOH B 2 .   ? 27.188 -6.221  36.741 1.00 45.04 ? 335 HOH A O   1 
HETATM 1925 O O   . HOH B 2 .   ? 32.943 -15.237 19.756 1.00 53.23 ? 336 HOH A O   1 
HETATM 1926 O O   . HOH B 2 .   ? 31.076 13.045  5.070  1.00 43.01 ? 337 HOH A O   1 
HETATM 1927 O O   . HOH B 2 .   ? 22.506 -9.550  17.345 1.00 43.52 ? 338 HOH A O   1 
HETATM 1928 O O   . HOH B 2 .   ? 21.009 5.581   32.806 1.00 34.26 ? 339 HOH A O   1 
HETATM 1929 O O   . HOH B 2 .   ? 32.535 -13.022 41.305 1.00 49.59 ? 340 HOH A O   1 
HETATM 1930 O O   . HOH B 2 .   ? 37.519 -5.857  32.086 1.00 31.94 ? 341 HOH A O   1 
HETATM 1931 O O   . HOH B 2 .   ? 29.910 -6.486  35.848 1.00 33.24 ? 342 HOH A O   1 
HETATM 1932 O O   . HOH B 2 .   ? 45.309 -9.689  33.180 1.00 36.98 ? 343 HOH A O   1 
HETATM 1933 O O   . HOH B 2 .   ? 20.746 -3.943  32.179 1.00 35.03 ? 344 HOH A O   1 
HETATM 1934 O O   . HOH B 2 .   ? 31.379 -5.378  21.088 1.00 39.47 ? 345 HOH A O   1 
HETATM 1935 O O   . HOH B 2 .   ? 34.515 0.711   25.430 1.00 30.87 ? 346 HOH A O   1 
HETATM 1936 O O   . HOH B 2 .   ? 41.723 2.272   0.858  1.00 41.18 ? 347 HOH A O   1 
HETATM 1937 O O   . HOH B 2 .   ? 34.993 4.241   22.761 1.00 30.05 ? 348 HOH A O   1 
HETATM 1938 O O   . HOH B 2 .   ? 26.633 3.295   3.047  1.00 67.64 ? 349 HOH A O   1 
HETATM 1939 O O   . HOH B 2 .   ? 27.507 15.161  13.996 1.00 50.62 ? 350 HOH A O   1 
HETATM 1940 O O   . HOH B 2 .   ? 23.870 14.086  18.583 1.00 45.47 ? 351 HOH A O   1 
HETATM 1941 O O   . HOH B 2 .   ? 20.309 13.365  20.875 1.00 39.09 ? 352 HOH A O   1 
HETATM 1942 O O   . HOH B 2 .   ? 25.339 -11.313 39.624 1.00 49.53 ? 353 HOH A O   1 
HETATM 1943 O O   . HOH B 2 .   ? 48.679 -8.048  31.909 1.00 45.96 ? 354 HOH A O   1 
HETATM 1944 O O   . HOH B 2 .   ? 13.395 6.193   10.497 1.00 53.11 ? 355 HOH A O   1 
HETATM 1945 O O   . HOH B 2 .   ? 20.276 8.592   22.998 1.00 38.53 ? 356 HOH A O   1 
HETATM 1946 O O   . HOH B 2 .   ? 42.301 -15.931 33.160 1.00 44.02 ? 357 HOH A O   1 
HETATM 1947 O O   . HOH B 2 .   ? 34.702 12.227  34.056 1.00 38.76 ? 358 HOH A O   1 
HETATM 1948 O O   . HOH B 2 .   ? 45.136 10.270  25.437 1.00 56.58 ? 359 HOH A O   1 
HETATM 1949 O O   . HOH B 2 .   ? 22.973 13.548  28.984 1.00 39.20 ? 360 HOH A O   1 
HETATM 1950 O O   . HOH B 2 .   ? 16.773 -6.965  27.249 1.00 47.42 ? 361 HOH A O   1 
HETATM 1951 O O   . HOH B 2 .   ? 31.574 14.710  16.483 1.00 45.61 ? 362 HOH A O   1 
HETATM 1952 O O   . HOH B 2 .   ? 22.442 9.656   1.883  1.00 50.00 ? 363 HOH A O   1 
HETATM 1953 O O   . HOH B 2 .   ? 44.136 12.167  7.905  1.00 53.60 ? 364 HOH A O   1 
HETATM 1954 O O   . HOH B 2 .   ? 34.141 -8.577  21.272 1.00 33.51 ? 365 HOH A O   1 
HETATM 1955 O O   . HOH B 2 .   ? 30.584 13.457  32.873 1.00 46.32 ? 366 HOH A O   1 
HETATM 1956 O O   . HOH B 2 .   ? 19.466 10.444  29.882 1.00 45.41 ? 367 HOH A O   1 
HETATM 1957 O O   . HOH B 2 .   ? 46.987 -4.432  22.823 1.00 42.17 ? 368 HOH A O   1 
HETATM 1958 O O   . HOH B 2 .   ? 41.744 12.117  34.008 1.00 51.15 ? 369 HOH A O   1 
HETATM 1959 O O   . HOH B 2 .   ? 28.705 -14.633 22.170 1.00 38.78 ? 370 HOH A O   1 
HETATM 1960 O O   . HOH B 2 .   ? 42.865 8.299   36.387 1.00 47.95 ? 371 HOH A O   1 
HETATM 1961 O O   . HOH B 2 .   ? 36.348 7.731   -0.063 1.00 47.71 ? 372 HOH A O   1 
HETATM 1962 O O   . HOH B 2 .   ? 29.183 -4.166  19.714 1.00 40.05 ? 373 HOH A O   1 
HETATM 1963 O O   . HOH B 2 .   ? 30.862 -2.022  22.540 1.00 34.92 ? 374 HOH A O   1 
HETATM 1964 O O   . HOH B 2 .   ? 20.213 -4.615  13.094 1.00 40.20 ? 375 HOH A O   1 
HETATM 1965 O O   . HOH B 2 .   ? 39.382 12.064  21.913 1.00 46.36 ? 376 HOH A O   1 
HETATM 1966 O O   . HOH B 2 .   ? 18.272 6.500   23.592 1.00 50.98 ? 377 HOH A O   1 
HETATM 1967 O O   . HOH B 2 .   ? 18.519 2.682   33.664 1.00 40.24 ? 378 HOH A O   1 
HETATM 1968 O O   . HOH B 2 .   ? 39.592 13.504  13.513 1.00 53.76 ? 379 HOH A O   1 
HETATM 1969 O O   . HOH B 2 .   ? 24.209 11.110  5.299  1.00 40.81 ? 380 HOH A O   1 
HETATM 1970 O O   . HOH B 2 .   ? 30.459 -16.518 29.536 1.00 40.53 ? 381 HOH A O   1 
HETATM 1971 O O   . HOH B 2 .   ? 16.363 -3.696  26.442 1.00 48.32 ? 382 HOH A O   1 
HETATM 1972 O O   . HOH B 2 .   ? 35.188 -2.308  12.844 1.00 32.49 ? 383 HOH A O   1 
HETATM 1973 O O   . HOH B 2 .   ? 47.845 0.641   39.004 1.00 48.32 ? 384 HOH A O   1 
HETATM 1974 O O   . HOH B 2 .   ? 24.985 -12.032 27.000 1.00 40.10 ? 385 HOH A O   1 
HETATM 1975 O O   . HOH B 2 .   ? 41.554 14.661  1.232  1.00 61.52 ? 386 HOH A O   1 
HETATM 1976 O O   . HOH B 2 .   ? 15.343 9.950   9.062  1.00 43.10 ? 387 HOH A O   1 
HETATM 1977 O O   . HOH B 2 .   ? 25.535 -7.047  33.335 1.00 43.20 ? 388 HOH A O   1 
HETATM 1978 O O   . HOH B 2 .   ? 31.600 4.482   41.025 1.00 48.20 ? 389 HOH A O   1 
HETATM 1979 O O   . HOH B 2 .   ? 25.523 -4.189  36.079 1.00 41.61 ? 390 HOH A O   1 
HETATM 1980 O O   . HOH B 2 .   ? 41.501 5.656   39.008 1.00 51.27 ? 391 HOH A O   1 
HETATM 1981 O O   . HOH B 2 .   ? 31.473 -4.253  30.913 1.00 29.04 ? 392 HOH A O   1 
HETATM 1982 O O   . HOH B 2 .   ? 42.796 8.520   31.698 1.00 45.51 ? 393 HOH A O   1 
HETATM 1983 O O   . HOH B 2 .   ? 22.477 4.716   35.085 1.00 36.90 ? 394 HOH A O   1 
HETATM 1984 O O   . HOH B 2 .   ? 50.274 -1.065  5.024  1.00 48.33 ? 395 HOH A O   1 
HETATM 1985 O O   . HOH B 2 .   ? 52.344 -5.057  42.296 1.00 46.59 ? 396 HOH A O   1 
HETATM 1986 O O   . HOH B 2 .   ? 18.978 -1.962  16.702 1.00 42.00 ? 397 HOH A O   1 
HETATM 1987 O O   . HOH B 2 .   ? 27.365 17.423  11.019 1.00 53.26 ? 398 HOH A O   1 
HETATM 1988 O O   . HOH B 2 .   ? 29.992 -5.493  15.902 1.00 51.98 ? 399 HOH A O   1 
HETATM 1989 O O   . HOH B 2 .   ? 43.505 -12.052 27.459 1.00 37.57 ? 400 HOH A O   1 
HETATM 1990 O O   . HOH B 2 .   ? 49.212 -5.470  34.368 1.00 40.00 ? 401 HOH A O   1 
HETATM 1991 O O   . HOH B 2 .   ? 45.393 -13.343 33.989 1.00 42.91 ? 402 HOH A O   1 
HETATM 1992 O O   . HOH B 2 .   ? 36.052 15.706  11.110 1.00 40.11 ? 403 HOH A O   1 
HETATM 1993 O O   . HOH B 2 .   ? 21.437 14.669  10.255 1.00 45.96 ? 404 HOH A O   1 
HETATM 1994 O O   . HOH B 2 .   ? 36.457 -11.323 14.899 1.00 54.19 ? 405 HOH A O   1 
HETATM 1995 O O   . HOH B 2 .   ? 23.286 -10.697 33.924 1.00 36.15 ? 406 HOH A O   1 
HETATM 1996 O O   . HOH B 2 .   ? 29.099 13.655  15.720 1.00 39.53 ? 407 HOH A O   1 
HETATM 1997 O O   . HOH B 2 .   ? 33.221 -6.473  7.740  1.00 40.80 ? 408 HOH A O   1 
HETATM 1998 O O   . HOH B 2 .   ? 22.701 -1.343  31.015 1.00 30.51 ? 409 HOH A O   1 
HETATM 1999 O O   . HOH B 2 .   ? 45.033 6.559   19.772 1.00 34.61 ? 410 HOH A O   1 
HETATM 2000 O O   . HOH B 2 .   ? 37.310 6.580   36.283 1.00 33.64 ? 411 HOH A O   1 
HETATM 2001 O O   . HOH B 2 .   ? 34.517 13.116  3.562  1.00 51.67 ? 412 HOH A O   1 
HETATM 2002 O O   . HOH B 2 .   ? 15.434 -0.018  32.873 1.00 46.30 ? 413 HOH A O   1 
HETATM 2003 O O   . HOH B 2 .   ? 23.244 14.109  14.736 1.00 47.27 ? 414 HOH A O   1 
HETATM 2004 O O   . HOH B 2 .   ? 50.398 -3.678  6.163  1.00 46.48 ? 415 HOH A O   1 
HETATM 2005 O O   . HOH B 2 .   ? 26.691 -4.876  24.997 1.00 37.63 ? 416 HOH A O   1 
HETATM 2006 O O   . HOH B 2 .   ? 49.890 -2.903  44.526 1.00 51.77 ? 417 HOH A O   1 
HETATM 2007 O O   . HOH B 2 .   ? 19.264 -2.428  23.996 1.00 47.33 ? 418 HOH A O   1 
HETATM 2008 O O   . HOH B 2 .   ? 38.903 2.024   17.715 1.00 29.36 ? 419 HOH A O   1 
HETATM 2009 O O   . HOH B 2 .   ? 20.012 5.601   3.236  1.00 51.37 ? 420 HOH A O   1 
HETATM 2010 O O   . HOH B 2 .   ? 46.297 7.355   11.801 1.00 38.90 ? 421 HOH A O   1 
HETATM 2011 O O   . HOH B 2 .   ? 19.533 -6.350  36.247 1.00 50.24 ? 422 HOH A O   1 
HETATM 2012 O O   . HOH B 2 .   ? 33.456 16.534  10.257 1.00 42.65 ? 423 HOH A O   1 
HETATM 2013 O O   . HOH B 2 .   ? 26.044 10.633  36.132 1.00 42.36 ? 424 HOH A O   1 
HETATM 2014 O O   . HOH B 2 .   ? 27.473 -12.370 23.131 1.00 33.88 ? 425 HOH A O   1 
HETATM 2015 O O   . HOH B 2 .   ? 41.888 -13.964 26.071 1.00 45.18 ? 426 HOH A O   1 
HETATM 2016 O O   . HOH B 2 .   ? 39.769 -15.259 22.263 1.00 49.06 ? 427 HOH A O   1 
HETATM 2017 O O   . HOH B 2 .   ? 30.543 -15.730 41.847 1.00 54.71 ? 428 HOH A O   1 
HETATM 2018 O O   . HOH B 2 .   ? 32.809 16.707  5.783  1.00 57.56 ? 429 HOH A O   1 
HETATM 2019 O O   . HOH B 2 .   ? 16.312 4.346   29.893 1.00 50.14 ? 430 HOH A O   1 
HETATM 2020 O O   . HOH B 2 .   ? 32.597 -3.415  37.625 1.00 33.78 ? 431 HOH A O   1 
HETATM 2021 O O   . HOH B 2 .   ? 46.727 4.351   19.594 1.00 33.96 ? 432 HOH A O   1 
HETATM 2022 O O   . HOH B 2 .   ? 45.048 -9.665  17.120 1.00 40.52 ? 433 HOH A O   1 
HETATM 2023 O O   . HOH B 2 .   ? 18.581 -4.165  6.287  1.00 50.98 ? 434 HOH A O   1 
HETATM 2024 O O   . HOH B 2 .   ? 22.351 10.014  15.771 1.00 37.10 ? 435 HOH A O   1 
HETATM 2025 O O   . HOH B 2 .   ? 20.643 1.312   34.789 1.00 34.66 ? 436 HOH A O   1 
HETATM 2026 O O   . HOH B 2 .   ? 15.677 10.372  6.281  1.00 38.06 ? 437 HOH A O   1 
HETATM 2027 O O   . HOH B 2 .   ? 36.435 3.571   20.566 1.00 29.63 ? 438 HOH A O   1 
HETATM 2028 O O   . HOH B 2 .   ? 29.347 -3.873  24.964 1.00 38.92 ? 439 HOH A O   1 
HETATM 2029 O O   . HOH B 2 .   ? 37.844 -2.545  11.805 1.00 35.33 ? 440 HOH A O   1 
HETATM 2030 O O   . HOH B 2 .   ? 16.959 4.468   27.284 1.00 62.73 ? 441 HOH A O   1 
HETATM 2031 O O   . HOH B 2 .   ? 49.626 -4.819  30.033 1.00 49.39 ? 442 HOH A O   1 
HETATM 2032 O O   . HOH B 2 .   ? 33.605 13.639  18.615 1.00 46.38 ? 443 HOH A O   1 
HETATM 2033 O O   . HOH B 2 .   ? 32.599 -17.420 24.084 1.00 51.66 ? 444 HOH A O   1 
HETATM 2034 O O   . HOH B 2 .   ? 27.957 -7.225  33.555 1.00 37.42 ? 445 HOH A O   1 
HETATM 2035 O O   . HOH B 2 .   ? 23.550 -5.667  34.925 1.00 44.01 ? 446 HOH A O   1 
HETATM 2036 O O   . HOH B 2 .   ? 34.980 4.765   39.295 1.00 44.50 ? 447 HOH A O   1 
HETATM 2037 O O   . HOH B 2 .   ? 32.133 11.262  26.882 1.00 36.78 ? 448 HOH A O   1 
HETATM 2038 O O   . HOH B 2 .   ? 30.879 -8.728  -5.571 1.00 55.65 ? 449 HOH A O   1 
HETATM 2039 O O   . HOH B 2 .   ? 36.874 12.513  22.773 1.00 44.82 ? 450 HOH A O   1 
HETATM 2040 O O   . HOH B 2 .   ? 41.281 -5.583  40.871 1.00 49.40 ? 451 HOH A O   1 
HETATM 2041 O O   . HOH B 2 .   ? 16.058 7.575   13.584 1.00 44.48 ? 452 HOH A O   1 
HETATM 2042 O O   . HOH B 2 .   ? 40.621 -12.910 13.267 1.00 55.16 ? 453 HOH A O   1 
HETATM 2043 O O   . HOH B 2 .   ? 23.374 4.010   4.292  1.00 40.87 ? 454 HOH A O   1 
HETATM 2044 O O   . HOH B 2 .   ? 41.458 -12.008 17.069 1.00 41.05 ? 455 HOH A O   1 
HETATM 2045 O O   . HOH B 2 .   ? 20.927 12.492  31.137 1.00 41.98 ? 456 HOH A O   1 
HETATM 2046 O O   . HOH B 2 .   ? 36.367 -11.089 12.292 1.00 43.54 ? 457 HOH A O   1 
HETATM 2047 O O   . HOH B 2 .   ? 49.628 1.546   8.436  1.00 44.62 ? 458 HOH A O   1 
HETATM 2048 O O   . HOH B 2 .   ? 34.254 -5.975  22.528 1.00 34.80 ? 459 HOH A O   1 
HETATM 2049 O O   . HOH B 2 .   ? 36.869 16.699  3.712  1.00 46.32 ? 460 HOH A O   1 
HETATM 2050 O O   . HOH B 2 .   ? 37.252 -14.256 17.569 1.00 54.67 ? 461 HOH A O   1 
HETATM 2051 O O   . HOH B 2 .   ? 32.410 -0.830  1.199  1.00 43.50 ? 462 HOH A O   1 
HETATM 2052 O O   . HOH B 2 .   ? 27.027 13.656  35.044 1.00 36.75 ? 463 HOH A O   1 
HETATM 2053 O O   . HOH B 2 .   ? 44.278 -8.774  4.736  1.00 43.82 ? 464 HOH A O   1 
HETATM 2054 O O   . HOH B 2 .   ? 48.231 -0.690  8.475  1.00 40.71 ? 465 HOH A O   1 
HETATM 2055 O O   . HOH B 2 .   ? 20.345 1.701   37.434 1.00 49.33 ? 466 HOH A O   1 
HETATM 2056 O O   . HOH B 2 .   ? 52.267 -6.884  17.765 1.00 52.92 ? 467 HOH A O   1 
HETATM 2057 O O   . HOH B 2 .   ? 46.611 -6.193  9.652  1.00 49.74 ? 468 HOH A O   1 
HETATM 2058 O O   . HOH B 2 .   ? 43.882 5.020   27.186 1.00 40.61 ? 469 HOH A O   1 
HETATM 2059 O O   . HOH B 2 .   ? 42.661 1.101   41.192 1.00 52.90 ? 470 HOH A O   1 
HETATM 2060 O O   . HOH B 2 .   ? 29.636 -12.052 42.196 1.00 44.23 ? 471 HOH A O   1 
HETATM 2061 O O   . HOH B 2 .   ? 18.072 0.454   16.584 1.00 56.18 ? 472 HOH A O   1 
HETATM 2062 O O   . HOH B 2 .   ? 49.127 -11.813 29.413 1.00 58.04 ? 473 HOH A O   1 
HETATM 2063 O O   . HOH B 2 .   ? 36.177 12.991  36.531 1.00 51.21 ? 474 HOH A O   1 
HETATM 2064 O O   . HOH B 2 .   ? 37.464 5.694   38.759 1.00 48.91 ? 475 HOH A O   1 
HETATM 2065 O O   . HOH B 2 .   ? 28.473 11.527  35.777 1.00 39.73 ? 476 HOH A O   1 
HETATM 2066 O O   . HOH B 2 .   ? 50.457 2.234   6.312  1.00 52.84 ? 477 HOH A O   1 
HETATM 2067 O O   . HOH B 2 .   ? 22.695 15.229  7.765  1.00 48.70 ? 478 HOH A O   1 
HETATM 2068 O O   . HOH B 2 .   ? 28.908 15.455  34.061 1.00 47.68 ? 479 HOH A O   1 
HETATM 2069 O O   . HOH B 2 .   ? 17.433 1.680   20.700 1.00 47.77 ? 480 HOH A O   1 
HETATM 2070 O O   . HOH B 2 .   ? 15.579 12.618  9.863  1.00 47.28 ? 481 HOH A O   1 
HETATM 2071 O O   . HOH B 2 .   ? 12.916 10.400  5.295  1.00 57.05 ? 482 HOH A O   1 
HETATM 2072 O O   . HOH B 2 .   ? 52.827 5.354   33.779 1.00 54.69 ? 483 HOH A O   1 
HETATM 2073 O O   . HOH B 2 .   ? 42.376 -13.450 11.434 1.00 53.63 ? 484 HOH A O   1 
HETATM 2074 O O   . HOH B 2 .   ? 44.515 6.116   37.118 1.00 44.01 ? 485 HOH A O   1 
HETATM 2075 O O   . HOH B 2 .   ? 45.509 -8.504  37.304 1.00 54.70 ? 486 HOH A O   1 
HETATM 2076 O O   . HOH B 2 .   ? 31.970 -18.312 31.670 1.00 46.89 ? 487 HOH A O   1 
HETATM 2077 O O   . HOH B 2 .   ? 48.370 -5.030  9.761  1.00 53.04 ? 488 HOH A O   1 
HETATM 2078 O O   . HOH B 2 .   ? 43.883 -11.796 18.667 1.00 52.51 ? 489 HOH A O   1 
HETATM 2079 O O   . HOH B 2 .   ? 36.243 -15.294 3.779  1.00 78.62 ? 490 HOH A O   1 
HETATM 2080 O O   . HOH B 2 .   ? 50.876 -5.195  32.370 1.00 43.37 ? 491 HOH A O   1 
HETATM 2081 O O   . HOH B 2 .   ? 31.453 11.755  39.274 1.00 59.10 ? 492 HOH A O   1 
HETATM 2082 O O   . HOH B 2 .   ? 17.120 14.051  8.139  1.00 42.01 ? 493 HOH A O   1 
HETATM 2083 O O   . HOH B 2 .   ? 43.723 -6.827  40.985 1.00 52.92 ? 494 HOH A O   1 
HETATM 2084 O O   . HOH B 2 .   ? 33.741 16.122  27.724 1.00 54.86 ? 495 HOH A O   1 
HETATM 2085 O O   . HOH B 2 .   ? 46.722 -9.841  35.435 1.00 52.37 ? 496 HOH A O   1 
HETATM 2086 O O   . HOH B 2 .   ? 16.804 3.780   21.979 1.00 49.35 ? 497 HOH A O   1 
HETATM 2087 O O   . HOH B 2 .   ? 18.548 15.996  9.438  1.00 50.02 ? 498 HOH A O   1 
HETATM 2088 O O   . HOH B 2 .   ? 48.180 -8.470  19.176 1.00 46.43 ? 499 HOH A O   1 
HETATM 2089 O O   . HOH B 2 .   ? 31.066 11.589  36.909 1.00 56.37 ? 500 HOH A O   1 
HETATM 2090 O O   . HOH B 2 .   ? 49.600 -3.111  8.717  1.00 44.81 ? 501 HOH A O   1 
HETATM 2091 O O   . HOH B 2 .   ? 40.604 -15.852 27.833 1.00 50.48 ? 502 HOH A O   1 
HETATM 2092 O O   . HOH B 2 .   ? 31.524 -4.332  23.229 1.00 52.00 ? 503 HOH A O   1 
HETATM 2093 O O   . HOH B 2 .   ? 19.859 -10.982 17.411 1.00 43.02 ? 504 HOH A O   1 
HETATM 2094 O O   . HOH B 2 .   ? 22.838 -7.401  37.319 1.00 49.99 ? 505 HOH A O   1 
HETATM 2095 O O   . HOH B 2 .   ? 17.418 9.263   30.521 1.00 44.89 ? 506 HOH A O   1 
HETATM 2096 O O   . HOH B 2 .   ? 47.604 9.322   12.761 1.00 49.26 ? 507 HOH A O   1 
HETATM 2097 O O   . HOH B 2 .   ? 18.222 -4.002  15.021 1.00 48.92 ? 508 HOH A O   1 
HETATM 2098 O O   . HOH B 2 .   ? 17.249 6.857   31.850 1.00 47.56 ? 509 HOH A O   1 
HETATM 2099 O O   . HOH B 2 .   ? 35.612 13.962  32.443 1.00 47.61 ? 510 HOH A O   1 
HETATM 2100 O O   . HOH B 2 .   ? 27.173 6.272   41.081 1.00 55.83 ? 511 HOH A O   1 
HETATM 2101 O O   . HOH B 2 .   ? 32.310 12.982  35.122 1.00 45.35 ? 512 HOH A O   1 
HETATM 2102 O O   . HOH B 2 .   ? 41.892 11.052  31.328 1.00 49.61 ? 513 HOH A O   1 
HETATM 2103 O O   . HOH B 2 .   ? 30.138 6.528   42.124 1.00 63.83 ? 514 HOH A O   1 
HETATM 2104 O O   . HOH B 2 .   ? 32.968 18.185  8.271  1.00 55.44 ? 515 HOH A O   1 
HETATM 2105 O O   . HOH B 2 .   ? 48.511 -6.704  22.401 1.00 51.17 ? 516 HOH A O   1 
HETATM 2106 O O   . HOH B 2 .   ? 30.275 -16.867 25.816 1.00 56.02 ? 517 HOH A O   1 
HETATM 2107 O O   . HOH B 2 .   ? 46.968 -6.172  37.859 1.00 52.32 ? 518 HOH A O   1 
# 
